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*** 5CQG ***elNémo ID: 220404205247136735Job options:ID = 220404205247136735 JOBID = 5CQG USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:
HEADER 5CQG
HEADER TRANSFERASE/TRANSFERASE INHIBITOR 21-JUL-15 5CQG
TITLE STRUCTURE OF TRIBOLIUM TELOMERASE IN COMPLEX WITH THE HIGHLY SPECIFIC
TITLE 2 INHIBITOR BIBR1532
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TELOMERASE REVERSE TRANSCRIPTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRIBOLIUM CASTANEUM;
SOURCE 3 ORGANISM_COMMON: RED FLOUR BEETLE;
SOURCE 4 ORGANISM_TAXID: 7070;
SOURCE 5 GENE: TERT, TCASGA2_TC010963;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TELOMERASE REVERSE TRANSCRIPTASE FOLD TERT BIBR15312, TELOMERASE
KEYWDS 2 INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BRYAN,C.RICE,H.HOFFMAN,M.HARKISHEIMER,M.SWEENEY,E.SKORDALAKES
REVDAT 3 10-OCT-18 5CQG 1 COMPND JRNL
REVDAT 2 13-SEP-17 5CQG 1 REMARK
REVDAT 1 09-SEP-15 5CQG 0
JRNL AUTH C.BRYAN,C.RICE,H.HOFFMAN,M.HARKISHEIMER,M.SWEENEY,
JRNL AUTH 2 E.SKORDALAKES
JRNL TITL STRUCTURAL BASIS OF TELOMERASE INHIBITION BY THE HIGHLY
JRNL TITL 2 SPECIFIC BIBR1532.
JRNL REF STRUCTURE V. 23 1934 2015
JRNL REFN ISSN 1878-4186
JRNL PMID 26365799
JRNL DOI 10.1016/J.STR.2015.08.006
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 91683
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4857
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6464
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.3580
REMARK 3 BIN FREE R VALUE SET COUNT : 333
REMARK 3 BIN FREE R VALUE : 0.3700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9964
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 409
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 2.70000
REMARK 3 B33 (A**2) : -2.78000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.252
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.216
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.859
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10282 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13860 ; 1.043 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1190 ; 6.511 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 470 ;34.082 ;22.979
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1922 ;18.885 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;15.695 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1494 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7650 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 596
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3100 5.6380 -50.5170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0957 T22: 0.2240
REMARK 3 T33: 0.0165 T12: 0.0153
REMARK 3 T13: 0.0044 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.7366 L22: 0.2405
REMARK 3 L33: 1.0439 L12: 0.0701
REMARK 3 L13: -0.6466 L23: 0.1246
REMARK 3 S TENSOR
REMARK 3 S11: 0.0724 S12: 0.2986 S13: -0.0057
REMARK 3 S21: -0.0183 S22: -0.0141 S23: -0.0267
REMARK 3 S31: -0.0191 S32: -0.3968 S33: -0.0583
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 596
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7610 34.8410 -21.8880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1009 T22: 0.2408
REMARK 3 T33: 0.0320 T12: -0.0289
REMARK 3 T13: 0.0170 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.3753 L22: 0.1821
REMARK 3 L33: 1.6145 L12: -0.0942
REMARK 3 L13: -0.4253 L23: -0.0243
REMARK 3 S TENSOR
REMARK 3 S11: -0.0508 S12: 0.1994 S13: 0.0559
REMARK 3 S21: 0.0600 S22: -0.0015 S23: 0.0022
REMARK 3 S31: 0.1212 S32: -0.5267 S33: 0.0523
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 5CQG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212034.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 97056
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.47100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 3DU6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M NANO3 100MM TRIS 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 42.45100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 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 PRO A 45 148.26 -38.96
REMARK 500 PHE A 83 -5.95 80.31
REMARK 500 TRP A 102 0.84 -67.63
REMARK 500 ILE A 126 -50.45 -127.46
REMARK 500 LEU A 141 -9.30 78.46
REMARK 500 LYS A 167 25.30 -78.07
REMARK 500 MET A 168 -160.32 -127.14
REMARK 500 ASP A 176 -12.67 77.11
REMARK 500 GLU A 177 49.36 -93.35
REMARK 500 VAL A 178 -36.38 -135.48
REMARK 500 LYS A 179 105.04 71.39
REMARK 500 GLN A 190 -84.43 53.49
REMARK 500 ASN A 192 -134.74 -112.03
REMARK 500 PRO A 201 -79.78 -93.68
REMARK 500 ASP A 202 -93.04 56.23
REMARK 500 SER A 203 92.20 46.21
REMARK 500 ALA A 204 -89.10 56.58
REMARK 500 GLU A 222 -71.53 -108.23
REMARK 500 LYS A 225 24.89 -71.38
REMARK 500 SER A 227 -83.53 -115.03
REMARK 500 ASP A 254 74.56 25.35
REMARK 500 PRO A 272 78.60 -117.63
REMARK 500 LEU A 276 -53.31 -125.26
REMARK 500 ASP A 277 -139.02 65.04
REMARK 500 PHE A 295 -135.61 -141.60
REMARK 500 ARG A 297 -18.09 66.11
REMARK 500 ASN A 303 60.37 -116.82
REMARK 500 PHE A 329 65.80 -116.89
REMARK 500 ASP A 333 133.84 143.86
REMARK 500 ARG A 399 -3.49 73.25
REMARK 500 LYS A 406 10.43 119.32
REMARK 500 LYS A 526 118.48 -178.36
REMARK 500 SER B 25 0.39 -69.44
REMARK 500 PHE B 83 -13.44 78.71
REMARK 500 HIS B 92 -20.23 -143.71
REMARK 500 LEU B 141 -3.98 73.87
REMARK 500 LYS B 166 -74.55 -68.34
REMARK 500 LYS B 167 31.55 -79.54
REMARK 500 VAL B 174 81.73 -150.31
REMARK 500 GLN B 175 -174.69 56.07
REMARK 500 GLU B 177 18.23 -159.21
REMARK 500 LYS B 179 81.17 -158.23
REMARK 500 ARG B 181 -53.68 96.57
REMARK 500 GLN B 190 94.03 -56.39
REMARK 500 ASP B 191 -0.41 70.75
REMARK 500 ASN B 192 -159.00 -138.82
REMARK 500 ASP B 202 59.04 74.24
REMARK 500 ARG B 205 141.82 74.62
REMARK 500 ASP B 254 70.67 42.19
REMARK 500 ILE B 271 116.66 -39.42
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS B 406 LEU B 407 -41.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 55C A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 55C B 601
DBREF 5CQG A 1 596 UNP Q0QHL8 Q0QHL8_TRICA 1 596
DBREF 5CQG B 1 596 UNP Q0QHL8 Q0QHL8_TRICA 1 596
SEQRES 1 A 596 MET VAL HIS TYR TYR ARG LEU SER LEU LYS SER ARG GLN
SEQRES 2 A 596 LYS ALA PRO LYS ILE VAL ASN SER LYS TYR ASN SER ILE
SEQRES 3 A 596 LEU ASN ILE ALA LEU LYS ASN PHE ARG LEU CYS LYS LYS
SEQRES 4 A 596 HIS LYS THR LYS LYS PRO VAL GLN ILE LEU ALA LEU LEU
SEQRES 5 A 596 GLN GLU ILE ILE PRO LYS SER TYR PHE GLY THR THR THR
SEQRES 6 A 596 ASN LEU LYS ARG PHE TYR LYS VAL VAL GLU LYS ILE LEU
SEQRES 7 A 596 THR GLN SER SER PHE GLU CYS ILE HIS LEU SER VAL LEU
SEQRES 8 A 596 HIS LYS CYS TYR ASP TYR ASP ALA ILE PRO TRP LEU GLN
SEQRES 9 A 596 ASN VAL GLU PRO ASN LEU ARG PRO LYS LEU LEU LEU LYS
SEQRES 10 A 596 HIS ASN LEU PHE LEU LEU ASP ASN ILE VAL LYS PRO ILE
SEQRES 11 A 596 ILE ALA PHE TYR TYR LYS PRO ILE LYS THR LEU ASN GLY
SEQRES 12 A 596 HIS GLU ILE LYS PHE ILE ARG LYS GLU GLU TYR ILE SER
SEQRES 13 A 596 PHE GLU SER LYS VAL PHE HIS LYS LEU LYS LYS MET LYS
SEQRES 14 A 596 TYR LEU VAL GLU VAL GLN ASP GLU VAL LYS PRO ARG GLY
SEQRES 15 A 596 VAL LEU ASN ILE ILE PRO LYS GLN ASP ASN PHE ARG ALA
SEQRES 16 A 596 ILE VAL SER ILE PHE PRO ASP SER ALA ARG LYS PRO PHE
SEQRES 17 A 596 PHE LYS LEU LEU THR SER LYS ILE TYR LYS VAL LEU GLU
SEQRES 18 A 596 GLU LYS TYR LYS THR SER GLY SER LEU TYR THR CYS TRP
SEQRES 19 A 596 SER GLU PHE THR GLN LYS THR GLN GLY GLN ILE TYR GLY
SEQRES 20 A 596 ILE LYS VAL ASP ILE ARG ASP ALA TYR GLY ASN VAL LYS
SEQRES 21 A 596 ILE PRO VAL LEU CYS LYS LEU ILE GLN SER ILE PRO THR
SEQRES 22 A 596 HIS LEU LEU ASP SER GLU LYS LYS ASN PHE ILE VAL ASP
SEQRES 23 A 596 HIS ILE SER ASN GLN PHE VAL ALA PHE ARG ARG LYS ILE
SEQRES 24 A 596 TYR LYS TRP ASN HIS GLY LEU LEU GLN GLY ASP PRO LEU
SEQRES 25 A 596 SER GLY CYS LEU CYS GLU LEU TYR MET ALA PHE MET ASP
SEQRES 26 A 596 ARG LEU TYR PHE SER ASN LEU ASP LYS ASP ALA PHE ILE
SEQRES 27 A 596 HIS ARG THR VAL ASP ASP TYR PHE PHE CYS SER PRO HIS
SEQRES 28 A 596 PRO HIS LYS VAL TYR ASP PHE GLU LEU LEU ILE LYS GLY
SEQRES 29 A 596 VAL TYR GLN VAL ASN PRO THR LYS THR ARG THR ASN LEU
SEQRES 30 A 596 PRO THR HIS ARG HIS PRO GLN ASP GLU ILE PRO TYR CYS
SEQRES 31 A 596 GLY LYS ILE PHE ASN LEU THR THR ARG GLN VAL ARG THR
SEQRES 32 A 596 LEU TYR LYS LEU PRO PRO ASN TYR GLU ILE ARG HIS LYS
SEQRES 33 A 596 PHE LYS LEU TRP ASN PHE ASN ASN GLN ILE SER ASP ASP
SEQRES 34 A 596 ASN PRO ALA ARG PHE LEU GLN LYS ALA MET ASP PHE PRO
SEQRES 35 A 596 PHE ILE CYS ASN SER PHE THR LYS PHE GLU PHE ASN THR
SEQRES 36 A 596 VAL PHE ASN ASP GLN ARG THR VAL PHE ALA ASN PHE TYR
SEQRES 37 A 596 ASP ALA MET ILE CYS VAL ALA TYR LYS PHE ASP ALA ALA
SEQRES 38 A 596 MET MET ALA LEU ARG THR SER PHE LEU VAL ASN ASP PHE
SEQRES 39 A 596 GLY PHE ILE TRP LEU VAL LEU SER SER THR VAL ARG ALA
SEQRES 40 A 596 TYR ALA SER ARG ALA PHE LYS LYS ILE VAL THR TYR LYS
SEQRES 41 A 596 GLY GLY LYS TYR ARG LYS VAL THR PHE GLN CYS LEU LYS
SEQRES 42 A 596 SER ILE ALA TRP ARG ALA PHE LEU ALA VAL LEU LYS ARG
SEQRES 43 A 596 ARG THR GLU ILE TYR LYS GLY LEU ILE ASP ARG ILE LYS
SEQRES 44 A 596 SER ARG GLU LYS LEU THR MET LYS PHE HIS ASP GLY GLU
SEQRES 45 A 596 VAL ASP ALA SER TYR PHE CYS LYS LEU PRO GLU LYS PHE
SEQRES 46 A 596 ARG PHE VAL LYS ILE ASN ARG LYS ALA SER ILE
SEQRES 1 B 596 MET VAL HIS TYR TYR ARG LEU SER LEU LYS SER ARG GLN
SEQRES 2 B 596 LYS ALA PRO LYS ILE VAL ASN SER LYS TYR ASN SER ILE
SEQRES 3 B 596 LEU ASN ILE ALA LEU LYS ASN PHE ARG LEU CYS LYS LYS
SEQRES 4 B 596 HIS LYS THR LYS LYS PRO VAL GLN ILE LEU ALA LEU LEU
SEQRES 5 B 596 GLN GLU ILE ILE PRO LYS SER TYR PHE GLY THR THR THR
SEQRES 6 B 596 ASN LEU LYS ARG PHE TYR LYS VAL VAL GLU LYS ILE LEU
SEQRES 7 B 596 THR GLN SER SER PHE GLU CYS ILE HIS LEU SER VAL LEU
SEQRES 8 B 596 HIS LYS CYS TYR ASP TYR ASP ALA ILE PRO TRP LEU GLN
SEQRES 9 B 596 ASN VAL GLU PRO ASN LEU ARG PRO LYS LEU LEU LEU LYS
SEQRES 10 B 596 HIS ASN LEU PHE LEU LEU ASP ASN ILE VAL LYS PRO ILE
SEQRES 11 B 596 ILE ALA PHE TYR TYR LYS PRO ILE LYS THR LEU ASN GLY
SEQRES 12 B 596 HIS GLU ILE LYS PHE ILE ARG LYS GLU GLU TYR ILE SER
SEQRES 13 B 596 PHE GLU SER LYS VAL PHE HIS LYS LEU LYS LYS MET LYS
SEQRES 14 B 596 TYR LEU VAL GLU VAL GLN ASP GLU VAL LYS PRO ARG GLY
SEQRES 15 B 596 VAL LEU ASN ILE ILE PRO LYS GLN ASP ASN PHE ARG ALA
SEQRES 16 B 596 ILE VAL SER ILE PHE PRO ASP SER ALA ARG LYS PRO PHE
SEQRES 17 B 596 PHE LYS LEU LEU THR SER LYS ILE TYR LYS VAL LEU GLU
SEQRES 18 B 596 GLU LYS TYR LYS THR SER GLY SER LEU TYR THR CYS TRP
SEQRES 19 B 596 SER GLU PHE THR GLN LYS THR GLN GLY GLN ILE TYR GLY
SEQRES 20 B 596 ILE LYS VAL ASP ILE ARG ASP ALA TYR GLY ASN VAL LYS
SEQRES 21 B 596 ILE PRO VAL LEU CYS LYS LEU ILE GLN SER ILE PRO THR
SEQRES 22 B 596 HIS LEU LEU ASP SER GLU LYS LYS ASN PHE ILE VAL ASP
SEQRES 23 B 596 HIS ILE SER ASN GLN PHE VAL ALA PHE ARG ARG LYS ILE
SEQRES 24 B 596 TYR LYS TRP ASN HIS GLY LEU LEU GLN GLY ASP PRO LEU
SEQRES 25 B 596 SER GLY CYS LEU CYS GLU LEU TYR MET ALA PHE MET ASP
SEQRES 26 B 596 ARG LEU TYR PHE SER ASN LEU ASP LYS ASP ALA PHE ILE
SEQRES 27 B 596 HIS ARG THR VAL ASP ASP TYR PHE PHE CYS SER PRO HIS
SEQRES 28 B 596 PRO HIS LYS VAL TYR ASP PHE GLU LEU LEU ILE LYS GLY
SEQRES 29 B 596 VAL TYR GLN VAL ASN PRO THR LYS THR ARG THR ASN LEU
SEQRES 30 B 596 PRO THR HIS ARG HIS PRO GLN ASP GLU ILE PRO TYR CYS
SEQRES 31 B 596 GLY LYS ILE PHE ASN LEU THR THR ARG GLN VAL ARG THR
SEQRES 32 B 596 LEU TYR LYS LEU PRO PRO ASN TYR GLU ILE ARG HIS LYS
SEQRES 33 B 596 PHE LYS LEU TRP ASN PHE ASN ASN GLN ILE SER ASP ASP
SEQRES 34 B 596 ASN PRO ALA ARG PHE LEU GLN LYS ALA MET ASP PHE PRO
SEQRES 35 B 596 PHE ILE CYS ASN SER PHE THR LYS PHE GLU PHE ASN THR
SEQRES 36 B 596 VAL PHE ASN ASP GLN ARG THR VAL PHE ALA ASN PHE TYR
SEQRES 37 B 596 ASP ALA MET ILE CYS VAL ALA TYR LYS PHE ASP ALA ALA
SEQRES 38 B 596 MET MET ALA LEU ARG THR SER PHE LEU VAL ASN ASP PHE
SEQRES 39 B 596 GLY PHE ILE TRP LEU VAL LEU SER SER THR VAL ARG ALA
SEQRES 40 B 596 TYR ALA SER ARG ALA PHE LYS LYS ILE VAL THR TYR LYS
SEQRES 41 B 596 GLY GLY LYS TYR ARG LYS VAL THR PHE GLN CYS LEU LYS
SEQRES 42 B 596 SER ILE ALA TRP ARG ALA PHE LEU ALA VAL LEU LYS ARG
SEQRES 43 B 596 ARG THR GLU ILE TYR LYS GLY LEU ILE ASP ARG ILE LYS
SEQRES 44 B 596 SER ARG GLU LYS LEU THR MET LYS PHE HIS ASP GLY GLU
SEQRES 45 B 596 VAL ASP ALA SER TYR PHE CYS LYS LEU PRO GLU LYS PHE
SEQRES 46 B 596 ARG PHE VAL LYS ILE ASN ARG LYS ALA SER ILE
HET 55C A 601 25
HET 55C B 601 25
HETNAM 55C 2-{[(2E)-3-(NAPHTHALEN-2-YL)BUT-2-ENOYL]AMINO}BENZOIC
HETNAM 2 55C ACID
HETSYN 55C BIBR 1532
FORMUL 3 55C 2(C21 H17 N O3)
FORMUL 5 HOH *409(H2 O)
HELIX 1 AA1 SER A 8 ARG A 12 5 5
HELIX 2 AA2 SER A 25 HIS A 40 1 16
HELIX 3 AA3 GLN A 47 ILE A 56 1 10
HELIX 4 AA4 PRO A 57 PHE A 61 5 5
HELIX 5 AA5 THR A 63 LEU A 78 1 16
HELIX 6 AA6 SER A 89 HIS A 92 5 4
HELIX 7 AA7 ASP A 96 GLN A 104 5 9
HELIX 8 AA8 GLU A 107 ASN A 109 5 3
HELIX 9 AA9 LEU A 110 ILE A 126 1 17
HELIX 10 AB1 ILE A 126 TYR A 134 1 9
HELIX 11 AB2 LYS A 151 LYS A 167 1 17
HELIX 12 AB3 ARG A 205 GLU A 221 1 17
HELIX 13 AB4 SER A 229 THR A 241 1 13
HELIX 14 AB5 LYS A 260 SER A 270 1 11
HELIX 15 AB6 ASP A 277 SER A 289 1 13
HELIX 16 AB7 LEU A 312 PHE A 329 1 18
HELIX 17 AB8 HIS A 351 TYR A 366 1 16
HELIX 18 AB9 GLU A 412 PHE A 417 5 6
HELIX 19 AC1 ASN A 430 ASP A 440 1 11
HELIX 20 AC2 PHE A 441 PHE A 448 5 8
HELIX 21 AC3 THR A 449 ASN A 454 1 6
HELIX 22 AC4 ASP A 459 SER A 488 1 30
HELIX 23 AC5 PHE A 496 TYR A 519 1 24
HELIX 24 AC6 THR A 528 LYS A 545 1 18
HELIX 25 AC7 ARG A 547 GLU A 562 1 16
HELIX 26 AC8 ASP A 574 LYS A 580 5 7
HELIX 27 AC9 PRO A 582 PHE A 587 1 6
HELIX 28 AD1 SER B 8 ARG B 12 5 5
HELIX 29 AD2 SER B 25 HIS B 40 1 16
HELIX 30 AD3 GLN B 47 ILE B 56 1 10
HELIX 31 AD4 PRO B 57 PHE B 61 5 5
HELIX 32 AD5 THR B 63 THR B 79 1 17
HELIX 33 AD6 SER B 89 HIS B 92 5 4
HELIX 34 AD7 ILE B 100 GLN B 104 5 5
HELIX 35 AD8 GLU B 107 ASN B 109 5 3
HELIX 36 AD9 LEU B 110 ILE B 126 1 17
HELIX 37 AE1 ILE B 126 TYR B 134 1 9
HELIX 38 AE2 LYS B 151 LYS B 167 1 17
HELIX 39 AE3 LYS B 206 LEU B 220 1 15
HELIX 40 AE4 SER B 229 THR B 241 1 13
HELIX 41 AE5 LYS B 260 GLN B 269 1 10
HELIX 42 AE6 GLU B 279 ASN B 290 1 12
HELIX 43 AE7 LEU B 312 PHE B 329 1 18
HELIX 44 AE8 HIS B 351 TYR B 366 1 16
HELIX 45 AE9 ASN B 369 THR B 373 5 5
HELIX 46 AF1 GLU B 412 PHE B 417 5 6
HELIX 47 AF2 ASN B 430 ASP B 440 1 11
HELIX 48 AF3 PHE B 441 PHE B 448 5 8
HELIX 49 AF4 THR B 449 ASN B 454 1 6
HELIX 50 AF5 ASP B 459 SER B 488 1 30
HELIX 51 AF6 PHE B 496 TYR B 519 1 24
HELIX 52 AF7 THR B 528 LYS B 545 1 18
HELIX 53 AF8 ARG B 547 GLU B 562 1 16
HELIX 54 AF9 ASP B 574 CYS B 579 5 6
HELIX 55 AG1 PRO B 582 PHE B 587 1 6
SHEET 1 AA1 2 TYR A 4 ARG A 6 0
SHEET 2 AA1 2 CYS A 85 HIS A 87 -1 O ILE A 86 N TYR A 5
SHEET 1 AA2 2 TYR A 135 LYS A 139 0
SHEET 2 AA2 2 ILE A 146 ARG A 150 -1 O LYS A 147 N ILE A 138
SHEET 1 AA3 3 LEU A 171 GLU A 173 0
SHEET 2 AA3 3 ILE A 299 TRP A 302 -1 O LYS A 301 N VAL A 172
SHEET 3 AA3 3 GLN A 291 ALA A 294 -1 N GLN A 291 O TRP A 302
SHEET 1 AA4 2 VAL A 183 LYS A 189 0
SHEET 2 AA4 2 ASN A 192 SER A 198 -1 O ILE A 196 N ASN A 185
SHEET 1 AA5 4 PHE A 337 ARG A 340 0
SHEET 2 AA5 4 ASP A 344 SER A 349 -1 O CYS A 348 N PHE A 337
SHEET 3 AA5 4 TYR A 246 ASP A 251 -1 N TYR A 246 O SER A 349
SHEET 4 AA5 4 ARG A 374 THR A 375 -1 O ARG A 374 N LYS A 249
SHEET 1 AA6 3 GLU A 386 TYR A 389 0
SHEET 2 AA6 3 LYS A 392 ASN A 395 -1 O PHE A 394 N ILE A 387
SHEET 3 AA6 3 VAL A 401 THR A 403 -1 O ARG A 402 N ILE A 393
SHEET 1 AA7 2 TYR B 4 ARG B 6 0
SHEET 2 AA7 2 CYS B 85 HIS B 87 -1 O ILE B 86 N TYR B 5
SHEET 1 AA8 2 TYR B 135 LYS B 139 0
SHEET 2 AA8 2 ILE B 146 ARG B 150 -1 O ILE B 149 N LYS B 136
SHEET 1 AA9 3 LEU B 171 GLU B 173 0
SHEET 2 AA9 3 ILE B 299 TRP B 302 -1 O LYS B 301 N VAL B 172
SHEET 3 AA9 3 GLN B 291 ALA B 294 -1 N GLN B 291 O TRP B 302
SHEET 1 AB1 2 VAL B 183 PRO B 188 0
SHEET 2 AB1 2 PHE B 193 SER B 198 -1 O ILE B 196 N ASN B 185
SHEET 1 AB2 4 PHE B 337 ARG B 340 0
SHEET 2 AB2 4 ASP B 344 SER B 349 -1 O CYS B 348 N PHE B 337
SHEET 3 AB2 4 TYR B 246 ASP B 251 -1 N VAL B 250 O TYR B 345
SHEET 4 AB2 4 ARG B 374 THR B 375 -1 O ARG B 374 N LYS B 249
SHEET 1 AB3 3 GLU B 386 TYR B 389 0
SHEET 2 AB3 3 LYS B 392 ASN B 395 -1 O LYS B 392 N TYR B 389
SHEET 3 AB3 3 VAL B 401 THR B 403 -1 O ARG B 402 N ILE B 393
CISPEP 1 PHE A 200 PRO A 201 0 -3.36
CISPEP 2 SER A 270 ILE A 271 0 -10.53
CISPEP 3 SER A 289 ASN A 290 0 20.56
CISPEP 4 TYR A 405 LYS A 406 0 11.85
CISPEP 5 ASP B 176 GLU B 177 0 -9.59
CISPEP 6 PHE B 200 PRO B 201 0 -0.23
SITE 1 AC1 8 MET A 483 ARG A 486 PHE A 494 ILE A 550
SITE 2 AC1 8 TYR A 551 LEU A 554 ARG A 557 HOH A 784
SITE 1 AC2 10 MET B 483 ARG B 486 PHE B 494 ILE B 550
SITE 2 AC2 10 TYR B 551 GLY B 553 LEU B 554 ARG B 557
SITE 3 AC2 10 HOH B 735 HOH B 841
CRYST1 117.719 84.902 123.333 90.00 116.20 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008495 0.000000 0.004180 0.00000
SCALE2 0.000000 0.011778 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009036 0.00000
ATOM 1 N MET A 1 21.546 28.956 -51.201 1.00 70.61 N
ANISOU 1 N MET A 1 10060 7996 8772 392 1875 90 N
ATOM 2 CA MET A 1 20.194 28.325 -51.232 1.00 67.59 C
ANISOU 2 CA MET A 1 9630 7704 8345 488 1783 169 C
ATOM 3 C MET A 1 20.265 26.786 -51.302 1.00 61.73 C
ANISOU 3 C MET A 1 8784 7083 7588 460 1607 137 C
ATOM 4 O MET A 1 19.755 26.102 -50.407 1.00 62.98 O
ANISOU 4 O MET A 1 8894 7290 7743 440 1514 117 O
ATOM 5 CB MET A 1 19.352 28.895 -52.394 1.00 71.70 C
ANISOU 5 CB MET A 1 10190 8232 8821 626 1854 292 C
ATOM 6 CG MET A 1 17.917 28.361 -52.458 1.00 76.51 C
ANISOU 6 CG MET A 1 10748 8943 9378 727 1772 375 C
ATOM 7 SD MET A 1 16.845 29.111 -53.717 1.00 81.54 S
ANISOU 7 SD MET A 1 11422 9606 9951 901 1859 527 S
ATOM 8 CE MET A 1 17.455 28.369 -55.232 1.00 72.65 C
ANISOU 8 CE MET A 1 10249 8565 8789 910 1795 535 C
ATOM 9 N VAL A 2 20.912 26.250 -52.342 1.00 56.42 N
ANISOU 9 N VAL A 2 8080 6451 6905 457 1568 129 N
ATOM 10 CA VAL A 2 20.817 24.800 -52.661 1.00 50.54 C
ANISOU 10 CA VAL A 2 7243 5819 6138 453 1416 115 C
ATOM 11 C VAL A 2 21.791 23.909 -51.897 1.00 45.98 C
ANISOU 11 C VAL A 2 6613 5257 5598 343 1325 12 C
ATOM 12 O VAL A 2 23.007 24.066 -52.020 1.00 48.84 O
ANISOU 12 O VAL A 2 6982 5581 5993 275 1356 -51 O
ATOM 13 CB VAL A 2 20.948 24.530 -54.172 1.00 49.90 C
ANISOU 13 CB VAL A 2 7147 5787 6022 507 1410 159 C
ATOM 14 CG1 VAL A 2 20.835 23.038 -54.459 1.00 48.57 C
ANISOU 14 CG1 VAL A 2 6890 5729 5834 495 1263 137 C
ATOM 15 CG2 VAL A 2 19.871 25.295 -54.935 1.00 52.76 C
ANISOU 15 CG2 VAL A 2 7550 6160 6334 630 1485 273 C
ATOM 16 N HIS A 3 21.245 22.947 -51.145 1.00 41.25 N
ANISOU 16 N HIS A 3 5958 4721 4993 331 1212 -1 N
ATOM 17 CA HIS A 3 22.043 22.044 -50.310 1.00 37.63 C
ANISOU 17 CA HIS A 3 5448 4284 4566 241 1121 -87 C
ATOM 18 C HIS A 3 21.996 20.608 -50.768 1.00 34.11 C
ANISOU 18 C HIS A 3 4930 3926 4104 247 996 -92 C
ATOM 19 O HIS A 3 22.870 19.823 -50.420 1.00 30.51 O
ANISOU 19 O HIS A 3 4432 3487 3674 184 930 -158 O
ATOM 20 CB HIS A 3 21.581 22.108 -48.854 1.00 39.77 C
ANISOU 20 CB HIS A 3 5719 4543 4846 208 1102 -107 C
ATOM 21 CG HIS A 3 21.731 23.472 -48.223 1.00 42.36 C
ANISOU 21 CG HIS A 3 6118 4779 5195 182 1227 -121 C
ATOM 22 ND1 HIS A 3 20.670 24.242 -47.900 1.00 43.03 N
ANISOU 22 ND1 HIS A 3 6250 4832 5266 237 1292 -64 N
ATOM 23 CD2 HIS A 3 22.864 24.200 -47.874 1.00 42.08 C
ANISOU 23 CD2 HIS A 3 6115 4678 5195 101 1306 -192 C
ATOM 24 CE1 HIS A 3 21.101 25.397 -47.367 1.00 43.39 C
ANISOU 24 CE1 HIS A 3 6359 4786 5338 193 1411 -97 C
ATOM 25 NE2 HIS A 3 22.444 25.373 -47.354 1.00 43.55 N
ANISOU 25 NE2 HIS A 3 6370 4789 5388 105 1419 -178 N
ATOM 26 N TYR A 4 20.979 20.270 -51.560 1.00 32.27 N
ANISOU 26 N TYR A 4 4682 3751 3826 324 969 -24 N
ATOM 27 CA TYR A 4 20.626 18.887 -51.867 1.00 31.67 C
ANISOU 27 CA TYR A 4 4541 3762 3729 330 853 -27 C
ATOM 28 C TYR A 4 20.924 18.490 -53.320 1.00 33.12 C
ANISOU 28 C TYR A 4 4705 3988 3891 357 846 -14 C
ATOM 29 O TYR A 4 20.712 19.265 -54.254 1.00 32.78 O
ANISOU 29 O TYR A 4 4694 3940 3820 414 920 37 O
ATOM 30 CB TYR A 4 19.117 18.658 -51.653 1.00 30.41 C
ANISOU 30 CB TYR A 4 4367 3660 3526 387 818 32 C
ATOM 31 CG TYR A 4 18.585 18.713 -50.242 1.00 28.58 C
ANISOU 31 CG TYR A 4 4140 3411 3306 363 799 22 C
ATOM 32 CD1 TYR A 4 19.439 18.799 -49.129 1.00 29.02 C
ANISOU 32 CD1 TYR A 4 4205 3412 3408 287 798 -42 C
ATOM 33 CD2 TYR A 4 17.218 18.611 -50.015 1.00 27.90 C
ANISOU 33 CD2 TYR A 4 4042 3376 3182 413 778 74 C
ATOM 34 CE1 TYR A 4 18.928 18.833 -47.831 1.00 28.23 C
ANISOU 34 CE1 TYR A 4 4109 3303 3314 263 780 -51 C
ATOM 35 CE2 TYR A 4 16.698 18.648 -48.734 1.00 28.18 C
ANISOU 35 CE2 TYR A 4 4082 3397 3227 391 762 65 C
ATOM 36 CZ TYR A 4 17.553 18.761 -47.643 1.00 28.67 C
ANISOU 36 CZ TYR A 4 4158 3399 3333 316 763 3 C
ATOM 37 OH TYR A 4 17.021 18.798 -46.378 1.00 27.77 O
ANISOU 37 OH TYR A 4 4048 3277 3223 293 748 -5 O
ATOM 38 N TYR A 5 21.354 17.252 -53.497 1.00 33.53 N
ANISOU 38 N TYR A 5 4704 4084 3951 322 757 -59 N
ATOM 39 CA TYR A 5 21.326 16.601 -54.799 1.00 33.44 C
ANISOU 39 CA TYR A 5 4662 4134 3907 348 729 -47 C
ATOM 40 C TYR A 5 20.202 15.560 -54.760 1.00 33.09 C
ANISOU 40 C TYR A 5 4574 4173 3826 367 644 -29 C
ATOM 41 O TYR A 5 20.089 14.792 -53.812 1.00 34.18 O
ANISOU 41 O TYR A 5 4688 4313 3983 328 579 -61 O
ATOM 42 CB TYR A 5 22.683 15.945 -55.080 1.00 34.15 C
ANISOU 42 CB TYR A 5 4728 4208 4037 291 701 -118 C
ATOM 43 CG TYR A 5 22.758 15.140 -56.366 1.00 35.03 C
ANISOU 43 CG TYR A 5 4806 4381 4122 306 669 -120 C
ATOM 44 CD1 TYR A 5 22.721 15.769 -57.624 1.00 34.73 C
ANISOU 44 CD1 TYR A 5 4788 4360 4048 351 732 -79 C
ATOM 45 CD2 TYR A 5 22.883 13.744 -56.329 1.00 34.81 C
ANISOU 45 CD2 TYR A 5 4729 4392 4103 275 581 -163 C
ATOM 46 CE1 TYR A 5 22.794 15.032 -58.799 1.00 34.05 C
ANISOU 46 CE1 TYR A 5 4668 4335 3931 359 703 -86 C
ATOM 47 CE2 TYR A 5 22.969 12.994 -57.505 1.00 35.44 C
ANISOU 47 CE2 TYR A 5 4780 4525 4159 281 558 -173 C
ATOM 48 CZ TYR A 5 22.919 13.636 -58.730 1.00 36.19 C
ANISOU 48 CZ TYR A 5 4890 4644 4214 321 616 -137 C
ATOM 49 OH TYR A 5 22.993 12.880 -59.883 1.00 39.11 O
ANISOU 49 OH TYR A 5 5229 5074 4555 322 593 -151 O
ATOM 50 N ARG A 6 19.327 15.592 -55.735 1.00 31.39 N
ANISOU 50 N ARG A 6 4346 4028 3552 426 652 24 N
ATOM 51 CA ARG A 6 18.213 14.692 -55.737 1.00 32.27 C
ANISOU 51 CA ARG A 6 4413 4227 3621 438 581 38 C
ATOM 52 C ARG A 6 18.669 13.364 -56.285 1.00 32.65 C
ANISOU 52 C ARG A 6 4418 4314 3673 394 514 -16 C
ATOM 53 O ARG A 6 19.452 13.337 -57.236 1.00 32.92 O
ANISOU 53 O ARG A 6 4451 4346 3709 390 534 -33 O
ATOM 54 CB ARG A 6 17.111 15.249 -56.626 1.00 34.90 C
ANISOU 54 CB ARG A 6 4741 4638 3880 519 617 115 C
ATOM 55 CG ARG A 6 16.294 16.329 -55.974 1.00 35.77 C
ANISOU 55 CG ARG A 6 4886 4727 3978 573 672 177 C
ATOM 56 CD ARG A 6 15.366 16.976 -56.974 1.00 39.65 C
ANISOU 56 CD ARG A 6 5372 5296 4395 667 717 262 C
ATOM 57 NE ARG A 6 16.091 17.470 -58.140 1.00 45.49 N
ANISOU 57 NE ARG A 6 6135 6025 5124 692 775 279 N
ATOM 58 CZ ARG A 6 15.604 18.353 -59.008 1.00 46.67 C
ANISOU 58 CZ ARG A 6 6302 6210 5217 781 843 361 C
ATOM 59 NH1 ARG A 6 14.382 18.850 -58.838 1.00 49.35 N
ANISOU 59 NH1 ARG A 6 6636 6604 5509 858 862 434 N
ATOM 60 NH2 ARG A 6 16.337 18.733 -60.045 1.00 45.56 N
ANISOU 60 NH2 ARG A 6 6184 6056 5069 797 895 372 N
ATOM 61 N LEU A 7 18.202 12.264 -55.691 1.00 31.10 N
ANISOU 61 N LEU A 7 4189 4148 3478 359 439 -45 N
ATOM 62 CA LEU A 7 18.614 10.908 -56.148 1.00 30.92 C
ANISOU 62 CA LEU A 7 4130 4151 3464 314 381 -101 C
ATOM 63 C LEU A 7 17.840 10.391 -57.376 1.00 32.22 C
ANISOU 63 C LEU A 7 4259 4422 3562 334 367 -88 C
ATOM 64 O LEU A 7 18.259 9.411 -58.026 1.00 32.82 O
ANISOU 64 O LEU A 7 4310 4518 3640 300 338 -135 O
ATOM 65 CB LEU A 7 18.532 9.884 -55.013 1.00 28.52 C
ANISOU 65 CB LEU A 7 3815 3827 3195 266 316 -140 C
ATOM 66 CG LEU A 7 19.307 10.112 -53.696 1.00 28.42 C
ANISOU 66 CG LEU A 7 3826 3728 3243 236 312 -163 C
ATOM 67 CD1 LEU A 7 19.167 8.882 -52.801 1.00 27.72 C
ANISOU 67 CD1 LEU A 7 3720 3634 3176 195 244 -196 C
ATOM 68 CD2 LEU A 7 20.785 10.452 -53.904 1.00 27.51 C
ANISOU 68 CD2 LEU A 7 3722 3553 3175 219 342 -197 C
ATOM 69 N SER A 8 16.734 11.054 -57.702 1.00 33.12 N
ANISOU 69 N SER A 8 4366 4604 3612 390 391 -25 N
ATOM 70 CA SER A 8 15.867 10.626 -58.804 1.00 35.35 C
ANISOU 70 CA SER A 8 4603 5010 3816 410 376 -10 C
ATOM 71 C SER A 8 16.582 10.555 -60.160 1.00 36.58 C
ANISOU 71 C SER A 8 4752 5191 3953 412 399 -24 C
ATOM 72 O SER A 8 17.354 11.445 -60.532 1.00 34.04 O
ANISOU 72 O SER A 8 4465 4818 3650 440 455 -3 O
ATOM 73 CB SER A 8 14.650 11.547 -58.925 1.00 37.75 C
ANISOU 73 CB SER A 8 4901 5388 4053 485 407 69 C
ATOM 74 OG SER A 8 13.783 11.111 -59.961 1.00 40.65 O
ANISOU 74 OG SER A 8 5214 5894 4335 503 388 82 O
ATOM 75 N LEU A 9 16.294 9.488 -60.890 1.00 37.96 N
ANISOU 75 N LEU A 9 4882 5447 4091 379 359 -64 N
ATOM 76 CA LEU A 9 16.810 9.285 -62.228 1.00 40.42 C
ANISOU 76 CA LEU A 9 5180 5804 4374 376 376 -82 C
ATOM 77 C LEU A 9 16.289 10.367 -63.180 1.00 44.40 C
ANISOU 77 C LEU A 9 5680 6387 4801 455 427 -4 C
ATOM 78 O LEU A 9 16.988 10.778 -64.104 1.00 46.13 O
ANISOU 78 O LEU A 9 5913 6601 5011 473 468 3 O
ATOM 79 CB LEU A 9 16.400 7.897 -62.720 1.00 37.86 C
ANISOU 79 CB LEU A 9 4807 5560 4017 318 326 -143 C
ATOM 80 CG LEU A 9 17.456 6.793 -62.688 1.00 36.95 C
ANISOU 80 CG LEU A 9 4697 5371 3968 248 304 -227 C
ATOM 81 CD1 LEU A 9 18.282 6.802 -61.404 1.00 33.58 C
ANISOU 81 CD1 LEU A 9 4309 4812 3636 230 294 -244 C
ATOM 82 CD2 LEU A 9 16.812 5.428 -62.946 1.00 35.22 C
ANISOU 82 CD2 LEU A 9 4439 5223 3718 188 262 -285 C
ATOM 83 N LYS A 10 15.076 10.851 -62.909 1.00 47.39 N
ANISOU 83 N LYS A 10 6043 6837 5125 506 427 56 N
ATOM 84 CA LYS A 10 14.403 11.863 -63.733 1.00 49.73 C
ANISOU 84 CA LYS A 10 6332 7222 5339 596 475 143 C
ATOM 85 C LYS A 10 15.274 13.056 -64.100 1.00 48.83 C
ANISOU 85 C LYS A 10 6277 7025 5249 647 554 190 C
ATOM 86 O LYS A 10 15.064 13.691 -65.136 1.00 51.11 O
ANISOU 86 O LYS A 10 6563 7385 5471 712 597 250 O
ATOM 87 CB LYS A 10 13.119 12.347 -63.045 1.00 53.98 C
ANISOU 87 CB LYS A 10 6855 7813 5838 650 472 205 C
ATOM 88 CG LYS A 10 11.986 11.331 -63.079 1.00 59.34 C
ANISOU 88 CG LYS A 10 7463 8627 6456 617 407 175 C
ATOM 89 CD LYS A 10 10.774 11.797 -62.286 1.00 61.89 C
ANISOU 89 CD LYS A 10 7770 8995 6749 666 404 231 C
ATOM 90 CE LYS A 10 9.747 10.676 -62.168 1.00 66.37 C
ANISOU 90 CE LYS A 10 8268 9682 7267 611 338 184 C
ATOM 91 NZ LYS A 10 8.424 11.158 -61.670 1.00 69.56 N
ANISOU 91 NZ LYS A 10 8639 10172 7617 670 337 244 N
ATOM 92 N SER A 11 16.253 13.360 -63.260 1.00 47.23 N
ANISOU 92 N SER A 11 6128 6678 5139 616 575 162 N
ATOM 93 CA SER A 11 17.115 14.516 -63.501 1.00 48.49 C
ANISOU 93 CA SER A 11 6348 6747 5327 651 659 197 C
ATOM 94 C SER A 11 18.412 14.188 -64.253 1.00 47.04 C
ANISOU 94 C SER A 11 6173 6523 5176 604 671 141 C
ATOM 95 O SER A 11 19.265 15.063 -64.413 1.00 46.31 O
ANISOU 95 O SER A 11 6131 6348 5116 617 741 155 O
ATOM 96 CB SER A 11 17.431 15.230 -62.192 1.00 45.58 C
ANISOU 96 CB SER A 11 6033 6252 5032 645 691 200 C
ATOM 97 OG SER A 11 17.692 14.285 -61.173 1.00 45.96 O
ANISOU 97 OG SER A 11 6065 6259 5139 568 623 127 O
ATOM 98 N ARG A 12 18.556 12.946 -64.721 1.00 45.57 N
ANISOU 98 N ARG A 12 5939 6393 4981 548 609 75 N
ATOM 99 CA ARG A 12 19.778 12.544 -65.453 1.00 46.49 C
ANISOU 99 CA ARG A 12 6058 6476 5128 502 618 17 C
ATOM 100 C ARG A 12 19.947 13.361 -66.716 1.00 49.14 C
ANISOU 100 C ARG A 12 6409 6852 5407 557 685 70 C
ATOM 101 O ARG A 12 18.968 13.877 -67.270 1.00 51.59 O
ANISOU 101 O ARG A 12 6709 7257 5635 627 705 145 O
ATOM 102 CB ARG A 12 19.769 11.047 -65.809 1.00 42.91 C
ANISOU 102 CB ARG A 12 5552 6083 4668 438 549 -59 C
ATOM 103 CG ARG A 12 18.732 10.633 -66.843 1.00 41.15 C
ANISOU 103 CG ARG A 12 5278 6015 4343 457 528 -40 C
ATOM 104 CD ARG A 12 18.392 9.172 -66.676 1.00 41.95 C
ANISOU 104 CD ARG A 12 5333 6160 4446 386 459 -116 C
ATOM 105 NE ARG A 12 17.571 8.632 -67.763 1.00 42.68 N
ANISOU 105 NE ARG A 12 5370 6405 4440 382 441 -121 N
ATOM 106 CZ ARG A 12 16.246 8.520 -67.724 1.00 41.39 C
ANISOU 106 CZ ARG A 12 5164 6358 4202 401 414 -92 C
ATOM 107 NH1 ARG A 12 15.560 8.928 -66.661 1.00 40.16 N
ANISOU 107 NH1 ARG A 12 5017 6179 4059 430 403 -51 N
ATOM 108 NH2 ARG A 12 15.606 8.001 -68.754 1.00 41.71 N
ANISOU 108 NH2 ARG A 12 5148 6547 4151 387 399 -108 N
ATOM 109 N GLN A 13 21.185 13.462 -67.186 1.00 48.91 N
ANISOU 109 N GLN A 13 6404 6758 5418 527 721 32 N
ATOM 110 CA GLN A 13 21.450 14.130 -68.445 1.00 50.28 C
ANISOU 110 CA GLN A 13 6594 6968 5539 569 785 76 C
ATOM 111 C GLN A 13 21.881 13.158 -69.535 1.00 50.23 C
ANISOU 111 C GLN A 13 6546 7031 5507 526 755 16 C
ATOM 112 O GLN A 13 22.371 12.068 -69.247 1.00 46.85 O
ANISOU 112 O GLN A 13 6091 6580 5128 455 702 -68 O
ATOM 113 CB GLN A 13 22.467 15.258 -68.254 1.00 52.66 C
ANISOU 113 CB GLN A 13 6964 7145 5898 577 871 91 C
ATOM 114 CG GLN A 13 21.846 16.553 -67.722 1.00 57.31 C
ANISOU 114 CG GLN A 13 7605 7694 6476 649 937 180 C
ATOM 115 CD GLN A 13 22.826 17.404 -66.927 1.00 58.30 C
ANISOU 115 CD GLN A 13 7794 7671 6684 622 1004 161 C
ATOM 116 OE1 GLN A 13 22.511 17.859 -65.824 1.00 58.04 O
ANISOU 116 OE1 GLN A 13 7787 7579 6687 627 1013 175 O
ATOM 117 NE2 GLN A 13 24.031 17.619 -67.482 1.00 55.71 N
ANISOU 117 NE2 GLN A 13 7490 7288 6388 586 1053 124 N
ATOM 118 N LYS A 14 21.628 13.550 -70.786 1.00 54.12 N
ANISOU 118 N LYS A 14 7033 7614 5916 572 793 65 N
ATOM 119 CA LYS A 14 22.171 12.882 -71.962 1.00 55.79 C
ANISOU 119 CA LYS A 14 7215 7884 6097 536 787 16 C
ATOM 120 C LYS A 14 23.646 13.270 -72.109 1.00 55.34 C
ANISOU 120 C LYS A 14 7203 7710 6112 505 843 -19 C
ATOM 121 O LYS A 14 23.971 14.448 -72.263 1.00 58.59 O
ANISOU 121 O LYS A 14 7667 8068 6523 550 922 38 O
ATOM 122 CB LYS A 14 21.374 13.292 -73.210 1.00 58.91 C
ANISOU 122 CB LYS A 14 7589 8422 6370 603 812 90 C
ATOM 123 CG LYS A 14 21.901 12.707 -74.511 1.00 62.25 C
ANISOU 123 CG LYS A 14 7983 8916 6750 567 815 43 C
ATOM 124 CD LYS A 14 20.993 13.038 -75.680 1.00 66.22 C
ANISOU 124 CD LYS A 14 8455 9585 7120 633 830 117 C
ATOM 125 CE LYS A 14 21.509 12.422 -76.976 1.00 69.66 C
ANISOU 125 CE LYS A 14 8860 10098 7508 591 831 65 C
ATOM 126 NZ LYS A 14 20.550 12.642 -78.100 1.00 72.22 N
ANISOU 126 NZ LYS A 14 9141 10608 7689 651 836 133 N
ATOM 127 N ALA A 15 24.534 12.281 -72.028 1.00 53.07 N
ANISOU 127 N ALA A 15 6895 7383 5887 428 807 -117 N
ATOM 128 CA ALA A 15 25.988 12.538 -72.032 1.00 50.22 C
ANISOU 128 CA ALA A 15 6565 6915 5601 391 852 -163 C
ATOM 129 C ALA A 15 26.471 13.025 -73.379 1.00 49.39 C
ANISOU 129 C ALA A 15 6474 6845 5445 409 917 -143 C
ATOM 130 O ALA A 15 26.079 12.476 -74.404 1.00 49.58 O
ANISOU 130 O ALA A 15 6461 6978 5397 410 898 -148 O
ATOM 131 CB ALA A 15 26.755 11.281 -71.644 1.00 46.97 C
ANISOU 131 CB ALA A 15 6119 6464 5261 316 796 -267 C
ATOM 132 N PRO A 16 27.343 14.047 -73.383 1.00 48.73 N
ANISOU 132 N PRO A 16 6444 6671 5399 417 996 -125 N
ATOM 133 CA PRO A 16 28.066 14.414 -74.604 1.00 49.86 C
ANISOU 133 CA PRO A 16 6603 6827 5511 417 1061 -123 C
ATOM 134 C PRO A 16 29.022 13.295 -74.987 1.00 51.43 C
ANISOU 134 C PRO A 16 6762 7027 5751 344 1025 -228 C
ATOM 135 O PRO A 16 29.180 12.336 -74.212 1.00 47.72 O
ANISOU 135 O PRO A 16 6259 6531 5341 298 958 -296 O
ATOM 136 CB PRO A 16 28.869 15.647 -74.176 1.00 49.77 C
ANISOU 136 CB PRO A 16 6660 6694 5554 422 1150 -101 C
ATOM 137 CG PRO A 16 29.030 15.496 -72.690 1.00 48.64 C
ANISOU 137 CG PRO A 16 6517 6466 5497 388 1112 -141 C
ATOM 138 CD PRO A 16 27.755 14.861 -72.224 1.00 47.17 C
ANISOU 138 CD PRO A 16 6293 6352 5275 414 1032 -117 C
ATOM 139 N LYS A 17 29.653 13.410 -76.164 1.00 52.28 N
ANISOU 139 N LYS A 17 6874 7162 5828 336 1073 -239 N
ATOM 140 CA LYS A 17 30.721 12.488 -76.558 1.00 51.67 C
ANISOU 140 CA LYS A 17 6764 7071 5796 268 1057 -340 C
ATOM 141 C LYS A 17 32.004 12.759 -75.790 1.00 49.83 C
ANISOU 141 C LYS A 17 6551 6714 5667 225 1085 -393 C
ATOM 142 O LYS A 17 32.617 11.836 -75.265 1.00 49.81 O
ANISOU 142 O LYS A 17 6513 6678 5733 177 1037 -474 O
ATOM 143 CB LYS A 17 30.977 12.522 -78.074 1.00 55.49 C
ANISOU 143 CB LYS A 17 7244 7629 6209 270 1101 -337 C
ATOM 144 CG LYS A 17 29.879 11.881 -78.925 1.00 58.24 C
ANISOU 144 CG LYS A 17 7550 8123 6454 289 1058 -318 C
ATOM 145 CD LYS A 17 29.266 10.652 -78.253 1.00 57.60 C
ANISOU 145 CD LYS A 17 7418 8070 6393 255 966 -372 C
ATOM 146 CE LYS A 17 28.571 9.755 -79.266 1.00 58.99 C
ANISOU 146 CE LYS A 17 7544 8387 6480 239 931 -398 C
ATOM 147 NZ LYS A 17 29.565 8.987 -80.075 1.00 58.60 N
ANISOU 147 NZ LYS A 17 7476 8336 6452 178 944 -488 N
ATOM 148 N ILE A 18 32.414 14.021 -75.736 1.00 50.80 N
ANISOU 148 N ILE A 18 6729 6772 5799 244 1169 -349 N
ATOM 149 CA ILE A 18 33.549 14.436 -74.897 1.00 51.56 C
ANISOU 149 CA ILE A 18 6844 6758 5987 200 1202 -398 C
ATOM 150 C ILE A 18 33.156 15.660 -74.055 1.00 53.54 C
ANISOU 150 C ILE A 18 7153 6942 6248 232 1253 -331 C
ATOM 151 O ILE A 18 32.062 16.198 -74.220 1.00 52.25 O
ANISOU 151 O ILE A 18 7016 6814 6019 296 1267 -243 O
ATOM 152 CB ILE A 18 34.854 14.694 -75.725 1.00 53.58 C
ANISOU 152 CB ILE A 18 7108 6986 6262 160 1272 -446 C
ATOM 153 CG1 ILE A 18 34.718 15.931 -76.638 1.00 53.54 C
ANISOU 153 CG1 ILE A 18 7167 6982 6193 200 1375 -367 C
ATOM 154 CG2 ILE A 18 35.265 13.443 -76.513 1.00 50.79 C
ANISOU 154 CG2 ILE A 18 6697 6694 5905 127 1224 -519 C
ATOM 155 CD1 ILE A 18 36.016 16.360 -77.316 1.00 52.67 C
ANISOU 155 CD1 ILE A 18 7075 6829 6106 156 1457 -411 C
ATOM 156 N VAL A 19 34.026 16.075 -73.135 1.00 55.96 N
ANISOU 156 N VAL A 19 7474 7157 6631 188 1280 -376 N
ATOM 157 CA VAL A 19 33.716 17.212 -72.259 1.00 59.76 C
ANISOU 157 CA VAL A 19 8011 7566 7128 206 1334 -326 C
ATOM 158 C VAL A 19 34.286 18.530 -72.789 1.00 65.37 C
ANISOU 158 C VAL A 19 8792 8214 7830 207 1463 -295 C
ATOM 159 O VAL A 19 35.095 18.531 -73.725 1.00 70.83 O
ANISOU 159 O VAL A 19 9483 8914 8515 182 1506 -325 O
ATOM 160 CB VAL A 19 34.154 16.966 -70.792 1.00 57.94 C
ANISOU 160 CB VAL A 19 7758 7277 6978 157 1289 -387 C
ATOM 161 CG1 VAL A 19 33.376 15.801 -70.197 1.00 57.32 C
ANISOU 161 CG1 VAL A 19 7626 7251 6900 169 1173 -396 C
ATOM 162 CG2 VAL A 19 35.652 16.722 -70.688 1.00 55.99 C
ANISOU 162 CG2 VAL A 19 7481 6995 6796 84 1302 -485 C
ATOM 163 N ASN A 20 33.856 19.644 -72.194 1.00 69.80 N
ANISOU 163 N ASN A 20 9416 8711 8392 235 1530 -236 N
ATOM 164 CA ASN A 20 34.269 20.982 -72.645 1.00 78.91 C
ANISOU 164 CA ASN A 20 10652 9792 9536 240 1669 -197 C
ATOM 165 C ASN A 20 35.495 21.544 -71.905 1.00 81.45 C
ANISOU 165 C ASN A 20 10993 10016 9937 154 1733 -278 C
ATOM 166 O ASN A 20 36.254 20.796 -71.283 1.00 80.78 O
ANISOU 166 O ASN A 20 10847 9936 9910 87 1667 -372 O
ATOM 167 CB ASN A 20 33.088 21.963 -72.584 1.00 81.92 C
ANISOU 167 CB ASN A 20 11101 10156 9866 328 1728 -79 C
ATOM 168 CG ASN A 20 32.413 21.981 -71.228 1.00 82.92 C
ANISOU 168 CG ASN A 20 11225 10255 10026 335 1681 -73 C
ATOM 169 OD1 ASN A 20 32.796 22.740 -70.342 1.00 84.46 O
ANISOU 169 OD1 ASN A 20 11461 10355 10272 297 1743 -95 O
ATOM 170 ND2 ASN A 20 31.395 21.143 -71.062 1.00 85.58 N
ANISOU 170 ND2 ASN A 20 11509 10676 10329 377 1576 -47 N
ATOM 171 N SER A 21 35.685 22.860 -71.987 1.00 85.70 N
ANISOU 171 N SER A 21 11617 10470 10474 155 1866 -240 N
ATOM 172 CA SER A 21 36.839 23.518 -71.365 1.00 87.07 C
ANISOU 172 CA SER A 21 11814 10552 10713 64 1945 -320 C
ATOM 173 C SER A 21 36.878 23.351 -69.850 1.00 82.72 C
ANISOU 173 C SER A 21 11233 9974 10221 18 1891 -376 C
ATOM 174 O SER A 21 37.955 23.322 -69.253 1.00 83.26 O
ANISOU 174 O SER A 21 11272 10016 10346 -71 1898 -474 O
ATOM 175 CB SER A 21 36.867 25.008 -71.718 1.00 89.61 C
ANISOU 175 CB SER A 21 12246 10780 11019 79 2110 -261 C
ATOM 176 OG SER A 21 37.512 25.221 -72.959 1.00 94.37 O
ANISOU 176 OG SER A 21 12871 11387 11595 71 2182 -259 O
ATOM 177 N LYS A 22 35.700 23.234 -69.243 1.00 80.11 N
ANISOU 177 N LYS A 22 10905 9659 9871 78 1836 -314 N
ATOM 178 CA LYS A 22 35.561 23.217 -67.787 1.00 76.30 C
ANISOU 178 CA LYS A 22 10407 9147 9435 44 1795 -351 C
ATOM 179 C LYS A 22 36.137 21.956 -67.140 1.00 72.13 C
ANISOU 179 C LYS A 22 9780 8676 8950 -9 1667 -443 C
ATOM 180 O LYS A 22 36.823 22.030 -66.113 1.00 72.09 O
ANISOU 180 O LYS A 22 9753 8642 8996 -80 1663 -518 O
ATOM 181 CB LYS A 22 34.089 23.375 -67.399 1.00 78.57 C
ANISOU 181 CB LYS A 22 10722 9444 9686 130 1768 -256 C
ATOM 182 CG LYS A 22 33.531 24.784 -67.570 1.00 82.32 C
ANISOU 182 CG LYS A 22 11302 9840 10135 181 1906 -168 C
ATOM 183 CD LYS A 22 32.034 24.762 -67.859 1.00 81.07 C
ANISOU 183 CD LYS A 22 11157 9733 9912 297 1875 -52 C
ATOM 184 CE LYS A 22 31.259 24.023 -66.779 1.00 78.05 C
ANISOU 184 CE LYS A 22 10720 9392 9541 305 1758 -60 C
ATOM 185 NZ LYS A 22 29.999 23.438 -67.316 1.00 79.30 N
ANISOU 185 NZ LYS A 22 10847 9650 9631 398 1682 21 N
ATOM 186 N TYR A 23 35.864 20.807 -67.752 1.00 66.83 N
ANISOU 186 N TYR A 23 9050 8088 8254 24 1569 -438 N
ATOM 187 CA TYR A 23 36.139 19.513 -67.128 1.00 60.24 C
ANISOU 187 CA TYR A 23 8128 7305 7453 -4 1444 -504 C
ATOM 188 C TYR A 23 37.478 18.919 -67.526 1.00 58.31 C
ANISOU 188 C TYR A 23 7828 7082 7244 -64 1432 -594 C
ATOM 189 O TYR A 23 37.940 19.100 -68.656 1.00 58.65 O
ANISOU 189 O TYR A 23 7885 7131 7267 -65 1487 -595 O
ATOM 190 CB TYR A 23 35.041 18.521 -67.469 1.00 56.69 C
ANISOU 190 CB TYR A 23 7646 6930 6961 60 1347 -454 C
ATOM 191 CG TYR A 23 33.672 18.898 -66.970 1.00 56.55 C
ANISOU 191 CG TYR A 23 7664 6911 6910 121 1338 -372 C
ATOM 192 CD1 TYR A 23 33.345 18.781 -65.621 1.00 54.84 C
ANISOU 192 CD1 TYR A 23 7436 6675 6726 106 1289 -385 C
ATOM 193 CD2 TYR A 23 32.685 19.332 -67.856 1.00 57.35 C
ANISOU 193 CD2 TYR A 23 7805 7040 6942 196 1375 -278 C
ATOM 194 CE1 TYR A 23 32.080 19.097 -65.163 1.00 54.77 C
ANISOU 194 CE1 TYR A 23 7455 6668 6686 162 1281 -312 C
ATOM 195 CE2 TYR A 23 31.417 19.657 -67.409 1.00 55.51 C
ANISOU 195 CE2 TYR A 23 7598 6816 6677 258 1366 -201 C
ATOM 196 CZ TYR A 23 31.119 19.534 -66.063 1.00 56.75 C
ANISOU 196 CZ TYR A 23 7744 6947 6871 239 1319 -220 C
ATOM 197 OH TYR A 23 29.859 19.848 -65.611 1.00 59.89 O
ANISOU 197 OH TYR A 23 8164 7354 7237 299 1311 -146 O
ATOM 198 N ASN A 24 38.081 18.181 -66.596 1.00 52.89 N
ANISOU 198 N ASN A 24 7076 6412 6607 -107 1357 -667 N
ATOM 199 CA ASN A 24 39.291 17.439 -66.873 1.00 48.25 C
ANISOU 199 CA ASN A 24 6422 5857 6053 -152 1329 -751 C
ATOM 200 C ASN A 24 39.019 16.308 -67.854 1.00 50.31 C
ANISOU 200 C ASN A 24 6648 6178 6289 -111 1264 -740 C
ATOM 201 O ASN A 24 37.966 15.662 -67.797 1.00 48.27 O
ANISOU 201 O ASN A 24 6383 5951 6004 -61 1195 -693 O
ATOM 202 CB ASN A 24 39.889 16.895 -65.579 1.00 47.44 C
ANISOU 202 CB ASN A 24 6255 5766 6001 -194 1260 -819 C
ATOM 203 CG ASN A 24 41.246 16.262 -65.783 1.00 47.62 C
ANISOU 203 CG ASN A 24 6207 5824 6062 -238 1243 -906 C
ATOM 204 OD1 ASN A 24 41.371 15.239 -66.454 1.00 49.00 O
ANISOU 204 OD1 ASN A 24 6341 6039 6236 -212 1190 -917 O
ATOM 205 ND2 ASN A 24 42.273 16.860 -65.195 1.00 46.11 N
ANISOU 205 ND2 ASN A 24 5997 5619 5902 -306 1290 -972 N
ATOM 206 N SER A 25 39.987 16.076 -68.746 1.00 48.99 N
ANISOU 206 N SER A 25 6455 6028 6131 -137 1293 -789 N
ATOM 207 CA SER A 25 39.883 15.080 -69.806 1.00 46.96 C
ANISOU 207 CA SER A 25 6168 5825 5850 -109 1250 -791 C
ATOM 208 C SER A 25 39.624 13.662 -69.333 1.00 42.99 C
ANISOU 208 C SER A 25 5604 5362 5368 -91 1136 -814 C
ATOM 209 O SER A 25 39.164 12.826 -70.106 1.00 42.28 O
ANISOU 209 O SER A 25 5499 5314 5249 -62 1097 -803 O
ATOM 210 CB SER A 25 41.155 15.085 -70.653 1.00 47.82 C
ANISOU 210 CB SER A 25 6253 5939 5975 -152 1303 -855 C
ATOM 211 OG SER A 25 41.059 16.063 -71.657 1.00 52.28 O
ANISOU 211 OG SER A 25 6881 6485 6495 -146 1401 -813 O
ATOM 212 N ILE A 26 39.958 13.374 -68.084 1.00 41.48 N
ANISOU 212 N ILE A 26 5376 5158 5224 -111 1087 -850 N
ATOM 213 CA ILE A 26 39.720 12.040 -67.531 1.00 40.59 C
ANISOU 213 CA ILE A 26 5212 5074 5134 -91 985 -866 C
ATOM 214 C ILE A 26 38.247 11.591 -67.708 1.00 39.53 C
ANISOU 214 C ILE A 26 5103 4961 4953 -41 938 -800 C
ATOM 215 O ILE A 26 37.967 10.410 -67.914 1.00 40.52 O
ANISOU 215 O ILE A 26 5198 5117 5079 -24 876 -812 O
ATOM 216 CB ILE A 26 40.189 11.937 -66.065 1.00 38.88 C
ANISOU 216 CB ILE A 26 4960 4845 4967 -113 943 -900 C
ATOM 217 CG1 ILE A 26 40.333 10.466 -65.645 1.00 39.52 C
ANISOU 217 CG1 ILE A 26 4981 4953 5079 -92 851 -929 C
ATOM 218 CG2 ILE A 26 39.258 12.722 -65.145 1.00 38.07 C
ANISOU 218 CG2 ILE A 26 4903 4714 4847 -105 946 -846 C
ATOM 219 CD1 ILE A 26 41.131 10.266 -64.367 1.00 41.02 C
ANISOU 219 CD1 ILE A 26 5120 5147 5316 -112 813 -972 C
ATOM 220 N LEU A 27 37.327 12.550 -67.705 1.00 39.39 N
ANISOU 220 N LEU A 27 5142 4930 4894 -20 976 -732 N
ATOM 221 CA LEU A 27 35.912 12.257 -67.912 1.00 39.19 C
ANISOU 221 CA LEU A 27 5136 4937 4816 26 939 -667 C
ATOM 222 C LEU A 27 35.590 11.677 -69.293 1.00 39.52 C
ANISOU 222 C LEU A 27 5170 5036 4809 45 937 -659 C
ATOM 223 O LEU A 27 34.622 10.928 -69.442 1.00 40.60 O
ANISOU 223 O LEU A 27 5296 5218 4912 70 883 -637 O
ATOM 224 CB LEU A 27 35.060 13.487 -67.653 1.00 38.75 C
ANISOU 224 CB LEU A 27 5141 4858 4724 53 989 -593 C
ATOM 225 CG LEU A 27 35.068 14.054 -66.237 1.00 38.94 C
ANISOU 225 CG LEU A 27 5178 4832 4785 36 988 -593 C
ATOM 226 CD1 LEU A 27 34.170 15.280 -66.188 1.00 38.54 C
ANISOU 226 CD1 LEU A 27 5192 4754 4693 70 1053 -515 C
ATOM 227 CD2 LEU A 27 34.634 13.017 -65.212 1.00 37.53 C
ANISOU 227 CD2 LEU A 27 4958 4669 4629 39 889 -606 C
ATOM 228 N ASN A 28 36.389 12.027 -70.296 1.00 39.03 N
ANISOU 228 N ASN A 28 5114 4975 4739 29 1000 -682 N
ATOM 229 CA ASN A 28 36.253 11.421 -71.625 1.00 39.39 C
ANISOU 229 CA ASN A 28 5146 5079 4740 38 1000 -687 C
ATOM 230 C ASN A 28 36.443 9.884 -71.657 1.00 38.91 C
ANISOU 230 C ASN A 28 5030 5046 4707 24 927 -749 C
ATOM 231 O ASN A 28 35.790 9.200 -72.441 1.00 37.66 O
ANISOU 231 O ASN A 28 4862 4943 4502 36 904 -744 O
ATOM 232 CB ASN A 28 37.208 12.079 -72.615 1.00 41.41 C
ANISOU 232 CB ASN A 28 5417 5326 4988 17 1084 -707 C
ATOM 233 CG ASN A 28 36.870 13.535 -72.875 1.00 43.84 C
ANISOU 233 CG ASN A 28 5792 5610 5255 39 1170 -635 C
ATOM 234 OD1 ASN A 28 35.774 14.002 -72.563 1.00 43.79 O
ANISOU 234 OD1 ASN A 28 5817 5609 5209 81 1166 -562 O
ATOM 235 ND2 ASN A 28 37.810 14.257 -73.469 1.00 45.24 N
ANISOU 235 ND2 ASN A 28 5991 5759 5439 13 1254 -654 N
ATOM 236 N ILE A 29 37.358 9.363 -70.827 1.00 37.39 N
ANISOU 236 N ILE A 29 4802 4816 4588 0 898 -808 N
ATOM 237 CA ILE A 29 37.607 7.916 -70.744 1.00 35.60 C
ANISOU 237 CA ILE A 29 4529 4600 4396 -5 837 -863 C
ATOM 238 C ILE A 29 36.345 7.198 -70.282 1.00 34.20 C
ANISOU 238 C ILE A 29 4354 4443 4196 15 773 -831 C
ATOM 239 O ILE A 29 35.859 6.273 -70.957 1.00 33.10 O
ANISOU 239 O ILE A 29 4203 4342 4029 15 750 -846 O
ATOM 240 CB ILE A 29 38.797 7.588 -69.806 1.00 36.08 C
ANISOU 240 CB ILE A 29 4549 4621 4536 -23 818 -919 C
ATOM 241 CG1 ILE A 29 40.079 8.253 -70.329 1.00 36.22 C
ANISOU 241 CG1 ILE A 29 4557 4629 4574 -52 885 -961 C
ATOM 242 CG2 ILE A 29 39.017 6.084 -69.719 1.00 35.67 C
ANISOU 242 CG2 ILE A 29 4457 4573 4522 -17 764 -966 C
ATOM 243 CD1 ILE A 29 41.194 8.308 -69.312 1.00 36.88 C
ANISOU 243 CD1 ILE A 29 4600 4689 4723 -72 876 -1007 C
ATOM 244 N ALA A 30 35.792 7.678 -69.167 1.00 33.23 N
ANISOU 244 N ALA A 30 4249 4296 4080 28 749 -790 N
ATOM 245 CA ALA A 30 34.552 7.165 -68.602 1.00 33.21 C
ANISOU 245 CA ALA A 30 4252 4311 4055 46 693 -755 C
ATOM 246 C ALA A 30 33.369 7.248 -69.578 1.00 33.97 C
ANISOU 246 C ALA A 30 4365 4473 4067 64 701 -711 C
ATOM 247 O ALA A 30 32.609 6.295 -69.711 1.00 36.89 O
ANISOU 247 O ALA A 30 4721 4880 4415 62 659 -718 O
ATOM 248 CB ALA A 30 34.231 7.886 -67.292 1.00 31.57 C
ANISOU 248 CB ALA A 30 4062 4067 3863 55 680 -716 C
ATOM 249 N LEU A 31 33.224 8.378 -70.261 1.00 33.82 N
ANISOU 249 N LEU A 31 4376 4473 4000 80 760 -665 N
ATOM 250 CA LEU A 31 32.196 8.525 -71.299 1.00 34.44 C
ANISOU 250 CA LEU A 31 4464 4630 3990 104 773 -620 C
ATOM 251 C LEU A 31 32.344 7.428 -72.348 1.00 34.48 C
ANISOU 251 C LEU A 31 4438 4688 3975 79 761 -674 C
ATOM 252 O LEU A 31 31.347 6.857 -72.815 1.00 34.00 O
ANISOU 252 O LEU A 31 4364 4700 3855 82 733 -665 O
ATOM 253 CB LEU A 31 32.295 9.913 -71.988 1.00 34.23 C
ANISOU 253 CB LEU A 31 4478 4608 3920 129 853 -564 C
ATOM 254 CG LEU A 31 31.695 11.134 -71.258 1.00 35.94 C
ANISOU 254 CG LEU A 31 4738 4793 4124 166 882 -488 C
ATOM 255 CD1 LEU A 31 32.030 12.445 -71.980 1.00 35.35 C
ANISOU 255 CD1 LEU A 31 4710 4703 4019 187 976 -442 C
ATOM 256 CD2 LEU A 31 30.180 10.980 -71.065 1.00 34.30 C
ANISOU 256 CD2 LEU A 31 4526 4647 3855 204 838 -430 C
ATOM 257 N LYS A 32 33.599 7.171 -72.723 1.00 35.18 N
ANISOU 257 N LYS A 32 4513 4743 4111 53 786 -735 N
ATOM 258 CA LYS A 32 33.976 6.175 -73.717 1.00 36.96 C
ANISOU 258 CA LYS A 32 4710 5003 4329 26 787 -797 C
ATOM 259 C LYS A 32 33.548 4.779 -73.259 1.00 36.28 C
ANISOU 259 C LYS A 32 4599 4918 4267 9 726 -839 C
ATOM 260 O LYS A 32 32.723 4.124 -73.908 1.00 35.78 O
ANISOU 260 O LYS A 32 4526 4921 4148 -2 711 -848 O
ATOM 261 CB LYS A 32 35.501 6.256 -73.935 1.00 40.47 C
ANISOU 261 CB LYS A 32 5144 5398 4835 4 827 -852 C
ATOM 262 CG LYS A 32 36.145 5.105 -74.687 1.00 42.43 C
ANISOU 262 CG LYS A 32 5360 5657 5103 -23 827 -930 C
ATOM 263 CD LYS A 32 35.934 5.247 -76.174 1.00 45.24 C
ANISOU 263 CD LYS A 32 5719 6086 5381 -32 869 -930 C
ATOM 264 CE LYS A 32 36.628 4.126 -76.932 1.00 47.65 C
ANISOU 264 CE LYS A 32 5995 6398 5709 -64 877 -1014 C
ATOM 265 NZ LYS A 32 36.283 4.192 -78.382 1.00 51.97 N
ANISOU 265 NZ LYS A 32 6543 7030 6170 -77 913 -1015 N
ATOM 266 N ASN A 33 34.067 4.372 -72.102 1.00 36.19 N
ANISOU 266 N ASN A 33 4579 4835 4335 7 694 -862 N
ATOM 267 CA ASN A 33 33.701 3.112 -71.456 1.00 35.57 C
ANISOU 267 CA ASN A 33 4486 4738 4288 -1 641 -893 C
ATOM 268 C ASN A 33 32.200 2.977 -71.231 1.00 36.03 C
ANISOU 268 C ASN A 33 4555 4845 4288 2 606 -851 C
ATOM 269 O ASN A 33 31.665 1.870 -71.293 1.00 36.62 O
ANISOU 269 O ASN A 33 4620 4936 4357 -18 580 -884 O
ATOM 270 CB ASN A 33 34.455 2.936 -70.128 1.00 34.84 C
ANISOU 270 CB ASN A 33 4386 4569 4281 8 614 -904 C
ATOM 271 CG ASN A 33 35.970 3.090 -70.280 1.00 36.10 C
ANISOU 271 CG ASN A 33 4526 4693 4497 3 646 -948 C
ATOM 272 OD1 ASN A 33 36.541 2.805 -71.336 1.00 37.03 O
ANISOU 272 OD1 ASN A 33 4631 4828 4609 -10 681 -990 O
ATOM 273 ND2 ASN A 33 36.621 3.546 -69.224 1.00 35.69 N
ANISOU 273 ND2 ASN A 33 4466 4598 4495 13 636 -941 N
ATOM 274 N PHE A 34 31.518 4.097 -70.990 1.00 34.48 N
ANISOU 274 N PHE A 34 4378 4673 4048 29 612 -781 N
ATOM 275 CA PHE A 34 30.048 4.087 -70.911 1.00 35.05 C
ANISOU 275 CA PHE A 34 4454 4810 4053 38 584 -737 C
ATOM 276 C PHE A 34 29.406 3.657 -72.235 1.00 34.38 C
ANISOU 276 C PHE A 34 4351 4824 3885 21 595 -752 C
ATOM 277 O PHE A 34 28.575 2.747 -72.270 1.00 34.70 O
ANISOU 277 O PHE A 34 4376 4909 3898 -3 564 -776 O
ATOM 278 CB PHE A 34 29.498 5.450 -70.440 1.00 35.52 C
ANISOU 278 CB PHE A 34 4539 4874 4082 79 597 -654 C
ATOM 279 CG PHE A 34 27.990 5.499 -70.327 1.00 36.91 C
ANISOU 279 CG PHE A 34 4712 5122 4187 96 569 -604 C
ATOM 280 CD1 PHE A 34 27.267 4.396 -69.885 1.00 38.11 C
ANISOU 280 CD1 PHE A 34 4846 5292 4339 71 519 -633 C
ATOM 281 CD2 PHE A 34 27.298 6.663 -70.626 1.00 37.85 C
ANISOU 281 CD2 PHE A 34 4848 5291 4240 141 597 -527 C
ATOM 282 CE1 PHE A 34 25.877 4.450 -69.780 1.00 37.90 C
ANISOU 282 CE1 PHE A 34 4812 5343 4246 82 494 -592 C
ATOM 283 CE2 PHE A 34 25.917 6.723 -70.524 1.00 35.84 C
ANISOU 283 CE2 PHE A 34 4584 5114 3918 163 572 -480 C
ATOM 284 CZ PHE A 34 25.208 5.624 -70.104 1.00 36.76 C
ANISOU 284 CZ PHE A 34 4675 5257 4033 131 518 -515 C
ATOM 285 N ARG A 35 29.807 4.302 -73.320 1.00 34.22 N
ANISOU 285 N ARG A 35 4334 4842 3824 29 643 -743 N
ATOM 286 CA ARG A 35 29.348 3.910 -74.652 1.00 36.33 C
ANISOU 286 CA ARG A 35 4580 5213 4010 9 658 -763 C
ATOM 287 C ARG A 35 29.723 2.451 -75.017 1.00 35.60 C
ANISOU 287 C ARG A 35 4465 5112 3948 -45 648 -859 C
ATOM 288 O ARG A 35 28.927 1.751 -75.647 1.00 35.96 O
ANISOU 288 O ARG A 35 4490 5241 3931 -76 638 -887 O
ATOM 289 CB ARG A 35 29.874 4.878 -75.729 1.00 36.39 C
ANISOU 289 CB ARG A 35 4598 5253 3973 29 716 -736 C
ATOM 290 CG ARG A 35 29.425 6.334 -75.566 1.00 35.80 C
ANISOU 290 CG ARG A 35 4554 5191 3858 87 743 -637 C
ATOM 291 CD ARG A 35 29.766 7.161 -76.806 1.00 37.26 C
ANISOU 291 CD ARG A 35 4751 5424 3981 107 806 -607 C
ATOM 292 NE ARG A 35 31.213 7.217 -77.087 1.00 37.02 N
ANISOU 292 NE ARG A 35 4729 5319 4014 81 848 -658 N
ATOM 293 CZ ARG A 35 32.051 8.128 -76.575 1.00 37.74 C
ANISOU 293 CZ ARG A 35 4853 5322 4163 94 887 -639 C
ATOM 294 NH1 ARG A 35 31.606 9.075 -75.742 1.00 37.61 N
ANISOU 294 NH1 ARG A 35 4867 5269 4150 133 894 -570 N
ATOM 295 NH2 ARG A 35 33.338 8.094 -76.887 1.00 36.81 N
ANISOU 295 NH2 ARG A 35 4734 5153 4097 65 924 -693 N
ATOM 296 N LEU A 36 30.926 2.014 -74.623 1.00 35.60 N
ANISOU 296 N LEU A 36 4469 5015 4042 -55 655 -908 N
ATOM 297 CA LEU A 36 31.404 0.645 -74.900 1.00 33.89 C
ANISOU 297 CA LEU A 36 4238 4771 3866 -98 656 -996 C
ATOM 298 C LEU A 36 30.530 -0.370 -74.184 1.00 32.74 C
ANISOU 298 C LEU A 36 4090 4617 3729 -119 615 -1014 C
ATOM 299 O LEU A 36 30.103 -1.348 -74.770 1.00 32.80 O
ANISOU 299 O LEU A 36 4087 4664 3708 -164 620 -1070 O
ATOM 300 CB LEU A 36 32.867 0.485 -74.470 1.00 32.80 C
ANISOU 300 CB LEU A 36 4100 4533 3829 -90 671 -1032 C
ATOM 301 CG LEU A 36 34.031 0.451 -75.474 1.00 35.22 C
ANISOU 301 CG LEU A 36 4396 4835 4152 -103 721 -1083 C
ATOM 302 CD1 LEU A 36 33.675 0.840 -76.919 1.00 34.76 C
ANISOU 302 CD1 LEU A 36 4332 4875 3998 -120 758 -1081 C
ATOM 303 CD2 LEU A 36 35.241 1.239 -74.964 1.00 34.73 C
ANISOU 303 CD2 LEU A 36 4334 4706 4154 -77 738 -1070 C
ATOM 304 N CYS A 37 30.255 -0.110 -72.911 1.00 33.18 N
ANISOU 304 N CYS A 37 4159 4622 3823 -93 578 -970 N
ATOM 305 CA CYS A 37 29.398 -0.969 -72.081 1.00 34.28 C
ANISOU 305 CA CYS A 37 4304 4747 3973 -110 539 -978 C
ATOM 306 C CYS A 37 27.990 -1.133 -72.692 1.00 35.09 C
ANISOU 306 C CYS A 37 4392 4963 3975 -139 531 -973 C
ATOM 307 O CYS A 37 27.424 -2.240 -72.699 1.00 33.01 O
ANISOU 307 O CYS A 37 4125 4712 3705 -185 523 -1024 O
ATOM 308 CB CYS A 37 29.284 -0.383 -70.660 1.00 34.19 C
ANISOU 308 CB CYS A 37 4308 4679 4003 -72 504 -918 C
ATOM 309 SG CYS A 37 28.313 -1.360 -69.487 1.00 39.03 S
ANISOU 309 SG CYS A 37 4931 5262 4635 -89 458 -920 S
ATOM 310 N LYS A 38 27.431 -0.025 -73.190 1.00 35.49 N
ANISOU 310 N LYS A 38 4435 5101 3947 -112 536 -912 N
ATOM 311 CA LYS A 38 26.103 -0.052 -73.787 1.00 37.54 C
ANISOU 311 CA LYS A 38 4671 5490 4101 -130 526 -900 C
ATOM 312 C LYS A 38 26.039 -0.912 -75.040 1.00 39.14 C
ANISOU 312 C LYS A 38 4849 5769 4252 -188 551 -975 C
ATOM 313 O LYS A 38 25.003 -1.516 -75.319 1.00 41.77 O
ANISOU 313 O LYS A 38 5158 6190 4519 -231 539 -1003 O
ATOM 314 CB LYS A 38 25.588 1.367 -74.059 1.00 39.30 C
ANISOU 314 CB LYS A 38 4891 5789 4251 -73 532 -809 C
ATOM 315 CG LYS A 38 25.095 2.076 -72.794 1.00 39.27 C
ANISOU 315 CG LYS A 38 4906 5742 4271 -29 503 -737 C
ATOM 316 CD LYS A 38 24.441 3.401 -73.115 1.00 39.48 C
ANISOU 316 CD LYS A 38 4933 5848 4220 29 518 -646 C
ATOM 317 CE LYS A 38 25.464 4.485 -73.403 1.00 39.61 C
ANISOU 317 CE LYS A 38 4978 5810 4261 70 564 -609 C
ATOM 318 NZ LYS A 38 24.768 5.773 -73.676 1.00 40.96 N
ANISOU 318 NZ LYS A 38 5157 6047 4356 134 587 -513 N
ATOM 319 N LYS A 39 27.153 -0.980 -75.778 1.00 39.19 N
ANISOU 319 N LYS A 39 4859 5742 4287 -195 589 -1015 N
ATOM 320 CA LYS A 39 27.222 -1.744 -77.033 1.00 40.03 C
ANISOU 320 CA LYS A 39 4945 5918 4347 -251 621 -1092 C
ATOM 321 C LYS A 39 27.459 -3.233 -76.818 1.00 39.69 C
ANISOU 321 C LYS A 39 4909 5804 4366 -311 629 -1185 C
ATOM 322 O LYS A 39 27.075 -4.041 -77.642 1.00 42.19 O
ANISOU 322 O LYS A 39 5208 6188 4632 -373 650 -1255 O
ATOM 323 CB LYS A 39 28.313 -1.195 -77.939 1.00 41.15 C
ANISOU 323 CB LYS A 39 5088 6053 4491 -235 664 -1096 C
ATOM 324 CG LYS A 39 28.023 0.173 -78.512 1.00 42.73 C
ANISOU 324 CG LYS A 39 5283 6341 4609 -186 675 -1012 C
ATOM 325 CD LYS A 39 29.209 0.685 -79.321 1.00 45.23 C
ANISOU 325 CD LYS A 39 5608 6634 4940 -174 724 -1020 C
ATOM 326 CE LYS A 39 28.932 2.067 -79.904 1.00 46.59 C
ANISOU 326 CE LYS A 39 5785 6884 5030 -121 745 -930 C
ATOM 327 NZ LYS A 39 30.204 2.771 -80.225 1.00 49.97 N
ANISOU 327 NZ LYS A 39 6236 7245 5503 -100 793 -923 N
ATOM 328 N HIS A 40 28.121 -3.581 -75.723 1.00 39.49 N
ANISOU 328 N HIS A 40 4911 5645 4449 -290 618 -1187 N
ATOM 329 CA HIS A 40 28.382 -4.966 -75.382 1.00 40.33 C
ANISOU 329 CA HIS A 40 5033 5667 4623 -331 631 -1263 C
ATOM 330 C HIS A 40 27.136 -5.705 -74.988 1.00 44.54 C
ANISOU 330 C HIS A 40 5566 6234 5121 -378 612 -1282 C
ATOM 331 O HIS A 40 26.566 -5.460 -73.924 1.00 45.92 O
ANISOU 331 O HIS A 40 5751 6386 5309 -353 572 -1229 O
ATOM 332 CB HIS A 40 29.402 -5.048 -74.253 1.00 37.01 C
ANISOU 332 CB HIS A 40 4637 5106 4320 -283 620 -1244 C
ATOM 333 CG HIS A 40 29.784 -6.463 -73.885 1.00 36.65 C
ANISOU 333 CG HIS A 40 4613 4962 4350 -309 641 -1312 C
ATOM 334 ND1 HIS A 40 30.043 -6.841 -72.614 1.00 35.18 N
ANISOU 334 ND1 HIS A 40 4449 4672 4245 -276 619 -1290 N
ATOM 335 CD2 HIS A 40 29.913 -7.619 -74.673 1.00 35.49 C
ANISOU 335 CD2 HIS A 40 4471 4806 4207 -366 690 -1402 C
ATOM 336 CE1 HIS A 40 30.343 -8.155 -72.594 1.00 34.81 C
ANISOU 336 CE1 HIS A 40 4423 4549 4252 -303 653 -1355 C
ATOM 337 NE2 HIS A 40 30.255 -8.627 -73.852 1.00 34.59 N
ANISOU 337 NE2 HIS A 40 4386 4575 4179 -360 699 -1426 N
ATOM 338 N LYS A 41 26.721 -6.647 -75.826 1.00 51.43 N
ANISOU 338 N LYS A 41 6429 7160 5949 -452 644 -1364 N
ATOM 339 CA LYS A 41 25.594 -7.513 -75.504 1.00 56.06 C
ANISOU 339 CA LYS A 41 7017 7775 6506 -514 638 -1402 C
ATOM 340 C LYS A 41 26.092 -8.762 -74.778 1.00 58.99 C
ANISOU 340 C LYS A 41 7433 7998 6983 -533 664 -1455 C
ATOM 341 O LYS A 41 26.724 -9.635 -75.373 1.00 63.99 O
ANISOU 341 O LYS A 41 8079 8584 7650 -570 716 -1533 O
ATOM 342 CB LYS A 41 24.802 -7.877 -76.770 1.00 59.38 C
ANISOU 342 CB LYS A 41 7401 8342 6815 -594 664 -1468 C
ATOM 343 CG LYS A 41 24.438 -6.684 -77.663 1.00 60.59 C
ANISOU 343 CG LYS A 41 7511 8651 6859 -566 648 -1414 C
ATOM 344 CD LYS A 41 23.451 -5.735 -76.981 1.00 62.20 C
ANISOU 344 CD LYS A 41 7698 8922 7012 -517 594 -1318 C
ATOM 345 CE LYS A 41 23.209 -4.477 -77.808 1.00 62.36 C
ANISOU 345 CE LYS A 41 7682 9076 6933 -469 585 -1249 C
ATOM 346 NZ LYS A 41 22.659 -3.358 -76.988 1.00 64.76 N
ANISOU 346 NZ LYS A 41 7986 9394 7223 -393 543 -1139 N
ATOM 347 N THR A 42 25.826 -8.811 -73.480 1.00 61.31 N
ANISOU 347 N THR A 42 7750 8217 7326 -503 630 -1408 N
ATOM 348 CA THR A 42 26.253 -9.907 -72.620 1.00 64.87 C
ANISOU 348 CA THR A 42 8246 8524 7876 -505 650 -1438 C
ATOM 349 C THR A 42 25.047 -10.732 -72.172 1.00 70.88 C
ANISOU 349 C THR A 42 9023 9297 8610 -571 653 -1469 C
ATOM 350 O THR A 42 23.968 -10.183 -71.909 1.00 65.76 O
ANISOU 350 O THR A 42 8351 8740 7892 -580 613 -1429 O
ATOM 351 CB THR A 42 27.005 -9.383 -71.367 1.00 66.02 C
ANISOU 351 CB THR A 42 8409 8567 8106 -416 611 -1359 C
ATOM 352 OG1 THR A 42 26.592 -10.118 -70.208 1.00 63.27 O
ANISOU 352 OG1 THR A 42 8097 8137 7805 -419 602 -1350 O
ATOM 353 CG2 THR A 42 26.716 -7.901 -71.130 1.00 61.21 C
ANISOU 353 CG2 THR A 42 7773 8033 7450 -366 559 -1272 C
ATOM 354 N LYS A 43 25.243 -12.047 -72.070 1.00 76.08 N
ANISOU 354 N LYS A 43 9723 9859 9325 -614 707 -1539 N
ATOM 355 CA LYS A 43 24.178 -12.968 -71.652 1.00 83.21 C
ANISOU 355 CA LYS A 43 10650 10754 10210 -688 725 -1581 C
ATOM 356 C LYS A 43 23.843 -12.868 -70.152 1.00 84.16 C
ANISOU 356 C LYS A 43 10797 10803 10375 -642 681 -1507 C
ATOM 357 O LYS A 43 22.669 -12.951 -69.767 1.00 83.05 O
ANISOU 357 O LYS A 43 10653 10718 10184 -688 664 -1505 O
ATOM 358 CB LYS A 43 24.544 -14.415 -72.015 1.00 85.29 C
ANISOU 358 CB LYS A 43 10959 10920 10525 -748 811 -1680 C
ATOM 359 CG LYS A 43 23.362 -15.262 -72.461 1.00 86.83 C
ANISOU 359 CG LYS A 43 11157 11182 10653 -869 854 -1768 C
ATOM 360 CD LYS A 43 23.781 -16.697 -72.747 1.00 88.56 C
ANISOU 360 CD LYS A 43 11433 11282 10933 -928 951 -1866 C
ATOM 361 CE LYS A 43 23.240 -17.185 -74.084 1.00 87.73 C
ANISOU 361 CE LYS A 43 11302 11287 10742 -1047 1008 -1981 C
ATOM 362 NZ LYS A 43 21.761 -17.056 -74.188 1.00 88.59 N
ANISOU 362 NZ LYS A 43 11373 11546 10741 -1134 985 -2004 N
ATOM 363 N LYS A 44 24.876 -12.673 -69.323 1.00 85.41 N
ANISOU 363 N LYS A 44 10978 10847 10623 -554 663 -1449 N
ATOM 364 CA LYS A 44 24.740 -12.749 -67.856 1.00 86.26 C
ANISOU 364 CA LYS A 44 11119 10871 10785 -509 630 -1386 C
ATOM 365 C LYS A 44 24.447 -11.407 -67.159 1.00 82.26 C
ANISOU 365 C LYS A 44 10581 10423 10249 -451 553 -1292 C
ATOM 366 O LYS A 44 25.109 -10.396 -67.435 1.00 73.76 O
ANISOU 366 O LYS A 44 9475 9380 9169 -398 528 -1252 O
ATOM 367 CB LYS A 44 25.958 -13.448 -67.225 1.00 88.60 C
ANISOU 367 CB LYS A 44 11458 11012 11192 -448 657 -1378 C
ATOM 368 CG LYS A 44 26.033 -14.948 -67.511 1.00 92.95 C
ANISOU 368 CG LYS A 44 12060 11471 11784 -501 740 -1459 C
ATOM 369 CD LYS A 44 25.064 -15.747 -66.646 1.00 94.74 C
ANISOU 369 CD LYS A 44 12333 11647 12014 -545 755 -1463 C
ATOM 370 CE LYS A 44 24.731 -17.103 -67.262 1.00 99.69 C
ANISOU 370 CE LYS A 44 13005 12225 12646 -637 849 -1565 C
ATOM 371 NZ LYS A 44 25.886 -18.047 -67.272 1.00101.31 N
ANISOU 371 NZ LYS A 44 13259 12285 12947 -593 917 -1589 N
ATOM 372 N PRO A 45 23.451 -11.411 -66.244 1.00 80.22 N
ANISOU 372 N PRO A 45 10333 10174 9970 -466 523 -1259 N
ATOM 373 CA PRO A 45 22.875 -10.261 -65.542 1.00 75.36 C
ANISOU 373 CA PRO A 45 9693 9620 9318 -427 459 -1178 C
ATOM 374 C PRO A 45 23.848 -9.168 -65.099 1.00 69.27 C
ANISOU 374 C PRO A 45 8909 8823 8585 -337 421 -1106 C
ATOM 375 O PRO A 45 24.994 -9.440 -64.733 1.00 67.06 O
ANISOU 375 O PRO A 45 8649 8446 8385 -291 430 -1101 O
ATOM 376 CB PRO A 45 22.202 -10.906 -64.333 1.00 79.73 C
ANISOU 376 CB PRO A 45 10284 10111 9896 -442 451 -1162 C
ATOM 377 CG PRO A 45 21.722 -12.219 -64.860 1.00 81.04 C
ANISOU 377 CG PRO A 45 10476 10261 10053 -531 513 -1251 C
ATOM 378 CD PRO A 45 22.725 -12.654 -65.905 1.00 82.30 C
ANISOU 378 CD PRO A 45 10638 10388 10241 -534 563 -1309 C
ATOM 379 N VAL A 46 23.340 -7.942 -65.092 1.00 64.56 N
ANISOU 379 N VAL A 46 8281 8316 7932 -314 381 -1052 N
ATOM 380 CA VAL A 46 24.148 -6.752 -64.926 1.00 61.21 C
ANISOU 380 CA VAL A 46 7841 7889 7526 -245 357 -994 C
ATOM 381 C VAL A 46 24.186 -6.297 -63.459 1.00 59.62 C
ANISOU 381 C VAL A 46 7656 7632 7365 -197 315 -927 C
ATOM 382 O VAL A 46 23.142 -6.013 -62.852 1.00 65.06 O
ANISOU 382 O VAL A 46 8343 8358 8015 -206 288 -893 O
ATOM 383 CB VAL A 46 23.652 -5.606 -65.864 1.00 59.16 C
ANISOU 383 CB VAL A 46 7542 7755 7179 -242 351 -971 C
ATOM 384 CG1 VAL A 46 23.386 -6.138 -67.268 1.00 53.79 C
ANISOU 384 CG1 VAL A 46 6843 7152 6443 -300 389 -1039 C
ATOM 385 CG2 VAL A 46 22.400 -4.945 -65.320 1.00 55.06 C
ANISOU 385 CG2 VAL A 46 7011 7309 6601 -239 316 -918 C
ATOM 386 N GLN A 47 25.383 -6.278 -62.882 1.00 53.22 N
ANISOU 386 N GLN A 47 6855 6735 6628 -148 311 -911 N
ATOM 387 CA GLN A 47 25.594 -5.645 -61.580 1.00 52.42 C
ANISOU 387 CA GLN A 47 6760 6597 6560 -101 271 -849 C
ATOM 388 C GLN A 47 26.147 -4.211 -61.753 1.00 45.76 C
ANISOU 388 C GLN A 47 5892 5790 5705 -62 261 -811 C
ATOM 389 O GLN A 47 27.285 -4.024 -62.190 1.00 43.13 O
ANISOU 389 O GLN A 47 5546 5435 5405 -40 279 -827 O
ATOM 390 CB GLN A 47 26.520 -6.503 -60.712 1.00 56.69 C
ANISOU 390 CB GLN A 47 7323 7033 7182 -70 271 -852 C
ATOM 391 CG GLN A 47 25.810 -7.581 -59.887 1.00 62.48 C
ANISOU 391 CG GLN A 47 8093 7715 7929 -92 269 -853 C
ATOM 392 CD GLN A 47 25.283 -7.066 -58.552 1.00 61.20 C
ANISOU 392 CD GLN A 47 7939 7551 7763 -72 224 -792 C
ATOM 393 OE1 GLN A 47 25.076 -5.864 -58.371 1.00 64.01 O
ANISOU 393 OE1 GLN A 47 8273 7960 8087 -57 197 -753 O
ATOM 394 NE2 GLN A 47 25.069 -7.976 -57.610 1.00 60.60 N
ANISOU 394 NE2 GLN A 47 7898 7409 7717 -72 222 -782 N
ATOM 395 N ILE A 48 25.327 -3.207 -61.449 1.00 41.64 N
ANISOU 395 N ILE A 48 5363 5323 5133 -55 240 -763 N
ATOM 396 CA ILE A 48 25.684 -1.820 -61.780 1.00 39.37 C
ANISOU 396 CA ILE A 48 5060 5073 4826 -25 246 -728 C
ATOM 397 C ILE A 48 27.004 -1.365 -61.114 1.00 37.86 C
ANISOU 397 C ILE A 48 4867 4818 4699 11 242 -717 C
ATOM 398 O ILE A 48 27.876 -0.792 -61.782 1.00 35.99 O
ANISOU 398 O ILE A 48 4617 4587 4471 23 267 -727 O
ATOM 399 CB ILE A 48 24.502 -0.824 -61.582 1.00 38.08 C
ANISOU 399 CB ILE A 48 4893 4977 4597 -18 232 -675 C
ATOM 400 CG1 ILE A 48 23.710 -0.664 -62.878 1.00 40.86 C
ANISOU 400 CG1 ILE A 48 5225 5428 4869 -37 253 -684 C
ATOM 401 CG2 ILE A 48 25.002 0.580 -61.285 1.00 35.08 C
ANISOU 401 CG2 ILE A 48 4514 4591 4223 21 239 -628 C
ATOM 402 CD1 ILE A 48 23.066 -1.911 -63.399 1.00 43.49 C
ANISOU 402 CD1 ILE A 48 5553 5793 5177 -90 257 -738 C
ATOM 403 N LEU A 49 27.163 -1.664 -59.826 1.00 37.35 N
ANISOU 403 N LEU A 49 4813 4699 4676 25 212 -699 N
ATOM 404 CA LEU A 49 28.395 -1.297 -59.090 1.00 37.45 C
ANISOU 404 CA LEU A 49 4816 4667 4744 57 204 -691 C
ATOM 405 C LEU A 49 29.610 -1.837 -59.816 1.00 36.62 C
ANISOU 405 C LEU A 49 4695 4537 4681 65 230 -737 C
ATOM 406 O LEU A 49 30.560 -1.106 -60.071 1.00 35.44 O
ANISOU 406 O LEU A 49 4525 4392 4546 78 245 -743 O
ATOM 407 CB LEU A 49 28.366 -1.822 -57.651 1.00 36.11 C
ANISOU 407 CB LEU A 49 4658 4451 4609 71 167 -669 C
ATOM 408 CG LEU A 49 28.007 -0.943 -56.435 1.00 36.74 C
ANISOU 408 CG LEU A 49 4742 4536 4679 81 139 -621 C
ATOM 409 CD1 LEU A 49 27.436 0.421 -56.790 1.00 34.92 C
ANISOU 409 CD1 LEU A 49 4512 4354 4401 76 154 -595 C
ATOM 410 CD2 LEU A 49 27.076 -1.687 -55.469 1.00 36.62 C
ANISOU 410 CD2 LEU A 49 4751 4502 4660 73 109 -600 C
ATOM 411 N ALA A 50 29.542 -3.113 -60.194 1.00 37.33 N
ANISOU 411 N ALA A 50 4795 4600 4788 52 240 -773 N
ATOM 412 CA ALA A 50 30.612 -3.774 -60.950 1.00 36.22 C
ANISOU 412 CA ALA A 50 4641 4432 4686 60 271 -822 C
ATOM 413 C ALA A 50 30.868 -3.179 -62.344 1.00 36.31 C
ANISOU 413 C ALA A 50 4637 4493 4666 43 307 -849 C
ATOM 414 O ALA A 50 32.018 -3.088 -62.771 1.00 38.95 O
ANISOU 414 O ALA A 50 4951 4815 5034 58 328 -875 O
ATOM 415 CB ALA A 50 30.341 -5.273 -61.051 1.00 37.16 C
ANISOU 415 CB ALA A 50 4785 4505 4828 46 285 -855 C
ATOM 416 N LEU A 51 29.814 -2.801 -63.066 1.00 34.69 N
ANISOU 416 N LEU A 51 4437 4349 4393 12 316 -844 N
ATOM 417 CA LEU A 51 30.010 -2.181 -64.386 1.00 34.36 C
ANISOU 417 CA LEU A 51 4380 4361 4312 1 350 -861 C
ATOM 418 C LEU A 51 30.668 -0.837 -64.221 1.00 32.26 C
ANISOU 418 C LEU A 51 4104 4102 4049 26 356 -828 C
ATOM 419 O LEU A 51 31.586 -0.479 -64.958 1.00 34.96 O
ANISOU 419 O LEU A 51 4431 4448 4402 30 387 -852 O
ATOM 420 CB LEU A 51 28.692 -2.006 -65.157 1.00 32.70 C
ANISOU 420 CB LEU A 51 4173 4231 4018 -29 356 -854 C
ATOM 421 CG LEU A 51 28.050 -3.221 -65.804 1.00 34.52 C
ANISOU 421 CG LEU A 51 4407 4481 4225 -74 369 -905 C
ATOM 422 CD1 LEU A 51 26.739 -2.814 -66.488 1.00 33.92 C
ANISOU 422 CD1 LEU A 51 4322 4511 4054 -101 368 -890 C
ATOM 423 CD2 LEU A 51 29.023 -3.869 -66.790 1.00 35.41 C
ANISOU 423 CD2 LEU A 51 4512 4573 4365 -87 409 -968 C
ATOM 424 N LEU A 52 30.184 -0.089 -63.249 1.00 32.45 N
ANISOU 424 N LEU A 52 4137 4126 4064 40 330 -778 N
ATOM 425 CA LEU A 52 30.591 1.297 -63.067 1.00 31.71 C
ANISOU 425 CA LEU A 52 4042 4041 3966 57 344 -746 C
ATOM 426 C LEU A 52 32.081 1.367 -62.709 1.00 31.04 C
ANISOU 426 C LEU A 52 3937 3913 3944 69 352 -773 C
ATOM 427 O LEU A 52 32.788 2.287 -63.124 1.00 28.42 O
ANISOU 427 O LEU A 52 3596 3588 3611 69 386 -776 O
ATOM 428 CB LEU A 52 29.739 1.925 -61.991 1.00 30.07 C
ANISOU 428 CB LEU A 52 3850 3834 3740 66 318 -693 C
ATOM 429 CG LEU A 52 28.957 3.215 -62.272 1.00 32.74 C
ANISOU 429 CG LEU A 52 4204 4216 4020 75 340 -643 C
ATOM 430 CD1 LEU A 52 28.635 3.441 -63.737 1.00 30.76 C
ANISOU 430 CD1 LEU A 52 3950 4025 3712 71 376 -646 C
ATOM 431 CD2 LEU A 52 27.690 3.270 -61.400 1.00 30.15 C
ANISOU 431 CD2 LEU A 52 3890 3902 3663 79 307 -601 C
ATOM 432 N GLN A 53 32.544 0.352 -61.984 1.00 30.93 N
ANISOU 432 N GLN A 53 3912 3856 3981 79 324 -792 N
ATOM 433 CA GLN A 53 33.934 0.259 -61.580 1.00 32.77 C
ANISOU 433 CA GLN A 53 4117 4062 4272 97 325 -817 C
ATOM 434 C GLN A 53 34.884 -0.061 -62.752 1.00 33.60 C
ANISOU 434 C GLN A 53 4200 4169 4394 94 365 -868 C
ATOM 435 O GLN A 53 36.089 0.191 -62.667 1.00 31.78 O
ANISOU 435 O GLN A 53 3940 3934 4200 105 377 -891 O
ATOM 436 CB GLN A 53 34.083 -0.714 -60.408 1.00 33.72 C
ANISOU 436 CB GLN A 53 4233 4144 4435 121 284 -811 C
ATOM 437 CG GLN A 53 33.940 0.004 -59.064 1.00 37.14 C
ANISOU 437 CG GLN A 53 4666 4578 4867 129 251 -771 C
ATOM 438 CD GLN A 53 33.388 -0.860 -57.953 1.00 38.67 C
ANISOU 438 CD GLN A 53 4874 4743 5074 145 209 -745 C
ATOM 439 OE1 GLN A 53 33.747 -2.021 -57.810 1.00 41.88 O
ANISOU 439 OE1 GLN A 53 5278 5117 5516 167 201 -758 O
ATOM 440 NE2 GLN A 53 32.511 -0.282 -57.149 1.00 40.52 N
ANISOU 440 NE2 GLN A 53 5127 4987 5280 135 186 -705 N
ATOM 441 N GLU A 54 34.321 -0.543 -63.861 1.00 32.67 N
ANISOU 441 N GLU A 54 4097 4070 4245 75 387 -888 N
ATOM 442 CA GLU A 54 35.062 -0.649 -65.111 1.00 34.45 C
ANISOU 442 CA GLU A 54 4307 4309 4473 65 430 -933 C
ATOM 443 C GLU A 54 34.951 0.615 -65.972 1.00 34.93 C
ANISOU 443 C GLU A 54 4373 4416 4482 49 466 -919 C
ATOM 444 O GLU A 54 35.843 0.931 -66.769 1.00 33.33 O
ANISOU 444 O GLU A 54 4153 4221 4286 43 505 -949 O
ATOM 445 CB GLU A 54 34.570 -1.843 -65.892 1.00 36.67 C
ANISOU 445 CB GLU A 54 4599 4587 4743 47 442 -969 C
ATOM 446 CG GLU A 54 34.658 -3.129 -65.097 1.00 39.03 C
ANISOU 446 CG GLU A 54 4905 4829 5095 65 421 -981 C
ATOM 447 CD GLU A 54 33.944 -4.245 -65.763 1.00 39.50 C
ANISOU 447 CD GLU A 54 4986 4883 5137 36 438 -1016 C
ATOM 448 OE1 GLU A 54 33.229 -3.966 -66.735 1.00 42.01 O
ANISOU 448 OE1 GLU A 54 5310 5257 5394 0 457 -1026 O
ATOM 449 OE2 GLU A 54 34.089 -5.397 -65.310 1.00 43.08 O
ANISOU 449 OE2 GLU A 54 5452 5279 5636 49 438 -1033 O
ATOM 450 N ILE A 55 33.842 1.326 -65.815 1.00 33.39 N
ANISOU 450 N ILE A 55 4201 4250 4233 45 457 -870 N
ATOM 451 CA ILE A 55 33.555 2.474 -66.642 1.00 32.56 C
ANISOU 451 CA ILE A 55 4109 4189 4073 40 494 -844 C
ATOM 452 C ILE A 55 34.335 3.693 -66.172 1.00 32.63 C
ANISOU 452 C ILE A 55 4117 4176 4102 47 518 -827 C
ATOM 453 O ILE A 55 34.985 4.355 -66.972 1.00 34.76 O
ANISOU 453 O ILE A 55 4386 4457 4363 39 566 -839 O
ATOM 454 CB ILE A 55 32.041 2.745 -66.686 1.00 32.73 C
ANISOU 454 CB ILE A 55 4152 4256 4026 41 480 -794 C
ATOM 455 CG1 ILE A 55 31.361 1.717 -67.587 1.00 31.42 C
ANISOU 455 CG1 ILE A 55 3981 4134 3822 20 477 -824 C
ATOM 456 CG2 ILE A 55 31.746 4.179 -67.125 1.00 32.33 C
ANISOU 456 CG2 ILE A 55 4120 4239 3924 54 518 -744 C
ATOM 457 CD1 ILE A 55 29.941 1.431 -67.189 1.00 30.59 C
ANISOU 457 CD1 ILE A 55 3886 4063 3673 15 443 -794 C
ATOM 458 N ILE A 56 34.272 3.978 -64.868 1.00 33.27 N
ANISOU 458 N ILE A 56 4201 4229 4209 55 488 -803 N
ATOM 459 CA ILE A 56 35.046 5.062 -64.260 1.00 31.73 C
ANISOU 459 CA ILE A 56 4003 4014 4037 52 510 -798 C
ATOM 460 C ILE A 56 36.406 4.534 -63.802 1.00 31.82 C
ANISOU 460 C ILE A 56 3973 4004 4112 50 499 -849 C
ATOM 461 O ILE A 56 36.496 3.733 -62.883 1.00 31.63 O
ANISOU 461 O ILE A 56 3931 3963 4122 63 452 -854 O
ATOM 462 CB ILE A 56 34.282 5.731 -63.084 1.00 31.15 C
ANISOU 462 CB ILE A 56 3953 3930 3953 58 489 -749 C
ATOM 463 CG1 ILE A 56 32.824 5.994 -63.478 1.00 30.62 C
ANISOU 463 CG1 ILE A 56 3918 3891 3822 70 490 -697 C
ATOM 464 CG2 ILE A 56 34.969 7.035 -62.665 1.00 30.78 C
ANISOU 464 CG2 ILE A 56 3912 3865 3918 43 532 -747 C
ATOM 465 CD1 ILE A 56 31.963 6.636 -62.397 1.00 30.16 C
ANISOU 465 CD1 ILE A 56 3883 3824 3750 79 473 -647 C
ATOM 466 N PRO A 57 37.476 4.986 -64.446 1.00 32.73 N
ANISOU 466 N PRO A 57 4070 4124 4242 35 545 -885 N
ATOM 467 CA PRO A 57 38.792 4.414 -64.154 1.00 33.02 C
ANISOU 467 CA PRO A 57 4056 4153 4334 38 537 -936 C
ATOM 468 C PRO A 57 39.221 4.777 -62.763 1.00 32.88 C
ANISOU 468 C PRO A 57 4016 4130 4344 37 509 -932 C
ATOM 469 O PRO A 57 38.884 5.875 -62.283 1.00 33.17 O
ANISOU 469 O PRO A 57 4077 4165 4360 19 526 -906 O
ATOM 470 CB PRO A 57 39.704 5.112 -65.173 1.00 33.73 C
ANISOU 470 CB PRO A 57 4136 4256 4421 14 601 -971 C
ATOM 471 CG PRO A 57 39.064 6.457 -65.374 1.00 33.01 C
ANISOU 471 CG PRO A 57 4092 4165 4283 -2 644 -929 C
ATOM 472 CD PRO A 57 37.568 6.232 -65.236 1.00 33.61 C
ANISOU 472 CD PRO A 57 4205 4244 4318 17 611 -874 C
ATOM 473 N LYS A 58 39.988 3.905 -62.120 1.00 33.58 N
ANISOU 473 N LYS A 58 4060 4220 4478 58 473 -958 N
ATOM 474 CA LYS A 58 40.345 4.133 -60.721 1.00 36.36 C
ANISOU 474 CA LYS A 58 4385 4581 4848 61 438 -952 C
ATOM 475 C LYS A 58 41.146 5.393 -60.508 1.00 37.71 C
ANISOU 475 C LYS A 58 4537 4774 5017 21 479 -978 C
ATOM 476 O LYS A 58 41.118 5.979 -59.417 1.00 40.35 O
ANISOU 476 O LYS A 58 4866 5117 5347 5 464 -968 O
ATOM 477 CB LYS A 58 41.095 2.959 -60.110 1.00 37.89 C
ANISOU 477 CB LYS A 58 4528 4782 5085 100 394 -970 C
ATOM 478 CG LYS A 58 40.915 2.935 -58.599 1.00 39.21 C
ANISOU 478 CG LYS A 58 4684 4958 5255 113 342 -941 C
ATOM 479 CD LYS A 58 41.922 2.052 -57.885 1.00 40.82 C
ANISOU 479 CD LYS A 58 4825 5186 5497 156 306 -957 C
ATOM 480 CE LYS A 58 41.821 2.267 -56.385 1.00 41.15 C
ANISOU 480 CE LYS A 58 4851 5253 5530 160 260 -930 C
ATOM 481 NZ LYS A 58 42.472 1.154 -55.655 1.00 42.89 N
ANISOU 481 NZ LYS A 58 5023 5491 5779 220 215 -924 N
ATOM 482 N SER A 59 41.864 5.805 -61.540 1.00 36.44 N
ANISOU 482 N SER A 59 4366 4621 4857 -1 535 -1015 N
ATOM 483 CA SER A 59 42.647 7.025 -61.485 1.00 37.70 C
ANISOU 483 CA SER A 59 4512 4796 5014 -48 589 -1047 C
ATOM 484 C SER A 59 41.790 8.275 -61.250 1.00 37.60 C
ANISOU 484 C SER A 59 4561 4758 4965 -78 625 -1009 C
ATOM 485 O SER A 59 42.319 9.324 -60.865 1.00 37.81 O
ANISOU 485 O SER A 59 4584 4790 4991 -123 669 -1032 O
ATOM 486 CB SER A 59 43.462 7.184 -62.763 1.00 36.92 C
ANISOU 486 CB SER A 59 4401 4705 4920 -67 648 -1090 C
ATOM 487 OG SER A 59 42.614 7.085 -63.882 1.00 37.30 O
ANISOU 487 OG SER A 59 4502 4730 4938 -55 670 -1060 O
ATOM 488 N TYR A 60 40.479 8.177 -61.491 1.00 36.29 N
ANISOU 488 N TYR A 60 4450 4568 4769 -54 612 -952 N
ATOM 489 CA TYR A 60 39.597 9.286 -61.157 1.00 35.73 C
ANISOU 489 CA TYR A 60 4435 4474 4665 -69 643 -908 C
ATOM 490 C TYR A 60 39.508 9.526 -59.647 1.00 35.12 C
ANISOU 490 C TYR A 60 4346 4398 4597 -80 608 -903 C
ATOM 491 O TYR A 60 39.415 10.672 -59.212 1.00 33.77 O
ANISOU 491 O TYR A 60 4203 4212 4414 -113 654 -898 O
ATOM 492 CB TYR A 60 38.196 9.153 -61.770 1.00 34.99 C
ANISOU 492 CB TYR A 60 4394 4368 4530 -37 637 -848 C
ATOM 493 CG TYR A 60 37.273 10.251 -61.290 1.00 34.33 C
ANISOU 493 CG TYR A 60 4364 4262 4415 -41 666 -797 C
ATOM 494 CD1 TYR A 60 37.328 11.521 -61.852 1.00 34.94 C
ANISOU 494 CD1 TYR A 60 4484 4319 4470 -60 751 -785 C
ATOM 495 CD2 TYR A 60 36.400 10.042 -60.221 1.00 35.08 C
ANISOU 495 CD2 TYR A 60 4469 4354 4506 -26 614 -763 C
ATOM 496 CE1 TYR A 60 36.514 12.537 -61.399 1.00 35.13 C
ANISOU 496 CE1 TYR A 60 4560 4316 4470 -57 787 -738 C
ATOM 497 CE2 TYR A 60 35.590 11.066 -59.737 1.00 33.43 C
ANISOU 497 CE2 TYR A 60 4307 4123 4270 -28 645 -719 C
ATOM 498 CZ TYR A 60 35.654 12.307 -60.334 1.00 33.97 C
ANISOU 498 CZ TYR A 60 4418 4168 4319 -42 733 -707 C
ATOM 499 OH TYR A 60 34.847 13.320 -59.904 1.00 35.38 O
ANISOU 499 OH TYR A 60 4648 4318 4474 -37 773 -660 O
ATOM 500 N PHE A 61 39.552 8.452 -58.859 1.00 34.90 N
ANISOU 500 N PHE A 61 4280 4389 4591 -54 533 -904 N
ATOM 501 CA PHE A 61 39.436 8.567 -57.392 1.00 35.97 C
ANISOU 501 CA PHE A 61 4402 4535 4730 -61 492 -896 C
ATOM 502 C PHE A 61 40.774 8.501 -56.665 1.00 38.21 C
ANISOU 502 C PHE A 61 4614 4864 5041 -82 479 -952 C
ATOM 503 O PHE A 61 40.850 8.849 -55.504 1.00 41.96 O
ANISOU 503 O PHE A 61 5073 5359 5512 -102 459 -956 O
ATOM 504 CB PHE A 61 38.549 7.464 -56.823 1.00 34.43 C
ANISOU 504 CB PHE A 61 4213 4334 4535 -17 418 -855 C
ATOM 505 CG PHE A 61 37.212 7.347 -57.484 1.00 33.02 C
ANISOU 505 CG PHE A 61 4092 4128 4326 3 421 -805 C
ATOM 506 CD1 PHE A 61 36.180 8.202 -57.144 1.00 31.39 C
ANISOU 506 CD1 PHE A 61 3933 3904 4087 -5 439 -763 C
ATOM 507 CD2 PHE A 61 36.972 6.346 -58.412 1.00 31.70 C
ANISOU 507 CD2 PHE A 61 3926 3958 4160 30 407 -804 C
ATOM 508 CE1 PHE A 61 34.936 8.083 -57.734 1.00 30.80 C
ANISOU 508 CE1 PHE A 61 3901 3821 3979 17 438 -717 C
ATOM 509 CE2 PHE A 61 35.722 6.218 -59.001 1.00 31.96 C
ANISOU 509 CE2 PHE A 61 4001 3982 4157 43 408 -764 C
ATOM 510 CZ PHE A 61 34.700 7.090 -58.659 1.00 30.82 C
ANISOU 510 CZ PHE A 61 3899 3832 3977 39 421 -718 C
ATOM 511 N GLY A 62 41.808 7.982 -57.319 1.00 39.79 N
ANISOU 511 N GLY A 62 4765 5087 5264 -74 485 -994 N
ATOM 512 CA GLY A 62 43.132 7.874 -56.698 1.00 40.22 C
ANISOU 512 CA GLY A 62 4739 5200 5340 -88 471 -1048 C
ATOM 513 C GLY A 62 43.298 6.714 -55.724 1.00 42.10 C
ANISOU 513 C GLY A 62 4929 5473 5595 -37 390 -1033 C
ATOM 514 O GLY A 62 44.262 5.963 -55.816 1.00 44.43 O
ANISOU 514 O GLY A 62 5160 5805 5914 -7 370 -1061 O
ATOM 515 N THR A 63 42.378 6.577 -54.769 1.00 42.38 N
ANISOU 515 N THR A 63 4993 5495 5615 -23 346 -987 N
ATOM 516 CA THR A 63 42.491 5.530 -53.730 1.00 41.37 C
ANISOU 516 CA THR A 63 4825 5397 5497 26 272 -965 C
ATOM 517 C THR A 63 41.196 4.762 -53.570 1.00 40.68 C
ANISOU 517 C THR A 63 4795 5257 5404 66 233 -903 C
ATOM 518 O THR A 63 40.117 5.242 -53.932 1.00 38.97 O
ANISOU 518 O THR A 63 4644 4996 5167 48 255 -875 O
ATOM 519 CB THR A 63 42.814 6.120 -52.340 1.00 42.42 C
ANISOU 519 CB THR A 63 4918 5587 5610 -4 249 -977 C
ATOM 520 OG1 THR A 63 41.814 7.081 -51.997 1.00 44.11 O
ANISOU 520 OG1 THR A 63 5195 5765 5797 -47 273 -955 O
ATOM 521 CG2 THR A 63 44.190 6.786 -52.311 1.00 41.21 C
ANISOU 521 CG2 THR A 63 4692 5505 5459 -49 282 -1047 C
ATOM 522 N THR A 64 41.304 3.576 -52.990 1.00 40.73 N
ANISOU 522 N THR A 64 4776 5271 5426 123 178 -880 N
ATOM 523 CA THR A 64 40.141 2.767 -52.675 1.00 40.92 C
ANISOU 523 CA THR A 64 4852 5249 5446 157 141 -825 C
ATOM 524 C THR A 64 39.177 3.519 -51.751 1.00 40.66 C
ANISOU 524 C THR A 64 4855 5211 5379 125 128 -794 C
ATOM 525 O THR A 64 37.960 3.452 -51.938 1.00 40.64 O
ANISOU 525 O THR A 64 4914 5165 5363 123 128 -759 O
ATOM 526 CB THR A 64 40.564 1.421 -52.054 1.00 42.26 C
ANISOU 526 CB THR A 64 4988 5428 5640 224 92 -805 C
ATOM 527 OG1 THR A 64 41.589 0.833 -52.865 1.00 43.17 O
ANISOU 527 OG1 THR A 64 5061 5552 5787 255 111 -838 O
ATOM 528 CG2 THR A 64 39.391 0.456 -51.973 1.00 42.24 C
ANISOU 528 CG2 THR A 64 5045 5364 5638 255 69 -756 C
ATOM 529 N THR A 65 39.722 4.269 -50.790 1.00 40.89 N
ANISOU 529 N THR A 65 4846 5293 5395 95 122 -813 N
ATOM 530 CA THR A 65 38.886 4.989 -49.819 1.00 39.46 C
ANISOU 530 CA THR A 65 4698 5110 5183 62 113 -788 C
ATOM 531 C THR A 65 38.062 6.084 -50.483 1.00 38.58 C
ANISOU 531 C THR A 65 4648 4955 5054 19 170 -786 C
ATOM 532 O THR A 65 36.863 6.183 -50.219 1.00 36.49 O
ANISOU 532 O THR A 65 4436 4657 4770 20 162 -744 O
ATOM 533 CB THR A 65 39.692 5.553 -48.629 1.00 41.53 C
ANISOU 533 CB THR A 65 4902 5446 5430 33 97 -816 C
ATOM 534 OG1 THR A 65 40.573 4.539 -48.125 1.00 42.98 O
ANISOU 534 OG1 THR A 65 5020 5683 5627 84 47 -816 O
ATOM 535 CG2 THR A 65 38.749 5.983 -47.499 1.00 40.28 C
ANISOU 535 CG2 THR A 65 4778 5284 5242 11 77 -785 C
ATOM 536 N ASN A 66 38.694 6.891 -51.347 1.00 36.29 N
ANISOU 536 N ASN A 66 4352 4667 4769 -15 230 -827 N
ATOM 537 CA ASN A 66 37.944 7.829 -52.196 1.00 36.79 C
ANISOU 537 CA ASN A 66 4478 4685 4816 -41 292 -816 C
ATOM 538 C ASN A 66 36.876 7.112 -53.059 1.00 37.86 C
ANISOU 538 C ASN A 66 4660 4779 4946 -1 281 -772 C
ATOM 539 O ASN A 66 35.700 7.506 -53.092 1.00 36.45 O
ANISOU 539 O ASN A 66 4534 4573 4742 -2 291 -731 O
ATOM 540 CB ASN A 66 38.887 8.625 -53.103 1.00 37.62 C
ANISOU 540 CB ASN A 66 4569 4795 4928 -78 361 -865 C
ATOM 541 CG ASN A 66 39.776 9.592 -52.333 1.00 40.58 C
ANISOU 541 CG ASN A 66 4908 5209 5300 -137 391 -916 C
ATOM 542 OD1 ASN A 66 39.537 9.881 -51.150 1.00 41.97 O
ANISOU 542 OD1 ASN A 66 5081 5404 5462 -156 369 -911 O
ATOM 543 ND2 ASN A 66 40.802 10.117 -53.010 1.00 38.47 N
ANISOU 543 ND2 ASN A 66 4615 4957 5044 -172 446 -969 N
ATOM 544 N LEU A 67 37.276 6.043 -53.737 1.00 36.98 N
ANISOU 544 N LEU A 67 4525 4668 4856 31 261 -782 N
ATOM 545 CA LEU A 67 36.336 5.330 -54.589 1.00 37.03 C
ANISOU 545 CA LEU A 67 4571 4644 4855 58 256 -752 C
ATOM 546 C LEU A 67 35.113 4.854 -53.767 1.00 37.18 C
ANISOU 546 C LEU A 67 4621 4647 4856 74 210 -704 C
ATOM 547 O LEU A 67 33.963 5.000 -54.197 1.00 36.47 O
ANISOU 547 O LEU A 67 4576 4542 4739 74 220 -673 O
ATOM 548 CB LEU A 67 37.042 4.170 -55.294 1.00 34.91 C
ANISOU 548 CB LEU A 67 4272 4376 4617 89 245 -778 C
ATOM 549 CG LEU A 67 36.237 3.195 -56.140 1.00 33.54 C
ANISOU 549 CG LEU A 67 4128 4174 4438 111 239 -762 C
ATOM 550 CD1 LEU A 67 37.170 2.566 -57.151 1.00 33.71 C
ANISOU 550 CD1 LEU A 67 4121 4197 4488 123 260 -804 C
ATOM 551 CD2 LEU A 67 35.593 2.117 -55.276 1.00 33.91 C
ANISOU 551 CD2 LEU A 67 4187 4203 4492 139 186 -731 C
ATOM 552 N LYS A 68 35.374 4.307 -52.584 1.00 38.69 N
ANISOU 552 N LYS A 68 4787 4851 5060 89 161 -697 N
ATOM 553 CA LYS A 68 34.313 3.742 -51.749 1.00 42.34 C
ANISOU 553 CA LYS A 68 5277 5298 5509 104 118 -654 C
ATOM 554 C LYS A 68 33.352 4.812 -51.236 1.00 40.17 C
ANISOU 554 C LYS A 68 5039 5020 5200 76 132 -627 C
ATOM 555 O LYS A 68 32.164 4.555 -51.021 1.00 40.81 O
ANISOU 555 O LYS A 68 5156 5086 5261 82 114 -590 O
ATOM 556 CB LYS A 68 34.902 2.932 -50.593 1.00 47.01 C
ANISOU 556 CB LYS A 68 5834 5908 6120 132 67 -648 C
ATOM 557 CG LYS A 68 34.868 1.431 -50.828 1.00 51.17 C
ANISOU 557 CG LYS A 68 6364 6407 6671 177 41 -637 C
ATOM 558 CD LYS A 68 35.987 0.712 -50.090 1.00 57.71 C
ANISOU 558 CD LYS A 68 7140 7260 7525 218 9 -641 C
ATOM 559 CE LYS A 68 35.694 -0.779 -49.981 1.00 57.84 C
ANISOU 559 CE LYS A 68 7178 7235 7562 267 -12 -613 C
ATOM 560 NZ LYS A 68 34.760 -1.047 -48.846 1.00 61.47 N
ANISOU 560 NZ LYS A 68 7670 7684 8001 270 -48 -566 N
ATOM 561 N ARG A 69 33.862 6.022 -51.113 1.00 39.01 N
ANISOU 561 N ARG A 69 4885 4888 5048 43 170 -649 N
ATOM 562 CA ARG A 69 33.070 7.143 -50.672 1.00 37.81 C
ANISOU 562 CA ARG A 69 4769 4726 4868 17 198 -628 C
ATOM 563 C ARG A 69 32.057 7.560 -51.750 1.00 36.81 C
ANISOU 563 C ARG A 69 4690 4576 4717 24 238 -600 C
ATOM 564 O ARG A 69 30.862 7.679 -51.457 1.00 37.83 O
ANISOU 564 O ARG A 69 4854 4698 4821 32 230 -559 O
ATOM 565 CB ARG A 69 33.988 8.304 -50.237 1.00 40.26 C
ANISOU 565 CB ARG A 69 5061 5054 5181 -26 240 -668 C
ATOM 566 CG ARG A 69 33.271 9.434 -49.516 1.00 46.04 C
ANISOU 566 CG ARG A 69 5831 5772 5889 -56 271 -651 C
ATOM 567 CD ARG A 69 34.235 10.467 -48.947 1.00 48.61 C
ANISOU 567 CD ARG A 69 6135 6116 6218 -110 314 -701 C
ATOM 568 NE ARG A 69 34.655 10.130 -47.587 1.00 55.63 N
ANISOU 568 NE ARG A 69 6981 7050 7105 -124 261 -717 N
ATOM 569 CZ ARG A 69 35.884 9.734 -47.256 1.00 58.11 C
ANISOU 569 CZ ARG A 69 7228 7418 7432 -133 234 -759 C
ATOM 570 NH1 ARG A 69 36.836 9.633 -48.188 1.00 57.90 N
ANISOU 570 NH1 ARG A 69 7171 7402 7426 -132 258 -795 N
ATOM 571 NH2 ARG A 69 36.169 9.450 -45.989 1.00 56.70 N
ANISOU 571 NH2 ARG A 69 7010 7290 7242 -140 185 -766 N
ATOM 572 N PHE A 70 32.524 7.745 -52.992 1.00 34.29 N
ANISOU 572 N PHE A 70 4370 4255 4403 25 280 -619 N
ATOM 573 CA PHE A 70 31.643 8.050 -54.131 1.00 33.11 C
ANISOU 573 CA PHE A 70 4258 4098 4223 38 316 -590 C
ATOM 574 C PHE A 70 30.545 6.987 -54.288 1.00 32.56 C
ANISOU 574 C PHE A 70 4198 4035 4136 64 270 -560 C
ATOM 575 O PHE A 70 29.388 7.333 -54.444 1.00 34.87 O
ANISOU 575 O PHE A 70 4521 4333 4393 73 280 -521 O
ATOM 576 CB PHE A 70 32.471 8.210 -55.440 1.00 32.10 C
ANISOU 576 CB PHE A 70 4119 3972 4103 35 362 -621 C
ATOM 577 CG PHE A 70 31.643 8.485 -56.693 1.00 30.32 C
ANISOU 577 CG PHE A 70 3927 3752 3839 53 399 -590 C
ATOM 578 CD1 PHE A 70 31.304 9.790 -57.059 1.00 31.56 C
ANISOU 578 CD1 PHE A 70 4121 3899 3969 51 464 -563 C
ATOM 579 CD2 PHE A 70 31.263 7.444 -57.544 1.00 30.45 C
ANISOU 579 CD2 PHE A 70 3935 3787 3845 70 373 -590 C
ATOM 580 CE1 PHE A 70 30.573 10.040 -58.226 1.00 29.74 C
ANISOU 580 CE1 PHE A 70 3916 3685 3696 76 497 -528 C
ATOM 581 CE2 PHE A 70 30.540 7.690 -58.710 1.00 27.24 C
ANISOU 581 CE2 PHE A 70 3551 3404 3396 84 405 -565 C
ATOM 582 CZ PHE A 70 30.207 8.979 -59.048 1.00 28.80 C
ANISOU 582 CZ PHE A 70 3780 3600 3562 91 463 -531 C
ATOM 583 N TYR A 71 30.917 5.705 -54.199 1.00 31.20 N
ANISOU 583 N TYR A 71 4000 3863 3989 74 225 -579 N
ATOM 584 CA TYR A 71 30.000 4.594 -54.518 1.00 30.88 C
ANISOU 584 CA TYR A 71 3971 3824 3935 88 194 -564 C
ATOM 585 C TYR A 71 28.923 4.351 -53.457 1.00 31.22 C
ANISOU 585 C TYR A 71 4033 3865 3962 90 156 -528 C
ATOM 586 O TYR A 71 27.895 3.742 -53.743 1.00 30.12 O
ANISOU 586 O TYR A 71 3909 3734 3798 92 142 -512 O
ATOM 587 CB TYR A 71 30.774 3.298 -54.839 1.00 30.08 C
ANISOU 587 CB TYR A 71 3846 3712 3871 100 173 -598 C
ATOM 588 CG TYR A 71 31.322 3.279 -56.262 1.00 32.33 C
ANISOU 588 CG TYR A 71 4120 4005 4157 98 212 -629 C
ATOM 589 CD1 TYR A 71 30.509 2.921 -57.337 1.00 32.05 C
ANISOU 589 CD1 TYR A 71 4102 3985 4090 95 226 -627 C
ATOM 590 CD2 TYR A 71 32.646 3.676 -56.541 1.00 31.87 C
ANISOU 590 CD2 TYR A 71 4033 3947 4126 95 238 -664 C
ATOM 591 CE1 TYR A 71 30.999 2.947 -58.646 1.00 33.06 C
ANISOU 591 CE1 TYR A 71 4220 4126 4212 91 264 -655 C
ATOM 592 CE2 TYR A 71 33.140 3.697 -57.847 1.00 31.98 C
ANISOU 592 CE2 TYR A 71 4040 3969 4140 91 277 -693 C
ATOM 593 CZ TYR A 71 32.304 3.330 -58.893 1.00 32.43 C
ANISOU 593 CZ TYR A 71 4117 4039 4164 91 289 -687 C
ATOM 594 OH TYR A 71 32.771 3.318 -60.190 1.00 34.74 O
ANISOU 594 OH TYR A 71 4402 4345 4451 85 328 -716 O
ATOM 595 N LYS A 72 29.142 4.850 -52.244 1.00 32.01 N
ANISOU 595 N LYS A 72 4131 3960 4071 83 142 -520 N
ATOM 596 CA LYS A 72 28.051 4.888 -51.250 1.00 33.78 C
ANISOU 596 CA LYS A 72 4376 4183 4272 80 116 -484 C
ATOM 597 C LYS A 72 26.900 5.750 -51.769 1.00 31.47 C
ANISOU 597 C LYS A 72 4113 3906 3937 81 150 -452 C
ATOM 598 O LYS A 72 25.740 5.434 -51.535 1.00 30.59 O
ANISOU 598 O LYS A 72 4017 3805 3799 85 130 -424 O
ATOM 599 CB LYS A 72 28.530 5.418 -49.895 1.00 35.74 C
ANISOU 599 CB LYS A 72 4615 4430 4532 68 102 -484 C
ATOM 600 CG LYS A 72 29.406 4.459 -49.098 1.00 39.47 C
ANISOU 600 CG LYS A 72 5057 4903 5036 78 57 -500 C
ATOM 601 CD LYS A 72 28.602 3.564 -48.169 1.00 43.39 C
ANISOU 601 CD LYS A 72 5568 5391 5524 87 10 -469 C
ATOM 602 CE LYS A 72 28.528 2.124 -48.672 1.00 49.65 C
ANISOU 602 CE LYS A 72 6364 6164 6334 109 -9 -470 C
ATOM 603 NZ LYS A 72 27.398 1.886 -49.629 1.00 53.02 N
ANISOU 603 NZ LYS A 72 6820 6588 6738 101 8 -463 N
ATOM 604 N VAL A 73 27.228 6.834 -52.477 1.00 29.09 N
ANISOU 604 N VAL A 73 3818 3606 3627 81 204 -454 N
ATOM 605 CA VAL A 73 26.209 7.632 -53.126 1.00 29.51 C
ANISOU 605 CA VAL A 73 3897 3676 3636 95 242 -417 C
ATOM 606 C VAL A 73 25.465 6.807 -54.200 1.00 29.24 C
ANISOU 606 C VAL A 73 3858 3677 3572 108 229 -411 C
ATOM 607 O VAL A 73 24.234 6.681 -54.165 1.00 29.42 O
ANISOU 607 O VAL A 73 3890 3730 3558 117 217 -380 O
ATOM 608 CB VAL A 73 26.824 8.878 -53.755 1.00 29.79 C
ANISOU 608 CB VAL A 73 3947 3701 3672 95 311 -420 C
ATOM 609 CG1 VAL A 73 25.777 9.614 -54.574 1.00 28.14 C
ANISOU 609 CG1 VAL A 73 3764 3514 3413 124 353 -373 C
ATOM 610 CG2 VAL A 73 27.449 9.756 -52.663 1.00 28.66 C
ANISOU 610 CG2 VAL A 73 3810 3527 3552 71 332 -434 C
ATOM 611 N VAL A 74 26.235 6.219 -55.109 1.00 26.90 N
ANISOU 611 N VAL A 74 3544 3383 3293 105 233 -445 N
ATOM 612 CA VAL A 74 25.719 5.344 -56.157 1.00 28.24 C
ANISOU 612 CA VAL A 74 3706 3586 3437 106 225 -454 C
ATOM 613 C VAL A 74 24.806 4.282 -55.574 1.00 29.06 C
ANISOU 613 C VAL A 74 3810 3698 3533 96 178 -450 C
ATOM 614 O VAL A 74 23.773 3.932 -56.157 1.00 30.75 O
ANISOU 614 O VAL A 74 4023 3957 3703 93 175 -441 O
ATOM 615 CB VAL A 74 26.886 4.655 -56.929 1.00 27.70 C
ANISOU 615 CB VAL A 74 3617 3504 3403 98 231 -503 C
ATOM 616 CG1 VAL A 74 26.374 3.575 -57.871 1.00 27.96 C
ANISOU 616 CG1 VAL A 74 3642 3566 3413 90 222 -523 C
ATOM 617 CG2 VAL A 74 27.695 5.681 -57.700 1.00 27.19 C
ANISOU 617 CG2 VAL A 74 3552 3438 3338 103 284 -510 C
ATOM 618 N GLU A 75 25.198 3.773 -54.421 1.00 28.90 N
ANISOU 618 N GLU A 75 3789 3639 3551 89 144 -458 N
ATOM 619 CA GLU A 75 24.459 2.765 -53.746 1.00 31.02 C
ANISOU 619 CA GLU A 75 4063 3902 3818 79 106 -454 C
ATOM 620 C GLU A 75 23.117 3.296 -53.196 1.00 30.26 C
ANISOU 620 C GLU A 75 3982 3836 3679 79 99 -413 C
ATOM 621 O GLU A 75 22.125 2.569 -53.168 1.00 29.76 O
ANISOU 621 O GLU A 75 3922 3795 3591 65 81 -409 O
ATOM 622 CB GLU A 75 25.334 2.163 -52.645 1.00 35.11 C
ANISOU 622 CB GLU A 75 4578 4373 4386 81 75 -465 C
ATOM 623 CG GLU A 75 24.647 1.121 -51.779 1.00 44.32 C
ANISOU 623 CG GLU A 75 5759 5523 5555 73 39 -455 C
ATOM 624 CD GLU A 75 25.523 -0.102 -51.520 1.00 54.06 C
ANISOU 624 CD GLU A 75 6990 6714 6836 82 22 -477 C
ATOM 625 OE1 GLU A 75 26.767 0.074 -51.370 1.00 58.51 O
ANISOU 625 OE1 GLU A 75 7532 7264 7434 100 22 -491 O
ATOM 626 OE2 GLU A 75 24.964 -1.240 -51.470 1.00 54.63 O
ANISOU 626 OE2 GLU A 75 7079 6767 6909 71 13 -482 O
ATOM 627 N LYS A 76 23.074 4.557 -52.768 1.00 28.57 N
ANISOU 627 N LYS A 76 3777 3622 3456 91 120 -384 N
ATOM 628 CA LYS A 76 21.791 5.152 -52.349 1.00 28.92 C
ANISOU 628 CA LYS A 76 3833 3696 3457 98 122 -343 C
ATOM 629 C LYS A 76 20.879 5.277 -53.539 1.00 29.47 C
ANISOU 629 C LYS A 76 3895 3829 3473 111 142 -328 C
ATOM 630 O LYS A 76 19.686 4.969 -53.465 1.00 27.86 O
ANISOU 630 O LYS A 76 3686 3670 3230 107 127 -311 O
ATOM 631 CB LYS A 76 21.991 6.526 -51.737 1.00 29.80 C
ANISOU 631 CB LYS A 76 3960 3788 3573 111 153 -319 C
ATOM 632 CG LYS A 76 22.530 6.469 -50.323 1.00 32.05 C
ANISOU 632 CG LYS A 76 4250 4034 3894 94 128 -328 C
ATOM 633 CD LYS A 76 22.423 7.817 -49.632 1.00 35.04 C
ANISOU 633 CD LYS A 76 4647 4398 4266 97 163 -306 C
ATOM 634 CE LYS A 76 22.528 7.639 -48.109 1.00 35.25 C
ANISOU 634 CE LYS A 76 4677 4405 4311 76 129 -311 C
ATOM 635 NZ LYS A 76 22.341 8.914 -47.359 1.00 34.47 N
ANISOU 635 NZ LYS A 76 4599 4292 4205 71 167 -296 N
ATOM 636 N ILE A 77 21.466 5.708 -54.658 1.00 29.60 N
ANISOU 636 N ILE A 77 3905 3856 3483 124 178 -336 N
ATOM 637 CA ILE A 77 20.718 5.929 -55.854 1.00 28.29 C
ANISOU 637 CA ILE A 77 3728 3759 3259 141 200 -318 C
ATOM 638 C ILE A 77 20.148 4.598 -56.268 1.00 29.46 C
ANISOU 638 C ILE A 77 3856 3948 3387 112 168 -349 C
ATOM 639 O ILE A 77 18.990 4.517 -56.732 1.00 32.27 O
ANISOU 639 O ILE A 77 4196 4380 3683 114 166 -333 O
ATOM 640 CB ILE A 77 21.625 6.541 -56.962 1.00 27.90 C
ANISOU 640 CB ILE A 77 3679 3708 3212 157 246 -325 C
ATOM 641 CG1 ILE A 77 21.971 7.999 -56.599 1.00 26.90 C
ANISOU 641 CG1 ILE A 77 3580 3545 3095 183 293 -290 C
ATOM 642 CG2 ILE A 77 20.969 6.426 -58.332 1.00 25.24 C
ANISOU 642 CG2 ILE A 77 3323 3453 2811 169 260 -316 C
ATOM 643 CD1 ILE A 77 22.855 8.709 -57.606 1.00 27.12 C
ANISOU 643 CD1 ILE A 77 3616 3563 3126 196 347 -294 C
ATOM 644 N LEU A 78 20.931 3.538 -56.071 1.00 27.42 N
ANISOU 644 N LEU A 78 3598 3641 3179 84 146 -395 N
ATOM 645 CA LEU A 78 20.466 2.194 -56.448 1.00 28.79 C
ANISOU 645 CA LEU A 78 3761 3837 3340 48 127 -433 C
ATOM 646 C LEU A 78 19.334 1.686 -55.550 1.00 29.57 C
ANISOU 646 C LEU A 78 3864 3949 3420 28 98 -421 C
ATOM 647 O LEU A 78 18.688 0.683 -55.877 1.00 30.01 O
ANISOU 647 O LEU A 78 3912 4035 3453 -7 90 -451 O
ATOM 648 CB LEU A 78 21.619 1.190 -56.473 1.00 26.75 C
ANISOU 648 CB LEU A 78 3507 3513 3142 32 122 -481 C
ATOM 649 CG LEU A 78 22.578 1.306 -57.653 1.00 26.58 C
ANISOU 649 CG LEU A 78 3474 3495 3130 38 152 -509 C
ATOM 650 CD1 LEU A 78 23.789 0.395 -57.429 1.00 25.80 C
ANISOU 650 CD1 LEU A 78 3378 3324 3098 32 146 -549 C
ATOM 651 CD2 LEU A 78 21.837 0.917 -58.923 1.00 26.63 C
ANISOU 651 CD2 LEU A 78 3463 3578 3077 17 167 -530 C
ATOM 652 N THR A 79 19.088 2.388 -54.441 1.00 28.69 N
ANISOU 652 N THR A 79 3766 3816 3317 46 87 -382 N
ATOM 653 CA THR A 79 18.131 1.934 -53.422 1.00 30.15 C
ANISOU 653 CA THR A 79 3959 4004 3492 26 60 -371 C
ATOM 654 C THR A 79 17.166 3.064 -52.992 1.00 30.49 C
ANISOU 654 C THR A 79 4000 4091 3493 52 66 -320 C
ATOM 655 O THR A 79 16.472 2.953 -51.969 1.00 28.15 O
ANISOU 655 O THR A 79 3712 3791 3193 42 47 -304 O
ATOM 656 CB THR A 79 18.874 1.432 -52.169 1.00 31.69 C
ANISOU 656 CB THR A 79 4176 4115 3747 19 35 -377 C
ATOM 657 OG1 THR A 79 19.711 2.486 -51.663 1.00 33.04 O
ANISOU 657 OG1 THR A 79 4354 4252 3946 47 44 -356 O
ATOM 658 CG2 THR A 79 19.738 0.188 -52.491 1.00 29.60 C
ANISOU 658 CG2 THR A 79 3917 3804 3526 1 31 -422 C
ATOM 659 N GLN A 80 17.099 4.121 -53.807 1.00 30.84 N
ANISOU 659 N GLN A 80 4034 4178 3504 89 99 -293 N
ATOM 660 CA GLN A 80 16.417 5.360 -53.438 1.00 31.10 C
ANISOU 660 CA GLN A 80 4072 4236 3507 128 120 -239 C
ATOM 661 C GLN A 80 14.944 5.174 -53.126 1.00 31.80 C
ANISOU 661 C GLN A 80 4143 4394 3543 123 103 -219 C
ATOM 662 O GLN A 80 14.326 4.199 -53.575 1.00 32.43 O
ANISOU 662 O GLN A 80 4199 4529 3593 90 84 -247 O
ATOM 663 CB GLN A 80 16.560 6.380 -54.544 1.00 30.58 C
ANISOU 663 CB GLN A 80 4001 4206 3410 172 165 -210 C
ATOM 664 CG GLN A 80 16.103 5.863 -55.902 1.00 33.44 C
ANISOU 664 CG GLN A 80 4330 4658 3717 168 166 -224 C
ATOM 665 CD GLN A 80 16.383 6.849 -57.013 1.00 34.38 C
ANISOU 665 CD GLN A 80 4447 4809 3805 215 212 -193 C
ATOM 666 OE1 GLN A 80 15.701 7.864 -57.133 1.00 33.45 O
ANISOU 666 OE1 GLN A 80 4330 4734 3645 267 242 -135 O
ATOM 667 NE2 GLN A 80 17.413 6.562 -57.827 1.00 35.10 N
ANISOU 667 NE2 GLN A 80 4540 4878 3919 202 224 -228 N
ATOM 668 N SER A 81 14.394 6.109 -52.349 1.00 29.73 N
ANISOU 668 N SER A 81 3892 4131 3272 153 115 -174 N
ATOM 669 CA SER A 81 12.941 6.286 -52.248 1.00 31.74 C
ANISOU 669 CA SER A 81 4123 4468 3465 167 112 -143 C
ATOM 670 C SER A 81 12.545 7.462 -53.146 1.00 33.53 C
ANISOU 670 C SER A 81 4338 4759 3643 233 157 -91 C
ATOM 671 O SER A 81 13.412 8.237 -53.550 1.00 36.86 O
ANISOU 671 O SER A 81 4782 5136 4087 263 193 -77 O
ATOM 672 CB SER A 81 12.553 6.605 -50.803 1.00 30.25 C
ANISOU 672 CB SER A 81 3956 4238 3297 164 103 -123 C
ATOM 673 OG SER A 81 12.558 5.460 -49.991 1.00 28.83 O
ANISOU 673 OG SER A 81 3782 4025 3144 109 62 -160 O
ATOM 674 N SER A 82 11.258 7.629 -53.444 1.00 32.69 N
ANISOU 674 N SER A 82 4196 4757 3467 259 158 -60 N
ATOM 675 CA SER A 82 10.819 8.845 -54.131 1.00 33.22 C
ANISOU 675 CA SER A 82 4254 4880 3484 338 204 4 C
ATOM 676 C SER A 82 11.169 10.024 -53.266 1.00 32.89 C
ANISOU 676 C SER A 82 4262 4749 3486 376 246 43 C
ATOM 677 O SER A 82 10.998 9.965 -52.058 1.00 34.66 O
ANISOU 677 O SER A 82 4504 4924 3741 352 231 36 O
ATOM 678 CB SER A 82 9.315 8.835 -54.356 1.00 34.56 C
ANISOU 678 CB SER A 82 4373 5183 3573 363 195 34 C
ATOM 679 OG SER A 82 8.958 7.894 -55.343 1.00 37.51 O
ANISOU 679 OG SER A 82 4697 5660 3895 329 168 -2 O
ATOM 680 N PHE A 83 11.677 11.088 -53.877 1.00 33.21 N
ANISOU 680 N PHE A 83 4327 4764 3526 431 303 82 N
ATOM 681 CA PHE A 83 11.910 12.369 -53.187 1.00 33.26 C
ANISOU 681 CA PHE A 83 4383 4689 3564 472 361 122 C
ATOM 682 C PHE A 83 13.192 12.421 -52.354 1.00 31.86 C
ANISOU 682 C PHE A 83 4250 4387 3467 421 365 77 C
ATOM 683 O PHE A 83 13.512 13.450 -51.786 1.00 31.40 O
ANISOU 683 O PHE A 83 4235 4258 3438 440 418 97 O
ATOM 684 CB PHE A 83 10.710 12.745 -52.288 1.00 37.45 C
ANISOU 684 CB PHE A 83 4908 5249 4070 499 364 159 C
ATOM 685 CG PHE A 83 9.455 13.113 -53.043 1.00 40.11 C
ANISOU 685 CG PHE A 83 5203 5709 4324 572 380 221 C
ATOM 686 CD1 PHE A 83 9.394 14.278 -53.807 1.00 42.40 C
ANISOU 686 CD1 PHE A 83 5511 6012 4585 660 451 289 C
ATOM 687 CD2 PHE A 83 8.310 12.320 -52.945 1.00 41.95 C
ANISOU 687 CD2 PHE A 83 5380 6050 4506 555 329 213 C
ATOM 688 CE1 PHE A 83 8.225 14.628 -54.487 1.00 43.16 C
ANISOU 688 CE1 PHE A 83 5563 6234 4598 738 465 353 C
ATOM 689 CE2 PHE A 83 7.139 12.663 -53.624 1.00 42.91 C
ANISOU 689 CE2 PHE A 83 5454 6304 4546 624 342 268 C
ATOM 690 CZ PHE A 83 7.099 13.816 -54.399 1.00 43.01 C
ANISOU 690 CZ PHE A 83 5478 6336 4525 720 408 342 C
ATOM 691 N GLU A 84 13.891 11.301 -52.233 1.00 30.06 N
ANISOU 691 N GLU A 84 4010 4137 3273 357 312 16 N
ATOM 692 CA GLU A 84 15.081 11.257 -51.411 1.00 30.79 C
ANISOU 692 CA GLU A 84 4133 4131 3435 312 307 -25 C
ATOM 693 C GLU A 84 16.197 12.083 -52.034 1.00 32.00 C
ANISOU 693 C GLU A 84 4313 4231 3613 326 364 -26 C
ATOM 694 O GLU A 84 16.376 12.092 -53.268 1.00 32.69 O
ANISOU 694 O GLU A 84 4388 4355 3675 349 382 -18 O
ATOM 695 CB GLU A 84 15.559 9.804 -51.208 1.00 31.61 C
ANISOU 695 CB GLU A 84 4214 4228 3565 251 240 -83 C
ATOM 696 CG GLU A 84 16.778 9.657 -50.312 1.00 29.07 C
ANISOU 696 CG GLU A 84 3914 3822 3309 210 228 -123 C
ATOM 697 CD GLU A 84 17.101 8.209 -50.011 1.00 30.43 C
ANISOU 697 CD GLU A 84 4069 3988 3505 165 165 -167 C
ATOM 698 OE1 GLU A 84 16.616 7.316 -50.745 1.00 32.21 O
ANISOU 698 OE1 GLU A 84 4270 4263 3703 157 141 -179 O
ATOM 699 OE2 GLU A 84 17.847 7.958 -49.043 1.00 30.76 O
ANISOU 699 OE2 GLU A 84 4121 3976 3590 136 144 -192 O
ATOM 700 N CYS A 85 16.939 12.769 -51.167 1.00 31.01 N
ANISOU 700 N CYS A 85 4222 4024 3534 308 395 -40 N
ATOM 701 CA CYS A 85 18.125 13.502 -51.543 1.00 29.95 C
ANISOU 701 CA CYS A 85 4115 3831 3432 303 450 -56 C
ATOM 702 C CYS A 85 19.253 13.068 -50.646 1.00 30.18 C
ANISOU 702 C CYS A 85 4143 3805 3517 241 419 -116 C
ATOM 703 O CYS A 85 19.028 12.383 -49.660 1.00 31.34 O
ANISOU 703 O CYS A 85 4277 3953 3675 211 365 -134 O
ATOM 704 CB CYS A 85 17.891 14.985 -51.340 1.00 29.57 C
ANISOU 704 CB CYS A 85 4113 3740 3379 341 538 -13 C
ATOM 705 SG CYS A 85 16.499 15.623 -52.297 1.00 30.08 S
ANISOU 705 SG CYS A 85 4179 3877 3373 434 581 73 S
ATOM 706 N ILE A 86 20.474 13.454 -51.008 1.00 31.33 N
ANISOU 706 N ILE A 86 4299 3908 3694 222 455 -147 N
ATOM 707 CA ILE A 86 21.580 13.587 -50.061 1.00 30.30 C
ANISOU 707 CA ILE A 86 4174 3726 3612 170 455 -197 C
ATOM 708 C ILE A 86 22.019 15.046 -50.121 1.00 31.64 C
ANISOU 708 C ILE A 86 4388 3842 3792 172 552 -192 C
ATOM 709 O ILE A 86 21.540 15.787 -50.978 1.00 32.64 O
ANISOU 709 O ILE A 86 4541 3969 3892 220 614 -146 O
ATOM 710 CB ILE A 86 22.767 12.709 -50.449 1.00 29.41 C
ANISOU 710 CB ILE A 86 4030 3614 3530 139 416 -249 C
ATOM 711 CG1 ILE A 86 23.055 12.839 -51.940 1.00 29.85 C
ANISOU 711 CG1 ILE A 86 4085 3684 3573 164 452 -242 C
ATOM 712 CG2 ILE A 86 22.477 11.258 -50.139 1.00 31.41 C
ANISOU 712 CG2 ILE A 86 4249 3901 3784 128 329 -262 C
ATOM 713 CD1 ILE A 86 24.517 13.066 -52.262 1.00 28.47 C
ANISOU 713 CD1 ILE A 86 3906 3476 3434 133 481 -290 C
ATOM 714 N HIS A 87 22.934 15.447 -49.231 1.00 32.49 N
ANISOU 714 N HIS A 87 4502 3906 3934 120 571 -239 N
ATOM 715 CA HIS A 87 23.628 16.747 -49.335 1.00 33.36 C
ANISOU 715 CA HIS A 87 4653 3959 4061 102 670 -254 C
ATOM 716 C HIS A 87 24.676 16.813 -50.427 1.00 34.69 C
ANISOU 716 C HIS A 87 4816 4119 4243 94 702 -280 C
ATOM 717 O HIS A 87 25.515 15.913 -50.552 1.00 33.76 O
ANISOU 717 O HIS A 87 4654 4025 4144 66 644 -324 O
ATOM 718 CB HIS A 87 24.285 17.117 -48.001 1.00 34.49 C
ANISOU 718 CB HIS A 87 4799 4073 4232 36 679 -308 C
ATOM 719 CG HIS A 87 23.296 17.475 -46.917 1.00 34.95 C
ANISOU 719 CG HIS A 87 4880 4123 4277 40 683 -284 C
ATOM 720 ND1 HIS A 87 22.708 16.540 -46.128 1.00 34.87 N
ANISOU 720 ND1 HIS A 87 4839 4152 4257 38 596 -278 N
ATOM 721 CD2 HIS A 87 22.771 18.706 -46.530 1.00 33.42 C
ANISOU 721 CD2 HIS A 87 4739 3879 4077 48 772 -262 C
ATOM 722 CE1 HIS A 87 21.853 17.150 -45.286 1.00 34.93 C
ANISOU 722 CE1 HIS A 87 4876 4143 4252 43 625 -255 C
ATOM 723 NE2 HIS A 87 21.900 18.476 -45.524 1.00 34.24 N
ANISOU 723 NE2 HIS A 87 4840 4001 4169 49 733 -247 N
ATOM 724 N LEU A 88 24.678 17.926 -51.168 1.00 34.37 N
ANISOU 724 N LEU A 88 4823 4040 4194 118 801 -253 N
ATOM 725 CA LEU A 88 25.682 18.210 -52.168 1.00 33.60 C
ANISOU 725 CA LEU A 88 4731 3925 4109 106 850 -276 C
ATOM 726 C LEU A 88 27.111 18.133 -51.592 1.00 35.67 C
ANISOU 726 C LEU A 88 4967 4171 4413 26 846 -362 C
ATOM 727 O LEU A 88 28.058 17.757 -52.302 1.00 35.80 O
ANISOU 727 O LEU A 88 4956 4200 4443 8 838 -397 O
ATOM 728 CB LEU A 88 25.427 19.585 -52.812 1.00 32.00 C
ANISOU 728 CB LEU A 88 4597 3668 3891 142 973 -230 C
ATOM 729 CG LEU A 88 24.422 19.684 -53.984 1.00 33.52 C
ANISOU 729 CG LEU A 88 4806 3893 4036 230 992 -146 C
ATOM 730 CD1 LEU A 88 24.080 21.141 -54.277 1.00 33.26 C
ANISOU 730 CD1 LEU A 88 4849 3797 3991 272 1121 -92 C
ATOM 731 CD2 LEU A 88 24.942 19.012 -55.271 1.00 32.54 C
ANISOU 731 CD2 LEU A 88 4650 3812 3900 240 964 -153 C
ATOM 732 N SER A 89 27.268 18.482 -50.316 1.00 34.75 N
ANISOU 732 N SER A 89 4855 4036 4313 -21 851 -396 N
ATOM 733 CA SER A 89 28.586 18.441 -49.665 1.00 34.91 C
ANISOU 733 CA SER A 89 4841 4059 4363 -99 844 -479 C
ATOM 734 C SER A 89 29.139 17.024 -49.444 1.00 34.39 C
ANISOU 734 C SER A 89 4702 4056 4309 -109 730 -511 C
ATOM 735 O SER A 89 30.340 16.858 -49.229 1.00 35.03 O
ANISOU 735 O SER A 89 4742 4154 4411 -159 720 -574 O
ATOM 736 CB SER A 89 28.555 19.192 -48.338 1.00 35.20 C
ANISOU 736 CB SER A 89 4898 4069 4405 -151 881 -509 C
ATOM 737 OG SER A 89 27.792 18.479 -47.372 1.00 35.76 O
ANISOU 737 OG SER A 89 4946 4175 4465 -138 796 -489 O
ATOM 738 N VAL A 90 28.275 16.008 -49.489 1.00 35.21 N
ANISOU 738 N VAL A 90 4787 4193 4397 -61 648 -468 N
ATOM 739 CA VAL A 90 28.738 14.597 -49.412 1.00 36.30 C
ANISOU 739 CA VAL A 90 4865 4379 4547 -61 550 -490 C
ATOM 740 C VAL A 90 29.693 14.290 -50.553 1.00 37.05 C
ANISOU 740 C VAL A 90 4936 4482 4657 -60 560 -518 C
ATOM 741 O VAL A 90 30.465 13.301 -50.514 1.00 40.20 O
ANISOU 741 O VAL A 90 5284 4913 5075 -68 499 -552 O
ATOM 742 CB VAL A 90 27.564 13.578 -49.480 1.00 38.02 C
ANISOU 742 CB VAL A 90 5077 4624 4744 -12 478 -440 C
ATOM 743 CG1 VAL A 90 28.094 12.160 -49.401 1.00 36.97 C
ANISOU 743 CG1 VAL A 90 4893 4524 4628 -12 393 -464 C
ATOM 744 CG2 VAL A 90 26.554 13.815 -48.354 1.00 37.89 C
ANISOU 744 CG2 VAL A 90 5081 4602 4711 -11 465 -411 C
ATOM 745 N LEU A 91 29.633 15.119 -51.587 1.00 34.78 N
ANISOU 745 N LEU A 91 4687 4166 4359 -46 639 -500 N
ATOM 746 CA LEU A 91 30.339 14.821 -52.815 1.00 34.62 C
ANISOU 746 CA LEU A 91 4651 4156 4347 -38 651 -516 C
ATOM 747 C LEU A 91 31.731 15.442 -52.812 1.00 37.82 C
ANISOU 747 C LEU A 91 5044 4546 4779 -95 706 -581 C
ATOM 748 O LEU A 91 32.504 15.259 -53.757 1.00 39.54 O
ANISOU 748 O LEU A 91 5244 4771 5006 -98 723 -606 O
ATOM 749 CB LEU A 91 29.507 15.261 -54.029 1.00 33.72 C
ANISOU 749 CB LEU A 91 4579 4031 4199 12 701 -457 C
ATOM 750 CG LEU A 91 28.140 14.557 -54.277 1.00 32.80 C
ANISOU 750 CG LEU A 91 4462 3950 4047 68 646 -397 C
ATOM 751 CD1 LEU A 91 27.418 15.112 -55.492 1.00 29.70 C
ANISOU 751 CD1 LEU A 91 4105 3564 3614 120 701 -340 C
ATOM 752 CD2 LEU A 91 28.294 13.038 -54.423 1.00 31.83 C
ANISOU 752 CD2 LEU A 91 4289 3871 3934 70 553 -420 C
ATOM 753 N HIS A 92 32.063 16.155 -51.735 1.00 39.46 N
ANISOU 753 N HIS A 92 5257 4738 4996 -145 736 -615 N
ATOM 754 CA HIS A 92 33.412 16.693 -51.581 1.00 41.01 C
ANISOU 754 CA HIS A 92 5431 4934 5214 -212 785 -689 C
ATOM 755 C HIS A 92 34.011 16.583 -50.205 1.00 42.80 C
ANISOU 755 C HIS A 92 5613 5197 5452 -267 747 -743 C
ATOM 756 O HIS A 92 35.236 16.531 -50.069 1.00 44.57 O
ANISOU 756 O HIS A 92 5787 5455 5691 -315 748 -810 O
ATOM 757 CB HIS A 92 33.512 18.119 -52.124 1.00 40.45 C
ANISOU 757 CB HIS A 92 5425 4801 5140 -236 913 -690 C
ATOM 758 CG HIS A 92 32.710 19.130 -51.357 1.00 39.45 C
ANISOU 758 CG HIS A 92 5359 4627 5003 -246 974 -666 C
ATOM 759 ND1 HIS A 92 33.172 19.722 -50.238 1.00 40.69 N
ANISOU 759 ND1 HIS A 92 5512 4778 5169 -316 1004 -722 N
ATOM 760 CD2 HIS A 92 31.456 19.687 -51.605 1.00 39.36 C
ANISOU 760 CD2 HIS A 92 5413 4572 4969 -190 1017 -590 C
ATOM 761 CE1 HIS A 92 32.258 20.602 -49.785 1.00 38.07 C
ANISOU 761 CE1 HIS A 92 5245 4392 4825 -308 1066 -686 C
ATOM 762 NE2 HIS A 92 31.210 20.582 -50.620 1.00 38.05 N
ANISOU 762 NE2 HIS A 92 5284 4366 4804 -226 1074 -602 N
ATOM 763 N LYS A 93 33.173 16.518 -49.174 1.00 44.09 N
ANISOU 763 N LYS A 93 5787 5361 5601 -260 711 -717 N
ATOM 764 CA LYS A 93 33.676 16.434 -47.794 1.00 47.52 C
ANISOU 764 CA LYS A 93 6180 5839 6038 -311 674 -765 C
ATOM 765 C LYS A 93 34.448 15.139 -47.542 1.00 47.99 C
ANISOU 765 C LYS A 93 6158 5969 6107 -300 574 -788 C
ATOM 766 O LYS A 93 33.990 14.055 -47.907 1.00 46.51 O
ANISOU 766 O LYS A 93 5958 5790 5921 -240 505 -745 O
ATOM 767 CB LYS A 93 32.528 16.536 -46.780 1.00 49.67 C
ANISOU 767 CB LYS A 93 6482 6099 6291 -299 651 -725 C
ATOM 768 CG LYS A 93 32.173 17.942 -46.319 1.00 53.77 C
ANISOU 768 CG LYS A 93 7062 6565 6802 -342 752 -735 C
ATOM 769 CD LYS A 93 30.967 17.897 -45.383 1.00 54.51 C
ANISOU 769 CD LYS A 93 7182 6652 6878 -321 721 -690 C
ATOM 770 CE LYS A 93 31.008 18.991 -44.324 1.00 56.97 C
ANISOU 770 CE LYS A 93 7521 6941 7183 -389 791 -732 C
ATOM 771 NZ LYS A 93 30.707 20.340 -44.877 1.00 57.66 N
ANISOU 771 NZ LYS A 93 7688 6945 7274 -397 923 -723 N
ATOM 772 N CYS A 94 35.618 15.268 -46.912 1.00 50.36 N
ANISOU 772 N CYS A 94 6401 6320 6411 -358 572 -858 N
ATOM 773 CA CYS A 94 36.391 14.123 -46.382 1.00 50.26 C
ANISOU 773 CA CYS A 94 6306 6387 6403 -345 479 -879 C
ATOM 774 C CYS A 94 37.082 13.239 -47.435 1.00 52.01 C
ANISOU 774 C CYS A 94 6487 6625 6646 -304 450 -882 C
ATOM 775 O CYS A 94 37.557 12.145 -47.109 1.00 55.07 O
ANISOU 775 O CYS A 94 6815 7067 7040 -272 372 -883 O
ATOM 776 CB CYS A 94 35.525 13.247 -45.462 1.00 53.71 C
ANISOU 776 CB CYS A 94 6740 6840 6826 -302 392 -827 C
ATOM 777 SG CYS A 94 34.815 14.095 -44.040 1.00 55.92 S
ANISOU 777 SG CYS A 94 7050 7117 7077 -350 411 -829 S
ATOM 778 N TYR A 95 37.132 13.693 -48.686 1.00 49.51 N
ANISOU 778 N TYR A 95 6207 6263 6341 -301 515 -882 N
ATOM 779 CA TYR A 95 37.925 13.004 -49.703 1.00 50.41 C
ANISOU 779 CA TYR A 95 6281 6395 6475 -276 502 -899 C
ATOM 780 C TYR A 95 39.416 13.229 -49.457 1.00 51.62 C
ANISOU 780 C TYR A 95 6362 6610 6637 -330 518 -978 C
ATOM 781 O TYR A 95 39.824 14.310 -49.038 1.00 51.78 O
ANISOU 781 O TYR A 95 6387 6636 6649 -402 582 -1027 O
ATOM 782 CB TYR A 95 37.560 13.492 -51.104 1.00 47.67 C
ANISOU 782 CB TYR A 95 5992 5988 6131 -261 572 -876 C
ATOM 783 CG TYR A 95 36.367 12.807 -51.697 1.00 46.58 C
ANISOU 783 CG TYR A 95 5894 5819 5984 -194 536 -805 C
ATOM 784 CD1 TYR A 95 35.070 13.179 -51.326 1.00 46.33 C
ANISOU 784 CD1 TYR A 95 5919 5753 5930 -177 541 -751 C
ATOM 785 CD2 TYR A 95 36.519 11.800 -52.652 1.00 47.00 C
ANISOU 785 CD2 TYR A 95 5927 5882 6049 -150 501 -796 C
ATOM 786 CE1 TYR A 95 33.958 12.555 -51.878 1.00 43.89 C
ANISOU 786 CE1 TYR A 95 5638 5428 5607 -120 509 -691 C
ATOM 787 CE2 TYR A 95 35.409 11.163 -53.207 1.00 45.81 C
ANISOU 787 CE2 TYR A 95 5809 5711 5885 -99 472 -740 C
ATOM 788 CZ TYR A 95 34.133 11.547 -52.818 1.00 45.53 C
ANISOU 788 CZ TYR A 95 5824 5651 5824 -85 474 -688 C
ATOM 789 OH TYR A 95 33.028 10.930 -53.361 1.00 44.69 O
ANISOU 789 OH TYR A 95 5742 5539 5699 -40 446 -638 O
ATOM 790 N ASP A 96 40.219 12.203 -49.722 1.00 51.54 N
ANISOU 790 N ASP A 96 6287 6651 6645 -296 464 -993 N
ATOM 791 CA ASP A 96 41.669 12.331 -49.684 1.00 52.39 C
ANISOU 791 CA ASP A 96 6317 6828 6760 -338 478 -1068 C
ATOM 792 C ASP A 96 42.108 13.098 -50.923 1.00 51.63 C
ANISOU 792 C ASP A 96 6248 6693 6675 -373 570 -1101 C
ATOM 793 O ASP A 96 42.242 12.525 -52.005 1.00 52.67 O
ANISOU 793 O ASP A 96 6380 6806 6824 -331 567 -1088 O
ATOM 794 CB ASP A 96 42.320 10.941 -49.637 1.00 55.08 C
ANISOU 794 CB ASP A 96 6582 7230 7116 -276 394 -1064 C
ATOM 795 CG ASP A 96 43.813 10.987 -49.315 1.00 57.61 C
ANISOU 795 CG ASP A 96 6803 7647 7436 -312 393 -1138 C
ATOM 796 OD1 ASP A 96 44.383 12.095 -49.185 1.00 57.24 O
ANISOU 796 OD1 ASP A 96 6746 7623 7378 -396 460 -1201 O
ATOM 797 OD2 ASP A 96 44.419 9.896 -49.196 1.00 58.97 O
ANISOU 797 OD2 ASP A 96 6909 7877 7621 -256 329 -1133 O
ATOM 798 N TYR A 97 42.306 14.401 -50.774 1.00 50.13 N
ANISOU 798 N TYR A 97 6086 6484 6474 -451 657 -1144 N
ATOM 799 CA TYR A 97 42.597 15.247 -51.928 1.00 52.52 C
ANISOU 799 CA TYR A 97 6433 6737 6786 -485 757 -1166 C
ATOM 800 C TYR A 97 44.022 15.099 -52.452 1.00 54.57 C
ANISOU 800 C TYR A 97 6618 7055 7060 -517 774 -1238 C
ATOM 801 O TYR A 97 44.258 15.254 -53.650 1.00 58.13 O
ANISOU 801 O TYR A 97 7093 7471 7522 -513 827 -1242 O
ATOM 802 CB TYR A 97 42.265 16.706 -51.641 1.00 50.77 C
ANISOU 802 CB TYR A 97 6280 6459 6551 -556 860 -1183 C
ATOM 803 CG TYR A 97 40.789 16.974 -51.669 1.00 51.32 C
ANISOU 803 CG TYR A 97 6440 6449 6608 -510 870 -1101 C
ATOM 804 CD1 TYR A 97 40.129 17.179 -52.876 1.00 51.19 C
ANISOU 804 CD1 TYR A 97 6494 6363 6592 -466 917 -1046 C
ATOM 805 CD2 TYR A 97 40.040 16.999 -50.491 1.00 50.57 C
ANISOU 805 CD2 TYR A 97 6356 6357 6498 -509 832 -1078 C
ATOM 806 CE1 TYR A 97 38.771 17.420 -52.916 1.00 51.36 C
ANISOU 806 CE1 TYR A 97 6589 6326 6597 -418 925 -969 C
ATOM 807 CE2 TYR A 97 38.680 17.231 -50.517 1.00 50.50 C
ANISOU 807 CE2 TYR A 97 6426 6283 6479 -465 841 -1003 C
ATOM 808 CZ TYR A 97 38.050 17.442 -51.736 1.00 53.36 C
ANISOU 808 CZ TYR A 97 6851 6582 6839 -418 887 -948 C
ATOM 809 OH TYR A 97 36.696 17.678 -51.786 1.00 54.13 O
ANISOU 809 OH TYR A 97 7018 6628 6921 -369 896 -873 O
ATOM 810 N ASP A 98 44.960 14.785 -51.561 1.00 54.20 N
ANISOU 810 N ASP A 98 6477 7105 7009 -545 729 -1294 N
ATOM 811 CA ASP A 98 46.362 14.600 -51.950 1.00 57.73 C
ANISOU 811 CA ASP A 98 6838 7627 7467 -573 739 -1366 C
ATOM 812 C ASP A 98 46.577 13.369 -52.841 1.00 57.24 C
ANISOU 812 C ASP A 98 6745 7572 7429 -487 683 -1336 C
ATOM 813 O ASP A 98 47.633 13.216 -53.456 1.00 58.58 O
ANISOU 813 O ASP A 98 6858 7786 7613 -500 703 -1387 O
ATOM 814 CB ASP A 98 47.256 14.507 -50.708 1.00 60.18 C
ANISOU 814 CB ASP A 98 7046 8058 7759 -615 695 -1428 C
ATOM 815 CG ASP A 98 47.557 15.868 -50.101 1.00 63.91 C
ANISOU 815 CG ASP A 98 7529 8543 8209 -732 781 -1500 C
ATOM 816 OD1 ASP A 98 47.866 16.803 -50.870 1.00 63.99 O
ANISOU 816 OD1 ASP A 98 7580 8504 8227 -796 887 -1542 O
ATOM 817 OD2 ASP A 98 47.486 16.000 -48.855 1.00 64.83 O
ANISOU 817 OD2 ASP A 98 7614 8717 8300 -763 748 -1516 O
ATOM 818 N ALA A 99 45.571 12.502 -52.905 1.00 54.10 N
ANISOU 818 N ALA A 99 6386 7131 7037 -405 619 -1257 N
ATOM 819 CA ALA A 99 45.706 11.219 -53.576 1.00 51.42 C
ANISOU 819 CA ALA A 99 6018 6797 6720 -325 563 -1229 C
ATOM 820 C ALA A 99 45.003 11.188 -54.930 1.00 49.79 C
ANISOU 820 C ALA A 99 5888 6507 6521 -296 602 -1189 C
ATOM 821 O ALA A 99 45.055 10.178 -55.628 1.00 51.49 O
ANISOU 821 O ALA A 99 6090 6717 6754 -237 568 -1171 O
ATOM 822 CB ALA A 99 45.198 10.099 -52.680 1.00 49.42 C
ANISOU 822 CB ALA A 99 5744 6566 6466 -255 463 -1176 C
ATOM 823 N ILE A 100 44.356 12.291 -55.297 1.00 46.62 N
ANISOU 823 N ILE A 100 5567 6042 6105 -335 676 -1174 N
ATOM 824 CA ILE A 100 43.652 12.374 -56.567 1.00 46.04 C
ANISOU 824 CA ILE A 100 5564 5900 6027 -307 717 -1132 C
ATOM 825 C ILE A 100 44.572 13.005 -57.610 1.00 48.02 C
ANISOU 825 C ILE A 100 5811 6149 6285 -352 802 -1183 C
ATOM 826 O ILE A 100 44.794 14.217 -57.588 1.00 49.18 O
ANISOU 826 O ILE A 100 5989 6273 6422 -418 886 -1213 O
ATOM 827 CB ILE A 100 42.309 13.152 -56.450 1.00 45.09 C
ANISOU 827 CB ILE A 100 5536 5712 5881 -305 749 -1071 C
ATOM 828 CG1 ILE A 100 41.369 12.455 -55.452 1.00 44.25 C
ANISOU 828 CG1 ILE A 100 5433 5611 5768 -261 664 -1021 C
ATOM 829 CG2 ILE A 100 41.625 13.269 -57.809 1.00 42.98 C
ANISOU 829 CG2 ILE A 100 5334 5393 5601 -273 792 -1025 C
ATOM 830 CD1 ILE A 100 40.272 13.343 -54.903 1.00 43.06 C
ANISOU 830 CD1 ILE A 100 5352 5413 5594 -274 694 -978 C
ATOM 831 N PRO A 101 45.119 12.172 -58.525 1.00 48.03 N
ANISOU 831 N PRO A 101 5776 6168 6303 -318 785 -1197 N
ATOM 832 CA PRO A 101 46.140 12.584 -59.491 1.00 48.69 C
ANISOU 832 CA PRO A 101 5841 6263 6396 -358 857 -1254 C
ATOM 833 C PRO A 101 45.726 13.779 -60.335 1.00 48.97 C
ANISOU 833 C PRO A 101 5963 6232 6410 -395 960 -1237 C
ATOM 834 O PRO A 101 46.499 14.737 -60.459 1.00 53.53 O
ANISOU 834 O PRO A 101 6539 6810 6988 -465 1043 -1291 O
ATOM 835 CB PRO A 101 46.312 11.338 -60.375 1.00 48.52 C
ANISOU 835 CB PRO A 101 5790 6254 6392 -296 812 -1245 C
ATOM 836 CG PRO A 101 45.929 10.206 -59.487 1.00 47.62 C
ANISOU 836 CG PRO A 101 5641 6162 6288 -237 712 -1214 C
ATOM 837 CD PRO A 101 44.797 10.739 -58.658 1.00 47.62 C
ANISOU 837 CD PRO A 101 5700 6128 6265 -242 700 -1163 C
ATOM 838 N TRP A 102 44.522 13.743 -60.903 1.00 47.91 N
ANISOU 838 N TRP A 102 5902 6044 6255 -347 960 -1163 N
ATOM 839 CA TRP A 102 44.106 14.799 -61.824 1.00 47.58 C
ANISOU 839 CA TRP A 102 5943 5944 6188 -363 1058 -1134 C
ATOM 840 C TRP A 102 43.919 16.136 -61.146 1.00 50.11 C
ANISOU 840 C TRP A 102 6316 6223 6499 -418 1133 -1136 C
ATOM 841 O TRP A 102 43.596 17.127 -61.800 1.00 49.32 O
ANISOU 841 O TRP A 102 6291 6066 6379 -430 1228 -1109 O
ATOM 842 CB TRP A 102 42.868 14.391 -62.621 1.00 47.37 C
ANISOU 842 CB TRP A 102 5972 5889 6135 -294 1036 -1053 C
ATOM 843 CG TRP A 102 41.606 14.192 -61.808 1.00 45.95 C
ANISOU 843 CG TRP A 102 5823 5696 5940 -253 978 -990 C
ATOM 844 CD1 TRP A 102 41.163 13.018 -61.203 1.00 46.43 C
ANISOU 844 CD1 TRP A 102 5845 5784 6010 -211 875 -973 C
ATOM 845 CD2 TRP A 102 40.557 15.188 -61.522 1.00 46.92 C
ANISOU 845 CD2 TRP A 102 6023 5770 6035 -248 1024 -931 C
ATOM 846 NE1 TRP A 102 39.953 13.218 -60.570 1.00 45.95 N
ANISOU 846 NE1 TRP A 102 5829 5700 5928 -186 852 -914 N
ATOM 847 CE2 TRP A 102 39.543 14.500 -60.716 1.00 46.20 C
ANISOU 847 CE2 TRP A 102 5928 5689 5938 -204 937 -887 C
ATOM 848 CE3 TRP A 102 40.378 16.539 -61.822 1.00 46.43 C
ANISOU 848 CE3 TRP A 102 6032 5655 5955 -272 1131 -911 C
ATOM 849 CZ2 TRP A 102 38.405 15.147 -60.255 1.00 45.69 C
ANISOU 849 CZ2 TRP A 102 5923 5590 5848 -186 953 -827 C
ATOM 850 CZ3 TRP A 102 39.225 17.180 -61.356 1.00 46.14 C
ANISOU 850 CZ3 TRP A 102 6058 5577 5894 -247 1150 -847 C
ATOM 851 CH2 TRP A 102 38.262 16.500 -60.588 1.00 46.35 C
ANISOU 851 CH2 TRP A 102 6073 5621 5914 -205 1061 -807 C
ATOM 852 N LEU A 103 44.168 16.183 -59.834 1.00 53.01 N
ANISOU 852 N LEU A 103 6642 6619 6877 -451 1098 -1170 N
ATOM 853 CA LEU A 103 43.937 17.393 -59.042 1.00 56.50 C
ANISOU 853 CA LEU A 103 7133 7023 7310 -507 1167 -1177 C
ATOM 854 C LEU A 103 45.209 18.042 -58.485 1.00 61.60 C
ANISOU 854 C LEU A 103 7730 7706 7969 -605 1221 -1276 C
ATOM 855 O LEU A 103 45.140 19.102 -57.857 1.00 59.72 O
ANISOU 855 O LEU A 103 7532 7433 7723 -666 1293 -1297 O
ATOM 856 CB LEU A 103 42.936 17.120 -57.904 1.00 54.37 C
ANISOU 856 CB LEU A 103 6872 6752 7031 -474 1095 -1131 C
ATOM 857 CG LEU A 103 41.435 17.204 -58.238 1.00 53.60 C
ANISOU 857 CG LEU A 103 6857 6597 6911 -406 1092 -1034 C
ATOM 858 CD1 LEU A 103 40.572 16.847 -57.031 1.00 51.21 C
ANISOU 858 CD1 LEU A 103 6551 6304 6602 -381 1017 -999 C
ATOM 859 CD2 LEU A 103 41.052 18.574 -58.784 1.00 52.35 C
ANISOU 859 CD2 LEU A 103 6793 6361 6735 -426 1218 -1006 C
ATOM 860 N GLN A 104 46.365 17.426 -58.739 1.00 68.00 N
ANISOU 860 N GLN A 104 8453 8585 8796 -621 1193 -1339 N
ATOM 861 CA GLN A 104 47.642 17.897 -58.166 1.00 72.28 C
ANISOU 861 CA GLN A 104 8927 9189 9346 -714 1231 -1441 C
ATOM 862 C GLN A 104 48.090 19.265 -58.679 1.00 72.89 C
ANISOU 862 C GLN A 104 9062 9213 9419 -802 1376 -1487 C
ATOM 863 O GLN A 104 48.681 20.043 -57.932 1.00 71.73 O
ANISOU 863 O GLN A 104 8897 9088 9269 -895 1432 -1559 O
ATOM 864 CB GLN A 104 48.759 16.865 -58.366 1.00 74.75 C
ANISOU 864 CB GLN A 104 9127 9596 9676 -699 1166 -1493 C
ATOM 865 CG GLN A 104 48.578 15.565 -57.584 1.00 80.55 C
ANISOU 865 CG GLN A 104 9791 10394 10417 -625 1031 -1464 C
ATOM 866 CD GLN A 104 48.467 15.773 -56.077 1.00 85.30 C
ANISOU 866 CD GLN A 104 10363 11040 11005 -657 992 -1480 C
ATOM 867 OE1 GLN A 104 47.388 16.081 -55.550 1.00 86.75 O
ANISOU 867 OE1 GLN A 104 10613 11169 11175 -644 987 -1426 O
ATOM 868 NE2 GLN A 104 49.578 15.574 -55.370 1.00 86.53 N
ANISOU 868 NE2 GLN A 104 10412 11303 11160 -696 963 -1553 N
ATOM 869 N ASN A 105 47.798 19.555 -59.946 1.00 75.44 N
ANISOU 869 N ASN A 105 9456 9467 9738 -777 1443 -1445 N
ATOM 870 CA ASN A 105 48.164 20.846 -60.559 1.00 80.35 C
ANISOU 870 CA ASN A 105 10148 10024 10354 -851 1592 -1476 C
ATOM 871 C ASN A 105 47.253 22.022 -60.164 1.00 79.32 C
ANISOU 871 C ASN A 105 10129 9798 10211 -871 1681 -1433 C
ATOM 872 O ASN A 105 47.395 23.132 -60.686 1.00 79.59 O
ANISOU 872 O ASN A 105 10241 9758 10240 -922 1816 -1444 O
ATOM 873 CB ASN A 105 48.255 20.722 -62.093 1.00 85.94 C
ANISOU 873 CB ASN A 105 10891 10701 11060 -814 1634 -1445 C
ATOM 874 CG ASN A 105 47.043 20.023 -62.711 1.00 90.90 C
ANISOU 874 CG ASN A 105 11562 11300 11672 -700 1567 -1337 C
ATOM 875 OD1 ASN A 105 45.998 19.851 -62.069 1.00 86.10 O
ANISOU 875 OD1 ASN A 105 10982 10675 11056 -651 1512 -1275 O
ATOM 876 ND2 ASN A 105 47.184 19.614 -63.971 1.00 91.07 N
ANISOU 876 ND2 ASN A 105 11589 11324 11689 -663 1575 -1318 N
ATOM 877 N VAL A 106 46.322 21.761 -59.248 1.00 77.04 N
ANISOU 877 N VAL A 106 9849 9506 9915 -828 1609 -1384 N
ATOM 878 CA VAL A 106 45.390 22.773 -58.743 1.00 75.20 C
ANISOU 878 CA VAL A 106 9714 9188 9671 -836 1682 -1342 C
ATOM 879 C VAL A 106 45.694 23.011 -57.264 1.00 75.69 C
ANISOU 879 C VAL A 106 9730 9292 9736 -911 1665 -1410 C
ATOM 880 O VAL A 106 45.790 22.054 -56.486 1.00 73.62 O
ANISOU 880 O VAL A 106 9380 9115 9475 -889 1541 -1423 O
ATOM 881 CB VAL A 106 43.916 22.306 -58.895 1.00 73.14 C
ANISOU 881 CB VAL A 106 9503 8890 9393 -722 1616 -1223 C
ATOM 882 CG1 VAL A 106 42.948 23.410 -58.497 1.00 72.02 C
ANISOU 882 CG1 VAL A 106 9467 8656 9239 -721 1703 -1173 C
ATOM 883 CG2 VAL A 106 43.634 21.834 -60.316 1.00 69.66 C
ANISOU 883 CG2 VAL A 106 9086 8439 8942 -645 1607 -1160 C
ATOM 884 N GLU A 107 45.849 24.275 -56.870 1.00 78.09 N
ANISOU 884 N GLU A 107 10094 9538 10039 -1000 1792 -1455 N
ATOM 885 CA GLU A 107 46.126 24.581 -55.462 1.00 82.32 C
ANISOU 885 CA GLU A 107 10588 10118 10571 -1082 1785 -1528 C
ATOM 886 C GLU A 107 44.943 24.226 -54.536 1.00 78.49 C
ANISOU 886 C GLU A 107 10119 9627 10076 -1017 1700 -1458 C
ATOM 887 O GLU A 107 43.777 24.481 -54.870 1.00 73.09 O
ANISOU 887 O GLU A 107 9527 8856 9386 -944 1723 -1363 O
ATOM 888 CB GLU A 107 46.629 26.028 -55.259 1.00 92.07 C
ANISOU 888 CB GLU A 107 11883 11290 11806 -1208 1953 -1607 C
ATOM 889 CG GLU A 107 45.554 27.102 -55.189 1.00 98.95 C
ANISOU 889 CG GLU A 107 12892 12027 12675 -1195 2064 -1544 C
ATOM 890 CD GLU A 107 45.218 27.687 -56.547 1.00105.51 C
ANISOU 890 CD GLU A 107 13830 12748 13508 -1148 2173 -1474 C
ATOM 891 OE1 GLU A 107 44.829 26.913 -57.456 1.00108.24 O
ANISOU 891 OE1 GLU A 107 14168 13106 13849 -1044 2100 -1395 O
ATOM 892 OE2 GLU A 107 45.334 28.923 -56.703 1.00105.71 O
ANISOU 892 OE2 GLU A 107 13949 12677 13538 -1215 2336 -1499 O
ATOM 893 N PRO A 108 45.256 23.604 -53.382 1.00 77.46 N
ANISOU 893 N PRO A 108 9895 9596 9939 -1041 1599 -1504 N
ATOM 894 CA PRO A 108 44.328 22.910 -52.485 1.00 76.16 C
ANISOU 894 CA PRO A 108 9714 9456 9764 -974 1486 -1445 C
ATOM 895 C PRO A 108 42.931 23.523 -52.343 1.00 76.44 C
ANISOU 895 C PRO A 108 9862 9387 9794 -929 1531 -1361 C
ATOM 896 O PRO A 108 41.946 22.783 -52.300 1.00 73.06 O
ANISOU 896 O PRO A 108 9441 8955 9360 -833 1440 -1276 O
ATOM 897 CB PRO A 108 45.065 22.943 -51.146 1.00 76.52 C
ANISOU 897 CB PRO A 108 9675 9601 9798 -1064 1455 -1539 C
ATOM 898 CG PRO A 108 46.509 22.877 -51.529 1.00 76.62 C
ANISOU 898 CG PRO A 108 9603 9692 9815 -1131 1475 -1633 C
ATOM 899 CD PRO A 108 46.648 23.514 -52.890 1.00 76.58 C
ANISOU 899 CD PRO A 108 9675 9595 9826 -1137 1590 -1622 C
ATOM 900 N ASN A 109 42.850 24.853 -52.279 1.00 78.93 N
ANISOU 900 N ASN A 109 10263 9616 10109 -997 1675 -1386 N
ATOM 901 CA ASN A 109 41.590 25.540 -51.949 1.00 79.67 C
ANISOU 901 CA ASN A 109 10459 9613 10196 -961 1730 -1316 C
ATOM 902 C ASN A 109 40.496 25.503 -53.035 1.00 75.35 C
ANISOU 902 C ASN A 109 9995 8986 9647 -843 1742 -1194 C
ATOM 903 O ASN A 109 39.315 25.694 -52.730 1.00 77.15 O
ANISOU 903 O ASN A 109 10283 9164 9866 -784 1741 -1118 O
ATOM 904 CB ASN A 109 41.848 26.982 -51.460 1.00 82.86 C
ANISOU 904 CB ASN A 109 10933 9945 10603 -1072 1889 -1384 C
ATOM 905 CG ASN A 109 42.639 27.814 -52.462 1.00 90.01 C
ANISOU 905 CG ASN A 109 11886 10790 11521 -1130 2030 -1426 C
ATOM 906 OD1 ASN A 109 42.078 28.370 -53.411 1.00 90.83 O
ANISOU 906 OD1 ASN A 109 12090 10792 11629 -1074 2120 -1352 O
ATOM 907 ND2 ASN A 109 43.950 27.917 -52.245 1.00 91.43 N
ANISOU 907 ND2 ASN A 109 11994 11040 11704 -1243 2054 -1545 N
ATOM 908 N LEU A 110 40.885 25.248 -54.286 1.00 69.31 N
ANISOU 908 N LEU A 110 9229 8219 8886 -811 1753 -1175 N
ATOM 909 CA LEU A 110 39.916 25.120 -55.384 1.00 63.75 C
ANISOU 909 CA LEU A 110 8588 7463 8170 -699 1756 -1062 C
ATOM 910 C LEU A 110 39.492 23.670 -55.642 1.00 61.50 C
ANISOU 910 C LEU A 110 8233 7254 7876 -609 1598 -1011 C
ATOM 911 O LEU A 110 38.560 23.418 -56.411 1.00 62.24 O
ANISOU 911 O LEU A 110 8368 7327 7954 -516 1579 -918 O
ATOM 912 CB LEU A 110 40.465 25.726 -56.684 1.00 64.88 C
ANISOU 912 CB LEU A 110 8781 7555 8315 -710 1868 -1063 C
ATOM 913 CG LEU A 110 40.634 27.244 -56.834 1.00 65.19 C
ANISOU 913 CG LEU A 110 8924 7485 8359 -772 2054 -1081 C
ATOM 914 CD1 LEU A 110 40.482 27.632 -58.298 1.00 64.16 C
ANISOU 914 CD1 LEU A 110 8866 7293 8216 -714 2138 -1013 C
ATOM 915 CD2 LEU A 110 39.644 28.018 -55.982 1.00 64.75 C
ANISOU 915 CD2 LEU A 110 8945 7356 8299 -761 2110 -1042 C
ATOM 916 N ARG A 111 40.175 22.723 -55.000 1.00 56.82 N
ANISOU 916 N ARG A 111 7538 6754 7294 -637 1490 -1070 N
ATOM 917 CA ARG A 111 39.963 21.304 -55.264 1.00 54.72 C
ANISOU 917 CA ARG A 111 7207 6557 7026 -562 1353 -1034 C
ATOM 918 C ARG A 111 38.534 20.828 -54.972 1.00 54.61 C
ANISOU 918 C ARG A 111 7221 6532 6996 -476 1281 -943 C
ATOM 919 O ARG A 111 37.890 20.243 -55.856 1.00 54.25 O
ANISOU 919 O ARG A 111 7187 6486 6937 -398 1242 -876 O
ATOM 920 CB ARG A 111 40.984 20.446 -54.514 1.00 53.56 C
ANISOU 920 CB ARG A 111 6948 6507 6893 -604 1261 -1112 C
ATOM 921 CG ARG A 111 42.340 20.416 -55.180 1.00 54.99 C
ANISOU 921 CG ARG A 111 7078 6725 7088 -654 1294 -1186 C
ATOM 922 CD ARG A 111 43.384 19.758 -54.304 1.00 55.93 C
ANISOU 922 CD ARG A 111 7084 6948 7216 -699 1218 -1265 C
ATOM 923 NE ARG A 111 44.727 19.964 -54.846 1.00 57.65 N
ANISOU 923 NE ARG A 111 7253 7204 7445 -763 1270 -1348 N
ATOM 924 CZ ARG A 111 45.834 19.437 -54.330 1.00 57.24 C
ANISOU 924 CZ ARG A 111 7093 7255 7398 -801 1217 -1423 C
ATOM 925 NH1 ARG A 111 45.768 18.662 -53.252 1.00 59.34 N
ANISOU 925 NH1 ARG A 111 7292 7595 7659 -778 1110 -1422 N
ATOM 926 NH2 ARG A 111 47.005 19.689 -54.888 1.00 53.47 N
ANISOU 926 NH2 ARG A 111 6573 6811 6930 -860 1272 -1498 N
ATOM 927 N PRO A 112 38.032 21.070 -53.736 1.00 50.68 N
ANISOU 927 N PRO A 112 6731 6031 6494 -495 1265 -944 N
ATOM 928 CA PRO A 112 36.700 20.579 -53.420 1.00 49.05 C
ANISOU 928 CA PRO A 112 6544 5820 6271 -418 1195 -863 C
ATOM 929 C PRO A 112 35.658 20.972 -54.451 1.00 48.21 C
ANISOU 929 C PRO A 112 6516 5657 6144 -343 1246 -772 C
ATOM 930 O PRO A 112 34.819 20.150 -54.796 1.00 49.74 O
ANISOU 930 O PRO A 112 6700 5877 6323 -268 1169 -710 O
ATOM 931 CB PRO A 112 36.405 21.219 -52.058 1.00 51.43 C
ANISOU 931 CB PRO A 112 6864 6105 6570 -466 1218 -885 C
ATOM 932 CG PRO A 112 37.748 21.295 -51.408 1.00 51.41 C
ANISOU 932 CG PRO A 112 6796 6153 6582 -562 1222 -990 C
ATOM 933 CD PRO A 112 38.720 21.589 -52.536 1.00 51.50 C
ANISOU 933 CD PRO A 112 6807 6155 6606 -589 1291 -1027 C
ATOM 934 N LYS A 113 35.729 22.197 -54.963 1.00 50.54 N
ANISOU 934 N LYS A 113 6886 5879 6438 -361 1379 -765 N
ATOM 935 CA LYS A 113 34.749 22.687 -55.941 1.00 51.81 C
ANISOU 935 CA LYS A 113 7122 5989 6572 -281 1439 -671 C
ATOM 936 C LYS A 113 34.807 21.900 -57.241 1.00 49.09 C
ANISOU 936 C LYS A 113 6752 5686 6214 -227 1393 -639 C
ATOM 937 O LYS A 113 33.772 21.614 -57.857 1.00 47.59 O
ANISOU 937 O LYS A 113 6581 5507 5992 -143 1365 -557 O
ATOM 938 CB LYS A 113 34.982 24.164 -56.244 1.00 57.49 C
ANISOU 938 CB LYS A 113 7931 6617 7296 -315 1603 -674 C
ATOM 939 CG LYS A 113 33.739 24.904 -56.712 1.00 63.47 C
ANISOU 939 CG LYS A 113 8777 7312 8024 -228 1675 -567 C
ATOM 940 CD LYS A 113 33.259 25.903 -55.657 1.00 68.99 C
ANISOU 940 CD LYS A 113 9539 7942 8732 -254 1755 -567 C
ATOM 941 CE LYS A 113 32.663 25.204 -54.438 1.00 70.87 C
ANISOU 941 CE LYS A 113 9725 8230 8970 -252 1642 -573 C
ATOM 942 NZ LYS A 113 32.772 26.041 -53.209 1.00 75.66 N
ANISOU 942 NZ LYS A 113 10363 8786 9594 -325 1710 -626 N
ATOM 943 N LEU A 114 36.020 21.570 -57.668 1.00 47.17 N
ANISOU 943 N LEU A 114 6461 5471 5990 -276 1389 -708 N
ATOM 944 CA LEU A 114 36.205 20.798 -58.884 1.00 45.82 C
ANISOU 944 CA LEU A 114 6261 5340 5808 -235 1350 -691 C
ATOM 945 C LEU A 114 35.721 19.359 -58.695 1.00 43.53 C
ANISOU 945 C LEU A 114 5905 5121 5513 -188 1208 -675 C
ATOM 946 O LEU A 114 34.944 18.851 -59.508 1.00 42.84 O
ANISOU 946 O LEU A 114 5824 5056 5397 -121 1173 -614 O
ATOM 947 CB LEU A 114 37.662 20.839 -59.331 1.00 47.05 C
ANISOU 947 CB LEU A 114 6380 5507 5987 -303 1387 -774 C
ATOM 948 CG LEU A 114 38.035 22.038 -60.204 1.00 50.08 C
ANISOU 948 CG LEU A 114 6837 5824 6364 -325 1532 -769 C
ATOM 949 CD1 LEU A 114 39.541 22.132 -60.377 1.00 50.48 C
ANISOU 949 CD1 LEU A 114 6846 5891 6443 -412 1571 -868 C
ATOM 950 CD2 LEU A 114 37.342 21.968 -61.561 1.00 51.00 C
ANISOU 950 CD2 LEU A 114 6996 5938 6444 -242 1549 -684 C
ATOM 951 N LEU A 115 36.154 18.716 -57.612 1.00 41.62 N
ANISOU 951 N LEU A 115 5601 4916 5296 -225 1130 -728 N
ATOM 952 CA LEU A 115 35.721 17.351 -57.326 1.00 41.04 C
ANISOU 952 CA LEU A 115 5472 4898 5222 -184 1005 -713 C
ATOM 953 C LEU A 115 34.195 17.253 -57.313 1.00 40.26 C
ANISOU 953 C LEU A 115 5413 4793 5091 -117 977 -628 C
ATOM 954 O LEU A 115 33.615 16.330 -57.909 1.00 44.23 O
ANISOU 954 O LEU A 115 5898 5332 5575 -66 914 -593 O
ATOM 955 CB LEU A 115 36.305 16.841 -56.010 1.00 40.73 C
ANISOU 955 CB LEU A 115 5371 4894 5208 -227 937 -770 C
ATOM 956 CG LEU A 115 35.980 15.374 -55.700 1.00 41.99 C
ANISOU 956 CG LEU A 115 5477 5105 5371 -184 815 -756 C
ATOM 957 CD1 LEU A 115 36.532 14.402 -56.752 1.00 40.23 C
ANISOU 957 CD1 LEU A 115 5213 4913 5157 -161 780 -772 C
ATOM 958 CD2 LEU A 115 36.478 15.003 -54.313 1.00 42.37 C
ANISOU 958 CD2 LEU A 115 5472 5188 5437 -219 756 -800 C
ATOM 959 N LEU A 116 33.550 18.226 -56.681 1.00 36.95 N
ANISOU 959 N LEU A 116 5047 4329 4661 -118 1032 -598 N
ATOM 960 CA LEU A 116 32.089 18.287 -56.633 1.00 37.07 C
ANISOU 960 CA LEU A 116 5100 4340 4643 -54 1018 -516 C
ATOM 961 C LEU A 116 31.531 18.385 -58.034 1.00 36.84 C
ANISOU 961 C LEU A 116 5101 4319 4577 7 1051 -454 C
ATOM 962 O LEU A 116 30.596 17.676 -58.395 1.00 35.66 O
ANISOU 962 O LEU A 116 4937 4213 4397 62 989 -406 O
ATOM 963 CB LEU A 116 31.601 19.484 -55.788 1.00 36.00 C
ANISOU 963 CB LEU A 116 5024 4146 4506 -66 1094 -497 C
ATOM 964 CG LEU A 116 30.088 19.793 -55.834 1.00 36.58 C
ANISOU 964 CG LEU A 116 5144 4212 4543 7 1103 -406 C
ATOM 965 CD1 LEU A 116 29.321 18.725 -55.069 1.00 35.33 C
ANISOU 965 CD1 LEU A 116 4940 4105 4378 27 987 -394 C
ATOM 966 CD2 LEU A 116 29.736 21.195 -55.308 1.00 35.40 C
ANISOU 966 CD2 LEU A 116 5068 3986 4393 1 1215 -384 C
ATOM 967 N LYS A 117 32.121 19.269 -58.823 1.00 39.14 N
ANISOU 967 N LYS A 117 5432 4571 4867 -4 1151 -458 N
ATOM 968 CA LYS A 117 31.655 19.520 -60.175 1.00 41.43 C
ANISOU 968 CA LYS A 117 5756 4869 5117 55 1196 -394 C
ATOM 969 C LYS A 117 31.792 18.263 -61.062 1.00 39.84 C
ANISOU 969 C LYS A 117 5496 4738 4902 73 1113 -406 C
ATOM 970 O LYS A 117 30.884 17.936 -61.833 1.00 38.84 O
ANISOU 970 O LYS A 117 5371 4656 4728 134 1090 -346 O
ATOM 971 CB LYS A 117 32.430 20.688 -60.759 1.00 43.63 C
ANISOU 971 CB LYS A 117 6090 5084 5401 27 1325 -405 C
ATOM 972 CG LYS A 117 31.893 21.214 -62.065 1.00 47.65 C
ANISOU 972 CG LYS A 117 6650 5591 5863 96 1394 -326 C
ATOM 973 CD LYS A 117 33.043 21.745 -62.912 1.00 49.56 C
ANISOU 973 CD LYS A 117 6914 5799 6117 54 1484 -364 C
ATOM 974 CE LYS A 117 32.602 22.929 -63.738 1.00 54.06 C
ANISOU 974 CE LYS A 117 7571 6318 6648 108 1609 -283 C
ATOM 975 NZ LYS A 117 33.764 23.793 -64.083 1.00 60.85 N
ANISOU 975 NZ LYS A 117 8474 7110 7535 45 1727 -331 N
ATOM 976 N HIS A 118 32.909 17.550 -60.921 1.00 39.04 N
ANISOU 976 N HIS A 118 5340 4653 4840 19 1071 -485 N
ATOM 977 CA HIS A 118 33.149 16.319 -61.704 1.00 40.03 C
ANISOU 977 CA HIS A 118 5411 4836 4960 31 999 -506 C
ATOM 978 C HIS A 118 32.356 15.144 -61.208 1.00 39.09 C
ANISOU 978 C HIS A 118 5253 4764 4836 56 891 -494 C
ATOM 979 O HIS A 118 31.798 14.381 -62.019 1.00 41.26 O
ANISOU 979 O HIS A 118 5511 5086 5079 91 851 -471 O
ATOM 980 CB HIS A 118 34.644 15.996 -61.785 1.00 40.57 C
ANISOU 980 CB HIS A 118 5436 4906 5073 -26 1000 -590 C
ATOM 981 CG HIS A 118 35.433 17.013 -62.573 1.00 43.36 C
ANISOU 981 CG HIS A 118 5825 5222 5425 -53 1110 -605 C
ATOM 982 ND1 HIS A 118 36.200 16.681 -63.633 1.00 44.92 N
ANISOU 982 ND1 HIS A 118 6001 5441 5623 -63 1125 -636 N
ATOM 983 CD2 HIS A 118 35.515 18.404 -62.449 1.00 43.69 C
ANISOU 983 CD2 HIS A 118 5931 5202 5465 -73 1219 -591 C
ATOM 984 CE1 HIS A 118 36.757 17.799 -64.144 1.00 45.30 C
ANISOU 984 CE1 HIS A 118 6096 5445 5669 -89 1235 -641 C
ATOM 985 NE2 HIS A 118 36.329 18.850 -63.424 1.00 43.32 N
ANISOU 985 NE2 HIS A 118 5901 5141 5417 -95 1295 -612 N
ATOM 986 N ASN A 119 32.269 14.993 -59.883 1.00 36.80 N
ANISOU 986 N ASN A 119 4949 4461 4571 35 848 -510 N
ATOM 987 CA ASN A 119 31.378 14.007 -59.307 1.00 34.99 C
ANISOU 987 CA ASN A 119 4695 4266 4334 60 757 -490 C
ATOM 988 C ASN A 119 29.964 14.208 -59.835 1.00 34.40 C
ANISOU 988 C ASN A 119 4651 4214 4203 117 764 -414 C
ATOM 989 O ASN A 119 29.317 13.250 -60.305 1.00 34.47 O
ANISOU 989 O ASN A 119 4634 4274 4186 141 705 -400 O
ATOM 990 CB ASN A 119 31.381 14.066 -57.768 1.00 35.40 C
ANISOU 990 CB ASN A 119 4738 4297 4413 32 725 -508 C
ATOM 991 CG ASN A 119 32.502 13.254 -57.141 1.00 34.30 C
ANISOU 991 CG ASN A 119 4542 4170 4318 -6 671 -576 C
ATOM 992 OD1 ASN A 119 32.659 13.243 -55.914 1.00 38.66 O
ANISOU 992 OD1 ASN A 119 5080 4719 4890 -31 642 -596 O
ATOM 993 ND2 ASN A 119 33.288 12.597 -57.958 1.00 32.24 N
ANISOU 993 ND2 ASN A 119 4248 3929 4071 -9 659 -611 N
ATOM 994 N LEU A 120 29.478 15.444 -59.780 1.00 31.65 N
ANISOU 994 N LEU A 120 4356 3833 3834 137 839 -365 N
ATOM 995 CA LEU A 120 28.160 15.734 -60.326 1.00 32.59 C
ANISOU 995 CA LEU A 120 4501 3984 3895 202 852 -286 C
ATOM 996 C LEU A 120 28.061 15.312 -61.806 1.00 34.35 C
ANISOU 996 C LEU A 120 4710 4265 4076 231 852 -269 C
ATOM 997 O LEU A 120 27.072 14.693 -62.224 1.00 37.00 O
ANISOU 997 O LEU A 120 5025 4667 4365 267 805 -235 O
ATOM 998 CB LEU A 120 27.785 17.212 -60.138 1.00 32.70 C
ANISOU 998 CB LEU A 120 4582 3946 3896 228 950 -233 C
ATOM 999 CG LEU A 120 27.321 17.678 -58.739 1.00 32.86 C
ANISOU 999 CG LEU A 120 4623 3926 3936 217 952 -226 C
ATOM 1000 CD1 LEU A 120 27.166 19.201 -58.704 1.00 32.93 C
ANISOU 1000 CD1 LEU A 120 4705 3867 3938 238 1072 -183 C
ATOM 1001 CD2 LEU A 120 26.024 16.986 -58.310 1.00 30.55 C
ANISOU 1001 CD2 LEU A 120 4305 3687 3612 255 873 -186 C
ATOM 1002 N PHE A 121 29.091 15.611 -62.594 1.00 34.02 N
ANISOU 1002 N PHE A 121 4676 4203 4046 210 905 -298 N
ATOM 1003 CA PHE A 121 29.055 15.221 -63.994 1.00 34.72 C
ANISOU 1003 CA PHE A 121 4750 4347 4092 234 908 -286 C
ATOM 1004 C PHE A 121 28.870 13.717 -64.107 1.00 33.78 C
ANISOU 1004 C PHE A 121 4572 4288 3973 221 811 -324 C
ATOM 1005 O PHE A 121 27.944 13.256 -64.781 1.00 34.48 O
ANISOU 1005 O PHE A 121 4647 4449 4006 254 782 -290 O
ATOM 1006 CB PHE A 121 30.304 15.685 -64.768 1.00 34.83 C
ANISOU 1006 CB PHE A 121 4778 4329 4126 204 978 -322 C
ATOM 1007 CG PHE A 121 30.309 15.251 -66.210 1.00 34.36 C
ANISOU 1007 CG PHE A 121 4703 4330 4021 224 981 -315 C
ATOM 1008 CD1 PHE A 121 30.712 13.970 -66.564 1.00 33.08 C
ANISOU 1008 CD1 PHE A 121 4486 4210 3872 197 913 -374 C
ATOM 1009 CD2 PHE A 121 29.876 16.118 -67.216 1.00 34.86 C
ANISOU 1009 CD2 PHE A 121 4807 4411 4024 274 1055 -246 C
ATOM 1010 CE1 PHE A 121 30.702 13.572 -67.887 1.00 34.05 C
ANISOU 1010 CE1 PHE A 121 4594 4392 3949 209 918 -372 C
ATOM 1011 CE2 PHE A 121 29.842 15.714 -68.532 1.00 33.65 C
ANISOU 1011 CE2 PHE A 121 4637 4326 3821 291 1055 -238 C
ATOM 1012 CZ PHE A 121 30.262 14.443 -68.869 1.00 33.61 C
ANISOU 1012 CZ PHE A 121 4575 4363 3830 254 986 -306 C
ATOM 1013 N LEU A 122 29.737 12.953 -63.439 1.00 33.99 N
ANISOU 1013 N LEU A 122 4565 4289 4058 173 764 -394 N
ATOM 1014 CA LEU A 122 29.625 11.478 -63.452 1.00 32.97 C
ANISOU 1014 CA LEU A 122 4387 4200 3937 160 680 -432 C
ATOM 1015 C LEU A 122 28.229 10.983 -63.090 1.00 33.67 C
ANISOU 1015 C LEU A 122 4471 4334 3989 186 625 -392 C
ATOM 1016 O LEU A 122 27.633 10.198 -63.825 1.00 35.56 O
ANISOU 1016 O LEU A 122 4688 4635 4188 195 594 -391 O
ATOM 1017 CB LEU A 122 30.665 10.831 -62.546 1.00 31.74 C
ANISOU 1017 CB LEU A 122 4201 4006 3851 119 640 -498 C
ATOM 1018 CG LEU A 122 32.119 10.974 -63.003 1.00 32.46 C
ANISOU 1018 CG LEU A 122 4278 4074 3980 88 679 -554 C
ATOM 1019 CD1 LEU A 122 33.091 10.523 -61.914 1.00 30.67 C
ANISOU 1019 CD1 LEU A 122 4017 3819 3815 55 642 -609 C
ATOM 1020 CD2 LEU A 122 32.345 10.216 -64.311 1.00 32.00 C
ANISOU 1020 CD2 LEU A 122 4198 4055 3903 91 676 -577 C
ATOM 1021 N LEU A 123 27.692 11.460 -61.973 1.00 34.78 N
ANISOU 1021 N LEU A 123 4630 4448 4138 194 618 -363 N
ATOM 1022 CA LEU A 123 26.383 10.999 -61.529 1.00 33.65 C
ANISOU 1022 CA LEU A 123 4478 4346 3961 214 568 -329 C
ATOM 1023 C LEU A 123 25.306 11.387 -62.522 1.00 34.21 C
ANISOU 1023 C LEU A 123 4556 4487 3954 262 593 -268 C
ATOM 1024 O LEU A 123 24.349 10.640 -62.704 1.00 35.20 O
ANISOU 1024 O LEU A 123 4655 4679 4039 270 546 -259 O
ATOM 1025 CB LEU A 123 26.020 11.560 -60.151 1.00 33.07 C
ANISOU 1025 CB LEU A 123 4425 4229 3908 215 564 -308 C
ATOM 1026 CG LEU A 123 26.873 11.234 -58.934 1.00 33.77 C
ANISOU 1026 CG LEU A 123 4503 4264 4062 172 532 -358 C
ATOM 1027 CD1 LEU A 123 26.534 12.225 -57.827 1.00 33.14 C
ANISOU 1027 CD1 LEU A 123 4456 4146 3990 175 559 -329 C
ATOM 1028 CD2 LEU A 123 26.704 9.789 -58.460 1.00 31.85 C
ANISOU 1028 CD2 LEU A 123 4224 4040 3835 155 450 -389 C
ATOM 1029 N ASP A 124 25.436 12.565 -63.137 1.00 34.08 N
ANISOU 1029 N ASP A 124 4575 4460 3913 294 669 -225 N
ATOM 1030 CA ASP A 124 24.363 13.075 -63.983 1.00 34.39 C
ANISOU 1030 CA ASP A 124 4621 4571 3872 354 698 -153 C
ATOM 1031 C ASP A 124 24.411 12.394 -65.332 1.00 34.04 C
ANISOU 1031 C ASP A 124 4545 4605 3783 353 686 -169 C
ATOM 1032 O ASP A 124 23.375 12.095 -65.905 1.00 34.82 O
ANISOU 1032 O ASP A 124 4618 4799 3811 382 663 -137 O
ATOM 1033 CB ASP A 124 24.443 14.607 -64.169 1.00 35.75 C
ANISOU 1033 CB ASP A 124 4851 4700 4033 399 795 -91 C
ATOM 1034 CG ASP A 124 23.944 15.404 -62.939 1.00 38.17 C
ANISOU 1034 CG ASP A 124 5192 4950 4360 416 816 -56 C
ATOM 1035 OD1 ASP A 124 23.040 14.942 -62.185 1.00 37.15 O
ANISOU 1035 OD1 ASP A 124 5042 4851 4222 421 759 -46 O
ATOM 1036 OD2 ASP A 124 24.449 16.533 -62.755 1.00 38.72 O
ANISOU 1036 OD2 ASP A 124 5314 4944 4454 422 899 -39 O
ATOM 1037 N ASN A 125 25.620 12.149 -65.836 1.00 33.27 N
ANISOU 1037 N ASN A 125 4444 4473 3721 316 702 -224 N
ATOM 1038 CA ASN A 125 25.805 11.667 -67.216 1.00 33.53 C
ANISOU 1038 CA ASN A 125 4454 4574 3711 313 707 -242 C
ATOM 1039 C ASN A 125 26.056 10.146 -67.386 1.00 33.22 C
ANISOU 1039 C ASN A 125 4367 4562 3691 262 641 -319 C
ATOM 1040 O ASN A 125 25.856 9.589 -68.460 1.00 34.51 O
ANISOU 1040 O ASN A 125 4505 4801 3805 257 635 -334 O
ATOM 1041 CB ASN A 125 26.899 12.483 -67.901 1.00 32.60 C
ANISOU 1041 CB ASN A 125 4367 4410 3608 312 784 -244 C
ATOM 1042 CG ASN A 125 26.531 13.952 -68.008 1.00 33.43 C
ANISOU 1042 CG ASN A 125 4526 4495 3680 369 865 -161 C
ATOM 1043 OD1 ASN A 125 26.970 14.772 -67.206 1.00 34.99 O
ANISOU 1043 OD1 ASN A 125 4763 4606 3926 363 908 -156 O
ATOM 1044 ND2 ASN A 125 25.653 14.269 -68.933 1.00 32.15 N
ANISOU 1044 ND2 ASN A 125 4363 4418 3432 426 885 -93 N
ATOM 1045 N ILE A 126 26.475 9.486 -66.322 1.00 32.41 N
ANISOU 1045 N ILE A 126 4256 4400 3658 225 597 -367 N
ATOM 1046 CA ILE A 126 26.950 8.110 -66.428 1.00 31.47 C
ANISOU 1046 CA ILE A 126 4103 4281 3571 181 551 -441 C
ATOM 1047 C ILE A 126 26.230 7.207 -65.437 1.00 30.56 C
ANISOU 1047 C ILE A 126 3973 4165 3472 165 486 -453 C
ATOM 1048 O ILE A 126 25.653 6.198 -65.825 1.00 32.04 O
ANISOU 1048 O ILE A 126 4136 4405 3631 146 453 -478 O
ATOM 1049 CB ILE A 126 28.486 8.057 -66.240 1.00 30.72 C
ANISOU 1049 CB ILE A 126 4009 4109 3553 152 569 -496 C
ATOM 1050 CG1 ILE A 126 29.152 9.007 -67.251 1.00 29.62 C
ANISOU 1050 CG1 ILE A 126 3888 3970 3394 163 641 -483 C
ATOM 1051 CG2 ILE A 126 29.006 6.618 -66.315 1.00 29.44 C
ANISOU 1051 CG2 ILE A 126 3814 3940 3430 117 527 -567 C
ATOM 1052 CD1 ILE A 126 30.581 8.678 -67.609 1.00 30.05 C
ANISOU 1052 CD1 ILE A 126 3927 3986 3501 130 659 -549 C
ATOM 1053 N VAL A 127 26.188 7.613 -64.173 1.00 29.16 N
ANISOU 1053 N VAL A 127 3812 3932 3333 171 473 -433 N
ATOM 1054 CA VAL A 127 25.585 6.749 -63.137 1.00 28.81 C
ANISOU 1054 CA VAL A 127 3758 3879 3308 154 413 -444 C
ATOM 1055 C VAL A 127 24.086 6.632 -63.288 1.00 27.45 C
ANISOU 1055 C VAL A 127 3577 3786 3066 169 393 -406 C
ATOM 1056 O VAL A 127 23.564 5.542 -63.436 1.00 27.91 O
ANISOU 1056 O VAL A 127 3613 3882 3108 143 357 -437 O
ATOM 1057 CB VAL A 127 25.977 7.164 -61.708 1.00 28.02 C
ANISOU 1057 CB VAL A 127 3675 3707 3264 153 403 -438 C
ATOM 1058 CG1 VAL A 127 25.297 6.264 -60.694 1.00 26.72 C
ANISOU 1058 CG1 VAL A 127 3503 3538 3112 138 344 -443 C
ATOM 1059 CG2 VAL A 127 27.503 7.104 -61.550 1.00 27.84 C
ANISOU 1059 CG2 VAL A 127 3646 3622 3306 132 415 -486 C
ATOM 1060 N LYS A 128 23.392 7.752 -63.300 1.00 27.71 N
ANISOU 1060 N LYS A 128 3626 3847 3054 211 422 -340 N
ATOM 1061 CA LYS A 128 21.954 7.708 -63.539 1.00 28.55 C
ANISOU 1061 CA LYS A 128 3715 4047 3085 233 406 -300 C
ATOM 1062 C LYS A 128 21.570 7.117 -64.913 1.00 30.05 C
ANISOU 1062 C LYS A 128 3871 4339 3207 224 405 -318 C
ATOM 1063 O LYS A 128 20.730 6.224 -64.970 1.00 30.50 O
ANISOU 1063 O LYS A 128 3898 4460 3229 198 367 -340 O
ATOM 1064 CB LYS A 128 21.314 9.057 -63.268 1.00 28.38 C
ANISOU 1064 CB LYS A 128 3717 4033 3030 291 444 -221 C
ATOM 1065 CG LYS A 128 21.191 9.322 -61.780 1.00 28.51 C
ANISOU 1065 CG LYS A 128 3756 3980 3095 287 427 -210 C
ATOM 1066 CD LYS A 128 20.947 10.780 -61.492 1.00 28.98 C
ANISOU 1066 CD LYS A 128 3852 4014 3143 340 484 -142 C
ATOM 1067 CE LYS A 128 20.685 10.965 -60.005 1.00 28.52 C
ANISOU 1067 CE LYS A 128 3812 3899 3125 331 466 -137 C
ATOM 1068 NZ LYS A 128 20.003 12.258 -59.735 1.00 28.78 N
ANISOU 1068 NZ LYS A 128 3876 3927 3130 387 519 -64 N
ATOM 1069 N PRO A 129 22.224 7.569 -66.015 1.00 30.79 N
ANISOU 1069 N PRO A 129 3969 4447 3281 238 450 -316 N
ATOM 1070 CA PRO A 129 21.885 6.939 -67.305 1.00 31.81 C
ANISOU 1070 CA PRO A 129 4063 4680 3343 222 447 -340 C
ATOM 1071 C PRO A 129 22.179 5.431 -67.417 1.00 32.49 C
ANISOU 1071 C PRO A 129 4125 4760 3459 155 411 -429 C
ATOM 1072 O PRO A 129 21.382 4.711 -68.047 1.00 32.55 O
ANISOU 1072 O PRO A 129 4099 4864 3404 129 392 -452 O
ATOM 1073 CB PRO A 129 22.707 7.746 -68.311 1.00 32.19 C
ANISOU 1073 CB PRO A 129 4128 4724 3378 248 505 -322 C
ATOM 1074 CG PRO A 129 22.733 9.118 -67.703 1.00 31.88 C
ANISOU 1074 CG PRO A 129 4130 4629 3354 302 546 -251 C
ATOM 1075 CD PRO A 129 22.907 8.863 -66.219 1.00 31.02 C
ANISOU 1075 CD PRO A 129 4034 4428 3322 277 512 -273 C
ATOM 1076 N ILE A 130 23.286 4.941 -66.830 1.00 31.82 N
ANISOU 1076 N ILE A 130 4057 4568 3464 126 404 -478 N
ATOM 1077 CA ILE A 130 23.513 3.483 -66.830 1.00 30.73 C
ANISOU 1077 CA ILE A 130 3904 4413 3359 70 376 -555 C
ATOM 1078 C ILE A 130 22.367 2.698 -66.192 1.00 30.73 C
ANISOU 1078 C ILE A 130 3891 4445 3339 44 335 -563 C
ATOM 1079 O ILE A 130 21.884 1.715 -66.760 1.00 31.47 O
ANISOU 1079 O ILE A 130 3962 4595 3398 0 326 -611 O
ATOM 1080 CB ILE A 130 24.865 3.043 -66.247 1.00 30.01 C
ANISOU 1080 CB ILE A 130 3828 4207 3366 55 375 -599 C
ATOM 1081 CG1 ILE A 130 25.171 1.634 -66.737 1.00 29.93 C
ANISOU 1081 CG1 ILE A 130 3804 4191 3375 7 369 -676 C
ATOM 1082 CG2 ILE A 130 24.866 3.045 -64.721 1.00 28.63 C
ANISOU 1082 CG2 ILE A 130 3670 3957 3248 62 343 -582 C
ATOM 1083 CD1 ILE A 130 26.470 1.550 -67.485 1.00 31.64 C
ANISOU 1083 CD1 ILE A 130 4018 4373 3629 3 403 -717 C
ATOM 1084 N ILE A 131 21.918 3.161 -65.033 1.00 30.57 N
ANISOU 1084 N ILE A 131 3886 4392 3336 67 314 -518 N
ATOM 1085 CA ILE A 131 20.777 2.566 -64.355 1.00 32.12 C
ANISOU 1085 CA ILE A 131 4072 4620 3510 45 278 -518 C
ATOM 1086 C ILE A 131 19.541 2.604 -65.263 1.00 33.74 C
ANISOU 1086 C ILE A 131 4240 4966 3611 43 279 -505 C
ATOM 1087 O ILE A 131 18.878 1.575 -65.450 1.00 35.36 O
ANISOU 1087 O ILE A 131 4423 5223 3787 -8 262 -552 O
ATOM 1088 CB ILE A 131 20.542 3.230 -62.967 1.00 32.78 C
ANISOU 1088 CB ILE A 131 4178 4647 3627 75 261 -467 C
ATOM 1089 CG1 ILE A 131 21.781 3.020 -62.090 1.00 31.12 C
ANISOU 1089 CG1 ILE A 131 3995 4316 3513 69 255 -490 C
ATOM 1090 CG2 ILE A 131 19.330 2.640 -62.242 1.00 33.56 C
ANISOU 1090 CG2 ILE A 131 4268 4781 3702 52 225 -465 C
ATOM 1091 CD1 ILE A 131 21.767 3.848 -60.826 1.00 31.02 C
ANISOU 1091 CD1 ILE A 131 4004 4249 3530 97 247 -444 C
ATOM 1092 N ALA A 132 19.290 3.753 -65.897 1.00 33.31 N
ANISOU 1092 N ALA A 132 4178 4977 3499 96 305 -444 N
ATOM 1093 CA ALA A 132 18.119 3.923 -66.762 1.00 34.42 C
ANISOU 1093 CA ALA A 132 4277 5270 3530 108 306 -419 C
ATOM 1094 C ALA A 132 18.196 3.037 -67.992 1.00 36.00 C
ANISOU 1094 C ALA A 132 4444 5547 3685 57 312 -485 C
ATOM 1095 O ALA A 132 17.169 2.632 -68.540 1.00 35.35 O
ANISOU 1095 O ALA A 132 4317 5594 3518 32 300 -499 O
ATOM 1096 CB ALA A 132 17.968 5.378 -67.179 1.00 34.72 C
ANISOU 1096 CB ALA A 132 4321 5350 3520 189 340 -331 C
ATOM 1097 N PHE A 133 19.424 2.753 -68.429 1.00 36.02 N
ANISOU 1097 N PHE A 133 4467 5476 3742 38 334 -529 N
ATOM 1098 CA PHE A 133 19.648 1.971 -69.626 1.00 36.47 C
ANISOU 1098 CA PHE A 133 4498 5594 3762 -10 348 -596 C
ATOM 1099 C PHE A 133 19.247 0.532 -69.390 1.00 36.50 C
ANISOU 1099 C PHE A 133 4490 5597 3778 -89 327 -677 C
ATOM 1100 O PHE A 133 18.686 -0.108 -70.272 1.00 39.62 O
ANISOU 1100 O PHE A 133 4849 6100 4104 -138 332 -725 O
ATOM 1101 CB PHE A 133 21.121 2.046 -70.070 1.00 37.49 C
ANISOU 1101 CB PHE A 133 4654 5634 3955 -8 381 -623 C
ATOM 1102 CG PHE A 133 21.393 1.339 -71.378 1.00 39.48 C
ANISOU 1102 CG PHE A 133 4881 5950 4166 -54 403 -689 C
ATOM 1103 CD1 PHE A 133 20.962 1.890 -72.590 1.00 40.15 C
ANISOU 1103 CD1 PHE A 133 4935 6169 4148 -36 423 -662 C
ATOM 1104 CD2 PHE A 133 22.065 0.119 -71.401 1.00 39.56 C
ANISOU 1104 CD2 PHE A 133 4900 5891 4239 -115 407 -777 C
ATOM 1105 CE1 PHE A 133 21.209 1.241 -73.792 1.00 41.26 C
ANISOU 1105 CE1 PHE A 133 5052 6375 4247 -84 444 -728 C
ATOM 1106 CE2 PHE A 133 22.310 -0.537 -72.602 1.00 42.03 C
ANISOU 1106 CE2 PHE A 133 5193 6261 4515 -162 433 -844 C
ATOM 1107 CZ PHE A 133 21.882 0.023 -73.799 1.00 41.35 C
ANISOU 1107 CZ PHE A 133 5073 6311 4324 -151 450 -822 C
ATOM 1108 N TYR A 134 19.533 0.030 -68.191 1.00 36.32 N
ANISOU 1108 N TYR A 134 4499 5457 3842 -103 308 -691 N
ATOM 1109 CA TYR A 134 19.248 -1.367 -67.843 1.00 35.53 C
ANISOU 1109 CA TYR A 134 4401 5328 3767 -176 298 -765 C
ATOM 1110 C TYR A 134 17.970 -1.582 -67.021 1.00 36.77 C
ANISOU 1110 C TYR A 134 4547 5529 3893 -194 268 -750 C
ATOM 1111 O TYR A 134 17.431 -2.693 -67.001 1.00 36.91 O
ANISOU 1111 O TYR A 134 4557 5564 3900 -264 267 -813 O
ATOM 1112 CB TYR A 134 20.458 -1.994 -67.132 1.00 33.82 C
ANISOU 1112 CB TYR A 134 4228 4954 3666 -182 302 -798 C
ATOM 1113 CG TYR A 134 21.705 -2.079 -68.014 1.00 33.77 C
ANISOU 1113 CG TYR A 134 4228 4910 3693 -180 336 -834 C
ATOM 1114 CD1 TYR A 134 21.735 -2.916 -69.123 1.00 33.55 C
ANISOU 1114 CD1 TYR A 134 4183 4932 3633 -235 363 -907 C
ATOM 1115 CD2 TYR A 134 22.842 -1.318 -67.729 1.00 31.72 C
ANISOU 1115 CD2 TYR A 134 3987 4569 3493 -128 343 -800 C
ATOM 1116 CE1 TYR A 134 22.862 -3.013 -69.921 1.00 35.09 C
ANISOU 1116 CE1 TYR A 134 4382 5093 3857 -234 396 -943 C
ATOM 1117 CE2 TYR A 134 23.971 -1.391 -68.523 1.00 32.04 C
ANISOU 1117 CE2 TYR A 134 4029 4580 3563 -128 375 -835 C
ATOM 1118 CZ TYR A 134 23.984 -2.252 -69.618 1.00 34.43 C
ANISOU 1118 CZ TYR A 134 4316 4929 3835 -179 400 -905 C
ATOM 1119 OH TYR A 134 25.089 -2.332 -70.439 1.00 33.29 O
ANISOU 1119 OH TYR A 134 4172 4759 3717 -180 435 -942 O
ATOM 1120 N TYR A 135 17.487 -0.537 -66.338 1.00 37.35 N
ANISOU 1120 N TYR A 135 4620 5616 3952 -135 249 -670 N
ATOM 1121 CA TYR A 135 16.310 -0.689 -65.449 1.00 38.00 C
ANISOU 1121 CA TYR A 135 4692 5732 4011 -148 220 -653 C
ATOM 1122 C TYR A 135 15.210 0.315 -65.660 1.00 39.20 C
ANISOU 1122 C TYR A 135 4805 6015 4071 -100 211 -585 C
ATOM 1123 O TYR A 135 15.460 1.465 -65.993 1.00 39.24 O
ANISOU 1123 O TYR A 135 4812 6038 4057 -30 226 -520 O
ATOM 1124 CB TYR A 135 16.720 -0.656 -63.982 1.00 35.43 C
ANISOU 1124 CB TYR A 135 4413 5271 3776 -129 202 -628 C
ATOM 1125 CG TYR A 135 17.623 -1.781 -63.612 1.00 36.99 C
ANISOU 1125 CG TYR A 135 4646 5348 4059 -171 207 -689 C
ATOM 1126 CD1 TYR A 135 17.110 -2.972 -63.132 1.00 37.30 C
ANISOU 1126 CD1 TYR A 135 4695 5365 4112 -234 201 -739 C
ATOM 1127 CD2 TYR A 135 19.010 -1.661 -63.750 1.00 37.09 C
ANISOU 1127 CD2 TYR A 135 4682 5268 4140 -146 223 -696 C
ATOM 1128 CE1 TYR A 135 17.944 -4.015 -62.799 1.00 39.13 C
ANISOU 1128 CE1 TYR A 135 4964 5481 4423 -263 214 -788 C
ATOM 1129 CE2 TYR A 135 19.845 -2.699 -63.417 1.00 37.23 C
ANISOU 1129 CE2 TYR A 135 4728 5180 4234 -174 230 -746 C
ATOM 1130 CZ TYR A 135 19.304 -3.871 -62.944 1.00 38.77 C
ANISOU 1130 CZ TYR A 135 4937 5350 4441 -228 227 -789 C
ATOM 1131 OH TYR A 135 20.131 -4.907 -62.605 1.00 42.53 O
ANISOU 1131 OH TYR A 135 5447 5716 4995 -245 241 -831 O
ATOM 1132 N LYS A 136 13.982 -0.139 -65.427 1.00 42.27 N
ANISOU 1132 N LYS A 136 5162 6495 4405 -138 192 -599 N
ATOM 1133 CA LYS A 136 12.832 0.738 -65.326 1.00 42.77 C
ANISOU 1133 CA LYS A 136 5186 6675 4389 -88 179 -531 C
ATOM 1134 C LYS A 136 12.523 0.955 -63.847 1.00 40.67 C
ANISOU 1134 C LYS A 136 4950 6325 4177 -70 158 -494 C
ATOM 1135 O LYS A 136 12.262 -0.004 -63.115 1.00 42.01 O
ANISOU 1135 O LYS A 136 5133 6449 4380 -133 143 -542 O
ATOM 1136 CB LYS A 136 11.635 0.121 -66.062 1.00 47.73 C
ANISOU 1136 CB LYS A 136 5746 7478 4910 -145 172 -575 C
ATOM 1137 CG LYS A 136 10.459 1.063 -66.321 1.00 53.26 C
ANISOU 1137 CG LYS A 136 6389 8342 5506 -83 163 -503 C
ATOM 1138 CD LYS A 136 10.850 2.263 -67.176 1.00 59.59 C
ANISOU 1138 CD LYS A 136 7185 9188 6267 9 185 -427 C
ATOM 1139 CE LYS A 136 9.716 2.697 -68.101 1.00 62.81 C
ANISOU 1139 CE LYS A 136 7512 9814 6536 43 182 -391 C
ATOM 1140 NZ LYS A 136 8.414 2.752 -67.382 1.00 65.90 N
ANISOU 1140 NZ LYS A 136 7863 10293 6882 48 157 -367 N
ATOM 1141 N PRO A 137 12.589 2.212 -63.388 1.00 39.33 N
ANISOU 1141 N PRO A 137 4798 6128 4017 13 163 -410 N
ATOM 1142 CA PRO A 137 12.163 2.509 -62.026 1.00 39.85 C
ANISOU 1142 CA PRO A 137 4886 6134 4120 31 145 -373 C
ATOM 1143 C PRO A 137 10.640 2.533 -61.913 1.00 43.26 C
ANISOU 1143 C PRO A 137 5265 6703 4467 29 128 -355 C
ATOM 1144 O PRO A 137 9.959 3.234 -62.664 1.00 46.28 O
ANISOU 1144 O PRO A 137 5601 7217 4762 79 137 -309 O
ATOM 1145 CB PRO A 137 12.749 3.895 -61.758 1.00 38.45 C
ANISOU 1145 CB PRO A 137 4742 5891 3973 117 168 -295 C
ATOM 1146 CG PRO A 137 12.933 4.508 -63.099 1.00 38.83 C
ANISOU 1146 CG PRO A 137 4769 6022 3962 159 197 -269 C
ATOM 1147 CD PRO A 137 13.125 3.394 -64.087 1.00 38.51 C
ANISOU 1147 CD PRO A 137 4701 6034 3896 90 192 -348 C
ATOM 1148 N ILE A 138 10.117 1.757 -60.982 1.00 45.38 N
ANISOU 1148 N ILE A 138 5538 6944 4758 -26 106 -389 N
ATOM 1149 CA ILE A 138 8.686 1.620 -60.811 1.00 46.98 C
ANISOU 1149 CA ILE A 138 5688 7275 4884 -43 90 -386 C
ATOM 1150 C ILE A 138 8.308 2.055 -59.391 1.00 46.77 C
ANISOU 1150 C ILE A 138 5690 7180 4899 -16 77 -341 C
ATOM 1151 O ILE A 138 8.831 1.511 -58.411 1.00 46.07 O
ANISOU 1151 O ILE A 138 5651 6960 4891 -53 67 -367 O
ATOM 1152 CB ILE A 138 8.239 0.159 -61.117 1.00 48.45 C
ANISOU 1152 CB ILE A 138 5849 7513 5045 -154 83 -484 C
ATOM 1153 CG1 ILE A 138 7.541 0.081 -62.472 1.00 51.73 C
ANISOU 1153 CG1 ILE A 138 6188 8118 5347 -170 89 -507 C
ATOM 1154 CG2 ILE A 138 7.278 -0.368 -60.065 1.00 51.25 C
ANISOU 1154 CG2 ILE A 138 6199 7874 5399 -202 66 -501 C
ATOM 1155 CD1 ILE A 138 8.464 0.091 -63.658 1.00 50.56 C
ANISOU 1155 CD1 ILE A 138 6043 7971 5194 -164 109 -526 C
ATOM 1156 N LYS A 139 7.444 3.065 -59.285 1.00 45.57 N
ANISOU 1156 N LYS A 139 5507 7116 4691 52 79 -271 N
ATOM 1157 CA LYS A 139 6.875 3.460 -57.990 1.00 46.33 C
ANISOU 1157 CA LYS A 139 5619 7171 4811 74 69 -232 C
ATOM 1158 C LYS A 139 5.764 2.496 -57.619 1.00 45.35 C
ANISOU 1158 C LYS A 139 5456 7127 4647 -2 47 -283 C
ATOM 1159 O LYS A 139 4.735 2.466 -58.280 1.00 45.50 O
ANISOU 1159 O LYS A 139 5404 7311 4571 -5 43 -286 O
ATOM 1160 CB LYS A 139 6.343 4.893 -58.030 1.00 47.82 C
ANISOU 1160 CB LYS A 139 5791 7421 4955 180 89 -138 C
ATOM 1161 CG LYS A 139 7.401 5.947 -58.324 1.00 49.80 C
ANISOU 1161 CG LYS A 139 6089 7585 5248 254 123 -86 C
ATOM 1162 CD LYS A 139 6.832 7.350 -58.166 1.00 55.61 C
ANISOU 1162 CD LYS A 139 6821 8356 5949 359 154 8 C
ATOM 1163 CE LYS A 139 7.699 8.397 -58.861 1.00 59.45 C
ANISOU 1163 CE LYS A 139 7342 8796 6447 433 201 61 C
ATOM 1164 NZ LYS A 139 9.022 8.582 -58.197 1.00 59.42 N
ANISOU 1164 NZ LYS A 139 7414 8614 6549 416 215 44 N
ATOM 1165 N THR A 140 5.993 1.685 -56.585 1.00 44.72 N
ANISOU 1165 N THR A 140 5421 6935 4635 -65 34 -324 N
ATOM 1166 CA THR A 140 5.014 0.688 -56.147 1.00 47.72 C
ANISOU 1166 CA THR A 140 5775 7369 4986 -148 20 -378 C
ATOM 1167 C THR A 140 3.787 1.374 -55.558 1.00 51.42 C
ANISOU 1167 C THR A 140 6204 7931 5403 -109 13 -328 C
ATOM 1168 O THR A 140 2.704 0.798 -55.531 1.00 52.97 O
ANISOU 1168 O THR A 140 6350 8235 5539 -165 5 -365 O
ATOM 1169 CB THR A 140 5.600 -0.304 -55.108 1.00 47.78 C
ANISOU 1169 CB THR A 140 5850 7220 5083 -215 14 -423 C
ATOM 1170 OG1 THR A 140 5.982 0.401 -53.911 1.00 46.67 O
ANISOU 1170 OG1 THR A 140 5758 6969 5005 -163 7 -366 O
ATOM 1171 CG2 THR A 140 6.825 -1.038 -55.680 1.00 44.78 C
ANISOU 1171 CG2 THR A 140 5509 6747 4758 -248 26 -472 C
ATOM 1172 N LEU A 141 3.978 2.619 -55.114 1.00 53.59 N
ANISOU 1172 N LEU A 141 6499 8163 5698 -15 21 -247 N
ATOM 1173 CA LEU A 141 2.930 3.445 -54.496 1.00 56.23 C
ANISOU 1173 CA LEU A 141 6805 8567 5993 40 21 -189 C
ATOM 1174 C LEU A 141 2.691 3.046 -53.041 1.00 57.38 C
ANISOU 1174 C LEU A 141 6989 8623 6191 -4 8 -203 C
ATOM 1175 O LEU A 141 1.990 3.741 -52.296 1.00 59.82 O
ANISOU 1175 O LEU A 141 7289 8953 6487 38 11 -155 O
ATOM 1176 CB LEU A 141 1.617 3.456 -55.317 1.00 58.26 C
ANISOU 1176 CB LEU A 141 6965 9036 6132 46 18 -188 C
ATOM 1177 CG LEU A 141 1.635 4.023 -56.756 1.00 58.76 C
ANISOU 1177 CG LEU A 141 6979 9224 6123 108 31 -156 C
ATOM 1178 CD1 LEU A 141 0.243 3.974 -57.367 1.00 62.57 C
ANISOU 1178 CD1 LEU A 141 7358 9930 6484 111 22 -157 C
ATOM 1179 CD2 LEU A 141 2.185 5.443 -56.822 1.00 57.24 C
ANISOU 1179 CD2 LEU A 141 6822 8973 5954 229 60 -62 C
ATOM 1180 N ASN A 142 3.295 1.937 -52.636 1.00 52.04 N
ANISOU 1180 N ASN A 142 6356 7842 5572 -87 -1 -265 N
ATOM 1181 CA ASN A 142 3.468 1.664 -51.229 1.00 52.53 C
ANISOU 1181 CA ASN A 142 6474 7784 5700 -115 -11 -266 C
ATOM 1182 C ASN A 142 4.497 2.617 -50.610 1.00 50.50 C
ANISOU 1182 C ASN A 142 6275 7399 5514 -47 -3 -213 C
ATOM 1183 O ASN A 142 5.714 2.356 -50.613 1.00 48.72 O
ANISOU 1183 O ASN A 142 6096 7061 5352 -56 -4 -229 O
ATOM 1184 CB ASN A 142 3.854 0.210 -50.995 1.00 54.87 C
ANISOU 1184 CB ASN A 142 6805 8004 6037 -213 -18 -340 C
ATOM 1185 CG ASN A 142 3.424 -0.280 -49.632 1.00 59.68 C
ANISOU 1185 CG ASN A 142 7447 8553 6676 -258 -27 -348 C
ATOM 1186 OD1 ASN A 142 3.464 0.471 -48.649 1.00 59.38 O
ANISOU 1186 OD1 ASN A 142 7433 8461 6665 -212 -32 -298 O
ATOM 1187 ND2 ASN A 142 2.999 -1.540 -49.561 1.00 61.20 N
ANISOU 1187 ND2 ASN A 142 7641 8753 6859 -351 -24 -412 N
ATOM 1188 N GLY A 143 3.995 3.724 -50.074 1.00 47.47 N
ANISOU 1188 N GLY A 143 5885 7034 5115 17 6 -152 N
ATOM 1189 CA GLY A 143 4.843 4.827 -49.670 1.00 45.66 C
ANISOU 1189 CA GLY A 143 5703 6707 4938 84 26 -102 C
ATOM 1190 C GLY A 143 5.684 5.327 -50.837 1.00 43.66 C
ANISOU 1190 C GLY A 143 5450 6452 4684 130 46 -88 C
ATOM 1191 O GLY A 143 5.210 5.437 -51.949 1.00 45.56 O
ANISOU 1191 O GLY A 143 5642 6807 4861 153 54 -81 O
ATOM 1192 N HIS A 144 6.943 5.614 -50.571 1.00 43.09 N
ANISOU 1192 N HIS A 144 5431 6258 4683 140 55 -86 N
ATOM 1193 CA HIS A 144 7.831 6.183 -51.569 1.00 43.21 C
ANISOU 1193 CA HIS A 144 5455 6258 4706 183 80 -72 C
ATOM 1194 C HIS A 144 8.739 5.132 -52.165 1.00 43.77 C
ANISOU 1194 C HIS A 144 5533 6291 4806 128 63 -132 C
ATOM 1195 O HIS A 144 9.703 5.449 -52.861 1.00 47.10 O
ANISOU 1195 O HIS A 144 5969 6676 5250 150 81 -131 O
ATOM 1196 CB HIS A 144 8.600 7.350 -50.965 1.00 40.19 C
ANISOU 1196 CB HIS A 144 5121 5774 4373 232 112 -31 C
ATOM 1197 CG HIS A 144 7.706 8.402 -50.350 1.00 39.29 C
ANISOU 1197 CG HIS A 144 5006 5686 4234 288 139 25 C
ATOM 1198 ND1 HIS A 144 7.426 8.440 -49.027 1.00 40.69 N
ANISOU 1198 ND1 HIS A 144 5205 5814 4438 268 130 25 N
ATOM 1199 CD2 HIS A 144 6.976 9.439 -50.932 1.00 40.34 C
ANISOU 1199 CD2 HIS A 144 5116 5897 4311 368 178 87 C
ATOM 1200 CE1 HIS A 144 6.586 9.466 -48.775 1.00 39.80 C
ANISOU 1200 CE1 HIS A 144 5087 5740 4295 329 164 80 C
ATOM 1201 NE2 HIS A 144 6.311 10.076 -49.939 1.00 38.48 N
ANISOU 1201 NE2 HIS A 144 4892 5649 4077 395 195 120 N
ATOM 1202 N GLU A 145 8.393 3.865 -51.940 1.00 43.36 N
ANISOU 1202 N GLU A 145 5471 6249 4752 55 34 -184 N
ATOM 1203 CA GLU A 145 9.170 2.748 -52.450 1.00 43.22 C
ANISOU 1203 CA GLU A 145 5464 6192 4765 0 25 -245 C
ATOM 1204 C GLU A 145 9.348 2.814 -53.962 1.00 43.47 C
ANISOU 1204 C GLU A 145 5462 6299 4754 14 41 -256 C
ATOM 1205 O GLU A 145 8.384 3.015 -54.696 1.00 43.20 O
ANISOU 1205 O GLU A 145 5376 6394 4641 26 46 -245 O
ATOM 1206 CB GLU A 145 8.533 1.412 -52.059 1.00 43.93 C
ANISOU 1206 CB GLU A 145 5548 6294 4847 -79 5 -297 C
ATOM 1207 CG GLU A 145 9.228 0.200 -52.679 1.00 45.90 C
ANISOU 1207 CG GLU A 145 5810 6504 5123 -137 6 -362 C
ATOM 1208 CD GLU A 145 8.542 -1.124 -52.362 1.00 48.53 C
ANISOU 1208 CD GLU A 145 6145 6847 5447 -221 1 -418 C
ATOM 1209 OE1 GLU A 145 9.247 -2.073 -51.976 1.00 52.04 O
ANISOU 1209 OE1 GLU A 145 6633 7189 5951 -258 2 -452 O
ATOM 1210 OE2 GLU A 145 7.303 -1.230 -52.509 1.00 49.05 O
ANISOU 1210 OE2 GLU A 145 6166 7023 5445 -249 0 -427 O
ATOM 1211 N ILE A 146 10.594 2.654 -54.415 1.00 41.80 N
ANISOU 1211 N ILE A 146 5277 6013 4591 13 49 -277 N
ATOM 1212 CA ILE A 146 10.873 2.435 -55.822 1.00 39.98 C
ANISOU 1212 CA ILE A 146 5020 5843 4327 8 63 -303 C
ATOM 1213 C ILE A 146 11.463 1.041 -56.020 1.00 40.90 C
ANISOU 1213 C ILE A 146 5150 5906 4481 -63 56 -378 C
ATOM 1214 O ILE A 146 12.311 0.599 -55.246 1.00 39.60 O
ANISOU 1214 O ILE A 146 5030 5623 4391 -77 48 -393 O
ATOM 1215 CB ILE A 146 11.806 3.518 -56.407 1.00 39.52 C
ANISOU 1215 CB ILE A 146 4977 5754 4285 73 91 -265 C
ATOM 1216 CG1 ILE A 146 11.071 4.863 -56.469 1.00 35.97 C
ANISOU 1216 CG1 ILE A 146 4510 5371 3783 148 112 -190 C
ATOM 1217 CG2 ILE A 146 12.293 3.122 -57.810 1.00 39.24 C
ANISOU 1217 CG2 ILE A 146 4920 5762 4225 58 104 -301 C
ATOM 1218 CD1 ILE A 146 11.976 6.055 -56.612 1.00 33.28 C
ANISOU 1218 CD1 ILE A 146 4204 4965 3475 210 149 -145 C
ATOM 1219 N LYS A 147 10.960 0.339 -57.030 1.00 40.93 N
ANISOU 1219 N LYS A 147 5117 6004 4429 -107 61 -424 N
ATOM 1220 CA LYS A 147 11.513 -0.940 -57.435 1.00 42.01 C
ANISOU 1220 CA LYS A 147 5268 6096 4596 -174 68 -499 C
ATOM 1221 C LYS A 147 12.156 -0.798 -58.820 1.00 40.80 C
ANISOU 1221 C LYS A 147 5097 5982 4422 -163 89 -517 C
ATOM 1222 O LYS A 147 11.644 -0.073 -59.695 1.00 37.63 O
ANISOU 1222 O LYS A 147 4651 5699 3946 -130 96 -490 O
ATOM 1223 CB LYS A 147 10.425 -2.009 -57.442 1.00 47.35 C
ANISOU 1223 CB LYS A 147 5921 6840 5227 -255 66 -554 C
ATOM 1224 CG LYS A 147 10.827 -3.313 -56.767 1.00 52.23 C
ANISOU 1224 CG LYS A 147 6588 7343 5913 -319 71 -607 C
ATOM 1225 CD LYS A 147 9.616 -4.000 -56.136 1.00 58.71 C
ANISOU 1225 CD LYS A 147 7401 8205 6701 -383 67 -633 C
ATOM 1226 CE LYS A 147 10.033 -4.976 -55.029 1.00 60.95 C
ANISOU 1226 CE LYS A 147 7749 8346 7062 -419 71 -652 C
ATOM 1227 NZ LYS A 147 9.153 -4.865 -53.826 1.00 58.67 N
ANISOU 1227 NZ LYS A 147 7466 8058 6764 -426 53 -622 N
ATOM 1228 N PHE A 148 13.312 -1.430 -58.992 1.00 38.06 N
ANISOU 1228 N PHE A 148 4783 5537 4141 -182 100 -557 N
ATOM 1229 CA PHE A 148 14.020 -1.364 -60.260 1.00 36.44 C
ANISOU 1229 CA PHE A 148 4565 5357 3923 -175 122 -581 C
ATOM 1230 C PHE A 148 13.875 -2.677 -60.976 1.00 37.51 C
ANISOU 1230 C PHE A 148 4689 5519 4041 -257 138 -665 C
ATOM 1231 O PHE A 148 14.400 -3.698 -60.522 1.00 36.70 O
ANISOU 1231 O PHE A 148 4626 5313 4004 -297 146 -710 O
ATOM 1232 CB PHE A 148 15.498 -1.022 -60.056 1.00 35.51 C
ANISOU 1232 CB PHE A 148 4486 5118 3888 -135 130 -567 C
ATOM 1233 CG PHE A 148 15.748 0.424 -59.688 1.00 33.90 C
ANISOU 1233 CG PHE A 148 4288 4900 3689 -59 130 -492 C
ATOM 1234 CD1 PHE A 148 15.568 1.442 -60.628 1.00 32.87 C
ANISOU 1234 CD1 PHE A 148 4133 4856 3500 -14 149 -453 C
ATOM 1235 CD2 PHE A 148 16.178 0.763 -58.408 1.00 32.20 C
ANISOU 1235 CD2 PHE A 148 4108 4587 3537 -36 116 -461 C
ATOM 1236 CE1 PHE A 148 15.795 2.765 -60.289 1.00 32.82 C
ANISOU 1236 CE1 PHE A 148 4141 4825 3501 52 161 -385 C
ATOM 1237 CE2 PHE A 148 16.410 2.087 -58.063 1.00 31.30 C
ANISOU 1237 CE2 PHE A 148 4005 4458 3429 23 125 -401 C
ATOM 1238 CZ PHE A 148 16.230 3.091 -59.009 1.00 31.87 C
ANISOU 1238 CZ PHE A 148 4057 4602 3447 67 151 -364 C
ATOM 1239 N ILE A 149 13.133 -2.644 -62.086 1.00 38.12 N
ANISOU 1239 N ILE A 149 4714 5740 4027 -279 148 -687 N
ATOM 1240 CA ILE A 149 12.845 -3.831 -62.881 1.00 41.45 C
ANISOU 1240 CA ILE A 149 5118 6213 4416 -368 169 -776 C
ATOM 1241 C ILE A 149 13.766 -3.835 -64.097 1.00 42.69 C
ANISOU 1241 C ILE A 149 5271 6377 4572 -364 195 -805 C
ATOM 1242 O ILE A 149 13.975 -2.792 -64.718 1.00 41.43 O
ANISOU 1242 O ILE A 149 5088 6274 4376 -301 194 -755 O
ATOM 1243 CB ILE A 149 11.364 -3.843 -63.350 1.00 42.07 C
ANISOU 1243 CB ILE A 149 5131 6472 4382 -407 162 -790 C
ATOM 1244 CG1 ILE A 149 10.422 -3.588 -62.168 1.00 42.58 C
ANISOU 1244 CG1 ILE A 149 5194 6544 4441 -396 136 -748 C
ATOM 1245 CG2 ILE A 149 11.013 -5.155 -64.041 1.00 42.64 C
ANISOU 1245 CG2 ILE A 149 5187 6594 4421 -517 190 -896 C
ATOM 1246 CD1 ILE A 149 10.585 -4.563 -61.019 1.00 42.24 C
ANISOU 1246 CD1 ILE A 149 5208 6363 4478 -446 138 -781 C
ATOM 1247 N ARG A 150 14.340 -4.996 -64.415 1.00 46.33 N
ANISOU 1247 N ARG A 150 5757 6771 5075 -427 223 -885 N
ATOM 1248 CA ARG A 150 15.169 -5.128 -65.617 1.00 50.92 C
ANISOU 1248 CA ARG A 150 6332 7363 5652 -434 252 -925 C
ATOM 1249 C ARG A 150 14.358 -4.699 -66.827 1.00 52.98 C
ANISOU 1249 C ARG A 150 6525 7811 5792 -447 254 -930 C
ATOM 1250 O ARG A 150 13.195 -5.086 -66.975 1.00 55.16 O
ANISOU 1250 O ARG A 150 6761 8204 5993 -503 250 -963 O
ATOM 1251 CB ARG A 150 15.685 -6.554 -65.783 1.00 54.88 C
ANISOU 1251 CB ARG A 150 6868 7776 6207 -509 289 -1017 C
ATOM 1252 CG ARG A 150 16.696 -6.962 -64.724 1.00 61.27 C
ANISOU 1252 CG ARG A 150 7742 8402 7136 -480 291 -1004 C
ATOM 1253 CD ARG A 150 17.620 -8.070 -65.206 1.00 70.15 C
ANISOU 1253 CD ARG A 150 8900 9434 8319 -520 337 -1080 C
ATOM 1254 NE ARG A 150 18.411 -7.659 -66.373 1.00 78.59 N
ANISOU 1254 NE ARG A 150 9948 10539 9373 -499 355 -1093 N
ATOM 1255 CZ ARG A 150 19.366 -8.397 -66.940 1.00 82.12 C
ANISOU 1255 CZ ARG A 150 10417 10914 9869 -519 396 -1151 C
ATOM 1256 NH1 ARG A 150 19.675 -9.592 -66.451 1.00 84.48 N
ANISOU 1256 NH1 ARG A 150 10763 11095 10237 -553 427 -1199 N
ATOM 1257 NH2 ARG A 150 20.019 -7.935 -67.999 1.00 86.38 N
ANISOU 1257 NH2 ARG A 150 10933 11496 10388 -500 410 -1160 N
ATOM 1258 N LYS A 151 14.957 -3.858 -67.662 1.00 53.15 N
ANISOU 1258 N LYS A 151 6532 7869 5792 -391 260 -896 N
ATOM 1259 CA LYS A 151 14.240 -3.196 -68.744 1.00 56.31 C
ANISOU 1259 CA LYS A 151 6868 8451 6073 -376 259 -874 C
ATOM 1260 C LYS A 151 13.606 -4.182 -69.734 1.00 58.85 C
ANISOU 1260 C LYS A 151 7145 8900 6314 -474 279 -969 C
ATOM 1261 O LYS A 151 12.485 -3.968 -70.180 1.00 61.04 O
ANISOU 1261 O LYS A 151 7358 9350 6482 -488 266 -964 O
ATOM 1262 CB LYS A 151 15.167 -2.219 -69.467 1.00 57.84 C
ANISOU 1262 CB LYS A 151 7069 8638 6269 -303 273 -824 C
ATOM 1263 CG LYS A 151 14.462 -1.090 -70.195 1.00 59.60 C
ANISOU 1263 CG LYS A 151 7240 9022 6382 -240 267 -752 C
ATOM 1264 CD LYS A 151 15.301 0.177 -70.124 1.00 60.81 C
ANISOU 1264 CD LYS A 151 7427 9103 6574 -142 277 -665 C
ATOM 1265 CE LYS A 151 14.960 1.152 -71.240 1.00 62.85 C
ANISOU 1265 CE LYS A 151 7645 9508 6726 -83 291 -605 C
ATOM 1266 NZ LYS A 151 15.468 2.513 -70.913 1.00 61.87 N
ANISOU 1266 NZ LYS A 151 7558 9313 6635 16 306 -506 N
ATOM 1267 N GLU A 152 14.312 -5.265 -70.055 1.00 60.44 N
ANISOU 1267 N GLU A 152 7377 9019 6567 -544 312 -1058 N
ATOM 1268 CA GLU A 152 13.782 -6.271 -70.993 1.00 64.85 C
ANISOU 1268 CA GLU A 152 7898 9686 7055 -651 342 -1163 C
ATOM 1269 C GLU A 152 12.565 -7.000 -70.422 1.00 63.60 C
ANISOU 1269 C GLU A 152 7720 9582 6861 -730 336 -1208 C
ATOM 1270 O GLU A 152 11.631 -7.326 -71.156 1.00 62.82 O
ANISOU 1270 O GLU A 152 7560 9652 6656 -800 343 -1263 O
ATOM 1271 CB GLU A 152 14.866 -7.265 -71.479 1.00 66.77 C
ANISOU 1271 CB GLU A 152 8186 9816 7368 -706 390 -1250 C
ATOM 1272 CG GLU A 152 15.841 -7.764 -70.410 1.00 75.06 C
ANISOU 1272 CG GLU A 152 9315 10645 8560 -686 400 -1247 C
ATOM 1273 CD GLU A 152 16.965 -6.773 -70.109 1.00 79.46 C
ANISOU 1273 CD GLU A 152 9900 11105 9186 -579 382 -1163 C
ATOM 1274 OE1 GLU A 152 17.473 -6.127 -71.054 1.00 85.81 O
ANISOU 1274 OE1 GLU A 152 10683 11965 9956 -544 390 -1147 O
ATOM 1275 OE2 GLU A 152 17.345 -6.638 -68.924 1.00 80.18 O
ANISOU 1275 OE2 GLU A 152 10034 11069 9361 -533 363 -1116 O
ATOM 1276 N GLU A 153 12.572 -7.232 -69.110 1.00 62.16 N
ANISOU 1276 N GLU A 153 7589 9266 6763 -719 324 -1184 N
ATOM 1277 CA GLU A 153 11.440 -7.866 -68.433 1.00 63.76 C
ANISOU 1277 CA GLU A 153 7780 9505 6939 -789 321 -1219 C
ATOM 1278 C GLU A 153 10.226 -6.956 -68.445 1.00 61.16 C
ANISOU 1278 C GLU A 153 7377 9356 6503 -754 280 -1159 C
ATOM 1279 O GLU A 153 9.098 -7.407 -68.673 1.00 61.32 O
ANISOU 1279 O GLU A 153 7343 9517 6438 -831 283 -1213 O
ATOM 1280 CB GLU A 153 11.799 -8.233 -66.996 1.00 66.80 C
ANISOU 1280 CB GLU A 153 8239 9701 7438 -773 316 -1195 C
ATOM 1281 CG GLU A 153 12.672 -9.468 -66.876 1.00 74.20 C
ANISOU 1281 CG GLU A 153 9246 10475 8469 -829 366 -1270 C
ATOM 1282 CD GLU A 153 13.143 -9.718 -65.456 1.00 79.71 C
ANISOU 1282 CD GLU A 153 10016 10991 9278 -792 358 -1229 C
ATOM 1283 OE1 GLU A 153 12.365 -9.446 -64.509 1.00 84.26 O
ANISOU 1283 OE1 GLU A 153 10588 11581 9844 -781 327 -1185 O
ATOM 1284 OE2 GLU A 153 14.291 -10.194 -65.288 1.00 80.14 O
ANISOU 1284 OE2 GLU A 153 10127 10895 9426 -772 382 -1239 O
ATOM 1285 N TYR A 154 10.464 -5.670 -68.211 1.00 57.23 N
ANISOU 1285 N TYR A 154 6876 8857 6010 -638 247 -1050 N
ATOM 1286 CA TYR A 154 9.392 -4.706 -68.183 1.00 55.30 C
ANISOU 1286 CA TYR A 154 6568 8771 5673 -583 214 -979 C
ATOM 1287 C TYR A 154 8.778 -4.536 -69.562 1.00 56.30 C
ANISOU 1287 C TYR A 154 6609 9117 5664 -603 218 -1002 C
ATOM 1288 O TYR A 154 7.554 -4.515 -69.698 1.00 57.42 O
ANISOU 1288 O TYR A 154 6679 9431 5705 -630 203 -1009 O
ATOM 1289 CB TYR A 154 9.859 -3.354 -67.644 1.00 53.29 C
ANISOU 1289 CB TYR A 154 6339 8448 5459 -453 191 -858 C
ATOM 1290 CG TYR A 154 8.831 -2.273 -67.855 1.00 54.76 C
ANISOU 1290 CG TYR A 154 6458 8805 5541 -382 167 -778 C
ATOM 1291 CD1 TYR A 154 7.700 -2.196 -67.041 1.00 56.02 C
ANISOU 1291 CD1 TYR A 154 6589 9024 5670 -385 144 -756 C
ATOM 1292 CD2 TYR A 154 8.956 -1.360 -68.899 1.00 55.51 C
ANISOU 1292 CD2 TYR A 154 6516 9008 5564 -311 172 -724 C
ATOM 1293 CE1 TYR A 154 6.730 -1.230 -67.249 1.00 58.39 C
ANISOU 1293 CE1 TYR A 154 6823 9488 5872 -314 126 -681 C
ATOM 1294 CE2 TYR A 154 7.996 -0.384 -69.113 1.00 59.35 C
ANISOU 1294 CE2 TYR A 154 6942 9655 5953 -236 156 -643 C
ATOM 1295 CZ TYR A 154 6.881 -0.324 -68.284 1.00 61.58 C
ANISOU 1295 CZ TYR A 154 7194 9996 6207 -235 133 -622 C
ATOM 1296 OH TYR A 154 5.917 0.645 -68.487 1.00 63.54 O
ANISOU 1296 OH TYR A 154 7378 10405 6357 -151 119 -539 O
ATOM 1297 N ILE A 155 9.624 -4.397 -70.579 1.00 56.31 N
ANISOU 1297 N ILE A 155 6613 9120 5659 -588 238 -1013 N
ATOM 1298 CA ILE A 155 9.142 -4.225 -71.945 1.00 58.16 C
ANISOU 1298 CA ILE A 155 6769 9568 5762 -604 243 -1033 C
ATOM 1299 C ILE A 155 8.320 -5.429 -72.409 1.00 60.63 C
ANISOU 1299 C ILE A 155 7031 10002 6002 -743 261 -1157 C
ATOM 1300 O ILE A 155 7.269 -5.270 -73.035 1.00 62.61 O
ANISOU 1300 O ILE A 155 7191 10475 6120 -763 248 -1165 O
ATOM 1301 CB ILE A 155 10.290 -3.917 -72.924 1.00 57.38 C
ANISOU 1301 CB ILE A 155 6691 9433 5677 -569 267 -1027 C
ATOM 1302 CG1 ILE A 155 10.806 -2.496 -72.669 1.00 54.90 C
ANISOU 1302 CG1 ILE A 155 6403 9062 5392 -429 252 -897 C
ATOM 1303 CG2 ILE A 155 9.829 -4.091 -74.375 1.00 55.81 C
ANISOU 1303 CG2 ILE A 155 6413 9450 5342 -617 279 -1078 C
ATOM 1304 CD1 ILE A 155 12.045 -2.137 -73.454 1.00 55.16 C
ANISOU 1304 CD1 ILE A 155 6469 9030 5458 -391 279 -886 C
ATOM 1305 N SER A 156 8.793 -6.626 -72.070 1.00 61.15 N
ANISOU 1305 N SER A 156 7155 9924 6153 -839 295 -1252 N
ATOM 1306 CA SER A 156 8.063 -7.856 -72.340 1.00 63.22 C
ANISOU 1306 CA SER A 156 7388 10266 6366 -984 325 -1379 C
ATOM 1307 C SER A 156 6.680 -7.810 -71.681 1.00 66.46 C
ANISOU 1307 C SER A 156 7744 10794 6711 -1008 298 -1369 C
ATOM 1308 O SER A 156 5.655 -8.014 -72.344 1.00 70.99 O
ANISOU 1308 O SER A 156 8229 11584 7158 -1076 297 -1422 O
ATOM 1309 CB SER A 156 8.880 -9.063 -71.861 1.00 62.80 C
ANISOU 1309 CB SER A 156 7427 9995 6438 -1061 374 -1462 C
ATOM 1310 OG SER A 156 8.054 -10.117 -71.407 1.00 65.92 O
ANISOU 1310 OG SER A 156 7823 10399 6824 -1179 400 -1552 O
ATOM 1311 N PHE A 157 6.661 -7.510 -70.382 1.00 67.42 N
ANISOU 1311 N PHE A 157 7915 10784 6916 -952 275 -1301 N
ATOM 1312 CA PHE A 157 5.422 -7.302 -69.637 1.00 64.89 C
ANISOU 1312 CA PHE A 157 7549 10559 6544 -954 246 -1274 C
ATOM 1313 C PHE A 157 4.553 -6.225 -70.302 1.00 65.53 C
ANISOU 1313 C PHE A 157 7525 10882 6488 -881 209 -1203 C
ATOM 1314 O PHE A 157 3.353 -6.420 -70.502 1.00 64.92 O
ANISOU 1314 O PHE A 157 7363 10997 6303 -938 200 -1241 O
ATOM 1315 CB PHE A 157 5.739 -6.933 -68.175 1.00 63.74 C
ANISOU 1315 CB PHE A 157 7478 10224 6515 -881 225 -1193 C
ATOM 1316 CG PHE A 157 4.579 -6.326 -67.431 1.00 63.26 C
ANISOU 1316 CG PHE A 157 7369 10263 6402 -843 188 -1132 C
ATOM 1317 CD1 PHE A 157 4.342 -4.949 -67.478 1.00 62.77 C
ANISOU 1317 CD1 PHE A 157 7267 10286 6294 -714 152 -1014 C
ATOM 1318 CD2 PHE A 157 3.724 -7.122 -66.682 1.00 64.53 C
ANISOU 1318 CD2 PHE A 157 7527 10428 6561 -935 197 -1190 C
ATOM 1319 CE1 PHE A 157 3.269 -4.387 -66.809 1.00 61.55 C
ANISOU 1319 CE1 PHE A 157 7067 10225 6092 -674 123 -958 C
ATOM 1320 CE2 PHE A 157 2.652 -6.564 -66.004 1.00 65.21 C
ANISOU 1320 CE2 PHE A 157 7566 10611 6600 -900 164 -1136 C
ATOM 1321 CZ PHE A 157 2.425 -5.196 -66.070 1.00 64.33 C
ANISOU 1321 CZ PHE A 157 7411 10588 6442 -767 127 -1020 C
ATOM 1322 N GLU A 158 5.174 -5.099 -70.653 1.00 65.39 N
ANISOU 1322 N GLU A 158 7514 10855 6474 -755 191 -1101 N
ATOM 1323 CA GLU A 158 4.462 -3.955 -71.226 1.00 66.50 C
ANISOU 1323 CA GLU A 158 7570 11201 6496 -658 162 -1011 C
ATOM 1324 C GLU A 158 3.810 -4.330 -72.558 1.00 69.13 C
ANISOU 1324 C GLU A 158 7802 11782 6680 -730 169 -1083 C
ATOM 1325 O GLU A 158 2.700 -3.893 -72.855 1.00 69.54 O
ANISOU 1325 O GLU A 158 7757 12056 6608 -706 145 -1053 O
ATOM 1326 CB GLU A 158 5.422 -2.774 -71.413 1.00 66.24 C
ANISOU 1326 CB GLU A 158 7580 11080 6505 -520 158 -898 C
ATOM 1327 CG GLU A 158 4.766 -1.451 -71.786 1.00 67.86 C
ANISOU 1327 CG GLU A 158 7720 11453 6609 -393 135 -779 C
ATOM 1328 CD GLU A 158 5.747 -0.465 -72.406 1.00 70.14 C
ANISOU 1328 CD GLU A 158 8045 11689 6915 -285 149 -695 C
ATOM 1329 OE1 GLU A 158 5.350 0.682 -72.693 1.00 72.45 O
ANISOU 1329 OE1 GLU A 158 8301 12088 7137 -168 141 -586 O
ATOM 1330 OE2 GLU A 158 6.918 -0.836 -72.616 1.00 71.94 O
ANISOU 1330 OE2 GLU A 158 8338 11768 7226 -315 173 -736 O
ATOM 1331 N SER A 159 4.506 -5.145 -73.348 1.00 68.86 N
ANISOU 1331 N SER A 159 7789 11715 6659 -818 204 -1179 N
ATOM 1332 CA SER A 159 3.992 -5.588 -74.637 1.00 71.73 C
ANISOU 1332 CA SER A 159 8062 12307 6884 -901 217 -1263 C
ATOM 1333 C SER A 159 2.862 -6.597 -74.471 1.00 72.48 C
ANISOU 1333 C SER A 159 8098 12525 6914 -1043 226 -1376 C
ATOM 1334 O SER A 159 1.845 -6.515 -75.160 1.00 71.31 O
ANISOU 1334 O SER A 159 7836 12639 6616 -1073 211 -1399 O
ATOM 1335 CB SER A 159 5.114 -6.172 -75.499 1.00 70.53 C
ANISOU 1335 CB SER A 159 7957 12070 6772 -956 259 -1337 C
ATOM 1336 OG SER A 159 5.908 -5.139 -76.058 1.00 71.33 O
ANISOU 1336 OG SER A 159 8073 12152 6874 -833 250 -1239 O
ATOM 1337 N LYS A 160 3.049 -7.534 -73.543 1.00 72.69 N
ANISOU 1337 N LYS A 160 8201 12365 7052 -1129 253 -1446 N
ATOM 1338 CA LYS A 160 2.074 -8.589 -73.269 1.00 75.23 C
ANISOU 1338 CA LYS A 160 8487 12763 7332 -1277 275 -1562 C
ATOM 1339 C LYS A 160 0.721 -8.022 -72.804 1.00 76.35 C
ANISOU 1339 C LYS A 160 8539 13090 7381 -1243 231 -1509 C
ATOM 1340 O LYS A 160 -0.328 -8.608 -73.067 1.00 80.27 O
ANISOU 1340 O LYS A 160 8951 13772 7773 -1355 240 -1599 O
ATOM 1341 CB LYS A 160 2.649 -9.572 -72.238 1.00 75.20 C
ANISOU 1341 CB LYS A 160 8602 12490 7481 -1347 315 -1620 C
ATOM 1342 CG LYS A 160 1.690 -10.643 -71.741 1.00 78.45 C
ANISOU 1342 CG LYS A 160 8999 12936 7872 -1495 346 -1730 C
ATOM 1343 CD LYS A 160 2.183 -11.233 -70.428 1.00 81.20 C
ANISOU 1343 CD LYS A 160 9467 13009 8374 -1508 371 -1729 C
ATOM 1344 CE LYS A 160 1.030 -11.521 -69.479 1.00 83.61 C
ANISOU 1344 CE LYS A 160 9749 13359 8658 -1566 365 -1748 C
ATOM 1345 NZ LYS A 160 1.438 -11.354 -68.055 1.00 80.54 N
ANISOU 1345 NZ LYS A 160 9457 12742 8402 -1493 352 -1666 N
ATOM 1346 N VAL A 161 0.756 -6.876 -72.129 1.00 76.19 N
ANISOU 1346 N VAL A 161 8533 13020 7395 -1091 188 -1367 N
ATOM 1347 CA VAL A 161 -0.462 -6.193 -71.680 1.00 75.41 C
ANISOU 1347 CA VAL A 161 8350 13087 7212 -1034 148 -1299 C
ATOM 1348 C VAL A 161 -1.042 -5.357 -72.825 1.00 77.09 C
ANISOU 1348 C VAL A 161 8443 13582 7265 -961 120 -1245 C
ATOM 1349 O VAL A 161 -2.265 -5.262 -72.985 1.00 78.37 O
ANISOU 1349 O VAL A 161 8492 13982 7300 -979 99 -1254 O
ATOM 1350 CB VAL A 161 -0.192 -5.309 -70.429 1.00 72.70 C
ANISOU 1350 CB VAL A 161 8078 12565 6977 -901 121 -1170 C
ATOM 1351 CG1 VAL A 161 -1.358 -4.367 -70.145 1.00 69.99 C
ANISOU 1351 CG1 VAL A 161 7645 12406 6540 -810 81 -1079 C
ATOM 1352 CG2 VAL A 161 0.105 -6.177 -69.211 1.00 70.13 C
ANISOU 1352 CG2 VAL A 161 7852 12008 6785 -979 143 -1223 C
ATOM 1353 N PHE A 162 -0.150 -4.770 -73.620 1.00 77.06 N
ANISOU 1353 N PHE A 162 8462 13552 7263 -878 122 -1189 N
ATOM 1354 CA PHE A 162 -0.521 -3.975 -74.792 1.00 81.07 C
ANISOU 1354 CA PHE A 162 8869 14309 7623 -800 103 -1130 C
ATOM 1355 C PHE A 162 -1.367 -4.771 -75.794 1.00 84.36 C
ANISOU 1355 C PHE A 162 9167 14997 7886 -934 110 -1253 C
ATOM 1356 O PHE A 162 -2.317 -4.237 -76.376 1.00 83.61 O
ANISOU 1356 O PHE A 162 8951 15178 7639 -888 82 -1213 O
ATOM 1357 CB PHE A 162 0.742 -3.425 -75.466 1.00 80.25 C
ANISOU 1357 CB PHE A 162 8830 14095 7566 -716 117 -1072 C
ATOM 1358 CG PHE A 162 0.498 -2.757 -76.792 1.00 82.65 C
ANISOU 1358 CG PHE A 162 9040 14643 7718 -650 106 -1023 C
ATOM 1359 CD1 PHE A 162 -0.316 -1.633 -76.888 1.00 82.74 C
ANISOU 1359 CD1 PHE A 162 8973 14835 7627 -513 74 -896 C
ATOM 1360 CD2 PHE A 162 1.119 -3.233 -77.947 1.00 84.81 C
ANISOU 1360 CD2 PHE A 162 9308 14961 7952 -718 132 -1098 C
ATOM 1361 CE1 PHE A 162 -0.520 -1.011 -78.109 1.00 84.64 C
ANISOU 1361 CE1 PHE A 162 9132 15302 7725 -442 67 -842 C
ATOM 1362 CE2 PHE A 162 0.916 -2.616 -79.173 1.00 84.53 C
ANISOU 1362 CE2 PHE A 162 9189 15155 7773 -655 123 -1050 C
ATOM 1363 CZ PHE A 162 0.099 -1.503 -79.254 1.00 85.79 C
ANISOU 1363 CZ PHE A 162 9271 15496 7828 -514 89 -918 C
ATOM 1364 N HIS A 163 -1.021 -6.044 -75.982 1.00 87.05 N
ANISOU 1364 N HIS A 163 9545 15264 8266 -1100 152 -1404 N
ATOM 1365 CA HIS A 163 -1.742 -6.914 -76.914 1.00 91.37 C
ANISOU 1365 CA HIS A 163 9989 16049 8675 -1252 171 -1543 C
ATOM 1366 C HIS A 163 -3.061 -7.380 -76.365 1.00 90.65 C
ANISOU 1366 C HIS A 163 9819 16105 8517 -1343 163 -1606 C
ATOM 1367 O HIS A 163 -4.010 -7.593 -77.121 1.00 92.20 O
ANISOU 1367 O HIS A 163 9886 16593 8553 -1415 156 -1671 O
ATOM 1368 CB HIS A 163 -0.876 -8.096 -77.341 1.00 93.87 C
ANISOU 1368 CB HIS A 163 10380 16225 9061 -1398 231 -1685 C
ATOM 1369 CG HIS A 163 0.270 -7.711 -78.249 1.00 97.56 C
ANISOU 1369 CG HIS A 163 10888 16633 9546 -1332 242 -1648 C
ATOM 1370 ND1 HIS A 163 0.078 -7.205 -79.485 1.00100.14 N
ANISOU 1370 ND1 HIS A 163 11120 17199 9727 -1296 226 -1626 N
ATOM 1371 CD2 HIS A 163 1.652 -7.764 -78.057 1.00 97.31 C
ANISOU 1371 CD2 HIS A 163 10984 16325 9665 -1295 268 -1629 C
ATOM 1372 CE1 HIS A 163 1.272 -6.948 -80.054 1.00101.89 C
ANISOU 1372 CE1 HIS A 163 11410 17297 10006 -1242 244 -1595 C
ATOM 1373 NE2 HIS A 163 2.234 -7.290 -79.179 1.00100.98 N
ANISOU 1373 NE2 HIS A 163 11428 16868 10072 -1243 269 -1599 N
ATOM 1374 N LYS A 164 -3.131 -7.535 -75.044 1.00 87.54 N
ANISOU 1374 N LYS A 164 9499 15519 8240 -1341 164 -1587 N
ATOM 1375 CA LYS A 164 -4.374 -7.886 -74.365 1.00 86.35 C
ANISOU 1375 CA LYS A 164 9283 15487 8040 -1415 156 -1633 C
ATOM 1376 C LYS A 164 -5.384 -6.743 -74.468 1.00 86.98 C
ANISOU 1376 C LYS A 164 9239 15818 7991 -1283 98 -1516 C
ATOM 1377 O LYS A 164 -6.565 -6.976 -74.713 1.00 91.33 O
ANISOU 1377 O LYS A 164 9664 16628 8406 -1353 88 -1574 O
ATOM 1378 CB LYS A 164 -4.102 -8.234 -72.901 1.00 85.22 C
ANISOU 1378 CB LYS A 164 9258 15060 8059 -1427 170 -1625 C
ATOM 1379 CG LYS A 164 -5.152 -9.131 -72.262 1.00 86.49 C
ANISOU 1379 CG LYS A 164 9384 15283 8194 -1573 192 -1733 C
ATOM 1380 CD LYS A 164 -4.719 -9.597 -70.879 1.00 85.84 C
ANISOU 1380 CD LYS A 164 9436 14898 8280 -1593 215 -1731 C
ATOM 1381 CE LYS A 164 -3.712 -10.736 -70.966 1.00 86.87 C
ANISOU 1381 CE LYS A 164 9682 14804 8519 -1708 281 -1838 C
ATOM 1382 NZ LYS A 164 -2.900 -10.856 -69.723 1.00 87.55 N
ANISOU 1382 NZ LYS A 164 9911 14569 8782 -1661 292 -1785 N
ATOM 1383 N LEU A 165 -4.904 -5.511 -74.301 1.00 86.64 N
ANISOU 1383 N LEU A 165 9231 15699 7988 -1092 67 -1353 N
ATOM 1384 CA LEU A 165 -5.735 -4.313 -74.479 1.00 86.62 C
ANISOU 1384 CA LEU A 165 9123 15918 7869 -940 20 -1222 C
ATOM 1385 C LEU A 165 -6.169 -4.153 -75.932 1.00 89.44 C
ANISOU 1385 C LEU A 165 9348 16591 8042 -941 9 -1239 C
ATOM 1386 O LEU A 165 -7.299 -3.750 -76.207 1.00 91.29 O
ANISOU 1386 O LEU A 165 9447 17108 8130 -902 -21 -1207 O
ATOM 1387 CB LEU A 165 -4.988 -3.054 -74.021 1.00 84.58 C
ANISOU 1387 CB LEU A 165 8951 15478 7706 -741 5 -1050 C
ATOM 1388 CG LEU A 165 -4.584 -2.921 -72.547 1.00 81.24 C
ANISOU 1388 CG LEU A 165 8648 14765 7452 -704 8 -1002 C
ATOM 1389 CD1 LEU A 165 -3.714 -1.687 -72.351 1.00 75.98 C
ANISOU 1389 CD1 LEU A 165 8064 13938 6867 -522 3 -848 C
ATOM 1390 CD2 LEU A 165 -5.803 -2.875 -71.637 1.00 78.26 C
ANISOU 1390 CD2 LEU A 165 8211 14482 7042 -709 -11 -993 C
ATOM 1391 N LYS A 166 -5.255 -4.460 -76.852 1.00 90.11 N
ANISOU 1391 N LYS A 166 9471 16632 8133 -980 34 -1285 N
ATOM 1392 CA LYS A 166 -5.557 -4.509 -78.281 1.00 92.74 C
ANISOU 1392 CA LYS A 166 9687 17254 8295 -1012 30 -1327 C
ATOM 1393 C LYS A 166 -6.630 -5.555 -78.581 1.00 94.38 C
ANISOU 1393 C LYS A 166 9777 17702 8380 -1199 39 -1489 C
ATOM 1394 O LYS A 166 -7.699 -5.229 -79.099 1.00 90.57 O
ANISOU 1394 O LYS A 166 9145 17542 7726 -1177 7 -1473 O
ATOM 1395 CB LYS A 166 -4.292 -4.832 -79.084 1.00 93.76 C
ANISOU 1395 CB LYS A 166 9897 17250 8478 -1048 64 -1371 C
ATOM 1396 CG LYS A 166 -3.630 -3.638 -79.752 1.00 95.67 C
ANISOU 1396 CG LYS A 166 10154 17498 8698 -868 49 -1221 C
ATOM 1397 CD LYS A 166 -2.509 -4.096 -80.677 1.00 98.55 C
ANISOU 1397 CD LYS A 166 10577 17778 9091 -931 85 -1290 C
ATOM 1398 CE LYS A 166 -2.246 -3.085 -81.783 1.00100.03 C
ANISOU 1398 CE LYS A 166 10719 18114 9172 -794 71 -1177 C
ATOM 1399 NZ LYS A 166 -1.463 -3.681 -82.899 1.00 98.76 N
ANISOU 1399 NZ LYS A 166 10571 17965 8986 -887 105 -1274 N
ATOM 1400 N LYS A 167 -6.337 -6.811 -78.246 1.00 97.05 N
ANISOU 1400 N LYS A 167 10185 17882 8804 -1382 86 -1643 N
ATOM 1401 CA LYS A 167 -7.247 -7.920 -78.525 1.00100.68 C
ANISOU 1401 CA LYS A 167 10552 18537 9162 -1585 112 -1818 C
ATOM 1402 C LYS A 167 -8.401 -7.988 -77.530 1.00101.81 C
ANISOU 1402 C LYS A 167 10640 18754 9288 -1611 94 -1824 C
ATOM 1403 O LYS A 167 -8.973 -9.051 -77.289 1.00105.30 O
ANISOU 1403 O LYS A 167 11059 19232 9714 -1795 130 -1974 O
ATOM 1404 CB LYS A 167 -6.485 -9.253 -78.607 1.00103.29 C
ANISOU 1404 CB LYS A 167 10985 18667 9591 -1772 183 -1984 C
ATOM 1405 CG LYS A 167 -6.368 -9.830 -80.020 1.00105.90 C
ANISOU 1405 CG LYS A 167 11248 19186 9801 -1892 213 -2107 C
ATOM 1406 CD LYS A 167 -6.180 -8.754 -81.090 1.00106.65 C
ANISOU 1406 CD LYS A 167 11269 19472 9781 -1740 168 -1988 C
ATOM 1407 CE LYS A 167 -4.714 -8.488 -81.390 1.00105.15 C
ANISOU 1407 CE LYS A 167 11206 19034 9709 -1660 187 -1931 C
ATOM 1408 NZ LYS A 167 -4.171 -9.473 -82.363 1.00104.94 N
ANISOU 1408 NZ LYS A 167 11194 19018 9661 -1820 244 -2087 N
ATOM 1409 N MET A 168 -8.720 -6.838 -76.945 1.00100.77 N
ANISOU 1409 N MET A 168 10492 18634 9162 -1426 44 -1658 N
ATOM 1410 CA MET A 168 -10.006 -6.613 -76.306 1.00 99.85 C
ANISOU 1410 CA MET A 168 10273 18691 8971 -1414 15 -1638 C
ATOM 1411 C MET A 168 -10.602 -5.338 -76.889 1.00 98.47 C
ANISOU 1411 C MET A 168 9973 18786 8652 -1227 -39 -1489 C
ATOM 1412 O MET A 168 -10.209 -4.899 -77.965 1.00 94.95 O
ANISOU 1412 O MET A 168 9493 18453 8128 -1159 -49 -1444 O
ATOM 1413 CB MET A 168 -9.848 -6.498 -74.789 1.00 98.98 C
ANISOU 1413 CB MET A 168 10281 18297 9029 -1369 17 -1580 C
ATOM 1414 CG MET A 168 -9.624 -7.825 -74.083 1.00 98.48 C
ANISOU 1414 CG MET A 168 10314 18022 9080 -1561 72 -1731 C
ATOM 1415 SD MET A 168 -9.182 -7.610 -72.350 1.00 99.92 S
ANISOU 1415 SD MET A 168 10652 17843 9468 -1486 73 -1644 S
ATOM 1416 CE MET A 168 -8.877 -9.305 -71.853 1.00 99.90 C
ANISOU 1416 CE MET A 168 10754 17629 9572 -1724 149 -1833 C
ATOM 1417 N LYS A 169 -11.551 -4.744 -76.182 1.00101.19 N
ANISOU 1417 N LYS A 169 10251 19233 8961 -1139 -72 -1408 N
ATOM 1418 CA LYS A 169 -12.163 -3.506 -76.644 1.00105.55 C
ANISOU 1418 CA LYS A 169 10687 20033 9381 -946 -119 -1255 C
ATOM 1419 C LYS A 169 -11.336 -2.308 -76.192 1.00102.13 C
ANISOU 1419 C LYS A 169 10371 19362 9068 -730 -127 -1067 C
ATOM 1420 O LYS A 169 -11.423 -1.228 -76.777 1.00102.26 O
ANISOU 1420 O LYS A 169 10334 19518 9000 -553 -151 -926 O
ATOM 1421 CB LYS A 169 -13.606 -3.375 -76.120 1.00110.30 C
ANISOU 1421 CB LYS A 169 11154 20870 9882 -942 -146 -1251 C
ATOM 1422 CG LYS A 169 -14.268 -4.688 -75.720 1.00111.35 C
ANISOU 1422 CG LYS A 169 11251 21051 10005 -1179 -120 -1444 C
ATOM 1423 CD LYS A 169 -15.721 -4.746 -76.164 1.00110.64 C
ANISOU 1423 CD LYS A 169 10951 21378 9708 -1223 -147 -1492 C
ATOM 1424 CE LYS A 169 -16.261 -6.158 -76.031 1.00109.26 C
ANISOU 1424 CE LYS A 169 10740 21264 9508 -1489 -108 -1710 C
ATOM 1425 NZ LYS A 169 -17.189 -6.497 -77.140 1.00112.83 N
ANISOU 1425 NZ LYS A 169 10994 22138 9736 -1588 -120 -1811 N
ATOM 1426 N TYR A 170 -10.509 -2.526 -75.169 1.00100.66 N
ANISOU 1426 N TYR A 170 10347 18820 9077 -749 -104 -1069 N
ATOM 1427 CA TYR A 170 -9.951 -1.444 -74.347 1.00 96.58 C
ANISOU 1427 CA TYR A 170 9939 18069 8686 -565 -110 -906 C
ATOM 1428 C TYR A 170 -9.109 -0.436 -75.126 1.00 93.60 C
ANISOU 1428 C TYR A 170 9600 17658 8304 -401 -110 -775 C
ATOM 1429 O TYR A 170 -9.222 0.772 -74.909 1.00 90.67 O
ANISOU 1429 O TYR A 170 9231 17287 7930 -212 -122 -614 O
ATOM 1430 CB TYR A 170 -9.156 -2.016 -73.158 1.00 96.53 C
ANISOU 1430 CB TYR A 170 10096 17698 8883 -640 -83 -953 C
ATOM 1431 CG TYR A 170 -9.946 -2.964 -72.256 1.00100.34 C
ANISOU 1431 CG TYR A 170 10560 18179 9386 -792 -75 -1069 C
ATOM 1432 CD1 TYR A 170 -11.308 -3.207 -72.475 1.00102.04 C
ANISOU 1432 CD1 TYR A 170 10617 18705 9448 -853 -92 -1125 C
ATOM 1433 CD2 TYR A 170 -9.338 -3.587 -71.164 1.00100.05 C
ANISOU 1433 CD2 TYR A 170 10661 17834 9519 -869 -49 -1118 C
ATOM 1434 CE1 TYR A 170 -12.028 -4.064 -71.657 1.00102.20 C
ANISOU 1434 CE1 TYR A 170 10623 18722 9486 -997 -79 -1234 C
ATOM 1435 CE2 TYR A 170 -10.055 -4.440 -70.333 1.00102.04 C
ANISOU 1435 CE2 TYR A 170 10903 18077 9789 -1005 -36 -1219 C
ATOM 1436 CZ TYR A 170 -11.399 -4.674 -70.587 1.00104.21 C
ANISOU 1436 CZ TYR A 170 11025 18657 9913 -1072 -49 -1278 C
ATOM 1437 OH TYR A 170 -12.121 -5.516 -69.776 1.00104.43 O
ANISOU 1437 OH TYR A 170 11042 18678 9956 -1213 -31 -1382 O
ATOM 1438 N LEU A 171 -8.281 -0.936 -76.038 1.00 94.47 N
ANISOU 1438 N LEU A 171 9742 17739 8412 -477 -91 -845 N
ATOM 1439 CA LEU A 171 -7.423 -0.084 -76.851 1.00 96.38 C
ANISOU 1439 CA LEU A 171 10024 17948 8648 -342 -85 -736 C
ATOM 1440 C LEU A 171 -7.657 -0.353 -78.338 1.00 98.39 C
ANISOU 1440 C LEU A 171 10161 18492 8727 -391 -90 -791 C
ATOM 1441 O LEU A 171 -7.350 -1.439 -78.833 1.00 99.11 O
ANISOU 1441 O LEU A 171 10254 18587 8813 -564 -70 -944 O
ATOM 1442 CB LEU A 171 -5.955 -0.328 -76.487 1.00 98.60 C
ANISOU 1442 CB LEU A 171 10477 17870 9114 -370 -52 -755 C
ATOM 1443 CG LEU A 171 -4.937 0.800 -76.680 1.00100.16 C
ANISOU 1443 CG LEU A 171 10767 17908 9379 -199 -40 -609 C
ATOM 1444 CD1 LEU A 171 -5.293 2.021 -75.843 1.00 99.28 C
ANISOU 1444 CD1 LEU A 171 10676 17744 9302 -19 -50 -448 C
ATOM 1445 CD2 LEU A 171 -3.537 0.311 -76.332 1.00100.07 C
ANISOU 1445 CD2 LEU A 171 10908 17568 9542 -264 -9 -663 C
ATOM 1446 N VAL A 172 -8.222 0.633 -79.037 1.00 99.61 N
ANISOU 1446 N VAL A 172 10213 18894 8737 -237 -113 -667 N
ATOM 1447 CA VAL A 172 -8.455 0.533 -80.485 1.00102.25 C
ANISOU 1447 CA VAL A 172 10429 19528 8890 -258 -122 -696 C
ATOM 1448 C VAL A 172 -7.502 1.457 -81.238 1.00104.21 C
ANISOU 1448 C VAL A 172 10742 19706 9146 -108 -107 -568 C
ATOM 1449 O VAL A 172 -7.369 2.635 -80.901 1.00104.17 O
ANISOU 1449 O VAL A 172 10784 19616 9179 84 -105 -399 O
ATOM 1450 CB VAL A 172 -9.917 0.879 -80.869 1.00102.39 C
ANISOU 1450 CB VAL A 172 10257 19942 8704 -202 -160 -657 C
ATOM 1451 CG1 VAL A 172 -10.068 1.017 -82.380 1.00102.87 C
ANISOU 1451 CG1 VAL A 172 10200 20311 8572 -182 -171 -651 C
ATOM 1452 CG2 VAL A 172 -10.879 -0.173 -80.334 1.00102.44 C
ANISOU 1452 CG2 VAL A 172 10182 20062 8678 -384 -170 -813 C
ATOM 1453 N GLU A 173 -6.847 0.912 -82.260 1.00107.08 N
ANISOU 1453 N GLU A 173 11110 20102 9472 -201 -90 -653 N
ATOM 1454 CA GLU A 173 -5.904 1.673 -83.070 1.00109.50 C
ANISOU 1454 CA GLU A 173 11476 20348 9778 -81 -71 -550 C
ATOM 1455 C GLU A 173 -6.610 2.792 -83.840 1.00113.70 C
ANISOU 1455 C GLU A 173 11895 21172 10134 104 -92 -392 C
ATOM 1456 O GLU A 173 -7.684 2.587 -84.413 1.00113.87 O
ANISOU 1456 O GLU A 173 11755 21537 9973 76 -122 -425 O
ATOM 1457 CB GLU A 173 -5.168 0.742 -84.030 1.00110.21 C
ANISOU 1457 CB GLU A 173 11580 20443 9852 -238 -48 -692 C
ATOM 1458 CG GLU A 173 -3.792 1.232 -84.446 1.00109.28 C
ANISOU 1458 CG GLU A 173 11588 20105 9827 -163 -15 -626 C
ATOM 1459 CD GLU A 173 -3.218 0.428 -85.594 1.00109.67 C
ANISOU 1459 CD GLU A 173 11622 20226 9819 -299 5 -753 C
ATOM 1460 OE1 GLU A 173 -3.062 -0.804 -85.447 1.00109.10 O
ANISOU 1460 OE1 GLU A 173 11568 20084 9800 -493 21 -927 O
ATOM 1461 OE2 GLU A 173 -2.924 1.029 -86.647 1.00111.78 O
ANISOU 1461 OE2 GLU A 173 11863 20618 9988 -211 10 -677 O
ATOM 1462 N VAL A 174 -6.002 3.976 -83.832 1.00116.75 N
ANISOU 1462 N VAL A 174 12366 21419 10573 295 -72 -222 N
ATOM 1463 CA VAL A 174 -6.556 5.148 -84.512 1.00119.85 C
ANISOU 1463 CA VAL A 174 12676 22045 10815 498 -80 -48 C
ATOM 1464 C VAL A 174 -5.713 5.528 -85.741 1.00124.24 C
ANISOU 1464 C VAL A 174 13260 22629 11313 552 -54 2 C
ATOM 1465 O VAL A 174 -4.550 5.135 -85.852 1.00121.42 O
ANISOU 1465 O VAL A 174 13019 22042 11074 469 -25 -65 O
ATOM 1466 CB VAL A 174 -6.730 6.333 -83.526 1.00117.12 C
ANISOU 1466 CB VAL A 174 12396 21549 10554 694 -67 125 C
ATOM 1467 CG1 VAL A 174 -6.534 7.674 -84.214 1.00119.45 C
ANISOU 1467 CG1 VAL A 174 12703 21900 10779 918 -41 323 C
ATOM 1468 CG2 VAL A 174 -8.103 6.272 -82.873 1.00117.09 C
ANISOU 1468 CG2 VAL A 174 12274 21735 10480 704 -104 125 C
ATOM 1469 N GLN A 175 -6.317 6.282 -86.659 1.00133.14 N
ANISOU 1469 N GLN A 175 14279 24049 12257 694 -65 122 N
ATOM 1470 CA GLN A 175 -5.722 6.576 -87.971 1.00138.92 C
ANISOU 1470 CA GLN A 175 15007 24883 12892 739 -45 165 C
ATOM 1471 C GLN A 175 -4.684 7.713 -87.949 1.00145.25 C
ANISOU 1471 C GLN A 175 15960 25427 13802 909 6 326 C
ATOM 1472 O GLN A 175 -4.214 8.152 -89.006 1.00146.59 O
ANISOU 1472 O GLN A 175 16133 25674 13889 978 28 392 O
ATOM 1473 CB GLN A 175 -6.825 6.890 -88.995 1.00137.15 C
ANISOU 1473 CB GLN A 175 14597 25100 12412 822 -78 229 C
ATOM 1474 CG GLN A 175 -7.847 5.772 -89.197 1.00135.86 C
ANISOU 1474 CG GLN A 175 14269 25235 12117 643 -126 61 C
ATOM 1475 CD GLN A 175 -8.972 5.780 -88.166 1.00131.92 C
ANISOU 1475 CD GLN A 175 13698 24805 11619 661 -157 68 C
ATOM 1476 OE1 GLN A 175 -9.054 6.670 -87.315 1.00127.71 O
ANISOU 1476 OE1 GLN A 175 13232 24115 11177 820 -144 209 O
ATOM 1477 NE2 GLN A 175 -9.847 4.784 -88.243 1.00130.78 N
ANISOU 1477 NE2 GLN A 175 13417 24899 11372 493 -192 -87 N
ATOM 1478 N ASP A 176 -4.329 8.171 -86.744 1.00149.55 N
ANISOU 1478 N ASP A 176 16628 25667 14526 968 29 383 N
ATOM 1479 CA ASP A 176 -3.389 9.295 -86.536 1.00150.26 C
ANISOU 1479 CA ASP A 176 16867 25490 14732 1125 85 531 C
ATOM 1480 C ASP A 176 -4.017 10.674 -86.787 1.00155.45 C
ANISOU 1480 C ASP A 176 17489 26290 15283 1371 106 748 C
ATOM 1481 O ASP A 176 -3.436 11.703 -86.425 1.00153.87 O
ANISOU 1481 O ASP A 176 17412 25868 15182 1514 160 883 O
ATOM 1482 CB ASP A 176 -2.105 9.122 -87.363 1.00146.35 C
ANISOU 1482 CB ASP A 176 16459 24869 14277 1068 120 490 C
ATOM 1483 CG ASP A 176 -1.390 7.814 -87.068 1.00144.45 C
ANISOU 1483 CG ASP A 176 16269 24456 14158 841 111 287 C
ATOM 1484 OD1 ASP A 176 -0.896 7.643 -85.932 1.00141.09 O
ANISOU 1484 OD1 ASP A 176 15950 23740 13915 796 121 249 O
ATOM 1485 OD2 ASP A 176 -1.321 6.958 -87.976 1.00143.66 O
ANISOU 1485 OD2 ASP A 176 16102 24513 13968 709 97 166 O
ATOM 1486 N GLU A 177 -5.204 10.680 -87.398 1.00160.07 N
ANISOU 1486 N GLU A 177 17906 27245 15666 1419 67 780 N
ATOM 1487 CA GLU A 177 -5.948 11.912 -87.675 1.00159.30 C
ANISOU 1487 CA GLU A 177 17754 27326 15447 1659 84 986 C
ATOM 1488 C GLU A 177 -6.943 12.219 -86.543 1.00161.93 C
ANISOU 1488 C GLU A 177 18049 27668 15809 1732 67 1037 C
ATOM 1489 O GLU A 177 -8.127 12.480 -86.792 1.00163.57 O
ANISOU 1489 O GLU A 177 18110 28183 15854 1827 38 1105 O
ATOM 1490 CB GLU A 177 -6.668 11.802 -89.032 1.00157.05 C
ANISOU 1490 CB GLU A 177 17297 27462 14910 1687 51 1005 C
ATOM 1491 CG GLU A 177 -7.263 13.104 -89.561 1.00155.32 C
ANISOU 1491 CG GLU A 177 17029 27435 14550 1951 77 1234 C
ATOM 1492 CD GLU A 177 -6.258 13.962 -90.307 1.00152.49 C
ANISOU 1492 CD GLU A 177 16787 26945 14205 2075 145 1361 C
ATOM 1493 OE1 GLU A 177 -5.269 14.415 -89.686 1.00152.25 O
ANISOU 1493 OE1 GLU A 177 16933 26550 14364 2098 202 1395 O
ATOM 1494 OE2 GLU A 177 -6.469 14.198 -91.517 1.00149.90 O
ANISOU 1494 OE2 GLU A 177 16372 26889 13692 2148 142 1429 O
ATOM 1495 N VAL A 178 -6.452 12.176 -85.302 1.00159.89 N
ANISOU 1495 N VAL A 178 17918 27075 15755 1685 86 1000 N
ATOM 1496 CA VAL A 178 -7.271 12.472 -84.114 1.00154.91 C
ANISOU 1496 CA VAL A 178 17274 26404 15178 1745 77 1042 C
ATOM 1497 C VAL A 178 -6.529 13.386 -83.118 1.00148.10 C
ANISOU 1497 C VAL A 178 16590 25170 14509 1849 141 1143 C
ATOM 1498 O VAL A 178 -7.145 14.254 -82.488 1.00145.74 O
ANISOU 1498 O VAL A 178 16294 24861 14218 2005 164 1270 O
ATOM 1499 CB VAL A 178 -7.776 11.176 -83.420 1.00154.83 C
ANISOU 1499 CB VAL A 178 17198 26428 15201 1532 19 849 C
ATOM 1500 CG1 VAL A 178 -8.363 11.482 -82.054 1.00151.94 C
ANISOU 1500 CG1 VAL A 178 16856 25942 14932 1580 19 885 C
ATOM 1501 CG2 VAL A 178 -8.819 10.471 -84.279 1.00156.43 C
ANISOU 1501 CG2 VAL A 178 17201 27042 15191 1458 -38 772 C
ATOM 1502 N LYS A 179 -5.213 13.187 -82.996 1.00139.25 N
ANISOU 1502 N LYS A 179 15615 23755 13539 1762 172 1082 N
ATOM 1503 CA LYS A 179 -4.335 14.040 -82.169 1.00132.98 C
ANISOU 1503 CA LYS A 179 14994 22605 12924 1844 239 1165 C
ATOM 1504 C LYS A 179 -4.547 13.846 -80.657 1.00131.99 C
ANISOU 1504 C LYS A 179 14918 22285 12946 1791 228 1114 C
ATOM 1505 O LYS A 179 -5.532 14.336 -80.093 1.00132.61 O
ANISOU 1505 O LYS A 179 14943 22453 12988 1895 225 1194 O
ATOM 1506 CB LYS A 179 -4.468 15.522 -82.563 1.00132.37 C
ANISOU 1506 CB LYS A 179 14950 22555 12788 2091 306 1382 C
ATOM 1507 CG LYS A 179 -3.319 16.406 -82.101 1.00128.62 C
ANISOU 1507 CG LYS A 179 14662 21728 12479 2161 390 1459 C
ATOM 1508 CD LYS A 179 -3.346 17.756 -82.803 1.00125.68 C
ANISOU 1508 CD LYS A 179 14321 21404 12025 2388 467 1663 C
ATOM 1509 CE LYS A 179 -2.178 18.628 -82.372 1.00121.33 C
ANISOU 1509 CE LYS A 179 13960 20501 11638 2444 560 1729 C
ATOM 1510 NZ LYS A 179 -2.114 19.900 -83.142 1.00118.05 N
ANISOU 1510 NZ LYS A 179 13588 20120 11145 2654 646 1922 N
ATOM 1511 N PRO A 180 -3.601 13.145 -79.996 1.00127.66 N
ANISOU 1511 N PRO A 180 14472 21468 12563 1634 225 986 N
ATOM 1512 CA PRO A 180 -3.747 12.700 -78.606 1.00121.75 C
ANISOU 1512 CA PRO A 180 13762 20547 11947 1546 205 908 C
ATOM 1513 C PRO A 180 -3.584 13.832 -77.600 1.00117.65 C
ANISOU 1513 C PRO A 180 13354 19801 11544 1684 261 1031 C
ATOM 1514 O PRO A 180 -3.056 14.889 -77.941 1.00119.60 O
ANISOU 1514 O PRO A 180 13680 19956 11805 1822 326 1158 O
ATOM 1515 CB PRO A 180 -2.610 11.693 -78.447 1.00119.92 C
ANISOU 1515 CB PRO A 180 13614 20107 11843 1357 194 752 C
ATOM 1516 CG PRO A 180 -1.556 12.175 -79.382 1.00121.80 C
ANISOU 1516 CG PRO A 180 13923 20270 12082 1406 240 803 C
ATOM 1517 CD PRO A 180 -2.266 12.824 -80.539 1.00124.70 C
ANISOU 1517 CD PRO A 180 14190 20928 12260 1546 247 921 C
ATOM 1518 N ARG A 181 -4.039 13.605 -76.370 1.00114.45 N
ANISOU 1518 N ARG A 181 12956 19307 11221 1641 242 990 N
ATOM 1519 CA ARG A 181 -3.886 14.590 -75.298 1.00112.98 C
ANISOU 1519 CA ARG A 181 12877 18895 11155 1750 296 1087 C
ATOM 1520 C ARG A 181 -3.348 13.962 -74.003 1.00107.64 C
ANISOU 1520 C ARG A 181 12288 17959 10651 1609 281 973 C
ATOM 1521 O ARG A 181 -3.822 14.264 -72.905 1.00108.11 O
ANISOU 1521 O ARG A 181 12367 17937 10772 1642 287 998 O
ATOM 1522 CB ARG A 181 -5.201 15.347 -75.057 1.00116.17 C
ANISOU 1522 CB ARG A 181 13196 19478 11462 1907 303 1208 C
ATOM 1523 CG ARG A 181 -5.538 16.352 -76.154 1.00119.55 C
ANISOU 1523 CG ARG A 181 13581 20090 11750 2100 344 1369 C
ATOM 1524 CD ARG A 181 -6.868 17.053 -75.912 1.00122.09 C
ANISOU 1524 CD ARG A 181 13811 20601 11975 2262 351 1490 C
ATOM 1525 NE ARG A 181 -7.153 18.036 -76.961 1.00124.52 N
ANISOU 1525 NE ARG A 181 14084 21079 12149 2460 397 1656 N
ATOM 1526 CZ ARG A 181 -8.237 18.809 -77.010 1.00124.70 C
ANISOU 1526 CZ ARG A 181 14026 21287 12065 2641 416 1793 C
ATOM 1527 NH1 ARG A 181 -9.169 18.731 -76.066 1.00122.78 N
ANISOU 1527 NH1 ARG A 181 13727 21090 11833 2647 392 1781 N
ATOM 1528 NH2 ARG A 181 -8.388 19.667 -78.010 1.00126.05 N
ANISOU 1528 NH2 ARG A 181 14174 21601 12116 2821 462 1946 N
ATOM 1529 N GLY A 182 -2.339 13.103 -74.156 1.00101.76 N
ANISOU 1529 N GLY A 182 11595 17086 9981 1459 264 851 N
ATOM 1530 CA GLY A 182 -1.691 12.411 -73.038 1.00 95.19 C
ANISOU 1530 CA GLY A 182 10848 16011 9309 1321 249 739 C
ATOM 1531 C GLY A 182 -1.110 11.081 -73.493 1.00 92.32 C
ANISOU 1531 C GLY A 182 10469 15648 8958 1140 209 584 C
ATOM 1532 O GLY A 182 -1.573 10.508 -74.479 1.00 93.75 O
ANISOU 1532 O GLY A 182 10547 16060 9011 1096 178 539 O
ATOM 1533 N VAL A 183 -0.101 10.584 -72.779 1.00 89.32 N
ANISOU 1533 N VAL A 183 10191 15016 8729 1037 212 501 N
ATOM 1534 CA VAL A 183 0.562 9.323 -73.159 1.00 89.91 C
ANISOU 1534 CA VAL A 183 10268 15061 8833 870 184 355 C
ATOM 1535 C VAL A 183 0.171 8.144 -72.248 1.00 89.51 C
ANISOU 1535 C VAL A 183 10197 14978 8833 723 140 228 C
ATOM 1536 O VAL A 183 0.197 8.260 -71.016 1.00 88.98 O
ANISOU 1536 O VAL A 183 10189 14746 8870 721 141 234 O
ATOM 1537 CB VAL A 183 2.111 9.484 -73.258 1.00 89.21 C
ANISOU 1537 CB VAL A 183 10301 14730 8863 854 222 344 C
ATOM 1538 CG1 VAL A 183 2.723 9.850 -71.910 1.00 88.38 C
ANISOU 1538 CG1 VAL A 183 10308 14355 8918 862 243 359 C
ATOM 1539 CG2 VAL A 183 2.761 8.230 -73.831 1.00 88.16 C
ANISOU 1539 CG2 VAL A 183 10162 14591 8744 699 200 204 C
ATOM 1540 N LEU A 184 -0.203 7.020 -72.865 1.00 87.74 N
ANISOU 1540 N LEU A 184 9891 14912 8532 597 106 115 N
ATOM 1541 CA LEU A 184 -0.611 5.824 -72.121 1.00 85.34 C
ANISOU 1541 CA LEU A 184 9567 14591 8265 448 73 -11 C
ATOM 1542 C LEU A 184 0.564 5.167 -71.407 1.00 82.31 C
ANISOU 1542 C LEU A 184 9300 13928 8046 350 82 -92 C
ATOM 1543 O LEU A 184 1.549 4.779 -72.037 1.00 86.08 O
ANISOU 1543 O LEU A 184 9820 14329 8557 299 97 -142 O
ATOM 1544 CB LEU A 184 -1.303 4.804 -73.037 1.00 86.14 C
ANISOU 1544 CB LEU A 184 9552 14939 8236 333 45 -118 C
ATOM 1545 CG LEU A 184 -1.609 3.423 -72.426 1.00 85.68 C
ANISOU 1545 CG LEU A 184 9482 14853 8217 155 24 -268 C
ATOM 1546 CD1 LEU A 184 -2.786 3.475 -71.461 1.00 84.58 C
ANISOU 1546 CD1 LEU A 184 9291 14786 8057 163 3 -253 C
ATOM 1547 CD2 LEU A 184 -1.860 2.391 -73.512 1.00 88.39 C
ANISOU 1547 CD2 LEU A 184 9740 15387 8453 24 16 -390 C
ATOM 1548 N ASN A 185 0.446 5.031 -70.092 1.00 78.66 N
ANISOU 1548 N ASN A 185 8886 13319 7680 327 75 -102 N
ATOM 1549 CA ASN A 185 1.481 4.399 -69.297 1.00 73.53 C
ANISOU 1549 CA ASN A 185 8340 12414 7181 241 81 -172 C
ATOM 1550 C ASN A 185 0.975 3.109 -68.674 1.00 70.64 C
ANISOU 1550 C ASN A 185 7953 12051 6834 96 56 -292 C
ATOM 1551 O ASN A 185 -0.070 3.094 -68.016 1.00 73.00 O
ANISOU 1551 O ASN A 185 8205 12431 7099 94 38 -285 O
ATOM 1552 CB ASN A 185 1.971 5.357 -68.212 1.00 74.54 C
ANISOU 1552 CB ASN A 185 8561 12339 7421 336 99 -82 C
ATOM 1553 CG ASN A 185 3.478 5.379 -68.097 1.00 76.68 C
ANISOU 1553 CG ASN A 185 8939 12380 7815 324 123 -95 C
ATOM 1554 OD1 ASN A 185 4.185 5.623 -69.078 1.00 74.90 O
ANISOU 1554 OD1 ASN A 185 8724 12162 7571 349 144 -83 O
ATOM 1555 ND2 ASN A 185 3.982 5.125 -66.895 1.00 77.60 N
ANISOU 1555 ND2 ASN A 185 9132 12297 8056 286 120 -121 N
ATOM 1556 N ILE A 186 1.706 2.024 -68.895 1.00 65.60 N
ANISOU 1556 N ILE A 186 7352 11324 6249 -24 62 -402 N
ATOM 1557 CA ILE A 186 1.357 0.739 -68.302 1.00 64.56 C
ANISOU 1557 CA ILE A 186 7219 11162 6148 -167 52 -519 C
ATOM 1558 C ILE A 186 2.225 0.484 -67.069 1.00 64.84 C
ANISOU 1558 C ILE A 186 7368 10925 6343 -187 59 -528 C
ATOM 1559 O ILE A 186 3.451 0.462 -67.159 1.00 65.39 O
ANISOU 1559 O ILE A 186 7514 10830 6499 -181 76 -532 O
ATOM 1560 CB ILE A 186 1.473 -0.416 -69.327 1.00 61.77 C
ANISOU 1560 CB ILE A 186 6828 10899 5742 -297 62 -644 C
ATOM 1561 CG1 ILE A 186 0.476 -0.204 -70.467 1.00 62.16 C
ANISOU 1561 CG1 ILE A 186 6750 11247 5619 -286 51 -640 C
ATOM 1562 CG2 ILE A 186 1.229 -1.766 -68.663 1.00 60.62 C
ANISOU 1562 CG2 ILE A 186 6701 10685 5644 -448 67 -766 C
ATOM 1563 CD1 ILE A 186 0.762 -1.028 -71.704 1.00 61.98 C
ANISOU 1563 CD1 ILE A 186 6692 11324 5533 -387 66 -742 C
ATOM 1564 N ILE A 187 1.573 0.332 -65.916 1.00 67.90 N
ANISOU 1564 N ILE A 187 7762 11274 6762 -206 45 -528 N
ATOM 1565 CA ILE A 187 2.257 0.119 -64.633 1.00 67.35 C
ANISOU 1565 CA ILE A 187 7792 10965 6831 -221 48 -529 C
ATOM 1566 C ILE A 187 1.981 -1.298 -64.149 1.00 66.69 C
ANISOU 1566 C ILE A 187 7719 10843 6775 -365 50 -644 C
ATOM 1567 O ILE A 187 0.830 -1.705 -64.097 1.00 68.40 O
ANISOU 1567 O ILE A 187 7867 11207 6915 -422 41 -684 O
ATOM 1568 CB ILE A 187 1.751 1.099 -63.533 1.00 69.58 C
ANISOU 1568 CB ILE A 187 8086 11212 7136 -126 37 -433 C
ATOM 1569 CG1 ILE A 187 1.703 2.550 -64.039 1.00 69.28 C
ANISOU 1569 CG1 ILE A 187 8026 11248 7048 20 45 -314 C
ATOM 1570 CG2 ILE A 187 2.582 0.971 -62.251 1.00 67.99 C
ANISOU 1570 CG2 ILE A 187 7989 10768 7074 -135 39 -429 C
ATOM 1571 CD1 ILE A 187 3.045 3.128 -64.430 1.00 71.22 C
ANISOU 1571 CD1 ILE A 187 8343 11355 7360 79 68 -274 C
ATOM 1572 N PRO A 188 3.031 -2.045 -63.765 1.00 68.54 N
ANISOU 1572 N PRO A 188 8040 10879 7120 -421 65 -696 N
ATOM 1573 CA PRO A 188 2.791 -3.348 -63.140 1.00 71.69 C
ANISOU 1573 CA PRO A 188 8466 11213 7558 -546 76 -792 C
ATOM 1574 C PRO A 188 2.171 -3.181 -61.751 1.00 75.95 C
ANISOU 1574 C PRO A 188 9025 11697 8133 -533 60 -754 C
ATOM 1575 O PRO A 188 2.699 -2.431 -60.927 1.00 76.43 O
ANISOU 1575 O PRO A 188 9142 11629 8269 -448 49 -675 O
ATOM 1576 CB PRO A 188 4.199 -3.963 -63.030 1.00 69.30 C
ANISOU 1576 CB PRO A 188 8258 10700 7372 -572 98 -827 C
ATOM 1577 CG PRO A 188 5.088 -3.098 -63.865 1.00 67.89 C
ANISOU 1577 CG PRO A 188 8084 10517 7194 -483 99 -772 C
ATOM 1578 CD PRO A 188 4.466 -1.737 -63.858 1.00 67.41 C
ANISOU 1578 CD PRO A 188 7974 10566 7069 -370 77 -667 C
ATOM 1579 N LYS A 189 1.036 -3.841 -61.520 1.00 83.31 N
ANISOU 1579 N LYS A 189 9908 12738 9007 -619 60 -813 N
ATOM 1580 CA LYS A 189 0.359 -3.809 -60.221 1.00 86.82 C
ANISOU 1580 CA LYS A 189 10367 13140 9478 -623 49 -789 C
ATOM 1581 C LYS A 189 0.283 -5.201 -59.610 1.00 92.51 C
ANISOU 1581 C LYS A 189 11136 13765 10249 -755 74 -886 C
ATOM 1582 O LYS A 189 -0.656 -5.955 -59.882 1.00 93.12 O
ANISOU 1582 O LYS A 189 11158 13969 10254 -859 88 -967 O
ATOM 1583 CB LYS A 189 -1.052 -3.208 -60.338 1.00 86.41 C
ANISOU 1583 CB LYS A 189 10210 13310 9311 -594 29 -758 C
ATOM 1584 CG LYS A 189 -1.110 -1.686 -60.271 1.00 86.47 C
ANISOU 1584 CG LYS A 189 10197 13355 9300 -439 9 -632 C
ATOM 1585 CD LYS A 189 -0.580 -1.140 -58.951 1.00 80.87 C
ANISOU 1585 CD LYS A 189 9576 12451 8700 -374 4 -563 C
ATOM 1586 CE LYS A 189 -0.271 0.346 -59.059 1.00 79.93 C
ANISOU 1586 CE LYS A 189 9460 12328 8582 -225 1 -446 C
ATOM 1587 NZ LYS A 189 0.519 0.823 -57.894 1.00 76.71 N
ANISOU 1587 NZ LYS A 189 9147 11712 8288 -175 2 -394 N
ATOM 1588 N GLN A 190 1.290 -5.532 -58.798 1.00 96.50 N
ANISOU 1588 N GLN A 190 11744 14048 10874 -750 83 -877 N
ATOM 1589 CA GLN A 190 1.328 -6.777 -58.016 1.00100.54 C
ANISOU 1589 CA GLN A 190 12320 14431 11447 -854 111 -947 C
ATOM 1590 C GLN A 190 1.120 -8.038 -58.866 1.00102.64 C
ANISOU 1590 C GLN A 190 12571 14751 11675 -988 154 -1069 C
ATOM 1591 O GLN A 190 2.088 -8.674 -59.287 1.00106.44 O
ANISOU 1591 O GLN A 190 13108 15121 12213 -1016 183 -1112 O
ATOM 1592 CB GLN A 190 0.333 -6.714 -56.847 1.00105.57 C
ANISOU 1592 CB GLN A 190 12951 15085 12075 -868 99 -926 C
ATOM 1593 CG GLN A 190 0.587 -5.553 -55.888 1.00110.84 C
ANISOU 1593 CG GLN A 190 13645 15678 12790 -747 65 -814 C
ATOM 1594 CD GLN A 190 -0.692 -4.942 -55.330 1.00112.60 C
ANISOU 1594 CD GLN A 190 13805 16029 12947 -726 45 -777 C
ATOM 1595 OE1 GLN A 190 -1.799 -5.328 -55.706 1.00117.19 O
ANISOU 1595 OE1 GLN A 190 14312 16773 13440 -796 52 -832 O
ATOM 1596 NE2 GLN A 190 -0.539 -3.970 -54.438 1.00112.37 N
ANISOU 1596 NE2 GLN A 190 13803 15932 12959 -629 23 -687 N
ATOM 1597 N ASP A 191 -0.139 -8.389 -59.116 1.00103.06 N
ANISOU 1597 N ASP A 191 12549 14977 11632 -1072 162 -1129 N
ATOM 1598 CA ASP A 191 -0.470 -9.540 -59.953 1.00103.94 C
ANISOU 1598 CA ASP A 191 12636 15164 11693 -1212 209 -1256 C
ATOM 1599 C ASP A 191 -0.937 -9.107 -61.345 1.00103.64 C
ANISOU 1599 C ASP A 191 12486 15361 11531 -1211 196 -1277 C
ATOM 1600 O ASP A 191 -0.757 -9.837 -62.324 1.00107.43 O
ANISOU 1600 O ASP A 191 12952 15886 11978 -1298 232 -1369 O
ATOM 1601 CB ASP A 191 -1.540 -10.406 -59.277 1.00105.33 C
ANISOU 1601 CB ASP A 191 12805 15371 11844 -1333 238 -1328 C
ATOM 1602 CG ASP A 191 -1.666 -11.785 -59.909 1.00107.24 C
ANISOU 1602 CG ASP A 191 13057 15620 12066 -1494 305 -1469 C
ATOM 1603 OD1 ASP A 191 -0.703 -12.580 -59.821 1.00108.03 O
ANISOU 1603 OD1 ASP A 191 13256 15530 12260 -1525 349 -1502 O
ATOM 1604 OD2 ASP A 191 -2.733 -12.078 -60.485 1.00106.12 O
ANISOU 1604 OD2 ASP A 191 12825 15679 11815 -1589 319 -1547 O
ATOM 1605 N ASN A 192 -1.540 -7.922 -61.425 1.00 99.11 N
ANISOU 1605 N ASN A 192 11834 14937 10886 -1110 149 -1191 N
ATOM 1606 CA ASN A 192 -2.047 -7.395 -62.692 1.00 95.82 C
ANISOU 1606 CA ASN A 192 11304 14760 10341 -1089 133 -1193 C
ATOM 1607 C ASN A 192 -1.274 -6.173 -63.191 1.00 87.62 C
ANISOU 1607 C ASN A 192 10267 13713 9311 -937 103 -1083 C
ATOM 1608 O ASN A 192 -0.042 -6.166 -63.184 1.00 83.98 O
ANISOU 1608 O ASN A 192 9890 13071 8945 -900 113 -1063 O
ATOM 1609 CB ASN A 192 -3.548 -7.090 -62.590 1.00100.44 C
ANISOU 1609 CB ASN A 192 11778 15575 10810 -1102 112 -1192 C
ATOM 1610 CG ASN A 192 -4.411 -8.214 -63.133 1.00104.56 C
ANISOU 1610 CG ASN A 192 12234 16250 11244 -1271 146 -1332 C
ATOM 1611 OD1 ASN A 192 -3.905 -9.190 -63.689 1.00106.73 O
ANISOU 1611 OD1 ASN A 192 12545 16467 11538 -1376 189 -1431 O
ATOM 1612 ND2 ASN A 192 -5.726 -8.080 -62.980 1.00108.16 N
ANISOU 1612 ND2 ASN A 192 12589 16905 11599 -1299 131 -1345 N
ATOM 1613 N PHE A 193 -2.007 -5.153 -63.634 1.00 80.24 N
ANISOU 1613 N PHE A 193 9237 12975 8274 -849 72 -1013 N
ATOM 1614 CA PHE A 193 -1.416 -3.926 -64.156 1.00 76.49 C
ANISOU 1614 CA PHE A 193 8759 12510 7793 -703 52 -904 C
ATOM 1615 C PHE A 193 -2.362 -2.741 -63.978 1.00 76.01 C
ANISOU 1615 C PHE A 193 8622 12604 7654 -587 21 -801 C
ATOM 1616 O PHE A 193 -3.512 -2.910 -63.590 1.00 77.51 O
ANISOU 1616 O PHE A 193 8747 12921 7782 -626 12 -822 O
ATOM 1617 CB PHE A 193 -1.078 -4.085 -65.640 1.00 72.32 C
ANISOU 1617 CB PHE A 193 8186 12101 7192 -725 63 -947 C
ATOM 1618 CG PHE A 193 -2.283 -4.115 -66.530 1.00 69.06 C
ANISOU 1618 CG PHE A 193 7638 11984 6617 -763 53 -984 C
ATOM 1619 CD1 PHE A 193 -2.834 -2.934 -67.020 1.00 68.37 C
ANISOU 1619 CD1 PHE A 193 7467 12078 6431 -636 26 -882 C
ATOM 1620 CD2 PHE A 193 -2.875 -5.323 -66.873 1.00 69.05 C
ANISOU 1620 CD2 PHE A 193 7591 12083 6559 -925 76 -1121 C
ATOM 1621 CE1 PHE A 193 -3.950 -2.957 -67.838 1.00 69.24 C
ANISOU 1621 CE1 PHE A 193 7443 12479 6383 -664 14 -912 C
ATOM 1622 CE2 PHE A 193 -3.990 -5.355 -67.695 1.00 70.25 C
ANISOU 1622 CE2 PHE A 193 7610 12527 6554 -966 66 -1161 C
ATOM 1623 CZ PHE A 193 -4.528 -4.170 -68.178 1.00 70.72 C
ANISOU 1623 CZ PHE A 193 7579 12779 6511 -832 31 -1054 C
ATOM 1624 N ARG A 194 -1.873 -1.548 -64.297 1.00 77.82 N
ANISOU 1624 N ARG A 194 8860 12822 7885 -445 12 -691 N
ATOM 1625 CA ARG A 194 -2.687 -0.344 -64.259 1.00 79.81 C
ANISOU 1625 CA ARG A 194 9045 13216 8062 -318 -6 -583 C
ATOM 1626 C ARG A 194 -2.363 0.520 -65.470 1.00 79.00 C
ANISOU 1626 C ARG A 194 8905 13221 7890 -214 -4 -513 C
ATOM 1627 O ARG A 194 -1.207 0.891 -65.689 1.00 78.29 O
ANISOU 1627 O ARG A 194 8892 12983 7872 -164 9 -477 O
ATOM 1628 CB ARG A 194 -2.427 0.428 -62.966 1.00 85.04 C
ANISOU 1628 CB ARG A 194 9784 13698 8826 -229 -8 -494 C
ATOM 1629 CG ARG A 194 -3.553 1.353 -62.560 1.00 93.65 C
ANISOU 1629 CG ARG A 194 10808 14924 9850 -133 -21 -409 C
ATOM 1630 CD ARG A 194 -3.155 2.207 -61.371 1.00100.44 C
ANISOU 1630 CD ARG A 194 11753 15595 10813 -41 -16 -320 C
ATOM 1631 NE ARG A 194 -4.070 3.331 -61.200 1.00109.57 N
ANISOU 1631 NE ARG A 194 12850 16875 11904 82 -17 -219 N
ATOM 1632 CZ ARG A 194 -3.787 4.442 -60.524 1.00114.76 C
ANISOU 1632 CZ ARG A 194 13566 17415 12622 200 -2 -117 C
ATOM 1633 NH1 ARG A 194 -2.600 4.597 -59.944 1.00119.22 N
ANISOU 1633 NH1 ARG A 194 14243 17744 13309 206 11 -106 N
ATOM 1634 NH2 ARG A 194 -4.694 5.408 -60.437 1.00117.81 N
ANISOU 1634 NH2 ARG A 194 13895 17926 12942 312 2 -29 N
ATOM 1635 N ALA A 195 -3.383 0.818 -66.268 1.00 76.87 N
ANISOU 1635 N ALA A 195 8516 13216 7476 -185 -17 -496 N
ATOM 1636 CA ALA A 195 -3.203 1.607 -67.476 1.00 77.40 C
ANISOU 1636 CA ALA A 195 8537 13414 7457 -85 -14 -427 C
ATOM 1637 C ALA A 195 -3.668 3.042 -67.270 1.00 79.01 C
ANISOU 1637 C ALA A 195 8717 13675 7625 91 -15 -277 C
ATOM 1638 O ALA A 195 -4.840 3.364 -67.466 1.00 79.78 O
ANISOU 1638 O ALA A 195 8708 13996 7606 135 -30 -243 O
ATOM 1639 CB ALA A 195 -3.933 0.966 -68.643 1.00 78.89 C
ANISOU 1639 CB ALA A 195 8604 13871 7497 -167 -23 -507 C
ATOM 1640 N ILE A 196 -2.733 3.900 -66.873 1.00 81.96 N
ANISOU 1640 N ILE A 196 9193 13847 8100 191 4 -190 N
ATOM 1641 CA ILE A 196 -3.030 5.304 -66.584 1.00 82.66 C
ANISOU 1641 CA ILE A 196 9284 13943 8177 360 18 -47 C
ATOM 1642 C ILE A 196 -2.437 6.226 -67.651 1.00 84.96 C
ANISOU 1642 C ILE A 196 9586 14266 8428 477 43 42 C
ATOM 1643 O ILE A 196 -1.581 5.807 -68.436 1.00 83.97 O
ANISOU 1643 O ILE A 196 9487 14104 8314 425 50 -5 O
ATOM 1644 CB ILE A 196 -2.520 5.720 -65.180 1.00 81.57 C
ANISOU 1644 CB ILE A 196 9257 13551 8183 390 32 -9 C
ATOM 1645 CG1 ILE A 196 -0.997 5.546 -65.072 1.00 82.34 C
ANISOU 1645 CG1 ILE A 196 9472 13404 8407 355 50 -36 C
ATOM 1646 CG2 ILE A 196 -3.231 4.919 -64.098 1.00 82.50 C
ANISOU 1646 CG2 ILE A 196 9362 13655 8329 290 9 -81 C
ATOM 1647 CD1 ILE A 196 -0.386 6.150 -63.821 1.00 80.72 C
ANISOU 1647 CD1 ILE A 196 9373 12965 8332 402 68 13 C
ATOM 1648 N VAL A 197 -2.896 7.477 -67.676 1.00 85.71 N
ANISOU 1648 N VAL A 197 9663 14424 8477 636 63 175 N
ATOM 1649 CA VAL A 197 -2.382 8.466 -68.623 1.00 85.10 C
ANISOU 1649 CA VAL A 197 9603 14368 8362 762 97 276 C
ATOM 1650 C VAL A 197 -1.664 9.624 -67.950 1.00 88.55 C
ANISOU 1650 C VAL A 197 10154 14582 8906 877 145 380 C
ATOM 1651 O VAL A 197 -2.140 10.182 -66.958 1.00 88.00 O
ANISOU 1651 O VAL A 197 10104 14454 8875 936 156 433 O
ATOM 1652 CB VAL A 197 -3.484 9.027 -69.545 1.00 82.57 C
ANISOU 1652 CB VAL A 197 9159 14341 7872 870 93 357 C
ATOM 1653 CG1 VAL A 197 -3.981 7.945 -70.479 1.00 83.39 C
ANISOU 1653 CG1 VAL A 197 9151 14675 7858 753 53 251 C
ATOM 1654 CG2 VAL A 197 -4.627 9.623 -68.737 1.00 80.51 C
ANISOU 1654 CG2 VAL A 197 8851 14157 7581 958 92 430 C
ATOM 1655 N SER A 198 -0.513 9.980 -68.503 1.00 94.87 N
ANISOU 1655 N SER A 198 11030 15261 9754 902 178 402 N
ATOM 1656 CA SER A 198 0.196 11.173 -68.085 1.00101.68 C
ANISOU 1656 CA SER A 198 11996 15935 10701 1013 235 502 C
ATOM 1657 C SER A 198 -0.094 12.295 -69.075 1.00108.17 C
ANISOU 1657 C SER A 198 12789 16887 11420 1171 277 632 C
ATOM 1658 O SER A 198 0.169 12.161 -70.274 1.00107.77 O
ANISOU 1658 O SER A 198 12705 16946 11294 1173 277 630 O
ATOM 1659 CB SER A 198 1.699 10.899 -67.998 1.00101.75 C
ANISOU 1659 CB SER A 198 12110 15715 10832 940 251 444 C
ATOM 1660 OG SER A 198 1.974 9.852 -67.078 1.00 96.38 O
ANISOU 1660 OG SER A 198 11458 14916 10244 805 214 332 O
ATOM 1661 N ILE A 199 -0.664 13.387 -68.572 1.00113.87 N
ANISOU 1661 N ILE A 199 13525 17602 12137 1307 316 747 N
ATOM 1662 CA ILE A 199 -1.004 14.539 -69.407 1.00122.15 C
ANISOU 1662 CA ILE A 199 14555 18765 13092 1477 367 888 C
ATOM 1663 C ILE A 199 0.236 15.420 -69.617 1.00128.36 C
ANISOU 1663 C ILE A 199 15466 19345 13960 1537 440 949 C
ATOM 1664 O ILE A 199 1.269 15.203 -68.978 1.00127.37 O
ANISOU 1664 O ILE A 199 15434 18995 13964 1452 449 884 O
ATOM 1665 CB ILE A 199 -2.163 15.375 -68.799 1.00121.69 C
ANISOU 1665 CB ILE A 199 14459 18783 12991 1608 389 993 C
ATOM 1666 CG1 ILE A 199 -3.006 14.541 -67.813 1.00118.69 C
ANISOU 1666 CG1 ILE A 199 14020 18452 12625 1512 329 907 C
ATOM 1667 CG2 ILE A 199 -3.020 15.992 -69.901 1.00122.82 C
ANISOU 1667 CG2 ILE A 199 14509 19183 12974 1754 403 1106 C
ATOM 1668 CD1 ILE A 199 -3.981 13.573 -68.459 1.00118.67 C
ANISOU 1668 CD1 ILE A 199 13870 18729 12488 1443 261 840 C
ATOM 1669 N PHE A 200 0.128 16.408 -70.508 1.00137.33 N
ANISOU 1669 N PHE A 200 16601 20564 15015 1683 495 1073 N
ATOM 1670 CA PHE A 200 1.273 17.252 -70.899 1.00145.67 C
ANISOU 1670 CA PHE A 200 17769 21448 16130 1740 573 1132 C
ATOM 1671 C PHE A 200 1.865 18.182 -69.814 1.00151.10 C
ANISOU 1671 C PHE A 200 18586 21870 16955 1784 646 1176 C
ATOM 1672 O PHE A 200 3.087 18.327 -69.744 1.00144.46 O
ANISOU 1672 O PHE A 200 17843 20832 16210 1735 683 1144 O
ATOM 1673 CB PHE A 200 0.966 18.038 -72.182 1.00149.86 C
ANISOU 1673 CB PHE A 200 18265 22145 16530 1887 617 1258 C
ATOM 1674 CG PHE A 200 0.863 17.177 -73.412 1.00153.42 C
ANISOU 1674 CG PHE A 200 18617 22811 16863 1826 560 1202 C
ATOM 1675 CD1 PHE A 200 2.007 16.761 -74.087 1.00154.97 C
ANISOU 1675 CD1 PHE A 200 18858 22928 17093 1739 563 1136 C
ATOM 1676 CD2 PHE A 200 -0.378 16.787 -73.902 1.00155.88 C
ANISOU 1676 CD2 PHE A 200 18787 23412 17028 1851 505 1212 C
ATOM 1677 CE1 PHE A 200 1.914 15.969 -75.224 1.00155.10 C
ANISOU 1677 CE1 PHE A 200 18786 23143 17001 1678 515 1079 C
ATOM 1678 CE2 PHE A 200 -0.476 15.997 -75.039 1.00155.61 C
ANISOU 1678 CE2 PHE A 200 18659 23584 16880 1785 456 1153 C
ATOM 1679 CZ PHE A 200 0.670 15.587 -75.700 1.00154.69 C
ANISOU 1679 CZ PHE A 200 18594 23379 16800 1698 462 1086 C
ATOM 1680 N PRO A 201 1.014 18.832 -68.981 1.00161.97 N
ANISOU 1680 N PRO A 201 19962 23243 18335 1873 671 1247 N
ATOM 1681 CA PRO A 201 -0.448 18.856 -68.969 1.00169.02 C
ANISOU 1681 CA PRO A 201 20743 24356 19117 1952 641 1301 C
ATOM 1682 C PRO A 201 -1.032 20.039 -69.753 1.00174.85 C
ANISOU 1682 C PRO A 201 21466 25216 19751 2152 712 1467 C
ATOM 1683 O PRO A 201 -1.452 19.866 -70.900 1.00180.13 O
ANISOU 1683 O PRO A 201 22045 26107 20287 2197 688 1501 O
ATOM 1684 CB PRO A 201 -0.784 18.977 -67.470 1.00167.75 C
ANISOU 1684 CB PRO A 201 20620 24064 19053 1930 644 1280 C
ATOM 1685 CG PRO A 201 0.472 19.469 -66.802 1.00163.66 C
ANISOU 1685 CG PRO A 201 20247 23254 18683 1896 706 1263 C
ATOM 1686 CD PRO A 201 1.560 19.581 -67.836 1.00161.78 C
ANISOU 1686 CD PRO A 201 20057 22966 18445 1887 737 1265 C
ATOM 1687 N ASP A 202 -1.046 21.222 -69.133 1.00174.41 N
ANISOU 1687 N ASP A 202 21498 25014 19754 2272 803 1569 N
ATOM 1688 CA ASP A 202 -1.629 22.436 -69.721 1.00175.55 C
ANISOU 1688 CA ASP A 202 21643 25245 19812 2479 886 1739 C
ATOM 1689 C ASP A 202 -3.102 22.252 -70.120 1.00184.28 C
ANISOU 1689 C ASP A 202 22596 26656 20763 2567 835 1794 C
ATOM 1690 O ASP A 202 -3.995 22.428 -69.287 1.00186.84 O
ANISOU 1690 O ASP A 202 22886 27013 21091 2611 832 1817 O
ATOM 1691 CB ASP A 202 -0.785 22.942 -70.904 1.00167.47 C
ANISOU 1691 CB ASP A 202 20676 24196 18756 2536 947 1802 C
ATOM 1692 CG ASP A 202 -1.149 24.358 -71.322 1.00162.74 C
ANISOU 1692 CG ASP A 202 20122 23607 18103 2754 1061 1987 C
ATOM 1693 OD1 ASP A 202 -1.445 25.190 -70.437 1.00158.58 O
ANISOU 1693 OD1 ASP A 202 19659 22954 17639 2838 1132 2051 O
ATOM 1694 OD2 ASP A 202 -1.129 24.642 -72.538 1.00159.89 O
ANISOU 1694 OD2 ASP A 202 19736 23377 17637 2843 1084 2068 O
ATOM 1695 N SER A 203 -3.333 21.877 -71.384 1.00189.34 N
ANISOU 1695 N SER A 203 23142 27528 21270 2585 795 1809 N
ATOM 1696 CA SER A 203 -4.685 21.691 -71.956 1.00190.30 C
ANISOU 1696 CA SER A 203 23103 27977 21224 2668 744 1861 C
ATOM 1697 C SER A 203 -5.653 22.834 -71.625 1.00190.76 C
ANISOU 1697 C SER A 203 23153 28087 21240 2874 813 2019 C
ATOM 1698 O SER A 203 -6.345 22.803 -70.601 1.00188.89 O
ANISOU 1698 O SER A 203 22892 27836 21040 2871 800 2002 O
ATOM 1699 CB SER A 203 -5.276 20.326 -71.569 1.00189.36 C
ANISOU 1699 CB SER A 203 22867 27998 21080 2501 628 1710 C
ATOM 1700 OG SER A 203 -5.265 20.133 -70.166 1.00187.78 O
ANISOU 1700 OG SER A 203 22721 27615 21009 2420 621 1641 O
ATOM 1701 N ALA A 204 -5.709 23.822 -72.521 1.00191.46 N
ANISOU 1701 N ALA A 204 23259 28241 21247 3056 890 2174 N
ATOM 1702 CA ALA A 204 -6.359 25.110 -72.253 1.00191.37 C
ANISOU 1702 CA ALA A 204 23280 28212 21217 3273 989 2344 C
ATOM 1703 C ALA A 204 -5.746 25.765 -71.012 1.00191.21 C
ANISOU 1703 C ALA A 204 23420 27855 21376 3259 1074 2338 C
ATOM 1704 O ALA A 204 -4.779 26.522 -71.120 1.00194.19 O
ANISOU 1704 O ALA A 204 23938 28012 21833 3295 1171 2386 O
ATOM 1705 CB ALA A 204 -7.871 24.949 -72.110 1.00189.30 C
ANISOU 1705 CB ALA A 204 22860 28227 20835 3354 936 2383 C
ATOM 1706 N ARG A 205 -6.303 25.454 -69.842 1.00186.54 N
ANISOU 1706 N ARG A 205 22803 27228 20844 3200 1038 2273 N
ATOM 1707 CA ARG A 205 -5.727 25.861 -68.560 1.00178.80 C
ANISOU 1707 CA ARG A 205 21960 25943 20033 3148 1099 2235 C
ATOM 1708 C ARG A 205 -6.007 24.809 -67.492 1.00172.82 C
ANISOU 1708 C ARG A 205 21150 25177 19335 2976 1001 2084 C
ATOM 1709 O ARG A 205 -7.039 24.137 -67.530 1.00170.90 O
ANISOU 1709 O ARG A 205 20765 25169 18997 2959 917 2054 O
ATOM 1710 CB ARG A 205 -6.276 27.224 -68.125 1.00179.77 C
ANISOU 1710 CB ARG A 205 22144 25991 20168 3350 1222 2390 C
ATOM 1711 CG ARG A 205 -5.446 28.407 -68.598 1.00181.20 C
ANISOU 1711 CG ARG A 205 22471 25985 20389 3467 1361 2504 C
ATOM 1712 CD ARG A 205 -6.299 29.651 -68.776 1.00183.44 C
ANISOU 1712 CD ARG A 205 22763 26327 20606 3717 1472 2695 C
ATOM 1713 NE ARG A 205 -5.584 30.702 -69.502 1.00184.70 N
ANISOU 1713 NE ARG A 205 23047 26356 20774 3838 1603 2815 N
ATOM 1714 CZ ARG A 205 -6.163 31.773 -70.043 1.00185.30 C
ANISOU 1714 CZ ARG A 205 23136 26499 20770 4071 1707 3000 C
ATOM 1715 NH1 ARG A 205 -7.478 31.946 -69.953 1.00185.79 N
ANISOU 1715 NH1 ARG A 205 23086 26768 20735 4213 1692 3088 N
ATOM 1716 NH2 ARG A 205 -5.425 32.671 -70.682 1.00183.39 N
ANISOU 1716 NH2 ARG A 205 23017 26118 20542 4164 1831 3100 N
ATOM 1717 N LYS A 206 -5.081 24.666 -66.548 1.00168.57 N
ANISOU 1717 N LYS A 206 20725 24372 18949 2846 1014 1988 N
ATOM 1718 CA LYS A 206 -5.247 23.720 -65.446 1.00165.68 C
ANISOU 1718 CA LYS A 206 20330 23968 18652 2684 932 1850 C
ATOM 1719 C LYS A 206 -6.267 24.184 -64.388 1.00168.05 C
ANISOU 1719 C LYS A 206 20611 24272 18966 2760 958 1894 C
ATOM 1720 O LYS A 206 -6.943 23.348 -63.785 1.00169.71 O
ANISOU 1720 O LYS A 206 20736 24581 19164 2668 876 1810 O
ATOM 1721 CB LYS A 206 -3.900 23.384 -64.797 1.00161.61 C
ANISOU 1721 CB LYS A 206 19935 23181 18287 2523 934 1736 C
ATOM 1722 CG LYS A 206 -3.914 22.089 -64.001 1.00159.79 C
ANISOU 1722 CG LYS A 206 19658 22948 18104 2333 828 1579 C
ATOM 1723 CD LYS A 206 -2.588 21.838 -63.308 1.00158.27 C
ANISOU 1723 CD LYS A 206 19584 22491 18058 2193 835 1480 C
ATOM 1724 CE LYS A 206 -2.654 20.585 -62.451 1.00156.27 C
ANISOU 1724 CE LYS A 206 19291 22231 17853 2020 737 1337 C
ATOM 1725 NZ LYS A 206 -1.349 20.290 -61.799 1.00154.89 N
ANISOU 1725 NZ LYS A 206 19220 21816 17812 1889 739 1243 N
ATOM 1726 N PRO A 207 -6.377 25.516 -64.155 1.00170.59 N
ANISOU 1726 N PRO A 207 21018 24483 19316 2925 1080 2024 N
ATOM 1727 CA PRO A 207 -7.421 26.038 -63.254 1.00166.67 C
ANISOU 1727 CA PRO A 207 20498 24008 18820 3019 1115 2080 C
ATOM 1728 C PRO A 207 -8.840 25.864 -63.801 1.00161.45 C
ANISOU 1728 C PRO A 207 19671 23670 18003 3129 1065 2147 C
ATOM 1729 O PRO A 207 -9.799 25.842 -63.026 1.00156.43 O
ANISOU 1729 O PRO A 207 18975 23103 17356 3154 1050 2147 O
ATOM 1730 CB PRO A 207 -7.080 27.532 -63.143 1.00170.30 C
ANISOU 1730 CB PRO A 207 21095 24274 19337 3178 1271 2211 C
ATOM 1731 CG PRO A 207 -6.241 27.829 -64.341 1.00173.25 C
ANISOU 1731 CG PRO A 207 21517 24629 19679 3218 1311 2262 C
ATOM 1732 CD PRO A 207 -5.443 26.582 -64.565 1.00172.65 C
ANISOU 1732 CD PRO A 207 21416 24556 19628 3012 1200 2110 C
ATOM 1733 N PHE A 208 -8.962 25.757 -65.125 1.00159.01 N
ANISOU 1733 N PHE A 208 19285 23562 17569 3194 1041 2202 N
ATOM 1734 CA PHE A 208 -10.243 25.471 -65.774 1.00153.92 C
ANISOU 1734 CA PHE A 208 18466 23257 16759 3282 980 2252 C
ATOM 1735 C PHE A 208 -10.780 24.116 -65.330 1.00148.42 C
ANISOU 1735 C PHE A 208 17649 22703 16040 3103 851 2100 C
ATOM 1736 O PHE A 208 -11.973 23.975 -65.063 1.00146.92 O
ANISOU 1736 O PHE A 208 17340 22709 15773 3149 817 2115 O
ATOM 1737 CB PHE A 208 -10.098 25.516 -67.302 1.00156.42 C
ANISOU 1737 CB PHE A 208 18728 23754 16948 3358 973 2323 C
ATOM 1738 CG PHE A 208 -11.327 25.062 -68.047 1.00155.87 C
ANISOU 1738 CG PHE A 208 18465 24060 16698 3418 896 2352 C
ATOM 1739 CD1 PHE A 208 -12.454 25.876 -68.122 1.00158.52 C
ANISOU 1739 CD1 PHE A 208 18727 24562 16938 3629 943 2498 C
ATOM 1740 CD2 PHE A 208 -11.354 23.825 -68.683 1.00153.90 C
ANISOU 1740 CD2 PHE A 208 18101 24002 16369 3265 781 2231 C
ATOM 1741 CE1 PHE A 208 -13.586 25.462 -68.810 1.00159.26 C
ANISOU 1741 CE1 PHE A 208 18631 25020 16858 3684 870 2523 C
ATOM 1742 CE2 PHE A 208 -12.482 23.406 -69.372 1.00156.05 C
ANISOU 1742 CE2 PHE A 208 18189 24632 16468 3310 712 2249 C
ATOM 1743 CZ PHE A 208 -13.600 24.225 -69.436 1.00158.32 C
ANISOU 1743 CZ PHE A 208 18398 25096 16658 3519 753 2395 C
ATOM 1744 N PHE A 209 -9.889 23.128 -65.252 1.00141.35 N
ANISOU 1744 N PHE A 209 16788 21705 15212 2900 786 1954 N
ATOM 1745 CA PHE A 209 -10.242 21.794 -64.770 1.00136.33 C
ANISOU 1745 CA PHE A 209 16064 21159 14575 2712 676 1798 C
ATOM 1746 C PHE A 209 -10.579 21.788 -63.278 1.00133.97 C
ANISOU 1746 C PHE A 209 15802 20722 14376 2662 682 1752 C
ATOM 1747 O PHE A 209 -11.552 21.157 -62.865 1.00133.93 O
ANISOU 1747 O PHE A 209 15686 20878 14320 2612 619 1697 O
ATOM 1748 CB PHE A 209 -9.115 20.792 -65.054 1.00131.99 C
ANISOU 1748 CB PHE A 209 15558 20508 14082 2519 619 1663 C
ATOM 1749 CG PHE A 209 -9.067 20.309 -66.480 1.00131.09 C
ANISOU 1749 CG PHE A 209 15356 20606 13843 2511 573 1658 C
ATOM 1750 CD1 PHE A 209 -10.211 19.828 -67.111 1.00131.21 C
ANISOU 1750 CD1 PHE A 209 15202 20950 13702 2532 511 1659 C
ATOM 1751 CD2 PHE A 209 -7.867 20.302 -67.183 1.00130.66 C
ANISOU 1751 CD2 PHE A 209 15384 20431 13826 2471 593 1644 C
ATOM 1752 CE1 PHE A 209 -10.163 19.374 -68.421 1.00128.99 C
ANISOU 1752 CE1 PHE A 209 14837 20873 13301 2516 469 1648 C
ATOM 1753 CE2 PHE A 209 -7.815 19.847 -68.492 1.00129.06 C
ANISOU 1753 CE2 PHE A 209 15102 20425 13508 2458 553 1635 C
ATOM 1754 CZ PHE A 209 -8.963 19.382 -69.111 1.00127.10 C
ANISOU 1754 CZ PHE A 209 14686 20504 13101 2479 491 1636 C
ATOM 1755 N LYS A 210 -9.777 22.494 -62.480 1.00131.46 N
ANISOU 1755 N LYS A 210 15637 20112 14196 2672 760 1770 N
ATOM 1756 CA LYS A 210 -9.936 22.493 -61.020 1.00128.81 C
ANISOU 1756 CA LYS A 210 15352 19621 13967 2611 770 1717 C
ATOM 1757 C LYS A 210 -11.250 23.134 -60.569 1.00130.62 C
ANISOU 1757 C LYS A 210 15512 19976 14139 2755 805 1808 C
ATOM 1758 O LYS A 210 -11.859 22.690 -59.593 1.00127.33 O
ANISOU 1758 O LYS A 210 15057 19573 13747 2684 767 1742 O
ATOM 1759 CB LYS A 210 -8.738 23.156 -60.327 1.00125.03 C
ANISOU 1759 CB LYS A 210 15051 18813 13640 2588 851 1714 C
ATOM 1760 CG LYS A 210 -8.641 22.851 -58.837 1.00121.13 C
ANISOU 1760 CG LYS A 210 14611 18150 13262 2470 839 1621 C
ATOM 1761 CD LYS A 210 -7.199 22.824 -58.358 1.00117.62 C
ANISOU 1761 CD LYS A 210 14308 17427 12953 2355 863 1549 C
ATOM 1762 CE LYS A 210 -7.114 22.374 -56.909 1.00114.51 C
ANISOU 1762 CE LYS A 210 13955 16894 12660 2225 836 1450 C
ATOM 1763 NZ LYS A 210 -5.743 21.916 -56.554 1.00110.40 N
ANISOU 1763 NZ LYS A 210 13531 16165 12249 2077 819 1350 N
ATOM 1764 N LEU A 211 -11.681 24.174 -61.280 1.00135.04 N
ANISOU 1764 N LEU A 211 16057 20628 14622 2962 879 1962 N
ATOM 1765 CA LEU A 211 -12.985 24.788 -61.019 1.00138.09 C
ANISOU 1765 CA LEU A 211 16362 21169 14936 3122 913 2062 C
ATOM 1766 C LEU A 211 -14.094 24.209 -61.911 1.00137.31 C
ANISOU 1766 C LEU A 211 16069 21438 14663 3161 831 2076 C
ATOM 1767 O LEU A 211 -15.240 24.666 -61.870 1.00140.70 O
ANISOU 1767 O LEU A 211 16405 22046 15009 3304 850 2164 O
ATOM 1768 CB LEU A 211 -12.914 26.322 -61.129 1.00141.36 C
ANISOU 1768 CB LEU A 211 16875 21465 15371 3341 1055 2230 C
ATOM 1769 CG LEU A 211 -12.551 27.094 -59.847 1.00138.39 C
ANISOU 1769 CG LEU A 211 16644 20794 15142 3347 1152 2234 C
ATOM 1770 CD1 LEU A 211 -11.045 27.278 -59.716 1.00134.41 C
ANISOU 1770 CD1 LEU A 211 16305 19997 14766 3250 1200 2185 C
ATOM 1771 CD2 LEU A 211 -13.260 28.442 -59.803 1.00137.17 C
ANISOU 1771 CD2 LEU A 211 16513 20644 14961 3586 1277 2402 C
ATOM 1772 N LEU A 212 -13.744 23.199 -62.707 1.00131.42 N
ANISOU 1772 N LEU A 212 15262 20809 13862 3031 742 1985 N
ATOM 1773 CA LEU A 212 -14.732 22.404 -63.434 1.00125.72 C
ANISOU 1773 CA LEU A 212 14351 20433 12981 3011 651 1955 C
ATOM 1774 C LEU A 212 -15.160 21.223 -62.569 1.00121.97 C
ANISOU 1774 C LEU A 212 13813 19997 12533 2815 562 1796 C
ATOM 1775 O LEU A 212 -16.350 20.936 -62.438 1.00119.58 O
ANISOU 1775 O LEU A 212 13370 19926 12137 2832 522 1789 O
ATOM 1776 CB LEU A 212 -14.156 21.914 -64.770 1.00122.86 C
ANISOU 1776 CB LEU A 212 13955 20183 12540 2966 607 1933 C
ATOM 1777 CG LEU A 212 -15.087 21.510 -65.924 1.00121.96 C
ANISOU 1777 CG LEU A 212 13654 20453 12232 3013 544 1956 C
ATOM 1778 CD1 LEU A 212 -15.521 20.056 -65.820 1.00119.80 C
ANISOU 1778 CD1 LEU A 212 13261 20343 11914 2803 432 1785 C
ATOM 1779 CD2 LEU A 212 -16.291 22.439 -66.044 1.00124.52 C
ANISOU 1779 CD2 LEU A 212 13883 20979 12447 3241 589 2111 C
ATOM 1780 N THR A 213 -14.179 20.548 -61.972 1.00121.92 N
ANISOU 1780 N THR A 213 13909 19760 12653 2630 537 1671 N
ATOM 1781 CA THR A 213 -14.449 19.468 -61.022 1.00122.24 C
ANISOU 1781 CA THR A 213 13919 19785 12741 2443 467 1524 C
ATOM 1782 C THR A 213 -15.081 19.997 -59.736 1.00120.39 C
ANISOU 1782 C THR A 213 13710 19463 12568 2495 509 1553 C
ATOM 1783 O THR A 213 -15.860 19.298 -59.086 1.00121.41 O
ANISOU 1783 O THR A 213 13759 19690 12679 2402 457 1472 O
ATOM 1784 CB THR A 213 -13.181 18.636 -60.694 1.00121.15 C
ANISOU 1784 CB THR A 213 13891 19413 12724 2245 435 1393 C
ATOM 1785 OG1 THR A 213 -13.482 17.687 -59.663 1.00121.01 O
ANISOU 1785 OG1 THR A 213 13857 19364 12758 2082 381 1267 O
ATOM 1786 CG2 THR A 213 -12.036 19.524 -60.225 1.00120.92 C
ANISOU 1786 CG2 THR A 213 14039 19069 12834 2292 518 1444 C
ATOM 1787 N SER A 214 -14.747 21.237 -59.383 1.00119.97 N
ANISOU 1787 N SER A 214 13769 19225 12586 2639 609 1666 N
ATOM 1788 CA SER A 214 -15.336 21.900 -58.224 1.00120.29 C
ANISOU 1788 CA SER A 214 13841 19178 12683 2711 665 1707 C
ATOM 1789 C SER A 214 -16.830 22.126 -58.434 1.00120.54 C
ANISOU 1789 C SER A 214 13715 19503 12582 2842 657 1780 C
ATOM 1790 O SER A 214 -17.614 22.084 -57.484 1.00119.17 O
ANISOU 1790 O SER A 214 13504 19351 12422 2832 655 1758 O
ATOM 1791 CB SER A 214 -14.633 23.229 -57.950 1.00120.99 C
ANISOU 1791 CB SER A 214 14086 19015 12868 2843 786 1816 C
ATOM 1792 OG SER A 214 -14.864 23.663 -56.622 1.00121.22 O
ANISOU 1792 OG SER A 214 14180 18885 12990 2847 836 1811 O
ATOM 1793 N LYS A 215 -17.217 22.357 -59.687 1.00119.94 N
ANISOU 1793 N LYS A 215 13542 19658 12371 2965 652 1867 N
ATOM 1794 CA LYS A 215 -18.625 22.461 -60.052 1.00122.74 C
ANISOU 1794 CA LYS A 215 13722 20335 12576 3085 632 1932 C
ATOM 1795 C LYS A 215 -19.341 21.113 -59.950 1.00121.03 C
ANISOU 1795 C LYS A 215 13359 20336 12288 2907 519 1787 C
ATOM 1796 O LYS A 215 -20.551 21.065 -59.713 1.00122.42 O
ANISOU 1796 O LYS A 215 13404 20728 12379 2955 500 1800 O
ATOM 1797 CB LYS A 215 -18.781 23.045 -61.459 1.00125.43 C
ANISOU 1797 CB LYS A 215 13998 20874 12786 3261 654 2064 C
ATOM 1798 CG LYS A 215 -18.816 24.565 -61.499 1.00127.65 C
ANISOU 1798 CG LYS A 215 14360 21056 13084 3511 780 2250 C
ATOM 1799 CD LYS A 215 -19.341 25.075 -62.833 1.00130.48 C
ANISOU 1799 CD LYS A 215 14611 21685 13279 3706 794 2391 C
ATOM 1800 CE LYS A 215 -19.822 26.515 -62.723 1.00129.45 C
ANISOU 1800 CE LYS A 215 14519 21522 13141 3973 917 2581 C
ATOM 1801 NZ LYS A 215 -20.384 27.019 -64.006 1.00131.59 N
ANISOU 1801 NZ LYS A 215 14681 22071 13245 4178 931 2730 N
ATOM 1802 N ILE A 216 -18.587 20.025 -60.115 1.00114.34 N
ANISOU 1802 N ILE A 216 12538 19427 11476 2701 451 1649 N
ATOM 1803 CA ILE A 216 -19.145 18.672 -60.033 1.00109.99 C
ANISOU 1803 CA ILE A 216 11867 19054 10867 2511 354 1499 C
ATOM 1804 C ILE A 216 -19.348 18.199 -58.587 1.00109.53 C
ANISOU 1804 C ILE A 216 11851 18851 10913 2380 343 1400 C
ATOM 1805 O ILE A 216 -20.399 17.646 -58.258 1.00111.26 O
ANISOU 1805 O ILE A 216 11946 19264 11064 2326 300 1343 O
ATOM 1806 CB ILE A 216 -18.303 17.653 -60.831 1.00105.86 C
ANISOU 1806 CB ILE A 216 11353 18531 10336 2345 293 1389 C
ATOM 1807 CG1 ILE A 216 -18.382 17.968 -62.327 1.00107.35 C
ANISOU 1807 CG1 ILE A 216 11458 18942 10386 2462 290 1474 C
ATOM 1808 CG2 ILE A 216 -18.781 16.230 -60.570 1.00103.92 C
ANISOU 1808 CG2 ILE A 216 11014 18412 10058 2128 208 1221 C
ATOM 1809 CD1 ILE A 216 -17.246 17.391 -63.144 1.00107.63 C
ANISOU 1809 CD1 ILE A 216 11553 18897 10442 2351 263 1409 C
ATOM 1810 N TYR A 217 -18.355 18.429 -57.726 1.00106.94 N
ANISOU 1810 N TYR A 217 11692 18194 10743 2331 383 1381 N
ATOM 1811 CA TYR A 217 -18.462 18.037 -56.315 1.00105.66 C
ANISOU 1811 CA TYR A 217 11583 17879 10683 2212 377 1295 C
ATOM 1812 C TYR A 217 -19.655 18.685 -55.618 1.00108.83 C
ANISOU 1812 C TYR A 217 11918 18381 11052 2333 413 1363 C
ATOM 1813 O TYR A 217 -20.187 18.142 -54.647 1.00108.80 O
ANISOU 1813 O TYR A 217 11888 18375 11075 2229 387 1281 O
ATOM 1814 CB TYR A 217 -17.167 18.324 -55.557 1.00104.06 C
ANISOU 1814 CB TYR A 217 11571 17318 10646 2162 420 1279 C
ATOM 1815 CG TYR A 217 -16.132 17.234 -55.708 1.00102.64 C
ANISOU 1815 CG TYR A 217 11449 17024 10525 1967 363 1153 C
ATOM 1816 CD1 TYR A 217 -16.273 16.014 -55.046 1.00103.21 C
ANISOU 1816 CD1 TYR A 217 11500 17092 10623 1773 299 1013 C
ATOM 1817 CD2 TYR A 217 -15.013 17.416 -56.518 1.00103.98 C
ANISOU 1817 CD2 TYR A 217 11697 17088 10722 1980 377 1176 C
ATOM 1818 CE1 TYR A 217 -15.329 15.007 -55.187 1.00101.73 C
ANISOU 1818 CE1 TYR A 217 11367 16796 10489 1604 253 903 C
ATOM 1819 CE2 TYR A 217 -14.061 16.415 -56.664 1.00101.64 C
ANISOU 1819 CE2 TYR A 217 11451 16688 10478 1808 328 1062 C
ATOM 1820 CZ TYR A 217 -14.225 15.214 -55.999 1.00 99.33 C
ANISOU 1820 CZ TYR A 217 11136 16391 10212 1625 267 928 C
ATOM 1821 OH TYR A 217 -13.286 14.220 -56.143 1.00 97.38 O
ANISOU 1821 OH TYR A 217 10941 16038 10018 1464 225 821 O
ATOM 1822 N LYS A 218 -20.069 19.846 -56.123 1.00113.22 N
ANISOU 1822 N LYS A 218 12447 19023 11548 2556 478 1515 N
ATOM 1823 CA LYS A 218 -21.345 20.440 -55.748 1.00114.84 C
ANISOU 1823 CA LYS A 218 12554 19393 11688 2695 509 1592 C
ATOM 1824 C LYS A 218 -22.466 19.465 -56.080 1.00115.33 C
ANISOU 1824 C LYS A 218 12421 19786 11613 2613 423 1514 C
ATOM 1825 O LYS A 218 -23.136 18.958 -55.182 1.00116.79 O
ANISOU 1825 O LYS A 218 12559 20005 11809 2519 397 1434 O
ATOM 1826 CB LYS A 218 -21.574 21.759 -56.491 1.00118.73 C
ANISOU 1826 CB LYS A 218 13037 19954 12118 2957 590 1776 C
ATOM 1827 CG LYS A 218 -20.639 22.890 -56.098 1.00122.15 C
ANISOU 1827 CG LYS A 218 13659 20069 12681 3059 698 1866 C
ATOM 1828 CD LYS A 218 -20.980 24.161 -56.862 1.00124.47 C
ANISOU 1828 CD LYS A 218 13938 20448 12904 3325 785 2052 C
ATOM 1829 CE LYS A 218 -19.912 25.226 -56.678 1.00123.65 C
ANISOU 1829 CE LYS A 218 14030 20027 12924 3410 898 2133 C
ATOM 1830 NZ LYS A 218 -20.249 26.469 -57.422 1.00125.50 N
ANISOU 1830 NZ LYS A 218 14260 20333 13090 3674 994 2320 N
ATOM 1831 N VAL A 219 -22.633 19.182 -57.375 1.00115.18 N
ANISOU 1831 N VAL A 219 12292 20008 11463 2639 380 1529 N
ATOM 1832 CA VAL A 219 -23.711 18.312 -57.877 1.00115.61 C
ANISOU 1832 CA VAL A 219 12145 20413 11365 2568 302 1457 C
ATOM 1833 C VAL A 219 -23.798 17.000 -57.098 1.00115.32 C
ANISOU 1833 C VAL A 219 12098 20343 11374 2315 238 1275 C
ATOM 1834 O VAL A 219 -24.893 16.488 -56.849 1.00115.50 O
ANISOU 1834 O VAL A 219 11982 20587 11315 2261 201 1216 O
ATOM 1835 CB VAL A 219 -23.544 17.994 -59.386 1.00113.61 C
ANISOU 1835 CB VAL A 219 11805 20376 10986 2577 258 1465 C
ATOM 1836 CG1 VAL A 219 -24.751 17.231 -59.915 1.00112.43 C
ANISOU 1836 CG1 VAL A 219 11436 20616 10665 2521 187 1401 C
ATOM 1837 CG2 VAL A 219 -23.331 19.269 -60.189 1.00115.28 C
ANISOU 1837 CG2 VAL A 219 12045 20597 11158 2824 326 1650 C
ATOM 1838 N LEU A 220 -22.639 16.472 -56.711 1.00114.52 N
ANISOU 1838 N LEU A 220 12144 19964 11401 2162 229 1188 N
ATOM 1839 CA LEU A 220 -22.564 15.227 -55.957 1.00113.71 C
ANISOU 1839 CA LEU A 220 12057 19789 11356 1924 178 1022 C
ATOM 1840 C LEU A 220 -23.327 15.333 -54.639 1.00114.51 C
ANISOU 1840 C LEU A 220 12154 19851 11503 1913 197 1006 C
ATOM 1841 O LEU A 220 -24.081 14.430 -54.280 1.00113.76 O
ANISOU 1841 O LEU A 220 11965 19894 11362 1777 153 898 O
ATOM 1842 CB LEU A 220 -21.105 14.850 -55.692 1.00111.89 C
ANISOU 1842 CB LEU A 220 12002 19241 11267 1802 179 961 C
ATOM 1843 CG LEU A 220 -20.678 13.398 -55.934 1.00111.79 C
ANISOU 1843 CG LEU A 220 11983 19231 11257 1570 113 801 C
ATOM 1844 CD1 LEU A 220 -19.243 13.199 -55.468 1.00110.07 C
ANISOU 1844 CD1 LEU A 220 11950 18676 11196 1480 125 760 C
ATOM 1845 CD2 LEU A 220 -21.602 12.400 -55.249 1.00111.85 C
ANISOU 1845 CD2 LEU A 220 11904 19359 11235 1414 73 680 C
ATOM 1846 N GLU A 221 -23.138 16.445 -53.931 1.00117.38 N
ANISOU 1846 N GLU A 221 12618 20026 11953 2054 269 1110 N
ATOM 1847 CA GLU A 221 -23.841 16.682 -52.666 1.00120.33 C
ANISOU 1847 CA GLU A 221 12994 20351 12372 2062 298 1106 C
ATOM 1848 C GLU A 221 -25.102 17.545 -52.828 1.00123.87 C
ANISOU 1848 C GLU A 221 13310 21039 12714 2261 332 1220 C
ATOM 1849 O GLU A 221 -25.570 18.159 -51.869 1.00127.66 O
ANISOU 1849 O GLU A 221 13815 21446 13242 2334 383 1263 O
ATOM 1850 CB GLU A 221 -22.891 17.261 -51.598 1.00121.36 C
ANISOU 1850 CB GLU A 221 13319 20118 12672 2065 357 1127 C
ATOM 1851 CG GLU A 221 -22.002 18.411 -52.064 1.00120.98 C
ANISOU 1851 CG GLU A 221 13386 19904 12675 2227 427 1252 C
ATOM 1852 CD GLU A 221 -22.590 19.779 -51.766 1.00121.00 C
ANISOU 1852 CD GLU A 221 13393 19906 12675 2449 517 1395 C
ATOM 1853 OE1 GLU A 221 -22.927 20.045 -50.593 1.00117.57 O
ANISOU 1853 OE1 GLU A 221 12998 19364 12307 2444 553 1386 O
ATOM 1854 OE2 GLU A 221 -22.695 20.600 -52.702 1.00122.10 O
ANISOU 1854 OE2 GLU A 221 13500 20145 12746 2631 557 1520 O
ATOM 1855 N GLU A 222 -25.653 17.567 -54.042 1.00126.45 N
ANISOU 1855 N GLU A 222 13493 21658 12893 2346 305 1267 N
ATOM 1856 CA GLU A 222 -26.894 18.292 -54.324 1.00126.22 C
ANISOU 1856 CA GLU A 222 13314 21900 12742 2538 329 1374 C
ATOM 1857 C GLU A 222 -28.053 17.327 -54.550 1.00125.69 C
ANISOU 1857 C GLU A 222 13046 22172 12537 2431 256 1275 C
ATOM 1858 O GLU A 222 -28.949 17.212 -53.711 1.00125.36 O
ANISOU 1858 O GLU A 222 12940 22204 12488 2407 258 1241 O
ATOM 1859 CB GLU A 222 -26.733 19.201 -55.551 1.00131.12 C
ANISOU 1859 CB GLU A 222 13911 22626 13282 2750 363 1526 C
ATOM 1860 CG GLU A 222 -25.787 20.380 -55.363 1.00131.84 C
ANISOU 1860 CG GLU A 222 14186 22414 13493 2897 456 1648 C
ATOM 1861 CD GLU A 222 -26.331 21.445 -54.428 1.00134.23 C
ANISOU 1861 CD GLU A 222 14526 22625 13848 3058 544 1748 C
ATOM 1862 OE1 GLU A 222 -27.564 21.658 -54.407 1.00136.74 O
ANISOU 1862 OE1 GLU A 222 14695 23193 14063 3162 545 1794 O
ATOM 1863 OE2 GLU A 222 -25.517 22.078 -53.721 1.00131.37 O
ANISOU 1863 OE2 GLU A 222 14340 21944 13628 3080 615 1779 O
ATOM 1864 N LYS A 223 -28.029 16.637 -55.689 1.00125.04 N
ANISOU 1864 N LYS A 223 12866 22298 12345 2361 195 1225 N
ATOM 1865 CA LYS A 223 -29.103 15.718 -56.063 1.00126.07 C
ANISOU 1865 CA LYS A 223 12796 22776 12329 2253 129 1125 C
ATOM 1866 C LYS A 223 -28.898 14.322 -55.465 1.00124.33 C
ANISOU 1866 C LYS A 223 12605 22468 12164 1966 78 930 C
ATOM 1867 O LYS A 223 -29.700 13.413 -55.698 1.00126.82 O
ANISOU 1867 O LYS A 223 12771 23039 12372 1834 28 820 O
ATOM 1868 CB LYS A 223 -29.260 15.648 -57.592 1.00126.59 C
ANISOU 1868 CB LYS A 223 12729 23135 12234 2314 91 1160 C
ATOM 1869 CG LYS A 223 -29.545 16.987 -58.272 1.00125.80 C
ANISOU 1869 CG LYS A 223 12585 23154 12058 2608 141 1360 C
ATOM 1870 CD LYS A 223 -30.754 17.698 -57.671 1.00126.61 C
ANISOU 1870 CD LYS A 223 12585 23406 12112 2767 177 1445 C
ATOM 1871 CE LYS A 223 -30.882 19.121 -58.197 1.00125.99 C
ANISOU 1871 CE LYS A 223 12506 23372 11991 3073 247 1658 C
ATOM 1872 NZ LYS A 223 -31.790 19.957 -57.362 1.00122.66 N
ANISOU 1872 NZ LYS A 223 12048 22977 11578 3237 306 1750 N
ATOM 1873 N TYR A 224 -27.821 14.166 -54.696 1.00121.81 N
ANISOU 1873 N TYR A 224 12478 21789 12011 1870 98 890 N
ATOM 1874 CA TYR A 224 -27.567 12.947 -53.921 1.00118.33 C
ANISOU 1874 CA TYR A 224 12096 21216 11648 1617 65 723 C
ATOM 1875 C TYR A 224 -27.464 13.310 -52.441 1.00116.10 C
ANISOU 1875 C TYR A 224 11936 20672 11504 1617 109 733 C
ATOM 1876 O TYR A 224 -26.477 13.909 -52.008 1.00113.00 O
ANISOU 1876 O TYR A 224 11711 19984 11240 1671 150 792 O
ATOM 1877 CB TYR A 224 -26.285 12.243 -54.402 1.00115.01 C
ANISOU 1877 CB TYR A 224 11790 20612 11294 1480 40 650 C
ATOM 1878 CG TYR A 224 -26.263 11.966 -55.894 1.00115.21 C
ANISOU 1878 CG TYR A 224 11710 20873 11190 1487 3 646 C
ATOM 1879 CD1 TYR A 224 -25.747 12.903 -56.792 1.00113.42 C
ANISOU 1879 CD1 TYR A 224 11510 20645 10940 1669 26 780 C
ATOM 1880 CD2 TYR A 224 -26.777 10.776 -56.409 1.00115.70 C
ANISOU 1880 CD2 TYR A 224 11647 21164 11149 1309 -50 507 C
ATOM 1881 CE1 TYR A 224 -25.746 12.661 -58.158 1.00113.10 C
ANISOU 1881 CE1 TYR A 224 11370 20829 10773 1678 -7 778 C
ATOM 1882 CE2 TYR A 224 -26.776 10.524 -57.773 1.00113.29 C
ANISOU 1882 CE2 TYR A 224 11241 21085 10718 1310 -82 498 C
ATOM 1883 CZ TYR A 224 -26.261 11.467 -58.642 1.00113.21 C
ANISOU 1883 CZ TYR A 224 11255 21074 10684 1496 -64 636 C
ATOM 1884 OH TYR A 224 -26.259 11.215 -59.994 1.00110.08 O
ANISOU 1884 OH TYR A 224 10758 20909 10158 1496 -96 627 O
ATOM 1885 N LYS A 225 -28.498 12.959 -51.677 1.00119.49 N
ANISOU 1885 N LYS A 225 12277 21220 11901 1554 103 674 N
ATOM 1886 CA LYS A 225 -28.604 13.342 -50.261 1.00121.12 C
ANISOU 1886 CA LYS A 225 12575 21223 12218 1564 146 686 C
ATOM 1887 C LYS A 225 -27.617 12.599 -49.353 1.00120.69 C
ANISOU 1887 C LYS A 225 12691 20852 12310 1375 140 584 C
ATOM 1888 O LYS A 225 -27.851 12.457 -48.147 1.00118.30 O
ANISOU 1888 O LYS A 225 12438 20431 12079 1308 157 543 O
ATOM 1889 CB LYS A 225 -30.040 13.154 -49.752 1.00120.17 C
ANISOU 1889 CB LYS A 225 12302 21342 12012 1549 141 650 C
ATOM 1890 CG LYS A 225 -30.977 14.307 -50.072 1.00121.02 C
ANISOU 1890 CG LYS A 225 12290 21665 12027 1792 177 791 C
ATOM 1891 CD LYS A 225 -32.288 14.176 -49.312 1.00121.06 C
ANISOU 1891 CD LYS A 225 12169 21849 11976 1774 181 753 C
ATOM 1892 CE LYS A 225 -33.233 15.321 -49.637 1.00119.73 C
ANISOU 1892 CE LYS A 225 11876 21901 11713 2028 220 898 C
ATOM 1893 NZ LYS A 225 -34.552 15.148 -48.972 1.00116.71 N
ANISOU 1893 NZ LYS A 225 11354 21723 11265 2008 220 855 N
ATOM 1894 N THR A 226 -26.510 12.142 -49.939 1.00119.74 N
ANISOU 1894 N THR A 226 12659 20602 12234 1297 117 549 N
ATOM 1895 CA THR A 226 -25.466 11.447 -49.198 1.00117.28 C
ANISOU 1895 CA THR A 226 12508 19995 12057 1133 111 462 C
ATOM 1896 C THR A 226 -24.703 12.420 -48.301 1.00116.80 C
ANISOU 1896 C THR A 226 12610 19635 12133 1232 166 548 C
ATOM 1897 O THR A 226 -24.379 13.540 -48.714 1.00113.42 O
ANISOU 1897 O THR A 226 12216 19164 11714 1413 207 671 O
ATOM 1898 CB THR A 226 -24.469 10.749 -50.148 1.00117.47 C
ANISOU 1898 CB THR A 226 12576 19969 12086 1037 75 408 C
ATOM 1899 OG1 THR A 226 -25.157 10.270 -51.311 1.00117.13 O
ANISOU 1899 OG1 THR A 226 12369 20239 11893 1015 37 372 O
ATOM 1900 CG2 THR A 226 -23.768 9.579 -49.443 1.00116.14 C
ANISOU 1900 CG2 THR A 226 12517 19593 12016 819 54 278 C
ATOM 1901 N SER A 227 -24.439 11.989 -47.070 1.00116.79 N
ANISOU 1901 N SER A 227 12708 19434 12234 1111 171 480 N
ATOM 1902 CA SER A 227 -23.566 12.720 -46.155 1.00115.88 C
ANISOU 1902 CA SER A 227 12756 19017 12253 1163 218 534 C
ATOM 1903 C SER A 227 -22.311 11.888 -45.856 1.00113.40 C
ANISOU 1903 C SER A 227 12580 18463 12044 1002 193 450 C
ATOM 1904 O SER A 227 -21.269 12.072 -46.494 1.00113.31 O
ANISOU 1904 O SER A 227 12642 18338 12070 1030 193 479 O
ATOM 1905 CB SER A 227 -24.313 13.085 -44.865 1.00116.79 C
ANISOU 1905 CB SER A 227 12875 19098 12401 1180 254 541 C
ATOM 1906 OG SER A 227 -24.877 11.936 -44.254 1.00117.73 O
ANISOU 1906 OG SER A 227 12950 19278 12503 1000 217 420 O
ATOM 1907 N GLY A 228 -22.422 10.970 -44.897 1.00107.41 N
ANISOU 1907 N GLY A 228 11852 17630 11326 838 173 349 N
ATOM 1908 CA GLY A 228 -21.375 9.989 -44.634 1.00 99.17 C
ANISOU 1908 CA GLY A 228 10918 16394 10365 676 145 262 C
ATOM 1909 C GLY A 228 -20.156 10.509 -43.886 1.00 92.88 C
ANISOU 1909 C GLY A 228 10291 15297 9702 700 173 299 C
ATOM 1910 O GLY A 228 -19.421 11.373 -44.380 1.00 95.89 O
ANISOU 1910 O GLY A 228 10726 15592 10114 817 198 379 O
ATOM 1911 N SER A 229 -19.960 9.987 -42.680 1.00 81.18 N
ANISOU 1911 N SER A 229 8888 13661 8294 585 172 239 N
ATOM 1912 CA SER A 229 -18.665 10.048 -42.001 1.00 74.28 C
ANISOU 1912 CA SER A 229 8170 12509 7542 550 181 238 C
ATOM 1913 C SER A 229 -18.412 8.714 -41.311 1.00 65.60 C
ANISOU 1913 C SER A 229 7119 11322 6481 362 147 130 C
ATOM 1914 O SER A 229 -19.179 8.310 -40.436 1.00 64.66 O
ANISOU 1914 O SER A 229 6977 11238 6352 291 149 87 O
ATOM 1915 CB SER A 229 -18.624 11.185 -40.982 1.00 73.97 C
ANISOU 1915 CB SER A 229 8201 12338 7566 650 235 308 C
ATOM 1916 OG SER A 229 -17.479 11.065 -40.158 1.00 71.33 O
ANISOU 1916 OG SER A 229 8005 11755 7340 585 238 286 O
ATOM 1917 N LEU A 230 -17.350 8.028 -41.723 1.00 59.50 N
ANISOU 1917 N LEU A 230 6413 10438 5752 284 121 89 N
ATOM 1918 CA LEU A 230 -17.064 6.671 -41.252 1.00 57.35 C
ANISOU 1918 CA LEU A 230 6188 10090 5512 110 93 -10 C
ATOM 1919 C LEU A 230 -17.164 6.564 -39.734 1.00 54.84 C
ANISOU 1919 C LEU A 230 5940 9642 5255 54 108 -27 C
ATOM 1920 O LEU A 230 -17.770 5.631 -39.208 1.00 54.78 O
ANISOU 1920 O LEU A 230 5911 9676 5227 -65 98 -98 O
ATOM 1921 CB LEU A 230 -15.670 6.233 -41.702 1.00 55.90 C
ANISOU 1921 CB LEU A 230 6095 9748 5393 70 76 -28 C
ATOM 1922 CG LEU A 230 -15.481 4.804 -42.220 1.00 56.25 C
ANISOU 1922 CG LEU A 230 6132 9817 5421 -77 46 -125 C
ATOM 1923 CD1 LEU A 230 -14.016 4.412 -42.087 1.00 53.21 C
ANISOU 1923 CD1 LEU A 230 5872 9213 5133 -119 37 -138 C
ATOM 1924 CD2 LEU A 230 -16.386 3.787 -41.529 1.00 55.08 C
ANISOU 1924 CD2 LEU A 230 5952 9732 5243 -212 43 -207 C
ATOM 1925 N TYR A 231 -16.575 7.536 -39.043 1.00 53.09 N
ANISOU 1925 N TYR A 231 5801 9266 5103 140 135 37 N
ATOM 1926 CA TYR A 231 -16.556 7.554 -37.594 1.00 51.60 C
ANISOU 1926 CA TYR A 231 5685 8946 4972 96 150 27 C
ATOM 1927 C TYR A 231 -17.955 7.685 -37.001 1.00 53.38 C
ANISOU 1927 C TYR A 231 5829 9312 5140 97 168 22 C
ATOM 1928 O TYR A 231 -18.317 6.950 -36.079 1.00 54.59 O
ANISOU 1928 O TYR A 231 5999 9438 5301 -12 163 -34 O
ATOM 1929 CB TYR A 231 -15.645 8.677 -37.080 1.00 49.35 C
ANISOU 1929 CB TYR A 231 5498 8485 4766 191 182 96 C
ATOM 1930 CG TYR A 231 -15.575 8.734 -35.578 1.00 47.14 C
ANISOU 1930 CG TYR A 231 5293 8074 4542 144 198 84 C
ATOM 1931 CD1 TYR A 231 -14.644 7.961 -34.876 1.00 45.39 C
ANISOU 1931 CD1 TYR A 231 5168 7691 4385 39 175 40 C
ATOM 1932 CD2 TYR A 231 -16.452 9.536 -34.851 1.00 46.92 C
ANISOU 1932 CD2 TYR A 231 5237 8090 4499 207 237 118 C
ATOM 1933 CE1 TYR A 231 -14.578 7.999 -33.497 1.00 43.84 C
ANISOU 1933 CE1 TYR A 231 5038 7387 4233 -2 188 31 C
ATOM 1934 CE2 TYR A 231 -16.399 9.577 -33.466 1.00 47.13 C
ANISOU 1934 CE2 TYR A 231 5331 8002 4571 159 253 104 C
ATOM 1935 CZ TYR A 231 -15.455 8.804 -32.795 1.00 46.27 C
ANISOU 1935 CZ TYR A 231 5317 7740 4522 52 226 61 C
ATOM 1936 OH TYR A 231 -15.393 8.831 -31.420 1.00 47.46 O
ANISOU 1936 OH TYR A 231 5532 7786 4711 4 240 48 O
ATOM 1937 N THR A 232 -18.731 8.631 -37.524 1.00 55.38 N
ANISOU 1937 N THR A 232 5994 9712 5335 226 192 83 N
ATOM 1938 CA THR A 232 -20.097 8.857 -37.053 1.00 57.08 C
ANISOU 1938 CA THR A 232 6118 10080 5490 246 212 84 C
ATOM 1939 C THR A 232 -20.969 7.631 -37.304 1.00 56.13 C
ANISOU 1939 C THR A 232 5905 10128 5295 115 180 -4 C
ATOM 1940 O THR A 232 -21.698 7.196 -36.418 1.00 57.09 O
ANISOU 1940 O THR A 232 6009 10276 5404 35 187 -49 O
ATOM 1941 CB THR A 232 -20.735 10.086 -37.726 1.00 58.90 C
ANISOU 1941 CB THR A 232 6263 10451 5664 424 245 175 C
ATOM 1942 OG1 THR A 232 -19.843 11.202 -37.628 1.00 61.70 O
ANISOU 1942 OG1 THR A 232 6712 10641 6090 540 283 254 O
ATOM 1943 CG2 THR A 232 -22.045 10.442 -37.057 1.00 59.53 C
ANISOU 1943 CG2 THR A 232 6262 10658 5695 458 273 184 C
ATOM 1944 N CYS A 233 -20.874 7.068 -38.506 1.00 55.66 N
ANISOU 1944 N CYS A 233 5788 10176 5183 86 151 -34 N
ATOM 1945 CA CYS A 233 -21.658 5.885 -38.864 1.00 57.53 C
ANISOU 1945 CA CYS A 233 5935 10578 5344 -47 127 -128 C
ATOM 1946 C CYS A 233 -21.387 4.729 -37.902 1.00 55.81 C
ANISOU 1946 C CYS A 233 5803 10221 5181 -219 121 -213 C
ATOM 1947 O CYS A 233 -22.305 4.231 -37.254 1.00 55.96 O
ANISOU 1947 O CYS A 233 5779 10316 5166 -303 131 -265 O
ATOM 1948 CB CYS A 233 -21.372 5.448 -40.307 1.00 60.86 C
ANISOU 1948 CB CYS A 233 6302 11108 5714 -60 99 -152 C
ATOM 1949 SG CYS A 233 -21.956 6.571 -41.603 1.00 63.40 S
ANISOU 1949 SG CYS A 233 6490 11661 5936 123 102 -63 S
ATOM 1950 N TRP A 234 -20.118 4.333 -37.789 1.00 53.96 N
ANISOU 1950 N TRP A 234 5691 9780 5029 -263 110 -222 N
ATOM 1951 CA TRP A 234 -19.728 3.211 -36.935 1.00 51.77 C
ANISOU 1951 CA TRP A 234 5505 9357 4805 -414 107 -292 C
ATOM 1952 C TRP A 234 -20.113 3.433 -35.505 1.00 51.62 C
ANISOU 1952 C TRP A 234 5530 9263 4820 -428 128 -282 C
ATOM 1953 O TRP A 234 -20.533 2.505 -34.809 1.00 52.54 O
ANISOU 1953 O TRP A 234 5662 9368 4932 -557 134 -348 O
ATOM 1954 CB TRP A 234 -18.229 2.955 -37.033 1.00 49.36 C
ANISOU 1954 CB TRP A 234 5323 8844 4587 -426 92 -283 C
ATOM 1955 CG TRP A 234 -17.781 1.740 -36.247 1.00 46.84 C
ANISOU 1955 CG TRP A 234 5098 8379 4319 -571 91 -349 C
ATOM 1956 CD1 TRP A 234 -17.087 1.716 -35.035 1.00 44.16 C
ANISOU 1956 CD1 TRP A 234 4875 7842 4060 -590 96 -331 C
ATOM 1957 CD2 TRP A 234 -17.994 0.331 -36.600 1.00 46.63 C
ANISOU 1957 CD2 TRP A 234 5060 8391 4264 -721 90 -443 C
ATOM 1958 NE1 TRP A 234 -16.856 0.420 -34.632 1.00 43.86 N
ANISOU 1958 NE1 TRP A 234 4899 7719 4045 -727 97 -397 N
ATOM 1959 CE2 TRP A 234 -17.377 -0.459 -35.536 1.00 46.10 C
ANISOU 1959 CE2 TRP A 234 5115 8130 4269 -813 97 -468 C
ATOM 1960 CE3 TRP A 234 -18.615 -0.331 -37.663 1.00 47.29 C
ANISOU 1960 CE3 TRP A 234 5049 8648 4270 -788 88 -510 C
ATOM 1961 CZ2 TRP A 234 -17.396 -1.850 -35.547 1.00 46.21 C
ANISOU 1961 CZ2 TRP A 234 5160 8114 4282 -960 109 -551 C
ATOM 1962 CZ3 TRP A 234 -18.623 -1.732 -37.665 1.00 47.25 C
ANISOU 1962 CZ3 TRP A 234 5075 8612 4264 -948 100 -603 C
ATOM 1963 CH2 TRP A 234 -18.022 -2.473 -36.632 1.00 46.16 C
ANISOU 1963 CH2 TRP A 234 5063 8273 4202 -1029 114 -621 C
ATOM 1964 N SER A 235 -19.979 4.672 -35.053 1.00 51.37 N
ANISOU 1964 N SER A 235 5520 9176 4819 -299 146 -201 N
ATOM 1965 CA SER A 235 -20.261 5.005 -33.672 1.00 52.68 C
ANISOU 1965 CA SER A 235 5734 9260 5019 -304 171 -188 C
ATOM 1966 C SER A 235 -21.753 4.889 -33.381 1.00 55.39 C
ANISOU 1966 C SER A 235 5969 9790 5285 -334 187 -219 C
ATOM 1967 O SER A 235 -22.162 4.196 -32.436 1.00 54.36 O
ANISOU 1967 O SER A 235 5862 9631 5159 -445 195 -271 O
ATOM 1968 CB SER A 235 -19.747 6.407 -33.347 1.00 51.66 C
ANISOU 1968 CB SER A 235 5654 9031 4940 -158 195 -98 C
ATOM 1969 OG SER A 235 -19.949 6.705 -31.988 1.00 51.94 O
ANISOU 1969 OG SER A 235 5742 8980 5012 -172 220 -92 O
ATOM 1970 N GLU A 236 -22.565 5.557 -34.198 1.00 57.24 N
ANISOU 1970 N GLU A 236 6081 10220 5446 -233 193 -186 N
ATOM 1971 CA GLU A 236 -24.016 5.502 -34.036 1.00 59.40 C
ANISOU 1971 CA GLU A 236 6233 10699 5637 -250 208 -214 C
ATOM 1972 C GLU A 236 -24.540 4.076 -34.204 1.00 57.60 C
ANISOU 1972 C GLU A 236 5959 10566 5358 -425 192 -322 C
ATOM 1973 O GLU A 236 -25.395 3.643 -33.436 1.00 58.08 O
ANISOU 1973 O GLU A 236 5990 10682 5392 -510 209 -372 O
ATOM 1974 CB GLU A 236 -24.717 6.479 -34.989 1.00 63.97 C
ANISOU 1974 CB GLU A 236 6683 11480 6140 -97 215 -151 C
ATOM 1975 CG GLU A 236 -24.829 7.899 -34.431 1.00 68.50 C
ANISOU 1975 CG GLU A 236 7276 12006 6745 64 256 -55 C
ATOM 1976 CD GLU A 236 -25.075 8.961 -35.500 1.00 72.12 C
ANISOU 1976 CD GLU A 236 7649 12599 7152 242 268 31 C
ATOM 1977 OE1 GLU A 236 -24.735 10.139 -35.249 1.00 73.51 O
ANISOU 1977 OE1 GLU A 236 7878 12676 7375 381 306 117 O
ATOM 1978 OE2 GLU A 236 -25.614 8.630 -36.582 1.00 73.61 O
ANISOU 1978 OE2 GLU A 236 7720 12996 7252 244 244 13 O
ATOM 1979 N PHE A 237 -23.983 3.342 -35.172 1.00 56.52 N
ANISOU 1979 N PHE A 237 5826 10435 5212 -485 166 -363 N
ATOM 1980 CA PHE A 237 -24.360 1.945 -35.414 1.00 56.18 C
ANISOU 1980 CA PHE A 237 5753 10464 5127 -661 161 -472 C
ATOM 1981 C PHE A 237 -24.071 1.007 -34.239 1.00 56.78 C
ANISOU 1981 C PHE A 237 5945 10363 5266 -802 176 -527 C
ATOM 1982 O PHE A 237 -24.968 0.302 -33.784 1.00 60.91 O
ANISOU 1982 O PHE A 237 6427 10970 5746 -918 195 -597 O
ATOM 1983 CB PHE A 237 -23.704 1.398 -36.688 1.00 55.30 C
ANISOU 1983 CB PHE A 237 5636 10373 5001 -690 136 -502 C
ATOM 1984 CG PHE A 237 -23.981 -0.067 -36.933 1.00 56.15 C
ANISOU 1984 CG PHE A 237 5731 10528 5075 -878 141 -620 C
ATOM 1985 CD1 PHE A 237 -25.221 -0.488 -37.422 1.00 58.40 C
ANISOU 1985 CD1 PHE A 237 5873 11064 5252 -950 149 -691 C
ATOM 1986 CD2 PHE A 237 -23.014 -1.027 -36.664 1.00 54.96 C
ANISOU 1986 CD2 PHE A 237 5709 10174 4998 -985 145 -662 C
ATOM 1987 CE1 PHE A 237 -25.478 -1.834 -37.641 1.00 58.32 C
ANISOU 1987 CE1 PHE A 237 5855 11091 5210 -1133 164 -808 C
ATOM 1988 CE2 PHE A 237 -23.267 -2.375 -36.882 1.00 56.03 C
ANISOU 1988 CE2 PHE A 237 5842 10339 5106 -1158 162 -771 C
ATOM 1989 CZ PHE A 237 -24.500 -2.779 -37.370 1.00 57.90 C
ANISOU 1989 CZ PHE A 237 5942 10818 5237 -1237 174 -848 C
ATOM 1990 N THR A 238 -22.824 0.984 -33.761 1.00 54.16 N
ANISOU 1990 N THR A 238 5754 9792 5029 -794 169 -494 N
ATOM 1991 CA THR A 238 -22.441 0.060 -32.689 1.00 52.60 C
ANISOU 1991 CA THR A 238 5672 9421 4889 -919 182 -536 C
ATOM 1992 C THR A 238 -23.222 0.312 -31.398 1.00 54.26 C
ANISOU 1992 C THR A 238 5885 9634 5097 -935 208 -531 C
ATOM 1993 O THR A 238 -23.592 -0.632 -30.701 1.00 53.06 O
ANISOU 1993 O THR A 238 5765 9453 4942 -1068 228 -594 O
ATOM 1994 CB THR A 238 -20.919 0.085 -32.376 1.00 50.80 C
ANISOU 1994 CB THR A 238 5589 8949 4761 -891 167 -492 C
ATOM 1995 OG1 THR A 238 -20.515 1.401 -31.986 1.00 49.89 O
ANISOU 1995 OG1 THR A 238 5501 8767 4686 -748 165 -403 O
ATOM 1996 CG2 THR A 238 -20.115 -0.354 -33.561 1.00 48.59 C
ANISOU 1996 CG2 THR A 238 5319 8652 4490 -898 146 -509 C
ATOM 1997 N GLN A 239 -23.477 1.583 -31.088 1.00 56.11 N
ANISOU 1997 N GLN A 239 6087 9897 5332 -800 213 -458 N
ATOM 1998 CA GLN A 239 -24.133 1.943 -29.828 1.00 58.99 C
ANISOU 1998 CA GLN A 239 6461 10250 5702 -802 240 -448 C
ATOM 1999 C GLN A 239 -25.605 1.525 -29.767 1.00 62.86 C
ANISOU 1999 C GLN A 239 6832 10945 6104 -878 261 -511 C
ATOM 2000 O GLN A 239 -26.107 1.179 -28.694 1.00 64.24 O
ANISOU 2000 O GLN A 239 7034 11092 6282 -958 285 -542 O
ATOM 2001 CB GLN A 239 -23.968 3.436 -29.511 1.00 59.83 C
ANISOU 2001 CB GLN A 239 6574 10320 5837 -637 251 -355 C
ATOM 2002 CG GLN A 239 -22.511 3.905 -29.372 1.00 63.00 C
ANISOU 2002 CG GLN A 239 7100 10510 6328 -573 238 -298 C
ATOM 2003 CD GLN A 239 -21.651 3.007 -28.480 1.00 63.12 C
ANISOU 2003 CD GLN A 239 7245 10330 6406 -685 231 -328 C
ATOM 2004 OE1 GLN A 239 -21.851 2.948 -27.263 1.00 65.20 O
ANISOU 2004 OE1 GLN A 239 7559 10525 6689 -730 249 -333 O
ATOM 2005 NE2 GLN A 239 -20.677 2.316 -29.083 1.00 59.73 N
ANISOU 2005 NE2 GLN A 239 6872 9812 6008 -727 205 -344 N
ATOM 2006 N LYS A 240 -26.289 1.525 -30.910 1.00 65.36 N
ANISOU 2006 N LYS A 240 7016 11474 6340 -859 252 -534 N
ATOM 2007 CA LYS A 240 -27.672 1.040 -30.946 1.00 68.66 C
ANISOU 2007 CA LYS A 240 7311 12108 6668 -945 269 -606 C
ATOM 2008 C LYS A 240 -27.795 -0.478 -31.118 1.00 69.72 C
ANISOU 2008 C LYS A 240 7457 12251 6779 -1140 277 -716 C
ATOM 2009 O LYS A 240 -28.796 -1.064 -30.722 1.00 77.51 O
ANISOU 2009 O LYS A 240 8387 13348 7713 -1250 304 -787 O
ATOM 2010 CB LYS A 240 -28.521 1.790 -31.985 1.00 69.34 C
ANISOU 2010 CB LYS A 240 7230 12452 6664 -833 261 -581 C
ATOM 2011 CG LYS A 240 -28.070 1.672 -33.430 1.00 68.66 C
ANISOU 2011 CG LYS A 240 7099 12442 6546 -803 230 -581 C
ATOM 2012 CD LYS A 240 -28.786 2.713 -34.277 1.00 71.69 C
ANISOU 2012 CD LYS A 240 7335 13053 6851 -646 223 -522 C
ATOM 2013 CE LYS A 240 -28.348 2.665 -35.732 1.00 73.89 C
ANISOU 2013 CE LYS A 240 7565 13419 7090 -607 193 -515 C
ATOM 2014 NZ LYS A 240 -29.035 3.704 -36.553 1.00 73.36 N
ANISOU 2014 NZ LYS A 240 7355 13576 6940 -442 188 -446 N
ATOM 2015 N THR A 241 -26.771 -1.110 -31.681 1.00 68.72 N
ANISOU 2015 N THR A 241 7411 12003 6694 -1184 261 -732 N
ATOM 2016 CA THR A 241 -26.811 -2.549 -31.939 1.00 68.72 C
ANISOU 2016 CA THR A 241 7432 11999 6677 -1364 277 -836 C
ATOM 2017 C THR A 241 -26.267 -3.352 -30.760 1.00 70.38 C
ANISOU 2017 C THR A 241 7796 11981 6963 -1470 302 -855 C
ATOM 2018 O THR A 241 -25.062 -3.355 -30.500 1.00 71.05 O
ANISOU 2018 O THR A 241 8007 11856 7131 -1435 288 -808 O
ATOM 2019 CB THR A 241 -26.027 -2.916 -33.210 1.00 68.98 C
ANISOU 2019 CB THR A 241 7470 12025 6712 -1366 254 -852 C
ATOM 2020 OG1 THR A 241 -26.296 -1.954 -34.240 1.00 69.57 O
ANISOU 2020 OG1 THR A 241 7424 12279 6730 -1230 226 -804 O
ATOM 2021 CG2 THR A 241 -26.418 -4.303 -33.693 1.00 70.08 C
ANISOU 2021 CG2 THR A 241 7586 12234 6805 -1551 281 -973 C
ATOM 2022 N GLN A 242 -27.160 -4.048 -30.064 1.00 72.75 N
ANISOU 2022 N GLN A 242 8082 12330 7229 -1599 341 -924 N
ATOM 2023 CA GLN A 242 -26.795 -4.787 -28.856 1.00 71.95 C
ANISOU 2023 CA GLN A 242 8119 12028 7188 -1696 372 -937 C
ATOM 2024 C GLN A 242 -26.323 -6.212 -29.154 1.00 68.27 C
ANISOU 2024 C GLN A 242 7736 11462 6742 -1847 399 -1012 C
ATOM 2025 O GLN A 242 -25.425 -6.725 -28.487 1.00 65.72 O
ANISOU 2025 O GLN A 242 7557 10920 6492 -1877 409 -990 O
ATOM 2026 CB GLN A 242 -27.964 -4.798 -27.871 1.00 77.90 C
ANISOU 2026 CB GLN A 242 8829 12867 7900 -1758 407 -967 C
ATOM 2027 CG GLN A 242 -28.357 -3.409 -27.390 1.00 83.22 C
ANISOU 2027 CG GLN A 242 9445 13605 8568 -1608 390 -888 C
ATOM 2028 CD GLN A 242 -29.489 -3.436 -26.385 1.00 91.75 C
ANISOU 2028 CD GLN A 242 10484 14765 9610 -1670 428 -920 C
ATOM 2029 OE1 GLN A 242 -30.612 -3.834 -26.708 1.00 96.12 O
ANISOU 2029 OE1 GLN A 242 10922 15516 10083 -1754 451 -997 O
ATOM 2030 NE2 GLN A 242 -29.204 -3.001 -25.156 1.00 92.77 N
ANISOU 2030 NE2 GLN A 242 10705 14750 9793 -1631 436 -865 N
ATOM 2031 N GLY A 243 -26.926 -6.838 -30.162 1.00 65.60 N
ANISOU 2031 N GLY A 243 7303 11287 6334 -1939 414 -1101 N
ATOM 2032 CA GLY A 243 -26.573 -8.202 -30.548 1.00 64.01 C
ANISOU 2032 CA GLY A 243 7171 11005 6144 -2090 452 -1184 C
ATOM 2033 C GLY A 243 -25.346 -8.304 -31.446 1.00 63.79 C
ANISOU 2033 C GLY A 243 7202 10870 6166 -2036 423 -1158 C
ATOM 2034 O GLY A 243 -24.733 -7.290 -31.811 1.00 62.30 O
ANISOU 2034 O GLY A 243 6998 10670 6001 -1881 372 -1073 O
ATOM 2035 N GLN A 244 -25.004 -9.540 -31.807 1.00 61.96 N
ANISOU 2035 N GLN A 244 7037 10556 5948 -2169 464 -1233 N
ATOM 2036 CA GLN A 244 -23.849 -9.841 -32.641 1.00 60.24 C
ANISOU 2036 CA GLN A 244 6883 10226 5778 -2142 449 -1223 C
ATOM 2037 C GLN A 244 -23.942 -9.129 -33.985 1.00 60.75 C
ANISOU 2037 C GLN A 244 6817 10477 5787 -2056 403 -1218 C
ATOM 2038 O GLN A 244 -24.936 -9.271 -34.703 1.00 66.14 O
ANISOU 2038 O GLN A 244 7367 11385 6376 -2121 414 -1294 O
ATOM 2039 CB GLN A 244 -23.734 -11.364 -32.842 1.00 59.32 C
ANISOU 2039 CB GLN A 244 6842 10023 5670 -2319 517 -1323 C
ATOM 2040 CG GLN A 244 -22.638 -11.814 -33.808 1.00 58.49 C
ANISOU 2040 CG GLN A 244 6795 9819 5607 -2311 512 -1331 C
ATOM 2041 CD GLN A 244 -21.230 -11.549 -33.291 1.00 55.81 C
ANISOU 2041 CD GLN A 244 6592 9238 5372 -2197 481 -1227 C
ATOM 2042 OE1 GLN A 244 -20.916 -11.820 -32.132 1.00 54.09 O
ANISOU 2042 OE1 GLN A 244 6487 8853 5210 -2206 501 -1188 O
ATOM 2043 NE2 GLN A 244 -20.369 -11.037 -34.163 1.00 55.32 N
ANISOU 2043 NE2 GLN A 244 6519 9164 5334 -2092 434 -1184 N
ATOM 2044 N ILE A 245 -22.909 -8.360 -34.321 1.00 57.29 N
ANISOU 2044 N ILE A 245 6413 9952 5400 -1911 353 -1129 N
ATOM 2045 CA ILE A 245 -22.856 -7.669 -35.606 1.00 55.21 C
ANISOU 2045 CA ILE A 245 6043 9843 5091 -1818 311 -1113 C
ATOM 2046 C ILE A 245 -22.354 -8.623 -36.689 1.00 56.37 C
ANISOU 2046 C ILE A 245 6206 9976 5233 -1908 329 -1188 C
ATOM 2047 O ILE A 245 -21.361 -9.320 -36.494 1.00 58.73 O
ANISOU 2047 O ILE A 245 6638 10065 5610 -1946 348 -1189 O
ATOM 2048 CB ILE A 245 -21.949 -6.417 -35.537 1.00 53.29 C
ANISOU 2048 CB ILE A 245 5833 9508 4905 -1628 259 -988 C
ATOM 2049 CG1 ILE A 245 -22.609 -5.313 -34.710 1.00 52.91 C
ANISOU 2049 CG1 ILE A 245 5737 9524 4843 -1528 245 -920 C
ATOM 2050 CG2 ILE A 245 -21.607 -5.903 -36.932 1.00 53.23 C
ANISOU 2050 CG2 ILE A 245 5749 9609 4865 -1541 223 -971 C
ATOM 2051 CD1 ILE A 245 -21.646 -4.240 -34.230 1.00 51.00 C
ANISOU 2051 CD1 ILE A 245 5569 9129 4677 -1371 212 -806 C
ATOM 2052 N TYR A 246 -23.059 -8.668 -37.817 1.00 55.93 N
ANISOU 2052 N TYR A 246 6015 10151 5083 -1945 327 -1253 N
ATOM 2053 CA TYR A 246 -22.568 -9.347 -39.016 1.00 55.70 C
ANISOU 2053 CA TYR A 246 5983 10138 5040 -2007 336 -1317 C
ATOM 2054 C TYR A 246 -22.248 -8.296 -40.050 1.00 55.15 C
ANISOU 2054 C TYR A 246 5830 10183 4941 -1854 278 -1250 C
ATOM 2055 O TYR A 246 -22.885 -7.245 -40.084 1.00 56.04 O
ANISOU 2055 O TYR A 246 5837 10455 5001 -1744 244 -1193 O
ATOM 2056 CB TYR A 246 -23.615 -10.334 -39.555 1.00 59.36 C
ANISOU 2056 CB TYR A 246 6358 10785 5411 -2189 387 -1458 C
ATOM 2057 CG TYR A 246 -23.811 -11.517 -38.642 1.00 59.90 C
ANISOU 2057 CG TYR A 246 6529 10714 5515 -2354 459 -1533 C
ATOM 2058 CD1 TYR A 246 -22.946 -12.609 -38.696 1.00 60.90 C
ANISOU 2058 CD1 TYR A 246 6792 10636 5711 -2448 507 -1577 C
ATOM 2059 CD2 TYR A 246 -24.818 -11.521 -37.682 1.00 60.89 C
ANISOU 2059 CD2 TYR A 246 6623 10901 5610 -2408 483 -1551 C
ATOM 2060 CE1 TYR A 246 -23.093 -13.682 -37.836 1.00 62.52 C
ANISOU 2060 CE1 TYR A 246 7102 10699 5952 -2589 581 -1634 C
ATOM 2061 CE2 TYR A 246 -24.971 -12.588 -36.812 1.00 63.16 C
ANISOU 2061 CE2 TYR A 246 7014 11050 5931 -2556 554 -1611 C
ATOM 2062 CZ TYR A 246 -24.107 -13.669 -36.899 1.00 63.71 C
ANISOU 2062 CZ TYR A 246 7222 10915 6069 -2645 605 -1651 C
ATOM 2063 OH TYR A 246 -24.252 -14.737 -36.044 1.00 67.57 O
ANISOU 2063 OH TYR A 246 7821 11259 6591 -2786 683 -1705 O
ATOM 2064 N GLY A 247 -21.250 -8.554 -40.884 1.00 54.38 N
ANISOU 2064 N GLY A 247 5782 10001 4878 -1842 270 -1252 N
ATOM 2065 CA GLY A 247 -20.825 -7.546 -41.841 1.00 53.79 C
ANISOU 2065 CA GLY A 247 5643 10010 4781 -1692 217 -1180 C
ATOM 2066 C GLY A 247 -19.931 -8.072 -42.926 1.00 54.79 C
ANISOU 2066 C GLY A 247 5803 10088 4924 -1721 219 -1217 C
ATOM 2067 O GLY A 247 -19.343 -9.146 -42.798 1.00 56.40 O
ANISOU 2067 O GLY A 247 6113 10129 5185 -1831 259 -1276 O
ATOM 2068 N ILE A 248 -19.823 -7.303 -43.999 1.00 54.02 N
ANISOU 2068 N ILE A 248 5617 10129 4776 -1616 180 -1177 N
ATOM 2069 CA ILE A 248 -19.025 -7.699 -45.135 1.00 55.65 C
ANISOU 2069 CA ILE A 248 5840 10316 4985 -1635 179 -1210 C
ATOM 2070 C ILE A 248 -18.298 -6.496 -45.722 1.00 53.90 C
ANISOU 2070 C ILE A 248 5606 10093 4779 -1451 128 -1098 C
ATOM 2071 O ILE A 248 -18.786 -5.374 -45.654 1.00 54.84 O
ANISOU 2071 O ILE A 248 5648 10329 4859 -1323 98 -1018 O
ATOM 2072 CB ILE A 248 -19.889 -8.422 -46.211 1.00 57.96 C
ANISOU 2072 CB ILE A 248 6009 10850 5161 -1768 202 -1334 C
ATOM 2073 CG1 ILE A 248 -19.009 -9.032 -47.303 1.00 58.95 C
ANISOU 2073 CG1 ILE A 248 6172 10927 5299 -1814 213 -1385 C
ATOM 2074 CG2 ILE A 248 -20.951 -7.496 -46.801 1.00 57.47 C
ANISOU 2074 CG2 ILE A 248 5769 11089 4975 -1686 165 -1307 C
ATOM 2075 CD1 ILE A 248 -19.726 -10.071 -48.143 1.00 62.78 C
ANISOU 2075 CD1 ILE A 248 6574 11588 5689 -1993 256 -1533 C
ATOM 2076 N LYS A 249 -17.109 -6.737 -46.250 1.00 53.59 N
ANISOU 2076 N LYS A 249 5649 9909 4802 -1436 126 -1091 N
ATOM 2077 CA LYS A 249 -16.420 -5.747 -47.055 1.00 55.58 C
ANISOU 2077 CA LYS A 249 5881 10179 5055 -1287 87 -1006 C
ATOM 2078 C LYS A 249 -16.230 -6.318 -48.448 1.00 55.94 C
ANISOU 2078 C LYS A 249 5877 10333 5044 -1351 93 -1081 C
ATOM 2079 O LYS A 249 -15.715 -7.420 -48.607 1.00 54.04 O
ANISOU 2079 O LYS A 249 5709 9980 4843 -1472 127 -1163 O
ATOM 2080 CB LYS A 249 -15.068 -5.375 -46.438 1.00 53.65 C
ANISOU 2080 CB LYS A 249 5779 9666 4938 -1197 76 -922 C
ATOM 2081 CG LYS A 249 -14.395 -4.147 -47.062 1.00 53.37 C
ANISOU 2081 CG LYS A 249 5730 9637 4911 -1027 40 -820 C
ATOM 2082 CD LYS A 249 -13.333 -4.510 -48.082 1.00 50.80 C
ANISOU 2082 CD LYS A 249 5443 9245 4610 -1036 39 -841 C
ATOM 2083 CE LYS A 249 -12.171 -5.238 -47.426 1.00 52.91 C
ANISOU 2083 CE LYS A 249 5860 9244 4997 -1084 56 -854 C
ATOM 2084 NZ LYS A 249 -11.053 -5.515 -48.373 1.00 53.05 N
ANISOU 2084 NZ LYS A 249 5920 9186 5049 -1078 56 -867 N
ATOM 2085 N VAL A 250 -16.673 -5.569 -49.451 1.00 59.20 N
ANISOU 2085 N VAL A 250 6166 10967 5361 -1269 65 -1052 N
ATOM 2086 CA VAL A 250 -16.584 -6.016 -50.835 1.00 64.66 C
ANISOU 2086 CA VAL A 250 6792 11794 5980 -1325 67 -1120 C
ATOM 2087 C VAL A 250 -15.682 -5.082 -51.637 1.00 67.44 C
ANISOU 2087 C VAL A 250 7152 12123 6346 -1172 34 -1026 C
ATOM 2088 O VAL A 250 -15.874 -3.861 -51.637 1.00 69.94 O
ANISOU 2088 O VAL A 250 7421 12513 6640 -1016 4 -918 O
ATOM 2089 CB VAL A 250 -17.979 -6.134 -51.500 1.00 66.29 C
ANISOU 2089 CB VAL A 250 6826 12327 6035 -1388 67 -1190 C
ATOM 2090 CG1 VAL A 250 -17.848 -6.585 -52.942 1.00 68.85 C
ANISOU 2090 CG1 VAL A 250 7082 12797 6279 -1448 70 -1263 C
ATOM 2091 CG2 VAL A 250 -18.865 -7.107 -50.733 1.00 67.20 C
ANISOU 2091 CG2 VAL A 250 6934 12464 6134 -1554 107 -1294 C
ATOM 2092 N ASP A 251 -14.690 -5.673 -52.302 1.00 68.81 N
ANISOU 2092 N ASP A 251 7392 12189 6563 -1218 46 -1067 N
ATOM 2093 CA ASP A 251 -13.734 -4.944 -53.114 1.00 71.19 C
ANISOU 2093 CA ASP A 251 7712 12454 6883 -1096 22 -993 C
ATOM 2094 C ASP A 251 -14.281 -4.801 -54.536 1.00 72.11 C
ANISOU 2094 C ASP A 251 7689 12845 6864 -1093 9 -1023 C
ATOM 2095 O ASP A 251 -14.525 -5.802 -55.211 1.00 75.24 O
ANISOU 2095 O ASP A 251 8046 13334 7205 -1236 33 -1141 O
ATOM 2096 CB ASP A 251 -12.425 -5.729 -53.158 1.00 75.46 C
ANISOU 2096 CB ASP A 251 8385 12756 7530 -1155 45 -1031 C
ATOM 2097 CG ASP A 251 -11.239 -4.913 -52.718 1.00 80.95 C
ANISOU 2097 CG ASP A 251 9185 13239 8334 -1018 26 -920 C
ATOM 2098 OD1 ASP A 251 -11.270 -4.382 -51.581 1.00 83.73 O
ANISOU 2098 OD1 ASP A 251 9584 13486 8743 -956 17 -852 O
ATOM 2099 OD2 ASP A 251 -10.259 -4.828 -53.497 1.00 84.02 O
ANISOU 2099 OD2 ASP A 251 9607 13565 8749 -981 22 -907 O
ATOM 2100 N ILE A 252 -14.466 -3.566 -54.994 1.00 69.13 N
ANISOU 2100 N ILE A 252 7238 12594 6431 -932 -22 -917 N
ATOM 2101 CA ILE A 252 -14.927 -3.332 -56.362 1.00 69.68 C
ANISOU 2101 CA ILE A 252 7176 12931 6367 -909 -37 -928 C
ATOM 2102 C ILE A 252 -13.780 -3.399 -57.367 1.00 69.38 C
ANISOU 2102 C ILE A 252 7187 12816 6354 -890 -37 -927 C
ATOM 2103 O ILE A 252 -12.832 -2.611 -57.290 1.00 67.11 O
ANISOU 2103 O ILE A 252 6980 12372 6145 -763 -47 -828 O
ATOM 2104 CB ILE A 252 -15.674 -1.989 -56.507 1.00 69.71 C
ANISOU 2104 CB ILE A 252 7073 13121 6288 -736 -66 -809 C
ATOM 2105 CG1 ILE A 252 -16.763 -1.872 -55.439 1.00 67.42 C
ANISOU 2105 CG1 ILE A 252 6741 12892 5983 -745 -64 -805 C
ATOM 2106 CG2 ILE A 252 -16.282 -1.862 -57.904 1.00 68.67 C
ANISOU 2106 CG2 ILE A 252 6790 13297 6001 -722 -82 -828 C
ATOM 2107 CD1 ILE A 252 -17.334 -0.482 -55.304 1.00 67.23 C
ANISOU 2107 CD1 ILE A 252 6648 12982 5914 -556 -83 -672 C
ATOM 2108 N ARG A 253 -13.879 -4.336 -58.311 1.00 72.55 N
ANISOU 2108 N ARG A 253 7540 13335 6689 -1023 -22 -1043 N
ATOM 2109 CA ARG A 253 -12.887 -4.464 -59.389 1.00 73.12 C
ANISOU 2109 CA ARG A 253 7643 13369 6768 -1017 -19 -1055 C
ATOM 2110 C ARG A 253 -13.034 -3.330 -60.407 1.00 71.62 C
ANISOU 2110 C ARG A 253 7356 13377 6480 -864 -52 -958 C
ATOM 2111 O ARG A 253 -14.144 -3.008 -60.836 1.00 71.17 O
ANISOU 2111 O ARG A 253 7156 13594 6289 -841 -69 -953 O
ATOM 2112 CB ARG A 253 -12.985 -5.836 -60.077 1.00 74.39 C
ANISOU 2112 CB ARG A 253 7782 13595 6884 -1213 14 -1216 C
ATOM 2113 CG ARG A 253 -11.871 -6.123 -61.076 1.00 77.12 C
ANISOU 2113 CG ARG A 253 8180 13865 7256 -1226 25 -1242 C
ATOM 2114 CD ARG A 253 -11.872 -7.581 -61.512 1.00 82.84 C
ANISOU 2114 CD ARG A 253 8915 14593 7967 -1432 74 -1408 C
ATOM 2115 NE ARG A 253 -11.198 -8.438 -60.540 1.00 86.34 N
ANISOU 2115 NE ARG A 253 9507 14745 8552 -1515 114 -1452 N
ATOM 2116 CZ ARG A 253 -11.037 -9.756 -60.665 1.00 90.73 C
ANISOU 2116 CZ ARG A 253 10112 15227 9132 -1688 171 -1586 C
ATOM 2117 NH1 ARG A 253 -11.508 -10.397 -61.729 1.00 90.54 N
ANISOU 2117 NH1 ARG A 253 9999 15401 8999 -1812 196 -1704 N
ATOM 2118 NH2 ARG A 253 -10.400 -10.436 -59.715 1.00 92.52 N
ANISOU 2118 NH2 ARG A 253 10479 15182 9492 -1737 208 -1604 N
ATOM 2119 N ASP A 254 -11.897 -2.721 -60.746 1.00 69.75 N
ANISOU 2119 N ASP A 254 7198 12994 6309 -756 -57 -878 N
ATOM 2120 CA ASP A 254 -11.793 -1.611 -61.701 1.00 66.35 C
ANISOU 2120 CA ASP A 254 6705 12697 5805 -600 -78 -773 C
ATOM 2121 C ASP A 254 -13.058 -0.768 -61.863 1.00 68.05 C
ANISOU 2121 C ASP A 254 6778 13185 5891 -498 -101 -703 C
ATOM 2122 O ASP A 254 -13.754 -0.877 -62.867 1.00 71.87 O
ANISOU 2122 O ASP A 254 7131 13943 6233 -519 -112 -738 O
ATOM 2123 CB ASP A 254 -11.304 -2.126 -63.054 1.00 66.49 C
ANISOU 2123 CB ASP A 254 6695 12802 5764 -662 -73 -840 C
ATOM 2124 CG ASP A 254 -10.687 -1.025 -63.917 1.00 68.80 C
ANISOU 2124 CG ASP A 254 6985 13123 6033 -498 -85 -723 C
ATOM 2125 OD1 ASP A 254 -10.629 0.144 -63.463 1.00 67.48 O
ANISOU 2125 OD1 ASP A 254 6841 12899 5897 -336 -94 -590 O
ATOM 2126 OD2 ASP A 254 -10.261 -1.333 -65.057 1.00 69.76 O
ANISOU 2126 OD2 ASP A 254 7083 13320 6103 -535 -81 -767 O
ATOM 2127 N ALA A 255 -13.349 0.073 -60.870 1.00 67.66 N
ANISOU 2127 N ALA A 255 6754 13065 5889 -386 -105 -605 N
ATOM 2128 CA ALA A 255 -14.510 0.959 -60.929 1.00 66.74 C
ANISOU 2128 CA ALA A 255 6511 13185 5661 -267 -121 -523 C
ATOM 2129 C ALA A 255 -14.392 1.966 -62.074 1.00 68.64 C
ANISOU 2129 C ALA A 255 6689 13574 5814 -108 -132 -417 C
ATOM 2130 O ALA A 255 -15.378 2.238 -62.774 1.00 70.52 O
ANISOU 2130 O ALA A 255 6780 14109 5904 -64 -148 -400 O
ATOM 2131 CB ALA A 255 -14.709 1.674 -59.610 1.00 64.42 C
ANISOU 2131 CB ALA A 255 6275 12751 5451 -177 -115 -439 C
ATOM 2132 N TYR A 256 -13.188 2.499 -62.272 1.00 67.36 N
ANISOU 2132 N TYR A 256 6639 13214 5740 -24 -120 -347 N
ATOM 2133 CA TYR A 256 -12.925 3.424 -63.375 1.00 71.39 C
ANISOU 2133 CA TYR A 256 7111 13833 6178 121 -121 -245 C
ATOM 2134 C TYR A 256 -13.242 2.794 -64.728 1.00 71.90 C
ANISOU 2134 C TYR A 256 7060 14154 6103 42 -137 -324 C
ATOM 2135 O TYR A 256 -13.933 3.392 -65.550 1.00 70.52 O
ANISOU 2135 O TYR A 256 6763 14239 5790 142 -150 -261 O
ATOM 2136 CB TYR A 256 -11.474 3.905 -63.358 1.00 72.70 C
ANISOU 2136 CB TYR A 256 7426 13725 6472 188 -101 -184 C
ATOM 2137 CG TYR A 256 -11.197 4.977 -62.329 1.00 79.83 C
ANISOU 2137 CG TYR A 256 8421 14434 7477 323 -81 -66 C
ATOM 2138 CD1 TYR A 256 -11.224 4.685 -60.965 1.00 79.07 C
ANISOU 2138 CD1 TYR A 256 8396 14161 7486 264 -77 -98 C
ATOM 2139 CD2 TYR A 256 -10.892 6.282 -62.714 1.00 83.82 C
ANISOU 2139 CD2 TYR A 256 8946 14927 7974 508 -61 74 C
ATOM 2140 CE1 TYR A 256 -10.973 5.663 -60.016 1.00 81.88 C
ANISOU 2140 CE1 TYR A 256 8834 14345 7932 379 -56 1 C
ATOM 2141 CE2 TYR A 256 -10.625 7.266 -61.768 1.00 83.29 C
ANISOU 2141 CE2 TYR A 256 8967 14675 8002 623 -33 173 C
ATOM 2142 CZ TYR A 256 -10.672 6.952 -60.422 1.00 83.36 C
ANISOU 2142 CZ TYR A 256 9040 14521 8110 556 -32 134 C
ATOM 2143 OH TYR A 256 -10.416 7.919 -59.470 1.00 85.42 O
ANISOU 2143 OH TYR A 256 9387 14605 8463 661 -2 225 O
ATOM 2144 N GLY A 257 -12.743 1.579 -64.939 1.00 72.88 N
ANISOU 2144 N GLY A 257 7222 14206 6261 -135 -132 -462 N
ATOM 2145 CA GLY A 257 -12.845 0.906 -66.230 1.00 74.11 C
ANISOU 2145 CA GLY A 257 7289 14567 6300 -229 -139 -552 C
ATOM 2146 C GLY A 257 -14.180 0.228 -66.471 1.00 77.41 C
ANISOU 2146 C GLY A 257 7551 15283 6576 -341 -153 -652 C
ATOM 2147 O GLY A 257 -14.489 -0.157 -67.601 1.00 77.87 O
ANISOU 2147 O GLY A 257 7504 15578 6505 -400 -161 -715 O
ATOM 2148 N ASN A 258 -14.966 0.068 -65.407 1.00 76.72 N
ANISOU 2148 N ASN A 258 7447 15190 6510 -377 -153 -672 N
ATOM 2149 CA ASN A 258 -16.300 -0.514 -65.520 1.00 76.42 C
ANISOU 2149 CA ASN A 258 7257 15438 6340 -482 -164 -764 C
ATOM 2150 C ASN A 258 -17.415 0.523 -65.604 1.00 76.89 C
ANISOU 2150 C ASN A 258 7178 15760 6277 -323 -189 -652 C
ATOM 2151 O ASN A 258 -18.599 0.174 -65.649 1.00 79.59 O
ANISOU 2151 O ASN A 258 7378 16360 6500 -390 -201 -716 O
ATOM 2152 CB ASN A 258 -16.559 -1.528 -64.401 1.00 74.72 C
ANISOU 2152 CB ASN A 258 7097 15085 6208 -652 -143 -881 C
ATOM 2153 CG ASN A 258 -15.834 -2.845 -64.635 1.00 75.49 C
ANISOU 2153 CG ASN A 258 7275 15042 6364 -849 -113 -1031 C
ATOM 2154 OD1 ASN A 258 -15.277 -3.430 -63.705 1.00 72.87 O
ANISOU 2154 OD1 ASN A 258 7074 14440 6171 -929 -88 -1074 O
ATOM 2155 ND2 ASN A 258 -15.817 -3.305 -65.891 1.00 73.53 N
ANISOU 2155 ND2 ASN A 258 6950 14976 6010 -923 -113 -1108 N
ATOM 2156 N VAL A 259 -17.034 1.797 -65.653 1.00 73.43 N
ANISOU 2156 N VAL A 259 6776 15257 5864 -111 -192 -486 N
ATOM 2157 CA VAL A 259 -17.980 2.844 -65.996 1.00 73.96 C
ANISOU 2157 CA VAL A 259 6710 15586 5802 64 -209 -365 C
ATOM 2158 C VAL A 259 -18.501 2.623 -67.421 1.00 75.16 C
ANISOU 2158 C VAL A 259 6702 16088 5766 41 -231 -404 C
ATOM 2159 O VAL A 259 -17.727 2.570 -68.387 1.00 74.54 O
ANISOU 2159 O VAL A 259 6650 16000 5670 42 -230 -406 O
ATOM 2160 CB VAL A 259 -17.366 4.248 -65.851 1.00 72.30 C
ANISOU 2160 CB VAL A 259 6589 15220 5662 294 -195 -180 C
ATOM 2161 CG1 VAL A 259 -18.289 5.303 -66.433 1.00 74.14 C
ANISOU 2161 CG1 VAL A 259 6681 15740 5746 485 -206 -49 C
ATOM 2162 CG2 VAL A 259 -17.102 4.549 -64.393 1.00 74.28 C
ANISOU 2162 CG2 VAL A 259 6967 15183 6071 321 -174 -141 C
ATOM 2163 N LYS A 260 -19.810 2.435 -67.531 1.00 76.45 N
ANISOU 2163 N LYS A 260 6696 16564 5788 10 -251 -445 N
ATOM 2164 CA LYS A 260 -20.473 2.403 -68.823 1.00 78.28 C
ANISOU 2164 CA LYS A 260 6750 17172 5818 17 -276 -462 C
ATOM 2165 C LYS A 260 -20.628 3.851 -69.273 1.00 77.10 C
ANISOU 2165 C LYS A 260 6554 17138 5601 285 -285 -261 C
ATOM 2166 O LYS A 260 -21.395 4.625 -68.686 1.00 75.07 O
ANISOU 2166 O LYS A 260 6245 16954 5323 423 -286 -159 O
ATOM 2167 CB LYS A 260 -21.827 1.696 -68.715 1.00 82.96 C
ANISOU 2167 CB LYS A 260 7174 18063 6283 -114 -292 -580 C
ATOM 2168 CG LYS A 260 -21.774 0.380 -67.940 1.00 86.72 C
ANISOU 2168 CG LYS A 260 7718 18379 6852 -362 -270 -761 C
ATOM 2169 CD LYS A 260 -22.848 0.329 -66.851 1.00 89.61 C
ANISOU 2169 CD LYS A 260 8026 18805 7218 -387 -270 -780 C
ATOM 2170 CE LYS A 260 -22.425 -0.516 -65.651 1.00 87.59 C
ANISOU 2170 CE LYS A 260 7921 18228 7131 -546 -238 -879 C
ATOM 2171 NZ LYS A 260 -22.906 -1.925 -65.726 1.00 88.39 N
ANISOU 2171 NZ LYS A 260 7967 18432 7182 -808 -220 -1084 N
ATOM 2172 N ILE A 261 -19.850 4.216 -70.290 1.00 78.48 N
ANISOU 2172 N ILE A 261 6759 17311 5749 360 -283 -201 N
ATOM 2173 CA ILE A 261 -19.725 5.607 -70.746 1.00 79.70 C
ANISOU 2173 CA ILE A 261 6911 17507 5865 619 -276 -1 C
ATOM 2174 C ILE A 261 -21.063 6.239 -71.180 1.00 80.26 C
ANISOU 2174 C ILE A 261 6782 17967 5745 759 -300 84 C
ATOM 2175 O ILE A 261 -21.396 7.346 -70.738 1.00 80.71 O
ANISOU 2175 O ILE A 261 6843 18008 5814 963 -285 242 O
ATOM 2176 CB ILE A 261 -18.655 5.739 -71.865 1.00 80.15 C
ANISOU 2176 CB ILE A 261 7027 17510 5913 647 -269 26 C
ATOM 2177 CG1 ILE A 261 -17.275 5.315 -71.348 1.00 79.55 C
ANISOU 2177 CG1 ILE A 261 7157 17029 6037 549 -242 -29 C
ATOM 2178 CG2 ILE A 261 -18.613 7.153 -72.423 1.00 81.74 C
ANISOU 2178 CG2 ILE A 261 7217 17784 6055 913 -256 233 C
ATOM 2179 CD1 ILE A 261 -16.934 5.858 -69.971 1.00 78.65 C
ANISOU 2179 CD1 ILE A 261 7184 16598 6099 621 -215 42 C
ATOM 2180 N PRO A 262 -21.835 5.535 -72.032 1.00 79.96 N
ANISOU 2180 N PRO A 262 6567 18283 5530 648 -333 -20 N
ATOM 2181 CA PRO A 262 -23.147 6.056 -72.426 1.00 82.67 C
ANISOU 2181 CA PRO A 262 6705 19022 5682 772 -359 51 C
ATOM 2182 C PRO A 262 -24.039 6.472 -71.235 1.00 82.62 C
ANISOU 2182 C PRO A 262 6670 19008 5714 845 -353 101 C
ATOM 2183 O PRO A 262 -24.644 7.550 -71.264 1.00 83.71 O
ANISOU 2183 O PRO A 262 6736 19287 5781 1068 -351 263 O
ATOM 2184 CB PRO A 262 -23.771 4.886 -73.186 1.00 84.03 C
ANISOU 2184 CB PRO A 262 6716 19513 5698 558 -391 -131 C
ATOM 2185 CG PRO A 262 -22.611 4.128 -73.750 1.00 82.50 C
ANISOU 2185 CG PRO A 262 6635 19137 5572 405 -379 -236 C
ATOM 2186 CD PRO A 262 -21.417 4.386 -72.863 1.00 80.15 C
ANISOU 2186 CD PRO A 262 6573 18369 5508 436 -343 -187 C
ATOM 2187 N VAL A 263 -24.106 5.630 -70.204 1.00 80.28 N
ANISOU 2187 N VAL A 263 6432 18542 5526 662 -347 -32 N
ATOM 2188 CA VAL A 263 -24.916 5.913 -69.015 1.00 79.34 C
ANISOU 2188 CA VAL A 263 6294 18399 5451 705 -340 -3 C
ATOM 2189 C VAL A 263 -24.438 7.175 -68.278 1.00 80.45 C
ANISOU 2189 C VAL A 263 6573 18267 5725 929 -305 181 C
ATOM 2190 O VAL A 263 -25.255 8.004 -67.858 1.00 79.42 O
ANISOU 2190 O VAL A 263 6373 18247 5554 1093 -298 294 O
ATOM 2191 CB VAL A 263 -24.952 4.695 -68.055 1.00 78.08 C
ANISOU 2191 CB VAL A 263 6192 18081 5394 452 -333 -188 C
ATOM 2192 CG1 VAL A 263 -25.542 5.069 -66.701 1.00 75.96 C
ANISOU 2192 CG1 VAL A 263 5948 17704 5207 505 -318 -145 C
ATOM 2193 CG2 VAL A 263 -25.731 3.547 -68.683 1.00 77.60 C
ANISOU 2193 CG2 VAL A 263 5966 18338 5181 241 -358 -368 C
ATOM 2194 N LEU A 264 -23.117 7.322 -68.139 1.00 81.05 N
ANISOU 2194 N LEU A 264 6843 17994 5956 934 -278 209 N
ATOM 2195 CA LEU A 264 -22.528 8.501 -67.488 1.00 81.15 C
ANISOU 2195 CA LEU A 264 7002 17728 6101 1129 -237 373 C
ATOM 2196 C LEU A 264 -22.847 9.806 -68.234 1.00 83.67 C
ANISOU 2196 C LEU A 264 7251 18228 6311 1397 -224 568 C
ATOM 2197 O LEU A 264 -23.129 10.829 -67.609 1.00 85.60 O
ANISOU 2197 O LEU A 264 7525 18400 6597 1579 -191 705 O
ATOM 2198 CB LEU A 264 -21.005 8.333 -67.305 1.00 79.33 C
ANISOU 2198 CB LEU A 264 6981 17115 6046 1066 -213 351 C
ATOM 2199 CG LEU A 264 -20.219 9.425 -66.557 1.00 76.45 C
ANISOU 2199 CG LEU A 264 6788 16419 5837 1227 -164 492 C
ATOM 2200 CD1 LEU A 264 -20.871 9.809 -65.236 1.00 75.24 C
ANISOU 2200 CD1 LEU A 264 6650 16183 5753 1275 -147 526 C
ATOM 2201 CD2 LEU A 264 -18.776 8.996 -66.328 1.00 76.19 C
ANISOU 2201 CD2 LEU A 264 6941 16037 5968 1117 -149 431 C
ATOM 2202 N CYS A 265 -22.815 9.762 -69.564 1.00 84.34 N
ANISOU 2202 N CYS A 265 7242 18546 6254 1422 -245 580 N
ATOM 2203 CA CYS A 265 -23.173 10.927 -70.378 1.00 87.97 C
ANISOU 2203 CA CYS A 265 7622 19212 6590 1675 -233 764 C
ATOM 2204 C CYS A 265 -24.588 11.423 -70.098 1.00 89.91 C
ANISOU 2204 C CYS A 265 7703 19742 6717 1804 -241 837 C
ATOM 2205 O CYS A 265 -24.783 12.597 -69.779 1.00 91.14 O
ANISOU 2205 O CYS A 265 7888 19848 6894 2031 -200 1009 O
ATOM 2206 CB CYS A 265 -23.006 10.624 -71.867 1.00 89.75 C
ANISOU 2206 CB CYS A 265 7754 19683 6663 1651 -261 743 C
ATOM 2207 SG CYS A 265 -21.306 10.259 -72.339 1.00 87.13 S
ANISOU 2207 SG CYS A 265 7614 19030 6461 1547 -243 691 S
ATOM 2208 N LYS A 266 -25.566 10.524 -70.204 1.00 91.32 N
ANISOU 2208 N LYS A 266 7710 20215 6773 1656 -288 703 N
ATOM 2209 CA LYS A 266 -26.969 10.865 -69.939 1.00 93.66 C
ANISOU 2209 CA LYS A 266 7828 20811 6946 1755 -301 750 C
ATOM 2210 C LYS A 266 -27.135 11.434 -68.534 1.00 94.62 C
ANISOU 2210 C LYS A 266 8048 20687 7214 1833 -261 813 C
ATOM 2211 O LYS A 266 -27.971 12.311 -68.298 1.00 97.38 O
ANISOU 2211 O LYS A 266 8316 21178 7504 2029 -245 943 O
ATOM 2212 CB LYS A 266 -27.880 9.643 -70.127 1.00 93.86 C
ANISOU 2212 CB LYS A 266 7675 21145 6842 1532 -353 560 C
ATOM 2213 CG LYS A 266 -27.744 8.943 -71.475 1.00 94.69 C
ANISOU 2213 CG LYS A 266 7678 21499 6800 1418 -391 468 C
ATOM 2214 CD LYS A 266 -28.284 9.787 -72.616 1.00 97.10 C
ANISOU 2214 CD LYS A 266 7826 22159 6906 1637 -406 619 C
ATOM 2215 CE LYS A 266 -27.990 9.131 -73.951 1.00 99.76 C
ANISOU 2215 CE LYS A 266 8085 22708 7110 1523 -439 530 C
ATOM 2216 NZ LYS A 266 -28.796 9.725 -75.051 1.00103.12 N
ANISOU 2216 NZ LYS A 266 8306 23572 7301 1699 -466 643 N
ATOM 2217 N LEU A 267 -26.323 10.929 -67.608 1.00 93.87 N
ANISOU 2217 N LEU A 267 8130 20227 7309 1683 -244 721 N
ATOM 2218 CA LEU A 267 -26.293 11.430 -66.245 1.00 93.53 C
ANISOU 2218 CA LEU A 267 8206 19909 7421 1739 -204 770 C
ATOM 2219 C LEU A 267 -25.807 12.878 -66.223 1.00 93.73 C
ANISOU 2219 C LEU A 267 8340 19764 7509 2004 -146 979 C
ATOM 2220 O LEU A 267 -26.357 13.720 -65.512 1.00 94.18 O
ANISOU 2220 O LEU A 267 8396 19794 7592 2160 -110 1087 O
ATOM 2221 CB LEU A 267 -25.368 10.558 -65.393 1.00 91.35 C
ANISOU 2221 CB LEU A 267 8102 19279 7328 1521 -199 631 C
ATOM 2222 CG LEU A 267 -25.725 10.271 -63.936 1.00 89.57 C
ANISOU 2222 CG LEU A 267 7927 18888 7215 1433 -187 566 C
ATOM 2223 CD1 LEU A 267 -24.600 9.474 -63.295 1.00 89.35 C
ANISOU 2223 CD1 LEU A 267 8083 18503 7362 1242 -181 450 C
ATOM 2224 CD2 LEU A 267 -25.984 11.548 -63.154 1.00 91.01 C
ANISOU 2224 CD2 LEU A 267 8160 18959 7459 1655 -139 730 C
ATOM 2225 N ILE A 268 -24.772 13.159 -67.007 1.00 94.35 N
ANISOU 2225 N ILE A 268 8515 19721 7612 2050 -131 1033 N
ATOM 2226 CA ILE A 268 -24.210 14.500 -67.073 1.00 96.08 C
ANISOU 2226 CA ILE A 268 8849 19763 7892 2287 -67 1224 C
ATOM 2227 C ILE A 268 -25.195 15.465 -67.731 1.00 99.90 C
ANISOU 2227 C ILE A 268 9182 20563 8209 2535 -54 1389 C
ATOM 2228 O ILE A 268 -25.472 16.537 -67.189 1.00100.25 O
ANISOU 2228 O ILE A 268 9268 20527 8296 2734 3 1534 O
ATOM 2229 CB ILE A 268 -22.846 14.510 -67.799 1.00 94.65 C
ANISOU 2229 CB ILE A 268 8804 19384 7773 2263 -53 1232 C
ATOM 2230 CG1 ILE A 268 -21.778 13.844 -66.922 1.00 90.66 C
ANISOU 2230 CG1 ILE A 268 8479 18502 7465 2071 -48 1108 C
ATOM 2231 CG2 ILE A 268 -22.428 15.934 -68.148 1.00 95.44 C
ANISOU 2231 CG2 ILE A 268 8989 19384 7890 2524 15 1439 C
ATOM 2232 CD1 ILE A 268 -20.712 13.105 -67.704 1.00 90.37 C
ANISOU 2232 CD1 ILE A 268 8505 18382 7448 1926 -70 1014 C
ATOM 2233 N GLN A 269 -25.746 15.058 -68.875 1.00102.61 N
ANISOU 2233 N GLN A 269 9350 21274 8363 2521 -105 1364 N
ATOM 2234 CA GLN A 269 -26.674 15.895 -69.639 1.00109.96 C
ANISOU 2234 CA GLN A 269 10120 22547 9113 2756 -99 1520 C
ATOM 2235 C GLN A 269 -27.741 16.519 -68.739 1.00113.61 C
ANISOU 2235 C GLN A 269 10515 23080 9569 2894 -73 1600 C
ATOM 2236 O GLN A 269 -27.898 17.741 -68.704 1.00115.61 O
ANISOU 2236 O GLN A 269 10798 23304 9823 3149 -12 1789 O
ATOM 2237 CB GLN A 269 -27.355 15.090 -70.760 1.00110.45 C
ANISOU 2237 CB GLN A 269 9964 23039 8960 2662 -173 1431 C
ATOM 2238 CG GLN A 269 -26.415 14.303 -71.667 1.00109.18 C
ANISOU 2238 CG GLN A 269 9847 22845 8789 2495 -204 1324 C
ATOM 2239 CD GLN A 269 -25.930 15.092 -72.870 1.00109.43 C
ANISOU 2239 CD GLN A 269 9890 22953 8736 2679 -182 1476 C
ATOM 2240 OE1 GLN A 269 -26.086 16.311 -72.936 1.00109.95 O
ANISOU 2240 OE1 GLN A 269 9976 23014 8785 2940 -130 1675 O
ATOM 2241 NE2 GLN A 269 -25.331 14.393 -73.832 1.00108.59 N
ANISOU 2241 NE2 GLN A 269 9774 22910 8574 2544 -215 1384 N
ATOM 2242 N SER A 270 -28.448 15.672 -67.995 1.00116.86 N
ANISOU 2242 N SER A 270 10845 23574 9983 2722 -113 1454 N
ATOM 2243 CA SER A 270 -29.628 16.094 -67.247 1.00122.44 C
ANISOU 2243 CA SER A 270 11445 24423 10651 2829 -100 1506 C
ATOM 2244 C SER A 270 -29.607 15.590 -65.801 1.00121.79 C
ANISOU 2244 C SER A 270 11459 24082 10731 2665 -93 1387 C
ATOM 2245 O SER A 270 -29.180 14.465 -65.548 1.00119.57 O
ANISOU 2245 O SER A 270 11223 23693 10513 2410 -129 1208 O
ATOM 2246 CB SER A 270 -30.899 15.598 -67.953 1.00125.96 C
ANISOU 2246 CB SER A 270 11622 25367 10869 2807 -164 1456 C
ATOM 2247 OG SER A 270 -31.351 16.529 -68.925 1.00126.61 O
ANISOU 2247 OG SER A 270 11590 25721 10794 3066 -152 1637 O
ATOM 2248 N ILE A 271 -30.045 16.420 -64.848 1.00125.23 N
ANISOU 2248 N ILE A 271 11932 24411 11237 2813 -40 1486 N
ATOM 2249 CA ILE A 271 -30.330 17.847 -65.077 1.00130.76 C
ANISOU 2249 CA ILE A 271 12627 25154 11898 3127 24 1711 C
ATOM 2250 C ILE A 271 -29.515 18.697 -64.088 1.00127.75 C
ANISOU 2250 C ILE A 271 12479 24334 11725 3214 109 1795 C
ATOM 2251 O ILE A 271 -29.912 18.871 -62.931 1.00123.25 O
ANISOU 2251 O ILE A 271 11944 23642 11243 3213 138 1784 O
ATOM 2252 CB ILE A 271 -31.851 18.199 -64.955 1.00134.12 C
ANISOU 2252 CB ILE A 271 12844 25934 12180 3268 18 1774 C
ATOM 2253 CG1 ILE A 271 -32.703 17.378 -65.937 1.00135.39 C
ANISOU 2253 CG1 ILE A 271 12760 26559 12123 3180 -65 1686 C
ATOM 2254 CG2 ILE A 271 -32.083 19.690 -65.198 1.00135.16 C
ANISOU 2254 CG2 ILE A 271 12986 26087 12280 3605 95 2015 C
ATOM 2255 CD1 ILE A 271 -34.199 17.618 -65.835 1.00136.11 C
ANISOU 2255 CD1 ILE A 271 12628 27023 12063 3297 -78 1731 C
ATOM 2256 N PRO A 272 -28.338 19.170 -64.522 1.00128.86 N
ANISOU 2256 N PRO A 272 12781 24231 11946 3268 149 1865 N
ATOM 2257 CA PRO A 272 -27.670 20.227 -63.788 1.00132.71 C
ANISOU 2257 CA PRO A 272 13467 24358 12596 3404 245 1981 C
ATOM 2258 C PRO A 272 -27.511 21.509 -64.628 1.00137.23 C
ANISOU 2258 C PRO A 272 14067 24959 13113 3687 317 2196 C
ATOM 2259 O PRO A 272 -26.428 21.775 -65.157 1.00139.24 O
ANISOU 2259 O PRO A 272 14453 25025 13424 3701 346 2235 O
ATOM 2260 CB PRO A 272 -26.296 19.604 -63.464 1.00129.72 C
ANISOU 2260 CB PRO A 272 13276 23628 12381 3195 236 1859 C
ATOM 2261 CG PRO A 272 -26.171 18.384 -64.351 1.00128.49 C
ANISOU 2261 CG PRO A 272 13022 23668 12128 2999 146 1717 C
ATOM 2262 CD PRO A 272 -27.365 18.362 -65.265 1.00128.69 C
ANISOU 2262 CD PRO A 272 12813 24150 11934 3095 104 1761 C
ATOM 2263 N THR A 273 -28.588 22.287 -64.749 1.00140.50 N
ANISOU 2263 N THR A 273 14356 25609 13416 3912 349 2334 N
ATOM 2264 CA THR A 273 -28.559 23.547 -65.510 1.00142.29 C
ANISOU 2264 CA THR A 273 14602 25877 13582 4203 428 2554 C
ATOM 2265 C THR A 273 -28.115 24.723 -64.633 1.00142.57 C
ANISOU 2265 C THR A 273 14834 25552 13783 4356 552 2675 C
ATOM 2266 O THR A 273 -27.292 25.542 -65.047 1.00140.80 O
ANISOU 2266 O THR A 273 14752 25134 13611 4483 629 2793 O
ATOM 2267 CB THR A 273 -29.926 23.870 -66.164 1.00143.36 C
ANISOU 2267 CB THR A 273 14504 26459 13506 4397 409 2663 C
ATOM 2268 OG1 THR A 273 -30.931 24.009 -65.152 1.00143.39 O
ANISOU 2268 OG1 THR A 273 14436 26521 13523 4435 423 2658 O
ATOM 2269 CG2 THR A 273 -30.340 22.770 -67.140 1.00142.94 C
ANISOU 2269 CG2 THR A 273 14252 26782 13275 4250 293 2547 C
ATOM 2270 N HIS A 274 -28.665 24.786 -63.421 1.00145.90 N
ANISOU 2270 N HIS A 274 15263 25886 14283 4335 573 2639 N
ATOM 2271 CA HIS A 274 -28.296 25.791 -62.417 1.00148.64 C
ANISOU 2271 CA HIS A 274 15795 25886 14796 4444 689 2723 C
ATOM 2272 C HIS A 274 -26.853 25.648 -62.005 1.00144.87 C
ANISOU 2272 C HIS A 274 15540 25003 14499 4288 714 2644 C
ATOM 2273 O HIS A 274 -26.260 26.568 -61.438 1.00144.02 O
ANISOU 2273 O HIS A 274 15610 24586 14526 4381 820 2724 O
ATOM 2274 CB HIS A 274 -29.221 25.659 -61.200 1.00154.26 C
ANISOU 2274 CB HIS A 274 16447 26619 15543 4409 688 2665 C
ATOM 2275 CG HIS A 274 -28.949 26.662 -60.094 1.00158.92 C
ANISOU 2275 CG HIS A 274 17214 26870 16297 4512 809 2740 C
ATOM 2276 ND1 HIS A 274 -29.382 27.937 -60.145 1.00162.07 N
ANISOU 2276 ND1 HIS A 274 17630 27271 16678 4792 919 2930 N
ATOM 2277 CD2 HIS A 274 -28.288 26.521 -58.870 1.00157.75 C
ANISOU 2277 CD2 HIS A 274 17231 26371 16332 4358 836 2639 C
ATOM 2278 CE1 HIS A 274 -29.005 28.584 -59.023 1.00161.22 C
ANISOU 2278 CE1 HIS A 274 17695 26825 16736 4809 1016 2944 C
ATOM 2279 NE2 HIS A 274 -28.337 27.717 -58.245 1.00157.58 N
ANISOU 2279 NE2 HIS A 274 17320 26155 16395 4542 962 2765 N
ATOM 2280 N LEU A 275 -26.267 24.496 -62.319 1.00141.36 N
ANISOU 2280 N LEU A 275 15088 24566 14057 4051 620 2486 N
ATOM 2281 CA LEU A 275 -24.947 24.140 -61.819 1.00139.43 C
ANISOU 2281 CA LEU A 275 15034 23958 13982 3868 625 2382 C
ATOM 2282 C LEU A 275 -23.887 24.140 -62.920 1.00142.67 C
ANISOU 2282 C LEU A 275 15516 24308 14381 3860 624 2406 C
ATOM 2283 O LEU A 275 -22.804 24.701 -62.743 1.00144.37 O
ANISOU 2283 O LEU A 275 15919 24209 14726 3876 695 2442 O
ATOM 2284 CB LEU A 275 -25.003 22.779 -61.124 1.00135.47 C
ANISOU 2284 CB LEU A 275 14495 23454 13522 3586 529 2171 C
ATOM 2285 CG LEU A 275 -26.175 22.597 -60.152 1.00134.65 C
ANISOU 2285 CG LEU A 275 14287 23470 13401 3571 515 2131 C
ATOM 2286 CD1 LEU A 275 -26.610 21.142 -60.080 1.00134.62 C
ANISOU 2286 CD1 LEU A 275 14156 23653 13340 3327 403 1944 C
ATOM 2287 CD2 LEU A 275 -25.842 23.138 -58.768 1.00132.97 C
ANISOU 2287 CD2 LEU A 275 14238 22920 13364 3570 591 2133 C
ATOM 2288 N LEU A 276 -24.204 23.514 -64.052 1.00144.61 N
ANISOU 2288 N LEU A 276 15611 24863 14469 3830 545 2381 N
ATOM 2289 CA LEU A 276 -23.279 23.445 -65.187 1.00146.87 C
ANISOU 2289 CA LEU A 276 15946 25133 14726 3819 537 2399 C
ATOM 2290 C LEU A 276 -23.919 23.972 -66.463 1.00150.28 C
ANISOU 2290 C LEU A 276 16238 25894 14966 4028 541 2547 C
ATOM 2291 O LEU A 276 -23.374 24.857 -67.128 1.00148.99 O
ANISOU 2291 O LEU A 276 16160 25648 14798 4193 614 2688 O
ATOM 2292 CB LEU A 276 -22.813 22.003 -65.419 1.00144.61 C
ANISOU 2292 CB LEU A 276 15625 24880 14437 3538 431 2199 C
ATOM 2293 CG LEU A 276 -21.816 21.364 -64.454 1.00141.41 C
ANISOU 2293 CG LEU A 276 15379 24130 14219 3316 421 2051 C
ATOM 2294 CD1 LEU A 276 -21.827 19.855 -64.634 1.00141.48 C
ANISOU 2294 CD1 LEU A 276 15300 24265 14188 3058 313 1857 C
ATOM 2295 CD2 LEU A 276 -20.414 21.919 -64.660 1.00139.21 C
ANISOU 2295 CD2 LEU A 276 15296 23538 14060 3340 486 2099 C
ATOM 2296 N ASP A 277 -25.085 23.419 -66.789 1.00153.98 N
ANISOU 2296 N ASP A 277 16490 26740 15273 4019 465 2512 N
ATOM 2297 CA ASP A 277 -25.746 23.638 -68.073 1.00159.07 C
ANISOU 2297 CA ASP A 277 16966 27763 15709 4175 442 2619 C
ATOM 2298 C ASP A 277 -24.928 23.061 -69.239 1.00158.69 C
ANISOU 2298 C ASP A 277 16922 27769 15603 4069 392 2565 C
ATOM 2299 O ASP A 277 -24.339 21.986 -69.113 1.00154.28 O
ANISOU 2299 O ASP A 277 16395 27117 15104 3815 328 2385 O
ATOM 2300 CB ASP A 277 -26.090 25.122 -68.289 1.00163.95 C
ANISOU 2300 CB ASP A 277 17611 28391 16291 4503 551 2860 C
ATOM 2301 CG ASP A 277 -27.360 25.318 -69.111 1.00168.18 C
ANISOU 2301 CG ASP A 277 17914 29385 16600 4682 519 2965 C
ATOM 2302 OD1 ASP A 277 -28.286 24.485 -68.999 1.00168.28 O
ANISOU 2302 OD1 ASP A 277 17741 29682 16513 4571 430 2854 O
ATOM 2303 OD2 ASP A 277 -27.434 26.311 -69.865 1.00169.36 O
ANISOU 2303 OD2 ASP A 277 18064 29614 16669 4934 587 3159 O
ATOM 2304 N SER A 278 -24.867 23.801 -70.347 1.00160.68 N
ANISOU 2304 N SER A 278 17151 28155 15743 4269 430 2725 N
ATOM 2305 CA SER A 278 -24.546 23.225 -71.656 1.00160.11 C
ANISOU 2305 CA SER A 278 17001 28291 15541 4201 367 2687 C
ATOM 2306 C SER A 278 -23.061 23.240 -72.038 1.00157.75 C
ANISOU 2306 C SER A 278 16892 27691 15355 4124 399 2667 C
ATOM 2307 O SER A 278 -22.482 22.190 -72.322 1.00154.14 O
ANISOU 2307 O SER A 278 16435 27219 14911 3895 329 2505 O
ATOM 2308 CB SER A 278 -25.389 23.891 -72.749 1.00162.92 C
ANISOU 2308 CB SER A 278 17196 29021 15682 4450 375 2863 C
ATOM 2309 OG SER A 278 -25.484 23.067 -73.896 1.00165.44 O
ANISOU 2309 OG SER A 278 17369 29652 15837 4346 286 2785 O
ATOM 2310 N GLU A 279 -22.460 24.430 -72.054 1.00160.13 N
ANISOU 2310 N GLU A 279 17350 27755 15734 4314 509 2832 N
ATOM 2311 CA GLU A 279 -21.075 24.604 -72.519 1.00158.96 C
ANISOU 2311 CA GLU A 279 17377 27341 15679 4273 552 2837 C
ATOM 2312 C GLU A 279 -20.136 23.647 -71.799 1.00152.98 C
ANISOU 2312 C GLU A 279 16733 26304 15088 3990 510 2634 C
ATOM 2313 O GLU A 279 -19.200 23.111 -72.396 1.00151.02 O
ANISOU 2313 O GLU A 279 16540 25980 14860 3857 482 2554 O
ATOM 2314 CB GLU A 279 -20.595 26.050 -72.321 1.00162.89 C
ANISOU 2314 CB GLU A 279 18050 27569 16270 4500 693 3027 C
ATOM 2315 CG GLU A 279 -21.703 27.073 -72.124 1.00169.46 C
ANISOU 2315 CG GLU A 279 18813 28545 17028 4770 760 3208 C
ATOM 2316 CD GLU A 279 -22.151 27.167 -70.675 1.00171.67 C
ANISOU 2316 CD GLU A 279 19129 28664 17433 4739 784 3162 C
ATOM 2317 OE1 GLU A 279 -21.436 27.801 -69.873 1.00171.15 O
ANISOU 2317 OE1 GLU A 279 19257 28228 17542 4754 877 3186 O
ATOM 2318 OE2 GLU A 279 -23.215 26.604 -70.338 1.00173.88 O
ANISOU 2318 OE2 GLU A 279 19242 29189 17633 4695 710 3097 O
ATOM 2319 N LYS A 280 -20.406 23.430 -70.515 1.00147.94 N
ANISOU 2319 N LYS A 280 16126 25518 14565 3904 507 2554 N
ATOM 2320 CA LYS A 280 -19.632 22.501 -69.709 1.00141.86 C
ANISOU 2320 CA LYS A 280 15453 24496 13948 3643 466 2366 C
ATOM 2321 C LYS A 280 -19.986 21.064 -70.080 1.00139.79 C
ANISOU 2321 C LYS A 280 15041 24477 13593 3423 346 2187 C
ATOM 2322 O LYS A 280 -19.099 20.266 -70.393 1.00138.89 O
ANISOU 2322 O LYS A 280 14981 24264 13525 3241 307 2064 O
ATOM 2323 CB LYS A 280 -19.882 22.735 -68.214 1.00140.16 C
ANISOU 2323 CB LYS A 280 15311 24067 13873 3627 502 2342 C
ATOM 2324 CG LYS A 280 -20.599 24.034 -67.875 1.00140.47 C
ANISOU 2324 CG LYS A 280 15355 24116 13897 3890 595 2527 C
ATOM 2325 CD LYS A 280 -19.660 25.228 -67.815 1.00137.92 C
ANISOU 2325 CD LYS A 280 15233 23479 13691 4033 719 2659 C
ATOM 2326 CE LYS A 280 -20.401 26.461 -67.327 1.00137.24 C
ANISOU 2326 CE LYS A 280 15161 23376 13605 4278 821 2828 C
ATOM 2327 NZ LYS A 280 -19.580 27.696 -67.438 1.00134.97 N
ANISOU 2327 NZ LYS A 280 15059 22816 13405 4439 956 2972 N
ATOM 2328 N LYS A 281 -21.285 20.748 -70.066 1.00137.65 N
ANISOU 2328 N LYS A 281 14581 24529 13188 3441 294 2172 N
ATOM 2329 CA LYS A 281 -21.754 19.380 -70.312 1.00134.65 C
ANISOU 2329 CA LYS A 281 14051 24390 12718 3223 189 1993 C
ATOM 2330 C LYS A 281 -21.255 18.835 -71.650 1.00131.88 C
ANISOU 2330 C LYS A 281 13652 24192 12261 3150 145 1949 C
ATOM 2331 O LYS A 281 -20.830 17.685 -71.733 1.00127.81 O
ANISOU 2331 O LYS A 281 13136 23654 11771 2915 86 1774 O
ATOM 2332 CB LYS A 281 -23.289 19.278 -70.208 1.00136.50 C
ANISOU 2332 CB LYS A 281 14075 24983 12803 3282 149 2003 C
ATOM 2333 CG LYS A 281 -24.044 19.459 -71.522 1.00142.49 C
ANISOU 2333 CG LYS A 281 14645 26163 13332 3416 119 2092 C
ATOM 2334 CD LYS A 281 -25.492 18.994 -71.424 1.00143.59 C
ANISOU 2334 CD LYS A 281 14557 26679 13321 3398 58 2042 C
ATOM 2335 CE LYS A 281 -26.455 20.160 -71.220 1.00146.59 C
ANISOU 2335 CE LYS A 281 14866 27196 13633 3680 112 2234 C
ATOM 2336 NZ LYS A 281 -27.871 19.770 -71.482 1.00145.03 N
ANISOU 2336 NZ LYS A 281 14414 27446 13243 3691 48 2206 N
ATOM 2337 N ASN A 282 -21.285 19.679 -72.680 1.00131.58 N
ANISOU 2337 N ASN A 282 13583 24300 12110 3355 180 2111 N
ATOM 2338 CA ASN A 282 -20.815 19.302 -74.007 1.00128.95 C
ANISOU 2338 CA ASN A 282 13207 24120 11667 3312 147 2091 C
ATOM 2339 C ASN A 282 -19.349 18.902 -73.996 1.00125.82 C
ANISOU 2339 C ASN A 282 12992 23389 11424 3155 159 1999 C
ATOM 2340 O ASN A 282 -18.962 17.929 -74.646 1.00125.01 O
ANISOU 2340 O ASN A 282 12850 23367 11278 2977 102 1866 O
ATOM 2341 CB ASN A 282 -21.039 20.443 -75.002 1.00132.31 C
ANISOU 2341 CB ASN A 282 13595 24716 11960 3588 198 2307 C
ATOM 2342 CG ASN A 282 -22.501 20.824 -75.137 1.00134.23 C
ANISOU 2342 CG ASN A 282 13640 25328 12031 3757 182 2406 C
ATOM 2343 OD1 ASN A 282 -23.378 19.963 -75.203 1.00133.52 O
ANISOU 2343 OD1 ASN A 282 13371 25532 11827 3639 101 2291 O
ATOM 2344 ND2 ASN A 282 -22.769 22.123 -75.181 1.00135.04 N
ANISOU 2344 ND2 ASN A 282 13775 25418 12113 4036 265 2620 N
ATOM 2345 N PHE A 283 -18.540 19.650 -73.244 1.00123.30 N
ANISOU 2345 N PHE A 283 12868 22698 11282 3219 238 2065 N
ATOM 2346 CA PHE A 283 -17.111 19.365 -73.128 1.00119.63 C
ANISOU 2346 CA PHE A 283 12581 21897 10974 3082 257 1986 C
ATOM 2347 C PHE A 283 -16.842 18.074 -72.366 1.00116.77 C
ANISOU 2347 C PHE A 283 12237 21417 10714 2809 194 1772 C
ATOM 2348 O PHE A 283 -15.913 17.336 -72.698 1.00116.50 O
ANISOU 2348 O PHE A 283 12263 21268 10731 2645 169 1658 O
ATOM 2349 CB PHE A 283 -16.359 20.526 -72.468 1.00118.58 C
ANISOU 2349 CB PHE A 283 12645 21409 11001 3217 362 2108 C
ATOM 2350 CG PHE A 283 -14.889 20.258 -72.279 1.00117.56 C
ANISOU 2350 CG PHE A 283 12693 20938 11034 3077 382 2024 C
ATOM 2351 CD1 PHE A 283 -14.005 20.356 -73.352 1.00116.93 C
ANISOU 2351 CD1 PHE A 283 12664 20837 10926 3086 399 2051 C
ATOM 2352 CD2 PHE A 283 -14.391 19.879 -71.035 1.00115.60 C
ANISOU 2352 CD2 PHE A 283 12557 20402 10963 2933 383 1916 C
ATOM 2353 CE1 PHE A 283 -12.653 20.095 -73.184 1.00116.12 C
ANISOU 2353 CE1 PHE A 283 12716 20431 10970 2957 417 1971 C
ATOM 2354 CE2 PHE A 283 -13.040 19.616 -70.862 1.00113.30 C
ANISOU 2354 CE2 PHE A 283 12419 19814 10815 2808 399 1839 C
ATOM 2355 CZ PHE A 283 -12.170 19.726 -71.937 1.00113.75 C
ANISOU 2355 CZ PHE A 283 12522 19853 10845 2819 416 1865 C
ATOM 2356 N ILE A 284 -17.642 17.815 -71.336 1.00112.18 N
ANISOU 2356 N ILE A 284 11606 20853 10162 2764 173 1720 N
ATOM 2357 CA ILE A 284 -17.514 16.581 -70.572 1.00108.60 C
ANISOU 2357 CA ILE A 284 11162 20304 9795 2513 117 1523 C
ATOM 2358 C ILE A 284 -18.029 15.387 -71.382 1.00109.85 C
ANISOU 2358 C ILE A 284 11155 20775 9807 2352 34 1387 C
ATOM 2359 O ILE A 284 -17.379 14.342 -71.426 1.00108.46 O
ANISOU 2359 O ILE A 284 11018 20503 9686 2142 0 1232 O
ATOM 2360 CB ILE A 284 -18.221 16.669 -69.201 1.00108.27 C
ANISOU 2360 CB ILE A 284 11121 20185 9829 2510 124 1509 C
ATOM 2361 CG1 ILE A 284 -17.801 17.947 -68.463 1.00107.04 C
ANISOU 2361 CG1 ILE A 284 11120 19749 9802 2683 216 1652 C
ATOM 2362 CG2 ILE A 284 -17.892 15.448 -68.350 1.00106.08 C
ANISOU 2362 CG2 ILE A 284 10890 19751 9664 2254 79 1316 C
ATOM 2363 CD1 ILE A 284 -18.634 18.263 -67.237 1.00105.91 C
ANISOU 2363 CD1 ILE A 284 10962 19570 9707 2729 234 1672 C
ATOM 2364 N VAL A 285 -19.173 15.562 -72.049 1.00110.69 N
ANISOU 2364 N VAL A 285 11076 21255 9723 2455 7 1446 N
ATOM 2365 CA VAL A 285 -19.784 14.495 -72.856 1.00110.70 C
ANISOU 2365 CA VAL A 285 10902 21594 9564 2310 -66 1319 C
ATOM 2366 C VAL A 285 -18.787 13.871 -73.835 1.00109.73 C
ANISOU 2366 C VAL A 285 10822 21437 9433 2185 -84 1237 C
ATOM 2367 O VAL A 285 -18.557 12.660 -73.814 1.00108.96 O
ANISOU 2367 O VAL A 285 10714 21327 9357 1952 -126 1055 O
ATOM 2368 CB VAL A 285 -21.048 14.985 -73.608 1.00113.81 C
ANISOU 2368 CB VAL A 285 11090 22412 9739 2479 -85 1426 C
ATOM 2369 CG1 VAL A 285 -21.463 13.996 -74.689 1.00114.90 C
ANISOU 2369 CG1 VAL A 285 11057 22900 9699 2338 -154 1305 C
ATOM 2370 CG2 VAL A 285 -22.193 15.200 -72.633 1.00114.42 C
ANISOU 2370 CG2 VAL A 285 11086 22581 9808 2536 -87 1448 C
ATOM 2371 N ASP A 286 -18.177 14.701 -74.673 1.00110.88 N
ANISOU 2371 N ASP A 286 11023 21554 9550 2340 -44 1371 N
ATOM 2372 CA ASP A 286 -17.229 14.197 -75.657 1.00111.09 C
ANISOU 2372 CA ASP A 286 11090 21556 9562 2238 -55 1305 C
ATOM 2373 C ASP A 286 -15.881 13.846 -75.027 1.00107.23 C
ANISOU 2373 C ASP A 286 10803 20654 9286 2103 -30 1220 C
ATOM 2374 O ASP A 286 -15.056 13.174 -75.643 1.00107.07 O
ANISOU 2374 O ASP A 286 10822 20578 9280 1969 -44 1124 O
ATOM 2375 CB ASP A 286 -17.066 15.177 -76.834 1.00115.35 C
ANISOU 2375 CB ASP A 286 11613 22230 9984 2447 -21 1478 C
ATOM 2376 CG ASP A 286 -16.382 16.479 -76.435 1.00116.23 C
ANISOU 2376 CG ASP A 286 11896 22043 10221 2643 65 1650 C
ATOM 2377 OD1 ASP A 286 -16.238 16.743 -75.220 1.00115.87 O
ANISOU 2377 OD1 ASP A 286 11959 21733 10333 2644 98 1653 O
ATOM 2378 OD2 ASP A 286 -15.991 17.241 -77.348 1.00113.42 O
ANISOU 2378 OD2 ASP A 286 11568 21722 9803 2794 106 1782 O
ATOM 2379 N HIS A 287 -15.666 14.290 -73.793 1.00108.38 N
ANISOU 2379 N HIS A 287 11070 20515 9592 2138 7 1254 N
ATOM 2380 CA HIS A 287 -14.422 13.983 -73.095 1.00106.55 C
ANISOU 2380 CA HIS A 287 11022 19899 9561 2016 30 1176 C
ATOM 2381 C HIS A 287 -14.363 12.549 -72.641 1.00103.73 C
ANISOU 2381 C HIS A 287 10650 19506 9254 1758 -23 970 C
ATOM 2382 O HIS A 287 -13.309 11.919 -72.725 1.00101.91 O
ANISOU 2382 O HIS A 287 10519 19082 9119 1620 -24 873 O
ATOM 2383 CB HIS A 287 -14.196 14.931 -71.927 1.00106.65 C
ANISOU 2383 CB HIS A 287 11169 19629 9724 2132 91 1275 C
ATOM 2384 CG HIS A 287 -12.744 15.260 -71.690 1.00107.59 C
ANISOU 2384 CG HIS A 287 11484 19386 10009 2118 142 1287 C
ATOM 2385 ND1 HIS A 287 -12.090 14.892 -70.573 1.00106.70 N
ANISOU 2385 ND1 HIS A 287 11494 18977 10069 1998 148 1201 N
ATOM 2386 CD2 HIS A 287 -11.816 15.931 -72.487 1.00108.30 C
ANISOU 2386 CD2 HIS A 287 11661 19378 10108 2212 190 1376 C
ATOM 2387 CE1 HIS A 287 -10.815 15.315 -70.642 1.00106.45 C
ANISOU 2387 CE1 HIS A 287 11614 18680 10151 2014 196 1231 C
ATOM 2388 NE2 HIS A 287 -10.649 15.948 -71.814 1.00109.03 N
ANISOU 2388 NE2 HIS A 287 11921 19125 10379 2141 223 1336 N
ATOM 2389 N ILE A 288 -15.500 12.022 -72.178 1.00102.22 N
ANISOU 2389 N ILE A 288 10335 19506 8998 1694 -62 902 N
ATOM 2390 CA ILE A 288 -15.599 10.628 -71.703 1.00101.18 C
ANISOU 2390 CA ILE A 288 10181 19358 8904 1446 -106 704 C
ATOM 2391 C ILE A 288 -15.431 9.638 -72.863 1.00 99.68 C
ANISOU 2391 C ILE A 288 9912 19354 8609 1297 -143 582 C
ATOM 2392 O ILE A 288 -14.797 8.592 -72.730 1.00 98.98 O
ANISOU 2392 O ILE A 288 9883 19124 8599 1100 -154 432 O
ATOM 2393 CB ILE A 288 -16.955 10.352 -70.993 1.00103.20 C
ANISOU 2393 CB ILE A 288 10310 19803 9098 1418 -134 666 C
ATOM 2394 CG1 ILE A 288 -17.441 11.572 -70.198 1.00103.88 C
ANISOU 2394 CG1 ILE A 288 10420 19827 9220 1624 -96 825 C
ATOM 2395 CG2 ILE A 288 -16.853 9.134 -70.088 1.00101.68 C
ANISOU 2395 CG2 ILE A 288 10160 19463 9009 1185 -155 487 C
ATOM 2396 CD1 ILE A 288 -16.526 11.990 -69.063 1.00103.82 C
ANISOU 2396 CD1 ILE A 288 10608 19415 9421 1638 -50 854 C
ATOM 2397 N SER A 289 -16.035 9.970 -73.990 1.00 99.15 N
ANISOU 2397 N SER A 289 9704 19610 8356 1393 -158 646 N
ATOM 2398 CA SER A 289 -15.773 9.288 -75.236 1.00101.06 C
ANISOU 2398 CA SER A 289 9879 20030 8488 1290 -183 562 C
ATOM 2399 C SER A 289 -15.816 10.380 -76.281 1.00104.38 C
ANISOU 2399 C SER A 289 10253 20619 8785 1509 -166 735 C
ATOM 2400 O SER A 289 -16.861 11.005 -76.476 1.00110.00 O
ANISOU 2400 O SER A 289 10836 21596 9362 1657 -174 839 O
ATOM 2401 CB SER A 289 -16.850 8.243 -75.508 1.00100.46 C
ANISOU 2401 CB SER A 289 9623 20277 8268 1131 -234 416 C
ATOM 2402 OG SER A 289 -18.142 8.808 -75.370 1.00 98.06 O
ANISOU 2402 OG SER A 289 9173 20244 7839 1261 -249 503 O
ATOM 2403 N ASN A 290 -14.699 10.617 -76.966 1.00101.62 N
ANISOU 2403 N ASN A 290 10007 20126 8476 1533 -138 769 N
ATOM 2404 CA ASN A 290 -13.612 9.655 -77.092 1.00 99.90 C
ANISOU 2404 CA ASN A 290 9888 19707 8360 1335 -140 621 C
ATOM 2405 C ASN A 290 -12.330 10.094 -76.392 1.00 98.25 C
ANISOU 2405 C ASN A 290 9891 19076 8362 1364 -92 663 C
ATOM 2406 O ASN A 290 -11.926 11.257 -76.472 1.00 98.62 O
ANISOU 2406 O ASN A 290 10015 19015 8440 1551 -46 823 O
ATOM 2407 CB ASN A 290 -13.323 9.431 -78.574 1.00101.76 C
ANISOU 2407 CB ASN A 290 10058 20147 8458 1314 -152 602 C
ATOM 2408 CG ASN A 290 -14.296 10.180 -79.475 1.00103.39 C
ANISOU 2408 CG ASN A 290 10104 20726 8452 1491 -165 734 C
ATOM 2409 OD1 ASN A 290 -14.475 11.393 -79.344 1.00103.09 O
ANISOU 2409 OD1 ASN A 290 10090 20670 8409 1716 -131 918 O
ATOM 2410 ND2 ASN A 290 -14.933 9.459 -80.388 1.00102.99 N
ANISOU 2410 ND2 ASN A 290 9889 21018 8223 1392 -209 640 N
ATOM 2411 N GLN A 291 -11.682 9.146 -75.728 1.00 94.81 N
ANISOU 2411 N GLN A 291 9547 18409 8067 1176 -97 517 N
ATOM 2412 CA GLN A 291 -10.432 9.407 -75.029 1.00 92.20 C
ANISOU 2412 CA GLN A 291 9408 17688 7935 1176 -57 534 C
ATOM 2413 C GLN A 291 -9.265 8.859 -75.841 1.00 92.56 C
ANISOU 2413 C GLN A 291 9520 17633 8013 1074 -50 457 C
ATOM 2414 O GLN A 291 -9.122 7.647 -75.993 1.00 92.68 O
ANISOU 2414 O GLN A 291 9514 17667 8032 880 -75 295 O
ATOM 2415 CB GLN A 291 -10.458 8.760 -73.645 1.00 88.85 C
ANISOU 2415 CB GLN A 291 9046 17059 7653 1050 -66 435 C
ATOM 2416 CG GLN A 291 -11.589 9.245 -72.755 1.00 87.84 C
ANISOU 2416 CG GLN A 291 8857 17012 7503 1137 -72 500 C
ATOM 2417 CD GLN A 291 -11.772 8.395 -71.508 1.00 85.56 C
ANISOU 2417 CD GLN A 291 8604 16581 7324 983 -88 379 C
ATOM 2418 OE1 GLN A 291 -11.714 7.166 -71.563 1.00 84.47 O
ANISOU 2418 OE1 GLN A 291 8444 16459 7189 788 -113 220 O
ATOM 2419 NE2 GLN A 291 -12.013 9.051 -70.377 1.00 82.99 N
ANISOU 2419 NE2 GLN A 291 8333 16112 7085 1071 -68 454 N
ATOM 2420 N PHE A 292 -8.436 9.755 -76.365 1.00 93.30 N
ANISOU 2420 N PHE A 292 9698 17620 8132 1204 -9 573 N
ATOM 2421 CA PHE A 292 -7.354 9.358 -77.263 1.00 94.67 C
ANISOU 2421 CA PHE A 292 9925 17725 8318 1128 1 515 C
ATOM 2422 C PHE A 292 -5.981 9.555 -76.633 1.00 93.79 C
ANISOU 2422 C PHE A 292 9998 17232 8406 1113 42 517 C
ATOM 2423 O PHE A 292 -5.707 10.594 -76.024 1.00 93.81 O
ANISOU 2423 O PHE A 292 10090 17059 8492 1251 82 639 O
ATOM 2424 CB PHE A 292 -7.453 10.102 -78.599 1.00100.03 C
ANISOU 2424 CB PHE A 292 10538 18623 8842 1268 15 631 C
ATOM 2425 CG PHE A 292 -8.071 11.471 -78.493 1.00104.23 C
ANISOU 2425 CG PHE A 292 11053 19228 9320 1504 44 826 C
ATOM 2426 CD1 PHE A 292 -7.382 12.521 -77.884 1.00105.76 C
ANISOU 2426 CD1 PHE A 292 11392 19143 9646 1635 105 947 C
ATOM 2427 CD2 PHE A 292 -9.340 11.713 -79.006 1.00106.24 C
ANISOU 2427 CD2 PHE A 292 11143 19833 9389 1595 17 888 C
ATOM 2428 CE1 PHE A 292 -7.950 13.781 -77.787 1.00107.63 C
ANISOU 2428 CE1 PHE A 292 11620 19435 9836 1853 144 1127 C
ATOM 2429 CE2 PHE A 292 -9.912 12.974 -78.917 1.00108.83 C
ANISOU 2429 CE2 PHE A 292 11456 20226 9667 1823 51 1075 C
ATOM 2430 CZ PHE A 292 -9.216 14.009 -78.307 1.00109.52 C
ANISOU 2430 CZ PHE A 292 11699 20019 9892 1953 117 1195 C
ATOM 2431 N VAL A 293 -5.121 8.550 -76.780 1.00 91.07 N
ANISOU 2431 N VAL A 293 9706 16763 8134 945 34 378 N
ATOM 2432 CA VAL A 293 -3.828 8.542 -76.098 1.00 88.53 C
ANISOU 2432 CA VAL A 293 9546 16089 8001 906 65 355 C
ATOM 2433 C VAL A 293 -2.644 8.210 -77.008 1.00 89.76 C
ANISOU 2433 C VAL A 293 9759 16164 8181 844 84 304 C
ATOM 2434 O VAL A 293 -2.736 7.361 -77.901 1.00 89.55 O
ANISOU 2434 O VAL A 293 9658 16303 8063 735 62 204 O
ATOM 2435 CB VAL A 293 -3.823 7.584 -74.886 1.00 86.50 C
ANISOU 2435 CB VAL A 293 9330 15669 7867 756 43 230 C
ATOM 2436 CG1 VAL A 293 -4.751 8.098 -73.801 1.00 85.16 C
ANISOU 2436 CG1 VAL A 293 9139 15504 7712 833 37 297 C
ATOM 2437 CG2 VAL A 293 -4.209 6.172 -75.304 1.00 88.80 C
ANISOU 2437 CG2 VAL A 293 9534 16112 8092 568 7 64 C
ATOM 2438 N ALA A 294 -1.529 8.892 -76.764 1.00 90.14 N
ANISOU 2438 N ALA A 294 9939 15957 8351 910 128 368 N
ATOM 2439 CA ALA A 294 -0.277 8.599 -77.441 1.00 91.23 C
ANISOU 2439 CA ALA A 294 10149 15972 8540 849 150 317 C
ATOM 2440 C ALA A 294 0.335 7.317 -76.892 1.00 91.04 C
ANISOU 2440 C ALA A 294 10173 15784 8633 662 132 153 C
ATOM 2441 O ALA A 294 0.204 7.008 -75.706 1.00 91.92 O
ANISOU 2441 O ALA A 294 10323 15757 8845 614 120 116 O
ATOM 2442 CB ALA A 294 0.693 9.760 -77.280 1.00 90.19 C
ANISOU 2442 CB ALA A 294 10142 15621 8504 977 208 436 C
ATOM 2443 N PHE A 295 0.988 6.564 -77.767 1.00 93.36 N
ANISOU 2443 N PHE A 295 10465 16097 8910 558 133 58 N
ATOM 2444 CA PHE A 295 1.741 5.393 -77.352 1.00 93.89 C
ANISOU 2444 CA PHE A 295 10592 15987 9095 395 129 -87 C
ATOM 2445 C PHE A 295 3.041 5.280 -78.168 1.00 99.50 C
ANISOU 2445 C PHE A 295 11368 16589 9848 366 160 -117 C
ATOM 2446 O PHE A 295 3.745 6.280 -78.367 1.00103.05 O
ANISOU 2446 O PHE A 295 11883 16938 10330 481 195 -13 O
ATOM 2447 CB PHE A 295 0.874 4.126 -77.448 1.00 89.65 C
ANISOU 2447 CB PHE A 295 9958 15621 8484 241 93 -226 C
ATOM 2448 CG PHE A 295 1.341 3.003 -76.561 1.00 85.64 C
ANISOU 2448 CG PHE A 295 9517 14908 8112 93 91 -355 C
ATOM 2449 CD1 PHE A 295 1.571 3.216 -75.208 1.00 83.27 C
ANISOU 2449 CD1 PHE A 295 9302 14385 7951 119 92 -324 C
ATOM 2450 CD2 PHE A 295 1.553 1.731 -77.079 1.00 83.81 C
ANISOU 2450 CD2 PHE A 295 9266 14708 7869 -69 93 -506 C
ATOM 2451 CE1 PHE A 295 2.015 2.184 -74.393 1.00 82.13 C
ANISOU 2451 CE1 PHE A 295 9220 14056 7927 -7 92 -434 C
ATOM 2452 CE2 PHE A 295 1.992 0.697 -76.269 1.00 79.53 C
ANISOU 2452 CE2 PHE A 295 8792 13971 7453 -195 99 -617 C
ATOM 2453 CZ PHE A 295 2.223 0.922 -74.926 1.00 80.68 C
ANISOU 2453 CZ PHE A 295 9020 13900 7732 -161 97 -577 C
ATOM 2454 N ARG A 296 3.359 4.074 -78.633 1.00 98.56 N
ANISOU 2454 N ARG A 296 11233 16486 9728 213 154 -261 N
ATOM 2455 CA ARG A 296 4.584 3.835 -79.394 1.00 93.97 C
ANISOU 2455 CA ARG A 296 10709 15804 9188 173 184 -306 C
ATOM 2456 C ARG A 296 4.477 4.415 -80.804 1.00 97.26 C
ANISOU 2456 C ARG A 296 11064 16432 9456 244 197 -243 C
ATOM 2457 O ARG A 296 4.143 3.707 -81.758 1.00 96.89 O
ANISOU 2457 O ARG A 296 10935 16582 9297 156 186 -328 O
ATOM 2458 CB ARG A 296 4.896 2.338 -79.436 1.00 87.13 C
ANISOU 2458 CB ARG A 296 9846 14890 8366 -10 181 -480 C
ATOM 2459 CG ARG A 296 5.104 1.735 -78.058 1.00 79.42 C
ANISOU 2459 CG ARG A 296 8941 13692 7541 -77 175 -536 C
ATOM 2460 CD ARG A 296 5.106 0.221 -78.105 1.00 75.02 C
ANISOU 2460 CD ARG A 296 8372 13128 7002 -255 176 -704 C
ATOM 2461 NE ARG A 296 5.512 -0.355 -76.826 1.00 69.86 N
ANISOU 2461 NE ARG A 296 7804 12235 6504 -310 178 -750 N
ATOM 2462 CZ ARG A 296 5.590 -1.661 -76.587 1.00 68.50 C
ANISOU 2462 CZ ARG A 296 7647 11999 6381 -455 188 -885 C
ATOM 2463 NH1 ARG A 296 5.279 -2.532 -77.541 1.00 69.07 N
ANISOU 2463 NH1 ARG A 296 7655 12226 6359 -570 201 -997 N
ATOM 2464 NH2 ARG A 296 5.969 -2.098 -75.395 1.00 64.74 N
ANISOU 2464 NH2 ARG A 296 7251 11304 6042 -486 191 -909 N
ATOM 2465 N ARG A 297 4.751 5.718 -80.910 1.00101.57 N
ANISOU 2465 N ARG A 297 11652 16938 10002 403 223 -94 N
ATOM 2466 CA ARG A 297 4.623 6.480 -82.164 1.00106.20 C
ANISOU 2466 CA ARG A 297 12189 17714 10446 504 241 -2 C
ATOM 2467 C ARG A 297 3.171 6.597 -82.646 1.00107.36 C
ANISOU 2467 C ARG A 297 12195 18187 10408 548 206 36 C
ATOM 2468 O ARG A 297 2.846 7.474 -83.450 1.00108.17 O
ANISOU 2468 O ARG A 297 12254 18455 10388 675 219 154 O
ATOM 2469 CB ARG A 297 5.534 5.911 -83.273 1.00107.16 C
ANISOU 2469 CB ARG A 297 12321 17843 10549 418 261 -86 C
ATOM 2470 CG ARG A 297 7.027 6.142 -83.051 1.00105.47 C
ANISOU 2470 CG ARG A 297 12240 17342 10492 421 305 -85 C
ATOM 2471 CD ARG A 297 7.838 5.860 -84.315 1.00107.55 C
ANISOU 2471 CD ARG A 297 12505 17650 10710 373 331 -135 C
ATOM 2472 NE ARG A 297 8.302 4.470 -84.395 1.00106.40 N
ANISOU 2472 NE ARG A 297 12361 17448 10618 199 323 -308 N
ATOM 2473 CZ ARG A 297 8.855 3.913 -85.476 1.00104.54 C
ANISOU 2473 CZ ARG A 297 12109 17274 10335 120 342 -389 C
ATOM 2474 NH1 ARG A 297 9.014 4.614 -86.592 1.00105.07 N
ANISOU 2474 NH1 ARG A 297 12155 17469 10295 198 365 -313 N
ATOM 2475 NH2 ARG A 297 9.245 2.644 -85.445 1.00100.81 N
ANISOU 2475 NH2 ARG A 297 11645 16734 9922 -34 342 -546 N
ATOM 2476 N LYS A 298 2.304 5.727 -82.127 1.00110.33 N
ANISOU 2476 N LYS A 298 12501 18652 10764 445 166 -58 N
ATOM 2477 CA LYS A 298 0.914 5.626 -82.585 1.00112.39 C
ANISOU 2477 CA LYS A 298 12614 19243 10846 453 129 -53 C
ATOM 2478 C LYS A 298 -0.080 6.258 -81.602 1.00111.70 C
ANISOU 2478 C LYS A 298 12498 19184 10757 555 110 40 C
ATOM 2479 O LYS A 298 0.226 6.437 -80.418 1.00108.49 O
ANISOU 2479 O LYS A 298 12183 18538 10498 569 119 57 O
ATOM 2480 CB LYS A 298 0.539 4.158 -82.838 1.00114.36 C
ANISOU 2480 CB LYS A 298 12787 19612 11049 252 102 -239 C
ATOM 2481 CG LYS A 298 1.332 3.477 -83.949 1.00117.01 C
ANISOU 2481 CG LYS A 298 13128 19973 11356 145 121 -341 C
ATOM 2482 CD LYS A 298 1.061 1.976 -84.002 1.00119.12 C
ANISOU 2482 CD LYS A 298 13346 20300 11611 -65 109 -536 C
ATOM 2483 CE LYS A 298 1.751 1.232 -82.862 1.00120.04 C
ANISOU 2483 CE LYS A 298 13578 20106 11925 -164 123 -625 C
ATOM 2484 NZ LYS A 298 1.483 -0.235 -82.891 1.00118.77 N
ANISOU 2484 NZ LYS A 298 13380 19986 11758 -368 124 -813 N
ATOM 2485 N ILE A 299 -1.270 6.582 -82.109 1.00110.86 N
ANISOU 2485 N ILE A 299 12260 19382 10478 625 85 98 N
ATOM 2486 CA ILE A 299 -2.344 7.185 -81.310 1.00109.42 C
ANISOU 2486 CA ILE A 299 12029 19275 10268 729 68 189 C
ATOM 2487 C ILE A 299 -3.522 6.205 -81.172 1.00107.48 C
ANISOU 2487 C ILE A 299 11651 19256 9929 603 19 72 C
ATOM 2488 O ILE A 299 -3.960 5.607 -82.161 1.00109.46 O
ANISOU 2488 O ILE A 299 11789 19765 10034 524 0 -3 O
ATOM 2489 CB ILE A 299 -2.823 8.521 -81.934 1.00110.53 C
ANISOU 2489 CB ILE A 299 12123 19587 10284 945 85 378 C
ATOM 2490 CG1 ILE A 299 -1.642 9.484 -82.106 1.00110.93 C
ANISOU 2490 CG1 ILE A 299 12311 19409 10427 1059 144 488 C
ATOM 2491 CG2 ILE A 299 -3.907 9.167 -81.081 1.00108.88 C
ANISOU 2491 CG2 ILE A 299 11869 19445 10056 1061 74 475 C
ATOM 2492 CD1 ILE A 299 -1.765 10.409 -83.299 1.00114.94 C
ANISOU 2492 CD1 ILE A 299 12776 20108 10788 1214 169 626 C
ATOM 2493 N TYR A 300 -4.017 6.041 -79.942 1.00100.25 N
ANISOU 2493 N TYR A 300 10750 18244 9096 579 5 53 N
ATOM 2494 CA TYR A 300 -5.082 5.073 -79.643 1.00 96.71 C
ANISOU 2494 CA TYR A 300 10191 17971 8581 446 -33 -67 C
ATOM 2495 C TYR A 300 -6.287 5.708 -78.943 1.00 93.28 C
ANISOU 2495 C TYR A 300 9683 17665 8094 556 -53 25 C
ATOM 2496 O TYR A 300 -6.145 6.674 -78.193 1.00 88.69 O
ANISOU 2496 O TYR A 300 9178 16920 7598 698 -33 152 O
ATOM 2497 CB TYR A 300 -4.541 3.935 -78.775 1.00 96.43 C
ANISOU 2497 CB TYR A 300 10243 17695 8701 264 -29 -219 C
ATOM 2498 CG TYR A 300 -3.653 2.948 -79.497 1.00 96.54 C
ANISOU 2498 CG TYR A 300 10293 17649 8739 112 -14 -355 C
ATOM 2499 CD1 TYR A 300 -2.312 3.241 -79.753 1.00 96.57 C
ANISOU 2499 CD1 TYR A 300 10417 17430 8845 146 18 -324 C
ATOM 2500 CD2 TYR A 300 -4.141 1.708 -79.895 1.00 98.00 C
ANISOU 2500 CD2 TYR A 300 10394 17992 8848 -71 -26 -520 C
ATOM 2501 CE1 TYR A 300 -1.491 2.333 -80.404 1.00 96.50 C
ANISOU 2501 CE1 TYR A 300 10439 17363 8861 10 35 -448 C
ATOM 2502 CE2 TYR A 300 -3.328 0.792 -80.546 1.00 99.09 C
ANISOU 2502 CE2 TYR A 300 10569 18067 9012 -212 -4 -648 C
ATOM 2503 CZ TYR A 300 -2.005 1.110 -80.800 1.00 97.28 C
ANISOU 2503 CZ TYR A 300 10456 17618 8884 -166 25 -609 C
ATOM 2504 OH TYR A 300 -1.198 0.206 -81.449 1.00 98.87 O
ANISOU 2504 OH TYR A 300 10694 17758 9113 -300 50 -735 O
ATOM 2505 N LYS A 301 -7.473 5.154 -79.199 1.00 94.00 N
ANISOU 2505 N LYS A 301 9622 18050 8041 486 -89 -42 N
ATOM 2506 CA LYS A 301 -8.674 5.506 -78.440 1.00 93.62 C
ANISOU 2506 CA LYS A 301 9493 18126 7949 554 -110 10 C
ATOM 2507 C LYS A 301 -8.898 4.526 -77.300 1.00 88.03 C
ANISOU 2507 C LYS A 301 8815 17283 7348 390 -121 -123 C
ATOM 2508 O LYS A 301 -8.867 3.306 -77.494 1.00 85.02 O
ANISOU 2508 O LYS A 301 8410 16932 6959 194 -128 -290 O
ATOM 2509 CB LYS A 301 -9.911 5.553 -79.338 1.00101.07 C
ANISOU 2509 CB LYS A 301 10242 19492 8665 585 -144 23 C
ATOM 2510 CG LYS A 301 -10.273 6.943 -79.830 1.00105.70 C
ANISOU 2510 CG LYS A 301 10783 20227 9149 831 -136 226 C
ATOM 2511 CD LYS A 301 -11.573 6.913 -80.612 1.00112.17 C
ANISOU 2511 CD LYS A 301 11397 21482 9740 858 -174 233 C
ATOM 2512 CE LYS A 301 -11.608 8.020 -81.656 1.00117.02 C
ANISOU 2512 CE LYS A 301 11965 22275 10221 1066 -162 406 C
ATOM 2513 NZ LYS A 301 -12.752 7.873 -82.602 1.00116.33 N
ANISOU 2513 NZ LYS A 301 11668 22637 9894 1077 -203 399 N
ATOM 2514 N TRP A 302 -9.108 5.074 -76.107 1.00 83.37 N
ANISOU 2514 N TRP A 302 8282 16536 6857 472 -115 -48 N
ATOM 2515 CA TRP A 302 -9.354 4.276 -74.923 1.00 80.19 C
ANISOU 2515 CA TRP A 302 7914 15996 6557 339 -122 -153 C
ATOM 2516 C TRP A 302 -10.822 4.052 -74.766 1.00 80.80 C
ANISOU 2516 C TRP A 302 7837 16356 6505 314 -153 -183 C
ATOM 2517 O TRP A 302 -11.581 4.988 -74.487 1.00 79.55 O
ANISOU 2517 O TRP A 302 7622 16309 6293 471 -160 -57 O
ATOM 2518 CB TRP A 302 -8.780 4.957 -73.685 1.00 78.11 C
ANISOU 2518 CB TRP A 302 7794 15413 6469 430 -100 -65 C
ATOM 2519 CG TRP A 302 -8.892 4.118 -72.435 1.00 76.28 C
ANISOU 2519 CG TRP A 302 7614 15014 6354 294 -104 -170 C
ATOM 2520 CD1 TRP A 302 -9.860 4.204 -71.442 1.00 75.08 C
ANISOU 2520 CD1 TRP A 302 7420 14900 6204 305 -117 -158 C
ATOM 2521 CD2 TRP A 302 -8.008 3.025 -72.014 1.00 74.74 C
ANISOU 2521 CD2 TRP A 302 7524 14581 6291 123 -93 -304 C
ATOM 2522 NE1 TRP A 302 -9.636 3.267 -70.461 1.00 74.20 N
ANISOU 2522 NE1 TRP A 302 7382 14596 6212 155 -114 -271 N
ATOM 2523 CE2 TRP A 302 -8.543 2.527 -70.749 1.00 73.18 C
ANISOU 2523 CE2 TRP A 302 7343 14296 6165 45 -99 -359 C
ATOM 2524 CE3 TRP A 302 -6.867 2.433 -72.543 1.00 73.48 C
ANISOU 2524 CE3 TRP A 302 7444 14280 6195 36 -75 -377 C
ATOM 2525 CZ2 TRP A 302 -7.948 1.485 -70.057 1.00 73.28 C
ANISOU 2525 CZ2 TRP A 302 7451 14087 6304 -108 -87 -477 C
ATOM 2526 CZ3 TRP A 302 -6.274 1.378 -71.837 1.00 72.39 C
ANISOU 2526 CZ3 TRP A 302 7398 13918 6186 -115 -63 -497 C
ATOM 2527 CH2 TRP A 302 -6.806 0.914 -70.626 1.00 71.22 C
ANISOU 2527 CH2 TRP A 302 7266 13689 6102 -184 -69 -543 C
ATOM 2528 N ASN A 303 -11.237 2.805 -74.965 1.00 82.24 N
ANISOU 2528 N ASN A 303 7948 16662 6634 114 -167 -353 N
ATOM 2529 CA ASN A 303 -12.642 2.430 -74.852 1.00 84.51 C
ANISOU 2529 CA ASN A 303 8080 17236 6792 56 -194 -410 C
ATOM 2530 C ASN A 303 -12.894 1.431 -73.732 1.00 82.99 C
ANISOU 2530 C ASN A 303 7927 16904 6699 -114 -189 -542 C
ATOM 2531 O ASN A 303 -13.349 0.310 -73.969 1.00 84.76 O
ANISOU 2531 O ASN A 303 8081 17260 6861 -303 -191 -702 O
ATOM 2532 CB ASN A 303 -13.169 1.901 -76.188 1.00 86.18 C
ANISOU 2532 CB ASN A 303 8138 17795 6811 -27 -212 -495 C
ATOM 2533 CG ASN A 303 -13.607 3.016 -77.118 1.00 90.17 C
ANISOU 2533 CG ASN A 303 8535 18566 7157 171 -230 -341 C
ATOM 2534 OD1 ASN A 303 -14.364 3.908 -76.722 1.00 92.04 O
ANISOU 2534 OD1 ASN A 303 8715 18904 7351 330 -241 -214 O
ATOM 2535 ND2 ASN A 303 -13.132 2.976 -78.361 1.00 90.18 N
ANISOU 2535 ND2 ASN A 303 8510 18682 7071 167 -228 -349 N
ATOM 2536 N HIS A 304 -12.568 1.842 -72.511 1.00 79.89 N
ANISOU 2536 N HIS A 304 7653 16240 6460 -51 -177 -477 N
ATOM 2537 CA HIS A 304 -12.888 1.063 -71.324 1.00 78.89 C
ANISOU 2537 CA HIS A 304 7565 15981 6425 -182 -172 -574 C
ATOM 2538 C HIS A 304 -13.143 1.957 -70.155 1.00 74.61 C
ANISOU 2538 C HIS A 304 7073 15310 5966 -44 -172 -452 C
ATOM 2539 O HIS A 304 -12.313 2.084 -69.258 1.00 71.89 O
ANISOU 2539 O HIS A 304 6876 14652 5786 -29 -153 -425 O
ATOM 2540 CB HIS A 304 -11.790 0.059 -71.006 1.00 79.94 C
ANISOU 2540 CB HIS A 304 7841 15824 6707 -338 -145 -690 C
ATOM 2541 CG HIS A 304 -12.148 -0.896 -69.895 1.00 82.90 C
ANISOU 2541 CG HIS A 304 8252 16084 7162 -492 -134 -803 C
ATOM 2542 ND1 HIS A 304 -11.404 -1.023 -68.778 1.00 82.47 N
ANISOU 2542 ND1 HIS A 304 8347 15702 7282 -503 -116 -795 N
ATOM 2543 CD2 HIS A 304 -13.231 -1.765 -69.747 1.00 83.94 C
ANISOU 2543 CD2 HIS A 304 8280 16402 7209 -641 -136 -926 C
ATOM 2544 CE1 HIS A 304 -11.967 -1.939 -67.969 1.00 81.81 C
ANISOU 2544 CE1 HIS A 304 8263 15591 7228 -649 -106 -903 C
ATOM 2545 NE2 HIS A 304 -13.089 -2.385 -68.559 1.00 83.06 N
ANISOU 2545 NE2 HIS A 304 8268 16059 7229 -735 -116 -985 N
ATOM 2546 N GLY A 305 -14.303 2.598 -70.168 1.00 73.92 N
ANISOU 2546 N GLY A 305 6856 15472 5759 59 -192 -378 N
ATOM 2547 CA GLY A 305 -14.698 3.488 -69.095 1.00 73.15 C
ANISOU 2547 CA GLY A 305 6787 15284 5722 196 -188 -262 C
ATOM 2548 C GLY A 305 -13.893 4.763 -69.091 1.00 71.92 C
ANISOU 2548 C GLY A 305 6732 14953 5638 398 -167 -94 C
ATOM 2549 O GLY A 305 -13.431 5.222 -70.133 1.00 72.05 O
ANISOU 2549 O GLY A 305 6741 15037 5598 480 -163 -33 O
ATOM 2550 N LEU A 306 -13.743 5.341 -67.907 1.00 73.19 N
ANISOU 2550 N LEU A 306 6990 14893 5924 473 -150 -22 N
ATOM 2551 CA LEU A 306 -12.898 6.504 -67.713 1.00 73.41 C
ANISOU 2551 CA LEU A 306 7136 14708 6046 643 -119 121 C
ATOM 2552 C LEU A 306 -11.428 6.105 -67.684 1.00 72.23 C
ANISOU 2552 C LEU A 306 7140 14268 6037 564 -101 71 C
ATOM 2553 O LEU A 306 -11.072 5.034 -67.176 1.00 70.11 O
ANISOU 2553 O LEU A 306 6925 13863 5850 395 -107 -57 O
ATOM 2554 CB LEU A 306 -13.264 7.202 -66.404 1.00 71.86 C
ANISOU 2554 CB LEU A 306 6990 14379 5935 734 -102 199 C
ATOM 2555 CG LEU A 306 -14.641 7.847 -66.325 1.00 72.13 C
ANISOU 2555 CG LEU A 306 6888 14668 5848 854 -109 279 C
ATOM 2556 CD1 LEU A 306 -14.983 8.156 -64.878 1.00 71.54 C
ANISOU 2556 CD1 LEU A 306 6869 14438 5874 878 -95 306 C
ATOM 2557 CD2 LEU A 306 -14.686 9.110 -67.169 1.00 74.43 C
ANISOU 2557 CD2 LEU A 306 7147 15077 6056 1072 -88 444 C
ATOM 2558 N LEU A 307 -10.582 6.970 -68.237 1.00 73.64 N
ANISOU 2558 N LEU A 307 7386 14354 6240 691 -76 174 N
ATOM 2559 CA LEU A 307 -9.132 6.811 -68.131 1.00 75.23 C
ANISOU 2559 CA LEU A 307 7737 14264 6582 646 -54 149 C
ATOM 2560 C LEU A 307 -8.628 7.251 -66.772 1.00 71.91 C
ANISOU 2560 C LEU A 307 7446 13552 6322 680 -31 191 C
ATOM 2561 O LEU A 307 -8.762 8.416 -66.407 1.00 71.56 O
ANISOU 2561 O LEU A 307 7430 13464 6295 838 -4 319 O
ATOM 2562 CB LEU A 307 -8.417 7.627 -69.205 1.00 76.87 C
ANISOU 2562 CB LEU A 307 7970 14481 6755 768 -30 246 C
ATOM 2563 CG LEU A 307 -7.938 6.914 -70.464 1.00 77.92 C
ANISOU 2563 CG LEU A 307 8069 14717 6820 676 -41 165 C
ATOM 2564 CD1 LEU A 307 -7.428 7.943 -71.456 1.00 78.72 C
ANISOU 2564 CD1 LEU A 307 8186 14852 6872 830 -14 290 C
ATOM 2565 CD2 LEU A 307 -6.861 5.887 -70.144 1.00 77.00 C
ANISOU 2565 CD2 LEU A 307 8058 14363 6834 512 -39 38 C
ATOM 2566 N GLN A 308 -8.049 6.320 -66.025 1.00 71.74 N
ANISOU 2566 N GLN A 308 7506 13334 6416 533 -37 82 N
ATOM 2567 CA GLN A 308 -7.277 6.676 -64.840 1.00 74.91 C
ANISOU 2567 CA GLN A 308 8045 13438 6978 554 -15 113 C
ATOM 2568 C GLN A 308 -6.140 7.612 -65.243 1.00 76.04 C
ANISOU 2568 C GLN A 308 8283 13428 7180 666 19 206 C
ATOM 2569 O GLN A 308 -5.403 7.329 -66.192 1.00 73.37 O
ANISOU 2569 O GLN A 308 7956 13091 6827 634 22 175 O
ATOM 2570 CB GLN A 308 -6.719 5.426 -64.164 1.00 74.22 C
ANISOU 2570 CB GLN A 308 8026 13178 6994 377 -28 -19 C
ATOM 2571 CG GLN A 308 -7.586 4.875 -63.045 1.00 74.93 C
ANISOU 2571 CG GLN A 308 8093 13275 7101 299 -43 -74 C
ATOM 2572 CD GLN A 308 -7.314 3.408 -62.769 1.00 74.89 C
ANISOU 2572 CD GLN A 308 8118 13190 7146 107 -54 -222 C
ATOM 2573 OE1 GLN A 308 -7.407 2.570 -63.668 1.00 75.12 O
ANISOU 2573 OE1 GLN A 308 8089 13347 7105 7 -62 -311 O
ATOM 2574 NE2 GLN A 308 -6.979 3.089 -61.522 1.00 73.39 N
ANISOU 2574 NE2 GLN A 308 8019 12788 7076 55 -49 -247 N
ATOM 2575 N GLY A 309 -6.023 8.737 -64.543 1.00 79.41 N
ANISOU 2575 N GLY A 309 8774 13728 7669 796 53 316 N
ATOM 2576 CA GLY A 309 -5.004 9.738 -64.864 1.00 84.73 C
ANISOU 2576 CA GLY A 309 9540 14254 8397 907 98 409 C
ATOM 2577 C GLY A 309 -5.566 11.046 -65.398 1.00 87.30 C
ANISOU 2577 C GLY A 309 9825 14709 8636 1096 133 556 C
ATOM 2578 O GLY A 309 -4.963 12.107 -65.217 1.00 90.13 O
ANISOU 2578 O GLY A 309 10272 14915 9056 1208 186 652 O
ATOM 2579 N ASP A 310 -6.712 10.972 -66.070 1.00 86.61 N
ANISOU 2579 N ASP A 310 9602 14906 8401 1132 110 573 N
ATOM 2580 CA ASP A 310 -7.428 12.172 -66.496 1.00 89.71 C
ANISOU 2580 CA ASP A 310 9940 15445 8698 1322 142 719 C
ATOM 2581 C ASP A 310 -7.981 12.897 -65.262 1.00 90.63 C
ANISOU 2581 C ASP A 310 10089 15472 8874 1404 170 786 C
ATOM 2582 O ASP A 310 -8.651 12.284 -64.429 1.00 90.16 O
ANISOU 2582 O ASP A 310 9990 15440 8826 1320 137 717 O
ATOM 2583 CB ASP A 310 -8.558 11.813 -67.473 1.00 89.17 C
ANISOU 2583 CB ASP A 310 9704 15724 8449 1330 103 712 C
ATOM 2584 CG ASP A 310 -9.112 13.026 -68.213 1.00 89.87 C
ANISOU 2584 CG ASP A 310 9738 15982 8426 1539 139 872 C
ATOM 2585 OD1 ASP A 310 -9.424 14.044 -67.565 1.00 92.21 O
ANISOU 2585 OD1 ASP A 310 10072 16208 8756 1678 183 983 O
ATOM 2586 OD2 ASP A 310 -9.264 12.949 -69.448 1.00 92.02 O
ANISOU 2586 OD2 ASP A 310 9927 16463 8571 1566 125 888 O
ATOM 2587 N PRO A 311 -7.677 14.201 -65.134 1.00 93.30 N
ANISOU 2587 N PRO A 311 10504 15694 9251 1564 236 918 N
ATOM 2588 CA PRO A 311 -8.093 15.043 -64.002 1.00 94.14 C
ANISOU 2588 CA PRO A 311 10656 15692 9419 1656 278 991 C
ATOM 2589 C PRO A 311 -9.574 14.925 -63.601 1.00 94.92 C
ANISOU 2589 C PRO A 311 10632 16002 9430 1684 250 998 C
ATOM 2590 O PRO A 311 -9.907 15.109 -62.428 1.00 95.30 O
ANISOU 2590 O PRO A 311 10713 15949 9548 1682 263 997 O
ATOM 2591 CB PRO A 311 -7.788 16.476 -64.493 1.00 95.60 C
ANISOU 2591 CB PRO A 311 10900 15826 9595 1850 360 1146 C
ATOM 2592 CG PRO A 311 -7.276 16.343 -65.902 1.00 95.49 C
ANISOU 2592 CG PRO A 311 10862 15912 9505 1858 354 1156 C
ATOM 2593 CD PRO A 311 -6.789 14.937 -66.047 1.00 94.12 C
ANISOU 2593 CD PRO A 311 10673 15735 9354 1656 285 998 C
ATOM 2594 N LEU A 312 -10.446 14.622 -64.560 1.00 95.26 N
ANISOU 2594 N LEU A 312 10531 16343 9319 1706 214 1003 N
ATOM 2595 CA LEU A 312 -11.885 14.580 -64.297 1.00 92.67 C
ANISOU 2595 CA LEU A 312 10071 16246 8891 1745 189 1017 C
ATOM 2596 C LEU A 312 -12.397 13.211 -63.853 1.00 88.92 C
ANISOU 2596 C LEU A 312 9523 15856 8405 1550 121 861 C
ATOM 2597 O LEU A 312 -13.483 13.106 -63.282 1.00 88.14 O
ANISOU 2597 O LEU A 312 9340 15886 8261 1552 105 852 O
ATOM 2598 CB LEU A 312 -12.671 15.065 -65.515 1.00 96.63 C
ANISOU 2598 CB LEU A 312 10442 17051 9220 1886 190 1115 C
ATOM 2599 CG LEU A 312 -12.766 16.580 -65.718 1.00100.18 C
ANISOU 2599 CG LEU A 312 10929 17480 9652 2124 267 1300 C
ATOM 2600 CD1 LEU A 312 -13.584 16.893 -66.961 1.00102.80 C
ANISOU 2600 CD1 LEU A 312 11117 18143 9799 2254 257 1388 C
ATOM 2601 CD2 LEU A 312 -13.362 17.270 -64.497 1.00101.46 C
ANISOU 2601 CD2 LEU A 312 11121 17549 9877 2209 308 1359 C
ATOM 2602 N SER A 313 -11.614 12.170 -64.110 1.00 84.85 N
ANISOU 2602 N SER A 313 9043 15264 7931 1383 88 739 N
ATOM 2603 CA SER A 313 -12.042 10.804 -63.833 1.00 82.90 C
ANISOU 2603 CA SER A 313 8733 15097 7667 1190 32 586 C
ATOM 2604 C SER A 313 -12.534 10.604 -62.399 1.00 81.17 C
ANISOU 2604 C SER A 313 8538 14775 7525 1137 30 548 C
ATOM 2605 O SER A 313 -13.636 10.103 -62.187 1.00 81.89 O
ANISOU 2605 O SER A 313 8518 15056 7540 1084 0 498 O
ATOM 2606 CB SER A 313 -10.934 9.807 -64.175 1.00 80.52 C
ANISOU 2606 CB SER A 313 8501 14661 7430 1030 14 470 C
ATOM 2607 OG SER A 313 -10.804 9.671 -65.580 1.00 82.76 O
ANISOU 2607 OG SER A 313 8718 15120 7606 1040 2 469 O
ATOM 2608 N GLY A 314 -11.728 11.027 -61.426 1.00 79.47 N
ANISOU 2608 N GLY A 314 8465 14271 7458 1151 63 573 N
ATOM 2609 CA GLY A 314 -12.044 10.839 -60.008 1.00 76.62 C
ANISOU 2609 CA GLY A 314 8145 13785 7182 1095 63 536 C
ATOM 2610 C GLY A 314 -13.432 11.313 -59.618 1.00 77.31 C
ANISOU 2610 C GLY A 314 8127 14058 7188 1183 67 592 C
ATOM 2611 O GLY A 314 -14.226 10.548 -59.070 1.00 78.26 O
ANISOU 2611 O GLY A 314 8181 14269 7283 1078 35 508 O
ATOM 2612 N CYS A 315 -13.724 12.578 -59.914 1.00 77.69 N
ANISOU 2612 N CYS A 315 8161 14162 7194 1378 110 734 N
ATOM 2613 CA CYS A 315 -14.993 13.203 -59.533 1.00 78.66 C
ANISOU 2613 CA CYS A 315 8193 14448 7247 1494 124 807 C
ATOM 2614 C CYS A 315 -16.174 12.687 -60.358 1.00 80.07 C
ANISOU 2614 C CYS A 315 8184 14981 7254 1480 79 778 C
ATOM 2615 O CYS A 315 -17.314 12.686 -59.889 1.00 80.79 O
ANISOU 2615 O CYS A 315 8180 15229 7288 1498 69 778 O
ATOM 2616 CB CYS A 315 -14.900 14.720 -59.679 1.00 80.37 C
ANISOU 2616 CB CYS A 315 8456 14611 7469 1716 195 974 C
ATOM 2617 SG CYS A 315 -14.852 15.291 -61.397 1.00 82.99 S
ANISOU 2617 SG CYS A 315 8717 15148 7666 1860 206 1077 S
ATOM 2618 N LEU A 316 -15.901 12.282 -61.595 1.00 77.65 N
ANISOU 2618 N LEU A 316 7826 14812 6864 1450 52 752 N
ATOM 2619 CA LEU A 316 -16.934 11.725 -62.449 1.00 78.76 C
ANISOU 2619 CA LEU A 316 7788 15300 6837 1418 7 710 C
ATOM 2620 C LEU A 316 -17.248 10.290 -62.056 1.00 79.00 C
ANISOU 2620 C LEU A 316 7774 15373 6868 1189 -40 535 C
ATOM 2621 O LEU A 316 -18.398 9.855 -62.143 1.00 81.89 O
ANISOU 2621 O LEU A 316 7994 15997 7120 1147 -69 488 O
ATOM 2622 CB LEU A 316 -16.538 11.816 -63.923 1.00 78.89 C
ANISOU 2622 CB LEU A 316 7763 15455 6757 1465 0 743 C
ATOM 2623 CG LEU A 316 -16.550 13.219 -64.538 1.00 79.42 C
ANISOU 2623 CG LEU A 316 7831 15572 6773 1708 48 926 C
ATOM 2624 CD1 LEU A 316 -16.062 13.172 -65.974 1.00 79.39 C
ANISOU 2624 CD1 LEU A 316 7794 15689 6679 1729 38 944 C
ATOM 2625 CD2 LEU A 316 -17.927 13.857 -64.464 1.00 80.83 C
ANISOU 2625 CD2 LEU A 316 7873 16002 6836 1855 54 1018 C
ATOM 2626 N CYS A 317 -16.229 9.564 -61.604 1.00 76.87 N
ANISOU 2626 N CYS A 317 7630 14850 6726 1043 -43 441 N
ATOM 2627 CA CYS A 317 -16.421 8.211 -61.096 1.00 75.84 C
ANISOU 2627 CA CYS A 317 7486 14709 6619 827 -75 280 C
ATOM 2628 C CYS A 317 -17.244 8.214 -59.809 1.00 76.18 C
ANISOU 2628 C CYS A 317 7518 14728 6697 810 -71 269 C
ATOM 2629 O CYS A 317 -18.090 7.346 -59.611 1.00 77.04 O
ANISOU 2629 O CYS A 317 7535 14989 6747 683 -96 166 O
ATOM 2630 CB CYS A 317 -15.082 7.514 -60.870 1.00 73.08 C
ANISOU 2630 CB CYS A 317 7284 14077 6404 698 -73 200 C
ATOM 2631 SG CYS A 317 -15.223 5.773 -60.402 1.00 70.80 S
ANISOU 2631 SG CYS A 317 6990 13768 6141 432 -101 3 S
ATOM 2632 N GLU A 318 -17.002 9.198 -58.945 1.00 75.93 N
ANISOU 2632 N GLU A 318 7580 14508 6760 933 -34 370 N
ATOM 2633 CA GLU A 318 -17.803 9.375 -57.731 1.00 76.59 C
ANISOU 2633 CA GLU A 318 7653 14573 6874 942 -24 376 C
ATOM 2634 C GLU A 318 -19.249 9.725 -58.079 1.00 76.59 C
ANISOU 2634 C GLU A 318 7477 14899 6723 1032 -33 420 C
ATOM 2635 O GLU A 318 -20.189 9.199 -57.484 1.00 77.59 O
ANISOU 2635 O GLU A 318 7526 15138 6814 950 -49 352 O
ATOM 2636 CB GLU A 318 -17.203 10.467 -56.843 1.00 79.54 C
ANISOU 2636 CB GLU A 318 8162 14686 7373 1067 25 482 C
ATOM 2637 CG GLU A 318 -15.936 10.058 -56.106 1.00 84.39 C
ANISOU 2637 CG GLU A 318 8942 14977 8144 961 31 425 C
ATOM 2638 CD GLU A 318 -15.564 11.032 -54.998 1.00 86.75 C
ANISOU 2638 CD GLU A 318 9357 15043 8558 1056 79 506 C
ATOM 2639 OE1 GLU A 318 -14.420 11.541 -55.016 1.00 87.59 O
ANISOU 2639 OE1 GLU A 318 9584 14938 8755 1100 107 550 O
ATOM 2640 OE2 GLU A 318 -16.416 11.293 -54.116 1.00 86.62 O
ANISOU 2640 OE2 GLU A 318 9310 15060 8540 1084 91 523 O
ATOM 2641 N LEU A 319 -19.405 10.626 -59.045 1.00 75.42 N
ANISOU 2641 N LEU A 319 7269 14903 6485 1205 -19 537 N
ATOM 2642 CA LEU A 319 -20.710 11.037 -59.549 1.00 75.05 C
ANISOU 2642 CA LEU A 319 7047 15188 6280 1316 -28 596 C
ATOM 2643 C LEU A 319 -21.482 9.833 -60.083 1.00 73.58 C
ANISOU 2643 C LEU A 319 6710 15276 5970 1151 -81 459 C
ATOM 2644 O LEU A 319 -22.619 9.589 -59.681 1.00 75.34 O
ANISOU 2644 O LEU A 319 6815 15685 6122 1121 -95 422 O
ATOM 2645 CB LEU A 319 -20.522 12.091 -60.648 1.00 76.92 C
ANISOU 2645 CB LEU A 319 7259 15523 6443 1520 -4 742 C
ATOM 2646 CG LEU A 319 -21.681 12.977 -61.114 1.00 78.01 C
ANISOU 2646 CG LEU A 319 7249 15951 6437 1717 6 867 C
ATOM 2647 CD1 LEU A 319 -22.332 12.402 -62.360 1.00 79.05 C
ANISOU 2647 CD1 LEU A 319 7202 16444 6387 1680 -43 822 C
ATOM 2648 CD2 LEU A 319 -22.699 13.218 -60.008 1.00 79.03 C
ANISOU 2648 CD2 LEU A 319 7331 16118 6576 1751 20 879 C
ATOM 2649 N TYR A 320 -20.844 9.082 -60.977 1.00 70.35 N
ANISOU 2649 N TYR A 320 6305 14886 5536 1038 -106 379 N
ATOM 2650 CA TYR A 320 -21.393 7.840 -61.508 1.00 70.62 C
ANISOU 2650 CA TYR A 320 6219 15145 5467 852 -148 229 C
ATOM 2651 C TYR A 320 -21.742 6.823 -60.408 1.00 72.47 C
ANISOU 2651 C TYR A 320 6474 15295 5766 658 -155 91 C
ATOM 2652 O TYR A 320 -22.855 6.278 -60.391 1.00 72.20 O
ANISOU 2652 O TYR A 320 6299 15505 5627 576 -174 15 O
ATOM 2653 CB TYR A 320 -20.413 7.241 -62.509 1.00 68.76 C
ANISOU 2653 CB TYR A 320 6028 14866 5231 760 -161 166 C
ATOM 2654 CG TYR A 320 -20.833 5.929 -63.133 1.00 70.35 C
ANISOU 2654 CG TYR A 320 6122 15274 5333 555 -194 1 C
ATOM 2655 CD1 TYR A 320 -21.668 5.896 -64.255 1.00 70.98 C
ANISOU 2655 CD1 TYR A 320 6020 15724 5224 579 -220 -3 C
ATOM 2656 CD2 TYR A 320 -20.353 4.718 -62.634 1.00 69.79 C
ANISOU 2656 CD2 TYR A 320 6135 15026 5354 337 -193 -149 C
ATOM 2657 CE1 TYR A 320 -22.031 4.692 -64.842 1.00 71.82 C
ANISOU 2657 CE1 TYR A 320 6029 16021 5237 379 -243 -164 C
ATOM 2658 CE2 TYR A 320 -20.709 3.511 -63.211 1.00 70.39 C
ANISOU 2658 CE2 TYR A 320 6124 15276 5345 143 -211 -306 C
ATOM 2659 CZ TYR A 320 -21.546 3.501 -64.313 1.00 72.10 C
ANISOU 2659 CZ TYR A 320 6158 15860 5374 159 -235 -318 C
ATOM 2660 OH TYR A 320 -21.887 2.297 -64.878 1.00 72.39 O
ANISOU 2660 OH TYR A 320 6110 16068 5324 -46 -246 -483 O
ATOM 2661 N MET A 321 -20.801 6.587 -59.489 1.00 71.07 N
ANISOU 2661 N MET A 321 6469 14777 5756 589 -136 63 N
ATOM 2662 CA MET A 321 -20.956 5.556 -58.452 1.00 70.66 C
ANISOU 2662 CA MET A 321 6460 14609 5777 400 -138 -65 C
ATOM 2663 C MET A 321 -22.067 5.882 -57.452 1.00 70.56 C
ANISOU 2663 C MET A 321 6386 14674 5749 438 -130 -42 C
ATOM 2664 O MET A 321 -22.689 4.977 -56.890 1.00 70.60 O
ANISOU 2664 O MET A 321 6351 14729 5743 281 -137 -157 O
ATOM 2665 CB MET A 321 -19.632 5.320 -57.706 1.00 73.28 C
ANISOU 2665 CB MET A 321 6992 14562 6289 340 -120 -83 C
ATOM 2666 CG MET A 321 -18.531 4.668 -58.536 1.00 75.01 C
ANISOU 2666 CG MET A 321 7277 14684 6537 250 -127 -145 C
ATOM 2667 SD MET A 321 -18.838 2.924 -58.878 1.00 78.94 S
ANISOU 2667 SD MET A 321 7717 15293 6982 -15 -143 -347 S
ATOM 2668 CE MET A 321 -18.264 2.191 -57.347 1.00 75.73 C
ANISOU 2668 CE MET A 321 7475 14549 6750 -147 -122 -417 C
ATOM 2669 N ALA A 322 -22.299 7.171 -57.215 1.00 69.14 N
ANISOU 2669 N ALA A 322 6204 14494 5572 646 -109 106 N
ATOM 2670 CA ALA A 322 -23.400 7.604 -56.359 1.00 70.17 C
ANISOU 2670 CA ALA A 322 6263 14720 5676 708 -98 141 C
ATOM 2671 C ALA A 322 -24.738 7.287 -57.028 1.00 73.30 C
ANISOU 2671 C ALA A 322 6446 15510 5891 687 -125 98 C
ATOM 2672 O ALA A 322 -25.708 6.927 -56.359 1.00 73.25 O
ANISOU 2672 O ALA A 322 6363 15615 5853 618 -128 39 O
ATOM 2673 CB ALA A 322 -23.291 9.090 -56.065 1.00 70.95 C
ANISOU 2673 CB ALA A 322 6412 14726 5816 943 -59 313 C
ATOM 2674 N PHE A 323 -24.769 7.419 -58.354 1.00 73.18 N
ANISOU 2674 N PHE A 323 6336 15710 5757 745 -145 126 N
ATOM 2675 CA PHE A 323 -25.950 7.122 -59.138 1.00 78.40 C
ANISOU 2675 CA PHE A 323 6786 16769 6233 726 -174 84 C
ATOM 2676 C PHE A 323 -26.271 5.630 -59.116 1.00 79.60 C
ANISOU 2676 C PHE A 323 6887 17006 6351 461 -196 -112 C
ATOM 2677 O PHE A 323 -27.442 5.249 -58.991 1.00 81.13 O
ANISOU 2677 O PHE A 323 6932 17452 6441 395 -208 -178 O
ATOM 2678 CB PHE A 323 -25.771 7.621 -60.579 1.00 81.13 C
ANISOU 2678 CB PHE A 323 7056 17307 6463 851 -189 164 C
ATOM 2679 CG PHE A 323 -26.944 7.343 -61.478 1.00 81.87 C
ANISOU 2679 CG PHE A 323 6921 17832 6351 838 -223 125 C
ATOM 2680 CD1 PHE A 323 -28.204 7.859 -61.187 1.00 83.85 C
ANISOU 2680 CD1 PHE A 323 7027 18326 6505 945 -224 181 C
ATOM 2681 CD2 PHE A 323 -26.782 6.590 -62.633 1.00 83.50 C
ANISOU 2681 CD2 PHE A 323 7055 18213 6456 723 -252 33 C
ATOM 2682 CE1 PHE A 323 -29.282 7.611 -62.021 1.00 86.05 C
ANISOU 2682 CE1 PHE A 323 7085 19022 6587 935 -257 144 C
ATOM 2683 CE2 PHE A 323 -27.854 6.344 -63.477 1.00 86.04 C
ANISOU 2683 CE2 PHE A 323 7161 18950 6580 707 -284 -7 C
ATOM 2684 CZ PHE A 323 -29.107 6.854 -63.170 1.00 87.42 C
ANISOU 2684 CZ PHE A 323 7185 19373 6657 813 -288 48 C
ATOM 2685 N MET A 324 -25.238 4.793 -59.232 1.00 77.79 N
ANISOU 2685 N MET A 324 6779 16566 6209 308 -195 -205 N
ATOM 2686 CA MET A 324 -25.414 3.341 -59.150 1.00 78.84 C
ANISOU 2686 CA MET A 324 6895 16729 6332 49 -201 -394 C
ATOM 2687 C MET A 324 -25.967 2.964 -57.777 1.00 79.56 C
ANISOU 2687 C MET A 324 7016 16718 6492 -42 -184 -451 C
ATOM 2688 O MET A 324 -26.743 2.011 -57.646 1.00 81.86 O
ANISOU 2688 O MET A 324 7221 17160 6720 -217 -185 -586 O
ATOM 2689 CB MET A 324 -24.095 2.604 -59.393 1.00 76.16 C
ANISOU 2689 CB MET A 324 6706 16132 6098 -73 -194 -465 C
ATOM 2690 CG MET A 324 -23.455 2.843 -60.747 1.00 77.23 C
ANISOU 2690 CG MET A 324 6824 16346 6172 -9 -208 -427 C
ATOM 2691 SD MET A 324 -24.139 1.836 -62.076 1.00 78.53 S
ANISOU 2691 SD MET A 324 6806 16884 6147 -170 -231 -573 S
ATOM 2692 CE MET A 324 -25.170 3.042 -62.906 1.00 81.75 C
ANISOU 2692 CE MET A 324 7014 17677 6369 58 -258 -431 C
ATOM 2693 N ASP A 325 -25.577 3.735 -56.765 1.00 77.18 N
ANISOU 2693 N ASP A 325 6838 16168 6318 73 -164 -348 N
ATOM 2694 CA ASP A 325 -26.012 3.503 -55.396 1.00 80.18 C
ANISOU 2694 CA ASP A 325 7262 16426 6774 6 -145 -385 C
ATOM 2695 C ASP A 325 -27.515 3.778 -55.197 1.00 80.74 C
ANISOU 2695 C ASP A 325 7155 16798 6721 48 -150 -379 C
ATOM 2696 O ASP A 325 -28.224 2.989 -54.564 1.00 79.43 O
ANISOU 2696 O ASP A 325 6948 16689 6542 -105 -143 -490 O
ATOM 2697 CB ASP A 325 -25.174 4.351 -54.437 1.00 81.33 C
ANISOU 2697 CB ASP A 325 7580 16243 7078 130 -121 -271 C
ATOM 2698 CG ASP A 325 -25.399 3.986 -52.994 1.00 85.45 C
ANISOU 2698 CG ASP A 325 8176 16595 7695 38 -101 -320 C
ATOM 2699 OD1 ASP A 325 -26.449 4.372 -52.438 1.00 88.42 O
ANISOU 2699 OD1 ASP A 325 8463 17109 8023 89 -94 -294 O
ATOM 2700 OD2 ASP A 325 -24.518 3.326 -52.407 1.00 91.06 O
ANISOU 2700 OD2 ASP A 325 9035 17035 8528 -79 -91 -379 O
ATOM 2701 N ARG A 326 -27.989 4.899 -55.729 1.00 80.81 N
ANISOU 2701 N ARG A 326 7063 16998 6643 260 -157 -246 N
ATOM 2702 CA ARG A 326 -29.408 5.246 -55.659 1.00 82.67 C
ANISOU 2702 CA ARG A 326 7115 17545 6750 326 -162 -226 C
ATOM 2703 C ARG A 326 -30.228 4.252 -56.487 1.00 81.90 C
ANISOU 2703 C ARG A 326 6840 17783 6493 163 -190 -366 C
ATOM 2704 O ARG A 326 -31.339 3.889 -56.117 1.00 81.20 O
ANISOU 2704 O ARG A 326 6626 17897 6326 87 -191 -437 O
ATOM 2705 CB ARG A 326 -29.617 6.671 -56.169 1.00 84.81 C
ANISOU 2705 CB ARG A 326 7325 17937 6961 603 -159 -42 C
ATOM 2706 CG ARG A 326 -30.923 7.322 -55.744 1.00 88.56 C
ANISOU 2706 CG ARG A 326 7657 18640 7352 725 -151 20 C
ATOM 2707 CD ARG A 326 -30.803 8.843 -55.738 1.00 90.86 C
ANISOU 2707 CD ARG A 326 7980 18877 7666 1010 -122 221 C
ATOM 2708 NE ARG A 326 -30.084 9.352 -56.908 1.00 90.51 N
ANISOU 2708 NE ARG A 326 7953 18850 7586 1131 -129 311 N
ATOM 2709 CZ ARG A 326 -30.654 9.960 -57.946 1.00 93.61 C
ANISOU 2709 CZ ARG A 326 8195 19543 7827 1291 -141 404 C
ATOM 2710 NH1 ARG A 326 -31.971 10.156 -57.974 1.00 94.43 N
ANISOU 2710 NH1 ARG A 326 8110 19969 7798 1357 -150 420 N
ATOM 2711 NH2 ARG A 326 -29.901 10.377 -58.960 1.00 91.87 N
ANISOU 2711 NH2 ARG A 326 8011 19308 7587 1390 -143 482 N
ATOM 2712 N LEU A 327 -29.630 3.796 -57.586 1.00 82.69 N
ANISOU 2712 N LEU A 327 6937 17930 6548 101 -208 -412 N
ATOM 2713 CA LEU A 327 -30.241 2.854 -58.524 1.00 82.73 C
ANISOU 2713 CA LEU A 327 6785 18245 6401 -59 -230 -550 C
ATOM 2714 C LEU A 327 -30.458 1.458 -57.927 1.00 83.06 C
ANISOU 2714 C LEU A 327 6852 18229 6476 -338 -213 -744 C
ATOM 2715 O LEU A 327 -31.570 0.933 -57.957 1.00 84.14 O
ANISOU 2715 O LEU A 327 6833 18639 6496 -448 -216 -844 O
ATOM 2716 CB LEU A 327 -29.355 2.746 -59.767 1.00 81.79 C
ANISOU 2716 CB LEU A 327 6692 18131 6253 -55 -246 -547 C
ATOM 2717 CG LEU A 327 -29.963 2.545 -61.152 1.00 82.30 C
ANISOU 2717 CG LEU A 327 6559 18593 6116 -71 -277 -589 C
ATOM 2718 CD1 LEU A 327 -31.095 3.530 -61.423 1.00 83.28 C
ANISOU 2718 CD1 LEU A 327 6496 19052 6094 127 -296 -471 C
ATOM 2719 CD2 LEU A 327 -28.866 2.681 -62.193 1.00 79.52 C
ANISOU 2719 CD2 LEU A 327 6279 18159 5775 -25 -286 -548 C
ATOM 2720 N TYR A 328 -29.392 0.871 -57.376 1.00 82.91 N
ANISOU 2720 N TYR A 328 7030 17855 6617 -449 -190 -794 N
ATOM 2721 CA TYR A 328 -29.407 -0.538 -56.966 1.00 80.30 C
ANISOU 2721 CA TYR A 328 6745 17440 6323 -717 -165 -977 C
ATOM 2722 C TYR A 328 -29.315 -0.783 -55.454 1.00 80.21 C
ANISOU 2722 C TYR A 328 6870 17148 6456 -780 -134 -994 C
ATOM 2723 O TYR A 328 -29.543 -1.905 -54.989 1.00 78.85 O
ANISOU 2723 O TYR A 328 6723 16931 6304 -995 -106 -1139 O
ATOM 2724 CB TYR A 328 -28.299 -1.311 -57.675 1.00 78.03 C
ANISOU 2724 CB TYR A 328 6562 17002 6084 -836 -158 -1053 C
ATOM 2725 CG TYR A 328 -28.295 -1.179 -59.180 1.00 76.72 C
ANISOU 2725 CG TYR A 328 6274 17095 5778 -796 -186 -1050 C
ATOM 2726 CD1 TYR A 328 -29.345 -1.688 -59.956 1.00 76.39 C
ANISOU 2726 CD1 TYR A 328 6033 17434 5556 -901 -197 -1157 C
ATOM 2727 CD2 TYR A 328 -27.228 -0.573 -59.831 1.00 74.04 C
ANISOU 2727 CD2 TYR A 328 6020 16625 5484 -662 -199 -946 C
ATOM 2728 CE1 TYR A 328 -29.333 -1.578 -61.337 1.00 75.71 C
ANISOU 2728 CE1 TYR A 328 5833 17596 5335 -868 -224 -1156 C
ATOM 2729 CE2 TYR A 328 -27.203 -0.460 -61.210 1.00 75.17 C
ANISOU 2729 CE2 TYR A 328 6057 17005 5499 -626 -223 -942 C
ATOM 2730 CZ TYR A 328 -28.257 -0.962 -61.960 1.00 77.05 C
ANISOU 2730 CZ TYR A 328 6096 17624 5555 -727 -237 -1045 C
ATOM 2731 OH TYR A 328 -28.217 -0.844 -63.332 1.00 77.42 O
ANISOU 2731 OH TYR A 328 6035 17913 5468 -692 -262 -1040 O
ATOM 2732 N PHE A 329 -28.977 0.256 -54.695 1.00 81.37 N
ANISOU 2732 N PHE A 329 7108 17106 6701 -598 -133 -848 N
ATOM 2733 CA PHE A 329 -28.869 0.133 -53.245 1.00 83.24 C
ANISOU 2733 CA PHE A 329 7472 17082 7071 -640 -105 -851 C
ATOM 2734 C PHE A 329 -29.897 1.027 -52.570 1.00 90.08 C
ANISOU 2734 C PHE A 329 8245 18082 7898 -505 -105 -765 C
ATOM 2735 O PHE A 329 -29.553 1.992 -51.872 1.00 94.02 O
ANISOU 2735 O PHE A 329 8834 18401 8489 -343 -97 -638 O
ATOM 2736 CB PHE A 329 -27.446 0.454 -52.774 1.00 80.64 C
ANISOU 2736 CB PHE A 329 7356 16368 6913 -574 -96 -772 C
ATOM 2737 CG PHE A 329 -26.403 -0.460 -53.348 1.00 77.87 C
ANISOU 2737 CG PHE A 329 7105 15868 6613 -707 -92 -856 C
ATOM 2738 CD1 PHE A 329 -26.155 -1.700 -52.774 1.00 77.05 C
ANISOU 2738 CD1 PHE A 329 7094 15601 6579 -918 -63 -988 C
ATOM 2739 CD2 PHE A 329 -25.685 -0.092 -54.476 1.00 77.09 C
ANISOU 2739 CD2 PHE A 329 7006 15794 6488 -619 -112 -804 C
ATOM 2740 CE1 PHE A 329 -25.209 -2.553 -53.313 1.00 74.95 C
ANISOU 2740 CE1 PHE A 329 6919 15198 6359 -1036 -53 -1065 C
ATOM 2741 CE2 PHE A 329 -24.738 -0.939 -55.019 1.00 76.17 C
ANISOU 2741 CE2 PHE A 329 6978 15545 6417 -742 -105 -885 C
ATOM 2742 CZ PHE A 329 -24.500 -2.170 -54.437 1.00 75.27 C
ANISOU 2742 CZ PHE A 329 6954 15267 6375 -948 -75 -1015 C
ATOM 2743 N SER A 330 -31.166 0.680 -52.781 1.00 93.27 N
ANISOU 2743 N SER A 330 8468 18808 8163 -578 -109 -843 N
ATOM 2744 CA SER A 330 -32.293 1.489 -52.334 1.00 95.09 C
ANISOU 2744 CA SER A 330 8571 19234 8324 -448 -111 -771 C
ATOM 2745 C SER A 330 -33.093 0.813 -51.224 1.00 95.65 C
ANISOU 2745 C SER A 330 8629 19301 8411 -604 -84 -875 C
ATOM 2746 O SER A 330 -33.720 1.491 -50.406 1.00 97.45 O
ANISOU 2746 O SER A 330 8828 19547 8650 -501 -74 -805 O
ATOM 2747 CB SER A 330 -33.211 1.824 -53.519 1.00 98.14 C
ANISOU 2747 CB SER A 330 8729 20040 8517 -369 -141 -755 C
ATOM 2748 OG SER A 330 -33.383 0.704 -54.375 1.00 98.02 O
ANISOU 2748 OG SER A 330 8631 20207 8405 -570 -150 -910 O
ATOM 2749 N ASN A 331 -33.068 -0.519 -51.197 1.00 96.85 N
ANISOU 2749 N ASN A 331 8806 19426 8565 -852 -66 -1041 N
ATOM 2750 CA ASN A 331 -33.833 -1.288 -50.208 1.00100.25 C
ANISOU 2750 CA ASN A 331 9226 19859 9004 -1025 -33 -1154 C
ATOM 2751 C ASN A 331 -32.971 -1.947 -49.138 1.00100.12 C
ANISOU 2751 C ASN A 331 9429 19455 9157 -1145 1 -1195 C
ATOM 2752 O ASN A 331 -33.309 -3.022 -48.629 1.00100.56 O
ANISOU 2752 O ASN A 331 9505 19481 9221 -1356 36 -1331 O
ATOM 2753 CB ASN A 331 -34.702 -2.332 -50.904 1.00102.31 C
ANISOU 2753 CB ASN A 331 9328 20422 9121 -1230 -27 -1324 C
ATOM 2754 CG ASN A 331 -35.651 -1.715 -51.902 1.00103.08 C
ANISOU 2754 CG ASN A 331 9192 20935 9037 -1116 -63 -1288 C
ATOM 2755 OD1 ASN A 331 -35.527 -1.936 -53.104 1.00104.32 O
ANISOU 2755 OD1 ASN A 331 9267 21269 9098 -1140 -85 -1324 O
ATOM 2756 ND2 ASN A 331 -36.583 -0.907 -51.411 1.00102.06 N
ANISOU 2756 ND2 ASN A 331 8953 20965 8859 -982 -69 -1210 N
ATOM 2757 N LEU A 332 -31.872 -1.281 -48.786 1.00 99.56 N
ANISOU 2757 N LEU A 332 9519 19092 9217 -1009 -5 -1075 N
ATOM 2758 CA LEU A 332 -30.910 -1.810 -47.824 1.00 97.38 C
ANISOU 2758 CA LEU A 332 9453 18443 9101 -1096 21 -1095 C
ATOM 2759 C LEU A 332 -31.468 -1.880 -46.396 1.00 94.62 C
ANISOU 2759 C LEU A 332 9145 17997 8806 -1142 51 -1107 C
ATOM 2760 O LEU A 332 -31.572 -2.969 -45.828 1.00 95.47 O
ANISOU 2760 O LEU A 332 9310 18016 8945 -1339 85 -1225 O
ATOM 2761 CB LEU A 332 -29.607 -0.997 -47.858 1.00 97.27 C
ANISOU 2761 CB LEU A 332 9585 18171 9202 -931 5 -962 C
ATOM 2762 CG LEU A 332 -28.782 -1.030 -49.150 1.00 98.13 C
ANISOU 2762 CG LEU A 332 9700 18296 9288 -902 -17 -952 C
ATOM 2763 CD1 LEU A 332 -27.649 -0.017 -49.092 1.00 96.99 C
ANISOU 2763 CD1 LEU A 332 9682 17921 9249 -714 -30 -807 C
ATOM 2764 CD2 LEU A 332 -28.242 -2.426 -49.419 1.00 97.23 C
ANISOU 2764 CD2 LEU A 332 9660 18078 9203 -1121 2 -1095 C
ATOM 2765 N ASP A 333 -31.830 -0.720 -45.838 1.00 91.07 N
ANISOU 2765 N ASP A 333 8669 17566 8367 -959 43 -985 N
ATOM 2766 CA ASP A 333 -32.296 -0.592 -44.444 1.00 89.53 C
ANISOU 2766 CA ASP A 333 8519 17266 8230 -972 71 -976 C
ATOM 2767 C ASP A 333 -31.790 0.722 -43.861 1.00 90.81 C
ANISOU 2767 C ASP A 333 8766 17256 8481 -753 66 -815 C
ATOM 2768 O ASP A 333 -30.613 1.059 -44.000 1.00 92.65 O
ANISOU 2768 O ASP A 333 9129 17268 8805 -677 56 -746 O
ATOM 2769 CB ASP A 333 -31.808 -1.766 -43.574 1.00 86.06 C
ANISOU 2769 CB ASP A 333 8234 16573 7890 -1175 105 -1077 C
ATOM 2770 CG ASP A 333 -32.448 -1.791 -42.182 1.00 86.57 C
ANISOU 2770 CG ASP A 333 8327 16572 7993 -1218 136 -1089 C
ATOM 2771 OD1 ASP A 333 -32.953 -0.749 -41.710 1.00 86.33 O
ANISOU 2771 OD1 ASP A 333 8245 16601 7954 -1065 131 -994 O
ATOM 2772 OD2 ASP A 333 -32.433 -2.868 -41.549 1.00 85.72 O
ANISOU 2772 OD2 ASP A 333 8297 16345 7925 -1407 170 -1192 O
ATOM 2773 N LYS A 334 -32.676 1.452 -43.195 1.00 93.16 N
ANISOU 2773 N LYS A 334 8991 17653 8752 -657 77 -761 N
ATOM 2774 CA LYS A 334 -32.292 2.690 -42.521 1.00 95.92 C
ANISOU 2774 CA LYS A 334 9422 17835 9186 -462 86 -619 C
ATOM 2775 C LYS A 334 -31.427 2.422 -41.270 1.00 94.45 C
ANISOU 2775 C LYS A 334 9438 17296 9151 -530 108 -623 C
ATOM 2776 O LYS A 334 -30.678 3.298 -40.821 1.00 93.31 O
ANISOU 2776 O LYS A 334 9405 16947 9100 -395 114 -517 O
ATOM 2777 CB LYS A 334 -33.536 3.508 -42.156 1.00 98.63 C
ANISOU 2777 CB LYS A 334 9626 18392 9455 -344 99 -566 C
ATOM 2778 CG LYS A 334 -33.264 4.988 -41.945 1.00 99.76 C
ANISOU 2778 CG LYS A 334 9808 18447 9647 -98 111 -405 C
ATOM 2779 CD LYS A 334 -34.103 5.536 -40.807 1.00101.92 C
ANISOU 2779 CD LYS A 334 10056 18734 9932 -44 144 -374 C
ATOM 2780 CE LYS A 334 -33.296 6.512 -39.964 1.00101.32 C
ANISOU 2780 CE LYS A 334 10140 18369 9987 89 172 -263 C
ATOM 2781 NZ LYS A 334 -34.059 6.969 -38.769 1.00100.26 N
ANISOU 2781 NZ LYS A 334 9996 18224 9873 123 210 -244 N
ATOM 2782 N ASP A 335 -31.524 1.204 -40.734 1.00 90.62 N
ANISOU 2782 N ASP A 335 8999 16746 8685 -741 124 -745 N
ATOM 2783 CA ASP A 335 -30.859 0.839 -39.482 1.00 85.86 C
ANISOU 2783 CA ASP A 335 8573 15840 8209 -818 146 -756 C
ATOM 2784 C ASP A 335 -29.557 0.049 -39.672 1.00 80.70 C
ANISOU 2784 C ASP A 335 8072 14948 7643 -913 140 -791 C
ATOM 2785 O ASP A 335 -28.838 -0.223 -38.704 1.00 80.68 O
ANISOU 2785 O ASP A 335 8223 14683 7748 -960 155 -787 O
ATOM 2786 CB ASP A 335 -31.823 0.068 -38.579 1.00 88.87 C
ANISOU 2786 CB ASP A 335 8921 16280 8563 -976 177 -854 C
ATOM 2787 CG ASP A 335 -32.997 0.913 -38.126 1.00 91.27 C
ANISOU 2787 CG ASP A 335 9101 16769 8805 -873 188 -809 C
ATOM 2788 OD1 ASP A 335 -32.776 2.079 -37.726 1.00 92.40 O
ANISOU 2788 OD1 ASP A 335 9280 16830 8997 -695 190 -690 O
ATOM 2789 OD2 ASP A 335 -34.140 0.410 -38.166 1.00 92.59 O
ANISOU 2789 OD2 ASP A 335 9137 17166 8877 -974 201 -895 O
ATOM 2790 N ALA A 336 -29.257 -0.316 -40.912 1.00 75.06 N
ANISOU 2790 N ALA A 336 7311 14330 6878 -938 120 -825 N
ATOM 2791 CA ALA A 336 -28.005 -0.987 -41.224 1.00 69.55 C
ANISOU 2791 CA ALA A 336 6747 13419 6258 -1009 115 -852 C
ATOM 2792 C ALA A 336 -26.845 0.004 -41.261 1.00 66.31 C
ANISOU 2792 C ALA A 336 6441 12814 5937 -838 96 -726 C
ATOM 2793 O ALA A 336 -27.050 1.216 -41.369 1.00 64.85 O
ANISOU 2793 O ALA A 336 6205 12699 5735 -660 88 -622 O
ATOM 2794 CB ALA A 336 -28.117 -1.723 -42.547 1.00 67.69 C
ANISOU 2794 CB ALA A 336 6422 13361 5934 -1101 104 -938 C
ATOM 2795 N PHE A 337 -25.629 -0.522 -41.146 1.00 63.35 N
ANISOU 2795 N PHE A 337 6215 12194 5660 -893 96 -738 N
ATOM 2796 CA PHE A 337 -24.420 0.260 -41.381 1.00 61.01 C
ANISOU 2796 CA PHE A 337 6014 11725 5442 -756 79 -639 C
ATOM 2797 C PHE A 337 -23.998 0.125 -42.836 1.00 59.18 C
ANISOU 2797 C PHE A 337 5733 11590 5161 -741 57 -651 C
ATOM 2798 O PHE A 337 -23.804 -0.987 -43.331 1.00 59.07 O
ANISOU 2798 O PHE A 337 5728 11581 5134 -886 60 -749 O
ATOM 2799 CB PHE A 337 -23.279 -0.213 -40.470 1.00 59.36 C
ANISOU 2799 CB PHE A 337 5986 11204 5362 -817 88 -642 C
ATOM 2800 CG PHE A 337 -21.954 0.430 -40.780 1.00 57.96 C
ANISOU 2800 CG PHE A 337 5906 10851 5264 -702 72 -559 C
ATOM 2801 CD1 PHE A 337 -21.129 -0.087 -41.767 1.00 56.35 C
ANISOU 2801 CD1 PHE A 337 5730 10611 5068 -737 58 -589 C
ATOM 2802 CD2 PHE A 337 -21.537 1.561 -40.087 1.00 57.01 C
ANISOU 2802 CD2 PHE A 337 5848 10602 5208 -563 75 -456 C
ATOM 2803 CE1 PHE A 337 -19.925 0.516 -42.066 1.00 56.03 C
ANISOU 2803 CE1 PHE A 337 5773 10417 5098 -634 45 -516 C
ATOM 2804 CE2 PHE A 337 -20.328 2.164 -40.379 1.00 55.04 C
ANISOU 2804 CE2 PHE A 337 5686 10198 5029 -466 65 -387 C
ATOM 2805 CZ PHE A 337 -19.520 1.642 -41.366 1.00 54.61 C
ANISOU 2805 CZ PHE A 337 5654 10114 4981 -501 48 -415 C
ATOM 2806 N ILE A 338 -23.857 1.256 -43.521 1.00 58.09 N
ANISOU 2806 N ILE A 338 5547 11526 4997 -566 40 -551 N
ATOM 2807 CA ILE A 338 -23.323 1.269 -44.885 1.00 57.82 C
ANISOU 2807 CA ILE A 338 5481 11565 4924 -530 19 -544 C
ATOM 2808 C ILE A 338 -22.291 2.383 -45.031 1.00 56.19 C
ANISOU 2808 C ILE A 338 5358 11202 4789 -359 14 -422 C
ATOM 2809 O ILE A 338 -22.496 3.498 -44.553 1.00 57.14 O
ANISOU 2809 O ILE A 338 5477 11307 4926 -215 25 -325 O
ATOM 2810 CB ILE A 338 -24.422 1.461 -45.966 1.00 58.93 C
ANISOU 2810 CB ILE A 338 5429 12047 4912 -495 5 -556 C
ATOM 2811 CG1 ILE A 338 -25.628 0.548 -45.718 1.00 62.12 C
ANISOU 2811 CG1 ILE A 338 5731 12637 5234 -653 16 -672 C
ATOM 2812 CG2 ILE A 338 -23.861 1.172 -47.351 1.00 59.96 C
ANISOU 2812 CG2 ILE A 338 5533 12250 4999 -506 -13 -578 C
ATOM 2813 CD1 ILE A 338 -26.830 1.237 -45.091 1.00 63.23 C
ANISOU 2813 CD1 ILE A 338 5768 12935 5319 -576 25 -631 C
ATOM 2814 N HIS A 339 -21.182 2.074 -45.688 1.00 54.04 N
ANISOU 2814 N HIS A 339 5160 10811 4561 -378 3 -431 N
ATOM 2815 CA HIS A 339 -20.213 3.089 -46.063 1.00 55.06 C
ANISOU 2815 CA HIS A 339 5353 10823 4743 -224 0 -324 C
ATOM 2816 C HIS A 339 -19.471 2.638 -47.274 1.00 55.38 C
ANISOU 2816 C HIS A 339 5396 10877 4766 -256 -16 -355 C
ATOM 2817 O HIS A 339 -19.237 1.439 -47.461 1.00 56.20 O
ANISOU 2817 O HIS A 339 5523 10953 4876 -412 -19 -459 O
ATOM 2818 CB HIS A 339 -19.240 3.387 -44.907 1.00 54.62 C
ANISOU 2818 CB HIS A 339 5457 10471 4824 -203 13 -282 C
ATOM 2819 CG HIS A 339 -18.501 4.704 -45.056 1.00 53.00 C
ANISOU 2819 CG HIS A 339 5306 10164 4667 -27 23 -162 C
ATOM 2820 ND1 HIS A 339 -17.386 4.835 -45.822 1.00 52.10 N
ANISOU 2820 ND1 HIS A 339 5251 9955 4590 8 15 -137 N
ATOM 2821 CD2 HIS A 339 -18.764 5.971 -44.519 1.00 51.37 C
ANISOU 2821 CD2 HIS A 339 5103 9939 4476 120 48 -62 C
ATOM 2822 CE1 HIS A 339 -16.958 6.115 -45.771 1.00 52.13 C
ANISOU 2822 CE1 HIS A 339 5295 9881 4630 167 35 -29 C
ATOM 2823 NE2 HIS A 339 -17.804 6.809 -44.973 1.00 52.56 N
ANISOU 2823 NE2 HIS A 339 5317 9979 4672 235 58 16 N
ATOM 2824 N ARG A 340 -19.090 3.592 -48.118 1.00 57.26 N
ANISOU 2824 N ARG A 340 5615 11156 4983 -107 -21 -265 N
ATOM 2825 CA ARG A 340 -18.474 3.267 -49.399 1.00 58.35 C
ANISOU 2825 CA ARG A 340 5739 11341 5089 -123 -36 -288 C
ATOM 2826 C ARG A 340 -17.374 4.252 -49.790 1.00 56.98 C
ANISOU 2826 C ARG A 340 5646 11028 4976 20 -31 -184 C
ATOM 2827 O ARG A 340 -17.368 5.402 -49.351 1.00 54.88 O
ANISOU 2827 O ARG A 340 5405 10707 4740 163 -13 -80 O
ATOM 2828 CB ARG A 340 -19.549 3.182 -50.507 1.00 61.57 C
ANISOU 2828 CB ARG A 340 5972 12079 5341 -119 -51 -313 C
ATOM 2829 CG ARG A 340 -20.383 4.448 -50.672 1.00 64.54 C
ANISOU 2829 CG ARG A 340 6248 12632 5642 63 -47 -200 C
ATOM 2830 CD ARG A 340 -21.433 4.304 -51.769 1.00 72.04 C
ANISOU 2830 CD ARG A 340 7015 13925 6429 65 -65 -227 C
ATOM 2831 NE ARG A 340 -21.427 5.458 -52.671 1.00 72.55 N
ANISOU 2831 NE ARG A 340 7024 14109 6433 259 -66 -104 N
ATOM 2832 CZ ARG A 340 -20.525 5.644 -53.630 1.00 73.16 C
ANISOU 2832 CZ ARG A 340 7140 14143 6515 306 -71 -71 C
ATOM 2833 NH1 ARG A 340 -19.569 4.741 -53.831 1.00 74.50 N
ANISOU 2833 NH1 ARG A 340 7398 14161 6748 172 -79 -155 N
ATOM 2834 NH2 ARG A 340 -20.574 6.731 -54.390 1.00 74.26 N
ANISOU 2834 NH2 ARG A 340 7231 14389 6596 490 -65 48 N
ATOM 2835 N THR A 341 -16.427 3.776 -50.593 1.00 58.27 N
ANISOU 2835 N THR A 341 5853 11124 5159 -25 -41 -217 N
ATOM 2836 CA THR A 341 -15.545 4.646 -51.354 1.00 61.58 C
ANISOU 2836 CA THR A 341 6311 11486 5598 104 -37 -130 C
ATOM 2837 C THR A 341 -15.690 4.215 -52.801 1.00 68.09 C
ANISOU 2837 C THR A 341 7040 12511 6318 75 -55 -170 C
ATOM 2838 O THR A 341 -16.546 3.389 -53.118 1.00 71.98 O
ANISOU 2838 O THR A 341 7433 13192 6723 -32 -68 -259 O
ATOM 2839 CB THR A 341 -14.063 4.508 -50.933 1.00 59.37 C
ANISOU 2839 CB THR A 341 6189 10912 5454 78 -30 -130 C
ATOM 2840 OG1 THR A 341 -13.602 3.185 -51.221 1.00 60.55 O
ANISOU 2840 OG1 THR A 341 6367 11018 5621 -80 -43 -242 O
ATOM 2841 CG2 THR A 341 -13.873 4.801 -49.450 1.00 56.92 C
ANISOU 2841 CG2 THR A 341 5975 10405 5244 85 -14 -105 C
ATOM 2842 N VAL A 342 -14.853 4.757 -53.681 1.00 72.64 N
ANISOU 2842 N VAL A 342 7647 13052 6902 163 -53 -112 N
ATOM 2843 CA VAL A 342 -14.878 4.348 -55.087 1.00 77.25 C
ANISOU 2843 CA VAL A 342 8147 13816 7387 134 -69 -151 C
ATOM 2844 C VAL A 342 -14.508 2.871 -55.255 1.00 79.59 C
ANISOU 2844 C VAL A 342 8470 14066 7704 -62 -79 -293 C
ATOM 2845 O VAL A 342 -15.011 2.196 -56.158 1.00 80.27 O
ANISOU 2845 O VAL A 342 8457 14353 7687 -145 -90 -369 O
ATOM 2846 CB VAL A 342 -13.977 5.237 -55.982 1.00 78.07 C
ANISOU 2846 CB VAL A 342 8288 13873 7499 268 -60 -57 C
ATOM 2847 CG1 VAL A 342 -14.768 6.434 -56.490 1.00 77.98 C
ANISOU 2847 CG1 VAL A 342 8179 14059 7389 447 -51 60 C
ATOM 2848 CG2 VAL A 342 -12.718 5.680 -55.238 1.00 74.07 C
ANISOU 2848 CG2 VAL A 342 7943 13057 7143 307 -39 -11 C
ATOM 2849 N ASP A 343 -13.645 2.375 -54.369 1.00 78.36 N
ANISOU 2849 N ASP A 343 8448 13648 7677 -137 -69 -328 N
ATOM 2850 CA ASP A 343 -13.173 0.990 -54.440 1.00 76.96 C
ANISOU 2850 CA ASP A 343 8318 13387 7536 -312 -68 -452 C
ATOM 2851 C ASP A 343 -13.949 0.045 -53.502 1.00 75.95 C
ANISOU 2851 C ASP A 343 8182 13262 7412 -453 -60 -543 C
ATOM 2852 O ASP A 343 -13.923 -1.175 -53.684 1.00 75.93 O
ANISOU 2852 O ASP A 343 8187 13256 7406 -610 -51 -658 O
ATOM 2853 CB ASP A 343 -11.664 0.902 -54.132 1.00 76.15 C
ANISOU 2853 CB ASP A 343 8366 12997 7569 -311 -59 -439 C
ATOM 2854 CG ASP A 343 -10.870 2.112 -54.643 1.00 77.27 C
ANISOU 2854 CG ASP A 343 8541 13083 7733 -150 -58 -326 C
ATOM 2855 OD1 ASP A 343 -11.270 2.721 -55.658 1.00 79.63 O
ANISOU 2855 OD1 ASP A 343 8749 13570 7935 -64 -63 -279 O
ATOM 2856 OD2 ASP A 343 -9.830 2.443 -54.026 1.00 72.91 O
ANISOU 2856 OD2 ASP A 343 8106 12299 7295 -111 -49 -284 O
ATOM 2857 N ASP A 344 -14.646 0.609 -52.515 1.00 72.98 N
ANISOU 2857 N ASP A 344 7792 12892 7042 -399 -58 -493 N
ATOM 2858 CA ASP A 344 -15.037 -0.156 -51.328 1.00 66.56 C
ANISOU 2858 CA ASP A 344 7021 11991 6276 -516 -46 -558 C
ATOM 2859 C ASP A 344 -16.489 -0.020 -50.967 1.00 64.80 C
ANISOU 2859 C ASP A 344 6684 11973 5964 -523 -46 -568 C
ATOM 2860 O ASP A 344 -17.037 1.075 -50.996 1.00 67.02 O
ANISOU 2860 O ASP A 344 6897 12367 6197 -383 -53 -476 O
ATOM 2861 CB ASP A 344 -14.226 0.301 -50.127 1.00 63.96 C
ANISOU 2861 CB ASP A 344 6828 11396 6078 -460 -39 -493 C
ATOM 2862 CG ASP A 344 -12.830 -0.228 -50.135 1.00 64.90 C
ANISOU 2862 CG ASP A 344 7073 11287 6300 -504 -35 -515 C
ATOM 2863 OD1 ASP A 344 -12.649 -1.437 -50.397 1.00 64.51 O
ANISOU 2863 OD1 ASP A 344 7041 11213 6253 -643 -26 -615 O
ATOM 2864 OD2 ASP A 344 -11.908 0.568 -49.853 1.00 67.63 O
ANISOU 2864 OD2 ASP A 344 7500 11473 6724 -399 -36 -433 O
ATOM 2865 N TYR A 345 -17.095 -1.138 -50.582 1.00 62.96 N
ANISOU 2865 N TYR A 345 6433 11778 5712 -687 -33 -679 N
ATOM 2866 CA TYR A 345 -18.369 -1.127 -49.881 1.00 62.43 C
ANISOU 2866 CA TYR A 345 6284 11845 5588 -715 -27 -698 C
ATOM 2867 C TYR A 345 -18.237 -1.883 -48.564 1.00 57.09 C
ANISOU 2867 C TYR A 345 5717 10969 5006 -828 -4 -748 C
ATOM 2868 O TYR A 345 -17.620 -2.946 -48.505 1.00 56.05 O
ANISOU 2868 O TYR A 345 5669 10698 4928 -956 12 -827 O
ATOM 2869 CB TYR A 345 -19.461 -1.761 -50.743 1.00 69.75 C
ANISOU 2869 CB TYR A 345 7060 13065 6376 -817 -28 -794 C
ATOM 2870 CG TYR A 345 -20.318 -0.776 -51.515 1.00 74.40 C
ANISOU 2870 CG TYR A 345 7493 13934 6840 -682 -50 -725 C
ATOM 2871 CD1 TYR A 345 -21.583 -0.409 -51.051 1.00 76.90 C
ANISOU 2871 CD1 TYR A 345 7701 14434 7083 -654 -50 -712 C
ATOM 2872 CD2 TYR A 345 -19.880 -0.233 -52.723 1.00 77.08 C
ANISOU 2872 CD2 TYR A 345 7793 14363 7131 -582 -68 -672 C
ATOM 2873 CE1 TYR A 345 -22.376 0.484 -51.758 1.00 79.70 C
ANISOU 2873 CE1 TYR A 345 7909 15053 7320 -521 -69 -643 C
ATOM 2874 CE2 TYR A 345 -20.667 0.662 -53.439 1.00 78.99 C
ANISOU 2874 CE2 TYR A 345 7892 14866 7253 -450 -86 -600 C
ATOM 2875 CZ TYR A 345 -21.912 1.016 -52.953 1.00 80.70 C
ANISOU 2875 CZ TYR A 345 8000 15261 7398 -416 -86 -584 C
ATOM 2876 OH TYR A 345 -22.697 1.903 -53.662 1.00 84.97 O
ANISOU 2876 OH TYR A 345 8398 16069 7818 -274 -102 -506 O
ATOM 2877 N PHE A 346 -18.820 -1.331 -47.510 1.00 53.95 N
ANISOU 2877 N PHE A 346 5317 10557 4623 -777 -1 -699 N
ATOM 2878 CA PHE A 346 -18.754 -1.940 -46.187 1.00 51.45 C
ANISOU 2878 CA PHE A 346 5100 10059 4388 -870 20 -734 C
ATOM 2879 C PHE A 346 -20.120 -1.883 -45.546 1.00 51.55 C
ANISOU 2879 C PHE A 346 5021 10230 4335 -900 30 -755 C
ATOM 2880 O PHE A 346 -20.666 -0.803 -45.330 1.00 53.17 O
ANISOU 2880 O PHE A 346 5165 10526 4509 -769 20 -672 O
ATOM 2881 CB PHE A 346 -17.711 -1.219 -45.316 1.00 49.83 C
ANISOU 2881 CB PHE A 346 5028 9599 4304 -765 16 -637 C
ATOM 2882 CG PHE A 346 -17.496 -1.845 -43.955 1.00 47.95 C
ANISOU 2882 CG PHE A 346 4901 9163 4151 -854 35 -665 C
ATOM 2883 CD1 PHE A 346 -17.575 -3.225 -43.776 1.00 47.62 C
ANISOU 2883 CD1 PHE A 346 4896 9078 4118 -1027 59 -773 C
ATOM 2884 CD2 PHE A 346 -17.166 -1.048 -42.860 1.00 46.05 C
ANISOU 2884 CD2 PHE A 346 4736 8775 3985 -763 34 -583 C
ATOM 2885 CE1 PHE A 346 -17.362 -3.792 -42.524 1.00 48.26 C
ANISOU 2885 CE1 PHE A 346 5084 8976 4274 -1099 79 -789 C
ATOM 2886 CE2 PHE A 346 -16.939 -1.609 -41.608 1.00 46.68 C
ANISOU 2886 CE2 PHE A 346 4918 8680 4138 -840 50 -603 C
ATOM 2887 CZ PHE A 346 -17.041 -2.981 -41.436 1.00 47.21 C
ANISOU 2887 CZ PHE A 346 5019 8708 4209 -1004 71 -702 C
ATOM 2888 N PHE A 347 -20.668 -3.053 -45.237 1.00 51.58 N
ANISOU 2888 N PHE A 347 5018 10260 4317 -1074 55 -868 N
ATOM 2889 CA PHE A 347 -22.060 -3.164 -44.822 1.00 52.23 C
ANISOU 2889 CA PHE A 347 4992 10533 4318 -1131 68 -912 C
ATOM 2890 C PHE A 347 -22.174 -4.060 -43.597 1.00 51.77 C
ANISOU 2890 C PHE A 347 5026 10320 4321 -1269 103 -975 C
ATOM 2891 O PHE A 347 -21.614 -5.155 -43.572 1.00 52.85 O
ANISOU 2891 O PHE A 347 5253 10321 4506 -1400 128 -1050 O
ATOM 2892 CB PHE A 347 -22.912 -3.719 -45.992 1.00 54.21 C
ANISOU 2892 CB PHE A 347 5092 11067 4436 -1222 69 -1008 C
ATOM 2893 CG PHE A 347 -24.364 -3.928 -45.650 1.00 55.50 C
ANISOU 2893 CG PHE A 347 5131 11450 4505 -1297 84 -1069 C
ATOM 2894 CD1 PHE A 347 -24.796 -5.120 -45.062 1.00 56.69 C
ANISOU 2894 CD1 PHE A 347 5311 11567 4660 -1491 126 -1187 C
ATOM 2895 CD2 PHE A 347 -25.299 -2.940 -45.911 1.00 56.29 C
ANISOU 2895 CD2 PHE A 347 5086 11790 4511 -1172 61 -1008 C
ATOM 2896 CE1 PHE A 347 -26.130 -5.316 -44.742 1.00 57.86 C
ANISOU 2896 CE1 PHE A 347 5342 11919 4720 -1567 143 -1249 C
ATOM 2897 CE2 PHE A 347 -26.639 -3.136 -45.605 1.00 59.40 C
ANISOU 2897 CE2 PHE A 347 5356 12397 4814 -1240 75 -1066 C
ATOM 2898 CZ PHE A 347 -27.054 -4.325 -45.018 1.00 59.37 C
ANISOU 2898 CZ PHE A 347 5380 12361 4816 -1442 115 -1190 C
ATOM 2899 N CYS A 348 -22.899 -3.592 -42.585 1.00 51.77 N
ANISOU 2899 N CYS A 348 5007 10341 4320 -1235 109 -941 N
ATOM 2900 CA CYS A 348 -23.124 -4.369 -41.371 1.00 52.71 C
ANISOU 2900 CA CYS A 348 5207 10332 4488 -1360 144 -993 C
ATOM 2901 C CYS A 348 -24.577 -4.297 -40.931 1.00 54.75 C
ANISOU 2901 C CYS A 348 5347 10794 4661 -1401 158 -1030 C
ATOM 2902 O CYS A 348 -25.257 -3.293 -41.169 1.00 54.91 O
ANISOU 2902 O CYS A 348 5250 10994 4616 -1278 137 -970 O
ATOM 2903 CB CYS A 348 -22.230 -3.881 -40.227 1.00 51.27 C
ANISOU 2903 CB CYS A 348 5169 9884 4424 -1278 139 -904 C
ATOM 2904 SG CYS A 348 -20.474 -3.863 -40.629 1.00 51.04 S
ANISOU 2904 SG CYS A 348 5278 9614 4500 -1218 121 -853 S
ATOM 2905 N SER A 349 -25.033 -5.370 -40.282 1.00 54.66 N
ANISOU 2905 N SER A 349 5368 10749 4652 -1572 200 -1126 N
ATOM 2906 CA SER A 349 -26.354 -5.449 -39.680 1.00 56.60 C
ANISOU 2906 CA SER A 349 5520 11154 4829 -1635 222 -1171 C
ATOM 2907 C SER A 349 -26.348 -6.585 -38.669 1.00 57.63 C
ANISOU 2907 C SER A 349 5764 11118 5014 -1804 273 -1247 C
ATOM 2908 O SER A 349 -25.610 -7.562 -38.838 1.00 57.06 O
ANISOU 2908 O SER A 349 5794 10893 4991 -1908 298 -1301 O
ATOM 2909 CB SER A 349 -27.427 -5.715 -40.752 1.00 58.52 C
ANISOU 2909 CB SER A 349 5584 11717 4934 -1703 224 -1258 C
ATOM 2910 OG SER A 349 -28.660 -6.119 -40.166 1.00 58.64 O
ANISOU 2910 OG SER A 349 5520 11874 4885 -1815 257 -1334 O
ATOM 2911 N PRO A 350 -27.171 -6.468 -37.612 1.00 59.28 N
ANISOU 2911 N PRO A 350 5957 11353 5213 -1829 294 -1248 N
ATOM 2912 CA PRO A 350 -27.366 -7.599 -36.696 1.00 61.33 C
ANISOU 2912 CA PRO A 350 6306 11490 5504 -2002 350 -1329 C
ATOM 2913 C PRO A 350 -28.123 -8.753 -37.367 1.00 64.49 C
ANISOU 2913 C PRO A 350 6631 12051 5821 -2196 396 -1476 C
ATOM 2914 O PRO A 350 -28.184 -9.853 -36.817 1.00 65.32 O
ANISOU 2914 O PRO A 350 6822 12045 5953 -2359 454 -1556 O
ATOM 2915 CB PRO A 350 -28.208 -6.997 -35.566 1.00 60.64 C
ANISOU 2915 CB PRO A 350 6186 11446 5406 -1963 356 -1291 C
ATOM 2916 CG PRO A 350 -28.891 -5.816 -36.178 1.00 59.77 C
ANISOU 2916 CG PRO A 350 5913 11578 5216 -1818 314 -1237 C
ATOM 2917 CD PRO A 350 -27.935 -5.274 -37.197 1.00 59.26 C
ANISOU 2917 CD PRO A 350 5859 11484 5173 -1693 271 -1172 C
ATOM 2918 N HIS A 351 -28.684 -8.490 -38.550 1.00 67.13 N
ANISOU 2918 N HIS A 351 6807 12646 6053 -2179 373 -1511 N
ATOM 2919 CA HIS A 351 -29.461 -9.489 -39.296 1.00 68.96 C
ANISOU 2919 CA HIS A 351 6943 13069 6188 -2363 414 -1658 C
ATOM 2920 C HIS A 351 -28.623 -10.126 -40.372 1.00 69.99 C
ANISOU 2920 C HIS A 351 7115 13145 6330 -2416 418 -1706 C
ATOM 2921 O HIS A 351 -28.377 -9.520 -41.423 1.00 70.86 O
ANISOU 2921 O HIS A 351 7146 13378 6398 -2311 371 -1668 O
ATOM 2922 CB HIS A 351 -30.741 -8.871 -39.870 1.00 69.45 C
ANISOU 2922 CB HIS A 351 6787 13486 6112 -2327 389 -1679 C
ATOM 2923 CG HIS A 351 -31.584 -8.152 -38.836 1.00 70.01 C
ANISOU 2923 CG HIS A 351 6808 13620 6171 -2258 385 -1626 C
ATOM 2924 ND1 HIS A 351 -32.101 -8.779 -37.754 1.00 70.88 N
ANISOU 2924 ND1 HIS A 351 6970 13659 6302 -2387 437 -1683 N
ATOM 2925 CD2 HIS A 351 -31.969 -6.814 -38.736 1.00 70.01 C
ANISOU 2925 CD2 HIS A 351 6714 13741 6143 -2065 337 -1515 C
ATOM 2926 CE1 HIS A 351 -32.780 -7.889 -37.002 1.00 70.50 C
ANISOU 2926 CE1 HIS A 351 6861 13687 6238 -2284 421 -1615 C
ATOM 2927 NE2 HIS A 351 -32.701 -6.688 -37.604 1.00 71.21 N
ANISOU 2927 NE2 HIS A 351 6862 13893 6299 -2085 362 -1513 N
ATOM 2928 N PRO A 352 -28.157 -11.364 -40.119 1.00 70.46 N
ANISOU 2928 N PRO A 352 7307 13015 6448 -2577 481 -1788 N
ATOM 2929 CA PRO A 352 -27.190 -12.026 -40.997 1.00 69.55 C
ANISOU 2929 CA PRO A 352 7265 12791 6367 -2624 495 -1827 C
ATOM 2930 C PRO A 352 -27.702 -12.148 -42.423 1.00 72.07 C
ANISOU 2930 C PRO A 352 7428 13387 6568 -2677 487 -1914 C
ATOM 2931 O PRO A 352 -26.923 -11.999 -43.365 1.00 70.46 O
ANISOU 2931 O PRO A 352 7230 13167 6372 -2615 458 -1891 O
ATOM 2932 CB PRO A 352 -27.029 -13.420 -40.372 1.00 70.49 C
ANISOU 2932 CB PRO A 352 7524 12712 6544 -2815 584 -1921 C
ATOM 2933 CG PRO A 352 -27.554 -13.299 -38.981 1.00 70.43 C
ANISOU 2933 CG PRO A 352 7558 12636 6565 -2821 602 -1888 C
ATOM 2934 CD PRO A 352 -28.617 -12.248 -39.033 1.00 70.79 C
ANISOU 2934 CD PRO A 352 7427 12952 6516 -2731 552 -1856 C
ATOM 2935 N HIS A 353 -29.006 -12.397 -42.580 1.00 74.08 N
ANISOU 2935 N HIS A 353 7536 13902 6706 -2790 511 -2013 N
ATOM 2936 CA HIS A 353 -29.591 -12.572 -43.910 1.00 77.01 C
ANISOU 2936 CA HIS A 353 7744 14565 6948 -2858 506 -2108 C
ATOM 2937 C HIS A 353 -29.458 -11.334 -44.760 1.00 76.88 C
ANISOU 2937 C HIS A 353 7613 14717 6880 -2654 421 -2002 C
ATOM 2938 O HIS A 353 -29.262 -11.433 -45.972 1.00 78.44 O
ANISOU 2938 O HIS A 353 7742 15043 7016 -2665 406 -2042 O
ATOM 2939 CB HIS A 353 -31.043 -13.071 -43.837 1.00 78.66 C
ANISOU 2939 CB HIS A 353 7813 15034 7040 -3023 551 -2238 C
ATOM 2940 CG HIS A 353 -32.061 -11.987 -43.545 1.00 80.30 C
ANISOU 2940 CG HIS A 353 7862 15479 7168 -2899 499 -2171 C
ATOM 2941 ND1 HIS A 353 -32.511 -11.727 -42.296 1.00 81.88 N
ANISOU 2941 ND1 HIS A 353 8095 15607 7407 -2877 510 -2128 N
ATOM 2942 CD2 HIS A 353 -32.723 -11.097 -44.395 1.00 79.11 C
ANISOU 2942 CD2 HIS A 353 7513 15649 6896 -2785 438 -2138 C
ATOM 2943 CE1 HIS A 353 -33.406 -10.721 -42.344 1.00 82.02 C
ANISOU 2943 CE1 HIS A 353 7947 15879 7336 -2755 461 -2072 C
ATOM 2944 NE2 HIS A 353 -33.532 -10.335 -43.629 1.00 80.74 N
ANISOU 2944 NE2 HIS A 353 7643 15956 7076 -2695 418 -2075 N
ATOM 2945 N LYS A 354 -29.528 -10.158 -44.133 1.00 75.19 N
ANISOU 2945 N LYS A 354 7384 14492 6692 -2467 369 -1865 N
ATOM 2946 CA LYS A 354 -29.320 -8.896 -44.855 1.00 75.89 C
ANISOU 2946 CA LYS A 354 7385 14703 6744 -2253 295 -1745 C
ATOM 2947 C LYS A 354 -27.888 -8.764 -45.402 1.00 74.85 C
ANISOU 2947 C LYS A 354 7374 14365 6700 -2167 272 -1680 C
ATOM 2948 O LYS A 354 -27.661 -8.094 -46.415 1.00 73.63 O
ANISOU 2948 O LYS A 354 7142 14338 6495 -2049 226 -1627 O
ATOM 2949 CB LYS A 354 -29.653 -7.692 -43.973 1.00 75.76 C
ANISOU 2949 CB LYS A 354 7349 14686 6751 -2075 260 -1614 C
ATOM 2950 CG LYS A 354 -31.126 -7.515 -43.665 1.00 76.25 C
ANISOU 2950 CG LYS A 354 7251 15016 6706 -2109 268 -1656 C
ATOM 2951 CD LYS A 354 -31.384 -6.150 -43.050 1.00 76.98 C
ANISOU 2951 CD LYS A 354 7307 15127 6811 -1897 229 -1512 C
ATOM 2952 CE LYS A 354 -32.443 -6.216 -41.960 1.00 80.30 C
ANISOU 2952 CE LYS A 354 7686 15611 7211 -1957 259 -1543 C
ATOM 2953 NZ LYS A 354 -33.802 -6.523 -42.490 1.00 84.43 N
ANISOU 2953 NZ LYS A 354 8008 16487 7583 -2056 270 -1648 N
ATOM 2954 N VAL A 355 -26.931 -9.405 -44.734 1.00 73.68 N
ANISOU 2954 N VAL A 355 7412 13903 6679 -2224 305 -1682 N
ATOM 2955 CA VAL A 355 -25.539 -9.382 -45.192 1.00 73.48 C
ANISOU 2955 CA VAL A 355 7506 13671 6741 -2156 288 -1630 C
ATOM 2956 C VAL A 355 -25.334 -10.284 -46.423 1.00 74.17 C
ANISOU 2956 C VAL A 355 7564 13838 6777 -2285 314 -1745 C
ATOM 2957 O VAL A 355 -24.434 -10.044 -47.223 1.00 74.12 O
ANISOU 2957 O VAL A 355 7588 13780 6795 -2209 287 -1705 O
ATOM 2958 CB VAL A 355 -24.539 -9.711 -44.055 1.00 70.02 C
ANISOU 2958 CB VAL A 355 7271 12879 6453 -2155 311 -1583 C
ATOM 2959 CG1 VAL A 355 -23.108 -9.538 -44.529 1.00 67.58 C
ANISOU 2959 CG1 VAL A 355 7070 12377 6230 -2063 287 -1518 C
ATOM 2960 CG2 VAL A 355 -24.790 -8.811 -42.851 1.00 68.36 C
ANISOU 2960 CG2 VAL A 355 7081 12607 6284 -2037 288 -1478 C
ATOM 2961 N TYR A 356 -26.187 -11.299 -46.579 1.00 78.30 N
ANISOU 2961 N TYR A 356 8027 14494 7226 -2485 370 -1893 N
ATOM 2962 CA TYR A 356 -26.252 -12.069 -47.833 1.00 80.31 C
ANISOU 2962 CA TYR A 356 8216 14895 7401 -2617 397 -2017 C
ATOM 2963 C TYR A 356 -26.955 -11.269 -48.914 1.00 79.31 C
ANISOU 2963 C TYR A 356 7887 15114 7132 -2533 341 -2003 C
ATOM 2964 O TYR A 356 -26.422 -11.096 -50.010 1.00 78.56 O
ANISOU 2964 O TYR A 356 7760 15080 7006 -2485 314 -1994 O
ATOM 2965 CB TYR A 356 -26.971 -13.411 -47.644 1.00 85.83 C
ANISOU 2965 CB TYR A 356 8916 15631 8063 -2870 485 -2189 C
ATOM 2966 CG TYR A 356 -26.287 -14.345 -46.680 1.00 90.01 C
ANISOU 2966 CG TYR A 356 9650 15824 8726 -2966 553 -2211 C
ATOM 2967 CD1 TYR A 356 -25.198 -15.121 -47.078 1.00 92.64 C
ANISOU 2967 CD1 TYR A 356 10117 15943 9138 -3022 593 -2246 C
ATOM 2968 CD2 TYR A 356 -26.728 -14.452 -45.364 1.00 92.74 C
ANISOU 2968 CD2 TYR A 356 10054 16066 9116 -2995 581 -2194 C
ATOM 2969 CE1 TYR A 356 -24.562 -15.974 -46.183 1.00 94.83 C
ANISOU 2969 CE1 TYR A 356 10582 15913 9535 -3097 658 -2256 C
ATOM 2970 CE2 TYR A 356 -26.105 -15.301 -44.460 1.00 95.52 C
ANISOU 2970 CE2 TYR A 356 10594 16114 9585 -3074 644 -2206 C
ATOM 2971 CZ TYR A 356 -25.024 -16.061 -44.868 1.00 96.04 C
ANISOU 2971 CZ TYR A 356 10790 15971 9726 -3121 683 -2234 C
ATOM 2972 OH TYR A 356 -24.413 -16.898 -43.955 1.00 95.52 O
ANISOU 2972 OH TYR A 356 10911 15608 9774 -3188 749 -2236 O
ATOM 2973 N ASP A 357 -28.156 -10.781 -48.602 1.00 79.57 N
ANISOU 2973 N ASP A 357 7779 15379 7074 -2512 324 -1999 N
ATOM 2974 CA ASP A 357 -28.914 -9.952 -49.542 1.00 79.95 C
ANISOU 2974 CA ASP A 357 7623 15774 6978 -2413 270 -1971 C
ATOM 2975 C ASP A 357 -28.033 -8.829 -50.082 1.00 76.94 C
ANISOU 2975 C ASP A 357 7262 15341 6631 -2185 204 -1819 C
ATOM 2976 O ASP A 357 -28.209 -8.389 -51.217 1.00 77.78 O
ANISOU 2976 O ASP A 357 7240 15680 6633 -2119 167 -1806 O
ATOM 2977 CB ASP A 357 -30.185 -9.382 -48.893 1.00 81.20 C
ANISOU 2977 CB ASP A 357 7651 16137 7063 -2373 256 -1949 C
ATOM 2978 CG ASP A 357 -31.147 -10.472 -48.412 1.00 82.97 C
ANISOU 2978 CG ASP A 357 7839 16443 7240 -2606 324 -2107 C
ATOM 2979 OD1 ASP A 357 -30.941 -11.655 -48.761 1.00 83.14 O
ANISOU 2979 OD1 ASP A 357 7913 16409 7264 -2804 383 -2244 O
ATOM 2980 OD2 ASP A 357 -32.106 -10.142 -47.673 1.00 82.12 O
ANISOU 2980 OD2 ASP A 357 7656 16450 7095 -2593 324 -2096 O
ATOM 2981 N PHE A 358 -27.065 -8.391 -49.277 1.00 72.42 N
ANISOU 2981 N PHE A 358 6851 14463 6201 -2071 194 -1706 N
ATOM 2982 CA PHE A 358 -26.109 -7.392 -49.735 1.00 68.83 C
ANISOU 2982 CA PHE A 358 6438 13922 5792 -1870 143 -1569 C
ATOM 2983 C PHE A 358 -24.997 -7.976 -50.593 1.00 68.08 C
ANISOU 2983 C PHE A 358 6428 13699 5740 -1920 153 -1609 C
ATOM 2984 O PHE A 358 -24.679 -7.423 -51.643 1.00 68.61 O
ANISOU 2984 O PHE A 358 6434 13878 5755 -1820 116 -1562 O
ATOM 2985 CB PHE A 358 -25.506 -6.589 -48.584 1.00 66.03 C
ANISOU 2985 CB PHE A 358 6211 13311 5565 -1722 128 -1433 C
ATOM 2986 CG PHE A 358 -24.671 -5.433 -49.051 1.00 62.64 C
ANISOU 2986 CG PHE A 358 5804 12823 5169 -1511 80 -1292 C
ATOM 2987 CD1 PHE A 358 -23.334 -5.610 -49.366 1.00 59.77 C
ANISOU 2987 CD1 PHE A 358 5573 12236 4900 -1493 79 -1269 C
ATOM 2988 CD2 PHE A 358 -25.244 -4.186 -49.244 1.00 61.65 C
ANISOU 2988 CD2 PHE A 358 5565 12881 4977 -1332 43 -1184 C
ATOM 2989 CE1 PHE A 358 -22.579 -4.556 -49.835 1.00 59.64 C
ANISOU 2989 CE1 PHE A 358 5576 12174 4910 -1309 41 -1146 C
ATOM 2990 CE2 PHE A 358 -24.493 -3.126 -49.701 1.00 59.93 C
ANISOU 2990 CE2 PHE A 358 5374 12607 4788 -1142 10 -1056 C
ATOM 2991 CZ PHE A 358 -23.159 -3.311 -50.001 1.00 59.79 C
ANISOU 2991 CZ PHE A 358 5488 12363 4863 -1135 9 -1039 C
ATOM 2992 N GLU A 359 -24.389 -9.073 -50.142 1.00 69.20 N
ANISOU 2992 N GLU A 359 6714 13603 5975 -2067 205 -1689 N
ATOM 2993 CA GLU A 359 -23.347 -9.724 -50.936 1.00 73.06 C
ANISOU 2993 CA GLU A 359 7287 13965 6506 -2126 223 -1736 C
ATOM 2994 C GLU A 359 -23.839 -10.082 -52.345 1.00 75.58 C
ANISOU 2994 C GLU A 359 7460 14569 6686 -2213 225 -1838 C
ATOM 2995 O GLU A 359 -23.201 -9.720 -53.339 1.00 77.02 O
ANISOU 2995 O GLU A 359 7627 14786 6850 -2133 195 -1801 O
ATOM 2996 CB GLU A 359 -22.780 -10.963 -50.237 1.00 74.08 C
ANISOU 2996 CB GLU A 359 7582 13818 6744 -2284 292 -1818 C
ATOM 2997 CG GLU A 359 -21.585 -11.562 -50.980 1.00 75.70 C
ANISOU 2997 CG GLU A 359 7889 13863 7011 -2321 312 -1851 C
ATOM 2998 CD GLU A 359 -20.953 -12.747 -50.270 1.00 78.10 C
ANISOU 2998 CD GLU A 359 8366 13879 7429 -2454 384 -1916 C
ATOM 2999 OE1 GLU A 359 -21.631 -13.382 -49.429 1.00 80.04 O
ANISOU 2999 OE1 GLU A 359 8634 14099 7678 -2575 433 -1980 O
ATOM 3000 OE2 GLU A 359 -19.770 -13.046 -50.563 1.00 79.27 O
ANISOU 3000 OE2 GLU A 359 8628 13826 7662 -2435 394 -1901 O
ATOM 3001 N LEU A 360 -24.970 -10.782 -52.424 1.00 78.06 N
ANISOU 3001 N LEU A 360 7668 15092 6898 -2379 262 -1969 N
ATOM 3002 CA LEU A 360 -25.534 -11.182 -53.716 1.00 81.43 C
ANISOU 3002 CA LEU A 360 7944 15814 7180 -2483 268 -2082 C
ATOM 3003 C LEU A 360 -25.855 -9.967 -54.590 1.00 79.48 C
ANISOU 3003 C LEU A 360 7539 15838 6822 -2299 192 -1981 C
ATOM 3004 O LEU A 360 -25.466 -9.923 -55.749 1.00 79.76 O
ANISOU 3004 O LEU A 360 7529 15974 6801 -2282 175 -1993 O
ATOM 3005 CB LEU A 360 -26.773 -12.067 -53.530 1.00 86.42 C
ANISOU 3005 CB LEU A 360 8480 16637 7718 -2693 322 -2239 C
ATOM 3006 CG LEU A 360 -26.569 -13.563 -53.239 1.00 88.49 C
ANISOU 3006 CG LEU A 360 8863 16718 8039 -2934 418 -2394 C
ATOM 3007 CD1 LEU A 360 -26.008 -13.811 -51.844 1.00 87.96 C
ANISOU 3007 CD1 LEU A 360 8988 16298 8133 -2925 451 -2340 C
ATOM 3008 CD2 LEU A 360 -27.882 -14.305 -53.405 1.00 91.20 C
ANISOU 3008 CD2 LEU A 360 9068 17329 8252 -3139 468 -2558 C
ATOM 3009 N LEU A 361 -26.529 -8.973 -54.012 1.00 78.66 N
ANISOU 3009 N LEU A 361 7360 15837 6690 -2156 152 -1876 N
ATOM 3010 CA LEU A 361 -26.869 -7.737 -54.727 1.00 77.48 C
ANISOU 3010 CA LEU A 361 7067 15930 6440 -1959 86 -1761 C
ATOM 3011 C LEU A 361 -25.649 -7.026 -55.320 1.00 77.72 C
ANISOU 3011 C LEU A 361 7179 15815 6533 -1793 51 -1641 C
ATOM 3012 O LEU A 361 -25.670 -6.630 -56.489 1.00 78.68 O
ANISOU 3012 O LEU A 361 7196 16144 6554 -1726 19 -1621 O
ATOM 3013 CB LEU A 361 -27.646 -6.780 -53.811 1.00 77.40 C
ANISOU 3013 CB LEU A 361 7001 15983 6423 -1820 60 -1655 C
ATOM 3014 CG LEU A 361 -27.748 -5.291 -54.179 1.00 77.73 C
ANISOU 3014 CG LEU A 361 6956 16159 6416 -1562 1 -1486 C
ATOM 3015 CD1 LEU A 361 -28.486 -5.079 -55.493 1.00 79.87 C
ANISOU 3015 CD1 LEU A 361 7021 16819 6504 -1541 -27 -1511 C
ATOM 3016 CD2 LEU A 361 -28.424 -4.509 -53.063 1.00 77.02 C
ANISOU 3016 CD2 LEU A 361 6847 16066 6350 -1450 -5 -1396 C
ATOM 3017 N ILE A 362 -24.597 -6.860 -54.513 1.00 74.89 N
ANISOU 3017 N ILE A 362 7006 15111 6338 -1727 57 -1563 N
ATOM 3018 CA ILE A 362 -23.428 -6.088 -54.920 1.00 72.89 C
ANISOU 3018 CA ILE A 362 6837 14702 6156 -1561 26 -1441 C
ATOM 3019 C ILE A 362 -22.663 -6.800 -56.031 1.00 73.05 C
ANISOU 3019 C ILE A 362 6885 14705 6165 -1653 40 -1521 C
ATOM 3020 O ILE A 362 -22.027 -6.158 -56.863 1.00 73.37 O
ANISOU 3020 O ILE A 362 6920 14763 6193 -1528 9 -1444 O
ATOM 3021 CB ILE A 362 -22.502 -5.757 -53.705 1.00 73.25 C
ANISOU 3021 CB ILE A 362 7068 14388 6374 -1479 31 -1346 C
ATOM 3022 CG1 ILE A 362 -21.899 -4.346 -53.823 1.00 71.61 C
ANISOU 3022 CG1 ILE A 362 6883 14122 6203 -1240 -10 -1175 C
ATOM 3023 CG2 ILE A 362 -21.433 -6.828 -53.494 1.00 71.42 C
ANISOU 3023 CG2 ILE A 362 7001 13871 6261 -1610 71 -1421 C
ATOM 3024 CD1 ILE A 362 -20.504 -4.294 -54.406 1.00 71.05 C
ANISOU 3024 CD1 ILE A 362 6924 13860 6212 -1192 -16 -1138 C
ATOM 3025 N LYS A 363 -22.736 -8.129 -56.044 1.00 75.01 N
ANISOU 3025 N LYS A 363 7166 14915 6417 -1871 92 -1678 N
ATOM 3026 CA LYS A 363 -22.134 -8.920 -57.117 1.00 79.59 C
ANISOU 3026 CA LYS A 363 7763 15499 6976 -1983 116 -1776 C
ATOM 3027 C LYS A 363 -22.890 -8.751 -58.429 1.00 81.85 C
ANISOU 3027 C LYS A 363 7855 16160 7082 -1994 92 -1822 C
ATOM 3028 O LYS A 363 -22.303 -8.852 -59.510 1.00 85.78 O
ANISOU 3028 O LYS A 363 8344 16699 7547 -1995 87 -1842 O
ATOM 3029 CB LYS A 363 -22.070 -10.398 -56.734 1.00 81.85 C
ANISOU 3029 CB LYS A 363 8141 15642 7316 -2217 192 -1935 C
ATOM 3030 CG LYS A 363 -20.743 -10.821 -56.130 1.00 83.88 C
ANISOU 3030 CG LYS A 363 8610 15512 7749 -2218 222 -1908 C
ATOM 3031 CD LYS A 363 -20.870 -12.151 -55.408 1.00 85.87 C
ANISOU 3031 CD LYS A 363 8958 15609 8060 -2423 302 -2037 C
ATOM 3032 CE LYS A 363 -19.531 -12.602 -54.853 1.00 85.48 C
ANISOU 3032 CE LYS A 363 9113 15186 8178 -2415 332 -2006 C
ATOM 3033 NZ LYS A 363 -19.713 -13.519 -53.693 1.00 86.56 N
ANISOU 3033 NZ LYS A 363 9358 15138 8392 -2545 397 -2067 N
ATOM 3034 N GLY A 364 -24.196 -8.504 -58.326 1.00 83.52 N
ANISOU 3034 N GLY A 364 7908 16652 7172 -2002 77 -1840 N
ATOM 3035 CA GLY A 364 -25.039 -8.250 -59.494 1.00 83.63 C
ANISOU 3035 CA GLY A 364 7717 17060 6999 -1996 47 -1872 C
ATOM 3036 C GLY A 364 -24.762 -6.897 -60.125 1.00 83.78 C
ANISOU 3036 C GLY A 364 7679 17175 6977 -1749 -15 -1703 C
ATOM 3037 O GLY A 364 -24.817 -6.752 -61.346 1.00 86.67 O
ANISOU 3037 O GLY A 364 7937 17766 7224 -1729 -37 -1715 O
ATOM 3038 N VAL A 365 -24.453 -5.906 -59.291 1.00 80.12 N
ANISOU 3038 N VAL A 365 7293 16538 6609 -1564 -39 -1548 N
ATOM 3039 CA VAL A 365 -24.166 -4.554 -59.768 1.00 79.46 C
ANISOU 3039 CA VAL A 365 7176 16512 6503 -1319 -88 -1376 C
ATOM 3040 C VAL A 365 -22.759 -4.443 -60.360 1.00 80.77 C
ANISOU 3040 C VAL A 365 7469 16464 6753 -1263 -90 -1330 C
ATOM 3041 O VAL A 365 -22.583 -3.939 -61.468 1.00 85.09 O
ANISOU 3041 O VAL A 365 7945 17169 7216 -1171 -116 -1280 O
ATOM 3042 CB VAL A 365 -24.342 -3.507 -58.645 1.00 76.11 C
ANISOU 3042 CB VAL A 365 6794 15971 6153 -1144 -103 -1231 C
ATOM 3043 CG1 VAL A 365 -24.014 -2.106 -59.149 1.00 74.10 C
ANISOU 3043 CG1 VAL A 365 6517 15758 5879 -892 -139 -1053 C
ATOM 3044 CG2 VAL A 365 -25.757 -3.562 -58.093 1.00 75.52 C
ANISOU 3044 CG2 VAL A 365 6583 16120 5988 -1188 -101 -1272 C
ATOM 3045 N TYR A 366 -21.765 -4.926 -59.618 1.00 81.01 N
ANISOU 3045 N TYR A 366 7685 16145 6948 -1320 -60 -1346 N
ATOM 3046 CA TYR A 366 -20.359 -4.691 -59.952 1.00 79.09 C
ANISOU 3046 CA TYR A 366 7577 15662 6809 -1244 -63 -1283 C
ATOM 3047 C TYR A 366 -19.595 -5.988 -60.224 1.00 78.91 C
ANISOU 3047 C TYR A 366 7653 15479 6847 -1433 -20 -1421 C
ATOM 3048 O TYR A 366 -20.035 -7.077 -59.845 1.00 77.34 O
ANISOU 3048 O TYR A 366 7461 15275 6650 -1622 19 -1555 O
ATOM 3049 CB TYR A 366 -19.659 -3.939 -58.809 1.00 76.25 C
ANISOU 3049 CB TYR A 366 7363 15004 6604 -1106 -67 -1154 C
ATOM 3050 CG TYR A 366 -20.199 -2.553 -58.488 1.00 75.99 C
ANISOU 3050 CG TYR A 366 7265 15068 6537 -898 -98 -1001 C
ATOM 3051 CD1 TYR A 366 -20.020 -1.488 -59.369 1.00 74.59 C
ANISOU 3051 CD1 TYR A 366 7031 15009 6298 -720 -126 -884 C
ATOM 3052 CD2 TYR A 366 -20.838 -2.296 -57.270 1.00 74.27 C
ANISOU 3052 CD2 TYR A 366 7056 14804 6358 -876 -93 -970 C
ATOM 3053 CE1 TYR A 366 -20.495 -0.219 -59.063 1.00 74.27 C
ANISOU 3053 CE1 TYR A 366 6942 15042 6233 -524 -143 -741 C
ATOM 3054 CE2 TYR A 366 -21.307 -1.027 -56.957 1.00 72.86 C
ANISOU 3054 CE2 TYR A 366 6827 14700 6156 -684 -113 -832 C
ATOM 3055 CZ TYR A 366 -21.132 0.005 -57.858 1.00 72.91 C
ANISOU 3055 CZ TYR A 366 6778 14822 6101 -507 -136 -717 C
ATOM 3056 OH TYR A 366 -21.591 1.265 -57.558 1.00 74.17 O
ANISOU 3056 OH TYR A 366 6895 15046 6240 -311 -145 -577 O
ATOM 3057 N GLN A 367 -18.445 -5.860 -60.881 1.00 80.66 N
ANISOU 3057 N GLN A 367 7955 15569 7122 -1381 -23 -1386 N
ATOM 3058 CA GLN A 367 -17.435 -6.909 -60.852 1.00 83.77 C
ANISOU 3058 CA GLN A 367 8490 15714 7624 -1515 19 -1478 C
ATOM 3059 C GLN A 367 -16.591 -6.695 -59.603 1.00 84.80 C
ANISOU 3059 C GLN A 367 8790 15499 7929 -1447 25 -1397 C
ATOM 3060 O GLN A 367 -16.082 -5.591 -59.368 1.00 85.35 O
ANISOU 3060 O GLN A 367 8900 15476 8050 -1265 -6 -1255 O
ATOM 3061 CB GLN A 367 -16.555 -6.861 -62.101 1.00 84.46 C
ANISOU 3061 CB GLN A 367 8585 15815 7691 -1487 13 -1477 C
ATOM 3062 CG GLN A 367 -16.174 -8.232 -62.650 1.00 87.20 C
ANISOU 3062 CG GLN A 367 8973 16112 8045 -1691 66 -1640 C
ATOM 3063 CD GLN A 367 -17.267 -8.847 -63.522 1.00 89.68 C
ANISOU 3063 CD GLN A 367 9124 16759 8188 -1838 78 -1775 C
ATOM 3064 OE1 GLN A 367 -18.350 -9.187 -63.039 1.00 89.73 O
ANISOU 3064 OE1 GLN A 367 9054 16901 8135 -1929 90 -1839 O
ATOM 3065 NE2 GLN A 367 -16.981 -8.998 -64.812 1.00 87.57 N
ANISOU 3065 NE2 GLN A 367 8801 16630 7839 -1866 78 -1821 N
ATOM 3066 N VAL A 368 -16.469 -7.739 -58.786 1.00 85.05 N
ANISOU 3066 N VAL A 368 8919 15348 8046 -1594 70 -1488 N
ATOM 3067 CA VAL A 368 -15.814 -7.623 -57.481 1.00 82.52 C
ANISOU 3067 CA VAL A 368 8749 14723 7879 -1544 77 -1420 C
ATOM 3068 C VAL A 368 -14.745 -8.696 -57.263 1.00 83.77 C
ANISOU 3068 C VAL A 368 9062 14607 8159 -1654 125 -1491 C
ATOM 3069 O VAL A 368 -14.916 -9.839 -57.680 1.00 86.97 O
ANISOU 3069 O VAL A 368 9463 15046 8535 -1826 172 -1628 O
ATOM 3070 CB VAL A 368 -16.841 -7.654 -56.323 1.00 78.60 C
ANISOU 3070 CB VAL A 368 8227 14259 7377 -1579 83 -1425 C
ATOM 3071 CG1 VAL A 368 -17.880 -6.557 -56.499 1.00 77.66 C
ANISOU 3071 CG1 VAL A 368 7957 14406 7143 -1455 39 -1346 C
ATOM 3072 CG2 VAL A 368 -17.508 -9.016 -56.214 1.00 78.37 C
ANISOU 3072 CG2 VAL A 368 8182 14279 7312 -1802 139 -1588 C
ATOM 3073 N ASN A 369 -13.647 -8.321 -56.611 1.00 82.49 N
ANISOU 3073 N ASN A 369 9033 14177 8129 -1554 115 -1399 N
ATOM 3074 CA ASN A 369 -12.590 -9.278 -56.266 1.00 84.73 C
ANISOU 3074 CA ASN A 369 9468 14188 8537 -1635 159 -1449 C
ATOM 3075 C ASN A 369 -13.025 -10.208 -55.132 1.00 85.09 C
ANISOU 3075 C ASN A 369 9580 14118 8633 -1763 204 -1516 C
ATOM 3076 O ASN A 369 -12.890 -9.855 -53.962 1.00 81.18 O
ANISOU 3076 O ASN A 369 9155 13472 8216 -1698 193 -1440 O
ATOM 3077 CB ASN A 369 -11.304 -8.548 -55.863 1.00 83.36 C
ANISOU 3077 CB ASN A 369 9407 13780 8483 -1484 132 -1327 C
ATOM 3078 CG ASN A 369 -10.804 -7.601 -56.935 1.00 85.70 C
ANISOU 3078 CG ASN A 369 9653 14167 8739 -1355 94 -1255 C
ATOM 3079 OD1 ASN A 369 -11.026 -7.820 -58.125 1.00 88.57 O
ANISOU 3079 OD1 ASN A 369 9933 14709 9009 -1402 98 -1315 O
ATOM 3080 ND2 ASN A 369 -10.115 -6.541 -56.515 1.00 83.76 N
ANISOU 3080 ND2 ASN A 369 9460 13800 8563 -1195 62 -1127 N
ATOM 3081 N PRO A 370 -13.528 -11.414 -55.476 1.00 88.06 N
ANISOU 3081 N PRO A 370 9936 14558 8962 -1949 262 -1661 N
ATOM 3082 CA PRO A 370 -14.182 -12.277 -54.484 1.00 88.43 C
ANISOU 3082 CA PRO A 370 10025 14542 9032 -2082 313 -1733 C
ATOM 3083 C PRO A 370 -13.221 -12.913 -53.465 1.00 87.32 C
ANISOU 3083 C PRO A 370 10064 14070 9041 -2098 351 -1715 C
ATOM 3084 O PRO A 370 -13.667 -13.373 -52.408 1.00 90.22 O
ANISOU 3084 O PRO A 370 10481 14355 9443 -2164 383 -1733 O
ATOM 3085 CB PRO A 370 -14.851 -13.350 -55.344 1.00 87.90 C
ANISOU 3085 CB PRO A 370 9888 14639 8870 -2277 371 -1898 C
ATOM 3086 CG PRO A 370 -13.982 -13.447 -56.551 1.00 87.72 C
ANISOU 3086 CG PRO A 370 9871 14614 8843 -2264 372 -1919 C
ATOM 3087 CD PRO A 370 -13.400 -12.081 -56.788 1.00 86.60 C
ANISOU 3087 CD PRO A 370 9707 14483 8712 -2052 293 -1769 C
ATOM 3088 N THR A 371 -11.925 -12.936 -53.777 1.00 84.13 N
ANISOU 3088 N THR A 371 9753 13489 8724 -2035 350 -1677 N
ATOM 3089 CA THR A 371 -10.915 -13.412 -52.828 1.00 81.37 C
ANISOU 3089 CA THR A 371 9566 12834 8514 -2021 377 -1640 C
ATOM 3090 C THR A 371 -10.583 -12.317 -51.816 1.00 80.79 C
ANISOU 3090 C THR A 371 9528 12663 8503 -1857 317 -1495 C
ATOM 3091 O THR A 371 -10.090 -12.600 -50.720 1.00 80.80 O
ANISOU 3091 O THR A 371 9644 12452 8602 -1845 332 -1457 O
ATOM 3092 CB THR A 371 -9.608 -13.861 -53.527 1.00 82.33 C
ANISOU 3092 CB THR A 371 9772 12802 8706 -2012 400 -1655 C
ATOM 3093 OG1 THR A 371 -8.791 -12.716 -53.823 1.00 80.06 O
ANISOU 3093 OG1 THR A 371 9477 12497 8445 -1840 333 -1539 O
ATOM 3094 CG2 THR A 371 -9.904 -14.644 -54.813 1.00 81.34 C
ANISOU 3094 CG2 THR A 371 9585 12819 8499 -2148 447 -1789 C
ATOM 3095 N LYS A 372 -10.852 -11.068 -52.195 1.00 78.64 N
ANISOU 3095 N LYS A 372 9158 12548 8172 -1730 253 -1415 N
ATOM 3096 CA LYS A 372 -10.584 -9.919 -51.335 1.00 75.42 C
ANISOU 3096 CA LYS A 372 8775 12066 7814 -1573 201 -1282 C
ATOM 3097 C LYS A 372 -11.790 -9.549 -50.468 1.00 70.96 C
ANISOU 3097 C LYS A 372 8149 11609 7201 -1577 190 -1264 C
ATOM 3098 O LYS A 372 -11.771 -8.543 -49.747 1.00 69.43 O
ANISOU 3098 O LYS A 372 7961 11383 7035 -1453 152 -1160 O
ATOM 3099 CB LYS A 372 -10.104 -8.715 -52.158 1.00 80.38 C
ANISOU 3099 CB LYS A 372 9349 12772 8418 -1422 149 -1194 C
ATOM 3100 CG LYS A 372 -8.617 -8.749 -52.497 1.00 83.04 C
ANISOU 3100 CG LYS A 372 9781 12921 8846 -1367 148 -1163 C
ATOM 3101 CD LYS A 372 -7.979 -7.378 -52.337 1.00 83.33 C
ANISOU 3101 CD LYS A 372 9829 12912 8920 -1189 98 -1032 C
ATOM 3102 CE LYS A 372 -6.504 -7.500 -51.989 1.00 85.35 C
ANISOU 3102 CE LYS A 372 10211 12918 9299 -1144 102 -994 C
ATOM 3103 NZ LYS A 372 -5.962 -6.251 -51.382 1.00 82.87 N
ANISOU 3103 NZ LYS A 372 9927 12523 9036 -994 63 -872 N
ATOM 3104 N THR A 373 -12.828 -10.374 -50.526 1.00 65.81 N
ANISOU 3104 N THR A 373 7442 11082 6478 -1723 230 -1370 N
ATOM 3105 CA THR A 373 -13.980 -10.188 -49.663 1.00 65.08 C
ANISOU 3105 CA THR A 373 7298 11085 6344 -1747 228 -1368 C
ATOM 3106 C THR A 373 -13.669 -10.631 -48.235 1.00 63.49 C
ANISOU 3106 C THR A 373 7227 10650 6246 -1772 254 -1345 C
ATOM 3107 O THR A 373 -13.040 -11.669 -48.024 1.00 65.59 O
ANISOU 3107 O THR A 373 7603 10736 6581 -1860 303 -1396 O
ATOM 3108 CB THR A 373 -15.199 -10.949 -50.191 1.00 63.65 C
ANISOU 3108 CB THR A 373 7010 11123 6049 -1906 266 -1498 C
ATOM 3109 OG1 THR A 373 -15.501 -10.486 -51.509 1.00 63.48 O
ANISOU 3109 OG1 THR A 373 6858 11337 5921 -1875 237 -1512 O
ATOM 3110 CG2 THR A 373 -16.390 -10.710 -49.298 1.00 61.71 C
ANISOU 3110 CG2 THR A 373 6704 10983 5758 -1926 264 -1493 C
ATOM 3111 N ARG A 374 -14.095 -9.824 -47.264 1.00 59.42 N
ANISOU 3111 N ARG A 374 6700 10137 5738 -1689 224 -1265 N
ATOM 3112 CA ARG A 374 -13.934 -10.155 -45.852 1.00 58.20 C
ANISOU 3112 CA ARG A 374 6656 9789 5666 -1709 244 -1239 C
ATOM 3113 C ARG A 374 -15.271 -10.087 -45.129 1.00 56.86 C
ANISOU 3113 C ARG A 374 6419 9750 5435 -1761 254 -1261 C
ATOM 3114 O ARG A 374 -15.968 -9.072 -45.189 1.00 56.57 O
ANISOU 3114 O ARG A 374 6277 9880 5335 -1674 214 -1211 O
ATOM 3115 CB ARG A 374 -12.921 -9.217 -45.177 1.00 58.46 C
ANISOU 3115 CB ARG A 374 6768 9653 5789 -1551 201 -1111 C
ATOM 3116 CG ARG A 374 -11.521 -9.254 -45.780 1.00 59.37 C
ANISOU 3116 CG ARG A 374 6955 9627 5973 -1495 191 -1085 C
ATOM 3117 CD ARG A 374 -10.868 -10.620 -45.612 1.00 61.16 C
ANISOU 3117 CD ARG A 374 7296 9672 6267 -1607 246 -1152 C
ATOM 3118 NE ARG A 374 -9.474 -10.624 -46.058 1.00 62.07 N
ANISOU 3118 NE ARG A 374 7486 9641 6457 -1542 237 -1118 N
ATOM 3119 CZ ARG A 374 -9.069 -10.972 -47.280 1.00 62.26 C
ANISOU 3119 CZ ARG A 374 7487 9706 6461 -1570 249 -1170 C
ATOM 3120 NH1 ARG A 374 -9.946 -11.353 -48.198 1.00 61.99 N
ANISOU 3120 NH1 ARG A 374 7357 9861 6332 -1665 271 -1262 N
ATOM 3121 NH2 ARG A 374 -7.779 -10.937 -47.583 1.00 61.91 N
ANISOU 3121 NH2 ARG A 374 7512 9520 6489 -1505 241 -1134 N
ATOM 3122 N THR A 375 -15.616 -11.172 -44.440 1.00 56.04 N
ANISOU 3122 N THR A 375 6376 9564 5349 -1901 311 -1334 N
ATOM 3123 CA THR A 375 -16.907 -11.295 -43.762 1.00 56.59 C
ANISOU 3123 CA THR A 375 6387 9754 5360 -1979 331 -1374 C
ATOM 3124 C THR A 375 -16.787 -12.232 -42.567 1.00 56.82 C
ANISOU 3124 C THR A 375 6545 9581 5461 -2074 387 -1397 C
ATOM 3125 O THR A 375 -15.860 -13.036 -42.503 1.00 55.92 O
ANISOU 3125 O THR A 375 6553 9270 5424 -2113 422 -1411 O
ATOM 3126 CB THR A 375 -18.002 -11.829 -44.720 1.00 58.13 C
ANISOU 3126 CB THR A 375 6452 10198 5436 -2111 361 -1497 C
ATOM 3127 OG1 THR A 375 -19.222 -12.016 -43.997 1.00 58.85 O
ANISOU 3127 OG1 THR A 375 6490 10396 5474 -2196 386 -1541 O
ATOM 3128 CG2 THR A 375 -17.585 -13.156 -45.335 1.00 58.81 C
ANISOU 3128 CG2 THR A 375 6602 10203 5539 -2261 427 -1609 C
ATOM 3129 N ASN A 376 -17.722 -12.117 -41.621 1.00 57.99 N
ANISOU 3129 N ASN A 376 6669 9780 5582 -2105 396 -1395 N
ATOM 3130 CA ASN A 376 -17.808 -13.056 -40.495 1.00 59.53 C
ANISOU 3130 CA ASN A 376 6977 9812 5828 -2210 456 -1425 C
ATOM 3131 C ASN A 376 -18.972 -14.049 -40.628 1.00 62.72 C
ANISOU 3131 C ASN A 376 7329 10341 6157 -2401 527 -1559 C
ATOM 3132 O ASN A 376 -19.292 -14.771 -39.675 1.00 64.87 O
ANISOU 3132 O ASN A 376 7679 10513 6455 -2498 583 -1589 O
ATOM 3133 CB ASN A 376 -17.900 -12.310 -39.158 1.00 57.55 C
ANISOU 3133 CB ASN A 376 6761 9488 5615 -2118 425 -1327 C
ATOM 3134 CG ASN A 376 -19.146 -11.444 -39.051 1.00 56.97 C
ANISOU 3134 CG ASN A 376 6546 9644 5453 -2088 396 -1320 C
ATOM 3135 OD1 ASN A 376 -19.678 -10.969 -40.059 1.00 57.76 O
ANISOU 3135 OD1 ASN A 376 6514 9959 5472 -2065 370 -1344 O
ATOM 3136 ND2 ASN A 376 -19.600 -11.209 -37.823 1.00 55.20 N
ANISOU 3136 ND2 ASN A 376 6349 9378 5244 -2080 400 -1283 N
ATOM 3137 N LEU A 377 -19.607 -14.067 -41.801 1.00 65.32 N
ANISOU 3137 N LEU A 377 7528 10897 6391 -2456 526 -1640 N
ATOM 3138 CA LEU A 377 -20.704 -15.006 -42.083 1.00 68.02 C
ANISOU 3138 CA LEU A 377 7807 11385 6651 -2649 595 -1782 C
ATOM 3139 C LEU A 377 -20.223 -16.458 -42.018 1.00 69.86 C
ANISOU 3139 C LEU A 377 8177 11424 6943 -2802 690 -1870 C
ATOM 3140 O LEU A 377 -19.263 -16.826 -42.700 1.00 69.00 O
ANISOU 3140 O LEU A 377 8131 11205 6879 -2792 701 -1877 O
ATOM 3141 CB LEU A 377 -21.333 -14.712 -43.449 1.00 66.48 C
ANISOU 3141 CB LEU A 377 7442 11477 6338 -2669 571 -1848 C
ATOM 3142 CG LEU A 377 -22.166 -13.434 -43.565 1.00 65.53 C
ANISOU 3142 CG LEU A 377 7162 11603 6133 -2549 497 -1786 C
ATOM 3143 CD1 LEU A 377 -22.390 -13.076 -45.022 1.00 64.41 C
ANISOU 3143 CD1 LEU A 377 6875 11704 5891 -2527 463 -1821 C
ATOM 3144 CD2 LEU A 377 -23.488 -13.556 -42.820 1.00 66.18 C
ANISOU 3144 CD2 LEU A 377 7173 11820 6152 -2638 525 -1836 C
ATOM 3145 N PRO A 378 -20.891 -17.287 -41.191 1.00 73.30 N
ANISOU 3145 N PRO A 378 8662 11810 7377 -2942 765 -1935 N
ATOM 3146 CA PRO A 378 -20.436 -18.658 -40.932 1.00 76.41 C
ANISOU 3146 CA PRO A 378 9208 11986 7836 -3077 867 -2002 C
ATOM 3147 C PRO A 378 -20.505 -19.591 -42.148 1.00 80.05 C
ANISOU 3147 C PRO A 378 9644 12516 8253 -3226 935 -2143 C
ATOM 3148 O PRO A 378 -19.868 -20.647 -42.140 1.00 82.02 O
ANISOU 3148 O PRO A 378 10029 12564 8570 -3309 1018 -2186 O
ATOM 3149 CB PRO A 378 -21.385 -19.141 -39.824 1.00 77.05 C
ANISOU 3149 CB PRO A 378 9315 12056 7901 -3191 928 -2041 C
ATOM 3150 CG PRO A 378 -21.920 -17.891 -39.203 1.00 75.90 C
ANISOU 3150 CG PRO A 378 9076 12035 7724 -3062 841 -1947 C
ATOM 3151 CD PRO A 378 -22.045 -16.931 -40.349 1.00 75.22 C
ANISOU 3151 CD PRO A 378 8834 12177 7566 -2966 761 -1934 C
ATOM 3152 N THR A 379 -21.249 -19.197 -43.183 1.00 81.92 N
ANISOU 3152 N THR A 379 9712 13035 8379 -3256 904 -2210 N
ATOM 3153 CA THR A 379 -21.386 -20.021 -44.390 1.00 85.84 C
ANISOU 3153 CA THR A 379 10167 13630 8819 -3405 965 -2352 C
ATOM 3154 C THR A 379 -20.180 -19.934 -45.323 1.00 83.99 C
ANISOU 3154 C THR A 379 9973 13307 8631 -3318 938 -2319 C
ATOM 3155 O THR A 379 -20.008 -20.788 -46.196 1.00 84.42 O
ANISOU 3155 O THR A 379 10042 13361 8670 -3441 1005 -2431 O
ATOM 3156 CB THR A 379 -22.657 -19.675 -45.192 1.00 88.73 C
ANISOU 3156 CB THR A 379 10324 14355 9033 -3477 942 -2443 C
ATOM 3157 OG1 THR A 379 -22.655 -18.277 -45.516 1.00 88.77 O
ANISOU 3157 OG1 THR A 379 10209 14520 8998 -3286 823 -2332 O
ATOM 3158 CG2 THR A 379 -23.918 -20.035 -44.394 1.00 88.94 C
ANISOU 3158 CG2 THR A 379 10308 14478 9005 -3611 994 -2515 C
ATOM 3159 N HIS A 380 -19.360 -18.900 -45.145 1.00 82.59 N
ANISOU 3159 N HIS A 380 9813 13058 8510 -3113 844 -2172 N
ATOM 3160 CA HIS A 380 -18.153 -18.716 -45.961 1.00 83.75 C
ANISOU 3160 CA HIS A 380 9999 13113 8706 -3016 813 -2128 C
ATOM 3161 C HIS A 380 -17.076 -19.694 -45.597 1.00 83.78 C
ANISOU 3161 C HIS A 380 10190 12812 8829 -3047 884 -2127 C
ATOM 3162 O HIS A 380 -17.094 -20.278 -44.508 1.00 83.75 O
ANISOU 3162 O HIS A 380 10300 12636 8886 -3093 939 -2116 O
ATOM 3163 CB HIS A 380 -17.626 -17.291 -45.832 1.00 83.62 C
ANISOU 3163 CB HIS A 380 9946 13112 8714 -2792 698 -1973 C
ATOM 3164 CG HIS A 380 -18.274 -16.312 -46.782 1.00 85.92 C
ANISOU 3164 CG HIS A 380 10055 13700 8891 -2730 627 -1969 C
ATOM 3165 ND1 HIS A 380 -17.587 -15.692 -47.764 1.00 85.58 N
ANISOU 3165 ND1 HIS A 380 9972 13705 8840 -2621 572 -1924 N
ATOM 3166 CD2 HIS A 380 -19.592 -15.852 -46.871 1.00 86.02 C
ANISOU 3166 CD2 HIS A 380 9911 13984 8787 -2759 604 -2002 C
ATOM 3167 CE1 HIS A 380 -18.420 -14.882 -48.449 1.00 86.38 C
ANISOU 3167 CE1 HIS A 380 9903 14091 8825 -2579 519 -1924 C
ATOM 3168 NE2 HIS A 380 -19.645 -14.980 -47.901 1.00 86.44 N
ANISOU 3168 NE2 HIS A 380 9837 14238 8766 -2660 537 -1971 N
ATOM 3169 N ARG A 381 -16.131 -19.885 -46.517 1.00 86.39 N
ANISOU 3169 N ARG A 381 10552 13078 9191 -3019 887 -2137 N
ATOM 3170 CA ARG A 381 -14.976 -20.755 -46.293 1.00 88.94 C
ANISOU 3170 CA ARG A 381 11049 13114 9631 -3026 951 -2126 C
ATOM 3171 C ARG A 381 -14.282 -20.381 -44.992 1.00 89.19 C
ANISOU 3171 C ARG A 381 11192 12930 9762 -2889 915 -1984 C
ATOM 3172 O ARG A 381 -14.241 -21.175 -44.046 1.00 87.87 O
ANISOU 3172 O ARG A 381 11147 12585 9654 -2949 986 -1987 O
ATOM 3173 CB ARG A 381 -13.982 -20.637 -47.454 1.00 91.21 C
ANISOU 3173 CB ARG A 381 11332 13386 9936 -2963 928 -2124 C
ATOM 3174 CG ARG A 381 -14.438 -21.269 -48.760 1.00 96.64 C
ANISOU 3174 CG ARG A 381 11942 14237 10539 -3115 985 -2277 C
ATOM 3175 CD ARG A 381 -13.829 -20.540 -49.950 1.00 97.37 C
ANISOU 3175 CD ARG A 381 11955 14437 10603 -3012 913 -2248 C
ATOM 3176 NE ARG A 381 -13.874 -21.328 -51.181 1.00101.97 N
ANISOU 3176 NE ARG A 381 12507 15101 11135 -3151 980 -2388 N
ATOM 3177 CZ ARG A 381 -14.936 -21.431 -51.980 1.00104.59 C
ANISOU 3177 CZ ARG A 381 12700 15701 11338 -3277 994 -2506 C
ATOM 3178 NH1 ARG A 381 -16.071 -20.809 -51.678 1.00104.90 N
ANISOU 3178 NH1 ARG A 381 12613 15956 11286 -3278 946 -2498 N
ATOM 3179 NH2 ARG A 381 -14.865 -22.169 -53.083 1.00104.36 N
ANISOU 3179 NH2 ARG A 381 12653 15730 11267 -3404 1059 -2635 N
ATOM 3180 N HIS A 382 -13.761 -19.154 -44.948 1.00 88.36 N
ANISOU 3180 N HIS A 382 11044 12853 9673 -2707 809 -1862 N
ATOM 3181 CA HIS A 382 -13.005 -18.665 -43.801 1.00 85.62 C
ANISOU 3181 CA HIS A 382 10793 12322 9417 -2567 765 -1725 C
ATOM 3182 C HIS A 382 -13.575 -17.372 -43.270 1.00 80.97 C
ANISOU 3182 C HIS A 382 10108 11869 8786 -2458 675 -1639 C
ATOM 3183 O HIS A 382 -13.085 -16.284 -43.607 1.00 76.52 O
ANISOU 3183 O HIS A 382 9493 11355 8225 -2312 592 -1556 O
ATOM 3184 CB HIS A 382 -11.529 -18.505 -44.165 1.00 89.31 C
ANISOU 3184 CB HIS A 382 11333 12631 9969 -2447 736 -1655 C
ATOM 3185 CG HIS A 382 -10.904 -19.756 -44.744 1.00 95.97 C
ANISOU 3185 CG HIS A 382 12271 13335 10857 -2542 828 -1737 C
ATOM 3186 ND1 HIS A 382 -10.627 -19.890 -46.059 1.00 98.55 N
ANISOU 3186 ND1 HIS A 382 12549 13741 11155 -2570 835 -1803 N
ATOM 3187 CD2 HIS A 382 -10.517 -20.953 -44.139 1.00 97.69 C
ANISOU 3187 CD2 HIS A 382 12636 13333 11149 -2616 923 -1760 C
ATOM 3188 CE1 HIS A 382 -10.086 -21.102 -46.283 1.00 98.51 C
ANISOU 3188 CE1 HIS A 382 12653 13571 11205 -2659 932 -1870 C
ATOM 3189 NE2 HIS A 382 -10.019 -21.752 -45.109 1.00100.85 N
ANISOU 3189 NE2 HIS A 382 13071 13682 11565 -2684 988 -1841 N
ATOM 3190 N PRO A 383 -14.633 -17.471 -42.436 1.00 78.21 N
ANISOU 3190 N PRO A 383 9737 11580 8398 -2529 697 -1661 N
ATOM 3191 CA PRO A 383 -15.223 -16.305 -41.771 1.00 77.03 C
ANISOU 3191 CA PRO A 383 9509 11542 8215 -2430 623 -1579 C
ATOM 3192 C PRO A 383 -14.228 -15.594 -40.849 1.00 74.68 C
ANISOU 3192 C PRO A 383 9298 11068 8007 -2269 568 -1440 C
ATOM 3193 O PRO A 383 -13.337 -16.233 -40.281 1.00 74.03 O
ANISOU 3193 O PRO A 383 9352 10763 8012 -2264 601 -1410 O
ATOM 3194 CB PRO A 383 -16.376 -16.905 -40.954 1.00 78.20 C
ANISOU 3194 CB PRO A 383 9656 11730 8324 -2564 683 -1643 C
ATOM 3195 CG PRO A 383 -16.053 -18.355 -40.823 1.00 78.77 C
ANISOU 3195 CG PRO A 383 9858 11622 8446 -2701 787 -1719 C
ATOM 3196 CD PRO A 383 -15.347 -18.713 -42.093 1.00 78.77 C
ANISOU 3196 CD PRO A 383 9857 11617 8454 -2714 801 -1769 C
ATOM 3197 N GLN A 384 -14.408 -14.283 -40.693 1.00 72.84 N
ANISOU 3197 N GLN A 384 8983 10940 7750 -2139 488 -1356 N
ATOM 3198 CA GLN A 384 -13.414 -13.422 -40.063 1.00 69.04 C
ANISOU 3198 CA GLN A 384 8562 10325 7343 -1980 429 -1230 C
ATOM 3199 C GLN A 384 -14.083 -12.300 -39.280 1.00 66.07 C
ANISOU 3199 C GLN A 384 8122 10042 6937 -1897 379 -1161 C
ATOM 3200 O GLN A 384 -14.933 -11.593 -39.813 1.00 65.97 O
ANISOU 3200 O GLN A 384 7981 10237 6844 -1876 350 -1172 O
ATOM 3201 CB GLN A 384 -12.520 -12.817 -41.137 1.00 68.35 C
ANISOU 3201 CB GLN A 384 8445 10256 7268 -1877 382 -1196 C
ATOM 3202 CG GLN A 384 -11.054 -12.812 -40.779 1.00 72.18 C
ANISOU 3202 CG GLN A 384 9048 10520 7857 -1786 366 -1120 C
ATOM 3203 CD GLN A 384 -10.186 -12.315 -41.916 1.00 72.73 C
ANISOU 3203 CD GLN A 384 9087 10609 7936 -1701 330 -1100 C
ATOM 3204 OE1 GLN A 384 -9.453 -13.087 -42.530 1.00 74.43 O
ANISOU 3204 OE1 GLN A 384 9356 10735 8187 -1739 362 -1140 O
ATOM 3205 NE2 GLN A 384 -10.267 -11.017 -42.204 1.00 71.41 N
ANISOU 3205 NE2 GLN A 384 8837 10557 7738 -1584 267 -1036 N
ATOM 3206 N ASP A 385 -13.677 -12.122 -38.025 1.00 64.19 N
ANISOU 3206 N ASP A 385 7974 9652 6761 -1845 370 -1086 N
ATOM 3207 CA ASP A 385 -14.214 -11.047 -37.181 1.00 62.22 C
ANISOU 3207 CA ASP A 385 7679 9467 6493 -1763 328 -1016 C
ATOM 3208 C ASP A 385 -13.675 -9.655 -37.533 1.00 58.84 C
ANISOU 3208 C ASP A 385 7202 9079 6074 -1600 258 -928 C
ATOM 3209 O ASP A 385 -14.374 -8.648 -37.381 1.00 57.29 O
ANISOU 3209 O ASP A 385 6921 9012 5832 -1534 228 -892 O
ATOM 3210 CB ASP A 385 -13.959 -11.348 -35.706 1.00 62.96 C
ANISOU 3210 CB ASP A 385 7886 9389 6646 -1770 345 -971 C
ATOM 3211 CG ASP A 385 -15.041 -12.209 -35.094 1.00 65.33 C
ANISOU 3211 CG ASP A 385 8192 9720 6907 -1912 406 -1041 C
ATOM 3212 OD1 ASP A 385 -16.028 -12.527 -35.798 1.00 67.55 O
ANISOU 3212 OD1 ASP A 385 8382 10168 7114 -2007 433 -1130 O
ATOM 3213 OD2 ASP A 385 -14.911 -12.557 -33.904 1.00 65.78 O
ANISOU 3213 OD2 ASP A 385 8344 9645 7005 -1930 428 -1009 O
ATOM 3214 N GLU A 386 -12.438 -9.605 -38.006 1.00 55.52 N
ANISOU 3214 N GLU A 386 6837 8544 5712 -1535 240 -894 N
ATOM 3215 CA GLU A 386 -11.765 -8.336 -38.212 1.00 53.91 C
ANISOU 3215 CA GLU A 386 6611 8341 5530 -1384 183 -807 C
ATOM 3216 C GLU A 386 -11.809 -7.950 -39.674 1.00 53.21 C
ANISOU 3216 C GLU A 386 6429 8396 5392 -1351 165 -829 C
ATOM 3217 O GLU A 386 -11.397 -8.719 -40.551 1.00 55.12 O
ANISOU 3217 O GLU A 386 6683 8621 5636 -1409 186 -885 O
ATOM 3218 CB GLU A 386 -10.329 -8.390 -37.685 1.00 53.11 C
ANISOU 3218 CB GLU A 386 6628 8026 5525 -1322 170 -746 C
ATOM 3219 CG GLU A 386 -10.251 -8.930 -36.268 1.00 55.08 C
ANISOU 3219 CG GLU A 386 6974 8136 5817 -1362 192 -727 C
ATOM 3220 CD GLU A 386 -9.098 -8.370 -35.465 1.00 58.31 C
ANISOU 3220 CD GLU A 386 7461 8395 6299 -1259 158 -639 C
ATOM 3221 OE1 GLU A 386 -7.945 -8.412 -35.964 1.00 59.88 O
ANISOU 3221 OE1 GLU A 386 7699 8505 6546 -1209 144 -619 O
ATOM 3222 OE2 GLU A 386 -9.349 -7.910 -34.320 1.00 55.86 O
ANISOU 3222 OE2 GLU A 386 7169 8059 5993 -1234 149 -595 O
ATOM 3223 N ILE A 387 -12.333 -6.760 -39.935 1.00 49.28 N
ANISOU 3223 N ILE A 387 5837 8042 4845 -1258 131 -783 N
ATOM 3224 CA ILE A 387 -12.589 -6.325 -41.294 1.00 48.73 C
ANISOU 3224 CA ILE A 387 5663 8141 4708 -1223 115 -798 C
ATOM 3225 C ILE A 387 -11.755 -5.092 -41.601 1.00 47.18 C
ANISOU 3225 C ILE A 387 5469 7912 4545 -1068 75 -705 C
ATOM 3226 O ILE A 387 -11.930 -4.053 -40.969 1.00 48.80 O
ANISOU 3226 O ILE A 387 5663 8122 4755 -973 57 -633 O
ATOM 3227 CB ILE A 387 -14.089 -6.000 -41.502 1.00 49.08 C
ANISOU 3227 CB ILE A 387 5576 8423 4650 -1245 117 -827 C
ATOM 3228 CG1 ILE A 387 -14.994 -7.168 -41.044 1.00 49.16 C
ANISOU 3228 CG1 ILE A 387 5584 8466 4627 -1407 162 -923 C
ATOM 3229 CG2 ILE A 387 -14.359 -5.580 -42.936 1.00 47.60 C
ANISOU 3229 CG2 ILE A 387 5274 8426 4383 -1205 99 -840 C
ATOM 3230 CD1 ILE A 387 -14.746 -8.499 -41.735 1.00 48.69 C
ANISOU 3230 CD1 ILE A 387 5557 8375 4567 -1542 203 -1023 C
ATOM 3231 N PRO A 388 -10.835 -5.201 -42.567 1.00 46.55 N
ANISOU 3231 N PRO A 388 5407 7793 4487 -1044 68 -709 N
ATOM 3232 CA PRO A 388 -10.087 -4.017 -42.947 1.00 47.13 C
ANISOU 3232 CA PRO A 388 5477 7845 4583 -903 37 -625 C
ATOM 3233 C PRO A 388 -10.906 -3.135 -43.885 1.00 48.96 C
ANISOU 3233 C PRO A 388 5583 8294 4723 -834 23 -605 C
ATOM 3234 O PRO A 388 -11.483 -3.633 -44.858 1.00 52.48 O
ANISOU 3234 O PRO A 388 5950 8892 5095 -896 30 -669 O
ATOM 3235 CB PRO A 388 -8.853 -4.593 -43.665 1.00 46.94 C
ANISOU 3235 CB PRO A 388 5515 7708 4611 -917 39 -647 C
ATOM 3236 CG PRO A 388 -9.314 -5.895 -44.224 1.00 48.76 C
ANISOU 3236 CG PRO A 388 5726 7995 4802 -1057 71 -751 C
ATOM 3237 CD PRO A 388 -10.451 -6.387 -43.356 1.00 48.92 C
ANISOU 3237 CD PRO A 388 5730 8065 4789 -1146 93 -791 C
ATOM 3238 N TYR A 389 -10.969 -1.840 -43.582 1.00 48.16 N
ANISOU 3238 N TYR A 389 5463 8209 4624 -707 7 -517 N
ATOM 3239 CA TYR A 389 -11.669 -0.875 -44.427 1.00 47.28 C
ANISOU 3239 CA TYR A 389 5240 8291 4430 -614 -1 -478 C
ATOM 3240 C TYR A 389 -11.168 0.543 -44.143 1.00 46.65 C
ANISOU 3240 C TYR A 389 5189 8145 4390 -462 -8 -371 C
ATOM 3241 O TYR A 389 -11.148 0.985 -42.993 1.00 45.99 O
ANISOU 3241 O TYR A 389 5156 7963 4353 -432 -2 -332 O
ATOM 3242 CB TYR A 389 -13.179 -0.970 -44.193 1.00 48.09 C
ANISOU 3242 CB TYR A 389 5244 8581 4447 -657 6 -509 C
ATOM 3243 CG TYR A 389 -13.983 0.048 -44.948 1.00 49.39 C
ANISOU 3243 CG TYR A 389 5288 8955 4521 -549 -2 -459 C
ATOM 3244 CD1 TYR A 389 -14.271 -0.126 -46.310 1.00 50.74 C
ANISOU 3244 CD1 TYR A 389 5365 9305 4607 -557 -10 -491 C
ATOM 3245 CD2 TYR A 389 -14.470 1.184 -44.311 1.00 48.75 C
ANISOU 3245 CD2 TYR A 389 5186 8899 4436 -437 0 -379 C
ATOM 3246 CE1 TYR A 389 -15.021 0.809 -47.012 1.00 50.29 C
ANISOU 3246 CE1 TYR A 389 5194 9453 4460 -448 -17 -437 C
ATOM 3247 CE2 TYR A 389 -15.218 2.125 -45.005 1.00 51.08 C
ANISOU 3247 CE2 TYR A 389 5372 9388 4648 -325 -1 -324 C
ATOM 3248 CZ TYR A 389 -15.492 1.933 -46.353 1.00 51.82 C
ANISOU 3248 CZ TYR A 389 5371 9663 4655 -328 -12 -350 C
ATOM 3249 OH TYR A 389 -16.231 2.871 -47.033 1.00 52.84 O
ANISOU 3249 OH TYR A 389 5390 9990 4695 -207 -14 -287 O
ATOM 3250 N CYS A 390 -10.744 1.234 -45.195 1.00 47.56 N
ANISOU 3250 N CYS A 390 5275 8310 4485 -370 -14 -328 N
ATOM 3251 CA CYS A 390 -10.247 2.614 -45.103 1.00 49.24 C
ANISOU 3251 CA CYS A 390 5513 8463 4730 -225 -9 -229 C
ATOM 3252 C CYS A 390 -9.084 2.847 -44.121 1.00 46.46 C
ANISOU 3252 C CYS A 390 5284 7877 4489 -209 -6 -199 C
ATOM 3253 O CYS A 390 -9.103 3.798 -43.347 1.00 40.87 O
ANISOU 3253 O CYS A 390 4604 7114 3810 -132 6 -138 O
ATOM 3254 CB CYS A 390 -11.396 3.571 -44.802 1.00 52.69 C
ANISOU 3254 CB CYS A 390 5876 9034 5109 -139 2 -174 C
ATOM 3255 SG CYS A 390 -12.504 3.741 -46.203 1.00 61.59 S
ANISOU 3255 SG CYS A 390 6850 10451 6101 -99 -3 -175 S
ATOM 3256 N GLY A 391 -8.070 1.984 -44.185 1.00 47.35 N
ANISOU 3256 N GLY A 391 5469 7862 4660 -280 -15 -243 N
ATOM 3257 CA GLY A 391 -6.913 2.076 -43.289 1.00 44.94 C
ANISOU 3257 CA GLY A 391 5272 7348 4453 -272 -16 -221 C
ATOM 3258 C GLY A 391 -7.233 1.742 -41.840 1.00 46.06 C
ANISOU 3258 C GLY A 391 5460 7413 4627 -327 -13 -232 C
ATOM 3259 O GLY A 391 -6.494 2.118 -40.923 1.00 48.40 O
ANISOU 3259 O GLY A 391 5832 7567 4991 -301 -13 -199 O
ATOM 3260 N LYS A 392 -8.336 1.042 -41.624 1.00 43.90 N
ANISOU 3260 N LYS A 392 5138 7239 4301 -406 -10 -280 N
ATOM 3261 CA LYS A 392 -8.734 0.674 -40.283 1.00 43.80 C
ANISOU 3261 CA LYS A 392 5165 7166 4311 -464 -4 -293 C
ATOM 3262 C LYS A 392 -9.135 -0.799 -40.223 1.00 44.48 C
ANISOU 3262 C LYS A 392 5255 7264 4381 -602 1 -377 C
ATOM 3263 O LYS A 392 -9.544 -1.384 -41.231 1.00 47.27 O
ANISOU 3263 O LYS A 392 5549 7730 4681 -652 4 -430 O
ATOM 3264 CB LYS A 392 -9.881 1.568 -39.811 1.00 44.72 C
ANISOU 3264 CB LYS A 392 5219 7393 4379 -409 6 -256 C
ATOM 3265 CG LYS A 392 -9.460 2.724 -38.916 1.00 48.13 C
ANISOU 3265 CG LYS A 392 5702 7724 4861 -318 14 -185 C
ATOM 3266 CD LYS A 392 -8.796 3.883 -39.647 1.00 49.03 C
ANISOU 3266 CD LYS A 392 5815 7825 4989 -197 21 -122 C
ATOM 3267 CE LYS A 392 -8.252 4.883 -38.635 1.00 49.73 C
ANISOU 3267 CE LYS A 392 5970 7786 5136 -132 37 -68 C
ATOM 3268 NZ LYS A 392 -7.663 6.110 -39.241 1.00 49.23 N
ANISOU 3268 NZ LYS A 392 5914 7702 5089 -15 57 -6 N
ATOM 3269 N ILE A 393 -8.993 -1.398 -39.048 1.00 42.85 N
ANISOU 3269 N ILE A 393 5122 6939 4219 -664 7 -390 N
ATOM 3270 CA ILE A 393 -9.503 -2.739 -38.805 1.00 42.81 C
ANISOU 3270 CA ILE A 393 5129 6937 4198 -795 25 -464 C
ATOM 3271 C ILE A 393 -10.664 -2.669 -37.822 1.00 42.66 C
ANISOU 3271 C ILE A 393 5083 6981 4144 -830 38 -469 C
ATOM 3272 O ILE A 393 -10.500 -2.232 -36.683 1.00 41.65 O
ANISOU 3272 O ILE A 393 5006 6765 4054 -799 35 -425 O
ATOM 3273 CB ILE A 393 -8.415 -3.681 -38.258 1.00 43.15 C
ANISOU 3273 CB ILE A 393 5285 6791 4319 -847 30 -477 C
ATOM 3274 CG1 ILE A 393 -7.268 -3.813 -39.265 1.00 44.31 C
ANISOU 3274 CG1 ILE A 393 5455 6879 4500 -816 20 -478 C
ATOM 3275 CG2 ILE A 393 -9.004 -5.052 -37.935 1.00 44.14 C
ANISOU 3275 CG2 ILE A 393 5433 6907 4428 -982 62 -550 C
ATOM 3276 CD1 ILE A 393 -5.941 -4.199 -38.643 1.00 43.89 C
ANISOU 3276 CD1 ILE A 393 5508 6633 4532 -807 15 -455 C
ATOM 3277 N PHE A 394 -11.839 -3.081 -38.292 1.00 42.77 N
ANISOU 3277 N PHE A 394 5011 7158 4081 -897 52 -525 N
ATOM 3278 CA PHE A 394 -13.042 -3.141 -37.480 1.00 43.90 C
ANISOU 3278 CA PHE A 394 5116 7382 4181 -945 68 -544 C
ATOM 3279 C PHE A 394 -13.256 -4.581 -37.008 1.00 44.85 C
ANISOU 3279 C PHE A 394 5288 7443 4309 -1093 99 -619 C
ATOM 3280 O PHE A 394 -13.306 -5.506 -37.809 1.00 48.61 O
ANISOU 3280 O PHE A 394 5751 7954 4762 -1179 116 -689 O
ATOM 3281 CB PHE A 394 -14.266 -2.667 -38.291 1.00 42.68 C
ANISOU 3281 CB PHE A 394 4822 7464 3929 -925 68 -560 C
ATOM 3282 CG PHE A 394 -14.166 -1.244 -38.783 1.00 41.37 C
ANISOU 3282 CG PHE A 394 4604 7365 3749 -773 48 -480 C
ATOM 3283 CD1 PHE A 394 -13.381 -0.925 -39.882 1.00 40.68 C
ANISOU 3283 CD1 PHE A 394 4511 7277 3669 -708 33 -458 C
ATOM 3284 CD2 PHE A 394 -14.871 -0.224 -38.149 1.00 41.30 C
ANISOU 3284 CD2 PHE A 394 4554 7417 3719 -693 52 -426 C
ATOM 3285 CE1 PHE A 394 -13.291 0.387 -40.330 1.00 41.00 C
ANISOU 3285 CE1 PHE A 394 4511 7371 3697 -567 23 -380 C
ATOM 3286 CE2 PHE A 394 -14.783 1.089 -38.592 1.00 40.46 C
ANISOU 3286 CE2 PHE A 394 4408 7360 3603 -548 45 -349 C
ATOM 3287 CZ PHE A 394 -13.990 1.396 -39.680 1.00 39.96 C
ANISOU 3287 CZ PHE A 394 4344 7290 3546 -485 32 -324 C
ATOM 3288 N ASN A 395 -13.360 -4.774 -35.707 1.00 45.30 N
ANISOU 3288 N ASN A 395 5410 7403 4397 -1124 111 -606 N
ATOM 3289 CA ASN A 395 -13.745 -6.071 -35.190 1.00 46.12 C
ANISOU 3289 CA ASN A 395 5560 7462 4500 -1263 150 -673 C
ATOM 3290 C ASN A 395 -15.257 -6.085 -34.955 1.00 45.70 C
ANISOU 3290 C ASN A 395 5418 7577 4369 -1326 170 -716 C
ATOM 3291 O ASN A 395 -15.769 -5.344 -34.126 1.00 44.29 O
ANISOU 3291 O ASN A 395 5220 7427 4181 -1279 164 -675 O
ATOM 3292 CB ASN A 395 -12.967 -6.389 -33.913 1.00 44.93 C
ANISOU 3292 CB ASN A 395 5535 7112 4423 -1267 154 -633 C
ATOM 3293 CG ASN A 395 -13.274 -7.767 -33.374 1.00 45.14 C
ANISOU 3293 CG ASN A 395 5625 7071 4452 -1403 202 -693 C
ATOM 3294 OD1 ASN A 395 -14.439 -8.137 -33.217 1.00 47.48 O
ANISOU 3294 OD1 ASN A 395 5873 7474 4693 -1491 233 -748 O
ATOM 3295 ND2 ASN A 395 -12.231 -8.523 -33.057 1.00 42.55 N
ANISOU 3295 ND2 ASN A 395 5409 6566 4190 -1420 214 -681 N
ATOM 3296 N LEU A 396 -15.965 -6.907 -35.717 1.00 46.65 N
ANISOU 3296 N LEU A 396 5478 7814 4430 -1433 198 -804 N
ATOM 3297 CA LEU A 396 -17.424 -6.893 -35.705 1.00 48.53 C
ANISOU 3297 CA LEU A 396 5609 8247 4582 -1493 216 -855 C
ATOM 3298 C LEU A 396 -17.999 -7.378 -34.383 1.00 49.96 C
ANISOU 3298 C LEU A 396 5841 8369 4771 -1575 249 -871 C
ATOM 3299 O LEU A 396 -19.130 -7.036 -34.031 1.00 50.60 O
ANISOU 3299 O LEU A 396 5841 8589 4794 -1590 257 -885 O
ATOM 3300 CB LEU A 396 -17.976 -7.721 -36.863 1.00 49.37 C
ANISOU 3300 CB LEU A 396 5640 8497 4621 -1602 241 -956 C
ATOM 3301 CG LEU A 396 -17.591 -7.231 -38.265 1.00 49.83 C
ANISOU 3301 CG LEU A 396 5627 8653 4650 -1527 208 -946 C
ATOM 3302 CD1 LEU A 396 -18.208 -8.125 -39.322 1.00 49.98 C
ANISOU 3302 CD1 LEU A 396 5570 8824 4594 -1653 238 -1057 C
ATOM 3303 CD2 LEU A 396 -17.988 -5.774 -38.492 1.00 48.78 C
ANISOU 3303 CD2 LEU A 396 5395 8662 4477 -1378 166 -868 C
ATOM 3304 N THR A 397 -17.200 -8.144 -33.638 1.00 50.09 N
ANISOU 3304 N THR A 397 5991 8180 4859 -1620 270 -864 N
ATOM 3305 CA THR A 397 -17.648 -8.713 -32.368 1.00 50.18 C
ANISOU 3305 CA THR A 397 6067 8117 4881 -1703 308 -876 C
ATOM 3306 C THR A 397 -17.366 -7.751 -31.221 1.00 48.85 C
ANISOU 3306 C THR A 397 5938 7870 4750 -1599 278 -784 C
ATOM 3307 O THR A 397 -18.273 -7.406 -30.470 1.00 50.48 O
ANISOU 3307 O THR A 397 6107 8149 4923 -1611 287 -783 O
ATOM 3308 CB THR A 397 -17.012 -10.105 -32.102 1.00 51.32 C
ANISOU 3308 CB THR A 397 6338 8083 5076 -1808 356 -914 C
ATOM 3309 OG1 THR A 397 -17.420 -11.029 -33.129 1.00 52.49 O
ANISOU 3309 OG1 THR A 397 6448 8312 5183 -1924 397 -1014 O
ATOM 3310 CG2 THR A 397 -17.437 -10.651 -30.738 1.00 49.08 C
ANISOU 3310 CG2 THR A 397 6129 7715 4802 -1884 396 -915 C
ATOM 3311 N THR A 398 -16.118 -7.293 -31.112 1.00 47.28 N
ANISOU 3311 N THR A 398 5809 7533 4618 -1499 243 -713 N
ATOM 3312 CA THR A 398 -15.707 -6.423 -30.005 1.00 45.98 C
ANISOU 3312 CA THR A 398 5693 7283 4494 -1408 219 -631 C
ATOM 3313 C THR A 398 -15.986 -4.941 -30.270 1.00 45.16 C
ANISOU 3313 C THR A 398 5499 7291 4366 -1284 185 -581 C
ATOM 3314 O THR A 398 -16.005 -4.128 -29.336 1.00 44.52 O
ANISOU 3314 O THR A 398 5436 7179 4301 -1222 175 -528 O
ATOM 3315 CB THR A 398 -14.212 -6.606 -29.655 1.00 46.63 C
ANISOU 3315 CB THR A 398 5892 7166 4656 -1362 201 -578 C
ATOM 3316 OG1 THR A 398 -13.402 -6.278 -30.795 1.00 45.13 O
ANISOU 3316 OG1 THR A 398 5682 6977 4486 -1292 173 -566 O
ATOM 3317 CG2 THR A 398 -13.924 -8.045 -29.217 1.00 45.81 C
ANISOU 3317 CG2 THR A 398 5890 6935 4580 -1470 242 -613 C
ATOM 3318 N ARG A 399 -16.183 -4.599 -31.545 1.00 44.75 N
ANISOU 3318 N ARG A 399 5358 7368 4277 -1246 171 -597 N
ATOM 3319 CA ARG A 399 -16.468 -3.222 -31.991 1.00 44.64 C
ANISOU 3319 CA ARG A 399 5255 7469 4235 -1120 147 -547 C
ATOM 3320 C ARG A 399 -15.255 -2.304 -31.935 1.00 45.14 C
ANISOU 3320 C ARG A 399 5375 7411 4363 -998 118 -468 C
ATOM 3321 O ARG A 399 -15.330 -1.140 -32.338 1.00 47.42 O
ANISOU 3321 O ARG A 399 5608 7769 4639 -887 105 -420 O
ATOM 3322 CB ARG A 399 -17.640 -2.604 -31.224 1.00 44.80 C
ANISOU 3322 CB ARG A 399 5213 7595 4211 -1108 160 -537 C
ATOM 3323 CG ARG A 399 -18.977 -3.261 -31.491 1.00 46.37 C
ANISOU 3323 CG ARG A 399 5321 7965 4330 -1211 187 -615 C
ATOM 3324 CD ARG A 399 -19.348 -4.223 -30.373 1.00 47.43 C
ANISOU 3324 CD ARG A 399 5521 8026 4474 -1337 221 -658 C
ATOM 3325 NE ARG A 399 -20.548 -4.996 -30.688 1.00 49.82 N
ANISOU 3325 NE ARG A 399 5743 8483 4702 -1458 253 -746 N
ATOM 3326 CZ ARG A 399 -21.793 -4.539 -30.572 1.00 48.86 C
ANISOU 3326 CZ ARG A 399 5512 8538 4511 -1456 263 -763 C
ATOM 3327 NH1 ARG A 399 -22.020 -3.299 -30.165 1.00 48.18 N
ANISOU 3327 NH1 ARG A 399 5388 8492 4424 -1334 246 -694 N
ATOM 3328 NH2 ARG A 399 -22.808 -5.324 -30.873 1.00 50.95 N
ANISOU 3328 NH2 ARG A 399 5706 8944 4709 -1579 294 -852 N
ATOM 3329 N GLN A 400 -14.142 -2.834 -31.433 1.00 44.04 N
ANISOU 3329 N GLN A 400 5347 7093 4291 -1019 113 -455 N
ATOM 3330 CA GLN A 400 -12.869 -2.126 -31.394 1.00 41.79 C
ANISOU 3330 CA GLN A 400 5121 6688 4068 -922 87 -393 C
ATOM 3331 C GLN A 400 -12.405 -1.765 -32.787 1.00 41.00 C
ANISOU 3331 C GLN A 400 4974 6638 3963 -859 70 -387 C
ATOM 3332 O GLN A 400 -12.629 -2.517 -33.735 1.00 42.00 O
ANISOU 3332 O GLN A 400 5065 6832 4060 -917 76 -440 O
ATOM 3333 CB GLN A 400 -11.802 -2.995 -30.727 1.00 41.76 C
ANISOU 3333 CB GLN A 400 5234 6505 4127 -968 85 -390 C
ATOM 3334 CG GLN A 400 -12.157 -3.458 -29.325 1.00 41.29 C
ANISOU 3334 CG GLN A 400 5232 6384 4072 -1033 103 -391 C
ATOM 3335 CD GLN A 400 -12.612 -2.314 -28.445 1.00 43.44 C
ANISOU 3335 CD GLN A 400 5482 6688 4334 -972 101 -349 C
ATOM 3336 OE1 GLN A 400 -13.816 -2.068 -28.287 1.00 47.11 O
ANISOU 3336 OE1 GLN A 400 5880 7272 4747 -991 119 -368 O
ATOM 3337 NE2 GLN A 400 -11.663 -1.600 -27.875 1.00 40.50 N
ANISOU 3337 NE2 GLN A 400 5163 6214 4008 -900 83 -295 N
ATOM 3338 N VAL A 401 -11.753 -0.613 -32.912 1.00 39.84 N
ANISOU 3338 N VAL A 401 4832 6459 3845 -745 54 -326 N
ATOM 3339 CA VAL A 401 -11.133 -0.233 -34.176 1.00 38.39 C
ANISOU 3339 CA VAL A 401 4621 6299 3665 -679 40 -312 C
ATOM 3340 C VAL A 401 -9.643 0.056 -33.988 1.00 38.14 C
ANISOU 3340 C VAL A 401 4675 6106 3709 -627 24 -272 C
ATOM 3341 O VAL A 401 -9.256 0.840 -33.120 1.00 37.31 O
ANISOU 3341 O VAL A 401 4612 5927 3638 -574 24 -226 O
ATOM 3342 CB VAL A 401 -11.848 0.958 -34.845 1.00 37.75 C
ANISOU 3342 CB VAL A 401 4444 6365 3533 -580 44 -277 C
ATOM 3343 CG1 VAL A 401 -11.182 1.306 -36.170 1.00 36.46 C
ANISOU 3343 CG1 VAL A 401 4257 6226 3370 -515 32 -260 C
ATOM 3344 CG2 VAL A 401 -13.324 0.645 -35.060 1.00 38.61 C
ANISOU 3344 CG2 VAL A 401 4455 6653 3560 -631 57 -319 C
ATOM 3345 N ARG A 402 -8.825 -0.591 -34.814 1.00 38.54 N
ANISOU 3345 N ARG A 402 4749 6111 3782 -647 13 -294 N
ATOM 3346 CA ARG A 402 -7.371 -0.426 -34.795 1.00 39.64 C
ANISOU 3346 CA ARG A 402 4960 6110 3989 -603 -1 -263 C
ATOM 3347 C ARG A 402 -6.908 0.156 -36.137 1.00 39.89 C
ANISOU 3347 C ARG A 402 4950 6189 4015 -532 -9 -249 C
ATOM 3348 O ARG A 402 -7.592 0.013 -37.158 1.00 39.45 O
ANISOU 3348 O ARG A 402 4822 6262 3905 -542 -5 -276 O
ATOM 3349 CB ARG A 402 -6.679 -1.787 -34.554 1.00 39.00 C
ANISOU 3349 CB ARG A 402 4953 5916 3946 -686 -3 -298 C
ATOM 3350 CG ARG A 402 -7.055 -2.501 -33.254 1.00 40.49 C
ANISOU 3350 CG ARG A 402 5194 6048 4141 -759 8 -309 C
ATOM 3351 CD ARG A 402 -6.321 -1.922 -32.029 1.00 42.52 C
ANISOU 3351 CD ARG A 402 5515 6195 4443 -714 -4 -257 C
ATOM 3352 NE ARG A 402 -4.862 -1.976 -32.167 1.00 42.24 N
ANISOU 3352 NE ARG A 402 5536 6046 4466 -675 -23 -234 N
ATOM 3353 CZ ARG A 402 -4.113 -3.021 -31.813 1.00 42.25 C
ANISOU 3353 CZ ARG A 402 5607 5942 4504 -717 -25 -241 C
ATOM 3354 NH1 ARG A 402 -4.677 -4.086 -31.261 1.00 44.71 N
ANISOU 3354 NH1 ARG A 402 5950 6234 4801 -800 -4 -268 N
ATOM 3355 NH2 ARG A 402 -2.797 -2.989 -31.981 1.00 38.98 N
ANISOU 3355 NH2 ARG A 402 5232 5439 4138 -672 -43 -220 N
ATOM 3356 N THR A 403 -5.752 0.813 -36.141 1.00 40.51 N
ANISOU 3356 N THR A 403 5074 6171 4146 -463 -18 -209 N
ATOM 3357 CA THR A 403 -5.139 1.250 -37.403 1.00 41.72 C
ANISOU 3357 CA THR A 403 5202 6347 4301 -403 -23 -197 C
ATOM 3358 C THR A 403 -4.583 0.046 -38.155 1.00 41.30 C
ANISOU 3358 C THR A 403 5166 6263 4261 -468 -31 -247 C
ATOM 3359 O THR A 403 -4.054 -0.869 -37.545 1.00 41.11 O
ANISOU 3359 O THR A 403 5206 6135 4277 -527 -34 -268 O
ATOM 3360 CB THR A 403 -4.002 2.237 -37.147 1.00 41.58 C
ANISOU 3360 CB THR A 403 5232 6226 4339 -324 -25 -148 C
ATOM 3361 OG1 THR A 403 -4.486 3.320 -36.352 1.00 44.88 O
ANISOU 3361 OG1 THR A 403 5645 6657 4750 -272 -8 -107 O
ATOM 3362 CG2 THR A 403 -3.417 2.767 -38.457 1.00 40.95 C
ANISOU 3362 CG2 THR A 403 5126 6172 4258 -260 -23 -133 C
ATOM 3363 N LEU A 404 -4.727 0.045 -39.475 1.00 43.58 N
ANISOU 3363 N LEU A 404 5398 6645 4513 -455 -30 -264 N
ATOM 3364 CA LEU A 404 -4.187 -1.029 -40.301 1.00 44.45 C
ANISOU 3364 CA LEU A 404 5523 6731 4634 -514 -31 -315 C
ATOM 3365 C LEU A 404 -2.770 -0.715 -40.778 1.00 44.62 C
ANISOU 3365 C LEU A 404 5587 6654 4711 -457 -41 -291 C
ATOM 3366 O LEU A 404 -2.484 0.388 -41.236 1.00 43.22 O
ANISOU 3366 O LEU A 404 5387 6501 4532 -370 -42 -247 O
ATOM 3367 CB LEU A 404 -5.105 -1.291 -41.492 1.00 45.81 C
ANISOU 3367 CB LEU A 404 5608 7069 4730 -543 -23 -357 C
ATOM 3368 CG LEU A 404 -4.638 -2.154 -42.677 1.00 46.25 C
ANISOU 3368 CG LEU A 404 5657 7135 4779 -591 -19 -411 C
ATOM 3369 CD1 LEU A 404 -4.581 -3.627 -42.311 1.00 45.50 C
ANISOU 3369 CD1 LEU A 404 5614 6963 4708 -707 -2 -477 C
ATOM 3370 CD2 LEU A 404 -5.547 -1.944 -43.886 1.00 45.26 C
ANISOU 3370 CD2 LEU A 404 5427 7203 4565 -588 -17 -434 C
ATOM 3371 N TYR A 405 -1.888 -1.698 -40.630 1.00 48.26 N
ANISOU 3371 N TYR A 405 6111 7001 5224 -505 -43 -318 N
ATOM 3372 CA TYR A 405 -0.553 -1.692 -41.230 1.00 49.36 C
ANISOU 3372 CA TYR A 405 6284 7056 5412 -469 -50 -312 C
ATOM 3373 C TYR A 405 -0.303 -3.129 -41.771 1.00 54.48 C
ANISOU 3373 C TYR A 405 6956 7672 6071 -552 -38 -375 C
ATOM 3374 O TYR A 405 -0.335 -4.079 -40.977 1.00 62.13 O
ANISOU 3374 O TYR A 405 7976 8567 7064 -614 -28 -395 O
ATOM 3375 CB TYR A 405 0.520 -1.367 -40.164 1.00 43.76 C
ANISOU 3375 CB TYR A 405 5644 6209 4770 -432 -63 -270 C
ATOM 3376 CG TYR A 405 0.244 -0.215 -39.194 1.00 40.29 C
ANISOU 3376 CG TYR A 405 5205 5771 4330 -380 -66 -220 C
ATOM 3377 CD1 TYR A 405 0.756 1.063 -39.434 1.00 39.42 C
ANISOU 3377 CD1 TYR A 405 5086 5658 4232 -296 -64 -178 C
ATOM 3378 CD2 TYR A 405 -0.437 -0.430 -37.982 1.00 38.72 C
ANISOU 3378 CD2 TYR A 405 5024 5562 4122 -417 -65 -217 C
ATOM 3379 CE1 TYR A 405 0.561 2.107 -38.530 1.00 37.00 C
ANISOU 3379 CE1 TYR A 405 4787 5341 3929 -253 -57 -137 C
ATOM 3380 CE2 TYR A 405 -0.643 0.613 -37.077 1.00 37.48 C
ANISOU 3380 CE2 TYR A 405 4871 5401 3966 -373 -64 -175 C
ATOM 3381 CZ TYR A 405 -0.143 1.884 -37.362 1.00 37.90 C
ANISOU 3381 CZ TYR A 405 4914 5451 4032 -292 -58 -137 C
ATOM 3382 OH TYR A 405 -0.332 2.935 -36.477 1.00 37.91 O
ANISOU 3382 OH TYR A 405 4924 5442 4036 -252 -47 -101 O
ATOM 3383 N LYS A 406 -0.044 -3.339 -43.072 1.00 60.28 N
ANISOU 3383 N LYS A 406 7660 8453 6790 -555 -32 -406 N
ATOM 3384 CA LYS A 406 0.284 -2.331 -44.108 1.00 65.17 C
ANISOU 3384 CA LYS A 406 8233 9136 7391 -477 -39 -378 C
ATOM 3385 C LYS A 406 1.688 -2.603 -44.711 1.00 62.75 C
ANISOU 3385 C LYS A 406 7967 8732 7140 -458 -40 -385 C
ATOM 3386 O LYS A 406 2.251 -1.761 -45.440 1.00 61.15 O
ANISOU 3386 O LYS A 406 7746 8547 6939 -390 -45 -357 O
ATOM 3387 CB LYS A 406 0.199 -0.900 -43.561 1.00 63.83 C
ANISOU 3387 CB LYS A 406 8053 8978 7221 -387 -49 -308 C
ATOM 3388 CG LYS A 406 -0.277 0.130 -44.565 1.00 65.05 C
ANISOU 3388 CG LYS A 406 8137 9260 7319 -320 -44 -280 C
ATOM 3389 CD LYS A 406 -0.042 1.536 -44.040 1.00 66.91 C
ANISOU 3389 CD LYS A 406 8383 9464 7572 -226 -41 -210 C
ATOM 3390 CE LYS A 406 1.408 1.743 -43.651 1.00 62.59 C
ANISOU 3390 CE LYS A 406 7906 8769 7104 -199 -46 -192 C
ATOM 3391 NZ LYS A 406 1.685 3.171 -43.338 1.00 66.98 N
ANISOU 3391 NZ LYS A 406 8471 9301 7674 -113 -32 -133 N
ATOM 3392 N LEU A 407 2.259 -3.764 -44.388 1.00 57.81 N
ANISOU 3392 N LEU A 407 7401 8002 6562 -515 -32 -420 N
ATOM 3393 CA LEU A 407 3.657 -4.023 -44.724 1.00 60.22 C
ANISOU 3393 CA LEU A 407 7750 8202 6929 -490 -33 -420 C
ATOM 3394 C LEU A 407 3.855 -5.374 -45.394 1.00 62.51 C
ANISOU 3394 C LEU A 407 8059 8462 7227 -563 -6 -486 C
ATOM 3395 O LEU A 407 3.744 -6.417 -44.745 1.00 61.98 O
ANISOU 3395 O LEU A 407 8041 8325 7183 -622 10 -511 O
ATOM 3396 CB LEU A 407 4.577 -3.912 -43.483 1.00 61.57 C
ANISOU 3396 CB LEU A 407 7985 8241 7165 -455 -48 -377 C
ATOM 3397 CG LEU A 407 4.860 -2.591 -42.728 1.00 58.23 C
ANISOU 3397 CG LEU A 407 7562 7806 6755 -381 -69 -315 C
ATOM 3398 CD1 LEU A 407 5.113 -1.412 -43.656 1.00 60.23 C
ANISOU 3398 CD1 LEU A 407 7774 8118 6993 -314 -69 -292 C
ATOM 3399 CD2 LEU A 407 3.774 -2.263 -41.715 1.00 57.46 C
ANISOU 3399 CD2 LEU A 407 7456 7749 6626 -394 -72 -295 C
ATOM 3400 N PRO A 408 4.167 -5.358 -46.703 1.00 62.91 N
ANISOU 3400 N PRO A 408 8078 8563 7262 -558 1 -515 N
ATOM 3401 CA PRO A 408 4.640 -6.551 -47.394 1.00 62.66 C
ANISOU 3401 CA PRO A 408 8073 8483 7252 -616 30 -577 C
ATOM 3402 C PRO A 408 5.869 -7.128 -46.686 1.00 65.57 C
ANISOU 3402 C PRO A 408 8521 8686 7705 -596 33 -560 C
ATOM 3403 O PRO A 408 6.593 -6.382 -46.012 1.00 62.48 O
ANISOU 3403 O PRO A 408 8148 8238 7352 -524 6 -501 O
ATOM 3404 CB PRO A 408 5.050 -6.015 -48.767 1.00 62.12 C
ANISOU 3404 CB PRO A 408 7957 8485 7159 -580 28 -586 C
ATOM 3405 CG PRO A 408 4.234 -4.793 -48.960 1.00 62.48 C
ANISOU 3405 CG PRO A 408 7936 8662 7141 -533 7 -546 C
ATOM 3406 CD PRO A 408 4.103 -4.187 -47.595 1.00 62.29 C
ANISOU 3406 CD PRO A 408 7938 8586 7142 -493 -11 -487 C
ATOM 3407 N PRO A 409 6.107 -8.452 -46.830 1.00 69.51 N
ANISOU 3407 N PRO A 409 9066 9110 8233 -659 71 -611 N
ATOM 3408 CA PRO A 409 7.370 -9.028 -46.350 1.00 67.74 C
ANISOU 3408 CA PRO A 409 8911 8737 8087 -626 78 -592 C
ATOM 3409 C PRO A 409 8.550 -8.410 -47.103 1.00 66.16 C
ANISOU 3409 C PRO A 409 8695 8524 7917 -555 61 -575 C
ATOM 3410 O PRO A 409 8.420 -8.084 -48.284 1.00 66.31 O
ANISOU 3410 O PRO A 409 8665 8627 7899 -561 66 -605 O
ATOM 3411 CB PRO A 409 7.232 -10.520 -46.694 1.00 70.37 C
ANISOU 3411 CB PRO A 409 9288 9015 8433 -710 135 -660 C
ATOM 3412 CG PRO A 409 6.200 -10.584 -47.778 1.00 69.40 C
ANISOU 3412 CG PRO A 409 9104 9025 8237 -783 155 -727 C
ATOM 3413 CD PRO A 409 5.254 -9.456 -47.502 1.00 69.37 C
ANISOU 3413 CD PRO A 409 9036 9145 8173 -760 115 -691 C
ATOM 3414 N ASN A 410 9.673 -8.213 -46.416 1.00 65.31 N
ANISOU 3414 N ASN A 410 8623 8320 7869 -490 42 -528 N
ATOM 3415 CA ASN A 410 10.867 -7.628 -47.039 1.00 64.12 C
ANISOU 3415 CA ASN A 410 8459 8152 7750 -426 28 -514 C
ATOM 3416 C ASN A 410 10.739 -6.135 -47.354 1.00 62.35 C
ANISOU 3416 C ASN A 410 8180 8017 7492 -376 -1 -480 C
ATOM 3417 O ASN A 410 11.597 -5.571 -48.062 1.00 62.87 O
ANISOU 3417 O ASN A 410 8228 8084 7572 -331 -5 -475 O
ATOM 3418 CB ASN A 410 11.239 -8.367 -48.342 1.00 68.49 C
ANISOU 3418 CB ASN A 410 9010 8703 8310 -457 64 -574 C
ATOM 3419 CG ASN A 410 11.448 -9.849 -48.144 1.00 72.48 C
ANISOU 3419 CG ASN A 410 9575 9107 8854 -503 108 -610 C
ATOM 3420 OD1 ASN A 410 11.880 -10.299 -47.079 1.00 76.60 O
ANISOU 3420 OD1 ASN A 410 10149 9533 9421 -480 106 -575 O
ATOM 3421 ND2 ASN A 410 11.148 -10.623 -49.179 1.00 77.13 N
ANISOU 3421 ND2 ASN A 410 10162 9718 9426 -567 151 -680 N
ATOM 3422 N TYR A 411 9.670 -5.497 -46.874 1.00 54.46 N
ANISOU 3422 N TYR A 411 7155 7090 6445 -383 -15 -458 N
ATOM 3423 CA TYR A 411 9.495 -4.071 -47.126 1.00 47.80 C
ANISOU 3423 CA TYR A 411 6266 6323 5569 -329 -33 -420 C
ATOM 3424 C TYR A 411 10.467 -3.275 -46.267 1.00 45.79 C
ANISOU 3424 C TYR A 411 6035 5999 5362 -267 -54 -370 C
ATOM 3425 O TYR A 411 10.606 -3.539 -45.075 1.00 46.52 O
ANISOU 3425 O TYR A 411 6163 6029 5482 -268 -66 -349 O
ATOM 3426 CB TYR A 411 8.063 -3.632 -46.865 1.00 44.19 C
ANISOU 3426 CB TYR A 411 5775 5965 5050 -349 -36 -410 C
ATOM 3427 CG TYR A 411 7.776 -2.185 -47.222 1.00 41.25 C
ANISOU 3427 CG TYR A 411 5357 5674 4639 -288 -44 -369 C
ATOM 3428 CD1 TYR A 411 7.425 -1.817 -48.523 1.00 40.18 C
ANISOU 3428 CD1 TYR A 411 5170 5642 4453 -277 -33 -381 C
ATOM 3429 CD2 TYR A 411 7.818 -1.186 -46.250 1.00 37.16 C
ANISOU 3429 CD2 TYR A 411 4849 5134 4134 -240 -57 -316 C
ATOM 3430 CE1 TYR A 411 7.142 -0.493 -48.842 1.00 37.34 C
ANISOU 3430 CE1 TYR A 411 4775 5354 4058 -212 -33 -334 C
ATOM 3431 CE2 TYR A 411 7.533 0.135 -46.563 1.00 35.06 C
ANISOU 3431 CE2 TYR A 411 4550 4931 3837 -181 -52 -276 C
ATOM 3432 CZ TYR A 411 7.206 0.478 -47.848 1.00 35.36 C
ANISOU 3432 CZ TYR A 411 4543 5065 3828 -163 -39 -282 C
ATOM 3433 OH TYR A 411 6.937 1.794 -48.148 1.00 36.15 O
ANISOU 3433 OH TYR A 411 4616 5220 3896 -96 -27 -233 O
ATOM 3434 N GLU A 412 11.153 -2.322 -46.893 1.00 40.16 N
ANISOU 3434 N GLU A 412 5301 5301 4655 -215 -55 -354 N
ATOM 3435 CA GLU A 412 12.059 -1.439 -46.193 1.00 37.69 C
ANISOU 3435 CA GLU A 412 5003 4936 4380 -163 -68 -315 C
ATOM 3436 C GLU A 412 11.308 -0.219 -45.702 1.00 36.18 C
ANISOU 3436 C GLU A 412 4795 4797 4155 -137 -71 -275 C
ATOM 3437 O GLU A 412 10.885 0.642 -46.482 1.00 40.41 O
ANISOU 3437 O GLU A 412 5298 5403 4652 -110 -56 -262 O
ATOM 3438 CB GLU A 412 13.221 -1.023 -47.095 1.00 38.29 C
ANISOU 3438 CB GLU A 412 5070 4995 4482 -127 -59 -321 C
ATOM 3439 CG GLU A 412 14.340 -2.035 -47.143 1.00 39.38 C
ANISOU 3439 CG GLU A 412 5234 5054 4675 -134 -60 -347 C
ATOM 3440 CD GLU A 412 15.446 -1.630 -48.098 1.00 40.38 C
ANISOU 3440 CD GLU A 412 5346 5171 4824 -102 -49 -359 C
ATOM 3441 OE1 GLU A 412 16.393 -0.913 -47.683 1.00 38.89 O
ANISOU 3441 OE1 GLU A 412 5160 4949 4666 -65 -56 -338 O
ATOM 3442 OE2 GLU A 412 15.368 -2.043 -49.263 1.00 40.63 O
ANISOU 3442 OE2 GLU A 412 5363 5234 4840 -118 -30 -392 O
ATOM 3443 N ILE A 413 11.190 -0.133 -44.396 1.00 34.58 N
ANISOU 3443 N ILE A 413 4615 4557 3964 -140 -85 -252 N
ATOM 3444 CA ILE A 413 10.264 0.780 -43.745 1.00 33.44 C
ANISOU 3444 CA ILE A 413 4460 4458 3787 -128 -84 -220 C
ATOM 3445 C ILE A 413 10.655 2.245 -44.003 1.00 32.41 C
ANISOU 3445 C ILE A 413 4318 4340 3657 -72 -66 -191 C
ATOM 3446 O ILE A 413 9.811 3.123 -43.990 1.00 32.30 O
ANISOU 3446 O ILE A 413 4286 4380 3606 -49 -51 -165 O
ATOM 3447 CB ILE A 413 10.144 0.436 -42.228 1.00 32.17 C
ANISOU 3447 CB ILE A 413 4332 4248 3642 -150 -102 -207 C
ATOM 3448 CG1 ILE A 413 8.997 1.202 -41.545 1.00 33.19 C
ANISOU 3448 CG1 ILE A 413 4449 4428 3732 -147 -97 -181 C
ATOM 3449 CG2 ILE A 413 11.489 0.593 -41.511 1.00 30.71 C
ANISOU 3449 CG2 ILE A 413 4173 3985 3507 -128 -116 -196 C
ATOM 3450 CD1 ILE A 413 7.647 0.544 -41.651 1.00 32.31 C
ANISOU 3450 CD1 ILE A 413 4319 4381 3575 -190 -94 -196 C
ATOM 3451 N ARG A 414 11.929 2.478 -44.309 1.00 31.75 N
ANISOU 3451 N ARG A 414 4244 4205 3612 -50 -63 -196 N
ATOM 3452 CA ARG A 414 12.414 3.819 -44.629 1.00 29.93 C
ANISOU 3452 CA ARG A 414 4009 3976 3386 -5 -37 -175 C
ATOM 3453 C ARG A 414 11.676 4.416 -45.810 1.00 31.03 C
ANISOU 3453 C ARG A 414 4119 4193 3479 23 -10 -161 C
ATOM 3454 O ARG A 414 11.721 5.629 -46.002 1.00 30.83 O
ANISOU 3454 O ARG A 414 4093 4174 3445 66 21 -132 O
ATOM 3455 CB ARG A 414 13.912 3.805 -44.909 1.00 29.40 C
ANISOU 3455 CB ARG A 414 3952 3851 3367 4 -36 -193 C
ATOM 3456 CG ARG A 414 14.286 3.175 -46.241 1.00 27.71 C
ANISOU 3456 CG ARG A 414 3723 3652 3154 2 -32 -220 C
ATOM 3457 CD ARG A 414 15.774 3.194 -46.469 1.00 26.93 C
ANISOU 3457 CD ARG A 414 3630 3498 3103 13 -29 -238 C
ATOM 3458 NE ARG A 414 16.141 2.172 -47.431 1.00 25.64 N
ANISOU 3458 NE ARG A 414 3458 3333 2948 0 -33 -271 N
ATOM 3459 CZ ARG A 414 16.070 2.320 -48.751 1.00 26.02 C
ANISOU 3459 CZ ARG A 414 3487 3424 2974 8 -11 -282 C
ATOM 3460 NH1 ARG A 414 15.643 3.466 -49.303 1.00 25.18 N
ANISOU 3460 NH1 ARG A 414 3368 3366 2833 39 15 -255 N
ATOM 3461 NH2 ARG A 414 16.383 1.305 -49.520 1.00 25.76 N
ANISOU 3461 NH2 ARG A 414 3450 3387 2951 -12 -12 -319 N
ATOM 3462 N HIS A 415 11.007 3.554 -46.596 1.00 33.08 N
ANISOU 3462 N HIS A 415 4353 4511 3704 0 -18 -182 N
ATOM 3463 CA HIS A 415 10.216 3.964 -47.765 1.00 34.46 C
ANISOU 3463 CA HIS A 415 4488 4782 3821 24 1 -171 C
ATOM 3464 C HIS A 415 8.917 4.609 -47.383 1.00 36.17 C
ANISOU 3464 C HIS A 415 4684 5069 3988 45 10 -136 C
ATOM 3465 O HIS A 415 8.291 5.266 -48.222 1.00 39.15 O
ANISOU 3465 O HIS A 415 5028 5530 4314 87 31 -109 O
ATOM 3466 CB HIS A 415 9.904 2.765 -48.685 1.00 37.27 C
ANISOU 3466 CB HIS A 415 4819 5189 4150 -20 -9 -216 C
ATOM 3467 CG HIS A 415 11.065 2.316 -49.528 1.00 38.91 C
ANISOU 3467 CG HIS A 415 5036 5356 4393 -26 -6 -247 C
ATOM 3468 ND1 HIS A 415 11.720 3.143 -50.362 1.00 37.95 N
ANISOU 3468 ND1 HIS A 415 4908 5238 4272 18 16 -231 N
ATOM 3469 CD2 HIS A 415 11.678 1.076 -49.648 1.00 38.92 C
ANISOU 3469 CD2 HIS A 415 5053 5305 4428 -71 -17 -295 C
ATOM 3470 CE1 HIS A 415 12.714 2.477 -50.952 1.00 38.83 C
ANISOU 3470 CE1 HIS A 415 5028 5306 4417 0 15 -269 C
ATOM 3471 NE2 HIS A 415 12.686 1.211 -50.516 1.00 37.79 N
ANISOU 3471 NE2 HIS A 415 4910 5141 4307 -52 -4 -307 N
ATOM 3472 N LYS A 416 8.453 4.375 -46.151 1.00 35.45 N
ANISOU 3472 N LYS A 416 4608 4952 3905 18 -5 -133 N
ATOM 3473 CA LYS A 416 7.228 5.011 -45.647 1.00 35.64 C
ANISOU 3473 CA LYS A 416 4614 5038 3887 39 4 -100 C
ATOM 3474 C LYS A 416 7.406 6.520 -45.418 1.00 34.75 C
ANISOU 3474 C LYS A 416 4516 4903 3781 105 42 -52 C
ATOM 3475 O LYS A 416 6.429 7.279 -45.427 1.00 35.80 O
ANISOU 3475 O LYS A 416 4628 5100 3873 147 65 -15 O
ATOM 3476 CB LYS A 416 6.745 4.332 -44.343 1.00 39.04 C
ANISOU 3476 CB LYS A 416 5063 5442 4328 -11 -19 -114 C
ATOM 3477 CG LYS A 416 5.342 3.688 -44.408 1.00 42.74 C
ANISOU 3477 CG LYS A 416 5492 6006 4739 -48 -28 -128 C
ATOM 3478 CD LYS A 416 4.963 3.244 -45.822 1.00 43.48 C
ANISOU 3478 CD LYS A 416 5539 6195 4786 -56 -25 -151 C
ATOM 3479 CE LYS A 416 3.588 2.616 -45.888 1.00 47.11 C
ANISOU 3479 CE LYS A 416 5953 6762 5184 -100 -31 -174 C
ATOM 3480 NZ LYS A 416 3.630 1.124 -45.948 1.00 47.43 N
ANISOU 3480 NZ LYS A 416 6004 6783 5234 -188 -45 -236 N
ATOM 3481 N PHE A 417 8.653 6.948 -45.274 1.00 30.52 N
ANISOU 3481 N PHE A 417 4017 4281 3298 115 53 -54 N
ATOM 3482 CA PHE A 417 8.956 8.265 -44.769 1.00 30.94 C
ANISOU 3482 CA PHE A 417 4097 4287 3369 157 93 -21 C
ATOM 3483 C PHE A 417 9.523 9.219 -45.817 1.00 32.68 C
ANISOU 3483 C PHE A 417 4322 4503 3589 212 139 0 C
ATOM 3484 O PHE A 417 10.136 8.800 -46.789 1.00 36.28 O
ANISOU 3484 O PHE A 417 4768 4966 4050 208 132 -18 O
ATOM 3485 CB PHE A 417 9.881 8.128 -43.553 1.00 29.88 C
ANISOU 3485 CB PHE A 417 4002 4061 3290 119 77 -44 C
ATOM 3486 CG PHE A 417 9.362 7.155 -42.522 1.00 29.06 C
ANISOU 3486 CG PHE A 417 3898 3956 3183 69 35 -61 C
ATOM 3487 CD1 PHE A 417 8.124 7.360 -41.924 1.00 29.29 C
ANISOU 3487 CD1 PHE A 417 3918 4032 3178 71 40 -41 C
ATOM 3488 CD2 PHE A 417 10.070 6.022 -42.196 1.00 29.46 C
ANISOU 3488 CD2 PHE A 417 3961 3964 3265 23 -3 -94 C
ATOM 3489 CE1 PHE A 417 7.621 6.474 -40.992 1.00 29.14 C
ANISOU 3489 CE1 PHE A 417 3902 4012 3155 21 6 -56 C
ATOM 3490 CE2 PHE A 417 9.572 5.114 -41.267 1.00 29.83 C
ANISOU 3490 CE2 PHE A 417 4016 4008 3309 -19 -35 -104 C
ATOM 3491 CZ PHE A 417 8.340 5.338 -40.674 1.00 29.28 C
ANISOU 3491 CZ PHE A 417 3938 3982 3204 -24 -29 -86 C
ATOM 3492 N LYS A 418 9.275 10.508 -45.627 1.00 34.28 N
ANISOU 3492 N LYS A 418 4542 4694 3786 263 192 42 N
ATOM 3493 CA LYS A 418 9.823 11.548 -46.481 1.00 34.71 C
ANISOU 3493 CA LYS A 418 4613 4730 3844 317 250 69 C
ATOM 3494 C LYS A 418 10.662 12.507 -45.629 1.00 34.92 C
ANISOU 3494 C LYS A 418 4691 4656 3921 312 294 65 C
ATOM 3495 O LYS A 418 10.126 13.398 -44.970 1.00 35.66 O
ANISOU 3495 O LYS A 418 4805 4733 4009 339 337 94 O
ATOM 3496 CB LYS A 418 8.693 12.297 -47.204 1.00 35.68 C
ANISOU 3496 CB LYS A 418 4713 4937 3907 393 290 128 C
ATOM 3497 CG LYS A 418 9.170 13.492 -48.021 1.00 37.79 C
ANISOU 3497 CG LYS A 418 5006 5176 4174 459 362 169 C
ATOM 3498 CD LYS A 418 8.022 14.217 -48.731 1.00 38.67 C
ANISOU 3498 CD LYS A 418 5092 5377 4221 548 403 239 C
ATOM 3499 CE LYS A 418 8.582 15.130 -49.815 1.00 41.04 C
ANISOU 3499 CE LYS A 418 5417 5660 4516 611 469 278 C
ATOM 3500 NZ LYS A 418 7.672 16.235 -50.227 1.00 44.31 N
ANISOU 3500 NZ LYS A 418 5831 6121 4881 715 536 361 N
ATOM 3501 N LEU A 419 11.981 12.315 -45.647 1.00 34.42 N
ANISOU 3501 N LEU A 419 4644 4530 3902 276 287 26 N
ATOM 3502 CA LEU A 419 12.877 13.095 -44.811 1.00 33.03 C
ANISOU 3502 CA LEU A 419 4508 4269 3770 254 323 8 C
ATOM 3503 C LEU A 419 13.424 14.317 -45.528 1.00 34.42 C
ANISOU 3503 C LEU A 419 4715 4406 3956 294 404 28 C
ATOM 3504 O LEU A 419 13.953 15.236 -44.892 1.00 34.19 O
ANISOU 3504 O LEU A 419 4724 4311 3955 282 458 18 O
ATOM 3505 CB LEU A 419 14.043 12.226 -44.353 1.00 35.51 C
ANISOU 3505 CB LEU A 419 4819 4546 4126 192 272 -45 C
ATOM 3506 CG LEU A 419 13.696 10.888 -43.696 1.00 38.46 C
ANISOU 3506 CG LEU A 419 5170 4944 4496 152 195 -65 C
ATOM 3507 CD1 LEU A 419 14.967 10.149 -43.302 1.00 36.38 C
ANISOU 3507 CD1 LEU A 419 4906 4641 4274 107 155 -110 C
ATOM 3508 CD2 LEU A 419 12.782 11.106 -42.483 1.00 39.51 C
ANISOU 3508 CD2 LEU A 419 5314 5083 4615 142 193 -51 C
ATOM 3509 N TRP A 420 13.324 14.308 -46.856 1.00 34.72 N
ANISOU 3509 N TRP A 420 4737 4486 3967 337 417 53 N
ATOM 3510 CA TRP A 420 13.952 15.320 -47.692 1.00 35.99 C
ANISOU 3510 CA TRP A 420 4928 4609 4135 373 493 71 C
ATOM 3511 C TRP A 420 12.928 16.092 -48.448 1.00 35.52 C
ANISOU 3511 C TRP A 420 4870 4597 4026 458 546 142 C
ATOM 3512 O TRP A 420 12.106 15.512 -49.159 1.00 36.06 O
ANISOU 3512 O TRP A 420 4896 4758 4046 488 510 167 O
ATOM 3513 CB TRP A 420 14.917 14.657 -48.679 1.00 35.69 C
ANISOU 3513 CB TRP A 420 4872 4578 4109 353 466 39 C
ATOM 3514 CG TRP A 420 15.901 13.760 -47.997 1.00 34.66 C
ANISOU 3514 CG TRP A 420 4731 4413 4023 280 407 -24 C
ATOM 3515 CD1 TRP A 420 15.773 12.402 -47.739 1.00 33.54 C
ANISOU 3515 CD1 TRP A 420 4555 4305 3881 244 325 -53 C
ATOM 3516 CD2 TRP A 420 17.194 14.136 -47.445 1.00 34.20 C
ANISOU 3516 CD2 TRP A 420 4695 4284 4015 236 429 -68 C
ATOM 3517 NE1 TRP A 420 16.879 11.929 -47.082 1.00 32.18 N
ANISOU 3517 NE1 TRP A 420 4384 4087 3754 193 295 -102 N
ATOM 3518 CE2 TRP A 420 17.773 12.923 -46.891 1.00 33.78 C
ANISOU 3518 CE2 TRP A 420 4614 4233 3986 184 351 -115 C
ATOM 3519 CE3 TRP A 420 17.915 15.312 -47.383 1.00 36.47 C
ANISOU 3519 CE3 TRP A 420 5021 4508 4325 233 507 -75 C
ATOM 3520 CZ2 TRP A 420 19.007 12.917 -46.274 1.00 35.57 C
ANISOU 3520 CZ2 TRP A 420 4844 4417 4254 138 345 -163 C
ATOM 3521 CZ3 TRP A 420 19.176 15.291 -46.764 1.00 37.39 C
ANISOU 3521 CZ3 TRP A 420 5140 4581 4485 173 503 -133 C
ATOM 3522 CH2 TRP A 420 19.697 14.124 -46.219 1.00 36.58 C
ANISOU 3522 CH2 TRP A 420 5002 4496 4400 130 420 -175 C
ATOM 3523 N ASN A 421 12.965 17.410 -48.315 1.00 35.42 N
ANISOU 3523 N ASN A 421 4907 4526 4023 497 639 175 N
ATOM 3524 CA ASN A 421 12.058 18.247 -49.074 1.00 38.01 C
ANISOU 3524 CA ASN A 421 5243 4893 4304 593 702 254 C
ATOM 3525 C ASN A 421 12.835 19.249 -49.892 1.00 37.81 C
ANISOU 3525 C ASN A 421 5265 4807 4292 628 793 276 C
ATOM 3526 O ASN A 421 13.332 20.250 -49.360 1.00 37.91 O
ANISOU 3526 O ASN A 421 5337 4722 4342 619 875 270 O
ATOM 3527 CB ASN A 421 11.023 18.948 -48.167 1.00 40.03 C
ANISOU 3527 CB ASN A 421 5517 5142 4550 631 742 292 C
ATOM 3528 CG ASN A 421 10.051 19.831 -48.956 1.00 43.43 C
ANISOU 3528 CG ASN A 421 5952 5620 4928 745 812 383 C
ATOM 3529 OD1 ASN A 421 10.152 19.956 -50.185 1.00 44.13 O
ANISOU 3529 OD1 ASN A 421 6032 5749 4985 797 831 420 O
ATOM 3530 ND2 ASN A 421 9.104 20.450 -48.250 1.00 44.61 N
ANISOU 3530 ND2 ASN A 421 6114 5768 5066 790 852 422 N
ATOM 3531 N PHE A 422 12.922 18.982 -51.196 1.00 36.59 N
ANISOU 3531 N PHE A 422 5087 4712 4104 663 784 299 N
ATOM 3532 CA PHE A 422 13.722 19.801 -52.093 1.00 36.37 C
ANISOU 3532 CA PHE A 422 5102 4632 4084 691 865 318 C
ATOM 3533 C PHE A 422 13.338 21.282 -52.074 1.00 36.90 C
ANISOU 3533 C PHE A 422 5232 4640 4145 769 987 387 C
ATOM 3534 O PHE A 422 14.156 22.125 -52.411 1.00 36.34 O
ANISOU 3534 O PHE A 422 5219 4485 4102 772 1075 389 O
ATOM 3535 CB PHE A 422 13.689 19.257 -53.524 1.00 36.16 C
ANISOU 3535 CB PHE A 422 5034 4695 4008 724 834 340 C
ATOM 3536 CG PHE A 422 14.843 19.729 -54.373 1.00 35.48 C
ANISOU 3536 CG PHE A 422 4985 4552 3944 719 893 330 C
ATOM 3537 CD1 PHE A 422 16.121 19.202 -54.184 1.00 32.44 C
ANISOU 3537 CD1 PHE A 422 4600 4111 3612 630 863 248 C
ATOM 3538 CD2 PHE A 422 14.657 20.726 -55.346 1.00 36.32 C
ANISOU 3538 CD2 PHE A 422 5126 4659 4014 806 984 407 C
ATOM 3539 CE1 PHE A 422 17.194 19.631 -54.960 1.00 33.27 C
ANISOU 3539 CE1 PHE A 422 4736 4168 3737 620 919 235 C
ATOM 3540 CE2 PHE A 422 15.736 21.171 -56.123 1.00 36.63 C
ANISOU 3540 CE2 PHE A 422 5204 4641 4073 797 1045 397 C
ATOM 3541 CZ PHE A 422 17.012 20.616 -55.927 1.00 34.20 C
ANISOU 3541 CZ PHE A 422 4891 4281 3820 699 1011 307 C
ATOM 3542 N ASN A 423 12.105 21.579 -51.667 1.00 38.67 N
ANISOU 3542 N ASN A 423 5448 4906 4337 831 998 442 N
ATOM 3543 CA ASN A 423 11.612 22.969 -51.529 1.00 42.26 C
ANISOU 3543 CA ASN A 423 5966 5302 4788 914 1119 513 C
ATOM 3544 C ASN A 423 11.950 23.643 -50.187 1.00 40.96 C
ANISOU 3544 C ASN A 423 5860 5017 4684 861 1177 471 C
ATOM 3545 O ASN A 423 11.764 24.858 -50.037 1.00 39.83 O
ANISOU 3545 O ASN A 423 5784 4797 4551 915 1295 517 O
ATOM 3546 CB ASN A 423 10.093 23.021 -51.723 1.00 46.69 C
ANISOU 3546 CB ASN A 423 6485 5970 5281 1015 1109 595 C
ATOM 3547 CG ASN A 423 9.643 22.351 -53.004 1.00 55.74 C
ANISOU 3547 CG ASN A 423 7563 7256 6356 1065 1050 633 C
ATOM 3548 OD1 ASN A 423 10.034 22.754 -54.111 1.00 60.88 O
ANISOU 3548 OD1 ASN A 423 8233 7912 6986 1113 1097 672 O
ATOM 3549 ND2 ASN A 423 8.812 21.315 -52.865 1.00 58.60 N
ANISOU 3549 ND2 ASN A 423 7847 7738 6679 1048 948 618 N
ATOM 3550 N ASN A 424 12.395 22.851 -49.204 1.00 37.39 N
ANISOU 3550 N ASN A 424 5384 4553 4268 757 1098 388 N
ATOM 3551 CA ASN A 424 12.709 23.371 -47.875 1.00 34.26 C
ANISOU 3551 CA ASN A 424 5033 4063 3922 695 1140 340 C
ATOM 3552 C ASN A 424 13.947 22.667 -47.357 1.00 32.80 C
ANISOU 3552 C ASN A 424 4834 3847 3781 578 1078 242 C
ATOM 3553 O ASN A 424 13.854 21.721 -46.577 1.00 31.96 O
ANISOU 3553 O ASN A 424 4683 3779 3679 520 983 198 O
ATOM 3554 CB ASN A 424 11.505 23.192 -46.925 1.00 34.18 C
ANISOU 3554 CB ASN A 424 4998 4095 3891 714 1107 358 C
ATOM 3555 CG ASN A 424 11.565 24.113 -45.698 1.00 34.16 C
ANISOU 3555 CG ASN A 424 5057 3993 3929 682 1189 333 C
ATOM 3556 OD1 ASN A 424 12.461 24.949 -45.571 1.00 34.74 O
ANISOU 3556 OD1 ASN A 424 5192 3963 4041 647 1279 303 O
ATOM 3557 ND2 ASN A 424 10.603 23.964 -44.801 1.00 33.21 N
ANISOU 3557 ND2 ASN A 424 4918 3904 3795 689 1162 342 N
ATOM 3558 N GLN A 425 15.108 23.121 -47.827 1.00 33.41 N
ANISOU 3558 N GLN A 425 4946 3858 3888 546 1135 212 N
ATOM 3559 CA GLN A 425 16.381 22.402 -47.661 1.00 33.95 C
ANISOU 3559 CA GLN A 425 4989 3916 3991 449 1074 127 C
ATOM 3560 C GLN A 425 17.122 22.829 -46.394 1.00 33.73 C
ANISOU 3560 C GLN A 425 4991 3814 4008 359 1106 53 C
ATOM 3561 O GLN A 425 17.104 24.004 -46.021 1.00 33.05 O
ANISOU 3561 O GLN A 425 4969 3649 3938 362 1218 59 O
ATOM 3562 CB GLN A 425 17.296 22.570 -48.903 1.00 33.16 C
ANISOU 3562 CB GLN A 425 4902 3801 3896 456 1111 126 C
ATOM 3563 CG GLN A 425 16.577 22.474 -50.246 1.00 33.32 C
ANISOU 3563 CG GLN A 425 4906 3889 3865 553 1110 206 C
ATOM 3564 CD GLN A 425 17.475 22.096 -51.436 1.00 33.73 C
ANISOU 3564 CD GLN A 425 4941 3958 3914 543 1097 190 C
ATOM 3565 OE1 GLN A 425 18.707 22.073 -51.347 1.00 32.72 O
ANISOU 3565 OE1 GLN A 425 4822 3780 3828 470 1106 123 O
ATOM 3566 NE2 GLN A 425 16.840 21.811 -52.567 1.00 33.12 N
ANISOU 3566 NE2 GLN A 425 4837 3961 3785 617 1077 251 N
ATOM 3567 N ILE A 426 17.785 21.867 -45.753 1.00 32.19 N
ANISOU 3567 N ILE A 426 4751 3648 3832 279 1012 -14 N
ATOM 3568 CA ILE A 426 18.417 22.072 -44.456 1.00 31.09 C
ANISOU 3568 CA ILE A 426 4621 3468 3723 190 1019 -86 C
ATOM 3569 C ILE A 426 19.909 21.859 -44.631 1.00 32.14 C
ANISOU 3569 C ILE A 426 4738 3586 3885 118 1008 -157 C
ATOM 3570 O ILE A 426 20.324 20.842 -45.188 1.00 31.81 O
ANISOU 3570 O ILE A 426 4647 3598 3841 115 924 -167 O
ATOM 3571 CB ILE A 426 17.850 21.067 -43.426 1.00 30.81 C
ANISOU 3571 CB ILE A 426 4538 3491 3676 165 911 -99 C
ATOM 3572 CG1 ILE A 426 16.332 21.240 -43.309 1.00 30.29 C
ANISOU 3572 CG1 ILE A 426 4481 3449 3578 238 919 -29 C
ATOM 3573 CG2 ILE A 426 18.584 21.161 -42.076 1.00 31.04 C
ANISOU 3573 CG2 ILE A 426 4568 3496 3728 71 905 -174 C
ATOM 3574 CD1 ILE A 426 15.630 20.258 -42.388 1.00 32.11 C
ANISOU 3574 CD1 ILE A 426 4668 3739 3792 219 820 -35 C
ATOM 3575 N SER A 427 20.734 22.818 -44.209 1.00 33.79 N
ANISOU 3575 N SER A 427 4988 3728 4121 57 1099 -209 N
ATOM 3576 CA SER A 427 22.170 22.687 -44.498 1.00 35.85 C
ANISOU 3576 CA SER A 427 5230 3985 4407 -8 1098 -277 C
ATOM 3577 C SER A 427 22.755 21.506 -43.730 1.00 34.83 C
ANISOU 3577 C SER A 427 5029 3922 4281 -67 975 -333 C
ATOM 3578 O SER A 427 22.164 21.036 -42.756 1.00 33.38 O
ANISOU 3578 O SER A 427 4826 3770 4086 -76 914 -331 O
ATOM 3579 CB SER A 427 22.957 23.980 -44.228 1.00 37.15 C
ANISOU 3579 CB SER A 427 5451 4067 4596 -71 1229 -330 C
ATOM 3580 OG SER A 427 23.392 24.070 -42.885 1.00 39.84 O
ANISOU 3580 OG SER A 427 5779 4411 4946 -160 1220 -404 O
ATOM 3581 N ASP A 428 23.918 21.050 -44.157 1.00 34.91 N
ANISOU 3581 N ASP A 428 5003 3953 4307 -105 944 -380 N
ATOM 3582 CA ASP A 428 24.502 19.851 -43.599 1.00 38.54 C
ANISOU 3582 CA ASP A 428 5393 4479 4770 -143 829 -421 C
ATOM 3583 C ASP A 428 24.980 19.991 -42.154 1.00 40.10 C
ANISOU 3583 C ASP A 428 5574 4690 4971 -222 818 -484 C
ATOM 3584 O ASP A 428 25.387 18.996 -41.536 1.00 43.61 O
ANISOU 3584 O ASP A 428 5961 5194 5412 -246 721 -510 O
ATOM 3585 CB ASP A 428 25.619 19.308 -44.508 1.00 38.94 C
ANISOU 3585 CB ASP A 428 5405 4552 4836 -153 802 -451 C
ATOM 3586 CG ASP A 428 26.768 20.285 -44.692 1.00 39.82 C
ANISOU 3586 CG ASP A 428 5536 4624 4969 -214 896 -512 C
ATOM 3587 OD1 ASP A 428 26.766 21.373 -44.077 1.00 42.29 O
ANISOU 3587 OD1 ASP A 428 5893 4889 5285 -257 986 -537 O
ATOM 3588 OD2 ASP A 428 27.704 19.948 -45.440 1.00 39.15 O
ANISOU 3588 OD2 ASP A 428 5421 4556 4896 -225 885 -539 O
ATOM 3589 N ASP A 429 24.933 21.209 -41.613 1.00 40.13 N
ANISOU 3589 N ASP A 429 5627 4639 4978 -262 920 -509 N
ATOM 3590 CA ASP A 429 25.365 21.423 -40.226 1.00 42.11 C
ANISOU 3590 CA ASP A 429 5862 4910 5225 -345 917 -576 C
ATOM 3591 C ASP A 429 24.221 21.745 -39.260 1.00 41.15 C
ANISOU 3591 C ASP A 429 5774 4773 5087 -336 930 -549 C
ATOM 3592 O ASP A 429 24.450 22.237 -38.152 1.00 43.95 O
ANISOU 3592 O ASP A 429 6133 5129 5436 -407 960 -603 O
ATOM 3593 CB ASP A 429 26.511 22.449 -40.129 1.00 46.21 C
ANISOU 3593 CB ASP A 429 6398 5397 5760 -432 1018 -657 C
ATOM 3594 CG ASP A 429 26.069 23.882 -40.436 1.00 51.81 C
ANISOU 3594 CG ASP A 429 7197 6005 6479 -428 1170 -645 C
ATOM 3595 OD1 ASP A 429 24.879 24.125 -40.738 1.00 50.36 O
ANISOU 3595 OD1 ASP A 429 7061 5782 6290 -350 1197 -568 O
ATOM 3596 OD2 ASP A 429 26.941 24.780 -40.374 1.00 57.08 O
ANISOU 3596 OD2 ASP A 429 7889 6636 7161 -504 1268 -714 O
ATOM 3597 N ASN A 430 22.994 21.472 -39.694 1.00 38.07 N
ANISOU 3597 N ASN A 430 5403 4376 4686 -251 910 -468 N
ATOM 3598 CA ASN A 430 21.836 21.571 -38.832 1.00 36.90 C
ANISOU 3598 CA ASN A 430 5274 4226 4520 -233 905 -436 C
ATOM 3599 C ASN A 430 21.086 20.251 -38.749 1.00 34.27 C
ANISOU 3599 C ASN A 430 4895 3957 4167 -186 781 -389 C
ATOM 3600 O ASN A 430 19.907 20.181 -39.095 1.00 35.09 O
ANISOU 3600 O ASN A 430 5016 4059 4256 -117 780 -323 O
ATOM 3601 CB ASN A 430 20.898 22.699 -39.288 1.00 39.62 C
ANISOU 3601 CB ASN A 430 5690 4496 4865 -176 1020 -384 C
ATOM 3602 CG ASN A 430 20.058 23.268 -38.133 1.00 43.69 C
ANISOU 3602 CG ASN A 430 6238 4990 5370 -191 1060 -384 C
ATOM 3603 OD1 ASN A 430 19.821 22.589 -37.114 1.00 42.50 O
ANISOU 3603 OD1 ASN A 430 6052 4892 5204 -222 979 -400 O
ATOM 3604 ND2 ASN A 430 19.605 24.513 -38.287 1.00 43.08 N
ANISOU 3604 ND2 ASN A 430 6232 4833 5301 -167 1191 -364 N
ATOM 3605 N PRO A 431 21.763 19.188 -38.278 1.00 32.07 N
ANISOU 3605 N PRO A 431 4559 3739 3886 -222 681 -422 N
ATOM 3606 CA PRO A 431 21.078 17.916 -38.127 1.00 31.11 C
ANISOU 3606 CA PRO A 431 4402 3669 3748 -185 573 -381 C
ATOM 3607 C PRO A 431 19.915 17.961 -37.137 1.00 31.21 C
ANISOU 3607 C PRO A 431 4431 3687 3738 -179 564 -355 C
ATOM 3608 O PRO A 431 18.901 17.288 -37.350 1.00 33.17 O
ANISOU 3608 O PRO A 431 4673 3958 3972 -129 516 -302 O
ATOM 3609 CB PRO A 431 22.191 16.968 -37.644 1.00 31.77 C
ANISOU 3609 CB PRO A 431 4429 3806 3836 -230 489 -426 C
ATOM 3610 CG PRO A 431 23.241 17.847 -37.091 1.00 31.96 C
ANISOU 3610 CG PRO A 431 4453 3820 3867 -303 548 -497 C
ATOM 3611 CD PRO A 431 23.187 19.094 -37.916 1.00 31.65 C
ANISOU 3611 CD PRO A 431 4468 3711 3843 -294 666 -495 C
ATOM 3612 N ALA A 432 20.028 18.783 -36.094 1.00 30.46 N
ANISOU 3612 N ALA A 432 4358 3574 3641 -234 617 -394 N
ATOM 3613 CA ALA A 432 18.987 18.855 -35.073 1.00 29.38 C
ANISOU 3613 CA ALA A 432 4236 3443 3482 -236 612 -377 C
ATOM 3614 C ALA A 432 17.643 19.304 -35.684 1.00 28.93 C
ANISOU 3614 C ALA A 432 4216 3355 3419 -160 662 -309 C
ATOM 3615 O ALA A 432 16.597 18.698 -35.428 1.00 27.15 O
ANISOU 3615 O ALA A 432 3980 3161 3172 -126 610 -267 O
ATOM 3616 CB ALA A 432 19.422 19.768 -33.926 1.00 29.64 C
ANISOU 3616 CB ALA A 432 4289 3460 3513 -315 674 -439 C
ATOM 3617 N ARG A 433 17.689 20.335 -36.521 1.00 28.90 N
ANISOU 3617 N ARG A 433 4255 3295 3431 -130 762 -296 N
ATOM 3618 CA ARG A 433 16.518 20.759 -37.271 1.00 30.33 C
ANISOU 3618 CA ARG A 433 4466 3456 3602 -44 810 -224 C
ATOM 3619 C ARG A 433 15.942 19.616 -38.132 1.00 30.32 C
ANISOU 3619 C ARG A 433 4421 3515 3582 16 719 -172 C
ATOM 3620 O ARG A 433 14.750 19.372 -38.115 1.00 32.24 O
ANISOU 3620 O ARG A 433 4658 3788 3801 64 699 -123 O
ATOM 3621 CB ARG A 433 16.861 21.974 -38.149 1.00 31.80 C
ANISOU 3621 CB ARG A 433 4703 3570 3806 -18 932 -216 C
ATOM 3622 CG ARG A 433 15.691 22.434 -38.990 1.00 33.13 C
ANISOU 3622 CG ARG A 433 4899 3727 3959 84 984 -132 C
ATOM 3623 CD ARG A 433 16.013 23.579 -39.933 1.00 35.74 C
ANISOU 3623 CD ARG A 433 5286 3987 4306 122 1106 -112 C
ATOM 3624 NE ARG A 433 14.958 23.689 -40.948 1.00 37.32 N
ANISOU 3624 NE ARG A 433 5491 4208 4481 234 1125 -21 N
ATOM 3625 CZ ARG A 433 15.093 24.303 -42.124 1.00 37.80 C
ANISOU 3625 CZ ARG A 433 5583 4237 4542 294 1198 21 C
ATOM 3626 NH1 ARG A 433 16.232 24.898 -42.456 1.00 37.49 N
ANISOU 3626 NH1 ARG A 433 5579 4133 4531 250 1268 -20 N
ATOM 3627 NH2 ARG A 433 14.077 24.323 -42.968 1.00 39.66 N
ANISOU 3627 NH2 ARG A 433 5812 4512 4744 398 1204 106 N
ATOM 3628 N PHE A 434 16.796 18.934 -38.886 1.00 29.68 N
ANISOU 3628 N PHE A 434 4309 3453 3511 9 670 -187 N
ATOM 3629 CA PHE A 434 16.380 17.766 -39.667 1.00 30.08 C
ANISOU 3629 CA PHE A 434 4320 3562 3547 51 585 -152 C
ATOM 3630 C PHE A 434 15.694 16.758 -38.761 1.00 29.19 C
ANISOU 3630 C PHE A 434 4178 3497 3415 35 499 -148 C
ATOM 3631 O PHE A 434 14.575 16.305 -39.053 1.00 27.53 O
ANISOU 3631 O PHE A 434 3954 3325 3179 79 471 -103 O
ATOM 3632 CB PHE A 434 17.604 17.132 -40.370 1.00 29.61 C
ANISOU 3632 CB PHE A 434 4232 3511 3507 29 545 -185 C
ATOM 3633 CG PHE A 434 17.291 15.912 -41.215 1.00 29.08 C
ANISOU 3633 CG PHE A 434 4126 3495 3426 63 467 -159 C
ATOM 3634 CD1 PHE A 434 16.884 16.045 -42.530 1.00 29.67 C
ANISOU 3634 CD1 PHE A 434 4202 3582 3487 122 492 -118 C
ATOM 3635 CD2 PHE A 434 17.532 14.624 -40.730 1.00 30.50 C
ANISOU 3635 CD2 PHE A 434 4268 3710 3608 33 373 -180 C
ATOM 3636 CE1 PHE A 434 16.664 14.927 -43.330 1.00 30.08 C
ANISOU 3636 CE1 PHE A 434 4218 3685 3525 143 425 -105 C
ATOM 3637 CE2 PHE A 434 17.325 13.499 -41.533 1.00 28.96 C
ANISOU 3637 CE2 PHE A 434 4044 3554 3405 56 312 -165 C
ATOM 3638 CZ PHE A 434 16.875 13.650 -42.826 1.00 27.69 C
ANISOU 3638 CZ PHE A 434 3883 3409 3228 106 338 -131 C
ATOM 3639 N LEU A 435 16.343 16.430 -37.642 1.00 30.11 N
ANISOU 3639 N LEU A 435 4283 3616 3541 -29 461 -195 N
ATOM 3640 CA LEU A 435 15.724 15.531 -36.674 1.00 30.90 C
ANISOU 3640 CA LEU A 435 4362 3754 3621 -47 387 -189 C
ATOM 3641 C LEU A 435 14.350 16.027 -36.227 1.00 31.00 C
ANISOU 3641 C LEU A 435 4396 3770 3611 -20 421 -153 C
ATOM 3642 O LEU A 435 13.364 15.294 -36.330 1.00 32.31 O
ANISOU 3642 O LEU A 435 4543 3976 3754 6 375 -119 O
ATOM 3643 CB LEU A 435 16.613 15.315 -35.467 1.00 32.59 C
ANISOU 3643 CB LEU A 435 4566 3975 3841 -116 354 -240 C
ATOM 3644 CG LEU A 435 16.647 13.877 -34.940 1.00 34.29 C
ANISOU 3644 CG LEU A 435 4747 4235 4046 -131 252 -238 C
ATOM 3645 CD1 LEU A 435 17.003 13.898 -33.468 1.00 32.65 C
ANISOU 3645 CD1 LEU A 435 4535 4042 3826 -188 233 -270 C
ATOM 3646 CD2 LEU A 435 15.346 13.134 -35.165 1.00 32.56 C
ANISOU 3646 CD2 LEU A 435 4524 4041 3806 -93 215 -190 C
ATOM 3647 N GLN A 436 14.284 17.274 -35.759 1.00 30.41 N
ANISOU 3647 N GLN A 436 4361 3652 3542 -29 508 -164 N
ATOM 3648 CA GLN A 436 13.037 17.831 -35.266 1.00 31.54 C
ANISOU 3648 CA GLN A 436 4525 3792 3665 -1 551 -132 C
ATOM 3649 C GLN A 436 11.978 17.894 -36.339 1.00 32.32 C
ANISOU 3649 C GLN A 436 4619 3914 3746 82 568 -68 C
ATOM 3650 O GLN A 436 10.811 17.580 -36.080 1.00 34.85 O
ANISOU 3650 O GLN A 436 4925 4275 4039 109 545 -35 O
ATOM 3651 CB GLN A 436 13.237 19.224 -34.678 1.00 32.87 C
ANISOU 3651 CB GLN A 436 4742 3898 3847 -24 657 -157 C
ATOM 3652 CG GLN A 436 14.079 19.254 -33.428 1.00 34.66 C
ANISOU 3652 CG GLN A 436 4968 4119 4079 -114 645 -224 C
ATOM 3653 CD GLN A 436 14.729 20.601 -33.214 1.00 39.08 C
ANISOU 3653 CD GLN A 436 5574 4613 4659 -151 757 -268 C
ATOM 3654 OE1 GLN A 436 14.590 21.508 -34.038 1.00 43.15 O
ANISOU 3654 OE1 GLN A 436 6129 5075 5190 -105 848 -244 O
ATOM 3655 NE2 GLN A 436 15.459 20.737 -32.114 1.00 38.61 N
ANISOU 3655 NE2 GLN A 436 5512 4558 4599 -237 755 -334 N
ATOM 3656 N LYS A 437 12.357 18.304 -37.543 1.00 31.05 N
ANISOU 3656 N LYS A 437 4468 3735 3595 124 609 -49 N
ATOM 3657 CA LYS A 437 11.386 18.350 -38.631 1.00 33.09 C
ANISOU 3657 CA LYS A 437 4714 4030 3826 209 623 13 C
ATOM 3658 C LYS A 437 10.819 16.937 -38.880 1.00 30.84 C
ANISOU 3658 C LYS A 437 4375 3826 3515 210 519 25 C
ATOM 3659 O LYS A 437 9.630 16.767 -39.091 1.00 33.33 O
ANISOU 3659 O LYS A 437 4670 4197 3797 255 509 66 O
ATOM 3660 CB LYS A 437 12.004 18.961 -39.907 1.00 34.89 C
ANISOU 3660 CB LYS A 437 4961 4229 4067 250 682 30 C
ATOM 3661 CG LYS A 437 11.000 19.276 -40.998 1.00 37.45 C
ANISOU 3661 CG LYS A 437 5278 4594 4357 347 715 103 C
ATOM 3662 CD LYS A 437 11.717 19.767 -42.240 1.00 43.09 C
ANISOU 3662 CD LYS A 437 6010 5281 5079 382 766 118 C
ATOM 3663 CE LYS A 437 10.971 19.380 -43.511 1.00 48.45 C
ANISOU 3663 CE LYS A 437 6651 6041 5714 459 742 177 C
ATOM 3664 NZ LYS A 437 9.918 20.369 -43.885 1.00 54.71 N
ANISOU 3664 NZ LYS A 437 7463 6846 6476 556 823 252 N
ATOM 3665 N ALA A 438 11.661 15.924 -38.782 1.00 29.05 N
ANISOU 3665 N ALA A 438 4126 3606 3303 157 445 -14 N
ATOM 3666 CA ALA A 438 11.204 14.550 -38.982 1.00 28.30 C
ANISOU 3666 CA ALA A 438 3989 3573 3188 149 357 -11 C
ATOM 3667 C ALA A 438 10.226 14.095 -37.887 1.00 29.86 C
ANISOU 3667 C ALA A 438 4178 3801 3365 127 322 -7 C
ATOM 3668 O ALA A 438 9.338 13.296 -38.145 1.00 29.89 O
ANISOU 3668 O ALA A 438 4151 3864 3339 138 278 10 O
ATOM 3669 CB ALA A 438 12.392 13.611 -39.071 1.00 26.74 C
ANISOU 3669 CB ALA A 438 3777 3365 3016 103 297 -52 C
ATOM 3670 N MET A 439 10.380 14.610 -36.671 1.00 30.81 N
ANISOU 3670 N MET A 439 4323 3885 3496 91 344 -27 N
ATOM 3671 CA MET A 439 9.479 14.214 -35.570 1.00 33.32 C
ANISOU 3671 CA MET A 439 4636 4230 3793 67 314 -25 C
ATOM 3672 C MET A 439 8.175 15.044 -35.460 1.00 35.06 C
ANISOU 3672 C MET A 439 4863 4469 3987 116 372 13 C
ATOM 3673 O MET A 439 7.327 14.751 -34.626 1.00 35.64 O
ANISOU 3673 O MET A 439 4929 4570 4040 99 352 17 O
ATOM 3674 CB MET A 439 10.232 14.167 -34.243 1.00 30.31 C
ANISOU 3674 CB MET A 439 4271 3816 3426 0 297 -67 C
ATOM 3675 CG MET A 439 11.272 13.060 -34.191 1.00 31.04 C
ANISOU 3675 CG MET A 439 4346 3912 3534 -39 224 -95 C
ATOM 3676 SD MET A 439 10.517 11.410 -34.249 1.00 32.77 S
ANISOU 3676 SD MET A 439 4536 4183 3731 -45 138 -78 S
ATOM 3677 CE MET A 439 10.712 10.895 -35.967 1.00 29.80 C
ANISOU 3677 CE MET A 439 4136 3824 3361 -5 126 -67 C
ATOM 3678 N ASP A 440 8.035 16.056 -36.314 1.00 36.17 N
ANISOU 3678 N ASP A 440 5018 4595 4128 178 445 44 N
ATOM 3679 CA ASP A 440 6.788 16.816 -36.479 1.00 41.00 C
ANISOU 3679 CA ASP A 440 5630 5234 4713 247 503 94 C
ATOM 3680 C ASP A 440 5.585 15.908 -36.793 1.00 43.75 C
ANISOU 3680 C ASP A 440 5925 5677 5017 269 445 121 C
ATOM 3681 O ASP A 440 5.695 14.943 -37.552 1.00 39.61 O
ANISOU 3681 O ASP A 440 5368 5200 4482 261 385 116 O
ATOM 3682 CB ASP A 440 6.932 17.861 -37.611 1.00 41.39 C
ANISOU 3682 CB ASP A 440 5699 5258 4766 323 584 133 C
ATOM 3683 CG ASP A 440 7.615 19.163 -37.158 1.00 43.12 C
ANISOU 3683 CG ASP A 440 5981 5381 5021 316 682 117 C
ATOM 3684 OD1 ASP A 440 7.722 19.412 -35.945 1.00 44.92 O
ANISOU 3684 OD1 ASP A 440 6233 5572 5263 262 696 81 O
ATOM 3685 OD2 ASP A 440 8.003 19.973 -38.035 1.00 46.45 O
ANISOU 3685 OD2 ASP A 440 6429 5764 5453 364 753 140 O
ATOM 3686 N PHE A 441 4.432 16.293 -36.255 1.00 48.33 N
ANISOU 3686 N PHE A 441 6500 6290 5573 297 473 146 N
ATOM 3687 CA PHE A 441 3.201 15.499 -36.249 1.00 56.35 C
ANISOU 3687 CA PHE A 441 7465 7400 6544 303 424 162 C
ATOM 3688 C PHE A 441 2.559 15.132 -37.615 1.00 60.40 C
ANISOU 3688 C PHE A 441 7925 8008 7016 360 406 197 C
ATOM 3689 O PHE A 441 2.123 13.990 -37.794 1.00 62.11 O
ANISOU 3689 O PHE A 441 8099 8294 7206 325 338 181 O
ATOM 3690 CB PHE A 441 2.179 16.199 -35.327 1.00 62.78 C
ANISOU 3690 CB PHE A 441 8287 8222 7343 325 472 180 C
ATOM 3691 CG PHE A 441 0.811 15.563 -35.301 1.00 68.58 C
ANISOU 3691 CG PHE A 441 8966 9062 8030 336 436 198 C
ATOM 3692 CD1 PHE A 441 0.564 14.429 -34.525 1.00 68.60 C
ANISOU 3692 CD1 PHE A 441 8951 9090 8022 258 366 162 C
ATOM 3693 CD2 PHE A 441 -0.255 16.142 -35.998 1.00 71.74 C
ANISOU 3693 CD2 PHE A 441 9331 9537 8390 427 478 252 C
ATOM 3694 CE1 PHE A 441 -0.706 13.869 -34.472 1.00 69.77 C
ANISOU 3694 CE1 PHE A 441 9049 9335 8125 259 340 172 C
ATOM 3695 CE2 PHE A 441 -1.526 15.582 -35.949 1.00 72.53 C
ANISOU 3695 CE2 PHE A 441 9371 9745 8440 433 446 263 C
ATOM 3696 CZ PHE A 441 -1.751 14.445 -35.184 1.00 71.53 C
ANISOU 3696 CZ PHE A 441 9229 9641 8307 344 378 219 C
ATOM 3697 N PRO A 442 2.480 16.088 -38.571 1.00 61.53 N
ANISOU 3697 N PRO A 442 8071 8157 7149 446 469 244 N
ATOM 3698 CA PRO A 442 1.600 15.877 -39.742 1.00 64.39 C
ANISOU 3698 CA PRO A 442 8374 8634 7456 511 458 286 C
ATOM 3699 C PRO A 442 1.694 14.501 -40.429 1.00 63.67 C
ANISOU 3699 C PRO A 442 8236 8612 7344 461 374 254 C
ATOM 3700 O PRO A 442 0.669 13.957 -40.843 1.00 67.56 O
ANISOU 3700 O PRO A 442 8667 9218 7782 473 344 265 O
ATOM 3701 CB PRO A 442 2.023 16.996 -40.699 1.00 62.09 C
ANISOU 3701 CB PRO A 442 8109 8310 7170 597 534 334 C
ATOM 3702 CG PRO A 442 2.433 18.095 -39.783 1.00 62.67 C
ANISOU 3702 CG PRO A 442 8252 8271 7289 600 612 333 C
ATOM 3703 CD PRO A 442 3.136 17.409 -38.632 1.00 63.73 C
ANISOU 3703 CD PRO A 442 8408 8344 7462 489 560 263 C
ATOM 3704 N PHE A 443 2.899 13.947 -40.534 1.00 61.41 N
ANISOU 3704 N PHE A 443 7975 8261 7097 404 341 213 N
ATOM 3705 CA PHE A 443 3.105 12.670 -41.230 1.00 64.53 C
ANISOU 3705 CA PHE A 443 8333 8705 7478 357 272 180 C
ATOM 3706 C PHE A 443 2.355 11.497 -40.566 1.00 63.49 C
ANISOU 3706 C PHE A 443 8172 8624 7326 290 213 147 C
ATOM 3707 O PHE A 443 1.916 10.563 -41.251 1.00 65.71 O
ANISOU 3707 O PHE A 443 8408 8987 7572 267 173 131 O
ATOM 3708 CB PHE A 443 4.614 12.348 -41.348 1.00 62.25 C
ANISOU 3708 CB PHE A 443 8082 8325 7242 312 254 142 C
ATOM 3709 CG PHE A 443 5.164 11.616 -40.158 1.00 58.55 C
ANISOU 3709 CG PHE A 443 7639 7794 6811 231 211 96 C
ATOM 3710 CD1 PHE A 443 5.501 12.310 -38.992 1.00 55.82 C
ANISOU 3710 CD1 PHE A 443 7335 7375 6496 217 240 91 C
ATOM 3711 CD2 PHE A 443 5.278 10.221 -40.171 1.00 57.11 C
ANISOU 3711 CD2 PHE A 443 7439 7630 6629 170 146 59 C
ATOM 3712 CE1 PHE A 443 5.980 11.637 -37.877 1.00 53.77 C
ANISOU 3712 CE1 PHE A 443 7096 7072 6262 147 198 54 C
ATOM 3713 CE2 PHE A 443 5.752 9.539 -39.055 1.00 55.03 C
ANISOU 3713 CE2 PHE A 443 7202 7312 6395 106 110 27 C
ATOM 3714 CZ PHE A 443 6.105 10.248 -37.910 1.00 56.08 C
ANISOU 3714 CZ PHE A 443 7371 7383 6553 96 132 27 C
ATOM 3715 N ILE A 444 2.225 11.549 -39.238 1.00 62.11 N
ANISOU 3715 N ILE A 444 8024 8402 7171 253 212 134 N
ATOM 3716 CA ILE A 444 1.636 10.439 -38.452 1.00 65.40 C
ANISOU 3716 CA ILE A 444 8425 8848 7574 181 161 102 C
ATOM 3717 C ILE A 444 0.167 10.739 -38.071 1.00 67.78 C
ANISOU 3717 C ILE A 444 8690 9234 7828 206 179 126 C
ATOM 3718 O ILE A 444 -0.445 9.995 -37.290 1.00 68.42 O
ANISOU 3718 O ILE A 444 8762 9339 7896 150 149 103 O
ATOM 3719 CB ILE A 444 2.518 10.094 -37.192 1.00 59.14 C
ANISOU 3719 CB ILE A 444 7684 7954 6829 115 139 70 C
ATOM 3720 CG1 ILE A 444 2.033 8.832 -36.445 1.00 59.38 C
ANISOU 3720 CG1 ILE A 444 7708 8005 6848 41 88 40 C
ATOM 3721 CG2 ILE A 444 2.585 11.268 -36.232 1.00 58.64 C
ANISOU 3721 CG2 ILE A 444 7658 7836 6786 136 189 85 C
ATOM 3722 CD1 ILE A 444 2.596 7.517 -36.955 1.00 52.08 C
ANISOU 3722 CD1 ILE A 444 6780 7072 5933 -7 40 7 C
ATOM 3723 N CYS A 445 -0.398 11.800 -38.663 1.00 69.28 N
ANISOU 3723 N CYS A 445 8858 9471 7990 295 231 175 N
ATOM 3724 CA CYS A 445 -1.722 12.324 -38.267 1.00 73.05 C
ANISOU 3724 CA CYS A 445 9302 10024 8427 338 261 206 C
ATOM 3725 C CYS A 445 -2.880 11.316 -38.398 1.00 73.25 C
ANISOU 3725 C CYS A 445 9260 10175 8396 300 217 187 C
ATOM 3726 O CYS A 445 -3.795 11.307 -37.560 1.00 71.58 O
ANISOU 3726 O CYS A 445 9032 9999 8164 286 221 186 O
ATOM 3727 CB CYS A 445 -2.052 13.668 -38.977 1.00 78.33 C
ANISOU 3727 CB CYS A 445 9963 10721 9077 455 332 271 C
ATOM 3728 SG CYS A 445 -2.486 13.611 -40.750 1.00 81.55 S
ANISOU 3728 SG CYS A 445 10300 11262 9421 528 327 308 S
ATOM 3729 N ASN A 446 -2.819 10.457 -39.424 1.00 70.77 N
ANISOU 3729 N ASN A 446 8906 9925 8055 276 178 166 N
ATOM 3730 CA ASN A 446 -3.862 9.436 -39.662 1.00 69.49 C
ANISOU 3730 CA ASN A 446 8678 9887 7836 226 141 136 C
ATOM 3731 C ASN A 446 -3.713 8.162 -38.807 1.00 67.64 C
ANISOU 3731 C ASN A 446 8469 9605 7624 112 97 76 C
ATOM 3732 O ASN A 446 -4.381 7.148 -39.046 1.00 68.24 O
ANISOU 3732 O ASN A 446 8502 9764 7661 51 68 39 O
ATOM 3733 CB ASN A 446 -3.982 9.103 -41.161 1.00 69.78 C
ANISOU 3733 CB ASN A 446 8656 10030 7825 248 127 135 C
ATOM 3734 CG ASN A 446 -5.030 9.961 -41.871 1.00 71.60 C
ANISOU 3734 CG ASN A 446 8817 10399 7987 347 159 190 C
ATOM 3735 OD1 ASN A 446 -6.176 10.076 -41.413 1.00 69.53 O
ANISOU 3735 OD1 ASN A 446 8509 10225 7683 358 167 200 O
ATOM 3736 ND2 ASN A 446 -4.645 10.555 -43.004 1.00 67.91 N
ANISOU 3736 ND2 ASN A 446 8338 9958 7504 423 180 229 N
ATOM 3737 N SER A 447 -2.830 8.234 -37.815 1.00 64.82 N
ANISOU 3737 N SER A 447 8183 9117 7327 83 95 69 N
ATOM 3738 CA SER A 447 -2.703 7.212 -36.790 1.00 61.21 C
ANISOU 3738 CA SER A 447 7759 8605 6892 -9 63 28 C
ATOM 3739 C SER A 447 -3.175 7.839 -35.478 1.00 61.78 C
ANISOU 3739 C SER A 447 7853 8649 6969 -5 86 44 C
ATOM 3740 O SER A 447 -3.269 7.166 -34.451 1.00 63.35 O
ANISOU 3740 O SER A 447 8079 8813 7178 -73 66 19 O
ATOM 3741 CB SER A 447 -1.236 6.795 -36.669 1.00 62.30 C
ANISOU 3741 CB SER A 447 7958 8624 7090 -40 41 9 C
ATOM 3742 OG SER A 447 -1.086 5.391 -36.635 1.00 63.63 O
ANISOU 3742 OG SER A 447 8134 8779 7262 -119 4 -32 O
ATOM 3743 N PHE A 448 -3.477 9.136 -35.536 1.00 58.57 N
ANISOU 3743 N PHE A 448 7439 8259 6556 77 133 86 N
ATOM 3744 CA PHE A 448 -3.822 9.928 -34.355 1.00 57.17 C
ANISOU 3744 CA PHE A 448 7288 8045 6389 91 167 102 C
ATOM 3745 C PHE A 448 -5.205 10.567 -34.467 1.00 52.49 C
ANISOU 3745 C PHE A 448 6637 7560 5744 151 203 134 C
ATOM 3746 O PHE A 448 -5.362 11.774 -34.264 1.00 53.24 O
ANISOU 3746 O PHE A 448 6744 7636 5846 224 259 172 O
ATOM 3747 CB PHE A 448 -2.773 11.023 -34.138 1.00 61.23 C
ANISOU 3747 CB PHE A 448 7859 8451 6952 134 207 122 C
ATOM 3748 CG PHE A 448 -1.770 10.703 -33.075 1.00 58.51 C
ANISOU 3748 CG PHE A 448 7575 8000 6653 66 186 91 C
ATOM 3749 CD1 PHE A 448 -0.929 9.601 -33.197 1.00 60.10 C
ANISOU 3749 CD1 PHE A 448 7793 8165 6875 6 133 60 C
ATOM 3750 CD2 PHE A 448 -1.650 11.519 -31.955 1.00 58.69 C
ANISOU 3750 CD2 PHE A 448 7639 7963 6697 65 223 94 C
ATOM 3751 CE1 PHE A 448 -0.006 9.302 -32.201 1.00 57.17 C
ANISOU 3751 CE1 PHE A 448 7472 7709 6540 -46 112 38 C
ATOM 3752 CE2 PHE A 448 -0.719 11.237 -30.967 1.00 57.43 C
ANISOU 3752 CE2 PHE A 448 7528 7721 6570 3 202 65 C
ATOM 3753 CZ PHE A 448 0.102 10.126 -31.091 1.00 57.83 C
ANISOU 3753 CZ PHE A 448 7589 7745 6636 -48 144 40 C
ATOM 3754 N THR A 449 -6.205 9.753 -34.783 1.00 48.45 N
ANISOU 3754 N THR A 449 6062 7164 5181 119 176 116 N
ATOM 3755 CA THR A 449 -7.550 10.249 -35.021 1.00 47.78 C
ANISOU 3755 CA THR A 449 5906 7209 5038 178 203 144 C
ATOM 3756 C THR A 449 -8.504 9.809 -33.909 1.00 47.64 C
ANISOU 3756 C THR A 449 5874 7226 4999 117 198 119 C
ATOM 3757 O THR A 449 -8.097 9.137 -32.946 1.00 46.38 O
ANISOU 3757 O THR A 449 5766 6985 4871 31 174 83 O
ATOM 3758 CB THR A 449 -8.092 9.732 -36.361 1.00 47.64 C
ANISOU 3758 CB THR A 449 5808 7329 4961 191 181 140 C
ATOM 3759 OG1 THR A 449 -8.357 8.329 -36.252 1.00 47.07 O
ANISOU 3759 OG1 THR A 449 5717 7294 4870 80 134 80 O
ATOM 3760 CG2 THR A 449 -7.081 9.958 -37.468 1.00 46.76 C
ANISOU 3760 CG2 THR A 449 5715 7182 4870 233 179 157 C
ATOM 3761 N LYS A 450 -9.777 10.177 -34.063 1.00 47.82 N
ANISOU 3761 N LYS A 450 5824 7377 4966 164 221 139 N
ATOM 3762 CA LYS A 450 -10.832 9.773 -33.136 1.00 46.59 C
ANISOU 3762 CA LYS A 450 5641 7279 4780 110 219 114 C
ATOM 3763 C LYS A 450 -11.009 8.261 -33.165 1.00 43.52 C
ANISOU 3763 C LYS A 450 5236 6928 4372 -8 168 52 C
ATOM 3764 O LYS A 450 -11.461 7.667 -32.195 1.00 42.60 O
ANISOU 3764 O LYS A 450 5131 6804 4251 -86 160 20 O
ATOM 3765 CB LYS A 450 -12.175 10.436 -33.488 1.00 51.60 C
ANISOU 3765 CB LYS A 450 6186 8066 5352 193 252 149 C
ATOM 3766 CG LYS A 450 -12.095 11.712 -34.314 1.00 56.48 C
ANISOU 3766 CG LYS A 450 6788 8705 5964 333 299 218 C
ATOM 3767 CD LYS A 450 -13.478 12.289 -34.604 1.00 58.73 C
ANISOU 3767 CD LYS A 450 6978 9152 6181 420 331 257 C
ATOM 3768 CE LYS A 450 -13.965 11.934 -36.001 1.00 60.66 C
ANISOU 3768 CE LYS A 450 7127 9564 6355 453 305 265 C
ATOM 3769 NZ LYS A 450 -13.194 12.626 -37.078 1.00 65.30 N
ANISOU 3769 NZ LYS A 450 7734 10123 6955 548 323 317 N
ATOM 3770 N PHE A 451 -10.678 7.646 -34.292 1.00 42.31 N
ANISOU 3770 N PHE A 451 5056 6814 4203 -23 140 35 N
ATOM 3771 CA PHE A 451 -10.789 6.199 -34.416 1.00 42.79 C
ANISOU 3771 CA PHE A 451 5108 6900 4248 -138 102 -27 C
ATOM 3772 C PHE A 451 -9.832 5.495 -33.469 1.00 41.85 C
ANISOU 3772 C PHE A 451 5085 6625 4191 -218 83 -53 C
ATOM 3773 O PHE A 451 -10.178 4.488 -32.873 1.00 41.30 O
ANISOU 3773 O PHE A 451 5026 6551 4113 -314 71 -95 O
ATOM 3774 CB PHE A 451 -10.511 5.757 -35.843 1.00 44.29 C
ANISOU 3774 CB PHE A 451 5258 7154 4414 -135 82 -41 C
ATOM 3775 CG PHE A 451 -11.745 5.592 -36.681 1.00 48.24 C
ANISOU 3775 CG PHE A 451 5648 7852 4829 -129 83 -55 C
ATOM 3776 CD1 PHE A 451 -12.721 4.660 -36.334 1.00 49.16 C
ANISOU 3776 CD1 PHE A 451 5721 8055 4901 -227 76 -111 C
ATOM 3777 CD2 PHE A 451 -11.915 6.337 -37.845 1.00 49.89 C
ANISOU 3777 CD2 PHE A 451 5793 8166 4997 -30 92 -14 C
ATOM 3778 CE1 PHE A 451 -13.853 4.492 -37.116 1.00 51.55 C
ANISOU 3778 CE1 PHE A 451 5912 8556 5119 -229 76 -131 C
ATOM 3779 CE2 PHE A 451 -13.043 6.166 -38.637 1.00 49.86 C
ANISOU 3779 CE2 PHE A 451 5677 8362 4905 -23 89 -27 C
ATOM 3780 CZ PHE A 451 -14.007 5.242 -38.276 1.00 50.68 C
ANISOU 3780 CZ PHE A 451 5732 8560 4964 -126 79 -89 C
ATOM 3781 N GLU A 452 -8.625 6.033 -33.335 1.00 40.72 N
ANISOU 3781 N GLU A 452 5007 6356 4105 -178 85 -26 N
ATOM 3782 CA GLU A 452 -7.642 5.429 -32.469 1.00 40.49 C
ANISOU 3782 CA GLU A 452 5063 6190 4131 -241 65 -44 C
ATOM 3783 C GLU A 452 -7.869 5.773 -31.001 1.00 38.75 C
ANISOU 3783 C GLU A 452 4881 5918 3923 -259 80 -37 C
ATOM 3784 O GLU A 452 -7.702 4.917 -30.142 1.00 36.18 O
ANISOU 3784 O GLU A 452 4600 5536 3611 -337 62 -61 O
ATOM 3785 CB GLU A 452 -6.225 5.801 -32.901 1.00 42.01 C
ANISOU 3785 CB GLU A 452 5304 6281 4376 -200 58 -26 C
ATOM 3786 CG GLU A 452 -5.744 5.047 -34.142 1.00 46.69 C
ANISOU 3786 CG GLU A 452 5879 6892 4966 -216 34 -49 C
ATOM 3787 CD GLU A 452 -6.204 5.681 -35.456 1.00 47.72 C
ANISOU 3787 CD GLU A 452 5941 7134 5056 -142 49 -27 C
ATOM 3788 OE1 GLU A 452 -6.063 5.023 -36.509 1.00 50.99 O
ANISOU 3788 OE1 GLU A 452 6327 7593 5453 -162 32 -51 O
ATOM 3789 OE2 GLU A 452 -6.689 6.838 -35.448 1.00 46.75 O
ANISOU 3789 OE2 GLU A 452 5792 7054 4916 -61 81 14 O
ATOM 3790 N PHE A 453 -8.280 7.012 -30.722 1.00 38.01 N
ANISOU 3790 N PHE A 453 4772 5845 3823 -185 117 -1 N
ATOM 3791 CA PHE A 453 -8.226 7.542 -29.351 1.00 37.04 C
ANISOU 3791 CA PHE A 453 4697 5652 3722 -194 138 6 C
ATOM 3792 C PHE A 453 -9.561 7.646 -28.604 1.00 37.11 C
ANISOU 3792 C PHE A 453 4670 5740 3690 -209 160 2 C
ATOM 3793 O PHE A 453 -9.574 7.932 -27.406 1.00 38.24 O
ANISOU 3793 O PHE A 453 4853 5830 3847 -231 176 1 O
ATOM 3794 CB PHE A 453 -7.497 8.891 -29.321 1.00 37.38 C
ANISOU 3794 CB PHE A 453 4775 5625 3802 -112 175 42 C
ATOM 3795 CG PHE A 453 -6.028 8.777 -29.558 1.00 39.03 C
ANISOU 3795 CG PHE A 453 5037 5730 4059 -119 153 38 C
ATOM 3796 CD1 PHE A 453 -5.192 8.279 -28.572 1.00 39.54 C
ANISOU 3796 CD1 PHE A 453 5163 5703 4156 -183 129 19 C
ATOM 3797 CD2 PHE A 453 -5.477 9.141 -30.772 1.00 40.44 C
ANISOU 3797 CD2 PHE A 453 5202 5912 4249 -60 158 56 C
ATOM 3798 CE1 PHE A 453 -3.838 8.145 -28.793 1.00 39.99 C
ANISOU 3798 CE1 PHE A 453 5262 5678 4255 -187 108 15 C
ATOM 3799 CE2 PHE A 453 -4.123 9.015 -30.991 1.00 40.44 C
ANISOU 3799 CE2 PHE A 453 5248 5822 4293 -69 139 49 C
ATOM 3800 CZ PHE A 453 -3.304 8.512 -30.004 1.00 40.59 C
ANISOU 3800 CZ PHE A 453 5323 5755 4344 -132 114 28 C
ATOM 3801 N ASN A 454 -10.675 7.413 -29.292 1.00 35.95 N
ANISOU 3801 N ASN A 454 4442 5726 3489 -201 163 -4 N
ATOM 3802 CA ASN A 454 -11.970 7.493 -28.641 1.00 36.16 C
ANISOU 3802 CA ASN A 454 4424 5840 3473 -216 185 -11 C
ATOM 3803 C ASN A 454 -12.132 6.410 -27.576 1.00 36.27 C
ANISOU 3803 C ASN A 454 4475 5817 3486 -332 165 -52 C
ATOM 3804 O ASN A 454 -11.570 5.318 -27.698 1.00 34.86 O
ANISOU 3804 O ASN A 454 4331 5592 3321 -404 132 -81 O
ATOM 3805 CB ASN A 454 -13.110 7.401 -29.671 1.00 37.58 C
ANISOU 3805 CB ASN A 454 4499 6189 3588 -187 188 -14 C
ATOM 3806 CG ASN A 454 -13.436 5.967 -30.059 1.00 36.59 C
ANISOU 3806 CG ASN A 454 4346 6124 3432 -292 153 -69 C
ATOM 3807 OD1 ASN A 454 -14.254 5.321 -29.414 1.00 37.53 O
ANISOU 3807 OD1 ASN A 454 4448 6289 3521 -369 155 -104 O
ATOM 3808 ND2 ASN A 454 -12.756 5.450 -31.080 1.00 35.49 N
ANISOU 3808 ND2 ASN A 454 4209 5975 3301 -301 127 -81 N
ATOM 3809 N THR A 455 -12.894 6.716 -26.528 1.00 37.05 N
ANISOU 3809 N THR A 455 4572 5934 3569 -346 191 -53 N
ATOM 3810 CA THR A 455 -13.373 5.678 -25.617 1.00 39.01 C
ANISOU 3810 CA THR A 455 4838 6182 3800 -454 180 -92 C
ATOM 3811 C THR A 455 -14.907 5.628 -25.580 1.00 41.02 C
ANISOU 3811 C THR A 455 5010 6582 3994 -468 202 -110 C
ATOM 3812 O THR A 455 -15.513 5.444 -24.522 1.00 43.02 O
ANISOU 3812 O THR A 455 5273 6838 4232 -521 217 -126 O
ATOM 3813 CB THR A 455 -12.781 5.800 -24.201 1.00 37.55 C
ANISOU 3813 CB THR A 455 4738 5879 3649 -488 184 -87 C
ATOM 3814 OG1 THR A 455 -12.808 7.165 -23.793 1.00 39.19 O
ANISOU 3814 OG1 THR A 455 4948 6071 3869 -409 222 -55 O
ATOM 3815 CG2 THR A 455 -11.339 5.298 -24.176 1.00 37.47 C
ANISOU 3815 CG2 THR A 455 4805 5745 3687 -512 149 -84 C
ATOM 3816 N VAL A 456 -15.514 5.788 -26.755 1.00 41.79 N
ANISOU 3816 N VAL A 456 5019 6804 4052 -420 204 -108 N
ATOM 3817 CA VAL A 456 -16.954 5.613 -26.933 1.00 41.85 C
ANISOU 3817 CA VAL A 456 4931 6977 3993 -437 219 -131 C
ATOM 3818 C VAL A 456 -17.214 4.140 -27.273 1.00 40.98 C
ANISOU 3818 C VAL A 456 4805 6910 3854 -558 194 -193 C
ATOM 3819 O VAL A 456 -17.759 3.396 -26.457 1.00 38.00 O
ANISOU 3819 O VAL A 456 4440 6535 3460 -655 201 -231 O
ATOM 3820 CB VAL A 456 -17.494 6.540 -28.055 1.00 44.60 C
ANISOU 3820 CB VAL A 456 5185 7456 4304 -319 234 -95 C
ATOM 3821 CG1 VAL A 456 -19.000 6.379 -28.216 1.00 44.44 C
ANISOU 3821 CG1 VAL A 456 5052 7624 4207 -332 248 -119 C
ATOM 3822 CG2 VAL A 456 -17.135 7.996 -27.763 1.00 44.65 C
ANISOU 3822 CG2 VAL A 456 5221 7396 4346 -198 271 -32 C
ATOM 3823 N PHE A 457 -16.779 3.713 -28.461 1.00 39.79 N
ANISOU 3823 N PHE A 457 4634 6784 3699 -557 170 -204 N
ATOM 3824 CA PHE A 457 -16.787 2.291 -28.794 1.00 40.75 C
ANISOU 3824 CA PHE A 457 4762 6913 3806 -676 154 -266 C
ATOM 3825 C PHE A 457 -15.498 1.535 -28.411 1.00 41.28 C
ANISOU 3825 C PHE A 457 4945 6800 3937 -731 135 -271 C
ATOM 3826 O PHE A 457 -15.556 0.360 -28.061 1.00 43.04 O
ANISOU 3826 O PHE A 457 5206 6987 4160 -840 136 -315 O
ATOM 3827 CB PHE A 457 -17.171 2.047 -30.266 1.00 40.09 C
ANISOU 3827 CB PHE A 457 4587 6973 3672 -668 144 -291 C
ATOM 3828 CG PHE A 457 -16.371 2.845 -31.258 1.00 40.26 C
ANISOU 3828 CG PHE A 457 4603 6980 3714 -557 130 -242 C
ATOM 3829 CD1 PHE A 457 -15.190 2.335 -31.793 1.00 39.26 C
ANISOU 3829 CD1 PHE A 457 4538 6746 3632 -575 107 -249 C
ATOM 3830 CD2 PHE A 457 -16.822 4.089 -31.698 1.00 40.77 C
ANISOU 3830 CD2 PHE A 457 4597 7140 3751 -432 144 -190 C
ATOM 3831 CE1 PHE A 457 -14.463 3.060 -32.725 1.00 38.96 C
ANISOU 3831 CE1 PHE A 457 4494 6696 3610 -477 98 -207 C
ATOM 3832 CE2 PHE A 457 -16.101 4.816 -32.634 1.00 40.42 C
ANISOU 3832 CE2 PHE A 457 4553 7081 3724 -331 138 -143 C
ATOM 3833 CZ PHE A 457 -14.918 4.302 -33.148 1.00 39.13 C
ANISOU 3833 CZ PHE A 457 4451 6811 3604 -357 114 -154 C
ATOM 3834 N ASN A 458 -14.348 2.204 -28.483 1.00 40.15 N
ANISOU 3834 N ASN A 458 4856 6550 3848 -653 121 -224 N
ATOM 3835 CA ASN A 458 -13.064 1.591 -28.103 1.00 39.47 C
ANISOU 3835 CA ASN A 458 4873 6303 3822 -689 102 -222 C
ATOM 3836 C ASN A 458 -12.854 1.528 -26.599 1.00 38.70 C
ANISOU 3836 C ASN A 458 4850 6103 3749 -725 108 -210 C
ATOM 3837 O ASN A 458 -13.085 2.511 -25.892 1.00 41.01 O
ANISOU 3837 O ASN A 458 5140 6397 4042 -674 123 -181 O
ATOM 3838 CB ASN A 458 -11.898 2.378 -28.707 1.00 36.93 C
ANISOU 3838 CB ASN A 458 4575 5912 3544 -596 87 -180 C
ATOM 3839 CG ASN A 458 -11.517 1.902 -30.093 1.00 37.59 C
ANISOU 3839 CG ASN A 458 4631 6028 3624 -594 70 -198 C
ATOM 3840 OD1 ASN A 458 -12.043 0.904 -30.594 1.00 38.85 O
ANISOU 3840 OD1 ASN A 458 4759 6252 3750 -670 69 -247 O
ATOM 3841 ND2 ASN A 458 -10.596 2.613 -30.724 1.00 34.60 N
ANISOU 3841 ND2 ASN A 458 4264 5605 3277 -512 61 -164 N
ATOM 3842 N ASP A 459 -12.363 0.401 -26.107 1.00 38.78 N
ANISOU 3842 N ASP A 459 4931 6022 3780 -807 99 -230 N
ATOM 3843 CA ASP A 459 -11.842 0.351 -24.727 1.00 39.20 C
ANISOU 3843 CA ASP A 459 5068 5965 3862 -828 97 -208 C
ATOM 3844 C ASP A 459 -10.545 1.143 -24.581 1.00 37.80 C
ANISOU 3844 C ASP A 459 4937 5690 3734 -752 78 -164 C
ATOM 3845 O ASP A 459 -9.874 1.484 -25.566 1.00 36.87 O
ANISOU 3845 O ASP A 459 4805 5565 3638 -695 64 -154 O
ATOM 3846 CB ASP A 459 -11.591 -1.088 -24.277 1.00 40.75 C
ANISOU 3846 CB ASP A 459 5332 6085 4066 -925 96 -231 C
ATOM 3847 CG ASP A 459 -12.868 -1.879 -24.128 1.00 44.95 C
ANISOU 3847 CG ASP A 459 5832 6697 4549 -1018 125 -278 C
ATOM 3848 OD1 ASP A 459 -13.686 -1.537 -23.235 1.00 46.33 O
ANISOU 3848 OD1 ASP A 459 5993 6913 4696 -1036 144 -278 O
ATOM 3849 OD2 ASP A 459 -13.045 -2.849 -24.896 1.00 46.14 O
ANISOU 3849 OD2 ASP A 459 5972 6868 4688 -1079 134 -319 O
ATOM 3850 N GLN A 460 -10.181 1.404 -23.341 1.00 36.90 N
ANISOU 3850 N GLN A 460 4878 5505 3634 -757 78 -143 N
ATOM 3851 CA GLN A 460 -8.943 2.090 -23.037 1.00 36.29 C
ANISOU 3851 CA GLN A 460 4847 5340 3599 -702 63 -111 C
ATOM 3852 C GLN A 460 -7.729 1.242 -23.427 1.00 34.51 C
ANISOU 3852 C GLN A 460 4672 5029 3410 -713 32 -108 C
ATOM 3853 O GLN A 460 -6.744 1.764 -23.955 1.00 33.51 O
ANISOU 3853 O GLN A 460 4551 4863 3316 -656 17 -91 O
ATOM 3854 CB GLN A 460 -8.924 2.444 -21.553 1.00 37.43 C
ANISOU 3854 CB GLN A 460 5036 5445 3740 -720 72 -97 C
ATOM 3855 CG GLN A 460 -7.702 3.174 -21.076 1.00 36.31 C
ANISOU 3855 CG GLN A 460 4936 5224 3632 -677 59 -72 C
ATOM 3856 CD GLN A 460 -7.867 3.634 -19.647 1.00 36.64 C
ANISOU 3856 CD GLN A 460 5008 5251 3659 -698 74 -66 C
ATOM 3857 OE1 GLN A 460 -8.892 4.212 -19.292 1.00 37.20 O
ANISOU 3857 OE1 GLN A 460 5048 5381 3705 -697 107 -74 O
ATOM 3858 NE2 GLN A 460 -6.858 3.394 -18.825 1.00 34.79 N
ANISOU 3858 NE2 GLN A 460 4833 4946 3439 -716 52 -53 N
ATOM 3859 N ARG A 461 -7.812 -0.068 -23.221 1.00 34.72 N
ANISOU 3859 N ARG A 461 4734 5026 3431 -786 28 -124 N
ATOM 3860 CA ARG A 461 -6.711 -0.951 -23.630 1.00 35.47 C
ANISOU 3860 CA ARG A 461 4877 5039 3561 -793 6 -120 C
ATOM 3861 C ARG A 461 -6.466 -0.887 -25.142 1.00 34.64 C
ANISOU 3861 C ARG A 461 4727 4964 3468 -757 0 -135 C
ATOM 3862 O ARG A 461 -5.337 -0.983 -25.609 1.00 35.92 O
ANISOU 3862 O ARG A 461 4915 5065 3668 -724 -19 -123 O
ATOM 3863 CB ARG A 461 -6.943 -2.386 -23.149 1.00 37.59 C
ANISOU 3863 CB ARG A 461 5197 5265 3819 -877 17 -133 C
ATOM 3864 CG ARG A 461 -8.173 -3.077 -23.722 1.00 40.75 C
ANISOU 3864 CG ARG A 461 5557 5741 4184 -945 46 -180 C
ATOM 3865 CD ARG A 461 -8.531 -4.287 -22.876 1.00 42.52 C
ANISOU 3865 CD ARG A 461 5843 5918 4395 -1033 70 -190 C
ATOM 3866 NE ARG A 461 -9.073 -5.384 -23.674 1.00 47.18 N
ANISOU 3866 NE ARG A 461 6426 6527 4972 -1105 99 -239 N
ATOM 3867 CZ ARG A 461 -10.332 -5.801 -23.615 1.00 49.47 C
ANISOU 3867 CZ ARG A 461 6685 6891 5219 -1183 134 -282 C
ATOM 3868 NH1 ARG A 461 -11.197 -5.214 -22.788 1.00 53.35 N
ANISOU 3868 NH1 ARG A 461 7148 7443 5676 -1193 143 -279 N
ATOM 3869 NH2 ARG A 461 -10.721 -6.815 -24.365 1.00 49.59 N
ANISOU 3869 NH2 ARG A 461 6696 6920 5224 -1257 164 -334 N
ATOM 3870 N THR A 462 -7.537 -0.668 -25.890 1.00 33.86 N
ANISOU 3870 N THR A 462 4558 4970 3334 -761 17 -161 N
ATOM 3871 CA THR A 462 -7.455 -0.462 -27.321 1.00 33.11 C
ANISOU 3871 CA THR A 462 4410 4928 3239 -723 13 -173 C
ATOM 3872 C THR A 462 -6.769 0.863 -27.687 1.00 31.23 C
ANISOU 3872 C THR A 462 4156 4682 3025 -625 5 -138 C
ATOM 3873 O THR A 462 -5.900 0.904 -28.559 1.00 29.99 O
ANISOU 3873 O THR A 462 4002 4496 2896 -589 -8 -134 O
ATOM 3874 CB THR A 462 -8.855 -0.573 -27.941 1.00 33.68 C
ANISOU 3874 CB THR A 462 4404 5135 3257 -754 34 -209 C
ATOM 3875 OG1 THR A 462 -9.325 -1.915 -27.745 1.00 34.93 O
ANISOU 3875 OG1 THR A 462 4585 5286 3398 -856 48 -250 O
ATOM 3876 CG2 THR A 462 -8.838 -0.253 -29.441 1.00 33.04 C
ANISOU 3876 CG2 THR A 462 4259 5129 3164 -707 29 -218 C
ATOM 3877 N VAL A 463 -7.137 1.929 -26.996 1.00 29.87 N
ANISOU 3877 N VAL A 463 3973 4532 2845 -586 19 -116 N
ATOM 3878 CA VAL A 463 -6.501 3.224 -27.212 1.00 29.84 C
ANISOU 3878 CA VAL A 463 3965 4507 2865 -500 25 -85 C
ATOM 3879 C VAL A 463 -4.976 3.110 -27.009 1.00 29.52 C
ANISOU 3879 C VAL A 463 3986 4354 2874 -490 1 -72 C
ATOM 3880 O VAL A 463 -4.187 3.530 -27.863 1.00 28.59 O
ANISOU 3880 O VAL A 463 3863 4217 2782 -440 -4 -63 O
ATOM 3881 CB VAL A 463 -7.102 4.289 -26.272 1.00 30.00 C
ANISOU 3881 CB VAL A 463 3979 4548 2872 -473 54 -67 C
ATOM 3882 CG1 VAL A 463 -6.266 5.555 -26.300 1.00 31.20 C
ANISOU 3882 CG1 VAL A 463 4147 4650 3056 -398 68 -40 C
ATOM 3883 CG2 VAL A 463 -8.544 4.592 -26.676 1.00 30.83 C
ANISOU 3883 CG2 VAL A 463 4007 4777 2927 -458 79 -74 C
ATOM 3884 N PHE A 464 -4.578 2.490 -25.897 1.00 29.52 N
ANISOU 3884 N PHE A 464 4043 4289 2884 -539 -12 -71 N
ATOM 3885 CA PHE A 464 -3.176 2.232 -25.608 1.00 29.47 C
ANISOU 3885 CA PHE A 464 4090 4190 2917 -534 -38 -59 C
ATOM 3886 C PHE A 464 -2.459 1.434 -26.726 1.00 30.11 C
ANISOU 3886 C PHE A 464 4173 4244 3022 -531 -57 -68 C
ATOM 3887 O PHE A 464 -1.356 1.787 -27.128 1.00 28.91 O
ANISOU 3887 O PHE A 464 4032 4048 2904 -489 -70 -59 O
ATOM 3888 CB PHE A 464 -3.038 1.529 -24.252 1.00 29.35 C
ANISOU 3888 CB PHE A 464 4129 4126 2896 -587 -50 -51 C
ATOM 3889 CG PHE A 464 -3.313 2.418 -23.072 1.00 30.67 C
ANISOU 3889 CG PHE A 464 4304 4301 3047 -585 -35 -41 C
ATOM 3890 CD1 PHE A 464 -3.228 3.817 -23.183 1.00 30.71 C
ANISOU 3890 CD1 PHE A 464 4285 4323 3059 -531 -14 -36 C
ATOM 3891 CD2 PHE A 464 -3.647 1.864 -21.828 1.00 31.38 C
ANISOU 3891 CD2 PHE A 464 4430 4378 3114 -640 -36 -36 C
ATOM 3892 CE1 PHE A 464 -3.462 4.633 -22.079 1.00 30.76 C
ANISOU 3892 CE1 PHE A 464 4302 4331 3052 -534 6 -32 C
ATOM 3893 CE2 PHE A 464 -3.899 2.680 -20.732 1.00 31.46 C
ANISOU 3893 CE2 PHE A 464 4447 4399 3107 -642 -21 -31 C
ATOM 3894 CZ PHE A 464 -3.794 4.060 -20.851 1.00 31.65 C
ANISOU 3894 CZ PHE A 464 4447 4438 3141 -591 0 -31 C
ATOM 3895 N ALA A 465 -3.093 0.373 -27.231 1.00 30.02 N
ANISOU 3895 N ALA A 465 4152 4260 2994 -579 -54 -93 N
ATOM 3896 CA ALA A 465 -2.509 -0.399 -28.351 1.00 30.28 C
ANISOU 3896 CA ALA A 465 4185 4270 3046 -582 -64 -109 C
ATOM 3897 C ALA A 465 -2.366 0.455 -29.615 1.00 30.12 C
ANISOU 3897 C ALA A 465 4113 4299 3030 -521 -61 -110 C
ATOM 3898 O ALA A 465 -1.318 0.477 -30.263 1.00 28.76 O
ANISOU 3898 O ALA A 465 3952 4083 2891 -488 -74 -106 O
ATOM 3899 CB ALA A 465 -3.353 -1.634 -28.643 1.00 29.68 C
ANISOU 3899 CB ALA A 465 4107 4222 2946 -656 -49 -145 C
ATOM 3900 N ASN A 466 -3.446 1.129 -29.986 1.00 31.30 N
ANISOU 3900 N ASN A 466 4204 4545 3141 -503 -42 -114 N
ATOM 3901 CA ASN A 466 -3.369 2.088 -31.066 1.00 31.14 C
ANISOU 3901 CA ASN A 466 4137 4575 3119 -433 -34 -103 C
ATOM 3902 C ASN A 466 -2.195 3.043 -30.852 1.00 29.66 C
ANISOU 3902 C ASN A 466 3981 4314 2973 -373 -37 -74 C
ATOM 3903 O ASN A 466 -1.395 3.242 -31.750 1.00 30.56 O
ANISOU 3903 O ASN A 466 4092 4409 3110 -336 -42 -71 O
ATOM 3904 CB ASN A 466 -4.696 2.844 -31.234 1.00 31.59 C
ANISOU 3904 CB ASN A 466 4130 4745 3127 -407 -9 -97 C
ATOM 3905 CG ASN A 466 -5.780 1.988 -31.869 1.00 32.93 C
ANISOU 3905 CG ASN A 466 4248 5016 3249 -461 -6 -134 C
ATOM 3906 OD1 ASN A 466 -5.492 1.116 -32.686 1.00 35.44 O
ANISOU 3906 OD1 ASN A 466 4563 5333 3568 -495 -17 -163 O
ATOM 3907 ND2 ASN A 466 -7.041 2.234 -31.495 1.00 32.28 N
ANISOU 3907 ND2 ASN A 466 4119 5024 3120 -471 11 -138 N
ATOM 3908 N PHE A 467 -2.066 3.596 -29.647 1.00 28.07 N
ANISOU 3908 N PHE A 467 3811 4073 2781 -372 -31 -57 N
ATOM 3909 CA PHE A 467 -1.018 4.579 -29.392 1.00 26.58 C
ANISOU 3909 CA PHE A 467 3649 3824 2627 -325 -26 -38 C
ATOM 3910 C PHE A 467 0.380 3.975 -29.509 1.00 26.76 C
ANISOU 3910 C PHE A 467 3708 3769 2689 -333 -56 -43 C
ATOM 3911 O PHE A 467 1.296 4.574 -30.100 1.00 26.63 O
ANISOU 3911 O PHE A 467 3692 3724 2700 -290 -53 -38 O
ATOM 3912 CB PHE A 467 -1.199 5.205 -28.016 1.00 26.38 C
ANISOU 3912 CB PHE A 467 3647 3778 2596 -335 -11 -29 C
ATOM 3913 CG PHE A 467 -0.192 6.271 -27.703 1.00 26.82 C
ANISOU 3913 CG PHE A 467 3727 3779 2681 -298 2 -19 C
ATOM 3914 CD1 PHE A 467 -0.091 7.406 -28.500 1.00 26.34 C
ANISOU 3914 CD1 PHE A 467 3647 3729 2630 -235 38 -8 C
ATOM 3915 CD2 PHE A 467 0.643 6.154 -26.591 1.00 26.94 C
ANISOU 3915 CD2 PHE A 467 3785 3738 2712 -330 -14 -22 C
ATOM 3916 CE1 PHE A 467 0.842 8.392 -28.213 1.00 27.01 C
ANISOU 3916 CE1 PHE A 467 3758 3758 2743 -211 60 -6 C
ATOM 3917 CE2 PHE A 467 1.554 7.143 -26.286 1.00 25.92 C
ANISOU 3917 CE2 PHE A 467 3673 3568 2605 -307 2 -23 C
ATOM 3918 CZ PHE A 467 1.653 8.261 -27.097 1.00 26.77 C
ANISOU 3918 CZ PHE A 467 3765 3678 2726 -252 42 -18 C
ATOM 3919 N TYR A 468 0.542 2.785 -28.944 1.00 25.58 N
ANISOU 3919 N TYR A 468 3590 3585 2541 -386 -80 -51 N
ATOM 3920 CA TYR A 468 1.822 2.117 -28.939 1.00 25.53 C
ANISOU 3920 CA TYR A 468 3620 3509 2571 -390 -107 -50 C
ATOM 3921 C TYR A 468 2.254 1.853 -30.386 1.00 26.07 C
ANISOU 3921 C TYR A 468 3667 3580 2656 -366 -110 -63 C
ATOM 3922 O TYR A 468 3.404 2.109 -30.761 1.00 26.59 O
ANISOU 3922 O TYR A 468 3741 3606 2756 -334 -120 -60 O
ATOM 3923 CB TYR A 468 1.706 0.820 -28.128 1.00 24.91 C
ANISOU 3923 CB TYR A 468 3580 3395 2485 -446 -123 -50 C
ATOM 3924 CG TYR A 468 2.954 -0.030 -28.065 1.00 24.25 C
ANISOU 3924 CG TYR A 468 3536 3241 2436 -443 -148 -43 C
ATOM 3925 CD1 TYR A 468 4.075 0.373 -27.310 1.00 23.16 C
ANISOU 3925 CD1 TYR A 468 3418 3064 2315 -419 -167 -24 C
ATOM 3926 CD2 TYR A 468 2.997 -1.270 -28.719 1.00 23.99 C
ANISOU 3926 CD2 TYR A 468 3518 3183 2414 -467 -148 -56 C
ATOM 3927 CE1 TYR A 468 5.190 -0.437 -27.212 1.00 23.43 C
ANISOU 3927 CE1 TYR A 468 3482 3044 2375 -410 -191 -12 C
ATOM 3928 CE2 TYR A 468 4.099 -2.096 -28.632 1.00 22.96 C
ANISOU 3928 CE2 TYR A 468 3425 2984 2314 -458 -165 -44 C
ATOM 3929 CZ TYR A 468 5.200 -1.694 -27.906 1.00 24.19 C
ANISOU 3929 CZ TYR A 468 3595 3108 2486 -424 -188 -19 C
ATOM 3930 OH TYR A 468 6.311 -2.534 -27.866 1.00 23.07 O
ANISOU 3930 OH TYR A 468 3484 2908 2373 -406 -205 -4 O
ATOM 3931 N ASP A 469 1.308 1.413 -31.209 1.00 26.43 N
ANISOU 3931 N ASP A 469 3681 3685 2677 -384 -99 -81 N
ATOM 3932 CA ASP A 469 1.566 1.153 -32.612 1.00 26.86 C
ANISOU 3932 CA ASP A 469 3710 3758 2738 -369 -98 -98 C
ATOM 3933 C ASP A 469 2.010 2.417 -33.361 1.00 27.57 C
ANISOU 3933 C ASP A 469 3772 3866 2837 -300 -86 -83 C
ATOM 3934 O ASP A 469 2.952 2.378 -34.176 1.00 26.94 O
ANISOU 3934 O ASP A 469 3694 3756 2784 -276 -93 -87 O
ATOM 3935 CB ASP A 469 0.316 0.574 -33.281 1.00 27.77 C
ANISOU 3935 CB ASP A 469 3784 3956 2810 -407 -85 -124 C
ATOM 3936 CG ASP A 469 0.089 -0.884 -32.939 1.00 28.33 C
ANISOU 3936 CG ASP A 469 3888 3995 2880 -481 -88 -150 C
ATOM 3937 OD1 ASP A 469 0.989 -1.513 -32.371 1.00 28.17 O
ANISOU 3937 OD1 ASP A 469 3922 3886 2895 -491 -100 -142 O
ATOM 3938 OD2 ASP A 469 -0.986 -1.409 -33.271 1.00 29.83 O
ANISOU 3938 OD2 ASP A 469 4048 4252 3031 -529 -73 -179 O
ATOM 3939 N ALA A 470 1.329 3.532 -33.111 1.00 28.23 N
ANISOU 3939 N ALA A 470 3833 3994 2899 -267 -63 -64 N
ATOM 3940 CA ALA A 470 1.683 4.791 -33.799 1.00 27.36 C
ANISOU 3940 CA ALA A 470 3704 3893 2796 -199 -39 -45 C
ATOM 3941 C ALA A 470 3.088 5.184 -33.394 1.00 27.42 C
ANISOU 3941 C ALA A 470 3752 3815 2850 -185 -45 -41 C
ATOM 3942 O ALA A 470 3.854 5.689 -34.202 1.00 30.82 O
ANISOU 3942 O ALA A 470 4179 4229 3301 -146 -35 -38 O
ATOM 3943 CB ALA A 470 0.684 5.897 -33.465 1.00 26.30 C
ANISOU 3943 CB ALA A 470 3547 3812 2633 -163 -4 -22 C
ATOM 3944 N MET A 471 3.451 4.897 -32.146 1.00 26.31 N
ANISOU 3944 N MET A 471 3647 3626 2721 -220 -61 -42 N
ATOM 3945 CA MET A 471 4.758 5.311 -31.640 1.00 25.90 C
ANISOU 3945 CA MET A 471 3625 3510 2705 -211 -68 -42 C
ATOM 3946 C MET A 471 5.900 4.413 -32.164 1.00 25.68 C
ANISOU 3946 C MET A 471 3607 3439 2708 -217 -99 -53 C
ATOM 3947 O MET A 471 7.015 4.888 -32.362 1.00 24.10 O
ANISOU 3947 O MET A 471 3413 3205 2536 -194 -97 -57 O
ATOM 3948 CB MET A 471 4.767 5.442 -30.101 1.00 25.52 C
ANISOU 3948 CB MET A 471 3605 3440 2651 -242 -73 -38 C
ATOM 3949 CG MET A 471 3.893 6.574 -29.537 1.00 25.65 C
ANISOU 3949 CG MET A 471 3615 3484 2645 -230 -33 -30 C
ATOM 3950 SD MET A 471 4.105 8.197 -30.341 1.00 26.99 S
ANISOU 3950 SD MET A 471 3772 3652 2828 -165 23 -22 S
ATOM 3951 CE MET A 471 5.835 8.543 -29.974 1.00 24.90 C
ANISOU 3951 CE MET A 471 3536 3320 2602 -175 16 -40 C
ATOM 3952 N ILE A 472 5.597 3.136 -32.430 1.00 25.95 N
ANISOU 3952 N ILE A 472 3645 3478 2737 -247 -119 -63 N
ATOM 3953 CA ILE A 472 6.505 2.246 -33.143 1.00 26.17 C
ANISOU 3953 CA ILE A 472 3680 3469 2793 -247 -138 -75 C
ATOM 3954 C ILE A 472 6.794 2.829 -34.551 1.00 27.69 C
ANISOU 3954 C ILE A 472 3843 3683 2994 -208 -121 -82 C
ATOM 3955 O ILE A 472 7.955 2.930 -34.979 1.00 26.48 O
ANISOU 3955 O ILE A 472 3694 3494 2873 -185 -127 -87 O
ATOM 3956 CB ILE A 472 5.888 0.823 -33.290 1.00 28.69 C
ANISOU 3956 CB ILE A 472 4009 3789 3100 -292 -147 -88 C
ATOM 3957 CG1 ILE A 472 5.825 0.084 -31.937 1.00 27.11 C
ANISOU 3957 CG1 ILE A 472 3849 3552 2897 -328 -162 -76 C
ATOM 3958 CG2 ILE A 472 6.598 0.009 -34.390 1.00 27.65 C
ANISOU 3958 CG2 ILE A 472 3877 3631 2994 -288 -151 -108 C
ATOM 3959 CD1 ILE A 472 7.155 -0.472 -31.459 1.00 27.29 C
ANISOU 3959 CD1 ILE A 472 3905 3509 2955 -316 -185 -64 C
ATOM 3960 N CYS A 473 5.752 3.252 -35.264 1.00 28.65 N
ANISOU 3960 N CYS A 473 3930 3870 3082 -195 -99 -81 N
ATOM 3961 CA CYS A 473 5.995 3.938 -36.542 1.00 30.34 C
ANISOU 3961 CA CYS A 473 4118 4111 3298 -150 -79 -80 C
ATOM 3962 C CYS A 473 6.911 5.146 -36.398 1.00 29.11 C
ANISOU 3962 C CYS A 473 3973 3916 3168 -110 -60 -67 C
ATOM 3963 O CYS A 473 7.875 5.272 -37.142 1.00 28.74 O
ANISOU 3963 O CYS A 473 3927 3845 3147 -89 -58 -74 O
ATOM 3964 CB CYS A 473 4.710 4.340 -37.223 1.00 32.04 C
ANISOU 3964 CB CYS A 473 4291 4416 3466 -133 -57 -72 C
ATOM 3965 SG CYS A 473 3.743 2.931 -37.727 1.00 40.70 S
ANISOU 3965 SG CYS A 473 5363 5573 4527 -189 -73 -103 S
ATOM 3966 N VAL A 474 6.578 6.051 -35.472 1.00 28.63 N
ANISOU 3966 N VAL A 474 3924 3853 3100 -102 -40 -51 N
ATOM 3967 CA VAL A 474 7.434 7.248 -35.172 1.00 26.70 C
ANISOU 3967 CA VAL A 474 3697 3567 2881 -76 -11 -46 C
ATOM 3968 C VAL A 474 8.884 6.861 -34.842 1.00 26.02 C
ANISOU 3968 C VAL A 474 3630 3422 2832 -96 -37 -65 C
ATOM 3969 O VAL A 474 9.833 7.557 -35.236 1.00 26.01 O
ANISOU 3969 O VAL A 474 3632 3394 2854 -76 -17 -73 O
ATOM 3970 CB VAL A 474 6.844 8.062 -33.982 1.00 26.96 C
ANISOU 3970 CB VAL A 474 3744 3599 2900 -82 14 -36 C
ATOM 3971 CG1 VAL A 474 7.814 9.128 -33.481 1.00 24.72 C
ANISOU 3971 CG1 VAL A 474 3485 3265 2642 -77 45 -44 C
ATOM 3972 CG2 VAL A 474 5.493 8.680 -34.378 1.00 26.45 C
ANISOU 3972 CG2 VAL A 474 3656 3593 2799 -47 50 -12 C
ATOM 3973 N ALA A 475 9.055 5.758 -34.114 1.00 25.19 N
ANISOU 3973 N ALA A 475 3537 3302 2730 -133 -79 -72 N
ATOM 3974 CA ALA A 475 10.387 5.313 -33.695 1.00 24.70 C
ANISOU 3974 CA ALA A 475 3488 3198 2697 -144 -108 -84 C
ATOM 3975 C ALA A 475 11.206 4.828 -34.910 1.00 26.28 C
ANISOU 3975 C ALA A 475 3676 3384 2924 -124 -116 -96 C
ATOM 3976 O ALA A 475 12.424 5.068 -34.999 1.00 27.95 O
ANISOU 3976 O ALA A 475 3887 3570 3163 -114 -119 -108 O
ATOM 3977 CB ALA A 475 10.269 4.215 -32.649 1.00 24.84 C
ANISOU 3977 CB ALA A 475 3524 3204 2707 -177 -145 -78 C
ATOM 3978 N TYR A 476 10.519 4.184 -35.852 1.00 25.46 N
ANISOU 3978 N TYR A 476 3560 3303 2808 -123 -116 -98 N
ATOM 3979 CA TYR A 476 11.117 3.738 -37.078 1.00 26.16 C
ANISOU 3979 CA TYR A 476 3638 3386 2916 -108 -117 -112 C
ATOM 3980 C TYR A 476 11.497 4.939 -37.941 1.00 26.32 C
ANISOU 3980 C TYR A 476 3643 3416 2942 -71 -82 -112 C
ATOM 3981 O TYR A 476 12.584 4.958 -38.529 1.00 26.72 O
ANISOU 3981 O TYR A 476 3689 3440 3020 -58 -82 -125 O
ATOM 3982 CB TYR A 476 10.170 2.820 -37.841 1.00 26.57 C
ANISOU 3982 CB TYR A 476 3677 3471 2944 -125 -120 -120 C
ATOM 3983 CG TYR A 476 10.276 1.359 -37.521 1.00 27.15 C
ANISOU 3983 CG TYR A 476 3772 3513 3030 -160 -145 -132 C
ATOM 3984 CD1 TYR A 476 11.491 0.682 -37.639 1.00 28.52 C
ANISOU 3984 CD1 TYR A 476 3959 3633 3241 -152 -160 -141 C
ATOM 3985 CD2 TYR A 476 9.136 0.622 -37.174 1.00 28.48 C
ANISOU 3985 CD2 TYR A 476 3946 3703 3169 -198 -146 -134 C
ATOM 3986 CE1 TYR A 476 11.580 -0.680 -37.373 1.00 30.01 C
ANISOU 3986 CE1 TYR A 476 4174 3784 3443 -176 -173 -146 C
ATOM 3987 CE2 TYR A 476 9.204 -0.743 -36.909 1.00 29.37 C
ANISOU 3987 CE2 TYR A 476 4088 3776 3295 -232 -157 -144 C
ATOM 3988 CZ TYR A 476 10.428 -1.386 -36.997 1.00 30.11 C
ANISOU 3988 CZ TYR A 476 4201 3809 3428 -217 -169 -147 C
ATOM 3989 OH TYR A 476 10.506 -2.723 -36.737 1.00 30.38 O
ANISOU 3989 OH TYR A 476 4270 3796 3476 -242 -170 -151 O
ATOM 3990 N LYS A 477 10.629 5.949 -37.998 1.00 25.54 N
ANISOU 3990 N LYS A 477 3536 3349 2816 -52 -49 -94 N
ATOM 3991 CA LYS A 477 11.015 7.209 -38.647 1.00 26.74 C
ANISOU 3991 CA LYS A 477 3686 3498 2974 -13 -4 -87 C
ATOM 3992 C LYS A 477 12.257 7.782 -37.967 1.00 27.30 C
ANISOU 3992 C LYS A 477 3775 3517 3079 -22 2 -102 C
ATOM 3993 O LYS A 477 13.152 8.265 -38.637 1.00 27.62 O
ANISOU 3993 O LYS A 477 3814 3537 3140 -6 24 -112 O
ATOM 3994 CB LYS A 477 9.879 8.231 -38.640 1.00 26.40 C
ANISOU 3994 CB LYS A 477 3639 3492 2899 16 37 -58 C
ATOM 3995 CG LYS A 477 9.929 9.181 -39.835 1.00 28.20 C
ANISOU 3995 CG LYS A 477 3859 3735 3121 68 86 -41 C
ATOM 3996 CD LYS A 477 9.298 10.563 -39.588 1.00 29.85 C
ANISOU 3996 CD LYS A 477 4079 3946 3314 108 147 -9 C
ATOM 3997 CE LYS A 477 8.687 11.073 -40.887 1.00 30.83 C
ANISOU 3997 CE LYS A 477 4182 4123 3407 170 182 23 C
ATOM 3998 NZ LYS A 477 8.717 12.538 -41.159 1.00 28.88 N
ANISOU 3998 NZ LYS A 477 3958 3852 3162 226 259 55 N
ATOM 3999 N PHE A 478 12.322 7.689 -36.630 1.00 27.16 N
ANISOU 3999 N PHE A 478 3772 3485 3062 -53 -15 -105 N
ATOM 4000 CA PHE A 478 13.452 8.249 -35.887 1.00 27.00 C
ANISOU 4000 CA PHE A 478 3761 3432 3064 -69 -9 -125 C
ATOM 4001 C PHE A 478 14.708 7.526 -36.323 1.00 28.03 C
ANISOU 4001 C PHE A 478 3880 3547 3224 -71 -40 -145 C
ATOM 4002 O PHE A 478 15.762 8.127 -36.545 1.00 26.23 O
ANISOU 4002 O PHE A 478 3647 3302 3017 -69 -20 -165 O
ATOM 4003 CB PHE A 478 13.246 8.066 -34.382 1.00 25.82 C
ANISOU 4003 CB PHE A 478 3624 3285 2901 -104 -32 -125 C
ATOM 4004 CG PHE A 478 14.474 8.364 -33.545 1.00 25.39 C
ANISOU 4004 CG PHE A 478 3569 3216 2861 -129 -40 -150 C
ATOM 4005 CD1 PHE A 478 15.358 7.354 -33.202 1.00 26.30 C
ANISOU 4005 CD1 PHE A 478 3673 3331 2986 -138 -91 -156 C
ATOM 4006 CD2 PHE A 478 14.700 9.638 -33.042 1.00 25.88 C
ANISOU 4006 CD2 PHE A 478 3641 3269 2921 -143 8 -167 C
ATOM 4007 CE1 PHE A 478 16.478 7.603 -32.406 1.00 27.36 C
ANISOU 4007 CE1 PHE A 478 3797 3472 3125 -160 -103 -179 C
ATOM 4008 CE2 PHE A 478 15.810 9.901 -32.244 1.00 27.15 C
ANISOU 4008 CE2 PHE A 478 3795 3432 3088 -176 1 -198 C
ATOM 4009 CZ PHE A 478 16.710 8.888 -31.934 1.00 26.65 C
ANISOU 4009 CZ PHE A 478 3711 3384 3030 -183 -57 -204 C
ATOM 4010 N ASP A 479 14.578 6.208 -36.431 1.00 29.48 N
ANISOU 4010 N ASP A 479 4060 3733 3408 -75 -84 -140 N
ATOM 4011 CA ASP A 479 15.688 5.368 -36.758 1.00 29.27 C
ANISOU 4011 CA ASP A 479 4024 3689 3409 -72 -113 -155 C
ATOM 4012 C ASP A 479 16.197 5.710 -38.177 1.00 28.87 C
ANISOU 4012 C ASP A 479 3958 3634 3375 -47 -86 -168 C
ATOM 4013 O ASP A 479 17.409 5.813 -38.405 1.00 25.81 O
ANISOU 4013 O ASP A 479 3560 3232 3014 -43 -87 -188 O
ATOM 4014 CB ASP A 479 15.261 3.915 -36.643 1.00 29.31 C
ANISOU 4014 CB ASP A 479 4036 3688 3410 -81 -150 -145 C
ATOM 4015 CG ASP A 479 16.285 2.986 -37.186 1.00 29.87 C
ANISOU 4015 CG ASP A 479 4100 3735 3511 -68 -170 -157 C
ATOM 4016 OD1 ASP A 479 17.405 2.944 -36.631 1.00 28.48 O
ANISOU 4016 OD1 ASP A 479 3917 3549 3353 -62 -188 -162 O
ATOM 4017 OD2 ASP A 479 15.957 2.292 -38.174 1.00 32.09 O
ANISOU 4017 OD2 ASP A 479 4381 4014 3796 -64 -166 -163 O
ATOM 4018 N ALA A 480 15.254 5.958 -39.093 1.00 28.07 N
ANISOU 4018 N ALA A 480 3855 3554 3254 -32 -61 -157 N
ATOM 4019 CA ALA A 480 15.583 6.296 -40.474 1.00 28.79 C
ANISOU 4019 CA ALA A 480 3935 3651 3353 -7 -33 -164 C
ATOM 4020 C ALA A 480 16.245 7.682 -40.592 1.00 29.44 C
ANISOU 4020 C ALA A 480 4021 3716 3446 5 14 -169 C
ATOM 4021 O ALA A 480 17.203 7.863 -41.365 1.00 30.33 O
ANISOU 4021 O ALA A 480 4127 3816 3581 14 29 -187 O
ATOM 4022 CB ALA A 480 14.334 6.202 -41.363 1.00 29.78 C
ANISOU 4022 CB ALA A 480 4051 3821 3443 7 -20 -147 C
ATOM 4023 N ALA A 481 15.733 8.651 -39.842 1.00 27.45 N
ANISOU 4023 N ALA A 481 3785 3463 3180 2 44 -156 N
ATOM 4024 CA ALA A 481 16.462 9.913 -39.593 1.00 29.54 C
ANISOU 4024 CA ALA A 481 4063 3700 3459 -1 94 -170 C
ATOM 4025 C ALA A 481 17.891 9.687 -39.068 1.00 31.53 C
ANISOU 4025 C ALA A 481 4304 3934 3739 -31 71 -208 C
ATOM 4026 O ALA A 481 18.851 10.329 -39.545 1.00 32.48 O
ANISOU 4026 O ALA A 481 4421 4038 3879 -33 106 -231 O
ATOM 4027 CB ALA A 481 15.682 10.804 -38.631 1.00 27.95 C
ANISOU 4027 CB ALA A 481 3883 3496 3240 -8 128 -157 C
ATOM 4028 N MET A 482 18.052 8.782 -38.103 1.00 31.30 N
ANISOU 4028 N MET A 482 4267 3915 3711 -53 16 -212 N
ATOM 4029 CA MET A 482 19.397 8.525 -37.578 1.00 32.86 C
ANISOU 4029 CA MET A 482 4444 4111 3927 -73 -9 -242 C
ATOM 4030 C MET A 482 20.307 8.079 -38.702 1.00 33.36 C
ANISOU 4030 C MET A 482 4489 4168 4017 -55 -14 -257 C
ATOM 4031 O MET A 482 21.504 8.377 -38.684 1.00 37.32 O
ANISOU 4031 O MET A 482 4971 4670 4536 -66 -7 -288 O
ATOM 4032 CB MET A 482 19.411 7.454 -36.473 1.00 32.01 C
ANISOU 4032 CB MET A 482 4331 4019 3811 -86 -71 -233 C
ATOM 4033 CG MET A 482 18.875 7.870 -35.117 1.00 32.08 C
ANISOU 4033 CG MET A 482 4352 4040 3794 -114 -72 -227 C
ATOM 4034 SD MET A 482 19.348 9.539 -34.620 1.00 34.28 S
ANISOU 4034 SD MET A 482 4636 4319 4070 -148 -9 -262 S
ATOM 4035 CE MET A 482 17.916 10.408 -35.272 1.00 34.34 C
ANISOU 4035 CE MET A 482 4677 4302 4067 -125 52 -235 C
ATOM 4036 N MET A 483 19.765 7.320 -39.653 1.00 33.05 N
ANISOU 4036 N MET A 483 4450 4128 3977 -30 -26 -241 N
ATOM 4037 CA MET A 483 20.614 6.740 -40.692 1.00 35.04 C
ANISOU 4037 CA MET A 483 4685 4374 4254 -14 -34 -258 C
ATOM 4038 C MET A 483 21.022 7.853 -41.637 1.00 33.38 C
ANISOU 4038 C MET A 483 4475 4156 4051 -7 23 -271 C
ATOM 4039 O MET A 483 22.174 7.972 -42.002 1.00 31.55 O
ANISOU 4039 O MET A 483 4226 3919 3842 -10 31 -300 O
ATOM 4040 CB MET A 483 19.913 5.598 -41.444 1.00 36.77 C
ANISOU 4040 CB MET A 483 4905 4595 4468 0 -56 -244 C
ATOM 4041 CG MET A 483 19.710 4.324 -40.632 1.00 41.63 C
ANISOU 4041 CG MET A 483 5526 5205 5084 -6 -106 -233 C
ATOM 4042 SD MET A 483 21.202 3.707 -39.798 1.00 45.21 S
ANISOU 4042 SD MET A 483 5961 5649 5566 -3 -143 -246 S
ATOM 4043 CE MET A 483 20.955 4.354 -38.143 1.00 44.56 C
ANISOU 4043 CE MET A 483 5885 5585 5459 -27 -155 -234 C
ATOM 4044 N ALA A 484 20.060 8.694 -41.979 1.00 33.96 N
ANISOU 4044 N ALA A 484 4569 4232 4102 4 65 -249 N
ATOM 4045 CA ALA A 484 20.322 9.856 -42.797 1.00 35.00 C
ANISOU 4045 CA ALA A 484 4711 4349 4235 16 131 -252 C
ATOM 4046 C ALA A 484 21.293 10.785 -42.102 1.00 34.59 C
ANISOU 4046 C ALA A 484 4663 4277 4201 -14 165 -284 C
ATOM 4047 O ALA A 484 22.153 11.360 -42.755 1.00 37.83 O
ANISOU 4047 O ALA A 484 5071 4672 4628 -18 206 -307 O
ATOM 4048 CB ALA A 484 19.017 10.588 -43.149 1.00 33.30 C
ANISOU 4048 CB ALA A 484 4518 4144 3989 45 173 -212 C
ATOM 4049 N LEU A 485 21.161 10.958 -40.784 1.00 35.64 N
ANISOU 4049 N LEU A 485 4801 4414 4327 -42 152 -290 N
ATOM 4050 CA LEU A 485 22.052 11.916 -40.085 1.00 36.26 C
ANISOU 4050 CA LEU A 485 4880 4480 4415 -84 191 -329 C
ATOM 4051 C LEU A 485 23.515 11.463 -40.180 1.00 35.61 C
ANISOU 4051 C LEU A 485 4760 4414 4355 -103 164 -371 C
ATOM 4052 O LEU A 485 24.415 12.290 -40.291 1.00 34.21 O
ANISOU 4052 O LEU A 485 4579 4229 4191 -131 212 -410 O
ATOM 4053 CB LEU A 485 21.646 12.165 -38.623 1.00 33.64 C
ANISOU 4053 CB LEU A 485 4557 4158 4065 -116 182 -332 C
ATOM 4054 CG LEU A 485 20.369 12.950 -38.255 1.00 35.29 C
ANISOU 4054 CG LEU A 485 4804 4350 4254 -108 226 -303 C
ATOM 4055 CD1 LEU A 485 20.228 12.996 -36.746 1.00 34.62 C
ANISOU 4055 CD1 LEU A 485 4719 4281 4152 -148 206 -317 C
ATOM 4056 CD2 LEU A 485 20.329 14.370 -38.819 1.00 36.74 C
ANISOU 4056 CD2 LEU A 485 5023 4493 4443 -102 325 -306 C
ATOM 4057 N ARG A 486 23.727 10.144 -40.163 1.00 35.58 N
ANISOU 4057 N ARG A 486 4729 4432 4358 -86 93 -363 N
ATOM 4058 CA ARG A 486 25.064 9.567 -40.250 1.00 38.42 C
ANISOU 4058 CA ARG A 486 5048 4812 4739 -91 62 -396 C
ATOM 4059 C ARG A 486 25.679 9.600 -41.666 1.00 37.86 C
ANISOU 4059 C ARG A 486 4968 4726 4690 -73 91 -410 C
ATOM 4060 O ARG A 486 26.870 9.891 -41.820 1.00 37.99 O
ANISOU 4060 O ARG A 486 4957 4754 4723 -91 107 -451 O
ATOM 4061 CB ARG A 486 25.049 8.139 -39.694 1.00 43.02 C
ANISOU 4061 CB ARG A 486 5610 5413 5320 -71 -13 -376 C
ATOM 4062 CG ARG A 486 26.134 7.208 -40.214 1.00 45.54 C
ANISOU 4062 CG ARG A 486 5893 5743 5664 -48 -45 -390 C
ATOM 4063 CD ARG A 486 27.546 7.690 -39.895 1.00 52.89 C
ANISOU 4063 CD ARG A 486 6781 6709 6603 -73 -38 -436 C
ATOM 4064 NE ARG A 486 27.937 7.436 -38.516 1.00 56.46 N
ANISOU 4064 NE ARG A 486 7205 7207 7037 -87 -81 -439 N
ATOM 4065 CZ ARG A 486 29.196 7.405 -38.091 1.00 61.65 C
ANISOU 4065 CZ ARG A 486 7810 7917 7695 -97 -98 -472 C
ATOM 4066 NH1 ARG A 486 30.193 7.606 -38.948 1.00 62.65 N
ANISOU 4066 NH1 ARG A 486 7907 8052 7845 -98 -74 -509 N
ATOM 4067 NH2 ARG A 486 29.461 7.178 -36.806 1.00 65.39 N
ANISOU 4067 NH2 ARG A 486 8257 8445 8142 -108 -139 -470 N
ATOM 4068 N THR A 487 24.864 9.317 -42.684 1.00 38.03 N
ANISOU 4068 N THR A 487 5010 4730 4707 -39 99 -380 N
ATOM 4069 CA THR A 487 25.352 9.096 -44.058 1.00 36.12 C
ANISOU 4069 CA THR A 487 4759 4481 4482 -19 116 -390 C
ATOM 4070 C THR A 487 25.376 10.336 -44.929 1.00 36.50 C
ANISOU 4070 C THR A 487 4830 4510 4527 -20 193 -393 C
ATOM 4071 O THR A 487 26.057 10.353 -45.953 1.00 38.00 O
ANISOU 4071 O THR A 487 5010 4696 4732 -13 215 -411 O
ATOM 4072 CB THR A 487 24.513 8.059 -44.809 1.00 35.98 C
ANISOU 4072 CB THR A 487 4748 4466 4457 12 85 -361 C
ATOM 4073 OG1 THR A 487 23.157 8.504 -44.865 1.00 34.91 O
ANISOU 4073 OG1 THR A 487 4642 4332 4291 23 105 -324 O
ATOM 4074 CG2 THR A 487 24.591 6.692 -44.132 1.00 36.63 C
ANISOU 4074 CG2 THR A 487 4813 4555 4547 17 18 -357 C
ATOM 4075 N SER A 488 24.604 11.351 -44.555 1.00 34.84 N
ANISOU 4075 N SER A 488 4654 4284 4298 -25 239 -374 N
ATOM 4076 CA SER A 488 24.520 12.581 -45.337 1.00 34.12 C
ANISOU 4076 CA SER A 488 4595 4165 4202 -17 323 -367 C
ATOM 4077 C SER A 488 24.931 13.863 -44.556 1.00 36.07 C
ANISOU 4077 C SER A 488 4864 4384 4455 -59 389 -394 C
ATOM 4078 O SER A 488 25.612 14.734 -45.101 1.00 39.31 O
ANISOU 4078 O SER A 488 5290 4769 4877 -75 459 -418 O
ATOM 4079 CB SER A 488 23.114 12.726 -45.901 1.00 31.88 C
ANISOU 4079 CB SER A 488 4338 3884 3888 27 339 -310 C
ATOM 4080 OG SER A 488 22.943 13.996 -46.489 1.00 32.49 O
ANISOU 4080 OG SER A 488 4453 3932 3958 44 427 -292 O
ATOM 4081 N PHE A 489 24.490 13.993 -43.308 1.00 33.14 N
ANISOU 4081 N PHE A 489 4500 4018 4074 -81 374 -394 N
ATOM 4082 CA PHE A 489 24.859 15.152 -42.499 1.00 35.70 C
ANISOU 4082 CA PHE A 489 4844 4318 4400 -131 438 -429 C
ATOM 4083 C PHE A 489 26.223 14.872 -41.926 1.00 37.60 C
ANISOU 4083 C PHE A 489 5039 4591 4655 -183 408 -491 C
ATOM 4084 O PHE A 489 26.865 15.743 -41.333 1.00 36.80 O
ANISOU 4084 O PHE A 489 4940 4484 4556 -239 459 -539 O
ATOM 4085 CB PHE A 489 23.865 15.364 -41.360 1.00 32.08 C
ANISOU 4085 CB PHE A 489 4407 3860 3922 -137 432 -408 C
ATOM 4086 CG PHE A 489 22.546 15.922 -41.802 1.00 30.65 C
ANISOU 4086 CG PHE A 489 4271 3651 3724 -88 479 -351 C
ATOM 4087 CD1 PHE A 489 21.589 15.098 -42.389 1.00 28.80 C
ANISOU 4087 CD1 PHE A 489 4028 3442 3473 -34 429 -300 C
ATOM 4088 CD2 PHE A 489 22.239 17.262 -41.586 1.00 29.97 C
ANISOU 4088 CD2 PHE A 489 4233 3517 3635 -96 575 -350 C
ATOM 4089 CE1 PHE A 489 20.370 15.597 -42.771 1.00 26.86 C
ANISOU 4089 CE1 PHE A 489 3813 3188 3205 14 469 -247 C
ATOM 4090 CE2 PHE A 489 21.018 17.769 -41.980 1.00 29.36 C
ANISOU 4090 CE2 PHE A 489 4192 3420 3540 -39 620 -290 C
ATOM 4091 CZ PHE A 489 20.088 16.937 -42.581 1.00 28.05 C
ANISOU 4091 CZ PHE A 489 4009 3293 3353 17 563 -238 C
ATOM 4092 N LEU A 490 26.645 13.626 -42.105 1.00 40.68 N
ANISOU 4092 N LEU A 490 5384 5018 5052 -163 328 -490 N
ATOM 4093 CA LEU A 490 27.895 13.119 -41.557 1.00 43.50 C
ANISOU 4093 CA LEU A 490 5686 5421 5419 -196 284 -538 C
ATOM 4094 C LEU A 490 28.068 13.457 -40.077 1.00 43.35 C
ANISOU 4094 C LEU A 490 5653 5433 5382 -246 274 -567 C
ATOM 4095 O LEU A 490 29.097 13.997 -39.683 1.00 47.88 O
ANISOU 4095 O LEU A 490 6199 6033 5956 -300 300 -625 O
ATOM 4096 CB LEU A 490 29.103 13.608 -42.386 1.00 42.83 C
ANISOU 4096 CB LEU A 490 5583 5333 5355 -219 333 -586 C
ATOM 4097 CG LEU A 490 29.104 13.412 -43.917 1.00 45.41 C
ANISOU 4097 CG LEU A 490 5921 5633 5697 -177 354 -566 C
ATOM 4098 CD1 LEU A 490 30.458 13.834 -44.505 1.00 42.96 C
ANISOU 4098 CD1 LEU A 490 5586 5330 5407 -210 397 -622 C
ATOM 4099 CD2 LEU A 490 28.747 11.976 -44.323 1.00 43.34 C
ANISOU 4099 CD2 LEU A 490 5639 5388 5438 -124 274 -529 C
ATOM 4100 N VAL A 491 27.080 13.106 -39.256 1.00 44.49 N
ANISOU 4100 N VAL A 491 5814 5582 5507 -234 236 -531 N
ATOM 4101 CA VAL A 491 27.189 13.292 -37.783 1.00 47.43 C
ANISOU 4101 CA VAL A 491 6171 5993 5856 -280 218 -555 C
ATOM 4102 C VAL A 491 28.028 12.177 -37.132 1.00 48.90 C
ANISOU 4102 C VAL A 491 6295 6248 6036 -277 131 -565 C
ATOM 4103 O VAL A 491 27.908 11.005 -37.498 1.00 52.37 O
ANISOU 4103 O VAL A 491 6722 6691 6484 -225 71 -527 O
ATOM 4104 CB VAL A 491 25.790 13.345 -37.104 1.00 46.99 C
ANISOU 4104 CB VAL A 491 6156 5917 5779 -268 212 -511 C
ATOM 4105 CG1 VAL A 491 25.900 13.389 -35.578 1.00 44.77 C
ANISOU 4105 CG1 VAL A 491 5857 5683 5470 -315 185 -534 C
ATOM 4106 CG2 VAL A 491 24.995 14.530 -37.613 1.00 44.26 C
ANISOU 4106 CG2 VAL A 491 5868 5510 5437 -266 304 -499 C
ATOM 4107 N ASN A 492 28.879 12.543 -36.180 1.00 52.78 N
ANISOU 4107 N ASN A 492 6748 6797 6509 -331 129 -615 N
ATOM 4108 CA ASN A 492 29.592 11.546 -35.365 1.00 61.09 C
ANISOU 4108 CA ASN A 492 7739 7928 7544 -321 46 -616 C
ATOM 4109 C ASN A 492 29.267 11.601 -33.865 1.00 63.24 C
ANISOU 4109 C ASN A 492 8004 8249 7775 -354 18 -616 C
ATOM 4110 O ASN A 492 29.314 10.568 -33.184 1.00 64.47 O
ANISOU 4110 O ASN A 492 8132 8451 7913 -322 -56 -583 O
ATOM 4111 CB ASN A 492 31.110 11.590 -35.603 1.00 63.96 C
ANISOU 4111 CB ASN A 492 8036 8351 7914 -343 46 -671 C
ATOM 4112 CG ASN A 492 31.582 12.935 -36.121 1.00 72.08 C
ANISOU 4112 CG ASN A 492 9077 9355 8953 -405 140 -734 C
ATOM 4113 OD1 ASN A 492 31.240 13.988 -35.568 1.00 76.76 O
ANISOU 4113 OD1 ASN A 492 9702 9933 9530 -463 200 -764 O
ATOM 4114 ND2 ASN A 492 32.370 12.909 -37.194 1.00 71.42 N
ANISOU 4114 ND2 ASN A 492 8974 9264 8897 -394 161 -755 N
ATOM 4115 N ASP A 493 28.938 12.796 -33.357 1.00 60.60 N
ANISOU 4115 N ASP A 493 7698 7901 7425 -416 83 -652 N
ATOM 4116 CA ASP A 493 28.444 12.937 -31.979 1.00 60.17 C
ANISOU 4116 CA ASP A 493 7648 7883 7330 -451 66 -652 C
ATOM 4117 C ASP A 493 26.924 13.102 -31.928 1.00 55.98 C
ANISOU 4117 C ASP A 493 7186 7282 6801 -430 87 -603 C
ATOM 4118 O ASP A 493 26.379 14.168 -32.251 1.00 53.40 O
ANISOU 4118 O ASP A 493 6909 6895 6486 -452 169 -616 O
ATOM 4119 CB ASP A 493 29.139 14.083 -31.227 1.00 62.10 C
ANISOU 4119 CB ASP A 493 7870 8175 7548 -544 122 -734 C
ATOM 4120 CG ASP A 493 28.862 14.051 -29.709 1.00 65.43 C
ANISOU 4120 CG ASP A 493 8277 8661 7919 -582 89 -740 C
ATOM 4121 OD1 ASP A 493 27.704 13.790 -29.301 1.00 62.89 O
ANISOU 4121 OD1 ASP A 493 8000 8304 7590 -556 73 -689 O
ATOM 4122 OD2 ASP A 493 29.805 14.300 -28.922 1.00 70.35 O
ANISOU 4122 OD2 ASP A 493 8843 9379 8506 -641 81 -799 O
ATOM 4123 N PHE A 494 26.253 12.047 -31.485 1.00 51.18 N
ANISOU 4123 N PHE A 494 6582 6684 6180 -386 17 -546 N
ATOM 4124 CA PHE A 494 24.804 12.014 -31.485 1.00 51.94 C
ANISOU 4124 CA PHE A 494 6733 6724 6275 -361 27 -497 C
ATOM 4125 C PHE A 494 24.190 12.505 -30.165 1.00 50.88 C
ANISOU 4125 C PHE A 494 6615 6611 6104 -406 38 -506 C
ATOM 4126 O PHE A 494 23.069 12.140 -29.833 1.00 53.11 O
ANISOU 4126 O PHE A 494 6929 6873 6377 -384 20 -461 O
ATOM 4127 CB PHE A 494 24.306 10.604 -31.839 1.00 53.06 C
ANISOU 4127 CB PHE A 494 6877 6856 6426 -294 -42 -434 C
ATOM 4128 CG PHE A 494 24.575 10.201 -33.272 1.00 53.62 C
ANISOU 4128 CG PHE A 494 6946 6891 6534 -249 -38 -422 C
ATOM 4129 CD1 PHE A 494 23.640 10.462 -34.271 1.00 52.47 C
ANISOU 4129 CD1 PHE A 494 6842 6687 6407 -223 0 -397 C
ATOM 4130 CD2 PHE A 494 25.766 9.567 -33.622 1.00 54.28 C
ANISOU 4130 CD2 PHE A 494 6983 7007 6633 -232 -73 -437 C
ATOM 4131 CE1 PHE A 494 23.883 10.096 -35.587 1.00 55.46 C
ANISOU 4131 CE1 PHE A 494 7218 7040 6814 -185 4 -389 C
ATOM 4132 CE2 PHE A 494 26.017 9.206 -34.935 1.00 56.46 C
ANISOU 4132 CE2 PHE A 494 7259 7250 6943 -195 -66 -430 C
ATOM 4133 CZ PHE A 494 25.073 9.468 -35.920 1.00 56.76 C
ANISOU 4133 CZ PHE A 494 7341 7230 6995 -174 -27 -407 C
ATOM 4134 N GLY A 495 24.914 13.361 -29.446 1.00 46.40 N
ANISOU 4134 N GLY A 495 6026 6085 5516 -475 72 -569 N
ATOM 4135 CA GLY A 495 24.497 13.817 -28.122 1.00 45.46 C
ANISOU 4135 CA GLY A 495 5916 5999 5357 -528 82 -588 C
ATOM 4136 C GLY A 495 23.200 14.616 -28.087 1.00 43.64 C
ANISOU 4136 C GLY A 495 5751 5696 5132 -532 150 -574 C
ATOM 4137 O GLY A 495 22.272 14.276 -27.329 1.00 42.38 O
ANISOU 4137 O GLY A 495 5610 5542 4949 -525 123 -540 O
ATOM 4138 N PHE A 496 23.154 15.685 -28.891 1.00 41.09 N
ANISOU 4138 N PHE A 496 5463 5308 4838 -542 242 -598 N
ATOM 4139 CA PHE A 496 21.960 16.516 -29.091 1.00 37.89 C
ANISOU 4139 CA PHE A 496 5122 4827 4444 -529 318 -577 C
ATOM 4140 C PHE A 496 20.679 15.704 -29.304 1.00 35.62 C
ANISOU 4140 C PHE A 496 4856 4520 4157 -460 271 -500 C
ATOM 4141 O PHE A 496 19.588 16.208 -29.080 1.00 34.24 O
ANISOU 4141 O PHE A 496 4721 4309 3977 -451 315 -479 O
ATOM 4142 CB PHE A 496 22.168 17.494 -30.275 1.00 38.49 C
ANISOU 4142 CB PHE A 496 5233 4833 4558 -520 413 -592 C
ATOM 4143 CG PHE A 496 22.053 16.845 -31.643 1.00 38.17 C
ANISOU 4143 CG PHE A 496 5190 4765 4545 -444 384 -540 C
ATOM 4144 CD1 PHE A 496 20.821 16.746 -32.280 1.00 38.49 C
ANISOU 4144 CD1 PHE A 496 5267 4763 4594 -378 394 -476 C
ATOM 4145 CD2 PHE A 496 23.178 16.325 -32.282 1.00 38.00 C
ANISOU 4145 CD2 PHE A 496 5127 4772 4539 -440 347 -558 C
ATOM 4146 CE1 PHE A 496 20.708 16.124 -33.518 1.00 40.92 C
ANISOU 4146 CE1 PHE A 496 5569 5058 4921 -315 366 -434 C
ATOM 4147 CE2 PHE A 496 23.076 15.726 -33.529 1.00 40.17 C
ANISOU 4147 CE2 PHE A 496 5401 5023 4838 -376 324 -516 C
ATOM 4148 CZ PHE A 496 21.837 15.620 -34.148 1.00 40.83 C
ANISOU 4148 CZ PHE A 496 5520 5067 4925 -316 333 -455 C
ATOM 4149 N ILE A 497 20.820 14.451 -29.736 1.00 35.16 N
ANISOU 4149 N ILE A 497 4768 4486 4104 -414 188 -461 N
ATOM 4150 CA ILE A 497 19.673 13.571 -29.966 1.00 35.20 C
ANISOU 4150 CA ILE A 497 4789 4479 4107 -358 143 -396 C
ATOM 4151 C ILE A 497 18.813 13.370 -28.710 1.00 34.34 C
ANISOU 4151 C ILE A 497 4691 4393 3964 -378 119 -380 C
ATOM 4152 O ILE A 497 17.562 13.398 -28.788 1.00 33.36 O
ANISOU 4152 O ILE A 497 4597 4243 3836 -352 134 -343 O
ATOM 4153 CB ILE A 497 20.107 12.213 -30.572 1.00 37.08 C
ANISOU 4153 CB ILE A 497 4995 4735 4356 -315 64 -366 C
ATOM 4154 CG1 ILE A 497 20.053 12.282 -32.087 1.00 37.32 C
ANISOU 4154 CG1 ILE A 497 5035 4723 4419 -271 92 -351 C
ATOM 4155 CG2 ILE A 497 19.226 11.055 -30.105 1.00 37.07 C
ANISOU 4155 CG2 ILE A 497 4998 4748 4337 -290 0 -317 C
ATOM 4156 CD1 ILE A 497 21.365 12.678 -32.711 1.00 40.25 C
ANISOU 4156 CD1 ILE A 497 5384 5096 4813 -285 116 -393 C
ATOM 4157 N TRP A 498 19.467 13.204 -27.558 1.00 32.25 N
ANISOU 4157 N TRP A 498 4399 4185 3669 -426 85 -410 N
ATOM 4158 CA TRP A 498 18.737 12.892 -26.314 1.00 31.12 C
ANISOU 4158 CA TRP A 498 4263 4071 3487 -446 56 -394 C
ATOM 4159 C TRP A 498 17.581 13.815 -26.033 1.00 30.65 C
ANISOU 4159 C TRP A 498 4248 3973 3424 -458 124 -393 C
ATOM 4160 O TRP A 498 16.453 13.367 -25.803 1.00 28.48 O
ANISOU 4160 O TRP A 498 3992 3691 3137 -434 106 -351 O
ATOM 4161 CB TRP A 498 19.660 12.856 -25.098 1.00 31.09 C
ANISOU 4161 CB TRP A 498 4223 4143 3445 -502 24 -434 C
ATOM 4162 CG TRP A 498 18.878 12.508 -23.871 1.00 30.42 C
ANISOU 4162 CG TRP A 498 4149 4089 3319 -520 -5 -412 C
ATOM 4163 CD1 TRP A 498 18.694 13.278 -22.735 1.00 31.28 C
ANISOU 4163 CD1 TRP A 498 4265 4226 3392 -582 29 -451 C
ATOM 4164 CD2 TRP A 498 18.038 11.318 -23.670 1.00 30.65 C
ANISOU 4164 CD2 TRP A 498 4190 4117 3337 -478 -66 -348 C
ATOM 4165 NE1 TRP A 498 17.845 12.648 -21.848 1.00 30.23 N
ANISOU 4165 NE1 TRP A 498 4145 4114 3226 -579 -10 -413 N
ATOM 4166 CE2 TRP A 498 17.419 11.466 -22.359 1.00 31.24 C
ANISOU 4166 CE2 TRP A 498 4277 4224 3368 -518 -67 -350 C
ATOM 4167 CE3 TRP A 498 17.767 10.178 -24.417 1.00 29.16 C
ANISOU 4167 CE3 TRP A 498 4004 3904 3170 -419 -113 -295 C
ATOM 4168 CZ2 TRP A 498 16.574 10.493 -21.827 1.00 30.27 C
ANISOU 4168 CZ2 TRP A 498 4169 4108 3224 -498 -114 -298 C
ATOM 4169 CZ3 TRP A 498 16.917 9.219 -23.882 1.00 30.04 C
ANISOU 4169 CZ3 TRP A 498 4132 4020 3261 -403 -156 -247 C
ATOM 4170 CH2 TRP A 498 16.340 9.370 -22.610 1.00 29.89 C
ANISOU 4170 CH2 TRP A 498 4125 4031 3199 -441 -157 -247 C
ATOM 4171 N LEU A 499 17.851 15.121 -26.045 1.00 31.19 N
ANISOU 4171 N LEU A 499 4335 4015 3501 -496 211 -442 N
ATOM 4172 CA LEU A 499 16.810 16.087 -25.721 1.00 31.30 C
ANISOU 4172 CA LEU A 499 4393 3987 3512 -505 288 -444 C
ATOM 4173 C LEU A 499 15.763 16.225 -26.817 1.00 29.24 C
ANISOU 4173 C LEU A 499 4162 3669 3277 -434 322 -391 C
ATOM 4174 O LEU A 499 14.609 16.507 -26.523 1.00 29.48 O
ANISOU 4174 O LEU A 499 4219 3682 3297 -418 352 -367 O
ATOM 4175 CB LEU A 499 17.402 17.455 -25.320 1.00 33.31 C
ANISOU 4175 CB LEU A 499 4664 4222 3766 -572 382 -515 C
ATOM 4176 CG LEU A 499 18.163 17.456 -23.978 1.00 35.43 C
ANISOU 4176 CG LEU A 499 4903 4565 3993 -655 357 -573 C
ATOM 4177 CD1 LEU A 499 19.151 18.611 -23.915 1.00 36.76 C
ANISOU 4177 CD1 LEU A 499 5072 4725 4167 -727 441 -656 C
ATOM 4178 CD2 LEU A 499 17.221 17.458 -22.759 1.00 35.01 C
ANISOU 4178 CD2 LEU A 499 4865 4531 3902 -680 353 -567 C
ATOM 4179 N VAL A 500 16.144 15.995 -28.072 1.00 27.93 N
ANISOU 4179 N VAL A 500 3988 3483 3140 -390 316 -373 N
ATOM 4180 CA VAL A 500 15.156 15.999 -29.154 1.00 28.39 C
ANISOU 4180 CA VAL A 500 4065 3507 3213 -318 338 -320 C
ATOM 4181 C VAL A 500 14.224 14.780 -28.985 1.00 28.60 C
ANISOU 4181 C VAL A 500 4077 3568 3220 -289 259 -272 C
ATOM 4182 O VAL A 500 12.999 14.919 -29.048 1.00 27.52 O
ANISOU 4182 O VAL A 500 3956 3425 3073 -258 280 -237 O
ATOM 4183 CB VAL A 500 15.815 15.966 -30.565 1.00 30.71 C
ANISOU 4183 CB VAL A 500 4351 3779 3537 -281 346 -313 C
ATOM 4184 CG1 VAL A 500 14.751 15.999 -31.666 1.00 28.14 C
ANISOU 4184 CG1 VAL A 500 4039 3433 3217 -207 369 -257 C
ATOM 4185 CG2 VAL A 500 16.821 17.110 -30.737 1.00 29.47 C
ANISOU 4185 CG2 VAL A 500 4209 3586 3399 -317 427 -365 C
ATOM 4186 N LEU A 501 14.816 13.598 -28.760 1.00 27.75 N
ANISOU 4186 N LEU A 501 3939 3498 3107 -300 174 -270 N
ATOM 4187 CA LEU A 501 14.054 12.386 -28.458 1.00 27.98 C
ANISOU 4187 CA LEU A 501 3959 3554 3116 -286 104 -231 C
ATOM 4188 C LEU A 501 13.093 12.612 -27.260 1.00 27.99 C
ANISOU 4188 C LEU A 501 3977 3569 3086 -313 115 -227 C
ATOM 4189 O LEU A 501 11.882 12.361 -27.377 1.00 26.96 O
ANISOU 4189 O LEU A 501 3856 3441 2946 -287 115 -193 O
ATOM 4190 CB LEU A 501 14.996 11.176 -28.187 1.00 28.31 C
ANISOU 4190 CB LEU A 501 3973 3627 3156 -296 23 -232 C
ATOM 4191 CG LEU A 501 14.313 9.816 -27.901 1.00 28.68 C
ANISOU 4191 CG LEU A 501 4018 3690 3186 -282 -41 -192 C
ATOM 4192 CD1 LEU A 501 13.269 9.492 -28.965 1.00 28.24 C
ANISOU 4192 CD1 LEU A 501 3970 3617 3140 -241 -32 -160 C
ATOM 4193 CD2 LEU A 501 15.304 8.661 -27.754 1.00 28.16 C
ANISOU 4193 CD2 LEU A 501 3931 3644 3123 -279 -108 -187 C
ATOM 4194 N SER A 502 13.635 13.104 -26.138 1.00 29.07 N
ANISOU 4194 N SER A 502 4116 3723 3206 -367 127 -265 N
ATOM 4195 CA SER A 502 12.829 13.470 -24.935 1.00 30.06 C
ANISOU 4195 CA SER A 502 4259 3861 3301 -401 147 -271 C
ATOM 4196 C SER A 502 11.660 14.436 -25.195 1.00 30.15 C
ANISOU 4196 C SER A 502 4300 3836 3317 -376 226 -259 C
ATOM 4197 O SER A 502 10.541 14.172 -24.750 1.00 31.80 O
ANISOU 4197 O SER A 502 4517 4058 3506 -369 219 -232 O
ATOM 4198 CB SER A 502 13.720 14.026 -23.810 1.00 32.04 C
ANISOU 4198 CB SER A 502 4504 4139 3530 -469 160 -325 C
ATOM 4199 OG SER A 502 14.716 13.082 -23.437 1.00 36.28 O
ANISOU 4199 OG SER A 502 5007 4725 4052 -484 82 -328 O
ATOM 4200 N SER A 503 11.922 15.566 -25.857 1.00 28.45 N
ANISOU 4200 N SER A 503 4103 3578 3128 -363 306 -277 N
ATOM 4201 CA SER A 503 10.848 16.468 -26.301 1.00 29.34 C
ANISOU 4201 CA SER A 503 4244 3653 3249 -319 386 -254 C
ATOM 4202 C SER A 503 9.770 15.756 -27.117 1.00 28.80 C
ANISOU 4202 C SER A 503 4162 3602 3177 -254 352 -195 C
ATOM 4203 O SER A 503 8.561 15.946 -26.876 1.00 29.45 O
ANISOU 4203 O SER A 503 4252 3694 3243 -231 376 -169 O
ATOM 4204 CB SER A 503 11.417 17.570 -27.168 1.00 32.58 C
ANISOU 4204 CB SER A 503 4677 4010 3692 -300 471 -270 C
ATOM 4205 OG SER A 503 12.327 18.319 -26.418 1.00 45.07 O
ANISOU 4205 OG SER A 503 6273 5577 5275 -369 515 -332 O
ATOM 4206 N THR A 504 10.210 14.963 -28.097 1.00 27.73 N
ANISOU 4206 N THR A 504 4003 3477 3054 -227 301 -178 N
ATOM 4207 CA THR A 504 9.314 14.172 -28.942 1.00 27.63 C
ANISOU 4207 CA THR A 504 3972 3491 3034 -177 264 -132 C
ATOM 4208 C THR A 504 8.397 13.265 -28.144 1.00 27.18 C
ANISOU 4208 C THR A 504 3904 3474 2946 -196 212 -116 C
ATOM 4209 O THR A 504 7.193 13.285 -28.350 1.00 29.24 O
ANISOU 4209 O THR A 504 4160 3757 3191 -165 227 -88 O
ATOM 4210 CB THR A 504 10.106 13.331 -29.956 1.00 28.41 C
ANISOU 4210 CB THR A 504 4048 3594 3150 -162 213 -129 C
ATOM 4211 OG1 THR A 504 11.002 14.187 -30.667 1.00 28.78 O
ANISOU 4211 OG1 THR A 504 4105 3604 3223 -149 264 -146 O
ATOM 4212 CG2 THR A 504 9.167 12.646 -30.952 1.00 28.18 C
ANISOU 4212 CG2 THR A 504 3999 3596 3110 -115 189 -90 C
ATOM 4213 N VAL A 505 8.951 12.468 -27.231 1.00 27.16 N
ANISOU 4213 N VAL A 505 3899 3486 2935 -245 153 -133 N
ATOM 4214 CA VAL A 505 8.098 11.596 -26.380 1.00 26.60 C
ANISOU 4214 CA VAL A 505 3825 3448 2833 -269 109 -117 C
ATOM 4215 C VAL A 505 7.113 12.444 -25.564 1.00 25.74 C
ANISOU 4215 C VAL A 505 3731 3343 2703 -278 163 -119 C
ATOM 4216 O VAL A 505 5.927 12.126 -25.465 1.00 25.07 O
ANISOU 4216 O VAL A 505 3641 3285 2599 -267 159 -96 O
ATOM 4217 CB VAL A 505 8.931 10.719 -25.429 1.00 26.74 C
ANISOU 4217 CB VAL A 505 3841 3478 2839 -315 46 -130 C
ATOM 4218 CG1 VAL A 505 8.038 10.041 -24.373 1.00 26.31 C
ANISOU 4218 CG1 VAL A 505 3794 3451 2750 -344 17 -115 C
ATOM 4219 CG2 VAL A 505 9.746 9.697 -26.210 1.00 25.56 C
ANISOU 4219 CG2 VAL A 505 3676 3325 2709 -298 -7 -121 C
ATOM 4220 N ARG A 506 7.603 13.550 -25.021 1.00 26.20 N
ANISOU 4220 N ARG A 506 3810 3376 2769 -300 218 -151 N
ATOM 4221 CA ARG A 506 6.731 14.493 -24.337 1.00 26.72 C
ANISOU 4221 CA ARG A 506 3895 3435 2821 -305 284 -156 C
ATOM 4222 C ARG A 506 5.591 14.979 -25.261 1.00 25.53 C
ANISOU 4222 C ARG A 506 3741 3283 2675 -235 334 -119 C
ATOM 4223 O ARG A 506 4.439 14.878 -24.910 1.00 24.59 O
ANISOU 4223 O ARG A 506 3616 3192 2533 -225 340 -100 O
ATOM 4224 CB ARG A 506 7.559 15.646 -23.736 1.00 28.71 C
ANISOU 4224 CB ARG A 506 4171 3652 3082 -345 348 -204 C
ATOM 4225 CG ARG A 506 6.733 16.692 -22.978 1.00 30.61 C
ANISOU 4225 CG ARG A 506 4439 3877 3312 -354 429 -217 C
ATOM 4226 CD ARG A 506 6.578 17.907 -23.906 1.00 33.81 C
ANISOU 4226 CD ARG A 506 4868 4228 3748 -298 528 -208 C
ATOM 4227 NE ARG A 506 5.212 18.392 -23.914 1.00 34.05 N
ANISOU 4227 NE ARG A 506 4907 4258 3770 -248 582 -175 N
ATOM 4228 CZ ARG A 506 4.679 19.148 -24.858 1.00 35.24 C
ANISOU 4228 CZ ARG A 506 5068 4382 3938 -172 651 -141 C
ATOM 4229 NH1 ARG A 506 5.391 19.517 -25.936 1.00 32.52 N
ANISOU 4229 NH1 ARG A 506 4731 4003 3622 -137 678 -133 N
ATOM 4230 NH2 ARG A 506 3.414 19.526 -24.718 1.00 35.95 N
ANISOU 4230 NH2 ARG A 506 5159 4485 4015 -126 696 -110 N
ATOM 4231 N ALA A 507 5.932 15.409 -26.473 1.00 25.37 N
ANISOU 4231 N ALA A 507 3719 3240 2680 -185 365 -106 N
ATOM 4232 CA ALA A 507 4.963 15.991 -27.409 1.00 25.91 C
ANISOU 4232 CA ALA A 507 3782 3312 2747 -109 418 -66 C
ATOM 4233 C ALA A 507 3.917 15.014 -27.893 1.00 26.59 C
ANISOU 4233 C ALA A 507 3830 3463 2808 -81 365 -30 C
ATOM 4234 O ALA A 507 2.737 15.382 -28.017 1.00 28.62 O
ANISOU 4234 O ALA A 507 4076 3751 3046 -36 400 -1 O
ATOM 4235 CB ALA A 507 5.676 16.624 -28.602 1.00 25.36 C
ANISOU 4235 CB ALA A 507 3722 3206 2707 -64 461 -58 C
ATOM 4236 N TYR A 508 4.330 13.782 -28.203 1.00 26.08 N
ANISOU 4236 N TYR A 508 3745 3421 2742 -105 285 -33 N
ATOM 4237 CA TYR A 508 3.381 12.785 -28.701 1.00 26.54 C
ANISOU 4237 CA TYR A 508 3768 3540 2775 -91 238 -9 C
ATOM 4238 C TYR A 508 2.459 12.289 -27.594 1.00 28.10 C
ANISOU 4238 C TYR A 508 3962 3770 2942 -131 218 -12 C
ATOM 4239 O TYR A 508 1.246 12.154 -27.798 1.00 28.05 O
ANISOU 4239 O TYR A 508 3929 3817 2909 -108 224 8 O
ATOM 4240 CB TYR A 508 4.107 11.639 -29.401 1.00 26.91 C
ANISOU 4240 CB TYR A 508 3800 3590 2832 -106 172 -15 C
ATOM 4241 CG TYR A 508 4.404 11.962 -30.855 1.00 28.45 C
ANISOU 4241 CG TYR A 508 3981 3787 3041 -50 192 0 C
ATOM 4242 CD1 TYR A 508 3.420 11.829 -31.821 1.00 28.76 C
ANISOU 4242 CD1 TYR A 508 3986 3885 3056 -4 197 27 C
ATOM 4243 CD2 TYR A 508 5.645 12.446 -31.248 1.00 28.95 C
ANISOU 4243 CD2 TYR A 508 4062 3799 3137 -45 209 -14 C
ATOM 4244 CE1 TYR A 508 3.671 12.119 -33.139 1.00 29.77 C
ANISOU 4244 CE1 TYR A 508 4098 4021 3188 47 215 43 C
ATOM 4245 CE2 TYR A 508 5.909 12.751 -32.579 1.00 30.44 C
ANISOU 4245 CE2 TYR A 508 4240 3988 3336 5 230 0 C
ATOM 4246 CZ TYR A 508 4.910 12.593 -33.522 1.00 30.42 C
ANISOU 4246 CZ TYR A 508 4205 4045 3306 53 233 32 C
ATOM 4247 OH TYR A 508 5.125 12.913 -34.859 1.00 29.76 O
ANISOU 4247 OH TYR A 508 4109 3971 3225 106 255 51 O
ATOM 4248 N ALA A 509 3.029 12.080 -26.404 1.00 28.14 N
ANISOU 4248 N ALA A 509 3992 3749 2949 -190 197 -37 N
ATOM 4249 CA ALA A 509 2.240 11.776 -25.209 1.00 29.78 C
ANISOU 4249 CA ALA A 509 4205 3981 3128 -232 187 -41 C
ATOM 4250 C ALA A 509 1.192 12.857 -24.912 1.00 29.84 C
ANISOU 4250 C ALA A 509 4213 4002 3123 -202 258 -32 C
ATOM 4251 O ALA A 509 0.071 12.554 -24.478 1.00 28.39 O
ANISOU 4251 O ALA A 509 4013 3861 2909 -210 256 -23 O
ATOM 4252 CB ALA A 509 3.156 11.574 -24.002 1.00 29.22 C
ANISOU 4252 CB ALA A 509 4160 3884 3056 -294 161 -67 C
ATOM 4253 N SER A 510 1.563 14.112 -25.149 1.00 29.96 N
ANISOU 4253 N SER A 510 4247 3976 3160 -167 327 -36 N
ATOM 4254 CA SER A 510 0.659 15.215 -24.904 1.00 32.88 C
ANISOU 4254 CA SER A 510 4624 4344 3523 -129 407 -25 C
ATOM 4255 C SER A 510 -0.466 15.273 -25.940 1.00 34.23 C
ANISOU 4255 C SER A 510 4756 4570 3678 -52 424 18 C
ATOM 4256 O SER A 510 -1.621 15.453 -25.588 1.00 36.23 O
ANISOU 4256 O SER A 510 4992 4865 3906 -34 449 32 O
ATOM 4257 CB SER A 510 1.418 16.534 -24.878 1.00 33.14 C
ANISOU 4257 CB SER A 510 4696 4308 3586 -116 488 -42 C
ATOM 4258 OG SER A 510 0.508 17.600 -24.979 1.00 34.34 O
ANISOU 4258 OG SER A 510 4856 4454 3737 -56 575 -19 O
ATOM 4259 N ARG A 511 -0.132 15.102 -27.213 1.00 36.55 N
ANISOU 4259 N ARG A 511 5032 4873 3982 -9 410 37 N
ATOM 4260 CA ARG A 511 -1.170 15.046 -28.250 1.00 37.41 C
ANISOU 4260 CA ARG A 511 5094 5054 4066 61 416 78 C
ATOM 4261 C ARG A 511 -2.130 13.894 -28.000 1.00 35.41 C
ANISOU 4261 C ARG A 511 4799 4880 3775 24 356 75 C
ATOM 4262 O ARG A 511 -3.333 14.052 -28.164 1.00 35.16 O
ANISOU 4262 O ARG A 511 4729 4917 3711 64 377 98 O
ATOM 4263 CB ARG A 511 -0.569 14.976 -29.666 1.00 39.99 C
ANISOU 4263 CB ARG A 511 5407 5381 4404 106 406 96 C
ATOM 4264 CG ARG A 511 0.002 16.311 -30.143 1.00 48.00 C
ANISOU 4264 CG ARG A 511 6457 6333 5449 165 488 112 C
ATOM 4265 CD ARG A 511 0.485 16.267 -31.594 1.00 51.53 C
ANISOU 4265 CD ARG A 511 6888 6789 5901 215 482 135 C
ATOM 4266 NE ARG A 511 1.638 17.153 -31.844 1.00 55.52 N
ANISOU 4266 NE ARG A 511 7441 7206 6446 225 537 126 N
ATOM 4267 CZ ARG A 511 2.896 16.729 -32.028 1.00 53.99 C
ANISOU 4267 CZ ARG A 511 7262 6971 6280 178 499 94 C
ATOM 4268 NH1 ARG A 511 3.183 15.439 -31.983 1.00 49.04 N
ANISOU 4268 NH1 ARG A 511 6610 6374 5647 124 410 71 N
ATOM 4269 NH2 ARG A 511 3.874 17.602 -32.258 1.00 53.79 N
ANISOU 4269 NH2 ARG A 511 7277 6871 6288 185 557 83 N
ATOM 4270 N ALA A 512 -1.598 12.742 -27.592 1.00 32.77 N
ANISOU 4270 N ALA A 512 4472 4535 3442 -49 287 48 N
ATOM 4271 CA ALA A 512 -2.441 11.618 -27.240 1.00 32.64 C
ANISOU 4271 CA ALA A 512 4429 4579 3394 -96 238 40 C
ATOM 4272 C ALA A 512 -3.406 11.973 -26.095 1.00 33.32 C
ANISOU 4272 C ALA A 512 4517 4687 3457 -113 269 38 C
ATOM 4273 O ALA A 512 -4.619 11.746 -26.214 1.00 33.09 O
ANISOU 4273 O ALA A 512 4445 4734 3392 -102 272 48 O
ATOM 4274 CB ALA A 512 -1.602 10.400 -26.885 1.00 30.50 C
ANISOU 4274 CB ALA A 512 4180 4275 3134 -168 171 16 C
ATOM 4275 N PHE A 513 -2.869 12.532 -25.000 1.00 32.93 N
ANISOU 4275 N PHE A 513 4513 4575 3424 -144 293 20 N
ATOM 4276 CA PHE A 513 -3.680 12.921 -23.832 1.00 33.67 C
ANISOU 4276 CA PHE A 513 4613 4680 3497 -165 326 13 C
ATOM 4277 C PHE A 513 -4.883 13.777 -24.244 1.00 34.93 C
ANISOU 4277 C PHE A 513 4739 4892 3640 -90 389 40 C
ATOM 4278 O PHE A 513 -6.014 13.506 -23.831 1.00 35.18 O
ANISOU 4278 O PHE A 513 4740 4986 3638 -100 390 43 O
ATOM 4279 CB PHE A 513 -2.819 13.658 -22.774 1.00 34.17 C
ANISOU 4279 CB PHE A 513 4729 4670 3581 -200 358 -12 C
ATOM 4280 CG PHE A 513 -3.533 13.908 -21.458 1.00 33.53 C
ANISOU 4280 CG PHE A 513 4661 4599 3476 -239 385 -27 C
ATOM 4281 CD1 PHE A 513 -4.325 15.046 -21.278 1.00 34.00 C
ANISOU 4281 CD1 PHE A 513 4721 4662 3535 -192 467 -19 C
ATOM 4282 CD2 PHE A 513 -3.408 13.006 -20.392 1.00 34.05 C
ANISOU 4282 CD2 PHE A 513 4741 4671 3522 -319 334 -47 C
ATOM 4283 CE1 PHE A 513 -4.981 15.279 -20.062 1.00 34.16 C
ANISOU 4283 CE1 PHE A 513 4752 4691 3534 -229 496 -37 C
ATOM 4284 CE2 PHE A 513 -4.060 13.233 -19.175 1.00 34.12 C
ANISOU 4284 CE2 PHE A 513 4763 4694 3507 -357 360 -62 C
ATOM 4285 CZ PHE A 513 -4.848 14.369 -19.010 1.00 33.78 C
ANISOU 4285 CZ PHE A 513 4717 4654 3463 -315 440 -60 C
ATOM 4286 N LYS A 514 -4.630 14.794 -25.069 1.00 36.98 N
ANISOU 4286 N LYS A 514 5002 5127 3920 -13 444 64 N
ATOM 4287 CA LYS A 514 -5.670 15.711 -25.540 1.00 38.83 C
ANISOU 4287 CA LYS A 514 5207 5407 4140 77 512 101 C
ATOM 4288 C LYS A 514 -6.712 15.019 -26.392 1.00 37.69 C
ANISOU 4288 C LYS A 514 4989 5376 3953 109 476 125 C
ATOM 4289 O LYS A 514 -7.900 15.230 -26.211 1.00 37.60 O
ANISOU 4289 O LYS A 514 4938 5435 3910 140 503 140 O
ATOM 4290 CB LYS A 514 -5.054 16.868 -26.326 1.00 43.97 C
ANISOU 4290 CB LYS A 514 5884 5998 4821 155 579 126 C
ATOM 4291 CG LYS A 514 -4.521 17.981 -25.443 1.00 51.97 C
ANISOU 4291 CG LYS A 514 6961 6915 5867 144 657 106 C
ATOM 4292 CD LYS A 514 -3.979 19.148 -26.262 1.00 58.77 C
ANISOU 4292 CD LYS A 514 7855 7714 6760 221 737 132 C
ATOM 4293 CE LYS A 514 -3.472 20.266 -25.352 1.00 61.54 C
ANISOU 4293 CE LYS A 514 8273 7965 7142 199 826 102 C
ATOM 4294 NZ LYS A 514 -2.627 19.739 -24.239 1.00 63.64 N
ANISOU 4294 NZ LYS A 514 8567 8196 7415 82 777 40 N
ATOM 4295 N LYS A 515 -6.263 14.193 -27.328 1.00 37.37 N
ANISOU 4295 N LYS A 515 4928 5358 3910 98 418 124 N
ATOM 4296 CA LYS A 515 -7.175 13.453 -28.182 1.00 38.69 C
ANISOU 4296 CA LYS A 515 5024 5642 4035 113 382 135 C
ATOM 4297 C LYS A 515 -8.072 12.532 -27.351 1.00 38.40 C
ANISOU 4297 C LYS A 515 4961 5663 3963 38 348 108 C
ATOM 4298 O LYS A 515 -9.267 12.439 -27.599 1.00 40.21 O
ANISOU 4298 O LYS A 515 5129 5999 4149 63 355 118 O
ATOM 4299 CB LYS A 515 -6.397 12.668 -29.241 1.00 40.87 C
ANISOU 4299 CB LYS A 515 5292 5917 4318 98 329 128 C
ATOM 4300 CG LYS A 515 -6.439 13.275 -30.638 1.00 44.42 C
ANISOU 4300 CG LYS A 515 5708 6411 4758 194 355 168 C
ATOM 4301 CD LYS A 515 -5.526 14.486 -30.780 1.00 48.33 C
ANISOU 4301 CD LYS A 515 6257 6808 5297 252 415 191 C
ATOM 4302 CE LYS A 515 -5.243 14.808 -32.248 1.00 50.97 C
ANISOU 4302 CE LYS A 515 6570 7170 5626 329 427 226 C
ATOM 4303 NZ LYS A 515 -6.404 15.439 -32.949 1.00 53.49 N
ANISOU 4303 NZ LYS A 515 6830 7594 5899 432 469 279 N
ATOM 4304 N ILE A 516 -7.492 11.892 -26.337 1.00 36.88 N
ANISOU 4304 N ILE A 516 4817 5405 3788 -49 314 74 N
ATOM 4305 CA ILE A 516 -8.224 11.000 -25.451 1.00 36.27 C
ANISOU 4305 CA ILE A 516 4730 5367 3683 -127 286 48 C
ATOM 4306 C ILE A 516 -9.288 11.759 -24.643 1.00 38.48 C
ANISOU 4306 C ILE A 516 4995 5684 3941 -105 340 55 C
ATOM 4307 O ILE A 516 -10.409 11.261 -24.459 1.00 37.66 O
ANISOU 4307 O ILE A 516 4844 5667 3796 -129 333 47 O
ATOM 4308 CB ILE A 516 -7.265 10.196 -24.525 1.00 34.97 C
ANISOU 4308 CB ILE A 516 4627 5118 3540 -217 242 20 C
ATOM 4309 CG1 ILE A 516 -6.597 9.060 -25.313 1.00 33.86 C
ANISOU 4309 CG1 ILE A 516 4486 4969 3408 -249 184 9 C
ATOM 4310 CG2 ILE A 516 -8.003 9.634 -23.312 1.00 34.17 C
ANISOU 4310 CG2 ILE A 516 4532 5038 3411 -288 235 0 C
ATOM 4311 CD1 ILE A 516 -5.444 8.382 -24.594 1.00 32.26 C
ANISOU 4311 CD1 ILE A 516 4344 4680 3233 -312 145 -6 C
ATOM 4312 N VAL A 517 -8.943 12.972 -24.198 1.00 38.32 N
ANISOU 4312 N VAL A 517 5013 5598 3948 -60 399 68 N
ATOM 4313 CA VAL A 517 -9.875 13.831 -23.473 1.00 39.34 C
ANISOU 4313 CA VAL A 517 5133 5750 4063 -28 462 76 C
ATOM 4314 C VAL A 517 -11.025 14.277 -24.381 1.00 42.51 C
ANISOU 4314 C VAL A 517 5461 6258 4431 65 496 113 C
ATOM 4315 O VAL A 517 -12.195 14.134 -24.032 1.00 44.53 O
ANISOU 4315 O VAL A 517 5669 6599 4649 63 506 111 O
ATOM 4316 CB VAL A 517 -9.148 15.055 -22.847 1.00 39.57 C
ANISOU 4316 CB VAL A 517 5228 5674 4132 -5 528 75 C
ATOM 4317 CG1 VAL A 517 -10.138 16.149 -22.445 1.00 40.00 C
ANISOU 4317 CG1 VAL A 517 5270 5750 4177 58 613 93 C
ATOM 4318 CG2 VAL A 517 -8.317 14.622 -21.637 1.00 36.98 C
ANISOU 4318 CG2 VAL A 517 4958 5274 3818 -106 498 34 C
ATOM 4319 N THR A 518 -10.682 14.791 -25.555 1.00 45.01 N
ANISOU 4319 N THR A 518 5765 6578 4759 148 513 147 N
ATOM 4320 CA THR A 518 -11.666 15.281 -26.522 1.00 48.00 C
ANISOU 4320 CA THR A 518 6071 7064 5102 252 545 192 C
ATOM 4321 C THR A 518 -12.696 14.223 -26.936 1.00 48.70 C
ANISOU 4321 C THR A 518 6073 7296 5131 221 491 180 C
ATOM 4322 O THR A 518 -13.878 14.531 -27.090 1.00 50.88 O
ANISOU 4322 O THR A 518 6282 7684 5366 278 520 202 O
ATOM 4323 CB THR A 518 -10.969 15.822 -27.783 1.00 47.29 C
ANISOU 4323 CB THR A 518 5986 6951 5029 335 561 231 C
ATOM 4324 OG1 THR A 518 -10.141 16.926 -27.421 1.00 47.92 O
ANISOU 4324 OG1 THR A 518 6143 6904 5160 368 627 241 O
ATOM 4325 CG2 THR A 518 -11.985 16.291 -28.815 1.00 48.93 C
ANISOU 4325 CG2 THR A 518 6114 7284 5191 450 591 284 C
ATOM 4326 N TYR A 519 -12.237 12.990 -27.127 1.00 45.66 N
ANISOU 4326 N TYR A 519 5691 6911 4744 130 419 143 N
ATOM 4327 CA TYR A 519 -13.094 11.928 -27.633 1.00 44.25 C
ANISOU 4327 CA TYR A 519 5436 6862 4512 88 373 122 C
ATOM 4328 C TYR A 519 -13.403 10.895 -26.567 1.00 43.27 C
ANISOU 4328 C TYR A 519 5327 6733 4378 -31 340 73 C
ATOM 4329 O TYR A 519 -13.683 9.735 -26.866 1.00 43.09 O
ANISOU 4329 O TYR A 519 5273 6769 4327 -105 295 39 O
ATOM 4330 CB TYR A 519 -12.465 11.294 -28.867 1.00 44.67 C
ANISOU 4330 CB TYR A 519 5475 6933 4565 83 327 118 C
ATOM 4331 CG TYR A 519 -12.244 12.306 -29.953 1.00 46.32 C
ANISOU 4331 CG TYR A 519 5666 7158 4776 204 362 171 C
ATOM 4332 CD1 TYR A 519 -13.319 13.024 -30.474 1.00 48.71 C
ANISOU 4332 CD1 TYR A 519 5893 7582 5032 304 402 214 C
ATOM 4333 CD2 TYR A 519 -10.962 12.584 -30.438 1.00 45.42 C
ANISOU 4333 CD2 TYR A 519 5609 6938 4708 224 360 183 C
ATOM 4334 CE1 TYR A 519 -13.135 13.977 -31.461 1.00 51.27 C
ANISOU 4334 CE1 TYR A 519 6204 7919 5354 424 441 271 C
ATOM 4335 CE2 TYR A 519 -10.768 13.535 -31.431 1.00 47.55 C
ANISOU 4335 CE2 TYR A 519 5868 7219 4979 335 400 234 C
ATOM 4336 CZ TYR A 519 -11.861 14.231 -31.935 1.00 49.66 C
ANISOU 4336 CZ TYR A 519 6065 7604 5199 437 441 281 C
ATOM 4337 OH TYR A 519 -11.708 15.180 -32.917 1.00 53.62 O
ANISOU 4337 OH TYR A 519 6558 8118 5697 556 486 341 O
ATOM 4338 N LYS A 520 -13.358 11.345 -25.317 1.00 42.72 N
ANISOU 4338 N LYS A 520 5309 6591 4330 -52 370 67 N
ATOM 4339 CA LYS A 520 -13.698 10.528 -24.165 1.00 43.06 C
ANISOU 4339 CA LYS A 520 5372 6625 4361 -157 350 28 C
ATOM 4340 C LYS A 520 -15.147 10.051 -24.234 1.00 43.06 C
ANISOU 4340 C LYS A 520 5288 6769 4301 -177 351 13 C
ATOM 4341 O LYS A 520 -16.052 10.823 -24.538 1.00 43.44 O
ANISOU 4341 O LYS A 520 5273 6909 4322 -96 391 38 O
ATOM 4342 CB LYS A 520 -13.473 11.338 -22.889 1.00 42.60 C
ANISOU 4342 CB LYS A 520 5374 6479 4329 -158 392 30 C
ATOM 4343 CG LYS A 520 -13.718 10.570 -21.599 1.00 43.79 C
ANISOU 4343 CG LYS A 520 5557 6613 4469 -264 374 -5 C
ATOM 4344 CD LYS A 520 -13.358 11.403 -20.379 1.00 42.74 C
ANISOU 4344 CD LYS A 520 5486 6394 4360 -268 416 -6 C
ATOM 4345 CE LYS A 520 -11.849 11.555 -20.252 1.00 43.67 C
ANISOU 4345 CE LYS A 520 5677 6391 4524 -280 399 -7 C
ATOM 4346 NZ LYS A 520 -11.492 12.449 -19.115 1.00 45.50 N
ANISOU 4346 NZ LYS A 520 5963 6548 4774 -287 445 -16 N
ATOM 4347 N GLY A 521 -15.354 8.771 -23.964 1.00 42.90 N
ANISOU 4347 N GLY A 521 5267 6769 4261 -285 310 -28 N
ATOM 4348 CA GLY A 521 -16.701 8.229 -23.848 1.00 44.96 C
ANISOU 4348 CA GLY A 521 5456 7161 4465 -329 314 -55 C
ATOM 4349 C GLY A 521 -16.864 7.327 -22.643 1.00 44.91 C
ANISOU 4349 C GLY A 521 5495 7113 4454 -447 303 -94 C
ATOM 4350 O GLY A 521 -15.945 7.179 -21.835 1.00 44.97 O
ANISOU 4350 O GLY A 521 5589 6995 4500 -487 291 -94 O
ATOM 4351 N GLY A 522 -18.021 6.681 -22.552 1.00 45.80 N
ANISOU 4351 N GLY A 522 5547 7339 4516 -506 306 -127 N
ATOM 4352 CA GLY A 522 -18.380 5.877 -21.389 1.00 43.68 C
ANISOU 4352 CA GLY A 522 5315 7046 4235 -616 307 -162 C
ATOM 4353 C GLY A 522 -17.402 4.783 -20.999 1.00 43.95 C
ANISOU 4353 C GLY A 522 5439 6959 4298 -707 271 -179 C
ATOM 4354 O GLY A 522 -17.471 4.278 -19.892 1.00 44.15 O
ANISOU 4354 O GLY A 522 5516 6936 4321 -784 275 -194 O
ATOM 4355 N LYS A 523 -16.491 4.407 -21.901 1.00 45.38 N
ANISOU 4355 N LYS A 523 5640 7095 4505 -696 239 -174 N
ATOM 4356 CA LYS A 523 -15.540 3.310 -21.619 1.00 43.15 C
ANISOU 4356 CA LYS A 523 5441 6701 4251 -773 208 -186 C
ATOM 4357 C LYS A 523 -14.229 3.802 -20.998 1.00 43.91 C
ANISOU 4357 C LYS A 523 5622 6662 4399 -739 195 -152 C
ATOM 4358 O LYS A 523 -13.343 2.997 -20.656 1.00 44.73 O
ANISOU 4358 O LYS A 523 5796 6670 4526 -789 169 -153 O
ATOM 4359 CB LYS A 523 -15.279 2.474 -22.878 1.00 42.35 C
ANISOU 4359 CB LYS A 523 5317 6623 4148 -794 183 -207 C
ATOM 4360 CG LYS A 523 -16.522 1.748 -23.375 1.00 42.32 C
ANISOU 4360 CG LYS A 523 5238 6753 4089 -859 196 -254 C
ATOM 4361 CD LYS A 523 -16.248 0.834 -24.544 1.00 41.19 C
ANISOU 4361 CD LYS A 523 5079 6629 3942 -896 177 -285 C
ATOM 4362 CE LYS A 523 -17.534 0.115 -24.921 1.00 43.78 C
ANISOU 4362 CE LYS A 523 5328 7097 4206 -976 196 -342 C
ATOM 4363 NZ LYS A 523 -17.420 -0.682 -26.164 1.00 42.40 N
ANISOU 4363 NZ LYS A 523 5123 6967 4018 -1015 185 -381 N
ATOM 4364 N TYR A 524 -14.113 5.118 -20.840 1.00 41.22 N
ANISOU 4364 N TYR A 524 5273 6315 4073 -655 217 -124 N
ATOM 4365 CA TYR A 524 -12.926 5.708 -20.242 1.00 41.66 C
ANISOU 4365 CA TYR A 524 5399 6257 4171 -628 213 -101 C
ATOM 4366 C TYR A 524 -12.773 5.201 -18.829 1.00 42.42 C
ANISOU 4366 C TYR A 524 5559 6293 4263 -705 208 -109 C
ATOM 4367 O TYR A 524 -13.763 5.081 -18.105 1.00 43.81 O
ANISOU 4367 O TYR A 524 5720 6520 4406 -747 231 -124 O
ATOM 4368 CB TYR A 524 -13.042 7.231 -20.221 1.00 41.61 C
ANISOU 4368 CB TYR A 524 5373 6260 4176 -535 255 -77 C
ATOM 4369 CG TYR A 524 -11.868 7.912 -19.569 1.00 40.66 C
ANISOU 4369 CG TYR A 524 5322 6031 4096 -517 259 -63 C
ATOM 4370 CD1 TYR A 524 -10.646 8.031 -20.242 1.00 39.67 C
ANISOU 4370 CD1 TYR A 524 5224 5838 4009 -484 236 -51 C
ATOM 4371 CD2 TYR A 524 -11.968 8.430 -18.286 1.00 40.48 C
ANISOU 4371 CD2 TYR A 524 5334 5976 4069 -539 288 -68 C
ATOM 4372 CE1 TYR A 524 -9.560 8.646 -19.649 1.00 39.93 C
ANISOU 4372 CE1 TYR A 524 5314 5782 4074 -475 241 -45 C
ATOM 4373 CE2 TYR A 524 -10.884 9.049 -17.677 1.00 40.97 C
ANISOU 4373 CE2 TYR A 524 5455 5950 4162 -533 293 -64 C
ATOM 4374 CZ TYR A 524 -9.683 9.157 -18.366 1.00 40.85 C
ANISOU 4374 CZ TYR A 524 5462 5875 4183 -502 270 -54 C
ATOM 4375 OH TYR A 524 -8.602 9.761 -17.772 1.00 41.13 O
ANISOU 4375 OH TYR A 524 5549 5834 4245 -502 277 -56 O
ATOM 4376 N ARG A 525 -11.543 4.898 -18.424 1.00 43.03 N
ANISOU 4376 N ARG A 525 5706 6271 4370 -722 179 -98 N
ATOM 4377 CA ARG A 525 -11.299 4.521 -17.025 1.00 43.00 C
ANISOU 4377 CA ARG A 525 5765 6215 4358 -784 175 -98 C
ATOM 4378 C ARG A 525 -10.464 5.596 -16.345 1.00 41.70 C
ANISOU 4378 C ARG A 525 5634 5994 4214 -746 184 -85 C
ATOM 4379 O ARG A 525 -10.928 6.280 -15.439 1.00 44.04 O
ANISOU 4379 O ARG A 525 5934 6304 4494 -752 218 -90 O
ATOM 4380 CB ARG A 525 -10.612 3.150 -16.897 1.00 43.80 C
ANISOU 4380 CB ARG A 525 5920 6255 4464 -845 136 -95 C
ATOM 4381 CG ARG A 525 -11.010 2.097 -17.921 1.00 48.69 C
ANISOU 4381 CG ARG A 525 6515 6907 5078 -874 127 -112 C
ATOM 4382 CD ARG A 525 -12.224 1.290 -17.511 1.00 52.70 C
ANISOU 4382 CD ARG A 525 7009 7468 5543 -954 149 -138 C
ATOM 4383 NE ARG A 525 -11.885 0.151 -16.654 1.00 59.67 N
ANISOU 4383 NE ARG A 525 7967 8281 6421 -1027 140 -132 N
ATOM 4384 CZ ARG A 525 -12.029 -1.135 -16.991 1.00 57.50 C
ANISOU 4384 CZ ARG A 525 7714 7989 6141 -1089 142 -148 C
ATOM 4385 NH1 ARG A 525 -12.496 -1.478 -18.185 1.00 53.88 N
ANISOU 4385 NH1 ARG A 525 7204 7586 5680 -1097 148 -178 N
ATOM 4386 NH2 ARG A 525 -11.703 -2.083 -16.119 1.00 56.18 N
ANISOU 4386 NH2 ARG A 525 7623 7751 5969 -1145 142 -133 N
ATOM 4387 N LYS A 526 -9.228 5.736 -16.803 1.00 40.95 N
ANISOU 4387 N LYS A 526 5564 5839 4154 -713 159 -72 N
ATOM 4388 CA LYS A 526 -8.295 6.713 -16.296 1.00 38.63 C
ANISOU 4388 CA LYS A 526 5301 5493 3882 -684 168 -66 C
ATOM 4389 C LYS A 526 -7.006 6.597 -17.091 1.00 36.88 C
ANISOU 4389 C LYS A 526 5095 5219 3698 -652 134 -56 C
ATOM 4390 O LYS A 526 -6.343 5.552 -17.063 1.00 34.85 O
ANISOU 4390 O LYS A 526 4867 4927 3444 -684 91 -48 O
ATOM 4391 CB LYS A 526 -8.001 6.476 -14.806 1.00 41.19 C
ANISOU 4391 CB LYS A 526 5677 5789 4185 -744 160 -69 C
ATOM 4392 CG LYS A 526 -6.926 7.401 -14.243 1.00 41.65 C
ANISOU 4392 CG LYS A 526 5764 5801 4259 -729 167 -72 C
ATOM 4393 CD LYS A 526 -6.590 7.078 -12.792 1.00 43.36 C
ANISOU 4393 CD LYS A 526 6025 6004 4443 -791 153 -74 C
ATOM 4394 CE LYS A 526 -5.457 7.960 -12.284 1.00 43.23 C
ANISOU 4394 CE LYS A 526 6031 5955 4437 -783 158 -85 C
ATOM 4395 NZ LYS A 526 -4.976 7.501 -10.951 1.00 46.45 N
ANISOU 4395 NZ LYS A 526 6478 6362 4808 -842 132 -83 N
ATOM 4396 N VAL A 527 -6.651 7.684 -17.776 1.00 35.50 N
ANISOU 4396 N VAL A 527 4902 5036 3551 -586 160 -54 N
ATOM 4397 CA VAL A 527 -5.416 7.771 -18.535 1.00 32.58 C
ANISOU 4397 CA VAL A 527 4543 4616 3216 -552 136 -47 C
ATOM 4398 C VAL A 527 -4.564 8.921 -17.989 1.00 31.78 C
ANISOU 4398 C VAL A 527 4469 4472 3135 -535 164 -55 C
ATOM 4399 O VAL A 527 -4.993 10.067 -18.009 1.00 33.55 O
ANISOU 4399 O VAL A 527 4681 4703 3363 -498 220 -59 O
ATOM 4400 CB VAL A 527 -5.692 8.027 -20.035 1.00 32.60 C
ANISOU 4400 CB VAL A 527 4501 4650 3236 -489 147 -38 C
ATOM 4401 CG1 VAL A 527 -4.377 8.244 -20.796 1.00 33.17 C
ANISOU 4401 CG1 VAL A 527 4586 4668 3346 -453 130 -33 C
ATOM 4402 CG2 VAL A 527 -6.468 6.864 -20.645 1.00 33.35 C
ANISOU 4402 CG2 VAL A 527 4565 4796 3309 -515 121 -40 C
ATOM 4403 N THR A 528 -3.353 8.625 -17.540 1.00 28.35 N
ANISOU 4403 N THR A 528 4068 3992 2709 -562 129 -58 N
ATOM 4404 CA THR A 528 -2.451 9.669 -17.150 1.00 29.73 C
ANISOU 4404 CA THR A 528 4263 4133 2900 -554 154 -74 C
ATOM 4405 C THR A 528 -1.455 9.984 -18.250 1.00 29.61 C
ANISOU 4405 C THR A 528 4241 4083 2923 -508 149 -72 C
ATOM 4406 O THR A 528 -1.183 9.158 -19.102 1.00 29.85 O
ANISOU 4406 O THR A 528 4261 4112 2967 -494 109 -58 O
ATOM 4407 CB THR A 528 -1.643 9.284 -15.931 1.00 29.55 C
ANISOU 4407 CB THR A 528 4273 4098 2856 -611 122 -83 C
ATOM 4408 OG1 THR A 528 -0.749 8.248 -16.311 1.00 29.11 O
ANISOU 4408 OG1 THR A 528 4224 4024 2810 -613 61 -66 O
ATOM 4409 CG2 THR A 528 -2.566 8.829 -14.767 1.00 29.48 C
ANISOU 4409 CG2 THR A 528 4276 4121 2803 -663 122 -82 C
ATOM 4410 N PHE A 529 -0.920 11.199 -18.210 1.00 29.37 N
ANISOU 4410 N PHE A 529 4220 4025 2912 -489 197 -90 N
ATOM 4411 CA PHE A 529 0.207 11.592 -19.036 1.00 29.87 C
ANISOU 4411 CA PHE A 529 4285 4051 3011 -458 197 -95 C
ATOM 4412 C PHE A 529 1.390 10.638 -18.832 1.00 31.00 C
ANISOU 4412 C PHE A 529 4438 4183 3155 -491 128 -96 C
ATOM 4413 O PHE A 529 2.056 10.238 -19.798 1.00 30.48 O
ANISOU 4413 O PHE A 529 4363 4103 3115 -464 99 -87 O
ATOM 4414 CB PHE A 529 0.634 13.024 -18.701 1.00 27.42 C
ANISOU 4414 CB PHE A 529 3995 3708 2716 -455 268 -124 C
ATOM 4415 CG PHE A 529 1.757 13.539 -19.565 1.00 26.65 C
ANISOU 4415 CG PHE A 529 3900 3570 2654 -427 280 -133 C
ATOM 4416 CD1 PHE A 529 1.508 13.988 -20.861 1.00 25.43 C
ANISOU 4416 CD1 PHE A 529 3732 3402 2526 -358 314 -112 C
ATOM 4417 CD2 PHE A 529 3.075 13.554 -19.093 1.00 26.25 C
ANISOU 4417 CD2 PHE A 529 3862 3502 2607 -470 258 -163 C
ATOM 4418 CE1 PHE A 529 2.539 14.469 -21.657 1.00 24.74 C
ANISOU 4418 CE1 PHE A 529 3651 3276 2472 -335 330 -121 C
ATOM 4419 CE2 PHE A 529 4.113 14.030 -19.897 1.00 26.19 C
ANISOU 4419 CE2 PHE A 529 3855 3462 2633 -449 273 -175 C
ATOM 4420 CZ PHE A 529 3.840 14.485 -21.179 1.00 24.86 C
ANISOU 4420 CZ PHE A 529 3680 3271 2494 -382 310 -154 C
ATOM 4421 N GLN A 530 1.643 10.294 -17.574 1.00 32.44 N
ANISOU 4421 N GLN A 530 4639 4378 3307 -546 104 -105 N
ATOM 4422 CA GLN A 530 2.710 9.363 -17.210 1.00 35.48 C
ANISOU 4422 CA GLN A 530 5033 4764 3685 -571 39 -99 C
ATOM 4423 C GLN A 530 2.558 8.014 -17.935 1.00 34.05 C
ANISOU 4423 C GLN A 530 4846 4579 3511 -554 -11 -66 C
ATOM 4424 O GLN A 530 3.529 7.497 -18.519 1.00 31.60 O
ANISOU 4424 O GLN A 530 4533 4251 3222 -536 -47 -58 O
ATOM 4425 CB GLN A 530 2.752 9.152 -15.686 1.00 37.60 C
ANISOU 4425 CB GLN A 530 5319 5059 3907 -628 24 -105 C
ATOM 4426 CG GLN A 530 3.191 10.376 -14.875 1.00 43.60 C
ANISOU 4426 CG GLN A 530 6085 5824 4654 -660 68 -148 C
ATOM 4427 CD GLN A 530 2.212 11.572 -14.937 1.00 45.84 C
ANISOU 4427 CD GLN A 530 6371 6096 4948 -649 150 -169 C
ATOM 4428 OE1 GLN A 530 0.982 11.412 -14.829 1.00 42.75 O
ANISOU 4428 OE1 GLN A 530 5978 5718 4544 -644 167 -153 O
ATOM 4429 NE2 GLN A 530 2.767 12.779 -15.097 1.00 45.90 N
ANISOU 4429 NE2 GLN A 530 6383 6078 4976 -646 207 -205 N
ATOM 4430 N CYS A 531 1.346 7.461 -17.919 1.00 32.16 N
ANISOU 4430 N CYS A 531 4605 4358 3254 -563 -7 -51 N
ATOM 4431 CA CYS A 531 1.106 6.174 -18.567 1.00 32.16 C
ANISOU 4431 CA CYS A 531 4604 4355 3259 -559 -44 -28 C
ATOM 4432 C CYS A 531 1.431 6.221 -20.084 1.00 30.93 C
ANISOU 4432 C CYS A 531 4425 4184 3142 -510 -44 -28 C
ATOM 4433 O CYS A 531 2.137 5.343 -20.617 1.00 29.33 O
ANISOU 4433 O CYS A 531 4227 3958 2956 -502 -81 -18 O
ATOM 4434 CB CYS A 531 -0.327 5.699 -18.327 1.00 33.86 C
ANISOU 4434 CB CYS A 531 4816 4600 3446 -585 -29 -23 C
ATOM 4435 SG CYS A 531 -0.683 4.070 -19.063 1.00 40.50 S
ANISOU 4435 SG CYS A 531 5662 5436 4291 -598 -62 -6 S
ATOM 4436 N LEU A 532 0.936 7.265 -20.755 1.00 29.20 N
ANISOU 4436 N LEU A 532 4181 3976 2934 -474 0 -38 N
ATOM 4437 CA LEU A 532 1.193 7.477 -22.153 1.00 27.22 C
ANISOU 4437 CA LEU A 532 3909 3720 2714 -425 7 -36 C
ATOM 4438 C LEU A 532 2.675 7.642 -22.442 1.00 27.68 C
ANISOU 4438 C LEU A 532 3976 3739 2802 -411 -10 -43 C
ATOM 4439 O LEU A 532 3.210 7.082 -23.423 1.00 27.50 O
ANISOU 4439 O LEU A 532 3944 3702 2801 -390 -35 -37 O
ATOM 4440 CB LEU A 532 0.420 8.692 -22.650 1.00 29.22 C
ANISOU 4440 CB LEU A 532 4140 3993 2968 -382 66 -37 C
ATOM 4441 CG LEU A 532 -1.102 8.538 -22.780 1.00 28.86 C
ANISOU 4441 CG LEU A 532 4067 4004 2894 -378 85 -28 C
ATOM 4442 CD1 LEU A 532 -1.764 9.894 -22.940 1.00 28.65 C
ANISOU 4442 CD1 LEU A 532 4024 3994 2866 -329 151 -24 C
ATOM 4443 CD2 LEU A 532 -1.462 7.610 -23.940 1.00 29.19 C
ANISOU 4443 CD2 LEU A 532 4079 4077 2934 -368 58 -21 C
ATOM 4444 N LYS A 533 3.363 8.391 -21.591 1.00 27.09 N
ANISOU 4444 N LYS A 533 3917 3650 2726 -428 3 -59 N
ATOM 4445 CA LYS A 533 4.771 8.619 -21.805 1.00 26.35 C
ANISOU 4445 CA LYS A 533 3824 3530 2655 -421 -10 -72 C
ATOM 4446 C LYS A 533 5.536 7.311 -21.779 1.00 25.68 C
ANISOU 4446 C LYS A 533 3744 3439 2572 -431 -74 -57 C
ATOM 4447 O LYS A 533 6.445 7.106 -22.583 1.00 24.29 O
ANISOU 4447 O LYS A 533 3560 3245 2425 -406 -92 -58 O
ATOM 4448 CB LYS A 533 5.303 9.553 -20.760 1.00 28.64 C
ANISOU 4448 CB LYS A 533 4127 3820 2934 -452 15 -99 C
ATOM 4449 CG LYS A 533 6.564 10.284 -21.159 1.00 31.37 C
ANISOU 4449 CG LYS A 533 4468 4143 3306 -443 31 -125 C
ATOM 4450 CD LYS A 533 6.556 11.682 -20.573 1.00 30.89 C
ANISOU 4450 CD LYS A 533 4419 4074 3241 -464 99 -160 C
ATOM 4451 CE LYS A 533 6.655 11.639 -19.053 1.00 33.01 C
ANISOU 4451 CE LYS A 533 4697 4373 3469 -524 86 -179 C
ATOM 4452 NZ LYS A 533 8.068 11.758 -18.598 1.00 34.41 N
ANISOU 4452 NZ LYS A 533 4867 4565 3640 -558 65 -210 N
ATOM 4453 N SER A 534 5.149 6.419 -20.871 1.00 25.92 N
ANISOU 4453 N SER A 534 3792 3483 2574 -463 -103 -41 N
ATOM 4454 CA SER A 534 5.783 5.089 -20.754 1.00 27.18 C
ANISOU 4454 CA SER A 534 3963 3629 2732 -467 -156 -18 C
ATOM 4455 C SER A 534 5.550 4.193 -21.959 1.00 27.58 C
ANISOU 4455 C SER A 534 4010 3660 2807 -444 -167 -6 C
ATOM 4456 O SER A 534 6.446 3.483 -22.379 1.00 29.26 O
ANISOU 4456 O SER A 534 4226 3850 3040 -426 -197 3 O
ATOM 4457 CB SER A 534 5.286 4.350 -19.510 1.00 26.81 C
ANISOU 4457 CB SER A 534 3943 3597 2645 -506 -174 2 C
ATOM 4458 OG SER A 534 5.731 4.996 -18.361 1.00 28.85 O
ANISOU 4458 OG SER A 534 4205 3881 2877 -530 -173 -9 O
ATOM 4459 N ILE A 535 4.318 4.167 -22.455 1.00 28.28 N
ANISOU 4459 N ILE A 535 4090 3763 2889 -447 -142 -7 N
ATOM 4460 CA ILE A 535 3.977 3.416 -23.670 1.00 27.70 C
ANISOU 4460 CA ILE A 535 4006 3685 2834 -433 -146 -6 C
ATOM 4461 C ILE A 535 4.859 3.886 -24.852 1.00 28.26 C
ANISOU 4461 C ILE A 535 4056 3740 2940 -389 -144 -16 C
ATOM 4462 O ILE A 535 5.447 3.056 -25.591 1.00 27.65 O
ANISOU 4462 O ILE A 535 3981 3639 2885 -377 -165 -14 O
ATOM 4463 CB ILE A 535 2.456 3.546 -23.951 1.00 27.42 C
ANISOU 4463 CB ILE A 535 3952 3691 2776 -445 -116 -12 C
ATOM 4464 CG1 ILE A 535 1.676 2.800 -22.852 1.00 27.37 C
ANISOU 4464 CG1 ILE A 535 3970 3693 2736 -496 -120 -4 C
ATOM 4465 CG2 ILE A 535 2.084 3.054 -25.343 1.00 27.69 C
ANISOU 4465 CG2 ILE A 535 3961 3737 2820 -430 -113 -20 C
ATOM 4466 CD1 ILE A 535 0.169 2.831 -23.006 1.00 27.78 C
ANISOU 4466 CD1 ILE A 535 3999 3794 2760 -516 -92 -13 C
ATOM 4467 N ALA A 536 5.031 5.208 -24.953 1.00 26.10 N
ANISOU 4467 N ALA A 536 3767 3474 2673 -367 -113 -28 N
ATOM 4468 CA ALA A 536 5.876 5.819 -25.979 1.00 26.11 C
ANISOU 4468 CA ALA A 536 3753 3460 2706 -328 -102 -38 C
ATOM 4469 C ALA A 536 7.348 5.390 -25.846 1.00 26.13 C
ANISOU 4469 C ALA A 536 3763 3433 2729 -327 -138 -41 C
ATOM 4470 O ALA A 536 7.963 4.987 -26.827 1.00 24.23 O
ANISOU 4470 O ALA A 536 3514 3177 2516 -303 -150 -43 O
ATOM 4471 CB ALA A 536 5.758 7.352 -25.934 1.00 24.70 C
ANISOU 4471 CB ALA A 536 3568 3287 2529 -310 -51 -49 C
ATOM 4472 N TRP A 537 7.907 5.486 -24.635 1.00 25.90 N
ANISOU 4472 N TRP A 537 3747 3406 2686 -351 -153 -42 N
ATOM 4473 CA TRP A 537 9.289 5.044 -24.411 1.00 26.90 C
ANISOU 4473 CA TRP A 537 3872 3522 2824 -346 -190 -42 C
ATOM 4474 C TRP A 537 9.445 3.587 -24.782 1.00 28.79 C
ANISOU 4474 C TRP A 537 4123 3741 3074 -335 -226 -18 C
ATOM 4475 O TRP A 537 10.497 3.163 -25.320 1.00 28.21 O
ANISOU 4475 O TRP A 537 4041 3650 3025 -310 -247 -17 O
ATOM 4476 CB TRP A 537 9.725 5.276 -22.962 1.00 25.60 C
ANISOU 4476 CB TRP A 537 3714 3381 2628 -377 -204 -44 C
ATOM 4477 CG TRP A 537 10.125 6.707 -22.687 1.00 24.64 C
ANISOU 4477 CG TRP A 537 3582 3274 2506 -391 -167 -80 C
ATOM 4478 CD1 TRP A 537 9.568 7.587 -21.745 1.00 24.16 C
ANISOU 4478 CD1 TRP A 537 3529 3232 2417 -424 -133 -96 C
ATOM 4479 CD2 TRP A 537 11.186 7.461 -23.342 1.00 23.32 C
ANISOU 4479 CD2 TRP A 537 3395 3099 2366 -376 -150 -108 C
ATOM 4480 NE1 TRP A 537 10.194 8.823 -21.800 1.00 24.36 N
ANISOU 4480 NE1 TRP A 537 3545 3256 2453 -433 -92 -135 N
ATOM 4481 CE2 TRP A 537 11.170 8.814 -22.740 1.00 24.08 C
ANISOU 4481 CE2 TRP A 537 3493 3205 2450 -407 -99 -144 C
ATOM 4482 CE3 TRP A 537 12.094 7.183 -24.359 1.00 22.88 C
ANISOU 4482 CE3 TRP A 537 3323 3027 2344 -345 -164 -111 C
ATOM 4483 CZ2 TRP A 537 12.053 9.805 -23.139 1.00 23.50 C
ANISOU 4483 CZ2 TRP A 537 3408 3123 2397 -410 -63 -181 C
ATOM 4484 CZ3 TRP A 537 12.968 8.191 -24.770 1.00 22.46 C
ANISOU 4484 CZ3 TRP A 537 3254 2970 2310 -346 -132 -146 C
ATOM 4485 CH2 TRP A 537 12.952 9.478 -24.166 1.00 23.83 C
ANISOU 4485 CH2 TRP A 537 3432 3150 2471 -379 -81 -181 C
ATOM 4486 N ARG A 538 8.400 2.809 -24.520 1.00 28.59 N
ANISOU 4486 N ARG A 538 4118 3714 3030 -355 -227 -1 N
ATOM 4487 CA ARG A 538 8.471 1.380 -24.782 1.00 31.71 C
ANISOU 4487 CA ARG A 538 4534 4080 3434 -352 -249 18 C
ATOM 4488 C ARG A 538 8.500 1.150 -26.274 1.00 30.17 C
ANISOU 4488 C ARG A 538 4323 3867 3270 -330 -239 4 C
ATOM 4489 O ARG A 538 9.108 0.209 -26.740 1.00 30.72 O
ANISOU 4489 O ARG A 538 4403 3905 3362 -315 -254 11 O
ATOM 4490 CB ARG A 538 7.311 0.614 -24.115 1.00 31.86 C
ANISOU 4490 CB ARG A 538 4582 4100 3424 -390 -244 34 C
ATOM 4491 CG ARG A 538 7.524 0.407 -22.622 1.00 34.97 C
ANISOU 4491 CG ARG A 538 5000 4502 3786 -408 -263 59 C
ATOM 4492 CD ARG A 538 6.610 -0.673 -22.114 1.00 38.89 C
ANISOU 4492 CD ARG A 538 5533 4981 4259 -441 -258 80 C
ATOM 4493 NE ARG A 538 6.673 -0.904 -20.664 1.00 42.46 N
ANISOU 4493 NE ARG A 538 6012 5445 4674 -459 -272 108 N
ATOM 4494 CZ ARG A 538 7.100 -2.039 -20.102 1.00 42.74 C
ANISOU 4494 CZ ARG A 538 6085 5451 4701 -451 -290 148 C
ATOM 4495 NH1 ARG A 538 7.578 -3.024 -20.860 1.00 43.43 N
ANISOU 4495 NH1 ARG A 538 6190 5489 4821 -425 -292 161 N
ATOM 4496 NH2 ARG A 538 7.065 -2.188 -18.786 1.00 39.27 N
ANISOU 4496 NH2 ARG A 538 5669 5031 4221 -467 -301 177 N
ATOM 4497 N ALA A 539 7.835 2.030 -27.018 1.00 29.92 N
ANISOU 4497 N ALA A 539 4267 3861 3239 -325 -209 -14 N
ATOM 4498 CA ALA A 539 7.704 1.856 -28.459 1.00 27.53 C
ANISOU 4498 CA ALA A 539 3946 3557 2956 -306 -197 -28 C
ATOM 4499 C ALA A 539 9.045 2.154 -29.101 1.00 28.15 C
ANISOU 4499 C ALA A 539 4012 3614 3068 -271 -206 -36 C
ATOM 4500 O ALA A 539 9.442 1.480 -30.056 1.00 30.53 O
ANISOU 4500 O ALA A 539 4310 3895 3392 -257 -212 -42 O
ATOM 4501 CB ALA A 539 6.618 2.751 -29.011 1.00 24.71 C
ANISOU 4501 CB ALA A 539 3562 3242 2581 -301 -164 -38 C
ATOM 4502 N PHE A 540 9.751 3.145 -28.553 1.00 27.22 N
ANISOU 4502 N PHE A 540 3887 3501 2952 -263 -203 -41 N
ATOM 4503 CA PHE A 540 11.070 3.502 -29.013 1.00 27.94 C
ANISOU 4503 CA PHE A 540 3963 3579 3072 -237 -209 -53 C
ATOM 4504 C PHE A 540 12.061 2.400 -28.682 1.00 30.29 C
ANISOU 4504 C PHE A 540 4270 3855 3382 -229 -248 -41 C
ATOM 4505 O PHE A 540 12.855 2.008 -29.530 1.00 32.30 O
ANISOU 4505 O PHE A 540 4514 4090 3665 -204 -256 -47 O
ATOM 4506 CB PHE A 540 11.512 4.855 -28.431 1.00 26.43 C
ANISOU 4506 CB PHE A 540 3763 3403 2876 -242 -188 -70 C
ATOM 4507 CG PHE A 540 11.117 6.036 -29.283 1.00 26.53 C
ANISOU 4507 CG PHE A 540 3764 3419 2895 -225 -139 -83 C
ATOM 4508 CD1 PHE A 540 11.909 6.437 -30.353 1.00 26.48 C
ANISOU 4508 CD1 PHE A 540 3743 3399 2918 -199 -123 -98 C
ATOM 4509 CD2 PHE A 540 9.930 6.715 -29.054 1.00 27.36 C
ANISOU 4509 CD2 PHE A 540 3874 3542 2979 -231 -104 -78 C
ATOM 4510 CE1 PHE A 540 11.530 7.511 -31.169 1.00 27.32 C
ANISOU 4510 CE1 PHE A 540 3844 3506 3029 -176 -73 -102 C
ATOM 4511 CE2 PHE A 540 9.542 7.793 -29.865 1.00 27.61 C
ANISOU 4511 CE2 PHE A 540 3898 3576 3016 -202 -53 -81 C
ATOM 4512 CZ PHE A 540 10.344 8.188 -30.923 1.00 27.06 C
ANISOU 4512 CZ PHE A 540 3817 3489 2972 -174 -37 -91 C
ATOM 4513 N LEU A 541 11.998 1.885 -27.453 1.00 32.01 N
ANISOU 4513 N LEU A 541 4508 4078 3576 -247 -271 -19 N
ATOM 4514 CA LEU A 541 12.832 0.763 -27.053 1.00 31.26 C
ANISOU 4514 CA LEU A 541 4425 3964 3487 -230 -305 4 C
ATOM 4515 C LEU A 541 12.683 -0.459 -27.948 1.00 32.77 C
ANISOU 4515 C LEU A 541 4635 4111 3703 -216 -303 12 C
ATOM 4516 O LEU A 541 13.653 -1.153 -28.221 1.00 35.86 O
ANISOU 4516 O LEU A 541 5028 4479 4119 -185 -318 22 O
ATOM 4517 CB LEU A 541 12.525 0.361 -25.627 1.00 33.32 C
ANISOU 4517 CB LEU A 541 4710 4237 3711 -250 -322 33 C
ATOM 4518 CG LEU A 541 13.077 1.257 -24.532 1.00 32.98 C
ANISOU 4518 CG LEU A 541 4649 4241 3640 -262 -334 27 C
ATOM 4519 CD1 LEU A 541 12.669 0.648 -23.227 1.00 34.14 C
ANISOU 4519 CD1 LEU A 541 4823 4399 3747 -281 -352 61 C
ATOM 4520 CD2 LEU A 541 14.603 1.393 -24.626 1.00 33.90 C
ANISOU 4520 CD2 LEU A 541 4733 4375 3770 -232 -357 19 C
ATOM 4521 N ALA A 542 11.471 -0.754 -28.382 1.00 31.36 N
ANISOU 4521 N ALA A 542 4471 3926 3518 -242 -280 6 N
ATOM 4522 CA ALA A 542 11.270 -1.971 -29.125 1.00 30.42 C
ANISOU 4522 CA ALA A 542 4373 3767 3416 -243 -272 7 C
ATOM 4523 C ALA A 542 11.932 -1.867 -30.523 1.00 29.49 C
ANISOU 4523 C ALA A 542 4231 3639 3334 -215 -264 -17 C
ATOM 4524 O ALA A 542 12.257 -2.870 -31.142 1.00 27.01 O
ANISOU 4524 O ALA A 542 3932 3285 3043 -206 -260 -19 O
ATOM 4525 CB ALA A 542 9.784 -2.295 -29.224 1.00 29.04 C
ANISOU 4525 CB ALA A 542 4213 3601 3219 -287 -248 -1 C
ATOM 4526 N VAL A 543 12.147 -0.641 -30.988 1.00 29.63 N
ANISOU 4526 N VAL A 543 4213 3689 3354 -204 -258 -37 N
ATOM 4527 CA VAL A 543 12.728 -0.411 -32.307 1.00 29.92 C
ANISOU 4527 CA VAL A 543 4226 3722 3419 -179 -247 -60 C
ATOM 4528 C VAL A 543 14.226 -0.247 -32.182 1.00 30.52 C
ANISOU 4528 C VAL A 543 4288 3787 3519 -146 -266 -59 C
ATOM 4529 O VAL A 543 14.979 -0.821 -32.942 1.00 31.58 O
ANISOU 4529 O VAL A 543 4418 3897 3683 -123 -268 -66 O
ATOM 4530 CB VAL A 543 12.150 0.861 -32.961 1.00 31.22 C
ANISOU 4530 CB VAL A 543 4364 3926 3572 -179 -221 -77 C
ATOM 4531 CG1 VAL A 543 13.021 1.312 -34.118 1.00 31.43 C
ANISOU 4531 CG1 VAL A 543 4367 3949 3626 -150 -211 -96 C
ATOM 4532 CG2 VAL A 543 10.726 0.629 -33.424 1.00 30.37 C
ANISOU 4532 CG2 VAL A 543 4255 3843 3438 -204 -202 -82 C
ATOM 4533 N LEU A 544 14.653 0.549 -31.212 1.00 30.52 N
ANISOU 4533 N LEU A 544 4278 3812 3505 -148 -278 -54 N
ATOM 4534 CA LEU A 544 16.057 0.805 -31.016 1.00 30.22 C
ANISOU 4534 CA LEU A 544 4216 3782 3482 -123 -296 -59 C
ATOM 4535 C LEU A 544 16.817 -0.491 -30.749 1.00 33.83 C
ANISOU 4535 C LEU A 544 4685 4214 3953 -95 -323 -33 C
ATOM 4536 O LEU A 544 18.005 -0.614 -31.126 1.00 33.06 O
ANISOU 4536 O LEU A 544 4564 4117 3880 -62 -334 -40 O
ATOM 4537 CB LEU A 544 16.265 1.791 -29.864 1.00 28.10 C
ANISOU 4537 CB LEU A 544 3936 3554 3187 -142 -301 -62 C
ATOM 4538 CG LEU A 544 15.767 3.236 -30.058 1.00 27.75 C
ANISOU 4538 CG LEU A 544 3882 3527 3134 -164 -263 -88 C
ATOM 4539 CD1 LEU A 544 15.826 4.006 -28.734 1.00 25.05 C
ANISOU 4539 CD1 LEU A 544 3536 3219 2760 -193 -264 -93 C
ATOM 4540 CD2 LEU A 544 16.554 3.950 -31.154 1.00 24.82 C
ANISOU 4540 CD2 LEU A 544 3487 3152 2792 -147 -240 -117 C
ATOM 4541 N LYS A 545 16.144 -1.450 -30.097 1.00 34.65 N
ANISOU 4541 N LYS A 545 4826 4297 4042 -104 -330 -3 N
ATOM 4542 CA LYS A 545 16.773 -2.737 -29.725 1.00 37.26 C
ANISOU 4542 CA LYS A 545 5178 4594 4382 -70 -347 31 C
ATOM 4543 C LYS A 545 17.201 -3.518 -30.955 1.00 37.72 C
ANISOU 4543 C LYS A 545 5242 4607 4484 -44 -332 19 C
ATOM 4544 O LYS A 545 18.072 -4.392 -30.875 1.00 37.03 O
ANISOU 4544 O LYS A 545 5161 4493 4415 0 -341 43 O
ATOM 4545 CB LYS A 545 15.815 -3.601 -28.901 1.00 37.60 C
ANISOU 4545 CB LYS A 545 5270 4612 4402 -91 -344 64 C
ATOM 4546 CG LYS A 545 15.986 -3.476 -27.400 1.00 40.98 C
ANISOU 4546 CG LYS A 545 5702 5076 4792 -90 -371 99 C
ATOM 4547 CD LYS A 545 14.734 -3.989 -26.720 1.00 43.47 C
ANISOU 4547 CD LYS A 545 6063 5372 5080 -127 -357 120 C
ATOM 4548 CE LYS A 545 15.075 -4.765 -25.477 1.00 47.91 C
ANISOU 4548 CE LYS A 545 6654 5933 5617 -104 -377 175 C
ATOM 4549 NZ LYS A 545 13.934 -5.627 -25.063 1.00 53.43 N
ANISOU 4549 NZ LYS A 545 7412 6589 6301 -137 -352 197 N
ATOM 4550 N ARG A 546 16.553 -3.222 -32.084 1.00 35.92 N
ANISOU 4550 N ARG A 546 5009 4372 4266 -68 -305 -15 N
ATOM 4551 CA ARG A 546 16.886 -3.857 -33.359 1.00 34.88 C
ANISOU 4551 CA ARG A 546 4878 4203 4170 -52 -286 -35 C
ATOM 4552 C ARG A 546 18.295 -3.520 -33.835 1.00 34.32 C
ANISOU 4552 C ARG A 546 4770 4142 4128 -10 -297 -47 C
ATOM 4553 O ARG A 546 18.801 -4.169 -34.749 1.00 33.55 O
ANISOU 4553 O ARG A 546 4674 4011 4062 11 -284 -60 O
ATOM 4554 CB ARG A 546 15.861 -3.512 -34.429 1.00 31.27 C
ANISOU 4554 CB ARG A 546 4416 3756 3707 -88 -257 -70 C
ATOM 4555 CG ARG A 546 14.531 -4.181 -34.208 1.00 32.06 C
ANISOU 4555 CG ARG A 546 4552 3845 3785 -132 -240 -67 C
ATOM 4556 CD ARG A 546 13.671 -4.102 -35.463 1.00 32.42 C
ANISOU 4556 CD ARG A 546 4584 3908 3824 -162 -212 -104 C
ATOM 4557 NE ARG A 546 14.216 -4.898 -36.556 1.00 28.87 N
ANISOU 4557 NE ARG A 546 4138 3422 3405 -152 -194 -128 N
ATOM 4558 CZ ARG A 546 13.593 -5.093 -37.713 1.00 29.81 C
ANISOU 4558 CZ ARG A 546 4248 3558 3519 -181 -168 -164 C
ATOM 4559 NH1 ARG A 546 12.385 -4.560 -37.930 1.00 28.35 N
ANISOU 4559 NH1 ARG A 546 4045 3430 3295 -216 -159 -178 N
ATOM 4560 NH2 ARG A 546 14.161 -5.850 -38.643 1.00 28.45 N
ANISOU 4560 NH2 ARG A 546 4084 3350 3377 -174 -149 -188 N
ATOM 4561 N ARG A 547 18.908 -2.499 -33.229 1.00 33.19 N
ANISOU 4561 N ARG A 547 4592 4047 3971 -4 -317 -49 N
ATOM 4562 CA ARG A 547 20.335 -2.185 -33.456 1.00 35.59 C
ANISOU 4562 CA ARG A 547 4854 4371 4294 31 -331 -60 C
ATOM 4563 C ARG A 547 21.032 -1.991 -32.125 1.00 36.62 C
ANISOU 4563 C ARG A 547 4965 4547 4401 45 -364 -37 C
ATOM 4564 O ARG A 547 21.486 -0.869 -31.807 1.00 34.64 O
ANISOU 4564 O ARG A 547 4678 4348 4135 29 -370 -60 O
ATOM 4565 CB ARG A 547 20.512 -0.902 -34.282 1.00 36.16 C
ANISOU 4565 CB ARG A 547 4893 4471 4372 14 -311 -102 C
ATOM 4566 CG ARG A 547 19.816 -0.874 -35.638 1.00 37.61 C
ANISOU 4566 CG ARG A 547 5087 4631 4570 1 -279 -126 C
ATOM 4567 CD ARG A 547 20.297 0.333 -36.457 1.00 38.52 C
ANISOU 4567 CD ARG A 547 5170 4770 4693 -1 -258 -159 C
ATOM 4568 NE ARG A 547 19.287 0.817 -37.399 1.00 38.18 N
ANISOU 4568 NE ARG A 547 5136 4729 4642 -19 -226 -172 N
ATOM 4569 CZ ARG A 547 19.135 0.361 -38.643 1.00 40.34 C
ANISOU 4569 CZ ARG A 547 5410 4988 4929 -14 -209 -187 C
ATOM 4570 NH1 ARG A 547 19.933 -0.598 -39.109 1.00 41.10 N
ANISOU 4570 NH1 ARG A 547 5504 5054 5054 7 -215 -195 N
ATOM 4571 NH2 ARG A 547 18.185 0.865 -39.430 1.00 38.19 N
ANISOU 4571 NH2 ARG A 547 5138 4734 4637 -28 -183 -195 N
ATOM 4572 N THR A 548 21.102 -3.065 -31.335 1.00 38.52 N
ANISOU 4572 N THR A 548 5232 4770 4634 73 -382 7 N
ATOM 4573 CA THR A 548 21.593 -2.982 -29.946 1.00 43.09 C
ANISOU 4573 CA THR A 548 5794 5402 5176 87 -417 39 C
ATOM 4574 C THR A 548 23.015 -2.429 -29.873 1.00 44.82 C
ANISOU 4574 C THR A 548 5950 5684 5395 113 -439 21 C
ATOM 4575 O THR A 548 23.342 -1.703 -28.945 1.00 50.95 O
ANISOU 4575 O THR A 548 6693 6529 6134 96 -460 16 O
ATOM 4576 CB THR A 548 21.528 -4.346 -29.189 1.00 44.04 C
ANISOU 4576 CB THR A 548 5955 5489 5288 126 -427 100 C
ATOM 4577 OG1 THR A 548 21.752 -5.422 -30.109 1.00 48.29 O
ANISOU 4577 OG1 THR A 548 6520 5958 5870 164 -405 108 O
ATOM 4578 CG2 THR A 548 20.173 -4.558 -28.523 1.00 41.51 C
ANISOU 4578 CG2 THR A 548 5686 5144 4939 84 -417 120 C
ATOM 4579 N GLU A 549 23.848 -2.762 -30.853 1.00 45.14 N
ANISOU 4579 N GLU A 549 5969 5706 5474 150 -431 7 N
ATOM 4580 CA GLU A 549 25.238 -2.250 -30.909 1.00 48.69 C
ANISOU 4580 CA GLU A 549 6352 6219 5926 173 -448 -16 C
ATOM 4581 C GLU A 549 25.307 -0.732 -31.122 1.00 45.19 C
ANISOU 4581 C GLU A 549 5875 5820 5473 116 -433 -74 C
ATOM 4582 O GLU A 549 26.048 -0.039 -30.447 1.00 49.65 O
ANISOU 4582 O GLU A 549 6392 6461 6011 103 -450 -92 O
ATOM 4583 CB GLU A 549 26.059 -2.986 -31.994 1.00 52.06 C
ANISOU 4583 CB GLU A 549 6767 6610 6400 225 -437 -20 C
ATOM 4584 CG GLU A 549 25.640 -2.703 -33.447 1.00 58.62 C
ANISOU 4584 CG GLU A 549 7615 7388 7270 198 -398 -64 C
ATOM 4585 CD GLU A 549 24.207 -3.148 -33.786 1.00 58.17 C
ANISOU 4585 CD GLU A 549 7621 7263 7216 168 -373 -54 C
ATOM 4586 OE1 GLU A 549 23.748 -4.175 -33.242 1.00 62.66 O
ANISOU 4586 OE1 GLU A 549 8233 7795 7780 186 -376 -12 O
ATOM 4587 OE2 GLU A 549 23.546 -2.484 -34.617 1.00 53.80 O
ANISOU 4587 OE2 GLU A 549 7075 6696 6668 128 -346 -89 O
ATOM 4588 N ILE A 550 24.530 -0.226 -32.061 1.00 41.11 N
ANISOU 4588 N ILE A 550 5384 5258 4977 82 -397 -102 N
ATOM 4589 CA ILE A 550 24.469 1.212 -32.303 1.00 39.63 C
ANISOU 4589 CA ILE A 550 5177 5096 4782 33 -370 -150 C
ATOM 4590 C ILE A 550 23.773 1.956 -31.147 1.00 39.48 C
ANISOU 4590 C ILE A 550 5170 5110 4721 -12 -372 -148 C
ATOM 4591 O ILE A 550 24.249 2.976 -30.682 1.00 38.79 O
ANISOU 4591 O ILE A 550 5052 5073 4614 -45 -365 -182 O
ATOM 4592 CB ILE A 550 23.786 1.507 -33.665 1.00 37.85 C
ANISOU 4592 CB ILE A 550 4977 4817 4585 20 -329 -171 C
ATOM 4593 CG1 ILE A 550 24.813 1.343 -34.809 1.00 38.76 C
ANISOU 4593 CG1 ILE A 550 5064 4923 4738 48 -319 -196 C
ATOM 4594 CG2 ILE A 550 23.211 2.901 -33.688 1.00 37.18 C
ANISOU 4594 CG2 ILE A 550 4897 4743 4485 -26 -294 -200 C
ATOM 4595 CD1 ILE A 550 24.264 0.753 -36.098 1.00 34.85 C
ANISOU 4595 CD1 ILE A 550 4598 4371 4272 61 -296 -196 C
ATOM 4596 N TYR A 551 22.670 1.404 -30.657 1.00 38.51 N
ANISOU 4596 N TYR A 551 5091 4958 4582 -16 -378 -112 N
ATOM 4597 CA TYR A 551 21.795 2.137 -29.757 1.00 36.18 C
ANISOU 4597 CA TYR A 551 4813 4682 4251 -61 -370 -114 C
ATOM 4598 C TYR A 551 21.938 1.748 -28.260 1.00 36.99 C
ANISOU 4598 C TYR A 551 4911 4832 4310 -61 -409 -83 C
ATOM 4599 O TYR A 551 21.202 2.254 -27.402 1.00 36.07 O
ANISOU 4599 O TYR A 551 4810 4734 4160 -100 -404 -82 O
ATOM 4600 CB TYR A 551 20.362 1.949 -30.217 1.00 33.41 C
ANISOU 4600 CB TYR A 551 4509 4279 3905 -74 -347 -100 C
ATOM 4601 CG TYR A 551 19.992 2.664 -31.502 1.00 30.82 C
ANISOU 4601 CG TYR A 551 4183 3924 3602 -83 -305 -130 C
ATOM 4602 CD1 TYR A 551 20.291 4.021 -31.695 1.00 30.86 C
ANISOU 4602 CD1 TYR A 551 4168 3948 3606 -106 -272 -167 C
ATOM 4603 CD2 TYR A 551 19.253 2.019 -32.470 1.00 28.79 C
ANISOU 4603 CD2 TYR A 551 3949 3625 3362 -71 -292 -121 C
ATOM 4604 CE1 TYR A 551 19.912 4.679 -32.859 1.00 29.21 C
ANISOU 4604 CE1 TYR A 551 3966 3714 3416 -106 -229 -185 C
ATOM 4605 CE2 TYR A 551 18.861 2.664 -33.611 1.00 29.21 C
ANISOU 4605 CE2 TYR A 551 4001 3666 3429 -75 -256 -142 C
ATOM 4606 CZ TYR A 551 19.188 3.996 -33.802 1.00 30.16 C
ANISOU 4606 CZ TYR A 551 4106 3804 3550 -87 -225 -170 C
ATOM 4607 OH TYR A 551 18.759 4.624 -34.951 1.00 31.29 O
ANISOU 4607 OH TYR A 551 4251 3935 3702 -83 -185 -182 O
ATOM 4608 N LYS A 552 22.885 0.855 -27.981 1.00 37.82 N
ANISOU 4608 N LYS A 552 4994 4961 4414 -14 -444 -55 N
ATOM 4609 CA LYS A 552 23.264 0.436 -26.633 1.00 41.02 C
ANISOU 4609 CA LYS A 552 5384 5426 4774 0 -484 -20 C
ATOM 4610 C LYS A 552 23.154 1.525 -25.568 1.00 37.78 C
ANISOU 4610 C LYS A 552 4954 5085 4315 -58 -485 -47 C
ATOM 4611 O LYS A 552 22.405 1.383 -24.592 1.00 37.54 O
ANISOU 4611 O LYS A 552 4951 5064 4247 -76 -494 -21 O
ATOM 4612 CB LYS A 552 24.706 -0.095 -26.658 1.00 46.40 C
ANISOU 4612 CB LYS A 552 6014 6155 5459 56 -514 -8 C
ATOM 4613 CG LYS A 552 25.230 -0.591 -25.315 1.00 53.36 C
ANISOU 4613 CG LYS A 552 6871 7114 6287 85 -559 35 C
ATOM 4614 CD LYS A 552 25.221 -2.109 -25.229 1.00 57.65 C
ANISOU 4614 CD LYS A 552 7450 7611 6841 161 -574 109 C
ATOM 4615 CE LYS A 552 25.826 -2.588 -23.913 1.00 63.10 C
ANISOU 4615 CE LYS A 552 8112 8387 7473 202 -618 162 C
ATOM 4616 NZ LYS A 552 24.992 -2.201 -22.734 1.00 62.62 N
ANISOU 4616 NZ LYS A 552 8074 8360 7357 151 -626 172 N
ATOM 4617 N GLY A 553 23.921 2.593 -25.744 1.00 35.52 N
ANISOU 4617 N GLY A 553 4620 4847 4027 -89 -470 -104 N
ATOM 4618 CA GLY A 553 23.978 3.673 -24.764 1.00 34.65 C
ANISOU 4618 CA GLY A 553 4487 4806 3871 -151 -463 -143 C
ATOM 4619 C GLY A 553 22.632 4.359 -24.600 1.00 34.16 C
ANISOU 4619 C GLY A 553 4475 4698 3804 -200 -424 -154 C
ATOM 4620 O GLY A 553 22.271 4.772 -23.502 1.00 35.20 O
ANISOU 4620 O GLY A 553 4609 4871 3891 -241 -426 -159 O
ATOM 4621 N LEU A 554 21.895 4.480 -25.703 1.00 32.39 N
ANISOU 4621 N LEU A 554 4287 4394 3624 -195 -388 -157 N
ATOM 4622 CA LEU A 554 20.624 5.187 -25.708 1.00 31.40 C
ANISOU 4622 CA LEU A 554 4203 4229 3497 -232 -346 -166 C
ATOM 4623 C LEU A 554 19.558 4.380 -24.952 1.00 31.96 C
ANISOU 4623 C LEU A 554 4313 4286 3544 -227 -367 -117 C
ATOM 4624 O LEU A 554 18.895 4.899 -24.069 1.00 30.96 O
ANISOU 4624 O LEU A 554 4201 4178 3384 -267 -355 -122 O
ATOM 4625 CB LEU A 554 20.196 5.460 -27.140 1.00 29.77 C
ANISOU 4625 CB LEU A 554 4016 3957 3338 -217 -306 -177 C
ATOM 4626 CG LEU A 554 18.943 6.291 -27.415 1.00 30.38 C
ANISOU 4626 CG LEU A 554 4128 3997 3418 -241 -255 -185 C
ATOM 4627 CD1 LEU A 554 18.954 7.588 -26.608 1.00 29.92 C
ANISOU 4627 CD1 LEU A 554 4065 3967 3333 -293 -218 -225 C
ATOM 4628 CD2 LEU A 554 18.851 6.581 -28.915 1.00 28.46 C
ANISOU 4628 CD2 LEU A 554 3889 3708 3215 -218 -219 -196 C
ATOM 4629 N ILE A 555 19.447 3.095 -25.293 1.00 33.19 N
ANISOU 4629 N ILE A 555 4487 4407 3716 -182 -394 -71 N
ATOM 4630 CA ILE A 555 18.622 2.139 -24.570 1.00 34.35 C
ANISOU 4630 CA ILE A 555 4673 4539 3840 -175 -414 -22 C
ATOM 4631 C ILE A 555 18.900 2.146 -23.067 1.00 35.77 C
ANISOU 4631 C ILE A 555 4840 4786 3964 -191 -444 -6 C
ATOM 4632 O ILE A 555 17.967 2.193 -22.271 1.00 39.71 O
ANISOU 4632 O ILE A 555 5367 5287 4431 -221 -439 7 O
ATOM 4633 CB ILE A 555 18.813 0.705 -25.122 1.00 33.96 C
ANISOU 4633 CB ILE A 555 4642 4443 3818 -122 -433 20 C
ATOM 4634 CG1 ILE A 555 18.422 0.642 -26.602 1.00 32.00 C
ANISOU 4634 CG1 ILE A 555 4406 4133 3617 -113 -403 1 C
ATOM 4635 CG2 ILE A 555 18.016 -0.303 -24.306 1.00 31.56 C
ANISOU 4635 CG2 ILE A 555 4384 4118 3488 -119 -446 72 C
ATOM 4636 CD1 ILE A 555 18.917 -0.612 -27.301 1.00 32.11 C
ANISOU 4636 CD1 ILE A 555 4431 4104 3665 -63 -413 26 C
ATOM 4637 N ASP A 556 20.175 2.105 -22.680 1.00 37.03 N
ANISOU 4637 N ASP A 556 4953 5010 4106 -172 -475 -8 N
ATOM 4638 CA ASP A 556 20.548 2.149 -21.266 1.00 36.95 C
ANISOU 4638 CA ASP A 556 4920 5084 4033 -186 -507 4 C
ATOM 4639 C ASP A 556 20.129 3.444 -20.613 1.00 36.85 C
ANISOU 4639 C ASP A 556 4901 5109 3988 -260 -478 -47 C
ATOM 4640 O ASP A 556 19.617 3.434 -19.491 1.00 38.91 O
ANISOU 4640 O ASP A 556 5176 5405 4201 -287 -488 -31 O
ATOM 4641 CB ASP A 556 22.050 1.929 -21.081 1.00 40.43 C
ANISOU 4641 CB ASP A 556 5299 5603 4458 -150 -544 5 C
ATOM 4642 CG ASP A 556 22.470 0.504 -21.407 1.00 46.16 C
ANISOU 4642 CG ASP A 556 6036 6298 5204 -68 -573 69 C
ATOM 4643 OD1 ASP A 556 21.591 -0.400 -21.396 1.00 48.05 O
ANISOU 4643 OD1 ASP A 556 6335 6468 5454 -47 -568 119 O
ATOM 4644 OD2 ASP A 556 23.670 0.284 -21.697 1.00 49.27 O
ANISOU 4644 OD2 ASP A 556 6380 6734 5605 -24 -595 68 O
ATOM 4645 N ARG A 557 20.352 4.568 -21.292 1.00 34.11 N
ANISOU 4645 N ARG A 557 4536 4754 3668 -292 -438 -108 N
ATOM 4646 CA ARG A 557 19.859 5.841 -20.772 1.00 34.99 C
ANISOU 4646 CA ARG A 557 4653 4882 3758 -361 -395 -159 C
ATOM 4647 C ARG A 557 18.335 5.798 -20.558 1.00 33.51 C
ANISOU 4647 C ARG A 557 4521 4641 3569 -376 -371 -135 C
ATOM 4648 O ARG A 557 17.841 6.296 -19.564 1.00 34.70 O
ANISOU 4648 O ARG A 557 4681 4823 3680 -421 -359 -148 O
ATOM 4649 CB ARG A 557 20.257 7.029 -21.680 1.00 34.99 C
ANISOU 4649 CB ARG A 557 4638 4861 3795 -388 -341 -223 C
ATOM 4650 CG ARG A 557 19.835 8.392 -21.142 1.00 36.64 C
ANISOU 4650 CG ARG A 557 4856 5079 3984 -458 -283 -278 C
ATOM 4651 CD ARG A 557 20.441 9.563 -21.929 1.00 38.33 C
ANISOU 4651 CD ARG A 557 5056 5276 4230 -487 -224 -342 C
ATOM 4652 NE ARG A 557 21.886 9.670 -21.735 1.00 41.41 N
ANISOU 4652 NE ARG A 557 5386 5744 4602 -504 -245 -381 N
ATOM 4653 CZ ARG A 557 22.650 10.694 -22.134 1.00 43.90 C
ANISOU 4653 CZ ARG A 557 5679 6068 4931 -547 -195 -449 C
ATOM 4654 NH1 ARG A 557 22.126 11.750 -22.762 1.00 41.11 N
ANISOU 4654 NH1 ARG A 557 5365 5642 4612 -571 -115 -481 N
ATOM 4655 NH2 ARG A 557 23.958 10.655 -21.901 1.00 43.36 N
ANISOU 4655 NH2 ARG A 557 5547 6086 4840 -563 -222 -483 N
ATOM 4656 N ILE A 558 17.597 5.183 -21.472 1.00 31.05 N
ANISOU 4656 N ILE A 558 4243 4255 3297 -340 -365 -104 N
ATOM 4657 CA ILE A 558 16.157 5.199 -21.340 1.00 30.46 C
ANISOU 4657 CA ILE A 558 4212 4140 3219 -357 -340 -88 C
ATOM 4658 C ILE A 558 15.743 4.392 -20.112 1.00 31.55 C
ANISOU 4658 C ILE A 558 4370 4307 3310 -363 -374 -45 C
ATOM 4659 O ILE A 558 14.927 4.833 -19.312 1.00 29.91 O
ANISOU 4659 O ILE A 558 4179 4112 3071 -403 -355 -52 O
ATOM 4660 CB ILE A 558 15.443 4.714 -22.620 1.00 28.70 C
ANISOU 4660 CB ILE A 558 4013 3847 3042 -323 -324 -70 C
ATOM 4661 CG1 ILE A 558 15.778 5.640 -23.797 1.00 27.00 C
ANISOU 4661 CG1 ILE A 558 3782 3608 2867 -318 -284 -110 C
ATOM 4662 CG2 ILE A 558 13.933 4.654 -22.397 1.00 28.21 C
ANISOU 4662 CG2 ILE A 558 3988 3761 2968 -342 -302 -54 C
ATOM 4663 CD1 ILE A 558 15.297 5.139 -25.149 1.00 25.41 C
ANISOU 4663 CD1 ILE A 558 3594 3354 2706 -282 -274 -95 C
ATOM 4664 N LYS A 559 16.361 3.230 -19.948 1.00 33.47 N
ANISOU 4664 N LYS A 559 4609 4560 3547 -322 -420 0 N
ATOM 4665 CA LYS A 559 16.037 2.346 -18.835 1.00 34.57 C
ANISOU 4665 CA LYS A 559 4772 4720 3641 -318 -450 50 C
ATOM 4666 C LYS A 559 16.459 2.923 -17.492 1.00 34.31 C
ANISOU 4666 C LYS A 559 4713 4777 3545 -355 -466 35 C
ATOM 4667 O LYS A 559 15.797 2.679 -16.481 1.00 32.55 O
ANISOU 4667 O LYS A 559 4515 4574 3279 -377 -471 61 O
ATOM 4668 CB LYS A 559 16.673 0.976 -19.030 1.00 35.88 C
ANISOU 4668 CB LYS A 559 4945 4870 3818 -254 -486 106 C
ATOM 4669 CG LYS A 559 16.116 0.223 -20.213 1.00 36.14 C
ANISOU 4669 CG LYS A 559 5013 4812 3905 -227 -467 121 C
ATOM 4670 CD LYS A 559 16.581 -1.213 -20.226 1.00 38.54 C
ANISOU 4670 CD LYS A 559 5339 5088 4216 -168 -492 181 C
ATOM 4671 CE LYS A 559 15.777 -1.993 -21.260 1.00 41.04 C
ANISOU 4671 CE LYS A 559 5700 5313 4579 -160 -462 189 C
ATOM 4672 NZ LYS A 559 16.338 -3.350 -21.466 1.00 45.82 N
ANISOU 4672 NZ LYS A 559 6329 5875 5203 -101 -473 240 N
ATOM 4673 N SER A 560 17.541 3.696 -17.467 1.00 33.60 N
ANISOU 4673 N SER A 560 4571 4748 3446 -368 -470 -8 N
ATOM 4674 CA SER A 560 17.965 4.262 -16.186 1.00 35.65 C
ANISOU 4674 CA SER A 560 4799 5106 3639 -413 -483 -31 C
ATOM 4675 C SER A 560 17.300 5.573 -15.836 1.00 35.00 C
ANISOU 4675 C SER A 560 4725 5026 3545 -487 -430 -93 C
ATOM 4676 O SER A 560 17.175 5.898 -14.648 1.00 35.77 O
ANISOU 4676 O SER A 560 4817 5189 3584 -532 -433 -105 O
ATOM 4677 CB SER A 560 19.494 4.354 -16.040 1.00 36.21 C
ANISOU 4677 CB SER A 560 4803 5267 3687 -399 -517 -50 C
ATOM 4678 OG SER A 560 20.085 5.003 -17.129 1.00 39.38 O
ANISOU 4678 OG SER A 560 5179 5643 4139 -400 -490 -100 O
ATOM 4679 N ARG A 561 16.857 6.317 -16.852 1.00 33.50 N
ANISOU 4679 N ARG A 561 4550 4766 3410 -496 -379 -129 N
ATOM 4680 CA ARG A 561 16.395 7.694 -16.646 1.00 34.11 C
ANISOU 4680 CA ARG A 561 4635 4840 3485 -559 -316 -192 C
ATOM 4681 C ARG A 561 14.891 7.846 -16.747 1.00 33.58 C
ANISOU 4681 C ARG A 561 4617 4708 3433 -565 -277 -178 C
ATOM 4682 O ARG A 561 14.329 8.755 -16.144 1.00 32.55 O
ANISOU 4682 O ARG A 561 4498 4584 3282 -615 -232 -214 O
ATOM 4683 CB ARG A 561 17.070 8.663 -17.623 1.00 35.75 C
ANISOU 4683 CB ARG A 561 4822 5026 3736 -567 -272 -248 C
ATOM 4684 CG ARG A 561 18.494 9.069 -17.251 1.00 37.80 C
ANISOU 4684 CG ARG A 561 5025 5370 3968 -597 -287 -296 C
ATOM 4685 CD ARG A 561 18.965 10.262 -18.084 1.00 38.52 C
ANISOU 4685 CD ARG A 561 5107 5431 4099 -626 -222 -363 C
ATOM 4686 NE ARG A 561 20.427 10.405 -18.066 1.00 41.81 N
ANISOU 4686 NE ARG A 561 5462 5923 4499 -642 -242 -404 N
ATOM 4687 CZ ARG A 561 21.107 11.413 -18.627 1.00 43.37 C
ANISOU 4687 CZ ARG A 561 5642 6114 4720 -679 -187 -471 C
ATOM 4688 NH1 ARG A 561 20.474 12.408 -19.272 1.00 41.74 N
ANISOU 4688 NH1 ARG A 561 5480 5822 4557 -698 -105 -501 N
ATOM 4689 NH2 ARG A 561 22.428 11.429 -18.538 1.00 42.14 N
ANISOU 4689 NH2 ARG A 561 5425 6041 4545 -695 -212 -508 N
ATOM 4690 N GLU A 562 14.242 6.984 -17.528 1.00 32.45 N
ANISOU 4690 N GLU A 562 4500 4504 3324 -518 -289 -130 N
ATOM 4691 CA GLU A 562 12.796 7.083 -17.722 1.00 32.31 C
ANISOU 4691 CA GLU A 562 4520 4436 3318 -522 -254 -118 C
ATOM 4692 C GLU A 562 12.045 5.986 -17.012 1.00 32.93 C
ANISOU 4692 C GLU A 562 4626 4518 3367 -519 -286 -67 C
ATOM 4693 O GLU A 562 12.554 4.898 -16.791 1.00 31.90 O
ANISOU 4693 O GLU A 562 4495 4400 3223 -491 -335 -25 O
ATOM 4694 CB GLU A 562 12.396 7.051 -19.212 1.00 32.09 C
ANISOU 4694 CB GLU A 562 4500 4342 3348 -481 -230 -113 C
ATOM 4695 CG GLU A 562 13.084 8.084 -20.102 1.00 33.27 C
ANISOU 4695 CG GLU A 562 4629 4476 3534 -476 -191 -157 C
ATOM 4696 CD GLU A 562 13.064 9.475 -19.507 1.00 31.53 C
ANISOU 4696 CD GLU A 562 4409 4271 3297 -525 -134 -209 C
ATOM 4697 OE1 GLU A 562 11.983 9.945 -19.079 1.00 31.77 O
ANISOU 4697 OE1 GLU A 562 4463 4290 3315 -545 -96 -211 O
ATOM 4698 OE2 GLU A 562 14.132 10.081 -19.462 1.00 31.73 O
ANISOU 4698 OE2 GLU A 562 4410 4321 3323 -547 -124 -250 O
ATOM 4699 N LYS A 563 10.801 6.308 -16.696 1.00 33.62 N
ANISOU 4699 N LYS A 563 4738 4590 3443 -544 -252 -69 N
ATOM 4700 CA LYS A 563 9.849 5.408 -16.128 1.00 33.96 C
ANISOU 4700 CA LYS A 563 4812 4628 3461 -550 -267 -28 C
ATOM 4701 C LYS A 563 9.216 4.575 -17.251 1.00 33.70 C
ANISOU 4701 C LYS A 563 4796 4539 3469 -514 -268 0 C
ATOM 4702 O LYS A 563 8.557 5.122 -18.133 1.00 34.02 O
ANISOU 4702 O LYS A 563 4833 4551 3540 -507 -230 -19 O
ATOM 4703 CB LYS A 563 8.794 6.267 -15.402 1.00 34.23 C
ANISOU 4703 CB LYS A 563 4859 4675 3470 -596 -221 -53 C
ATOM 4704 CG LYS A 563 7.553 5.543 -14.926 1.00 35.57 C
ANISOU 4704 CG LYS A 563 5059 4836 3617 -610 -221 -21 C
ATOM 4705 CD LYS A 563 7.873 4.569 -13.810 1.00 35.47 C
ANISOU 4705 CD LYS A 563 5063 4858 3556 -621 -267 18 C
ATOM 4706 CE LYS A 563 7.477 5.150 -12.463 1.00 37.65 C
ANISOU 4706 CE LYS A 563 5345 5183 3777 -675 -251 0 C
ATOM 4707 NZ LYS A 563 7.515 4.121 -11.376 1.00 35.76 N
ANISOU 4707 NZ LYS A 563 5128 4975 3483 -684 -290 49 N
ATOM 4708 N LEU A 564 9.402 3.256 -17.202 1.00 35.96 N
ANISOU 4708 N LEU A 564 5099 4810 3751 -492 -306 45 N
ATOM 4709 CA LEU A 564 8.885 2.329 -18.247 1.00 36.60 C
ANISOU 4709 CA LEU A 564 5198 4838 3868 -467 -304 66 C
ATOM 4710 C LEU A 564 7.716 1.435 -17.780 1.00 36.85 C
ANISOU 4710 C LEU A 564 5268 4853 3877 -491 -297 95 C
ATOM 4711 O LEU A 564 7.065 0.757 -18.593 1.00 36.74 O
ANISOU 4711 O LEU A 564 5268 4802 3887 -486 -285 101 O
ATOM 4712 CB LEU A 564 10.018 1.445 -18.783 1.00 38.08 C
ANISOU 4712 CB LEU A 564 5382 5005 4080 -421 -338 90 C
ATOM 4713 CG LEU A 564 11.235 2.139 -19.416 1.00 39.43 C
ANISOU 4713 CG LEU A 564 5514 5189 4279 -395 -345 62 C
ATOM 4714 CD1 LEU A 564 12.335 1.121 -19.641 1.00 39.53 C
ANISOU 4714 CD1 LEU A 564 5523 5190 4304 -349 -383 94 C
ATOM 4715 CD2 LEU A 564 10.857 2.813 -20.728 1.00 38.03 C
ANISOU 4715 CD2 LEU A 564 5322 4982 4144 -388 -310 28 C
ATOM 4716 N THR A 565 7.466 1.422 -16.476 1.00 37.30 N
ANISOU 4716 N THR A 565 5341 4942 3886 -522 -303 109 N
ATOM 4717 CA THR A 565 6.371 0.640 -15.901 1.00 37.08 C
ANISOU 4717 CA THR A 565 5351 4903 3832 -552 -292 135 C
ATOM 4718 C THR A 565 5.129 1.529 -15.805 1.00 38.08 C
ANISOU 4718 C THR A 565 5469 5049 3949 -590 -251 100 C
ATOM 4719 O THR A 565 5.240 2.718 -15.533 1.00 39.47 O
ANISOU 4719 O THR A 565 5622 5256 4119 -600 -236 68 O
ATOM 4720 CB THR A 565 6.743 0.102 -14.509 1.00 36.00 C
ANISOU 4720 CB THR A 565 5239 4794 3643 -562 -319 174 C
ATOM 4721 OG1 THR A 565 7.136 1.190 -13.666 1.00 34.08 O
ANISOU 4721 OG1 THR A 565 4969 4612 3366 -583 -322 148 O
ATOM 4722 CG2 THR A 565 7.900 -0.903 -14.608 1.00 35.83 C
ANISOU 4722 CG2 THR A 565 5228 4755 3629 -512 -355 220 C
ATOM 4723 N MET A 566 3.959 0.967 -16.077 1.00 38.52 N
ANISOU 4723 N MET A 566 5542 5086 4006 -611 -229 104 N
ATOM 4724 CA MET A 566 2.715 1.718 -15.951 1.00 39.54 C
ANISOU 4724 CA MET A 566 5659 5242 4122 -641 -191 76 C
ATOM 4725 C MET A 566 1.644 0.895 -15.265 1.00 40.37 C
ANISOU 4725 C MET A 566 5796 5348 4194 -685 -179 94 C
ATOM 4726 O MET A 566 1.682 -0.323 -15.287 1.00 41.02 O
ANISOU 4726 O MET A 566 5912 5398 4276 -690 -190 123 O
ATOM 4727 CB MET A 566 2.207 2.204 -17.316 1.00 40.55 C
ANISOU 4727 CB MET A 566 5754 5365 4287 -619 -165 49 C
ATOM 4728 CG MET A 566 1.981 1.117 -18.350 1.00 43.09 C
ANISOU 4728 CG MET A 566 6082 5656 4632 -611 -170 58 C
ATOM 4729 SD MET A 566 3.483 0.737 -19.276 1.00 51.11 S
ANISOU 4729 SD MET A 566 7095 6633 5692 -560 -202 67 S
ATOM 4730 CE MET A 566 2.831 -0.010 -20.761 1.00 39.78 C
ANISOU 4730 CE MET A 566 5650 5179 4285 -557 -186 54 C
ATOM 4731 N LYS A 567 0.696 1.584 -14.646 1.00 40.35 N
ANISOU 4731 N LYS A 567 5785 5381 4164 -718 -149 74 N
ATOM 4732 CA LYS A 567 -0.452 0.954 -14.032 1.00 40.47 C
ANISOU 4732 CA LYS A 567 5824 5405 4147 -765 -130 82 C
ATOM 4733 C LYS A 567 -1.588 0.819 -15.065 1.00 39.00 C
ANISOU 4733 C LYS A 567 5613 5225 3978 -772 -101 59 C
ATOM 4734 O LYS A 567 -1.919 1.783 -15.763 1.00 36.11 O
ANISOU 4734 O LYS A 567 5204 4884 3629 -748 -81 33 O
ATOM 4735 CB LYS A 567 -0.907 1.803 -12.841 1.00 40.23 C
ANISOU 4735 CB LYS A 567 5791 5416 4076 -797 -111 69 C
ATOM 4736 CG LYS A 567 -2.025 1.194 -12.017 1.00 40.45 C
ANISOU 4736 CG LYS A 567 5846 5458 4064 -851 -91 77 C
ATOM 4737 CD LYS A 567 -2.470 2.167 -10.939 1.00 40.74 C
ANISOU 4737 CD LYS A 567 5875 5538 4064 -880 -68 57 C
ATOM 4738 CE LYS A 567 -3.454 1.519 -9.961 1.00 43.37 C
ANISOU 4738 CE LYS A 567 6238 5886 4351 -937 -51 69 C
ATOM 4739 NZ LYS A 567 -3.367 2.182 -8.618 1.00 43.97 N
ANISOU 4739 NZ LYS A 567 6325 6000 4383 -966 -44 63 N
ATOM 4740 N PHE A 568 -2.171 -0.376 -15.154 1.00 37.56 N
ANISOU 4740 N PHE A 568 5458 5025 3788 -805 -95 70 N
ATOM 4741 CA PHE A 568 -3.305 -0.628 -16.057 1.00 37.34 C
ANISOU 4741 CA PHE A 568 5403 5018 3766 -825 -66 43 C
ATOM 4742 C PHE A 568 -4.614 -0.693 -15.281 1.00 37.91 C
ANISOU 4742 C PHE A 568 5476 5129 3797 -882 -34 31 C
ATOM 4743 O PHE A 568 -4.628 -1.069 -14.113 1.00 41.84 O
ANISOU 4743 O PHE A 568 6015 5616 4264 -915 -35 52 O
ATOM 4744 CB PHE A 568 -3.116 -1.939 -16.829 1.00 37.11 C
ANISOU 4744 CB PHE A 568 5398 4942 3757 -835 -70 50 C
ATOM 4745 CG PHE A 568 -2.026 -1.895 -17.863 1.00 38.56 C
ANISOU 4745 CG PHE A 568 5571 5096 3985 -781 -94 53 C
ATOM 4746 CD1 PHE A 568 -2.160 -1.109 -19.016 1.00 37.94 C
ANISOU 4746 CD1 PHE A 568 5437 5050 3928 -747 -89 25 C
ATOM 4747 CD2 PHE A 568 -0.875 -2.672 -17.715 1.00 38.78 C
ANISOU 4747 CD2 PHE A 568 5641 5064 4029 -759 -120 86 C
ATOM 4748 CE1 PHE A 568 -1.153 -1.085 -19.980 1.00 38.34 C
ANISOU 4748 CE1 PHE A 568 5477 5071 4017 -700 -109 26 C
ATOM 4749 CE2 PHE A 568 0.132 -2.653 -18.686 1.00 39.18 C
ANISOU 4749 CE2 PHE A 568 5679 5088 4120 -710 -140 86 C
ATOM 4750 CZ PHE A 568 -0.005 -1.856 -19.809 1.00 37.40 C
ANISOU 4750 CZ PHE A 568 5400 4893 3917 -684 -135 54 C
ATOM 4751 N HIS A 569 -5.718 -0.353 -15.930 1.00 37.96 N
ANISOU 4751 N HIS A 569 5434 5188 3799 -891 -6 0 N
ATOM 4752 CA HIS A 569 -7.009 -0.288 -15.242 1.00 37.38 C
ANISOU 4752 CA HIS A 569 5349 5164 3686 -942 26 -16 C
ATOM 4753 C HIS A 569 -8.036 -1.223 -15.781 1.00 37.85 C
ANISOU 4753 C HIS A 569 5398 5248 3732 -994 49 -39 C
ATOM 4754 O HIS A 569 -9.192 -1.209 -15.355 1.00 38.30 O
ANISOU 4754 O HIS A 569 5436 5358 3757 -1039 79 -59 O
ATOM 4755 CB HIS A 569 -7.530 1.131 -15.247 1.00 36.38 C
ANISOU 4755 CB HIS A 569 5170 5096 3555 -908 47 -34 C
ATOM 4756 CG HIS A 569 -6.716 2.058 -14.416 1.00 37.01 C
ANISOU 4756 CG HIS A 569 5268 5155 3637 -881 38 -22 C
ATOM 4757 ND1 HIS A 569 -5.760 2.839 -14.937 1.00 37.63 N
ANISOU 4757 ND1 HIS A 569 5335 5214 3748 -825 25 -19 N
ATOM 4758 CD2 HIS A 569 -6.717 2.296 -13.051 1.00 38.02 C
ANISOU 4758 CD2 HIS A 569 5426 5284 3733 -913 44 -15 C
ATOM 4759 CE1 HIS A 569 -5.184 3.559 -13.961 1.00 36.80 C
ANISOU 4759 CE1 HIS A 569 5249 5099 3633 -824 25 -17 C
ATOM 4760 NE2 HIS A 569 -5.770 3.228 -12.807 1.00 39.22 N
ANISOU 4760 NE2 HIS A 569 5580 5422 3899 -877 35 -14 N
ATOM 4761 N ASP A 570 -7.627 -2.066 -16.712 1.00 38.56 N
ANISOU 4761 N ASP A 570 5498 5304 3847 -993 40 -42 N
ATOM 4762 CA ASP A 570 -8.512 -3.090 -17.233 1.00 41.94 C
ANISOU 4762 CA ASP A 570 5922 5750 4262 -1056 67 -71 C
ATOM 4763 C ASP A 570 -7.817 -4.446 -17.113 1.00 41.55 C
ANISOU 4763 C ASP A 570 5950 5609 4228 -1085 66 -50 C
ATOM 4764 O ASP A 570 -6.706 -4.625 -17.595 1.00 42.72 O
ANISOU 4764 O ASP A 570 6117 5701 4411 -1039 40 -30 O
ATOM 4765 CB ASP A 570 -8.885 -2.765 -18.690 1.00 42.21 C
ANISOU 4765 CB ASP A 570 5884 5845 4307 -1031 70 -106 C
ATOM 4766 CG ASP A 570 -9.820 -3.798 -19.309 1.00 45.17 C
ANISOU 4766 CG ASP A 570 6244 6254 4663 -1105 101 -148 C
ATOM 4767 OD1 ASP A 570 -9.884 -4.937 -18.807 1.00 44.44 O
ANISOU 4767 OD1 ASP A 570 6213 6106 4564 -1171 121 -148 O
ATOM 4768 OD2 ASP A 570 -10.483 -3.471 -20.324 1.00 47.86 O
ANISOU 4768 OD2 ASP A 570 6511 6680 4993 -1098 109 -182 O
ATOM 4769 N GLY A 571 -8.462 -5.392 -16.446 1.00 42.44 N
ANISOU 4769 N GLY A 571 6106 5702 4313 -1159 98 -53 N
ATOM 4770 CA GLY A 571 -7.871 -6.728 -16.252 1.00 44.18 C
ANISOU 4770 CA GLY A 571 6411 5827 4548 -1184 110 -27 C
ATOM 4771 C GLY A 571 -7.838 -7.570 -17.522 1.00 42.98 C
ANISOU 4771 C GLY A 571 6257 5649 4422 -1204 129 -60 C
ATOM 4772 O GLY A 571 -7.303 -8.676 -17.537 1.00 44.26 O
ANISOU 4772 O GLY A 571 6489 5724 4603 -1219 146 -41 O
ATOM 4773 N GLU A 572 -8.406 -7.030 -18.589 1.00 44.68 N
ANISOU 4773 N GLU A 572 6392 5944 4637 -1202 129 -107 N
ATOM 4774 CA GLU A 572 -8.538 -7.730 -19.859 1.00 44.98 C
ANISOU 4774 CA GLU A 572 6415 5984 4691 -1231 149 -150 C
ATOM 4775 C GLU A 572 -7.392 -7.328 -20.776 1.00 42.56 C
ANISOU 4775 C GLU A 572 6091 5652 4427 -1149 110 -135 C
ATOM 4776 O GLU A 572 -7.211 -7.899 -21.864 1.00 41.08 O
ANISOU 4776 O GLU A 572 5896 5451 4259 -1160 121 -165 O
ATOM 4777 CB GLU A 572 -9.858 -7.332 -20.503 1.00 49.04 C
ANISOU 4777 CB GLU A 572 6840 6621 5169 -1273 168 -210 C
ATOM 4778 CG GLU A 572 -10.543 -8.435 -21.276 1.00 55.51 C
ANISOU 4778 CG GLU A 572 7657 7456 5977 -1362 215 -270 C
ATOM 4779 CD GLU A 572 -11.526 -9.198 -20.433 1.00 57.45 C
ANISOU 4779 CD GLU A 572 7938 7702 6187 -1462 266 -292 C
ATOM 4780 OE1 GLU A 572 -11.764 -8.777 -19.290 1.00 58.35 O
ANISOU 4780 OE1 GLU A 572 8068 7819 6283 -1458 262 -261 O
ATOM 4781 OE2 GLU A 572 -12.059 -10.222 -20.918 1.00 65.96 O
ANISOU 4781 OE2 GLU A 572 9029 8777 7254 -1551 316 -344 O
ATOM 4782 N VAL A 573 -6.634 -6.325 -20.342 1.00 40.05 N
ANISOU 4782 N VAL A 573 5764 5331 4122 -1073 68 -95 N
ATOM 4783 CA VAL A 573 -5.489 -5.835 -21.093 1.00 38.95 C
ANISOU 4783 CA VAL A 573 5609 5168 4021 -995 32 -79 C
ATOM 4784 C VAL A 573 -4.548 -6.982 -21.396 1.00 39.16 C
ANISOU 4784 C VAL A 573 5699 5096 4082 -994 35 -63 C
ATOM 4785 O VAL A 573 -4.361 -7.893 -20.561 1.00 37.34 O
ANISOU 4785 O VAL A 573 5543 4795 3849 -1021 53 -35 O
ATOM 4786 CB VAL A 573 -4.733 -4.727 -20.308 1.00 38.66 C
ANISOU 4786 CB VAL A 573 5570 5128 3990 -929 -4 -38 C
ATOM 4787 CG1 VAL A 573 -3.874 -5.314 -19.191 1.00 36.74 C
ANISOU 4787 CG1 VAL A 573 5402 4806 3750 -924 -16 10 C
ATOM 4788 CG2 VAL A 573 -3.909 -3.849 -21.251 1.00 37.65 C
ANISOU 4788 CG2 VAL A 573 5399 5012 3894 -855 -33 -39 C
ATOM 4789 N ASP A 574 -3.982 -6.961 -22.599 1.00 39.75 N
ANISOU 4789 N ASP A 574 5748 5166 4188 -959 24 -80 N
ATOM 4790 CA ASP A 574 -2.831 -7.803 -22.896 1.00 39.75 C
ANISOU 4790 CA ASP A 574 5803 5071 4228 -933 21 -58 C
ATOM 4791 C ASP A 574 -1.593 -7.005 -22.594 1.00 37.26 C
ANISOU 4791 C ASP A 574 5484 4737 3936 -848 -26 -14 C
ATOM 4792 O ASP A 574 -1.194 -6.140 -23.374 1.00 35.26 O
ANISOU 4792 O ASP A 574 5178 4519 3698 -800 -50 -25 O
ATOM 4793 CB ASP A 574 -2.808 -8.259 -24.347 1.00 40.91 C
ANISOU 4793 CB ASP A 574 5926 5221 4396 -945 37 -103 C
ATOM 4794 CG ASP A 574 -1.662 -9.220 -24.628 1.00 43.44 C
ANISOU 4794 CG ASP A 574 6308 5436 4760 -919 43 -82 C
ATOM 4795 OD1 ASP A 574 -0.784 -9.367 -23.758 1.00 43.31 O
ANISOU 4795 OD1 ASP A 574 6341 5356 4757 -875 25 -26 O
ATOM 4796 OD2 ASP A 574 -1.647 -9.844 -25.706 1.00 48.29 O
ANISOU 4796 OD2 ASP A 574 6920 6035 5392 -943 68 -121 O
ATOM 4797 N ALA A 575 -1.003 -7.276 -21.437 1.00 37.40 N
ANISOU 4797 N ALA A 575 5555 4703 3949 -831 -38 35 N
ATOM 4798 CA ALA A 575 0.150 -6.499 -20.966 1.00 36.17 C
ANISOU 4798 CA ALA A 575 5393 4545 3805 -760 -84 73 C
ATOM 4799 C ALA A 575 1.383 -6.842 -21.795 1.00 34.03 C
ANISOU 4799 C ALA A 575 5128 4223 3579 -706 -100 83 C
ATOM 4800 O ALA A 575 2.306 -6.036 -21.898 1.00 31.51 O
ANISOU 4800 O ALA A 575 4778 3918 3275 -649 -136 95 O
ATOM 4801 CB ALA A 575 0.405 -6.767 -19.494 1.00 34.69 C
ANISOU 4801 CB ALA A 575 5256 4333 3591 -761 -92 124 C
ATOM 4802 N SER A 576 1.378 -8.036 -22.393 1.00 32.16 N
ANISOU 4802 N SER A 576 4929 3926 3362 -728 -69 75 N
ATOM 4803 CA SER A 576 2.509 -8.493 -23.167 1.00 32.96 C
ANISOU 4803 CA SER A 576 5042 3972 3506 -678 -77 84 C
ATOM 4804 C SER A 576 2.684 -7.662 -24.425 1.00 33.08 C
ANISOU 4804 C SER A 576 4990 4035 3543 -654 -93 43 C
ATOM 4805 O SER A 576 3.805 -7.477 -24.914 1.00 34.59 O
ANISOU 4805 O SER A 576 5170 4206 3766 -596 -117 54 O
ATOM 4806 CB SER A 576 2.410 -9.984 -23.500 1.00 33.97 C
ANISOU 4806 CB SER A 576 5236 4017 3654 -712 -27 80 C
ATOM 4807 OG SER A 576 1.268 -10.275 -24.305 1.00 35.54 O
ANISOU 4807 OG SER A 576 5417 4243 3843 -787 13 18 O
ATOM 4808 N TYR A 577 1.594 -7.121 -24.937 1.00 32.78 N
ANISOU 4808 N TYR A 577 4905 4067 3483 -694 -80 0 N
ATOM 4809 CA TYR A 577 1.685 -6.338 -26.160 1.00 32.63 C
ANISOU 4809 CA TYR A 577 4823 4098 3477 -667 -91 -33 C
ATOM 4810 C TYR A 577 2.767 -5.262 -26.046 1.00 32.19 C
ANISOU 4810 C TYR A 577 4740 4050 3439 -596 -131 -8 C
ATOM 4811 O TYR A 577 3.460 -4.974 -27.014 1.00 32.53 O
ANISOU 4811 O TYR A 577 4757 4091 3509 -557 -141 -20 O
ATOM 4812 CB TYR A 577 0.334 -5.725 -26.523 1.00 31.97 C
ANISOU 4812 CB TYR A 577 4684 4106 3357 -706 -75 -71 C
ATOM 4813 CG TYR A 577 0.259 -5.251 -27.944 1.00 32.63 C
ANISOU 4813 CG TYR A 577 4708 4242 3447 -688 -75 -106 C
ATOM 4814 CD1 TYR A 577 0.262 -6.164 -29.007 1.00 32.81 C
ANISOU 4814 CD1 TYR A 577 4735 4248 3483 -717 -53 -141 C
ATOM 4815 CD2 TYR A 577 0.189 -3.884 -28.244 1.00 32.05 C
ANISOU 4815 CD2 TYR A 577 4578 4234 3366 -641 -91 -103 C
ATOM 4816 CE1 TYR A 577 0.184 -5.728 -30.320 1.00 33.06 C
ANISOU 4816 CE1 TYR A 577 4709 4339 3513 -700 -54 -172 C
ATOM 4817 CE2 TYR A 577 0.104 -3.446 -29.554 1.00 31.13 C
ANISOU 4817 CE2 TYR A 577 4408 4170 3250 -618 -88 -128 C
ATOM 4818 CZ TYR A 577 0.110 -4.369 -30.586 1.00 32.33 C
ANISOU 4818 CZ TYR A 577 4560 4314 3409 -648 -73 -162 C
ATOM 4819 OH TYR A 577 0.038 -3.939 -31.898 1.00 33.90 O
ANISOU 4819 OH TYR A 577 4704 4573 3602 -626 -72 -186 O
ATOM 4820 N PHE A 578 2.957 -4.726 -24.846 1.00 31.23 N
ANISOU 4820 N PHE A 578 4630 3935 3301 -583 -150 23 N
ATOM 4821 CA PHE A 578 3.816 -3.556 -24.666 1.00 32.79 C
ANISOU 4821 CA PHE A 578 4797 4154 3507 -530 -180 35 C
ATOM 4822 C PHE A 578 5.299 -3.877 -24.420 1.00 34.47 C
ANISOU 4822 C PHE A 578 5032 4319 3746 -483 -208 66 C
ATOM 4823 O PHE A 578 6.136 -2.965 -24.266 1.00 34.39 O
ANISOU 4823 O PHE A 578 4995 4328 3742 -445 -231 70 O
ATOM 4824 CB PHE A 578 3.215 -2.631 -23.592 1.00 32.65 C
ANISOU 4824 CB PHE A 578 4767 4183 3453 -545 -181 41 C
ATOM 4825 CG PHE A 578 1.781 -2.248 -23.878 1.00 32.13 C
ANISOU 4825 CG PHE A 578 4671 4174 3361 -581 -152 12 C
ATOM 4826 CD1 PHE A 578 1.480 -1.216 -24.788 1.00 32.40 C
ANISOU 4826 CD1 PHE A 578 4651 4258 3399 -555 -143 -10 C
ATOM 4827 CD2 PHE A 578 0.734 -2.975 -23.331 1.00 30.72 C
ANISOU 4827 CD2 PHE A 578 4516 4001 3154 -639 -131 9 C
ATOM 4828 CE1 PHE A 578 0.151 -0.895 -25.094 1.00 32.57 C
ANISOU 4828 CE1 PHE A 578 4637 4344 3393 -579 -118 -32 C
ATOM 4829 CE2 PHE A 578 -0.591 -2.672 -23.652 1.00 31.51 C
ANISOU 4829 CE2 PHE A 578 4578 4165 3227 -672 -105 -20 C
ATOM 4830 CZ PHE A 578 -0.883 -1.622 -24.522 1.00 30.85 C
ANISOU 4830 CZ PHE A 578 4435 4140 3145 -639 -101 -39 C
ATOM 4831 N CYS A 579 5.613 -5.171 -24.460 1.00 37.24 N
ANISOU 4831 N CYS A 579 5428 4608 4111 -485 -200 83 N
ATOM 4832 CA CYS A 579 6.933 -5.720 -24.128 1.00 40.88 C
ANISOU 4832 CA CYS A 579 5916 5023 4593 -435 -222 122 C
ATOM 4833 C CYS A 579 7.821 -5.796 -25.352 1.00 41.30 C
ANISOU 4833 C CYS A 579 5947 5054 4689 -395 -226 105 C
ATOM 4834 O CYS A 579 9.045 -5.832 -25.238 1.00 41.84 O
ANISOU 4834 O CYS A 579 6013 5107 4775 -343 -251 129 O
ATOM 4835 CB CYS A 579 6.782 -7.165 -23.637 1.00 44.81 C
ANISOU 4835 CB CYS A 579 6482 5454 5088 -450 -198 155 C
ATOM 4836 SG CYS A 579 6.291 -7.388 -21.932 1.00 53.93 S
ANISOU 4836 SG CYS A 579 7680 6616 6194 -476 -199 200 S
ATOM 4837 N LYS A 580 7.195 -5.897 -26.517 1.00 38.90 N
ANISOU 4837 N LYS A 580 5628 4753 4398 -421 -200 63 N
ATOM 4838 CA LYS A 580 7.882 -6.350 -27.711 1.00 38.86 C
ANISOU 4838 CA LYS A 580 5618 4714 4433 -395 -193 45 C
ATOM 4839 C LYS A 580 7.352 -5.655 -28.956 1.00 36.27 C
ANISOU 4839 C LYS A 580 5239 4435 4106 -409 -183 -2 C
ATOM 4840 O LYS A 580 6.259 -5.093 -28.951 1.00 34.47 O
ANISOU 4840 O LYS A 580 4986 4261 3847 -444 -173 -21 O
ATOM 4841 CB LYS A 580 7.690 -7.869 -27.861 1.00 40.50 C
ANISOU 4841 CB LYS A 580 5884 4849 4654 -420 -156 49 C
ATOM 4842 CG LYS A 580 6.217 -8.293 -27.890 1.00 41.55 C
ANISOU 4842 CG LYS A 580 6032 4994 4759 -497 -118 19 C
ATOM 4843 CD LYS A 580 6.019 -9.793 -27.673 1.00 43.51 C
ANISOU 4843 CD LYS A 580 6354 5160 5017 -530 -73 28 C
ATOM 4844 CE LYS A 580 4.536 -10.152 -27.484 1.00 44.63 C
ANISOU 4844 CE LYS A 580 6510 5323 5124 -617 -34 -2 C
ATOM 4845 NZ LYS A 580 3.686 -9.878 -28.686 1.00 44.95 N
ANISOU 4845 NZ LYS A 580 6498 5426 5153 -665 -16 -69 N
ATOM 4846 N LEU A 581 8.136 -5.700 -30.019 1.00 34.35 N
ANISOU 4846 N LEU A 581 4978 4176 3895 -378 -184 -18 N
ATOM 4847 CA LEU A 581 7.629 -5.414 -31.336 1.00 36.64 C
ANISOU 4847 CA LEU A 581 5230 4504 4185 -394 -167 -62 C
ATOM 4848 C LEU A 581 6.433 -6.309 -31.586 1.00 36.80 C
ANISOU 4848 C LEU A 581 5269 4526 4185 -460 -131 -90 C
ATOM 4849 O LEU A 581 6.545 -7.513 -31.437 1.00 39.71 O
ANISOU 4849 O LEU A 581 5688 4829 4568 -481 -108 -88 O
ATOM 4850 CB LEU A 581 8.714 -5.713 -32.385 1.00 36.89 C
ANISOU 4850 CB LEU A 581 5256 4501 4257 -357 -167 -75 C
ATOM 4851 CG LEU A 581 9.362 -4.578 -33.180 1.00 39.02 C
ANISOU 4851 CG LEU A 581 5476 4809 4539 -315 -183 -86 C
ATOM 4852 CD1 LEU A 581 9.100 -3.193 -32.603 1.00 38.34 C
ANISOU 4852 CD1 LEU A 581 5359 4778 4429 -303 -198 -74 C
ATOM 4853 CD2 LEU A 581 10.856 -4.810 -33.377 1.00 39.84 C
ANISOU 4853 CD2 LEU A 581 5585 4867 4685 -264 -198 -75 C
ATOM 4854 N PRO A 582 5.284 -5.726 -31.972 1.00 36.42 N
ANISOU 4854 N PRO A 582 5180 4556 4102 -493 -121 -118 N
ATOM 4855 CA PRO A 582 4.193 -6.531 -32.505 1.00 36.94 C
ANISOU 4855 CA PRO A 582 5246 4643 4144 -562 -85 -159 C
ATOM 4856 C PRO A 582 4.629 -7.185 -33.804 1.00 39.01 C
ANISOU 4856 C PRO A 582 5506 4885 4431 -567 -66 -196 C
ATOM 4857 O PRO A 582 5.369 -6.576 -34.592 1.00 38.62 O
ANISOU 4857 O PRO A 582 5424 4848 4399 -518 -83 -197 O
ATOM 4858 CB PRO A 582 3.102 -5.495 -32.804 1.00 35.95 C
ANISOU 4858 CB PRO A 582 5056 4625 3975 -572 -87 -176 C
ATOM 4859 CG PRO A 582 3.491 -4.281 -32.037 1.00 35.29 C
ANISOU 4859 CG PRO A 582 4960 4553 3893 -518 -116 -137 C
ATOM 4860 CD PRO A 582 4.977 -4.294 -32.030 1.00 35.45 C
ANISOU 4860 CD PRO A 582 5004 4507 3958 -466 -137 -114 C
ATOM 4861 N GLU A 583 4.156 -8.396 -34.051 1.00 42.10 N
ANISOU 4861 N GLU A 583 5930 5244 4820 -630 -26 -229 N
ATOM 4862 CA GLU A 583 4.614 -9.149 -35.216 1.00 45.68 C
ANISOU 4862 CA GLU A 583 6392 5666 5298 -641 0 -268 C
ATOM 4863 C GLU A 583 4.405 -8.426 -36.588 1.00 41.97 C
ANISOU 4863 C GLU A 583 5847 5289 4807 -635 -7 -307 C
ATOM 4864 O GLU A 583 5.241 -8.535 -37.478 1.00 40.38 O
ANISOU 4864 O GLU A 583 5641 5064 4634 -607 -6 -320 O
ATOM 4865 CB GLU A 583 4.074 -10.591 -35.198 1.00 50.78 C
ANISOU 4865 CB GLU A 583 7092 6255 5944 -721 57 -304 C
ATOM 4866 CG GLU A 583 4.224 -11.328 -33.848 1.00 58.76 C
ANISOU 4866 CG GLU A 583 8181 7172 6970 -724 71 -259 C
ATOM 4867 CD GLU A 583 5.553 -11.069 -33.101 1.00 65.67 C
ANISOU 4867 CD GLU A 583 9084 7983 7884 -632 33 -190 C
ATOM 4868 OE1 GLU A 583 6.484 -11.899 -33.233 1.00 64.63 O
ANISOU 4868 OE1 GLU A 583 9000 7761 7794 -602 53 -176 O
ATOM 4869 OE2 GLU A 583 5.656 -10.066 -32.341 1.00 65.10 O
ANISOU 4869 OE2 GLU A 583 8984 7952 7796 -591 -11 -151 O
ATOM 4870 N LYS A 584 3.350 -7.632 -36.722 1.00 39.59 N
ANISOU 4870 N LYS A 584 5489 5096 4457 -652 -15 -318 N
ATOM 4871 CA LYS A 584 3.184 -6.833 -37.949 1.00 39.69 C
ANISOU 4871 CA LYS A 584 5430 5203 4444 -630 -24 -340 C
ATOM 4872 C LYS A 584 4.337 -5.845 -38.196 1.00 39.66 C
ANISOU 4872 C LYS A 584 5413 5181 4472 -543 -56 -303 C
ATOM 4873 O LYS A 584 4.586 -5.467 -39.331 1.00 44.33 O
ANISOU 4873 O LYS A 584 5966 5816 5059 -520 -56 -321 O
ATOM 4874 CB LYS A 584 1.836 -6.115 -37.970 1.00 37.38 C
ANISOU 4874 CB LYS A 584 5076 5035 4089 -650 -26 -349 C
ATOM 4875 CG LYS A 584 1.671 -5.067 -36.889 1.00 38.74 C
ANISOU 4875 CG LYS A 584 5244 5218 4256 -605 -51 -297 C
ATOM 4876 CD LYS A 584 0.207 -4.727 -36.687 1.00 40.04 C
ANISOU 4876 CD LYS A 584 5361 5490 4362 -640 -42 -309 C
ATOM 4877 CE LYS A 584 0.059 -3.559 -35.735 1.00 41.01 C
ANISOU 4877 CE LYS A 584 5476 5627 4480 -588 -60 -260 C
ATOM 4878 NZ LYS A 584 -1.161 -3.721 -34.904 1.00 41.33 N
ANISOU 4878 NZ LYS A 584 5508 5713 4480 -639 -48 -267 N
ATOM 4879 N PHE A 585 5.040 -5.444 -37.133 1.00 38.72 N
ANISOU 4879 N PHE A 585 5326 5002 4383 -498 -79 -255 N
ATOM 4880 CA PHE A 585 6.189 -4.537 -37.256 1.00 37.14 C
ANISOU 4880 CA PHE A 585 5116 4781 4213 -425 -104 -226 C
ATOM 4881 C PHE A 585 7.547 -5.245 -37.085 1.00 37.97 C
ANISOU 4881 C PHE A 585 5266 4787 4372 -399 -110 -215 C
ATOM 4882 O PHE A 585 8.601 -4.624 -37.239 1.00 35.79 O
ANISOU 4882 O PHE A 585 4981 4494 4124 -345 -128 -198 O
ATOM 4883 CB PHE A 585 6.090 -3.407 -36.210 1.00 35.30 C
ANISOU 4883 CB PHE A 585 4875 4566 3970 -392 -125 -185 C
ATOM 4884 CG PHE A 585 4.953 -2.425 -36.449 1.00 33.24 C
ANISOU 4884 CG PHE A 585 4564 4402 3662 -391 -118 -187 C
ATOM 4885 CD1 PHE A 585 4.923 -1.633 -37.584 1.00 31.01 C
ANISOU 4885 CD1 PHE A 585 4234 4181 3366 -356 -112 -193 C
ATOM 4886 CD2 PHE A 585 3.957 -2.253 -35.494 1.00 30.81 C
ANISOU 4886 CD2 PHE A 585 4256 4125 3323 -417 -115 -176 C
ATOM 4887 CE1 PHE A 585 3.904 -0.711 -37.782 1.00 31.55 C
ANISOU 4887 CE1 PHE A 585 4257 4340 3390 -341 -103 -185 C
ATOM 4888 CE2 PHE A 585 2.942 -1.336 -35.691 1.00 31.27 C
ANISOU 4888 CE2 PHE A 585 4266 4274 3339 -406 -106 -172 C
ATOM 4889 CZ PHE A 585 2.915 -0.559 -36.834 1.00 29.92 C
ANISOU 4889 CZ PHE A 585 4048 4163 3154 -364 -99 -174 C
ATOM 4890 N ARG A 586 7.517 -6.529 -36.730 1.00 40.66 N
ANISOU 4890 N ARG A 586 5657 5063 4727 -437 -90 -222 N
ATOM 4891 CA ARG A 586 8.711 -7.214 -36.236 1.00 42.51 C
ANISOU 4891 CA ARG A 586 5939 5202 5007 -402 -95 -196 C
ATOM 4892 C ARG A 586 9.725 -7.543 -37.334 1.00 43.87 C
ANISOU 4892 C ARG A 586 6107 5342 5217 -374 -86 -217 C
ATOM 4893 O ARG A 586 10.920 -7.640 -37.051 1.00 47.80 O
ANISOU 4893 O ARG A 586 6621 5786 5752 -321 -101 -189 O
ATOM 4894 CB ARG A 586 8.337 -8.480 -35.445 1.00 44.83 C
ANISOU 4894 CB ARG A 586 6297 5430 5304 -444 -67 -188 C
ATOM 4895 CG ARG A 586 9.493 -9.125 -34.689 1.00 49.22 C
ANISOU 4895 CG ARG A 586 6905 5896 5901 -394 -73 -143 C
ATOM 4896 CD ARG A 586 9.023 -10.025 -33.546 1.00 55.53 C
ANISOU 4896 CD ARG A 586 7767 6641 6691 -423 -52 -115 C
ATOM 4897 NE ARG A 586 8.829 -11.425 -33.941 1.00 62.99 N
ANISOU 4897 NE ARG A 586 8767 7509 7654 -464 5 -139 N
ATOM 4898 CZ ARG A 586 9.718 -12.410 -33.750 1.00 68.59 C
ANISOU 4898 CZ ARG A 586 9534 8122 8404 -426 28 -111 C
ATOM 4899 NH1 ARG A 586 10.898 -12.160 -33.183 1.00 69.87 N
ANISOU 4899 NH1 ARG A 586 9695 8263 8587 -343 -8 -57 N
ATOM 4900 NH2 ARG A 586 9.430 -13.656 -34.134 1.00 63.06 N
ANISOU 4900 NH2 ARG A 586 8891 7348 7720 -472 94 -140 N
ATOM 4901 N PHE A 587 9.265 -7.694 -38.573 1.00 41.78 N
ANISOU 4901 N PHE A 587 5816 5117 4939 -407 -63 -266 N
ATOM 4902 CA PHE A 587 10.152 -8.153 -39.650 1.00 46.54 C
ANISOU 4902 CA PHE A 587 6419 5685 5576 -390 -47 -293 C
ATOM 4903 C PHE A 587 10.227 -7.200 -40.838 1.00 47.70 C
ANISOU 4903 C PHE A 587 6507 5909 5708 -372 -56 -315 C
ATOM 4904 O PHE A 587 10.490 -7.635 -41.959 1.00 48.51 O
ANISOU 4904 O PHE A 587 6601 6010 5818 -384 -34 -355 O
ATOM 4905 CB PHE A 587 9.738 -9.551 -40.161 1.00 49.39 C
ANISOU 4905 CB PHE A 587 6820 6003 5943 -453 4 -339 C
ATOM 4906 CG PHE A 587 9.527 -10.575 -39.071 1.00 51.66 C
ANISOU 4906 CG PHE A 587 7175 6209 6242 -478 28 -318 C
ATOM 4907 CD1 PHE A 587 10.608 -11.080 -38.339 1.00 52.47 C
ANISOU 4907 CD1 PHE A 587 7326 6218 6390 -421 24 -272 C
ATOM 4908 CD2 PHE A 587 8.246 -11.063 -38.799 1.00 52.62 C
ANISOU 4908 CD2 PHE A 587 7311 6352 6327 -556 57 -344 C
ATOM 4909 CE1 PHE A 587 10.411 -12.039 -37.351 1.00 53.51 C
ANISOU 4909 CE1 PHE A 587 7525 6274 6530 -437 51 -245 C
ATOM 4910 CE2 PHE A 587 8.044 -12.024 -37.810 1.00 53.59 C
ANISOU 4910 CE2 PHE A 587 7504 6395 6461 -581 87 -324 C
ATOM 4911 CZ PHE A 587 9.125 -12.515 -37.092 1.00 54.31 C
ANISOU 4911 CZ PHE A 587 7648 6387 6597 -519 85 -271 C
ATOM 4912 N VAL A 588 9.986 -5.907 -40.611 1.00 46.43 N
ANISOU 4912 N VAL A 588 6306 5812 5521 -343 -83 -290 N
ATOM 4913 CA VAL A 588 10.240 -4.909 -41.656 1.00 40.52 C
ANISOU 4913 CA VAL A 588 5509 5124 4763 -311 -89 -298 C
ATOM 4914 C VAL A 588 11.739 -4.817 -41.835 1.00 38.08 C
ANISOU 4914 C VAL A 588 5208 4756 4504 -259 -99 -288 C
ATOM 4915 O VAL A 588 12.485 -4.987 -40.871 1.00 36.71 O
ANISOU 4915 O VAL A 588 5062 4522 4361 -233 -115 -258 O
ATOM 4916 CB VAL A 588 9.646 -3.506 -41.320 1.00 39.88 C
ANISOU 4916 CB VAL A 588 5391 5113 4646 -286 -105 -268 C
ATOM 4917 CG1 VAL A 588 8.167 -3.603 -41.007 1.00 39.96 C
ANISOU 4917 CG1 VAL A 588 5389 5186 4606 -332 -97 -275 C
ATOM 4918 CG2 VAL A 588 10.382 -2.843 -40.179 1.00 35.39 C
ANISOU 4918 CG2 VAL A 588 4840 4502 4103 -245 -128 -227 C
ATOM 4919 N LYS A 589 12.192 -4.601 -43.065 1.00 38.60 N
ANISOU 4919 N LYS A 589 5247 4843 4573 -245 -88 -312 N
ATOM 4920 CA LYS A 589 13.632 -4.470 -43.317 1.00 38.98 C
ANISOU 4920 CA LYS A 589 5298 4844 4669 -197 -95 -307 C
ATOM 4921 C LYS A 589 14.124 -3.090 -42.881 1.00 37.99 C
ANISOU 4921 C LYS A 589 5151 4739 4545 -152 -116 -274 C
ATOM 4922 O LYS A 589 13.510 -2.069 -43.210 1.00 35.55 O
ANISOU 4922 O LYS A 589 4812 4492 4201 -147 -112 -268 O
ATOM 4923 CB LYS A 589 13.957 -4.701 -44.799 1.00 43.08 C
ANISOU 4923 CB LYS A 589 5797 5380 5191 -202 -73 -348 C
ATOM 4924 CG LYS A 589 14.453 -6.103 -45.138 1.00 47.34 C
ANISOU 4924 CG LYS A 589 6370 5850 5766 -221 -49 -380 C
ATOM 4925 CD LYS A 589 15.447 -6.076 -46.302 1.00 49.20 C
ANISOU 4925 CD LYS A 589 6588 6078 6027 -197 -35 -406 C
ATOM 4926 CE LYS A 589 14.845 -6.671 -47.573 1.00 54.64 C
ANISOU 4926 CE LYS A 589 7265 6805 6688 -248 -1 -462 C
ATOM 4927 NZ LYS A 589 15.395 -6.075 -48.833 1.00 54.27 N
ANISOU 4927 NZ LYS A 589 7182 6802 6636 -227 4 -482 N
ATOM 4928 N ILE A 590 15.229 -3.058 -42.141 1.00 36.19 N
ANISOU 4928 N ILE A 590 4936 4461 4354 -119 -134 -254 N
ATOM 4929 CA ILE A 590 15.850 -1.787 -41.771 1.00 35.09 C
ANISOU 4929 CA ILE A 590 4775 4338 4218 -85 -147 -234 C
ATOM 4930 C ILE A 590 17.283 -1.665 -42.302 1.00 35.46 C
ANISOU 4930 C ILE A 590 4808 4360 4303 -51 -146 -246 C
ATOM 4931 O ILE A 590 17.999 -0.730 -41.975 1.00 35.31 O
ANISOU 4931 O ILE A 590 4774 4349 4293 -29 -153 -238 O
ATOM 4932 CB ILE A 590 15.811 -1.557 -40.239 1.00 35.09 C
ANISOU 4932 CB ILE A 590 4791 4327 4214 -84 -170 -202 C
ATOM 4933 CG1 ILE A 590 16.754 -2.540 -39.507 1.00 35.34 C
ANISOU 4933 CG1 ILE A 590 4845 4303 4279 -67 -188 -190 C
ATOM 4934 CG2 ILE A 590 14.383 -1.694 -39.735 1.00 34.12 C
ANISOU 4934 CG2 ILE A 590 4680 4228 4052 -120 -167 -193 C
ATOM 4935 CD1 ILE A 590 16.812 -2.356 -38.005 1.00 35.00 C
ANISOU 4935 CD1 ILE A 590 4814 4258 4226 -63 -213 -157 C
ATOM 4936 N ASN A 591 17.716 -2.634 -43.087 1.00 37.03 N
ANISOU 4936 N ASN A 591 5013 4529 4525 -51 -135 -270 N
ATOM 4937 CA ASN A 591 19.072 -2.596 -43.597 1.00 39.74 C
ANISOU 4937 CA ASN A 591 5341 4852 4907 -17 -133 -284 C
ATOM 4938 C ASN A 591 19.069 -2.309 -45.087 1.00 40.12 C
ANISOU 4938 C ASN A 591 5367 4927 4947 -22 -107 -315 C
ATOM 4939 O ASN A 591 18.419 -3.012 -45.865 1.00 38.76 O
ANISOU 4939 O ASN A 591 5202 4762 4762 -49 -89 -339 O
ATOM 4940 CB ASN A 591 19.824 -3.896 -43.294 1.00 42.30 C
ANISOU 4940 CB ASN A 591 5688 5115 5270 0 -137 -283 C
ATOM 4941 CG ASN A 591 20.168 -4.047 -41.821 1.00 44.05 C
ANISOU 4941 CG ASN A 591 5922 5316 5497 19 -166 -244 C
ATOM 4942 OD1 ASN A 591 20.471 -3.063 -41.126 1.00 46.98 O
ANISOU 4942 OD1 ASN A 591 6273 5719 5858 29 -186 -229 O
ATOM 4943 ND2 ASN A 591 20.138 -5.284 -41.337 1.00 42.06 N
ANISOU 4943 ND2 ASN A 591 5706 5013 5260 24 -163 -230 N
ATOM 4944 N ARG A 592 19.784 -1.259 -45.463 1.00 37.02 N
ANISOU 4944 N ARG A 592 4950 4554 4561 0 -102 -317 N
ATOM 4945 CA ARG A 592 19.831 -0.807 -46.834 1.00 40.06 C
ANISOU 4945 CA ARG A 592 5315 4970 4935 1 -75 -339 C
ATOM 4946 C ARG A 592 20.975 -1.472 -47.591 1.00 40.44 C
ANISOU 4946 C ARG A 592 5356 4985 5021 15 -65 -369 C
ATOM 4947 O ARG A 592 22.141 -1.268 -47.253 1.00 45.03 O
ANISOU 4947 O ARG A 592 5927 5545 5637 41 -74 -369 O
ATOM 4948 CB ARG A 592 20.041 0.711 -46.830 1.00 37.64 C
ANISOU 4948 CB ARG A 592 4992 4693 4616 18 -64 -324 C
ATOM 4949 CG ARG A 592 19.576 1.395 -48.082 1.00 34.00 C
ANISOU 4949 CG ARG A 592 4517 4278 4123 22 -34 -329 C
ATOM 4950 CD ARG A 592 19.732 2.902 -47.997 1.00 31.45 C
ANISOU 4950 CD ARG A 592 4189 3970 3789 41 -11 -308 C
ATOM 4951 NE ARG A 592 19.363 3.521 -49.272 1.00 29.01 N
ANISOU 4951 NE ARG A 592 3869 3705 3448 54 21 -306 N
ATOM 4952 CZ ARG A 592 19.001 4.791 -49.402 1.00 29.49 C
ANISOU 4952 CZ ARG A 592 3932 3788 3484 76 52 -278 C
ATOM 4953 NH1 ARG A 592 18.907 5.561 -48.325 1.00 30.41 N
ANISOU 4953 NH1 ARG A 592 4062 3886 3604 78 56 -257 N
ATOM 4954 NH2 ARG A 592 18.693 5.283 -50.596 1.00 28.83 N
ANISOU 4954 NH2 ARG A 592 3837 3747 3367 95 84 -269 N
ATOM 4955 N LYS A 593 20.665 -2.241 -48.621 1.00 42.07 N
ANISOU 4955 N LYS A 593 5566 5196 5223 -2 -46 -399 N
ATOM 4956 CA LYS A 593 21.728 -2.707 -49.536 1.00 49.33 C
ANISOU 4956 CA LYS A 593 6475 6091 6175 10 -28 -432 C
ATOM 4957 C LYS A 593 21.314 -2.828 -51.012 1.00 48.97 C
ANISOU 4957 C LYS A 593 6418 6084 6102 -12 1 -467 C
ATOM 4958 O LYS A 593 20.180 -3.200 -51.316 1.00 46.76 O
ANISOU 4958 O LYS A 593 6144 5837 5784 -48 8 -477 O
ATOM 4959 CB LYS A 593 22.356 -4.017 -49.047 1.00 54.48 C
ANISOU 4959 CB LYS A 593 7150 6675 6873 21 -32 -438 C
ATOM 4960 CG LYS A 593 23.845 -4.138 -49.389 1.00 60.39 C
ANISOU 4960 CG LYS A 593 7881 7396 7668 59 -26 -454 C
ATOM 4961 CD LYS A 593 24.486 -5.365 -48.745 1.00 64.18 C
ANISOU 4961 CD LYS A 593 8382 7810 8191 86 -29 -447 C
ATOM 4962 CE LYS A 593 24.093 -6.650 -49.461 1.00 66.97 C
ANISOU 4962 CE LYS A 593 8768 8122 8556 62 6 -479 C
ATOM 4963 NZ LYS A 593 24.750 -6.773 -50.796 1.00 70.58 N
ANISOU 4963 NZ LYS A 593 9207 8581 9029 63 37 -524 N
ATOM 4964 N ALA A 594 22.258 -2.530 -51.913 1.00 51.13 N
ANISOU 4964 N ALA A 594 6674 6360 6394 4 18 -488 N
ATOM 4965 CA ALA A 594 22.032 -2.601 -53.376 1.00 50.97 C
ANISOU 4965 CA ALA A 594 6639 6382 6346 -14 48 -522 C
ATOM 4966 C ALA A 594 21.771 -4.014 -53.871 1.00 52.06 C
ANISOU 4966 C ALA A 594 6793 6497 6490 -49 66 -565 C
ATOM 4967 O ALA A 594 22.487 -4.951 -53.507 1.00 50.73 O
ANISOU 4967 O ALA A 594 6644 6258 6371 -39 69 -578 O
ATOM 4968 CB ALA A 594 23.199 -1.992 -54.130 1.00 50.40 C
ANISOU 4968 CB ALA A 594 6546 6308 6293 11 65 -535 C
ATOM 4969 N SER A 595 20.748 -4.150 -54.717 1.00 53.29 N
ANISOU 4969 N SER A 595 6939 6715 6592 -89 82 -588 N
ATOM 4970 CA SER A 595 20.281 -5.458 -55.198 1.00 57.62 C
ANISOU 4970 CA SER A 595 7503 7252 7135 -139 106 -638 C
ATOM 4971 C SER A 595 20.184 -5.514 -56.737 1.00 56.20 C
ANISOU 4971 C SER A 595 7299 7135 6918 -167 137 -685 C
ATOM 4972 O SER A 595 19.662 -6.481 -57.299 1.00 57.40 O
ANISOU 4972 O SER A 595 7458 7299 7052 -221 163 -736 O
ATOM 4973 CB SER A 595 18.919 -5.795 -54.559 1.00 58.61 C
ANISOU 4973 CB SER A 595 7641 7404 7223 -180 97 -631 C
ATOM 4974 OG SER A 595 18.438 -7.065 -54.977 1.00 60.21 O
ANISOU 4974 OG SER A 595 7862 7593 7419 -239 129 -685 O
ATOM 4975 N ILE A 596 20.672 -4.467 -57.402 1.00 52.59 N
ANISOU 4975 N ILE A 596 6815 6721 6446 -135 137 -670 N
ATOM 4976 CA ILE A 596 20.788 -4.451 -58.866 1.00 52.39 C
ANISOU 4976 CA ILE A 596 6765 6753 6386 -152 166 -710 C
ATOM 4977 C ILE A 596 22.123 -3.832 -59.355 1.00 52.94 C
ANISOU 4977 C ILE A 596 6825 6797 6492 -109 177 -706 C
ATOM 4978 O ILE A 596 22.612 -4.137 -60.458 1.00 51.16 O
ANISOU 4978 O ILE A 596 6590 6585 6264 -123 206 -749 O
ATOM 4979 CB ILE A 596 19.555 -3.789 -59.571 1.00 50.28 C
ANISOU 4979 CB ILE A 596 6464 6611 6027 -171 165 -699 C
ATOM 4980 CG1 ILE A 596 19.526 -2.256 -59.413 1.00 48.36 C
ANISOU 4980 CG1 ILE A 596 6205 6408 5760 -115 151 -634 C
ATOM 4981 CG2 ILE A 596 18.245 -4.429 -59.129 1.00 51.79 C
ANISOU 4981 CG2 ILE A 596 6657 6840 6181 -220 157 -711 C
ATOM 4982 CD1 ILE A 596 19.222 -1.767 -58.020 1.00 47.53 C
ANISOU 4982 CD1 ILE A 596 6116 6266 5674 -91 123 -582 C
TER 4983 ILE A 596
ATOM 9967 N CYS C 601 23.393 7.687 -27.103 1.00 45.67 C
ATOM 9968 CA CYS C 601 23.279 8.880 -25.002 1.00 42.96 C
ATOM 9969 C CYS C 601 22.702 9.961 -25.669 1.00 46.11 C
ATOM 9970 O CYS C 601 23.626 7.742 -25.724 1.00 47.79 C
ATOM 9971 CB CYS C 601 24.648 6.148 -34.078 1.00 51.71 N
ATOM 9972 N CYS C 601 22.640 7.167 -34.299 1.00 50.41 O
ATOM 9973 CA CYS C 601 23.584 6.802 -33.616 1.00 52.65 C
ATOM 9974 C CYS C 601 24.877 5.733 -35.395 1.00 56.66 C
ATOM 9975 O CYS C 601 23.910 5.877 -36.393 1.00 51.36 C
ATOM 9976 CB CYS C 601 24.174 5.416 -37.677 1.00 51.23 C
ATOM 9977 CG CYS C 601 25.378 4.785 -37.968 1.00 52.22 C
ATOM 9978 CD1 CYS C 601 26.337 4.627 -36.974 1.00 55.05 C
ATOM 9979 CD2 CYS C 601 26.087 5.093 -35.682 1.00 57.44 C
ATOM 9980 CA CYS C 601 27.124 4.899 -34.604 1.00 60.92 C
ATOM 9981 C CYS C 601 28.000 4.019 -34.757 1.00 67.00 O
ATOM 9982 O CYS C 601 27.099 5.614 -33.578 1.00 63.88 O
ATOM 9983 CB CYS C 601 23.650 7.014 -32.145 1.00 50.33 C
ATOM 9984 OG CYS C 601 22.672 7.487 -31.350 1.00 48.91 C
ATOM 9985 N CYS C 601 21.334 7.915 -31.903 1.00 48.34 C
ATOM 9986 CA CYS C 601 22.932 7.578 -29.866 1.00 48.23 C
ATOM 9987 C CYS C 601 23.507 6.483 -29.196 1.00 48.28 C
ATOM 9988 O CYS C 601 23.744 6.540 -27.823 1.00 48.28 C
ATOM 9989 CB CYS C 601 22.809 8.776 -27.764 1.00 45.97 C
ATOM 9990 CG1 CYS C 601 22.582 8.722 -29.146 1.00 45.44 C
ATOM 9991 CG2 CYS C 601 22.464 9.920 -27.045 1.00 43.13 C
HETATM10017 O HOH A 701 20.948 13.940 -61.869 1.00 44.50 O
HETATM10018 O HOH A 702 -3.632 -6.009 -30.429 1.00 38.75 O
HETATM10019 O HOH A 703 25.202 16.459 -69.877 1.00 37.74 O
HETATM10020 O HOH A 704 29.024 18.936 -63.133 1.00 41.39 O
HETATM10021 O HOH A 705 10.168 9.553 -17.435 1.00 30.77 O
HETATM10022 O HOH A 706 19.031 -2.391 -55.091 1.00 54.90 O
HETATM10023 O HOH A 707 -7.537 4.293 -67.407 1.00 60.65 O
HETATM10024 O HOH A 708 13.542 -1.639 -50.962 1.00 47.49 O
HETATM10025 O HOH A 709 27.273 17.813 -39.940 1.00 52.60 O
HETATM10026 O HOH A 710 13.672 1.312 -16.379 1.00 39.26 O
HETATM10027 O HOH A 711 12.568 -8.344 -35.241 1.00 43.31 O
HETATM10028 O HOH A 712 -9.202 10.799 -15.524 1.00 41.58 O
HETATM10029 O HOH A 713 3.853 -12.265 -29.616 1.00 47.84 O
HETATM10030 O HOH A 714 37.125 5.981 -80.022 1.00 48.72 O
HETATM10031 O HOH A 715 13.056 7.624 -45.079 1.00 32.01 O
HETATM10032 O HOH A 716 -35.897 -7.069 -41.100 1.00 57.66 O
HETATM10033 O HOH A 717 1.349 -2.874 -15.213 1.00 39.30 O
HETATM10034 O HOH A 718 19.445 18.713 -28.495 1.00 34.54 O
HETATM10035 O HOH A 719 -14.459 -8.260 -52.684 1.00 49.83 O
HETATM10036 O HOH A 720 27.844 16.396 -45.834 1.00 41.78 O
HETATM10037 O HOH A 721 8.373 21.790 -45.402 1.00 48.90 O
HETATM10038 O HOH A 722 14.295 -4.491 -22.593 1.00 46.92 O
HETATM10039 O HOH A 723 -7.772 -10.038 -23.232 1.00 53.07 O
HETATM10040 O HOH A 724 7.038 -7.328 -39.868 1.00 40.34 O
HETATM10041 O HOH A 725 -28.952 -5.869 -31.492 1.00 61.33 O
HETATM10042 O HOH A 726 11.327 10.067 -49.465 1.00 37.11 O
HETATM10043 O HOH A 727 30.745 10.674 -52.109 1.00 44.45 O
HETATM10044 O HOH A 728 35.343 3.708 -60.534 1.00 24.00 O
HETATM10045 O HOH A 729 14.967 5.912 -48.660 1.00 34.57 O
HETATM10046 O HOH A 730 15.427 25.347 -49.184 1.00 32.09 O
HETATM10047 O HOH A 731 29.158 6.713 -81.333 1.00 38.11 O
HETATM10048 O HOH A 732 3.786 2.929 -41.772 1.00 44.77 O
HETATM10049 O HOH A 733 13.448 2.609 -39.358 1.00 31.74 O
HETATM10050 O HOH A 734 23.459 13.222 -24.498 1.00 44.71 O
HETATM10051 O HOH A 735 -11.056 8.640 -25.110 1.00 35.05 O
HETATM10052 O HOH A 736 24.765 -3.971 -72.490 1.00 38.66 O
HETATM10053 O HOH A 737 32.163 3.857 -78.808 1.00 28.96 O
HETATM10054 O HOH A 738 9.020 -2.207 -25.643 1.00 32.10 O
HETATM10055 O HOH A 739 30.223 18.760 -70.970 1.00 40.10 O
HETATM10056 O HOH A 740 -12.440 0.535 -21.144 1.00 34.20 O
HETATM10057 O HOH A 741 -2.250 3.336 -34.649 1.00 37.53 O
HETATM10058 O HOH A 742 13.101 17.740 -44.414 1.00 34.52 O
HETATM10059 O HOH A 743 14.330 18.995 -46.288 1.00 33.20 O
HETATM10060 O HOH A 744 44.445 19.280 -50.978 1.00 65.32 O
HETATM10061 O HOH A 745 -3.521 -0.468 -33.965 1.00 43.14 O
HETATM10062 O HOH A 746 25.230 20.302 -49.192 1.00 36.03 O
HETATM10063 O HOH A 747 11.054 -2.197 -49.960 1.00 41.15 O
HETATM10064 O HOH A 748 25.545 3.845 -49.226 1.00 31.29 O
HETATM10065 O HOH A 749 3.948 5.251 -16.309 1.00 46.97 O
HETATM10066 O HOH A 750 13.856 0.531 -43.977 1.00 30.46 O
HETATM10067 O HOH A 751 -2.979 -3.498 -36.941 1.00 49.56 O
HETATM10068 O HOH A 752 34.302 -3.831 -61.452 1.00 35.55 O
HETATM10069 O HOH A 753 14.621 1.513 -54.087 1.00 39.26 O
HETATM10070 O HOH A 754 12.790 -5.455 -30.380 1.00 33.93 O
HETATM10071 O HOH A 755 -15.956 -2.644 -24.912 1.00 43.17 O
HETATM10072 O HOH A 756 20.263 6.054 -70.170 1.00 35.95 O
HETATM10073 O HOH A 757 -10.984 -4.228 -14.549 1.00 47.23 O
HETATM10074 O HOH A 758 42.556 3.508 -49.734 1.00 45.39 O
HETATM10075 O HOH A 759 29.346 9.113 -49.653 1.00 38.36 O
HETATM10076 O HOH A 760 31.673 12.312 -48.237 1.00 45.39 O
HETATM10077 O HOH A 761 29.201 9.586 -74.471 1.00 37.01 O
HETATM10078 O HOH A 762 13.712 -7.269 -62.974 1.00 55.64 O
HETATM10079 O HOH A 763 -15.548 9.282 -43.407 1.00 48.08 O
HETATM10080 O HOH A 764 43.028 16.389 -73.574 1.00 45.20 O
HETATM10081 O HOH A 765 -10.805 -6.831 -30.003 1.00 38.88 O
HETATM10082 O HOH A 766 14.036 9.724 -55.928 1.00 24.62 O
HETATM10083 O HOH A 767 11.390 2.349 -15.495 1.00 33.68 O
HETATM10084 O HOH A 768 18.978 -3.583 -22.291 1.00 40.86 O
HETATM10085 O HOH A 769 24.629 10.179 -74.978 1.00 35.57 O
HETATM10086 O HOH A 770 -1.381 -2.808 -14.068 1.00 31.27 O
HETATM10087 O HOH A 771 -0.133 -6.042 -33.754 1.00 49.88 O
HETATM10088 O HOH A 772 3.514 -6.278 -29.480 1.00 35.24 O
HETATM10089 O HOH A 773 14.812 11.875 -55.570 1.00 23.84 O
HETATM10090 O HOH A 774 23.764 5.189 -21.176 1.00 38.50 O
HETATM10091 O HOH A 775 17.544 9.072 -46.497 1.00 40.14 O
HETATM10092 O HOH A 776 4.010 -4.608 -20.203 1.00 30.35 O
HETATM10093 O HOH A 777 26.699 18.390 -67.157 1.00 51.86 O
HETATM10094 O HOH A 778 6.376 -5.270 -19.704 1.00 37.24 O
HETATM10095 O HOH A 779 19.864 9.824 -48.506 1.00 36.87 O
HETATM10096 O HOH A 780 23.672 -0.441 -77.538 1.00 49.46 O
HETATM10097 O HOH A 781 15.685 -9.657 -62.915 1.00 72.71 O
HETATM10098 O HOH A 782 -2.238 4.451 -14.946 1.00 46.74 O
HETATM10099 O HOH A 783 7.964 17.770 -47.892 1.00 48.94 O
HETATM10100 O HOH A 784 29.598 6.965 -34.000 1.00 59.35 O
HETATM10101 O HOH A 785 39.151 1.288 -62.747 1.00 40.03 O
HETATM10102 O HOH A 786 -3.432 5.808 -17.432 1.00 33.23 O
HETATM10103 O HOH A 787 -9.214 0.472 -66.958 1.00 61.61 O
HETATM10104 O HOH A 788 24.793 21.977 -46.677 1.00 35.82 O
HETATM10105 O HOH A 789 11.093 -4.230 -26.348 1.00 37.10 O
HETATM10106 O HOH A 790 37.189 1.226 -60.260 1.00 27.93 O
HETATM10107 O HOH A 791 31.131 2.634 -82.911 1.00 63.19 O
HETATM10108 O HOH A 792 12.564 12.411 -48.839 1.00 33.98 O
HETATM10109 O HOH A 793 20.325 8.122 -45.505 1.00 34.43 O
HETATM10110 O HOH A 794 13.429 15.265 -42.087 1.00 25.14 O
HETATM10111 O HOH A 795 22.323 6.436 -72.359 1.00 38.76 O
HETATM10112 O HOH A 796 -9.850 -0.859 -21.295 1.00 47.35 O
HETATM10113 O HOH A 797 20.859 15.960 -25.503 1.00 43.02 O
HETATM10114 O HOH A 798 17.837 13.488 -19.025 1.00 43.14 O
HETATM10115 O HOH A 799 21.504 0.111 -43.633 1.00 45.64 O
HETATM10116 O HOH A 800 12.976 9.169 -46.873 1.00 40.30 O
HETATM10117 O HOH A 801 -5.624 4.849 -40.875 1.00 45.75 O
HETATM10118 O HOH A 802 4.636 -1.795 -16.439 1.00 40.99 O
HETATM10119 O HOH A 803 24.559 -3.064 -57.994 1.00 49.49 O
HETATM10120 O HOH A 804 23.135 13.854 -19.918 1.00 52.16 O
HETATM10121 O HOH A 805 6.002 8.084 -17.163 1.00 31.56 O
HETATM10122 O HOH A 806 14.250 3.458 -67.692 1.00 47.14 O
HETATM10123 O HOH A 807 7.868 -4.798 -51.242 1.00 46.51 O
HETATM10124 O HOH A 808 37.572 0.274 -68.986 1.00 44.87 O
HETATM10125 O HOH A 809 42.025 18.102 -69.049 1.00 41.74 O
HETATM10126 O HOH A 810 1.067 2.009 -48.149 1.00 45.07 O
HETATM10127 O HOH A 811 12.531 16.077 -52.603 1.00 42.47 O
HETATM10128 O HOH A 812 9.616 -3.033 -22.953 1.00 30.38 O
HETATM10129 O HOH A 813 16.928 6.020 -43.616 1.00 28.69 O
HETATM10130 O HOH A 814 27.722 -4.621 -58.442 1.00 57.62 O
HETATM10131 O HOH A 815 22.743 -9.317 -68.774 1.00 47.90 O
HETATM10132 O HOH A 816 20.589 19.100 -57.172 1.00 36.63 O
HETATM10133 O HOH A 817 7.250 10.998 -43.570 1.00 30.90 O
HETATM10134 O HOH A 818 -4.317 -1.509 -11.233 1.00 44.84 O
HETATM10135 O HOH A 819 20.210 -5.757 -32.580 1.00 46.80 O
HETATM10136 O HOH A 820 26.534 18.101 -64.093 1.00 41.75 O
HETATM10137 O HOH A 821 -1.057 22.207 -24.005 1.00 47.53 O
HETATM10138 O HOH A 822 0.890 -7.720 -35.118 1.00 29.33 O
HETATM10139 O HOH A 823 26.375 -3.089 -80.343 1.00 42.07 O
HETATM10140 O HOH A 824 8.150 7.987 -18.698 1.00 42.88 O
HETATM10141 O HOH A 825 -8.631 -7.184 -48.113 1.00 54.60 O
HETATM10142 O HOH A 826 -3.254 5.652 -12.482 1.00 58.40 O
HETATM10143 O HOH A 827 -3.259 3.485 -17.773 1.00 44.73 O
HETATM10144 O HOH A 828 13.193 7.831 -65.269 1.00 62.26 O
HETATM10145 O HOH A 829 39.408 2.836 -68.535 1.00 44.71 O
HETATM10146 O HOH A 830 16.398 0.464 -45.007 1.00 38.87 O
HETATM10147 O HOH A 831 43.660 15.807 -68.271 1.00 56.20 O
HETATM10148 O HOH A 832 26.765 -2.381 -49.369 1.00 47.91 O
HETATM10149 O HOH A 833 11.901 18.440 -57.213 1.00 45.93 O
HETATM10150 O HOH A 834 10.513 14.906 -42.398 1.00 38.66 O
HETATM10151 O HOH A 835 10.023 13.493 -21.861 1.00 39.55 O
HETATM10152 O HOH A 836 27.305 -4.635 -70.871 1.00 42.07 O
HETATM10153 O HOH A 837 -10.356 -11.757 -37.565 1.00 43.17 O
HETATM10154 O HOH A 838 -19.644 -0.642 -28.224 1.00 33.20 O
HETATM10155 O HOH A 839 9.860 17.732 -52.227 1.00 37.66 O
HETATM10156 O HOH A 840 3.308 7.996 -42.074 1.00 54.18 O
HETATM10157 O HOH A 841 18.004 -6.671 -36.275 1.00 39.03 O
HETATM10158 O HOH A 842 19.531 8.789 -70.079 1.00 44.09 O
HETATM10159 O HOH A 843 4.444 19.133 -34.830 1.00 44.21 O
HETATM10160 O HOH A 844 -3.236 -5.253 -58.411 1.00 59.20 O
HETATM10161 O HOH A 845 25.130 26.561 -43.186 1.00 44.76 O
HETATM10162 O HOH A 846 27.808 -7.078 -64.567 1.00 38.50 O
HETATM10163 O HOH A 847 10.173 1.390 -13.175 1.00 43.65 O
HETATM10164 O HOH A 848 17.263 -6.063 -42.157 1.00 27.45 O
HETATM10165 O HOH A 849 2.306 -9.130 -31.356 1.00 45.36 O
HETATM10166 O HOH A 850 9.988 -8.012 -30.942 1.00 38.47 O
HETATM10167 O HOH A 851 15.340 -0.539 -52.040 1.00 33.56 O
HETATM10168 O HOH A 852 14.181 7.203 -59.870 1.00 45.04 O
HETATM10169 O HOH A 853 2.294 18.571 -29.018 1.00 39.47 O
HETATM10170 O HOH A 854 -11.420 10.193 -38.286 1.00 55.53 O
HETATM10171 O HOH A 855 -7.631 -4.939 -30.192 1.00 57.66 O
HETATM10172 O HOH A 856 10.852 12.018 -56.887 1.00 37.24 O
HETATM10173 O HOH A 857 5.948 3.452 -64.885 1.00 58.52 O
HETATM10174 O HOH A 858 -7.731 -0.552 -46.254 1.00 45.11 O
HETATM10175 O HOH A 859 19.224 4.310 -45.298 1.00 47.53 O
HETATM10176 O HOH A 860 -14.332 9.712 -40.079 1.00 56.56 O
HETATM10177 O HOH A 861 12.699 -1.963 -53.210 1.00 36.41 O
HETATM10178 O HOH A 862 25.332 -0.502 -47.703 1.00 54.53 O
HETATM10179 O HOH A 863 27.398 20.780 -37.685 1.00 45.99 O
HETATM10180 O HOH A 864 -10.293 -11.608 -56.609 1.00 75.21 O
HETATM10181 O HOH A 865 -9.351 13.158 -35.465 1.00 50.82 O
HETATM10182 O HOH A 866 11.783 22.729 -40.553 1.00 30.13 O
HETATM10183 O HOH A 867 14.388 2.606 -42.027 1.00 34.75 O
HETATM10184 O HOH A 868 14.919 -3.205 -56.624 1.00 41.35 O
HETATM10185 O HOH A 869 -17.141 4.975 -75.056 1.00 66.61 O
HETATM10186 O HOH A 870 19.800 24.957 -41.712 1.00 30.60 O
HETATM10187 O HOH A 871 21.331 28.173 -45.727 1.00 46.02 O
HETATM10188 O HOH A 872 9.680 -5.630 -21.879 1.00 52.91 O
HETATM10189 O HOH A 873 -15.190 0.382 -19.251 1.00 47.08 O
HETATM10190 O HOH A 874 17.806 12.868 -70.356 1.00 51.78 O
HETATM10191 O HOH A 875 -19.896 -11.329 -59.590 1.00 60.83 O
HETATM10192 O HOH A 876 6.271 13.331 -16.099 1.00 52.37 O
HETATM10193 O HOH A 877 1.196 4.556 -48.198 1.00 42.28 O
HETATM10194 O HOH A 878 24.069 1.320 -45.855 1.00 48.19 O
HETATM10195 O HOH A 879 13.915 14.635 -60.042 1.00 53.21 O
HETATM10196 O HOH A 880 -21.792 11.133 -51.985 1.00 66.48 O
HETATM10197 O HOH A 881 12.565 -2.923 -23.232 1.00 42.49 O
HETATM10198 O HOH A 882 -19.972 11.386 -34.091 1.00 59.56 O
HETATM10199 O HOH A 883 -5.908 -0.497 -19.486 1.00 27.62 O
HETATM10200 O HOH A 884 -19.862 2.442 -21.840 1.00 58.01 O
HETATM10201 O HOH A 885 1.168 5.176 -14.814 1.00 40.04 O
HETATM10202 O HOH A 886 8.461 15.141 -19.965 1.00 33.05 O
HETATM10203 O HOH A 887 4.880 8.973 -53.146 1.00 60.81 O
HETATM10204 O HOH A 888 12.263 1.272 -69.553 1.00 59.98 O
HETATM10205 O HOH A 889 27.963 -3.436 -51.882 1.00 44.90 O
HETATM10206 O HOH A 890 -33.575 26.583 -65.818 1.00 70.93 O
HETATM10207 O HOH A 891 40.240 -1.738 -56.633 1.00 63.78 O
HETATM10208 O HOH A 892 6.366 12.989 -44.669 1.00 47.90 O
HETATM10209 O HOH A 893 12.000 7.939 -61.092 1.00 48.36 O
HETATM10210 O HOH A 894 -7.736 -4.143 -47.033 1.00 47.93 O
HETATM10211 O HOH A 895 26.308 -5.745 -68.928 1.00 41.74 O
HETATM10212 O HOH A 896 15.555 7.146 -45.952 1.00 34.57 O
HETATM10213 O HOH A 897 29.676 -1.834 -49.233 1.00 38.96 O
HETATM10214 O HOH A 898 8.944 18.708 -29.910 1.00 34.94 O
HETATM10215 O HOH A 899 -0.029 -9.387 -30.434 1.00 45.87 O
HETATM10216 O HOH A 900 13.203 5.468 -66.518 1.00 43.95 O
HETATM10217 O HOH A 901 40.215 20.699 -64.077 1.00 51.68 O
HETATM10218 O HOH A 902 13.190 13.914 -56.583 1.00 41.21 O
HETATM10219 O HOH A 903 -3.176 -6.050 -27.819 1.00 59.51 O
HETATM10220 O HOH A 904 0.425 -12.329 -20.585 1.00 50.98 O
HETATM10221 O HOH A 905 16.651 3.329 -42.727 1.00 30.48 O
HETATM10222 O HOH A 906 24.189 2.236 -77.765 1.00 46.05 O
HETATM10223 O HOH A 907 -5.444 22.581 -26.425 1.00 55.79 O
HETATM10224 O HOH A 908 17.815 20.324 -27.519 1.00 38.40 O
HETATM10225 O HOH A 909 12.238 16.218 -55.352 1.00 48.06 O
HETATM10226 O HOH A 910 23.357 19.645 -58.368 1.00 36.71 O
CONECT 9967 9970 9988 9989
CONECT 9968 9969 9970
CONECT 9969 9968 9991
CONECT 9970 9967 9968
CONECT 9971 9973 9974
CONECT 9972 9973
CONECT 9973 9971 9972 9983
CONECT 9974 9971 9975 9979
CONECT 9975 9974 9976
CONECT 9976 9975 9977
CONECT 9977 9976 9978
CONECT 9978 9977 9979
CONECT 9979 9974 9978 9980
CONECT 9980 9979 9981 9982
CONECT 9981 9980
CONECT 9982 9980
CONECT 9983 9973 9984
CONECT 9984 9983 9985 9986
CONECT 9985 9984
CONECT 9986 9984 9987 9990
CONECT 9987 9986 9988
CONECT 9988 9967 9987
CONECT 9989 9967 9990 9991
CONECT 9990 9986 9989
CONECT 9991 9969 9989
CONECT 9992 99951001310014
CONECT 9993 9994 9995
CONECT 9994 999310016
CONECT 9995 9992 9993
CONECT 9996 9998 9999
CONECT 9997 9998
CONECT 9998 9996 999710008
CONECT 9999 99961000010004
CONECT10000 999910001
CONECT100011000010002
CONECT100021000110003
CONECT100031000210004
CONECT10004 99991000310005
CONECT10005100041000610007
CONECT1000610005
CONECT1000710005
CONECT10008 999810009
CONECT10009100081001010011
CONECT1001010009
CONECT10011100091001210015
CONECT100121001110013
CONECT10013 999210012
CONECT10014 99921001510016
CONECT100151001110014
CONECT10016 999410014
MASTER 371 0 2 55 32 0 5 610423 2 50 92
END
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