HEADER MEMBRANE PROTEIN 06-JUN-22 8A2P
TITLE ROOM-TEMPERATURE STRUCTURE OF THE STABILISED A2A-LUAA47070 COMPLEX
TITLE 2 DETERMINED BY SYNCHROTRON SERIAL CRYSTALLOGRAPHY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOCHROME B-562;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADORA2A, ADORA2, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BAC TO BAC
KEYWDS ADENOSINE RECEPTOR A2A, SOLUBLE CYTOCHROME B562, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR I.MORAES,T.O.C.KWAN,D.AXFORD
REVDAT 2 18-OCT-23 8A2P 1 JRNL
REVDAT 1 30-AUG-23 8A2P 0
JRNL AUTH J.BIRCH,T.O.C.KWAN,P.J.JUDGE,D.AXFORD,P.ALLER,A.BUTRYN,
JRNL AUTH 2 R.I.REIS,J.F.BADA JUAREZ,J.VINALS,R.L.OWEN,E.NANGO,R.TANAKA,
JRNL AUTH 3 K.TONO,Y.JOTI,T.TANAKA,S.OWADA,M.SUGAHARA,S.IWATA,
JRNL AUTH 4 A.M.ORVILLE,A.WATTS,I.MORAES
JRNL TITL A VERSATILE APPROACH TO HIGH-DENSITY MICROCRYSTALS IN
JRNL TITL 2 LIPIDIC CUBIC PHASE FOR ROOM-TEMPERATURE SERIAL
JRNL TITL 3 CRYSTALLOGRAPHY.
JRNL REF J.APPL.CRYSTALLOGR. V. 56 1361 2023
JRNL REFN ISSN 0021-8898
JRNL PMID 37791355
JRNL DOI 10.1107/S1600576723006428
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 90.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 6398
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 696
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) : 3.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 469
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2986
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 164
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 84.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 118.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.60000
REMARK 3 B22 (A**2) : -2.08000
REMARK 3 B33 (A**2) : 0.48000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.632
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.394
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 57.019
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
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): 3246 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4421 ; 1.466 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 388 ; 3.702 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 123 ;41.262 ;23.577
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 504 ;13.264 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;10.895 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 522 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2337 ; 0.004 ; 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): 3245 ; 0.757 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 1 ;36.002 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3183 ;17.791 ; 5.000
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 : 1
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 : NULL 0 NULL 0
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8510 -17.2520 18.6620
REMARK 3 T TENSOR
REMARK 3 T11: 0.3765 T22: 0.3200
REMARK 3 T33: 0.3293 T12: 0.0255
REMARK 3 T13: 0.0126 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.3621 L22: 0.2747
REMARK 3 L33: 0.1460 L12: 0.1662
REMARK 3 L13: 0.1697 L23: -0.0176
REMARK 3 S TENSOR
REMARK 3 S11: -0.0147 S12: 0.0169 S13: -0.0559
REMARK 3 S21: -0.0678 S22: 0.0150 S23: -0.1480
REMARK 3 S31: 0.0806 S32: -0.0409 S33: -0.0002
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: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN USED IF PRESENT IN THE INPUT
REMARK 4
REMARK 4 8A2P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUN-22.
REMARK 100 THE DEPOSITION ID IS D_1292123412.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-19
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 4.0-5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96862
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : DIALS 1.10.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7126
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 90.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 88.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 36.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.110
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER V3.24
REMARK 200 STARTING MODEL: 5OLV
REMARK 200
REMARK 200 REMARK: PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM CITRATE PH 4.5, 0.05
REMARK 280 M SODIUM THIOCYANATE, 29% (V/V) POLYETHYLENE GLYCOL 400, 2% (V/V)
REMARK 280 2,5-HEXANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.31900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.31900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 20.21850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.91950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 20.21850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.91950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.31900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 20.21850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.91950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.31900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 20.21850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.91950
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1043
REMARK 465 THR A 1044
REMARK 465 PRO A 1045
REMARK 465 PRO A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 PRO A 1056
REMARK 465 GLU A 1057
REMARK 465 MET A 1058
REMARK 465 HIS A 306
REMARK 465 VAL A 307
REMARK 465 LEU A 308
REMARK 465 ARG A 309
REMARK 465 GLN A 310
REMARK 465 GLN A 311
REMARK 465 GLU A 312
REMARK 465 PRO A 313
REMARK 465 PHE A 314
REMARK 465 LYS A 315
REMARK 465 ALA A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 58 -52.32 -124.16
REMARK 500 TYR A1101 -46.41 -136.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLA A 1206
REMARK 610 OLA A 1207
REMARK 610 OLA A 1208
DBREF 8A2P A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 8A2P A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 8A2P A 219 316 UNP P29274 AA2AR_HUMAN 219 316
SEQADV 8A2P ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 8A2P PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 8A2P LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION
SEQADV 8A2P ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION
SEQADV 8A2P ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION
SEQADV 8A2P ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION
SEQADV 8A2P ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION
SEQADV 8A2P ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION
SEQADV 8A2P TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 8A2P ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 8A2P LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 8A2P ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION
SEQADV 8A2P ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION
SEQADV 8A2P ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION
SEQADV 8A2P HIS A 317 UNP P29274 EXPRESSION TAG
SEQADV 8A2P HIS A 318 UNP P29274 EXPRESSION TAG
SEQADV 8A2P HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 8A2P HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 8A2P HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 8A2P HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 8A2P HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 8A2P HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 8A2P HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 8A2P HIS A 326 UNP P29274 EXPRESSION TAG
SEQRES 1 A 423 ALA PRO PRO ILE MET GLY SER SER VAL TYR ILE THR VAL
SEQRES 2 A 423 GLU LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL
SEQRES 3 A 423 LEU VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN
SEQRES 4 A 423 ASN VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA
SEQRES 5 A 423 ASP ILE LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE
SEQRES 6 A 423 THR ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS
SEQRES 7 A 423 LEU PHE ILE ALA CYS PHE VAL LEU VAL LEU ALA GLN SER
SEQRES 8 A 423 SER ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR
SEQRES 9 A 423 ILE ALA ILE ALA ILE PRO LEU ARG TYR ASN GLY LEU VAL
SEQRES 10 A 423 THR GLY THR ARG ALA ALA GLY ILE ILE ALA ILE CYS TRP
SEQRES 11 A 423 VAL LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY
SEQRES 12 A 423 TRP ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS
SEQRES 13 A 423 SER GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE
SEQRES 14 A 423 GLU ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN
SEQRES 15 A 423 PHE PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU
SEQRES 16 A 423 GLY VAL TYR LEU ARG ILE PHE ALA ALA ALA ARG ARG GLN
SEQRES 17 A 423 LEU ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP
SEQRES 18 A 423 ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN
SEQRES 19 A 423 VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU
SEQRES 20 A 423 ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS
SEQRES 21 A 423 SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY
SEQRES 22 A 423 PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS
SEQRES 23 A 423 LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA
SEQRES 24 A 423 ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN
SEQRES 25 A 423 LYS TYR LEU GLU ARG ALA ARG SER THR LEU GLN LYS GLU
SEQRES 26 A 423 VAL HIS ALA ALA LYS SER ALA ALA ILE ILE ALA GLY LEU
SEQRES 27 A 423 PHE ALA LEU CYS TRP LEU PRO LEU HIS ILE ILE ASN CYS
SEQRES 28 A 423 PHE THR PHE PHE CYS PRO ASP CYS SER HIS ALA PRO LEU
SEQRES 29 A 423 TRP LEU MET TYR LEU ALA ILE VAL LEU ALA HIS THR ASN
SEQRES 30 A 423 SER VAL VAL ASN PRO PHE ILE TYR ALA TYR ARG ILE ARG
SEQRES 31 A 423 GLU PHE ARG GLN THR PHE ARG LYS ILE ILE ARG SER HIS
SEQRES 32 A 423 VAL LEU ARG GLN GLN GLU PRO PHE LYS ALA HIS HIS HIS
SEQRES 33 A 423 HIS HIS HIS HIS HIS HIS HIS
HET 9Y2 A1201 24
HET CLR A1202 28
HET CLR A1203 28
HET CLR A1204 28
HET OLA A1205 20
HET OLA A1206 18
HET OLA A1207 8
HET OLA A1208 9
HET NA A1209 1
HETNAM 9Y2 4-(3,3-DIMETHYLBUTANOYLAMINO)-3,5-BIS(FLUORANYL)-~{N}-
HETNAM 2 9Y2 (1,3-THIAZOL-2-YL)BENZAMIDE
HETNAM CLR CHOLESTEROL
HETNAM OLA OLEIC ACID
HETNAM NA SODIUM ION
FORMUL 2 9Y2 C16 H17 F2 N3 O2 S
FORMUL 3 CLR 3(C27 H46 O)
FORMUL 6 OLA 4(C18 H34 O2)
FORMUL 10 NA NA 1+
FORMUL 11 HOH *12(H2 O)
HELIX 1 AA1 PRO A 1 ASN A 34 1 34
HELIX 2 AA2 ASN A 39 LEU A 58 1 20
HELIX 3 AA3 LEU A 58 THR A 68 1 11
HELIX 4 AA4 CYS A 74 ILE A 108 1 35
HELIX 5 AA5 ARG A 111 VAL A 116 1 6
HELIX 6 AA6 THR A 117 LEU A 137 1 21
HELIX 7 AA7 THR A 138 GLY A 142 5 5
HELIX 8 AA8 LYS A 150 GLN A 157 1 8
HELIX 9 AA9 LEU A 167 VAL A 172 1 6
HELIX 10 AB1 PRO A 173 TYR A 179 1 7
HELIX 11 AB2 VAL A 186 LEU A 208 1 23
HELIX 12 AB3 ASP A 1002 LYS A 1019 1 18
HELIX 13 AB4 ASN A 1022 LYS A 1042 1 21
HELIX 14 AB5 ASP A 1060 GLU A 1081 1 22
HELIX 15 AB6 LYS A 1083 ASN A 1099 1 17
HELIX 16 AB7 TYR A 1101 LEU A 1106 1 6
HELIX 17 AB8 ARG A 220 CYS A 259 1 40
HELIX 18 AB9 PRO A 266 ILE A 292 1 27
HELIX 19 AC1 ILE A 292 SER A 305 1 14
SHEET 1 AA1 2 CYS A 71 ALA A 73 0
SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72
SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03
LINK OD1 ASP A 52 NA NA A1209 1555 1555 2.62
CRYST1 40.437 181.839 144.638 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.024730 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005499 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006914 0.00000
ATOM 1 N ALA A 0 -22.259 22.589 0.325 1.00148.93 N
ANISOU 1 N ALA A 0 18824 18604 19159 -104 -857 486 N
ATOM 2 CA ALA A 0 -23.326 21.643 -0.081 1.00151.33 C
ANISOU 2 CA ALA A 0 19158 18935 19404 -121 -832 473 C
ATOM 3 C ALA A 0 -24.329 21.472 1.051 1.00155.17 C
ANISOU 3 C ALA A 0 19627 19416 19915 -70 -847 421 C
ATOM 4 O ALA A 0 -23.959 21.583 2.220 1.00160.55 O
ANISOU 4 O ALA A 0 20283 20084 20633 -18 -844 383 O
ATOM 5 CB ALA A 0 -22.724 20.305 -0.468 1.00142.76 C
ANISOU 5 CB ALA A 0 18112 17886 18246 -139 -746 463 C
ATOM 6 N PRO A 1 -25.603 21.226 0.711 1.00153.12 N
ANISOU 6 N PRO A 1 19378 19167 19634 -85 -865 419 N
ATOM 7 CA PRO A 1 -26.591 20.949 1.742 1.00148.31 C
ANISOU 7 CA PRO A 1 18753 18559 19040 -39 -872 368 C
ATOM 8 C PRO A 1 -26.210 19.728 2.575 1.00144.98 C
ANISOU 8 C PRO A 1 18345 18160 18581 -6 -800 322 C
ATOM 9 O PRO A 1 -25.628 18.771 2.055 1.00142.46 O
ANISOU 9 O PRO A 1 18060 17865 18205 -30 -740 328 O
ATOM 10 CB PRO A 1 -27.867 20.681 0.945 1.00147.99 C
ANISOU 10 CB PRO A 1 18730 18532 18967 -74 -890 384 C
ATOM 11 CG PRO A 1 -27.677 21.449 -0.312 1.00149.79 C
ANISOU 11 CG PRO A 1 18967 18749 19198 -130 -930 446 C
ATOM 12 CD PRO A 1 -26.221 21.304 -0.623 1.00151.80 C
ANISOU 12 CD PRO A 1 19234 19009 19432 -145 -886 465 C
ATOM 13 N PRO A 2 -26.512 19.759 3.878 1.00141.99 N
ANISOU 13 N PRO A 2 17939 17775 18235 48 -807 273 N
ATOM 14 CA PRO A 2 -26.182 18.613 4.724 1.00138.70 C
ANISOU 14 CA PRO A 2 17534 17380 17785 78 -744 231 C
ATOM 15 C PRO A 2 -27.022 17.371 4.421 1.00135.20 C
ANISOU 15 C PRO A 2 17124 16970 17277 61 -703 218 C
ATOM 16 O PRO A 2 -26.552 16.252 4.636 1.00139.60 O
ANISOU 16 O PRO A 2 17704 17547 17791 65 -642 200 O
ATOM 17 CB PRO A 2 -26.476 19.122 6.139 1.00137.83 C
ANISOU 17 CB PRO A 2 17385 17256 17729 136 -773 186 C
ATOM 18 CG PRO A 2 -26.526 20.609 6.025 1.00138.55 C
ANISOU 18 CG PRO A 2 17442 17311 17888 138 -846 206 C
ATOM 19 CD PRO A 2 -27.091 20.858 4.663 1.00140.86 C
ANISOU 19 CD PRO A 2 17752 17604 18163 85 -873 254 C
ATOM 20 N ILE A 3 -28.239 17.561 3.924 1.00129.89 N
ANISOU 20 N ILE A 3 16452 16301 16600 41 -739 229 N
ATOM 21 CA ILE A 3 -29.145 16.450 3.669 1.00125.72 C
ANISOU 21 CA ILE A 3 15953 15802 16014 25 -707 217 C
ATOM 22 C ILE A 3 -28.702 15.568 2.498 1.00124.64 C
ANISOU 22 C ILE A 3 15862 15685 15810 -25 -659 246 C
ATOM 23 O ILE A 3 -29.026 14.384 2.469 1.00120.59 O
ANISOU 23 O ILE A 3 15377 15197 15244 -31 -613 229 O
ATOM 24 CB ILE A 3 -30.593 16.951 3.484 1.00122.05 C
ANISOU 24 CB ILE A 3 15472 15333 15568 18 -763 221 C
ATOM 25 CG1 ILE A 3 -31.580 15.778 3.537 1.00118.70 C
ANISOU 25 CG1 ILE A 3 15070 14939 15091 13 -731 200 C
ATOM 26 CG2 ILE A 3 -30.743 17.744 2.190 1.00120.92 C
ANISOU 26 CG2 ILE A 3 15336 15175 15432 -32 -808 276 C
ATOM 27 CD1 ILE A 3 -33.006 16.147 3.902 1.00119.69 C
ANISOU 27 CD1 ILE A 3 15170 15064 15244 27 -777 184 C
ATOM 28 N MET A 4 -27.959 16.126 1.553 1.00125.39 N
ANISOU 28 N MET A 4 15966 15771 15907 -60 -668 289 N
ATOM 29 CA MET A 4 -27.466 15.337 0.424 1.00123.18 C
ANISOU 29 CA MET A 4 15730 15512 15562 -109 -620 314 C
ATOM 30 C MET A 4 -26.475 14.267 0.874 1.00121.47 C
ANISOU 30 C MET A 4 15529 15309 15316 -90 -547 285 C
ATOM 31 O MET A 4 -26.641 13.087 0.567 1.00115.13 O
ANISOU 31 O MET A 4 14760 14530 14456 -105 -498 273 O
ATOM 32 CB MET A 4 -26.836 16.232 -0.638 1.00123.38 C
ANISOU 32 CB MET A 4 15757 15525 15597 -152 -646 366 C
ATOM 33 CG MET A 4 -27.824 17.022 -1.480 1.00125.96 C
ANISOU 33 CG MET A 4 16082 15844 15934 -190 -709 405 C
ATOM 34 SD MET A 4 -27.067 17.613 -3.006 1.00131.42 S
ANISOU 34 SD MET A 4 16793 16536 16603 -259 -720 471 S
ATOM 35 CE MET A 4 -27.072 16.126 -4.014 1.00127.81 C
ANISOU 35 CE MET A 4 16394 16120 16046 -306 -646 471 C
ATOM 36 N GLY A 5 -25.453 14.685 1.618 1.00119.89 N
ANISOU 36 N GLY A 5 15304 15092 15157 -56 -543 275 N
ATOM 37 CA GLY A 5 -24.515 13.735 2.211 1.00119.15 C
ANISOU 37 CA GLY A 5 15219 15006 15046 -32 -480 246 C
ATOM 38 C GLY A 5 -25.197 12.764 3.167 1.00116.25 C
ANISOU 38 C GLY A 5 14855 14653 14661 1 -458 200 C
ATOM 39 O GLY A 5 -24.778 11.611 3.289 1.00116.97 O
ANISOU 39 O GLY A 5 14969 14759 14716 4 -401 181 O
ATOM 40 N ASER A 6 -26.247 13.231 3.840 0.53113.84 N
ANISOU 40 N ASER A 6 14526 14342 14385 25 -503 184 N
ATOM 41 N BSER A 6 -26.246 13.233 3.840 0.47113.21 N
ANISOU 41 N BSER A 6 14446 14263 14305 25 -503 184 N
ATOM 42 CA ASER A 6 -27.009 12.387 4.754 0.53110.78 C
ANISOU 42 CA ASER A 6 14139 13971 13982 53 -486 143 C
ATOM 43 CA BSER A 6 -27.010 12.390 4.752 0.47110.62 C
ANISOU 43 CA BSER A 6 14119 13951 13962 53 -486 143 C
ATOM 44 C ASER A 6 -27.907 11.390 4.029 0.53110.13 C
ANISOU 44 C ASER A 6 14092 13913 13838 20 -464 146 C
ATOM 45 C BSER A 6 -27.884 11.377 4.020 0.47109.55 C
ANISOU 45 C BSER A 6 14019 13839 13764 20 -463 147 C
ATOM 46 O ASER A 6 -28.302 10.386 4.624 0.53108.20 O
ANISOU 46 O ASER A 6 13858 13686 13567 35 -434 116 O
ATOM 47 O BSER A 6 -28.243 10.351 4.601 0.47108.15 O
ANISOU 47 O BSER A 6 13853 13679 13559 35 -431 117 O
ATOM 48 CB ASER A 6 -27.839 13.246 5.708 0.53112.86 C
ANISOU 48 CB ASER A 6 14362 14223 14295 89 -540 122 C
ATOM 49 CB BSER A 6 -27.866 13.249 5.683 0.47109.61 C
ANISOU 49 CB BSER A 6 13952 13812 13884 88 -541 123 C
ATOM 50 OG ASER A 6 -27.009 14.111 6.457 0.53107.32 O
ANISOU 50 OG ASER A 6 13629 13499 13649 122 -560 115 O
ATOM 51 OG BSER A 6 -28.813 12.454 6.370 0.47110.82 O
ANISOU 51 OG BSER A 6 14107 13986 14015 106 -528 89 O
ATOM 52 N SER A 7 -28.237 11.657 2.768 1.00108.70 N
ANISOU 52 N SER A 7 13931 13735 13636 -27 -480 184 N
ATOM 53 CA SER A 7 -29.078 10.739 1.999 1.00104.62 C
ANISOU 53 CA SER A 7 13451 13240 13060 -63 -461 189 C
ATOM 54 C SER A 7 -28.349 9.432 1.690 1.00 99.18 C
ANISOU 54 C SER A 7 12799 12567 12317 -76 -391 179 C
ATOM 55 O SER A 7 -28.964 8.362 1.701 1.00 97.63 O
ANISOU 55 O SER A 7 12627 12389 12079 -82 -364 162 O
ATOM 56 CB SER A 7 -29.566 11.394 0.720 1.00105.07 C
ANISOU 56 CB SER A 7 13520 13295 13108 -113 -498 234 C
ATOM 57 OG SER A 7 -30.304 12.563 1.006 1.00109.55 O
ANISOU 57 OG SER A 7 14052 13844 13730 -100 -565 242 O
ATOM 58 N VAL A 8 -27.046 9.521 1.440 1.00 96.34 N
ANISOU 58 N VAL A 8 12443 12200 11962 -79 -362 188 N
ATOM 59 CA VAL A 8 -26.250 8.323 1.208 1.00 95.41 C
ANISOU 59 CA VAL A 8 12355 12094 11802 -87 -295 175 C
ATOM 60 C VAL A 8 -26.168 7.491 2.490 1.00 96.59 C
ANISOU 60 C VAL A 8 12496 12246 11959 -41 -269 132 C
ATOM 61 O VAL A 8 -26.273 6.261 2.447 1.00 94.92 O
ANISOU 61 O VAL A 8 12312 12049 11706 -47 -226 114 O
ATOM 62 CB VAL A 8 -24.852 8.685 0.673 1.00 94.61 C
ANISOU 62 CB VAL A 8 12254 11985 11709 -100 -272 195 C
ATOM 63 CG1 VAL A 8 -23.959 7.459 0.598 1.00 93.61 C
ANISOU 63 CG1 VAL A 8 12151 11867 11548 -99 -202 174 C
ATOM 64 CG2 VAL A 8 -24.970 9.326 -0.699 1.00 94.75 C
ANISOU 64 CG2 VAL A 8 12287 12007 11707 -154 -293 238 C
ATOM 65 N TYR A 9 -26.004 8.163 3.626 1.00 96.94 N
ANISOU 65 N TYR A 9 12502 12275 12055 2 -296 117 N
ATOM 66 CA TYR A 9 -25.850 7.470 4.903 1.00 94.32 C
ANISOU 66 CA TYR A 9 12160 11946 11733 44 -274 79 C
ATOM 67 C TYR A 9 -27.129 6.727 5.302 1.00 91.06 C
ANISOU 67 C TYR A 9 11755 11551 11292 47 -277 58 C
ATOM 68 O TYR A 9 -27.072 5.566 5.713 1.00 88.76 O
ANISOU 68 O TYR A 9 11481 11271 10974 55 -239 36 O
ATOM 69 CB TYR A 9 -25.425 8.458 5.991 1.00 94.88 C
ANISOU 69 CB TYR A 9 12187 11997 11865 86 -307 69 C
ATOM 70 CG TYR A 9 -25.548 7.933 7.397 1.00 96.64 C
ANISOU 70 CG TYR A 9 12396 12225 12099 127 -298 30 C
ATOM 71 CD1 TYR A 9 -24.580 7.078 7.931 1.00 96.62 C
ANISOU 71 CD1 TYR A 9 12400 12221 12091 144 -254 13 C
ATOM 72 CD2 TYR A 9 -26.631 8.290 8.201 1.00 98.29 C
ANISOU 72 CD2 TYR A 9 12581 12440 12323 149 -336 11 C
ATOM 73 CE1 TYR A 9 -24.683 6.598 9.227 1.00 98.34 C
ANISOU 73 CE1 TYR A 9 12604 12443 12317 179 -249 -18 C
ATOM 74 CE2 TYR A 9 -26.746 7.810 9.496 1.00100.09 C
ANISOU 74 CE2 TYR A 9 12796 12676 12557 184 -327 -23 C
ATOM 75 CZ TYR A 9 -25.770 6.970 10.004 1.00 99.95 C
ANISOU 75 CZ TYR A 9 12787 12657 12532 197 -285 -36 C
ATOM 76 OH TYR A 9 -25.887 6.500 11.287 1.00100.71 O
ANISOU 76 OH TYR A 9 12870 12762 12632 228 -280 -67 O
ATOM 77 N ILE A 10 -28.275 7.389 5.168 1.00 88.92 N
ANISOU 77 N ILE A 10 11473 11284 11030 40 -324 67 N
ATOM 78 CA ILE A 10 -29.540 6.783 5.576 1.00 87.80 C
ANISOU 78 CA ILE A 10 11334 11160 10866 44 -331 49 C
ATOM 79 C ILE A 10 -29.887 5.595 4.675 1.00 92.13 C
ANISOU 79 C ILE A 10 11928 11726 11352 6 -296 55 C
ATOM 80 O ILE A 10 -30.360 4.560 5.154 1.00 92.72 O
ANISOU 80 O ILE A 10 12015 11816 11399 13 -273 34 O
ATOM 81 CB ILE A 10 -30.664 7.829 5.606 1.00 84.58 C
ANISOU 81 CB ILE A 10 10899 10750 10488 45 -391 56 C
ATOM 82 CG1 ILE A 10 -30.354 8.883 6.671 1.00 83.23 C
ANISOU 82 CG1 ILE A 10 10683 10562 10379 88 -424 40 C
ATOM 83 CG2 ILE A 10 -32.011 7.170 5.881 1.00 82.89 C
ANISOU 83 CG2 ILE A 10 10689 10557 10247 43 -396 41 C
ATOM 84 CD1 ILE A 10 -31.294 10.067 6.670 1.00 82.98 C
ANISOU 84 CD1 ILE A 10 10620 10522 10388 92 -485 47 C
ATOM 85 N THR A 11 -29.630 5.735 3.378 1.00 92.54 N
ANISOU 85 N THR A 11 12004 11775 11380 -36 -290 86 N
ATOM 86 CA THR A 11 -29.904 4.652 2.437 1.00 91.95 C
ANISOU 86 CA THR A 11 11975 11716 11246 -74 -256 92 C
ATOM 87 C THR A 11 -29.049 3.420 2.751 1.00 93.05 C
ANISOU 87 C THR A 11 12135 11859 11362 -63 -197 67 C
ATOM 88 O THR A 11 -29.562 2.297 2.803 1.00 93.19 O
ANISOU 88 O THR A 11 12176 11890 11343 -69 -174 52 O
ATOM 89 CB THR A 11 -29.679 5.121 0.996 1.00 89.67 C
ANISOU 89 CB THR A 11 11708 11426 10937 -122 -261 129 C
ATOM 90 OG1 THR A 11 -30.500 6.265 0.742 1.00 87.16 O
ANISOU 90 OG1 THR A 11 11369 11102 10644 -133 -322 153 O
ATOM 91 CG2 THR A 11 -30.028 4.027 0.011 1.00 88.63 C
ANISOU 91 CG2 THR A 11 11624 11312 10740 -164 -229 133 C
ATOM 92 N VAL A 12 -27.756 3.632 2.974 1.00 92.15 N
ANISOU 92 N VAL A 12 12009 11731 11272 -46 -175 64 N
ATOM 93 CA VAL A 12 -26.862 2.533 3.334 1.00 88.64 C
ANISOU 93 CA VAL A 12 11578 11285 10815 -32 -122 41 C
ATOM 94 C VAL A 12 -27.283 1.928 4.675 1.00 88.45 C
ANISOU 94 C VAL A 12 11540 11265 10803 5 -123 11 C
ATOM 95 O VAL A 12 -27.295 0.705 4.836 1.00 89.82 O
ANISOU 95 O VAL A 12 11736 11445 10947 5 -89 -8 O
ATOM 96 CB VAL A 12 -25.395 3.004 3.349 1.00 86.69 C
ANISOU 96 CB VAL A 12 11316 11021 10600 -19 -103 46 C
ATOM 97 CG1 VAL A 12 -24.488 2.001 4.031 1.00 86.12 C
ANISOU 97 CG1 VAL A 12 11248 10943 10532 6 -58 19 C
ATOM 98 CG2 VAL A 12 -24.912 3.261 1.931 1.00 85.88 C
ANISOU 98 CG2 VAL A 12 11236 10921 10474 -63 -88 73 C
ATOM 99 N GLU A 13 -27.652 2.780 5.625 1.00 88.12 N
ANISOU 99 N GLU A 13 11461 11219 10800 36 -163 5 N
ATOM 100 CA GLU A 13 -28.071 2.295 6.940 1.00 88.48 C
ANISOU 100 CA GLU A 13 11490 11273 10855 69 -166 -24 C
ATOM 101 C GLU A 13 -29.307 1.406 6.845 1.00 87.54 C
ANISOU 101 C GLU A 13 11393 11175 10695 52 -165 -30 C
ATOM 102 O GLU A 13 -29.390 0.379 7.523 1.00 90.32 O
ANISOU 102 O GLU A 13 11753 11535 11031 63 -143 -51 O
ATOM 103 CB GLU A 13 -28.315 3.461 7.895 1.00 90.33 C
ANISOU 103 CB GLU A 13 11682 11502 11139 101 -211 -30 C
ATOM 104 CG GLU A 13 -27.051 4.001 8.540 1.00 93.27 C
ANISOU 104 CG GLU A 13 12030 11855 11554 131 -207 -36 C
ATOM 105 CD GLU A 13 -26.640 3.231 9.778 1.00 94.60 C
ANISOU 105 CD GLU A 13 12190 12025 11727 162 -185 -64 C
ATOM 106 OE1 GLU A 13 -26.744 3.797 10.884 1.00 93.54 O
ANISOU 106 OE1 GLU A 13 12025 11890 11626 193 -211 -80 O
ATOM 107 OE2 GLU A 13 -26.221 2.063 9.649 1.00 95.37 O
ANISOU 107 OE2 GLU A 13 12314 12125 11798 154 -144 -70 O
ATOM 108 N LEU A 14 -30.260 1.783 6.000 1.00 84.17 N
ANISOU 108 N LEU A 14 10975 10756 10250 23 -191 -11 N
ATOM 109 CA LEU A 14 -31.448 0.957 5.819 1.00 82.59 C
ANISOU 109 CA LEU A 14 10795 10575 10010 3 -192 -14 C
ATOM 110 C LEU A 14 -31.132 -0.329 5.066 1.00 82.65 C
ANISOU 110 C LEU A 14 10848 10585 9969 -25 -146 -15 C
ATOM 111 O LEU A 14 -31.662 -1.391 5.402 1.00 83.61 O
ANISOU 111 O LEU A 14 10986 10719 10064 -26 -132 -29 O
ATOM 112 CB LEU A 14 -32.548 1.746 5.120 1.00 81.78 C
ANISOU 112 CB LEU A 14 10689 10478 9906 -21 -235 8 C
ATOM 113 CG LEU A 14 -33.171 2.872 5.942 1.00 80.12 C
ANISOU 113 CG LEU A 14 10433 10267 9743 8 -283 2 C
ATOM 114 CD1 LEU A 14 -34.022 3.768 5.056 1.00 80.56 C
ANISOU 114 CD1 LEU A 14 10484 10320 9804 -19 -327 29 C
ATOM 115 CD2 LEU A 14 -33.983 2.308 7.101 1.00 81.31 C
ANISOU 115 CD2 LEU A 14 10567 10436 9890 32 -285 -26 C
ATOM 116 N ALA A 15 -30.259 -0.246 4.064 1.00 81.67 N
ANISOU 116 N ALA A 15 10744 10451 9835 -47 -123 0 N
ATOM 117 CA ALA A 15 -29.862 -1.443 3.315 1.00 80.71 C
ANISOU 117 CA ALA A 15 10665 10331 9670 -72 -77 -5 C
ATOM 118 C ALA A 15 -29.216 -2.476 4.242 1.00 80.75 C
ANISOU 118 C ALA A 15 10670 10331 9680 -43 -43 -33 C
ATOM 119 O ALA A 15 -29.474 -3.674 4.117 1.00 79.49 O
ANISOU 119 O ALA A 15 10539 10177 9487 -55 -18 -45 O
ATOM 120 CB ALA A 15 -28.933 -1.080 2.170 1.00 80.40 C
ANISOU 120 CB ALA A 15 10642 10284 9623 -98 -56 12 C
ATOM 121 N ILE A 16 -28.405 -2.003 5.183 1.00 83.90 N
ANISOU 121 N ILE A 16 11037 10719 10124 -7 -44 -43 N
ATOM 122 CA ILE A 16 -27.794 -2.889 6.165 1.00 85.87 C
ANISOU 122 CA ILE A 16 11282 10961 10384 21 -18 -66 C
ATOM 123 C ILE A 16 -28.867 -3.492 7.076 1.00 88.26 C
ANISOU 123 C ILE A 16 11580 11279 10675 31 -35 -80 C
ATOM 124 O ILE A 16 -28.793 -4.671 7.435 1.00 91.09 O
ANISOU 124 O ILE A 16 11954 11638 11016 33 -11 -95 O
ATOM 125 CB ILE A 16 -26.716 -2.146 6.971 1.00 84.75 C
ANISOU 125 CB ILE A 16 11105 10802 10292 56 -21 -71 C
ATOM 126 CG1 ILE A 16 -25.582 -1.715 6.042 1.00 81.68 C
ANISOU 126 CG1 ILE A 16 10723 10400 9913 43 1 -57 C
ATOM 127 CG2 ILE A 16 -26.154 -3.035 8.070 1.00 85.18 C
ANISOU 127 CG2 ILE A 16 11153 10850 10360 84 -1 -93 C
ATOM 128 CD1 ILE A 16 -24.610 -0.736 6.668 1.00 79.47 C
ANISOU 128 CD1 ILE A 16 10407 10103 9684 73 -10 -54 C
ATOM 129 N ALA A 17 -29.871 -2.692 7.430 1.00 86.28 N
ANISOU 129 N ALA A 17 11307 11042 10433 36 -76 -75 N
ATOM 130 CA ALA A 17 -30.933 -3.167 8.317 1.00 83.85 C
ANISOU 130 CA ALA A 17 10990 10754 10115 45 -93 -87 C
ATOM 131 C ALA A 17 -31.750 -4.288 7.673 1.00 82.54 C
ANISOU 131 C ALA A 17 10861 10599 9900 13 -80 -84 C
ATOM 132 O ALA A 17 -32.145 -5.238 8.352 1.00 84.52 O
ANISOU 132 O ALA A 17 11118 10861 10137 18 -73 -97 O
ATOM 133 CB ALA A 17 -31.830 -2.016 8.748 1.00 82.42 C
ANISOU 133 CB ALA A 17 10775 10584 9957 57 -139 -84 C
ATOM 134 N VAL A 18 -31.980 -4.188 6.366 1.00 79.01 N
ANISOU 134 N VAL A 18 10441 10152 9428 -22 -78 -67 N
ATOM 135 CA VAL A 18 -32.750 -5.207 5.662 1.00 77.82 C
ANISOU 135 CA VAL A 18 10328 10011 9230 -55 -68 -63 C
ATOM 136 C VAL A 18 -31.997 -6.537 5.669 1.00 80.33 C
ANISOU 136 C VAL A 18 10674 10319 9530 -56 -25 -79 C
ATOM 137 O VAL A 18 -32.574 -7.586 5.977 1.00 78.14 O
ANISOU 137 O VAL A 18 10411 10049 9229 -62 -20 -88 O
ATOM 138 CB VAL A 18 -33.078 -4.754 4.232 1.00 77.80 C
ANISOU 138 CB VAL A 18 10348 10008 9202 -94 -76 -40 C
ATOM 139 CG1 VAL A 18 -33.766 -5.860 3.453 1.00 78.14 C
ANISOU 139 CG1 VAL A 18 10434 10060 9194 -130 -63 -38 C
ATOM 140 CG2 VAL A 18 -33.949 -3.512 4.269 1.00 79.03 C
ANISOU 140 CG2 VAL A 18 10475 10172 9379 -93 -125 -24 C
ATOM 141 N LEU A 19 -30.710 -6.492 5.349 1.00 83.68 N
ANISOU 141 N LEU A 19 11102 10724 9968 -50 5 -83 N
ATOM 142 CA LEU A 19 -29.901 -7.706 5.354 1.00 86.10 C
ANISOU 142 CA LEU A 19 11432 11017 10265 -48 46 -101 C
ATOM 143 C LEU A 19 -29.695 -8.251 6.763 1.00 89.79 C
ANISOU 143 C LEU A 19 11879 11482 10757 -15 46 -118 C
ATOM 144 O LEU A 19 -29.510 -9.457 6.938 1.00 85.34 O
ANISOU 144 O LEU A 19 11333 10910 10180 -16 68 -131 O
ATOM 145 CB LEU A 19 -28.564 -7.464 4.662 1.00 83.42 C
ANISOU 145 CB LEU A 19 11097 10659 9938 -49 79 -101 C
ATOM 146 CG LEU A 19 -28.642 -7.074 3.186 1.00 80.97 C
ANISOU 146 CG LEU A 19 10813 10353 9597 -88 86 -85 C
ATOM 147 CD1 LEU A 19 -27.271 -6.685 2.658 1.00 83.26 C
ANISOU 147 CD1 LEU A 19 11101 10630 9905 -86 117 -85 C
ATOM 148 CD2 LEU A 19 -29.270 -8.158 2.322 1.00 81.59 C
ANISOU 148 CD2 LEU A 19 10936 10439 9625 -123 102 -89 C
ATOM 149 N ALA A 20 -29.733 -7.373 7.763 1.00 91.73 N
ANISOU 149 N ALA A 20 12085 11732 11036 13 19 -117 N
ATOM 150 CA ALA A 20 -29.566 -7.817 9.148 1.00 91.04 C
ANISOU 150 CA ALA A 20 11976 11645 10969 42 16 -131 C
ATOM 151 C ALA A 20 -30.789 -8.601 9.625 1.00 90.78 C
ANISOU 151 C ALA A 20 11951 11633 10907 32 1 -134 C
ATOM 152 O ALA A 20 -30.645 -9.620 10.303 1.00 90.20 O
ANISOU 152 O ALA A 20 11883 11558 10831 38 12 -144 O
ATOM 153 CB ALA A 20 -29.290 -6.636 10.065 1.00 92.63 C
ANISOU 153 CB ALA A 20 12136 11848 11212 74 -9 -132 C
ATOM 154 N ILE A 21 -31.981 -8.148 9.253 1.00 88.51 N
ANISOU 154 N ILE A 21 11663 11366 10601 15 -25 -123 N
ATOM 155 CA ILE A 21 -33.203 -8.816 9.691 1.00 88.17 C
ANISOU 155 CA ILE A 21 11624 11346 10531 4 -41 -124 C
ATOM 156 C ILE A 21 -33.396 -10.132 8.932 1.00 86.44 C
ANISOU 156 C ILE A 21 11448 11121 10273 -26 -20 -123 C
ATOM 157 O ILE A 21 -33.643 -11.178 9.542 1.00 88.09 O
ANISOU 157 O ILE A 21 11664 11334 10470 -26 -16 -130 O
ATOM 158 CB ILE A 21 -34.428 -7.900 9.535 1.00 88.39 C
ANISOU 158 CB ILE A 21 11634 11396 10555 -4 -77 -113 C
ATOM 159 CG1 ILE A 21 -34.265 -6.655 10.403 1.00 87.96 C
ANISOU 159 CG1 ILE A 21 11534 11345 10541 28 -100 -119 C
ATOM 160 CG2 ILE A 21 -35.702 -8.640 9.918 1.00 88.97 C
ANISOU 160 CG2 ILE A 21 11711 11494 10600 -18 -92 -113 C
ATOM 161 CD1 ILE A 21 -35.276 -5.573 10.106 1.00 84.71 C
ANISOU 161 CD1 ILE A 21 11102 10947 10135 23 -136 -109 C
ATOM 162 N LEU A 22 -33.281 -10.079 7.609 1.00 82.68 N
ANISOU 162 N LEU A 22 11001 10636 9778 -52 -7 -115 N
ATOM 163 CA LEU A 22 -33.505 -11.266 6.790 1.00 79.75 C
ANISOU 163 CA LEU A 22 10673 10259 9368 -82 13 -116 C
ATOM 164 C LEU A 22 -32.524 -12.384 7.119 1.00 77.32 C
ANISOU 164 C LEU A 22 10379 9930 9068 -71 45 -134 C
ATOM 165 O LEU A 22 -32.928 -13.516 7.398 1.00 77.95 O
ANISOU 165 O LEU A 22 10476 10011 9131 -79 47 -139 O
ATOM 166 CB LEU A 22 -33.451 -10.915 5.304 1.00 79.61 C
ANISOU 166 CB LEU A 22 10684 10236 9328 -112 22 -105 C
ATOM 167 CG LEU A 22 -34.557 -10.005 4.762 1.00 79.49 C
ANISOU 167 CG LEU A 22 10664 10240 9300 -132 -12 -84 C
ATOM 168 CD1 LEU A 22 -34.270 -9.641 3.319 1.00 80.67 C
ANISOU 168 CD1 LEU A 22 10840 10382 9428 -163 -1 -73 C
ATOM 169 CD2 LEU A 22 -35.939 -10.630 4.894 1.00 81.75 C
ANISOU 169 CD2 LEU A 22 10959 10545 9558 -151 -35 -79 C
ATOM 170 N GLY A 23 -31.237 -12.055 7.123 1.00 77.75 N
ANISOU 170 N GLY A 23 10425 9965 9153 -52 68 -142 N
ATOM 171 CA GLY A 23 -30.207 -13.072 7.311 1.00 78.64 C
ANISOU 171 CA GLY A 23 10549 10053 9277 -41 100 -159 C
ATOM 172 C GLY A 23 -30.332 -13.796 8.639 1.00 79.91 C
ANISOU 172 C GLY A 23 10695 10214 9452 -23 88 -165 C
ATOM 173 O GLY A 23 -30.291 -15.022 8.698 1.00 81.40 O
ANISOU 173 O GLY A 23 10905 10392 9631 -30 100 -174 O
ATOM 174 N ASN A 24 -30.498 -13.031 9.712 1.00 81.86 N
ANISOU 174 N ASN A 24 10905 10476 9722 1 63 -161 N
ATOM 175 CA ASN A 24 -30.528 -13.614 11.049 1.00 85.10 C
ANISOU 175 CA ASN A 24 11298 10891 10146 18 52 -166 C
ATOM 176 C ASN A 24 -31.859 -14.267 11.396 1.00 88.40 C
ANISOU 176 C ASN A 24 11723 11332 10531 -1 30 -159 C
ATOM 177 O ASN A 24 -31.895 -15.143 12.261 1.00 90.84 O
ANISOU 177 O ASN A 24 12031 11643 10843 2 26 -162 O
ATOM 178 CB ASN A 24 -30.140 -12.578 12.093 1.00 85.93 C
ANISOU 178 CB ASN A 24 11362 11002 10287 49 35 -166 C
ATOM 179 CG ASN A 24 -28.705 -12.115 11.947 1.00 87.98 C
ANISOU 179 CG ASN A 24 11612 11235 10583 69 57 -172 C
ATOM 180 OD1 ASN A 24 -27.791 -12.676 12.554 1.00 86.33 O
ANISOU 180 OD1 ASN A 24 11397 11005 10398 85 69 -179 O
ATOM 181 ND2 ASN A 24 -28.498 -11.086 11.131 1.00 91.65 N
ANISOU 181 ND2 ASN A 24 12073 11697 11052 67 59 -166 N
ATOM 182 N VAL A 25 -32.946 -13.847 10.748 1.00 91.70 N
ANISOU 182 N VAL A 25 12149 11772 10922 -22 14 -149 N
ATOM 183 CA VAL A 25 -34.212 -14.571 10.882 1.00 93.03 C
ANISOU 183 CA VAL A 25 12328 11961 11057 -44 -3 -142 C
ATOM 184 C VAL A 25 -34.092 -15.948 10.219 1.00 93.45 C
ANISOU 184 C VAL A 25 12424 11995 11088 -67 16 -146 C
ATOM 185 O VAL A 25 -34.614 -16.941 10.735 1.00 94.13 O
ANISOU 185 O VAL A 25 12518 12087 11160 -77 7 -144 O
ATOM 186 CB VAL A 25 -35.386 -13.748 10.313 1.00 90.81 C
ANISOU 186 CB VAL A 25 12043 11705 10756 -61 -27 -130 C
ATOM 187 CG1 VAL A 25 -36.565 -14.617 9.918 1.00 89.10 C
ANISOU 187 CG1 VAL A 25 11852 11503 10500 -93 -37 -120 C
ATOM 188 CG2 VAL A 25 -35.851 -12.713 11.325 1.00 88.00 C
ANISOU 188 CG2 VAL A 25 11642 11375 10420 -39 -53 -129 C
ATOM 189 N LEU A 26 -33.380 -16.009 9.095 1.00 94.79 N
ANISOU 189 N LEU A 26 12620 12141 11255 -76 43 -152 N
ATOM 190 CA LEU A 26 -33.134 -17.279 8.424 1.00 94.80 C
ANISOU 190 CA LEU A 26 12661 12121 11239 -95 65 -161 C
ATOM 191 C LEU A 26 -32.338 -18.248 9.303 1.00 92.50 C
ANISOU 191 C LEU A 26 12366 11807 10974 -77 75 -173 C
ATOM 192 O LEU A 26 -32.529 -19.457 9.215 1.00 86.95 O
ANISOU 192 O LEU A 26 11687 11092 10257 -92 78 -177 O
ATOM 193 CB LEU A 26 -32.416 -17.039 7.097 1.00 97.27 C
ANISOU 193 CB LEU A 26 12998 12415 11545 -106 95 -169 C
ATOM 194 CG LEU A 26 -32.274 -18.215 6.133 1.00100.48 C
ANISOU 194 CG LEU A 26 13449 12802 11928 -130 119 -182 C
ATOM 195 CD1 LEU A 26 -33.627 -18.740 5.679 1.00100.69 C
ANISOU 195 CD1 LEU A 26 13502 12845 11911 -164 99 -171 C
ATOM 196 CD2 LEU A 26 -31.432 -17.810 4.934 1.00101.70 C
ANISOU 196 CD2 LEU A 26 13620 12942 12078 -137 152 -191 C
ATOM 197 N VAL A 27 -31.468 -17.714 10.157 1.00 92.73 N
ANISOU 197 N VAL A 27 12362 11829 11041 -46 77 -176 N
ATOM 198 CA VAL A 27 -30.692 -18.555 11.065 1.00 92.95 C
ANISOU 198 CA VAL A 27 12383 11837 11098 -29 82 -184 C
ATOM 199 C VAL A 27 -31.596 -19.161 12.139 1.00 96.95 C
ANISOU 199 C VAL A 27 12881 12364 11592 -35 52 -174 C
ATOM 200 O VAL A 27 -31.535 -20.363 12.410 1.00101.45 O
ANISOU 200 O VAL A 27 13466 12918 12162 -43 52 -175 O
ATOM 201 CB VAL A 27 -29.531 -17.767 11.699 1.00 89.12 C
ANISOU 201 CB VAL A 27 11866 11340 10656 4 90 -189 C
ATOM 202 CG1 VAL A 27 -28.810 -18.599 12.742 1.00 85.59 C
ANISOU 202 CG1 VAL A 27 11408 10872 10240 20 88 -193 C
ATOM 203 CG2 VAL A 27 -28.557 -17.310 10.628 1.00 91.41 C
ANISOU 203 CG2 VAL A 27 12165 11608 10959 8 122 -199 C
ATOM 204 N CYS A 28 -32.441 -18.332 12.739 1.00 97.60 N
ANISOU 204 N CYS A 28 12938 12482 11665 -33 27 -163 N
ATOM 205 CA CYS A 28 -33.312 -18.799 13.815 1.00 99.35 C
ANISOU 205 CA CYS A 28 13146 12730 11874 -39 0 -152 C
ATOM 206 C CYS A 28 -34.363 -19.786 13.304 1.00104.71 C
ANISOU 206 C CYS A 28 13855 13415 12514 -72 -9 -144 C
ATOM 207 O CYS A 28 -34.737 -20.713 14.020 1.00107.90 O
ANISOU 207 O CYS A 28 14261 13826 12912 -82 -23 -137 O
ATOM 208 CB CYS A 28 -33.967 -17.620 14.526 1.00 96.19 C
ANISOU 208 CB CYS A 28 12709 12367 11473 -27 -22 -147 C
ATOM 209 SG CYS A 28 -32.789 -16.492 15.308 1.00 89.93 S
ANISOU 209 SG CYS A 28 11878 11566 10724 12 -18 -156 S
ATOM 210 N TRP A 29 -34.815 -19.602 12.066 1.00109.38 N
ANISOU 210 N TRP A 29 14470 14006 13082 -91 -1 -144 N
ATOM 211 CA TRP A 29 -35.776 -20.533 11.482 1.00114.25 C
ANISOU 211 CA TRP A 29 15120 14628 13663 -124 -9 -137 C
ATOM 212 C TRP A 29 -35.135 -21.885 11.174 1.00111.74 C
ANISOU 212 C TRP A 29 14834 14272 13349 -133 7 -147 C
ATOM 213 O TRP A 29 -35.807 -22.915 11.236 1.00111.80 O
ANISOU 213 O TRP A 29 14860 14281 13337 -155 -6 -140 O
ATOM 214 CB TRP A 29 -36.414 -19.927 10.233 1.00123.28 C
ANISOU 214 CB TRP A 29 16281 15780 14780 -144 -8 -132 C
ATOM 215 CG TRP A 29 -37.749 -20.514 9.878 1.00134.10 C
ANISOU 215 CG TRP A 29 17671 17169 16112 -177 -28 -119 C
ATOM 216 CD1 TRP A 29 -38.069 -21.187 8.731 1.00135.74 C
ANISOU 216 CD1 TRP A 29 17921 17363 16291 -207 -21 -119 C
ATOM 217 CD2 TRP A 29 -38.941 -20.480 10.667 1.00139.82 C
ANISOU 217 CD2 TRP A 29 18374 17929 16822 -186 -58 -103 C
ATOM 218 NE1 TRP A 29 -39.387 -21.569 8.758 1.00140.79 N
ANISOU 218 NE1 TRP A 29 18566 18026 16901 -232 -48 -103 N
ATOM 219 CE2 TRP A 29 -39.946 -21.153 9.935 1.00142.82 C
ANISOU 219 CE2 TRP A 29 18784 18315 17167 -220 -70 -93 C
ATOM 220 CE3 TRP A 29 -39.262 -19.946 11.924 1.00140.95 C
ANISOU 220 CE3 TRP A 29 18475 18103 16978 -168 -76 -98 C
ATOM 221 CZ2 TRP A 29 -41.249 -21.310 10.416 1.00142.87 C
ANISOU 221 CZ2 TRP A 29 18777 18355 17152 -237 -98 -75 C
ATOM 222 CZ3 TRP A 29 -40.556 -20.103 12.403 1.00139.37 C
ANISOU 222 CZ3 TRP A 29 18262 17939 16755 -185 -103 -84 C
ATOM 223 CH2 TRP A 29 -41.534 -20.780 11.649 1.00139.84 C
ANISOU 223 CH2 TRP A 29 18350 18002 16782 -219 -113 -72 C
ATOM 224 N ALA A 30 -33.842 -21.884 10.859 1.00108.71 N
ANISOU 224 N ALA A 30 14455 13856 12995 -115 35 -163 N
ATOM 225 CA ALA A 30 -33.131 -23.138 10.593 1.00106.87 C
ANISOU 225 CA ALA A 30 14248 13584 12773 -118 52 -177 C
ATOM 226 C ALA A 30 -32.908 -23.932 11.879 1.00106.01 C
ANISOU 226 C ALA A 30 14124 13467 12688 -109 35 -171 C
ATOM 227 O ALA A 30 -33.006 -25.160 11.878 1.00107.62 O
ANISOU 227 O ALA A 30 14350 13652 12890 -123 29 -172 O
ATOM 228 CB ALA A 30 -31.813 -22.870 9.882 1.00104.36 C
ANISOU 228 CB ALA A 30 13937 13235 12482 -101 89 -198 C
ATOM 229 N VAL A 31 -32.606 -23.236 12.970 1.00105.30 N
ANISOU 229 N VAL A 31 13996 13392 12620 -86 24 -165 N
ATOM 230 CA VAL A 31 -32.437 -23.895 14.260 1.00105.21 C
ANISOU 230 CA VAL A 31 13968 13379 12628 -80 4 -156 C
ATOM 231 C VAL A 31 -33.777 -24.438 14.763 1.00108.71 C
ANISOU 231 C VAL A 31 14413 13854 13036 -106 -27 -137 C
ATOM 232 O VAL A 31 -33.820 -25.482 15.418 1.00107.41 O
ANISOU 232 O VAL A 31 14253 13680 12877 -116 -43 -128 O
ATOM 233 CB VAL A 31 -31.793 -22.940 15.278 1.00103.17 C
ANISOU 233 CB VAL A 31 13669 13131 12398 -51 0 -155 C
ATOM 234 CG1 VAL A 31 -31.638 -23.604 16.635 1.00102.78 C
ANISOU 234 CG1 VAL A 31 13604 13083 12366 -48 -23 -143 C
ATOM 235 CG2 VAL A 31 -30.441 -22.469 14.767 1.00101.81 C
ANISOU 235 CG2 VAL A 31 13495 12926 12263 -26 30 -172 C
ATOM 236 N TRP A 32 -34.868 -23.756 14.426 1.00111.77 N
ANISOU 236 N TRP A 32 14799 14279 13392 -119 -36 -129 N
ATOM 237 CA TRP A 32 -36.189 -24.197 14.866 1.00120.06 C
ANISOU 237 CA TRP A 32 15846 15362 14407 -145 -65 -110 C
ATOM 238 C TRP A 32 -36.612 -25.494 14.174 1.00122.54 C
ANISOU 238 C TRP A 32 16201 15655 14702 -174 -68 -107 C
ATOM 239 O TRP A 32 -37.207 -26.369 14.801 1.00120.97 O
ANISOU 239 O TRP A 32 16004 15466 14492 -193 -91 -91 O
ATOM 240 CB TRP A 32 -37.221 -23.102 14.625 1.00125.54 C
ANISOU 240 CB TRP A 32 16525 16097 15076 -150 -73 -104 C
ATOM 241 CG TRP A 32 -38.542 -23.371 15.263 1.00132.87 C
ANISOU 241 CG TRP A 32 17442 17067 15976 -171 -102 -85 C
ATOM 242 CD1 TRP A 32 -39.652 -23.884 14.659 1.00133.91 C
ANISOU 242 CD1 TRP A 32 17595 17210 16074 -202 -114 -73 C
ATOM 243 CD2 TRP A 32 -38.898 -23.131 16.624 1.00138.40 C
ANISOU 243 CD2 TRP A 32 18105 17804 16676 -165 -121 -76 C
ATOM 244 NE1 TRP A 32 -40.680 -23.981 15.562 1.00137.06 N
ANISOU 244 NE1 TRP A 32 17971 17652 16454 -215 -139 -57 N
ATOM 245 CE2 TRP A 32 -40.248 -23.525 16.777 1.00140.32 C
ANISOU 245 CE2 TRP A 32 18348 18081 16885 -193 -143 -59 C
ATOM 246 CE3 TRP A 32 -38.212 -22.621 17.733 1.00141.30 C
ANISOU 246 CE3 TRP A 32 18440 18179 17068 -140 -121 -81 C
ATOM 247 CZ2 TRP A 32 -40.927 -23.429 17.995 1.00140.42 C
ANISOU 247 CZ2 TRP A 32 18328 18139 16887 -198 -163 -48 C
ATOM 248 CZ3 TRP A 32 -38.887 -22.524 18.947 1.00142.55 C
ANISOU 248 CZ3 TRP A 32 18568 18381 17213 -144 -142 -71 C
ATOM 249 CH2 TRP A 32 -40.234 -22.928 19.066 1.00141.62 C
ANISOU 249 CH2 TRP A 32 18449 18300 17060 -173 -161 -55 C
ATOM 250 N LEU A 33 -36.294 -25.620 12.890 1.00124.44 N
ANISOU 250 N LEU A 33 16474 15869 14940 -180 -46 -121 N
ATOM 251 CA LEU A 33 -36.703 -26.797 12.130 1.00126.34 C
ANISOU 251 CA LEU A 33 16754 16088 15160 -208 -48 -122 C
ATOM 252 C LEU A 33 -35.793 -27.989 12.396 1.00125.87 C
ANISOU 252 C LEU A 33 16708 15984 15131 -203 -44 -132 C
ATOM 253 O LEU A 33 -36.252 -29.041 12.859 1.00129.40 O
ANISOU 253 O LEU A 33 17165 16428 15573 -221 -67 -119 O
ATOM 254 CB LEU A 33 -36.752 -26.481 10.635 1.00129.52 C
ANISOU 254 CB LEU A 33 17188 16481 15543 -219 -26 -135 C
ATOM 255 CG LEU A 33 -37.789 -25.457 10.168 1.00134.44 C
ANISOU 255 CG LEU A 33 17805 17143 16134 -231 -35 -123 C
ATOM 256 CD1 LEU A 33 -37.445 -24.953 8.777 1.00136.60 C
ANISOU 256 CD1 LEU A 33 18102 17401 16397 -236 -9 -138 C
ATOM 257 CD2 LEU A 33 -39.204 -26.018 10.208 1.00136.89 C
ANISOU 257 CD2 LEU A 33 18125 17478 16410 -263 -65 -103 C
ATOM 258 N ASN A 34 -34.503 -27.824 12.117 1.00121.70 N
ANISOU 258 N ASN A 34 16180 15423 14637 -178 -15 -153 N
ATOM 259 CA ASN A 34 -33.566 -28.942 12.166 1.00121.53 C
ANISOU 259 CA ASN A 34 16173 15354 14650 -172 -7 -167 C
ATOM 260 C ASN A 34 -33.386 -29.445 13.592 1.00122.73 C
ANISOU 260 C ASN A 34 16299 15504 14827 -166 -34 -150 C
ATOM 261 O ASN A 34 -33.188 -28.657 14.514 1.00121.28 O
ANISOU 261 O ASN A 34 16081 15344 14655 -148 -41 -140 O
ATOM 262 CB ASN A 34 -32.219 -28.540 11.566 1.00120.00 C
ANISOU 262 CB ASN A 34 15979 15128 14489 -146 31 -194 C
ATOM 263 CG ASN A 34 -31.404 -29.733 11.097 1.00119.64 C
ANISOU 263 CG ASN A 34 15957 15029 14470 -145 47 -217 C
ATOM 264 OD1 ASN A 34 -31.376 -30.782 11.742 1.00120.23 O
ANISOU 264 OD1 ASN A 34 16034 15082 14564 -150 25 -211 O
ATOM 265 ND2 ASN A 34 -30.731 -29.575 9.965 1.00119.81 N
ANISOU 265 ND2 ASN A 34 15997 15029 14496 -139 84 -245 N
ATOM 266 N SER A 35 -33.469 -30.760 13.763 1.00126.92 N
ANISOU 266 N SER A 35 16849 16009 15366 -182 -52 -146 N
ATOM 267 CA SER A 35 -33.221 -31.380 15.060 1.00127.84 C
ANISOU 267 CA SER A 35 16945 16118 15508 -180 -80 -128 C
ATOM 268 C SER A 35 -31.730 -31.428 15.389 1.00126.36 C
ANISOU 268 C SER A 35 16743 15890 15377 -149 -64 -143 C
ATOM 269 O SER A 35 -31.359 -31.351 16.562 1.00127.98 O
ANISOU 269 O SER A 35 16920 16100 15605 -139 -83 -128 O
ATOM 270 CB SER A 35 -33.808 -32.790 15.091 1.00131.31 C
ANISOU 270 CB SER A 35 17411 16541 15941 -210 -108 -116 C
ATOM 271 OG SER A 35 -35.161 -32.780 14.672 1.00134.36 O
ANISOU 271 OG SER A 35 17812 16962 16278 -239 -121 -102 O
ATOM 272 N ASN A 36 -30.882 -31.561 14.371 1.00123.59 N
ANISOU 272 N ASN A 36 16411 15500 15048 -136 -31 -173 N
ATOM 273 CA ASN A 36 -29.437 -31.625 14.597 1.00121.27 C
ANISOU 273 CA ASN A 36 16102 15164 14811 -106 -13 -190 C
ATOM 274 C ASN A 36 -28.875 -30.281 15.051 1.00117.87 C
ANISOU 274 C ASN A 36 15637 14756 14391 -80 0 -189 C
ATOM 275 O ASN A 36 -27.993 -30.228 15.908 1.00114.01 O
ANISOU 275 O ASN A 36 15124 14251 13945 -59 -6 -185 O
ATOM 276 CB ASN A 36 -28.718 -32.105 13.339 1.00123.78 C
ANISOU 276 CB ASN A 36 16448 15438 15146 -100 22 -226 C
ATOM 277 CG ASN A 36 -29.331 -33.365 12.761 1.00129.99 C
ANISOU 277 CG ASN A 36 17271 16203 15918 -127 10 -231 C
ATOM 278 OD1 ASN A 36 -29.538 -34.357 13.464 1.00136.08 O
ANISOU 278 OD1 ASN A 36 18043 16957 16703 -139 -23 -215 O
ATOM 279 ND2 ASN A 36 -29.627 -33.331 11.467 1.00133.17 N
ANISOU 279 ND2 ASN A 36 17704 16605 16290 -138 36 -253 N
ATOM 280 N LEU A 37 -29.415 -29.194 14.506 1.00114.81 N
ANISOU 280 N LEU A 37 15249 14405 13968 -81 14 -190 N
ATOM 281 CA LEU A 37 -28.999 -27.844 14.869 1.00114.33 C
ANISOU 281 CA LEU A 37 15158 14368 13916 -57 24 -188 C
ATOM 282 C LEU A 37 -29.494 -27.393 16.244 1.00115.58 C
ANISOU 282 C LEU A 37 15284 14564 14067 -56 -8 -163 C
ATOM 283 O LEU A 37 -29.308 -26.232 16.599 1.00116.52 O
ANISOU 283 O LEU A 37 15377 14707 14189 -39 -4 -161 O
ATOM 284 CB LEU A 37 -29.451 -26.848 13.798 1.00110.35 C
ANISOU 284 CB LEU A 37 14663 13889 13378 -61 46 -197 C
ATOM 285 CG LEU A 37 -28.821 -27.017 12.419 1.00107.00 C
ANISOU 285 CG LEU A 37 14265 13433 12958 -60 85 -224 C
ATOM 286 CD1 LEU A 37 -29.420 -26.019 11.444 1.00105.48 C
ANISOU 286 CD1 LEU A 37 14082 13270 12725 -70 99 -226 C
ATOM 287 CD2 LEU A 37 -27.313 -26.853 12.502 1.00103.06 C
ANISOU 287 CD2 LEU A 37 13748 12898 12510 -29 110 -242 C
ATOM 288 N GLN A 38 -30.122 -28.284 17.011 1.00117.13 N
ANISOU 288 N GLN A 38 15482 14768 14253 -77 -41 -143 N
ATOM 289 CA GLN A 38 -30.619 -27.946 18.343 1.00115.73 C
ANISOU 289 CA GLN A 38 15276 14630 14065 -80 -71 -120 C
ATOM 290 C GLN A 38 -29.669 -28.529 19.380 1.00118.13 C
ANISOU 290 C GLN A 38 15565 14907 14414 -70 -87 -112 C
ATOM 291 O GLN A 38 -29.800 -29.682 19.787 1.00124.05 O
ANISOU 291 O GLN A 38 16324 15638 15169 -88 -111 -98 O
ATOM 292 CB GLN A 38 -32.048 -28.451 18.531 1.00115.03 C
ANISOU 292 CB GLN A 38 15198 14577 13931 -114 -98 -99 C
ATOM 293 CG GLN A 38 -33.055 -27.784 17.618 1.00116.66 C
ANISOU 293 CG GLN A 38 15415 14815 14095 -125 -88 -104 C
ATOM 294 CD GLN A 38 -34.396 -28.490 17.609 1.00120.77 C
ANISOU 294 CD GLN A 38 15952 15362 14575 -160 -112 -85 C
ATOM 295 OE1 GLN A 38 -34.872 -28.965 18.644 1.00123.64 O
ANISOU 295 OE1 GLN A 38 16301 15746 14929 -175 -141 -63 O
ATOM 296 NE2 GLN A 38 -35.030 -28.544 16.445 1.00122.23 N
ANISOU 296 NE2 GLN A 38 16163 15546 14732 -175 -102 -92 N
ATOM 297 N ASN A 39 -28.700 -27.722 19.791 1.00114.32 N
ANISOU 297 N ASN A 39 15057 14416 13962 -41 -76 -119 N
ATOM 298 CA ASN A 39 -27.756 -28.097 20.834 1.00114.62 C
ANISOU 298 CA ASN A 39 15077 14431 14044 -30 -92 -109 C
ATOM 299 C ASN A 39 -27.236 -26.834 21.504 1.00111.73 C
ANISOU 299 C ASN A 39 14677 14085 13690 -5 -89 -110 C
ATOM 300 O ASN A 39 -27.564 -25.716 21.086 1.00111.11 O
ANISOU 300 O ASN A 39 14591 14035 13590 4 -73 -120 O
ATOM 301 CB ASN A 39 -26.621 -28.965 20.273 1.00118.27 C
ANISOU 301 CB ASN A 39 15552 14828 14556 -19 -77 -125 C
ATOM 302 CG ASN A 39 -25.979 -28.360 19.048 1.00119.04 C
ANISOU 302 CG ASN A 39 15658 14905 14666 2 -33 -154 C
ATOM 303 OD1 ASN A 39 -25.121 -27.484 19.153 1.00117.19 O
ANISOU 303 OD1 ASN A 39 15402 14666 14458 28 -17 -162 O
ATOM 304 ND2 ASN A 39 -26.392 -28.825 17.874 1.00120.46 N
ANISOU 304 ND2 ASN A 39 15869 15074 14826 -11 -15 -169 N
ATOM 305 N VAL A 40 -26.422 -27.017 22.537 1.00111.54 N
ANISOU 305 N VAL A 40 14633 14045 13702 4 -106 -100 N
ATOM 306 CA VAL A 40 -26.024 -25.915 23.405 1.00108.61 C
ANISOU 306 CA VAL A 40 14230 13697 13339 23 -111 -97 C
ATOM 307 C VAL A 40 -25.244 -24.845 22.637 1.00105.47 C
ANISOU 307 C VAL A 40 13825 13285 12964 54 -77 -119 C
ATOM 308 O VAL A 40 -25.445 -23.647 22.852 1.00106.49 O
ANISOU 308 O VAL A 40 13935 13448 13078 65 -75 -122 O
ATOM 309 CB VAL A 40 -25.220 -26.433 24.613 1.00110.69 C
ANISOU 309 CB VAL A 40 14478 13941 13640 25 -139 -80 C
ATOM 310 CG1 VAL A 40 -24.720 -25.286 25.469 1.00111.82 C
ANISOU 310 CG1 VAL A 40 14589 14104 13793 45 -143 -79 C
ATOM 311 CG2 VAL A 40 -26.076 -27.371 25.450 1.00110.76 C
ANISOU 311 CG2 VAL A 40 14492 13972 13621 -9 -175 -54 C
ATOM 312 N THR A 41 -24.378 -25.273 21.729 1.00102.99 N
ANISOU 312 N THR A 41 13525 12923 12684 65 -52 -135 N
ATOM 313 CA THR A 41 -23.573 -24.323 20.971 1.00102.00 C
ANISOU 313 CA THR A 41 13392 12783 12581 91 -18 -154 C
ATOM 314 C THR A 41 -24.450 -23.417 20.102 1.00100.74 C
ANISOU 314 C THR A 41 13241 12659 12376 86 -2 -163 C
ATOM 315 O THR A 41 -24.205 -22.214 20.007 1.00105.96 O
ANISOU 315 O THR A 41 13884 13334 13040 104 9 -168 O
ATOM 316 CB THR A 41 -22.530 -25.043 20.112 1.00103.30 C
ANISOU 316 CB THR A 41 13571 12892 12788 101 9 -172 C
ATOM 317 OG1 THR A 41 -21.892 -26.052 20.901 1.00109.97 O
ANISOU 317 OG1 THR A 41 14409 13700 13673 101 -12 -162 O
ATOM 318 CG2 THR A 41 -21.485 -24.064 19.612 1.00101.19 C
ANISOU 318 CG2 THR A 41 13287 12608 12551 129 40 -187 C
ATOM 319 N ASN A 42 -25.482 -23.986 19.490 1.00 98.19 N
ANISOU 319 N ASN A 42 12944 12350 12015 62 -3 -162 N
ATOM 320 CA ASN A 42 -26.336 -23.197 18.610 1.00 96.36 C
ANISOU 320 CA ASN A 42 12722 12149 11742 54 10 -168 C
ATOM 321 C ASN A 42 -27.269 -22.268 19.374 1.00 95.80 C
ANISOU 321 C ASN A 42 12628 12130 11640 52 -12 -156 C
ATOM 322 O ASN A 42 -27.758 -21.294 18.799 1.00 96.05 O
ANISOU 322 O ASN A 42 12657 12186 11651 54 -4 -161 O
ATOM 323 CB ASN A 42 -27.136 -24.106 17.678 1.00 97.29 C
ANISOU 323 CB ASN A 42 12875 12263 11828 28 16 -171 C
ATOM 324 CG ASN A 42 -26.303 -24.659 16.537 1.00 97.36 C
ANISOU 324 CG ASN A 42 12907 12226 11860 32 48 -192 C
ATOM 325 OD1 ASN A 42 -25.569 -23.930 15.871 1.00 99.14 O
ANISOU 325 OD1 ASN A 42 13127 12440 12101 49 77 -206 O
ATOM 326 ND2 ASN A 42 -26.424 -25.955 16.296 1.00102.49 N
ANISOU 326 ND2 ASN A 42 13581 12849 12510 16 45 -195 N
ATOM 327 N TYR A 43 -27.525 -22.553 20.652 1.00 95.34 N
ANISOU 327 N TYR A 43 12554 12091 11580 46 -42 -141 N
ATOM 328 CA TYR A 43 -28.375 -21.663 21.445 1.00 96.69 C
ANISOU 328 CA TYR A 43 12701 12314 11722 45 -62 -134 C
ATOM 329 C TYR A 43 -27.711 -20.310 21.668 1.00 94.27 C
ANISOU 329 C TYR A 43 12368 12012 11439 74 -54 -143 C
ATOM 330 O TYR A 43 -28.379 -19.276 21.668 1.00 91.54 O
ANISOU 330 O TYR A 43 12007 11701 11072 78 -58 -147 O
ATOM 331 CB TYR A 43 -28.771 -22.321 22.762 1.00100.76 C
ANISOU 331 CB TYR A 43 13206 12851 12227 29 -93 -115 C
ATOM 332 CG TYR A 43 -29.595 -23.567 22.574 1.00109.49 C
ANISOU 332 CG TYR A 43 14336 13959 13306 -2 -105 -103 C
ATOM 333 CD1 TYR A 43 -30.591 -23.628 21.590 1.00111.15 C
ANISOU 333 CD1 TYR A 43 14567 14184 13481 -19 -97 -106 C
ATOM 334 CD2 TYR A 43 -29.391 -24.684 23.383 1.00112.72 C
ANISOU 334 CD2 TYR A 43 14748 14354 13725 -17 -127 -86 C
ATOM 335 CE1 TYR A 43 -31.349 -24.771 21.412 1.00114.98 C
ANISOU 335 CE1 TYR A 43 15076 14669 13943 -49 -109 -94 C
ATOM 336 CE2 TYR A 43 -30.143 -25.838 23.212 1.00116.88 C
ANISOU 336 CE2 TYR A 43 15297 14881 14230 -47 -141 -73 C
ATOM 337 CZ TYR A 43 -31.123 -25.872 22.230 1.00118.05 C
ANISOU 337 CZ TYR A 43 15467 15044 14344 -63 -132 -78 C
ATOM 338 OH TYR A 43 -31.877 -27.005 22.053 1.00125.16 O
ANISOU 338 OH TYR A 43 16390 15943 15222 -93 -147 -64 O
ATOM 339 N PHE A 44 -26.394 -20.312 21.852 1.00 95.45 N
ANISOU 339 N PHE A 44 12509 12124 11634 95 -45 -147 N
ATOM 340 CA PHE A 44 -25.650 -19.056 21.874 1.00 95.13 C
ANISOU 340 CA PHE A 44 12446 12081 11620 122 -36 -156 C
ATOM 341 C PHE A 44 -25.566 -18.423 20.486 1.00 91.81 C
ANISOU 341 C PHE A 44 12036 11649 11197 128 -8 -169 C
ATOM 342 O PHE A 44 -25.427 -17.205 20.379 1.00 91.09 O
ANISOU 342 O PHE A 44 11929 11570 11113 144 -5 -174 O
ATOM 343 CB PHE A 44 -24.259 -19.267 22.458 1.00 96.36 C
ANISOU 343 CB PHE A 44 12589 12198 11826 141 -36 -155 C
ATOM 344 CG PHE A 44 -24.260 -19.648 23.902 1.00 95.51 C
ANISOU 344 CG PHE A 44 12466 12103 11721 136 -67 -141 C
ATOM 345 CD1 PHE A 44 -24.639 -18.729 24.878 1.00 97.47 C
ANISOU 345 CD1 PHE A 44 12688 12391 11955 142 -87 -139 C
ATOM 346 CD2 PHE A 44 -23.873 -20.925 24.293 1.00 94.61 C
ANISOU 346 CD2 PHE A 44 12362 11961 11624 124 -78 -130 C
ATOM 347 CE1 PHE A 44 -24.648 -19.082 26.216 1.00 98.44 C
ANISOU 347 CE1 PHE A 44 12797 12529 12075 133 -116 -126 C
ATOM 348 CE2 PHE A 44 -23.870 -21.284 25.635 1.00 96.26 C
ANISOU 348 CE2 PHE A 44 12558 12184 11835 115 -109 -114 C
ATOM 349 CZ PHE A 44 -24.255 -20.359 26.600 1.00 97.73 C
ANISOU 349 CZ PHE A 44 12720 12414 12001 119 -127 -112 C
ATOM 350 N VAL A 45 -25.654 -19.237 19.436 1.00 89.28 N
ANISOU 350 N VAL A 45 11746 11307 10868 113 12 -173 N
ATOM 351 CA VAL A 45 -25.716 -18.705 18.077 1.00 87.78 C
ANISOU 351 CA VAL A 45 11571 11113 10667 112 37 -183 C
ATOM 352 C VAL A 45 -27.041 -17.971 17.851 1.00 86.82 C
ANISOU 352 C VAL A 45 11448 11035 10502 99 24 -179 C
ATOM 353 O VAL A 45 -27.074 -16.927 17.198 1.00 86.23 O
ANISOU 353 O VAL A 45 11369 10969 10426 105 33 -183 O
ATOM 354 CB VAL A 45 -25.508 -19.825 17.038 1.00 87.36 C
ANISOU 354 CB VAL A 45 11552 11028 10611 97 61 -191 C
ATOM 355 CG1 VAL A 45 -25.766 -19.334 15.627 1.00 87.15 C
ANISOU 355 CG1 VAL A 45 11545 11005 10563 88 85 -200 C
ATOM 356 CG2 VAL A 45 -24.101 -20.388 17.148 1.00 87.31 C
ANISOU 356 CG2 VAL A 45 11543 10976 10656 114 77 -199 C
ATOM 357 N VAL A 46 -28.127 -18.509 18.398 1.00 85.28 N
ANISOU 357 N VAL A 46 11257 10869 10276 80 2 -169 N
ATOM 358 CA VAL A 46 -29.426 -17.848 18.284 1.00 84.21 C
ANISOU 358 CA VAL A 46 11116 10776 10103 68 -12 -165 C
ATOM 359 C VAL A 46 -29.472 -16.599 19.165 1.00 86.90 C
ANISOU 359 C VAL A 46 11420 11143 10454 88 -29 -167 C
ATOM 360 O VAL A 46 -30.023 -15.569 18.766 1.00 84.94 O
ANISOU 360 O VAL A 46 11162 10916 10196 91 -32 -170 O
ATOM 361 CB VAL A 46 -30.573 -18.819 18.613 1.00 83.60 C
ANISOU 361 CB VAL A 46 11052 10723 9990 40 -31 -154 C
ATOM 362 CG1 VAL A 46 -31.914 -18.119 18.540 1.00 83.43 C
ANISOU 362 CG1 VAL A 46 11021 10745 9933 29 -46 -151 C
ATOM 363 CG2 VAL A 46 -30.557 -19.993 17.653 1.00 82.32 C
ANISOU 363 CG2 VAL A 46 10928 10531 9819 20 -16 -155 C
ATOM 364 N SER A 47 -28.885 -16.685 20.355 1.00 90.17 N
ANISOU 364 N SER A 47 11814 11557 10890 102 -40 -166 N
ATOM 365 CA SER A 47 -28.739 -15.501 21.203 1.00 90.41 C
ANISOU 365 CA SER A 47 11810 11607 10934 124 -54 -171 C
ATOM 366 C SER A 47 -27.901 -14.425 20.503 1.00 89.69 C
ANISOU 366 C SER A 47 11711 11493 10873 145 -39 -179 C
ATOM 367 O SER A 47 -28.112 -13.233 20.723 1.00 90.39 O
ANISOU 367 O SER A 47 11776 11601 10967 160 -49 -185 O
ATOM 368 CB SER A 47 -28.130 -15.874 22.556 1.00 88.75 C
ANISOU 368 CB SER A 47 11584 11396 10743 131 -69 -167 C
ATOM 369 OG SER A 47 -27.893 -14.716 23.338 1.00 86.10 O
ANISOU 369 OG SER A 47 11217 11077 10422 153 -81 -174 O
ATOM 370 N LEU A 48 -26.959 -14.850 19.661 1.00 86.84 N
ANISOU 370 N LEU A 48 11370 11093 10534 148 -14 -180 N
ATOM 371 CA LEU A 48 -26.206 -13.913 18.838 1.00 82.24 C
ANISOU 371 CA LEU A 48 10782 10489 9975 163 3 -186 C
ATOM 372 C LEU A 48 -27.098 -13.277 17.775 1.00 78.37 C
ANISOU 372 C LEU A 48 10302 10017 9457 150 6 -185 C
ATOM 373 O LEU A 48 -27.220 -12.049 17.705 1.00 77.38 O
ANISOU 373 O LEU A 48 10158 9904 9340 161 -3 -187 O
ATOM 374 CB LEU A 48 -25.004 -14.615 18.201 1.00 84.68 C
ANISOU 374 CB LEU A 48 11109 10755 10312 166 32 -189 C
ATOM 375 CG LEU A 48 -23.788 -13.761 17.842 1.00 86.39 C
ANISOU 375 CG LEU A 48 11311 10945 10568 188 48 -193 C
ATOM 376 CD1 LEU A 48 -23.592 -12.653 18.857 1.00 87.91 C
ANISOU 376 CD1 LEU A 48 11469 11152 10781 210 25 -192 C
ATOM 377 CD2 LEU A 48 -22.536 -14.618 17.750 1.00 86.34 C
ANISOU 377 CD2 LEU A 48 11311 10897 10597 195 70 -197 C
ATOM 378 N ALA A 49 -27.737 -14.110 16.956 1.00 78.82 N
ANISOU 378 N ALA A 49 10390 10075 9483 125 16 -183 N
ATOM 379 CA ALA A 49 -28.624 -13.611 15.904 1.00 78.77 C
ANISOU 379 CA ALA A 49 10396 10084 9448 108 16 -180 C
ATOM 380 C ALA A 49 -29.813 -12.838 16.473 1.00 78.48 C
ANISOU 380 C ALA A 49 10336 10088 9393 107 -13 -177 C
ATOM 381 O ALA A 49 -30.408 -12.033 15.765 1.00 78.22 O
ANISOU 381 O ALA A 49 10302 10067 9350 101 -19 -174 O
ATOM 382 CB ALA A 49 -29.106 -14.751 15.018 1.00 79.55 C
ANISOU 382 CB ALA A 49 10533 10177 9517 80 30 -178 C
ATOM 383 N ALA A 50 -30.150 -13.078 17.741 1.00 75.96 N
ANISOU 383 N ALA A 50 9999 9790 9072 113 -32 -178 N
ATOM 384 CA ALA A 50 -31.211 -12.314 18.392 1.00 75.49 C
ANISOU 384 CA ALA A 50 9913 9771 9000 116 -57 -180 C
ATOM 385 C ALA A 50 -30.836 -10.835 18.488 1.00 75.64 C
ANISOU 385 C ALA A 50 9904 9790 9048 141 -66 -187 C
ATOM 386 O ALA A 50 -31.641 -9.959 18.153 1.00 73.09 O
ANISOU 386 O ALA A 50 9568 9485 8717 139 -79 -188 O
ATOM 387 CB ALA A 50 -31.519 -12.889 19.765 1.00 76.37 C
ANISOU 387 CB ALA A 50 10010 9906 9102 115 -73 -180 C
ATOM 388 N ALA A 51 -29.608 -10.562 18.925 1.00 78.39 N
ANISOU 388 N ALA A 51 10240 10114 9430 163 -59 -191 N
ATOM 389 CA ALA A 51 -29.120 -9.185 19.013 1.00 80.30 C
ANISOU 389 CA ALA A 51 10456 10351 9705 187 -68 -197 C
ATOM 390 C ALA A 51 -28.932 -8.558 17.631 1.00 81.47 C
ANISOU 390 C ALA A 51 10616 10480 9858 181 -57 -191 C
ATOM 391 O ALA A 51 -29.132 -7.356 17.469 1.00 81.37 O
ANISOU 391 O ALA A 51 10584 10474 9860 191 -72 -193 O
ATOM 392 CB ALA A 51 -27.828 -9.124 19.808 1.00 81.11 C
ANISOU 392 CB ALA A 51 10544 10431 9843 209 -65 -201 C
ATOM 393 N ASP A 52 -28.565 -9.372 16.641 1.00 81.96 N
ANISOU 393 N ASP A 52 10710 10521 9910 164 -31 -184 N
ATOM 394 CA ASP A 52 -28.346 -8.867 15.286 1.00 82.38 C
ANISOU 394 CA ASP A 52 10778 10558 9963 154 -18 -178 C
ATOM 395 C ASP A 52 -29.646 -8.412 14.626 1.00 82.57 C
ANISOU 395 C ASP A 52 10807 10607 9959 135 -35 -171 C
ATOM 396 O ASP A 52 -29.651 -7.425 13.886 1.00 82.84 O
ANISOU 396 O ASP A 52 10837 10638 10003 133 -41 -165 O
ATOM 397 CB ASP A 52 -27.644 -9.917 14.430 1.00 84.78 C
ANISOU 397 CB ASP A 52 11115 10835 10260 139 16 -176 C
ATOM 398 CG ASP A 52 -26.156 -10.005 14.710 1.00 87.69 C
ANISOU 398 CG ASP A 52 11477 11174 10668 160 35 -181 C
ATOM 399 OD1 ASP A 52 -25.565 -8.984 15.131 1.00 89.50 O
ANISOU 399 OD1 ASP A 52 11678 11398 10929 182 24 -181 O
ATOM 400 OD2 ASP A 52 -25.570 -11.091 14.506 1.00 90.16 O
ANISOU 400 OD2 ASP A 52 11810 11466 10982 154 58 -185 O
ATOM 401 N ILE A 53 -30.744 -9.109 14.905 1.00 82.15 N
ANISOU 401 N ILE A 53 10761 10577 9874 119 -44 -171 N
ATOM 402 CA ILE A 53 -32.048 -8.664 14.420 1.00 80.71 C
ANISOU 402 CA ILE A 53 10578 10419 9668 102 -64 -165 C
ATOM 403 C ILE A 53 -32.428 -7.334 15.085 1.00 80.36 C
ANISOU 403 C ILE A 53 10494 10392 9647 124 -93 -171 C
ATOM 404 O ILE A 53 -32.869 -6.397 14.409 1.00 78.97 O
ANISOU 404 O ILE A 53 10310 10218 9475 120 -108 -165 O
ATOM 405 CB ILE A 53 -33.126 -9.736 14.644 1.00 78.85 C
ANISOU 405 CB ILE A 53 10358 10207 9395 81 -69 -163 C
ATOM 406 CG1 ILE A 53 -32.774 -11.005 13.872 1.00 78.42 C
ANISOU 406 CG1 ILE A 53 10345 10131 9320 59 -43 -158 C
ATOM 407 CG2 ILE A 53 -34.484 -9.238 14.174 1.00 77.67 C
ANISOU 407 CG2 ILE A 53 10204 10083 9226 65 -91 -156 C
ATOM 408 CD1 ILE A 53 -33.653 -12.195 14.202 1.00 76.32 C
ANISOU 408 CD1 ILE A 53 10094 9883 9022 39 -47 -155 C
ATOM 409 N LEU A 54 -32.218 -7.244 16.396 1.00 80.52 N
ANISOU 409 N LEU A 54 10487 10423 9683 147 -102 -183 N
ATOM 410 CA LEU A 54 -32.549 -6.036 17.146 1.00 81.59 C
ANISOU 410 CA LEU A 54 10583 10575 9841 169 -129 -195 C
ATOM 411 C LEU A 54 -31.713 -4.823 16.740 1.00 81.72 C
ANISOU 411 C LEU A 54 10586 10568 9896 187 -134 -193 C
ATOM 412 O LEU A 54 -32.073 -3.698 17.077 1.00 79.97 O
ANISOU 412 O LEU A 54 10334 10355 9695 203 -159 -201 O
ATOM 413 CB LEU A 54 -32.421 -6.292 18.648 1.00 81.30 C
ANISOU 413 CB LEU A 54 10524 10556 9808 187 -134 -209 C
ATOM 414 CG LEU A 54 -33.442 -7.259 19.255 1.00 79.04 C
ANISOU 414 CG LEU A 54 10242 10304 9485 170 -138 -211 C
ATOM 415 CD1 LEU A 54 -33.063 -7.654 20.673 1.00 77.09 C
ANISOU 415 CD1 LEU A 54 9980 10070 9241 182 -140 -221 C
ATOM 416 CD2 LEU A 54 -34.845 -6.672 19.222 1.00 78.48 C
ANISOU 416 CD2 LEU A 54 10152 10266 9402 164 -159 -215 C
ATOM 417 N VAL A 55 -30.611 -5.044 16.027 1.00 83.11 N
ANISOU 417 N VAL A 55 10784 10713 10083 184 -111 -184 N
ATOM 418 CA VAL A 55 -29.831 -3.932 15.493 1.00 84.36 C
ANISOU 418 CA VAL A 55 10930 10847 10274 195 -115 -178 C
ATOM 419 C VAL A 55 -30.584 -3.259 14.349 1.00 85.43 C
ANISOU 419 C VAL A 55 11072 10986 10400 176 -128 -165 C
ATOM 420 O VAL A 55 -30.722 -2.033 14.313 1.00 87.50 O
ANISOU 420 O VAL A 55 11310 11247 10690 187 -154 -164 O
ATOM 421 CB VAL A 55 -28.434 -4.400 15.047 1.00 83.85 C
ANISOU 421 CB VAL A 55 10885 10752 10223 195 -83 -172 C
ATOM 422 CG1 VAL A 55 -27.730 -3.317 14.252 1.00 83.25 C
ANISOU 422 CG1 VAL A 55 10802 10654 10174 199 -85 -162 C
ATOM 423 CG2 VAL A 55 -27.597 -4.780 16.253 1.00 84.13 C
ANISOU 423 CG2 VAL A 55 10907 10780 10280 218 -78 -184 C
ATOM 424 N GLY A 56 -31.075 -4.060 13.410 1.00 84.38 N
ANISOU 424 N GLY A 56 10972 10856 10232 146 -114 -154 N
ATOM 425 CA GLY A 56 -31.810 -3.517 12.272 1.00 82.12 C
ANISOU 425 CA GLY A 56 10696 10573 9934 122 -128 -139 C
ATOM 426 C GLY A 56 -33.181 -2.974 12.649 1.00 78.86 C
ANISOU 426 C GLY A 56 10259 10186 9517 123 -162 -142 C
ATOM 427 O GLY A 56 -33.676 -2.047 12.014 1.00 79.96 O
ANISOU 427 O GLY A 56 10390 10325 9667 116 -186 -132 O
ATOM 428 N VAL A 57 -33.796 -3.539 13.679 1.00 75.34 N
ANISOU 428 N VAL A 57 9802 9764 9060 132 -166 -157 N
ATOM 429 CA VAL A 57 -35.145 -3.130 14.044 1.00 78.00 C
ANISOU 429 CA VAL A 57 10116 10129 9392 132 -195 -163 C
ATOM 430 C VAL A 57 -35.137 -1.880 14.930 1.00 82.91 C
ANISOU 430 C VAL A 57 10692 10756 10055 164 -222 -179 C
ATOM 431 O VAL A 57 -36.038 -1.043 14.842 1.00 86.15 O
ANISOU 431 O VAL A 57 11079 11177 10478 166 -251 -181 O
ATOM 432 CB VAL A 57 -35.910 -4.293 14.696 1.00 78.58 C
ANISOU 432 CB VAL A 57 10196 10230 9431 122 -187 -169 C
ATOM 433 CG1 VAL A 57 -37.329 -3.892 15.059 1.00 77.18 C
ANISOU 433 CG1 VAL A 57 9992 10084 9248 120 -215 -176 C
ATOM 434 CG2 VAL A 57 -35.955 -5.479 13.750 1.00 79.14 C
ANISOU 434 CG2 VAL A 57 10312 10293 9464 89 -164 -154 C
ATOM 435 N LEU A 58 -34.121 -1.745 15.774 1.00 86.95 N
ANISOU 435 N LEU A 58 11191 11257 10589 190 -213 -192 N
ATOM 436 CA LEU A 58 -34.068 -0.651 16.743 1.00 87.60 C
ANISOU 436 CA LEU A 58 11231 11345 10709 221 -238 -212 C
ATOM 437 C LEU A 58 -32.807 0.191 16.639 1.00 84.21 C
ANISOU 437 C LEU A 58 10793 10883 10318 240 -239 -209 C
ATOM 438 O LEU A 58 -32.891 1.415 16.528 1.00 81.48 O
ANISOU 438 O LEU A 58 10423 10528 10007 253 -267 -211 O
ATOM 439 CB LEU A 58 -34.227 -1.198 18.166 1.00 88.23 C
ANISOU 439 CB LEU A 58 11296 11452 10778 236 -233 -234 C
ATOM 440 CG LEU A 58 -35.602 -1.711 18.602 1.00 87.86 C
ANISOU 440 CG LEU A 58 11240 11443 10698 224 -240 -243 C
ATOM 441 CD1 LEU A 58 -35.479 -2.574 19.849 1.00 83.84 C
ANISOU 441 CD1 LEU A 58 10728 10958 10170 230 -227 -256 C
ATOM 442 CD2 LEU A 58 -36.585 -0.572 18.832 1.00 90.27 C
ANISOU 442 CD2 LEU A 58 11507 11767 11026 238 -272 -258 C
ATOM 443 N ALA A 59 -31.637 -0.447 16.666 1.00 83.38 N
ANISOU 443 N ALA A 59 10708 10759 10213 241 -212 -204 N
ATOM 444 CA ALA A 59 -30.374 0.294 16.754 1.00 81.98 C
ANISOU 444 CA ALA A 59 10519 10553 10075 261 -213 -203 C
ATOM 445 C ALA A 59 -30.110 1.147 15.509 1.00 83.52 C
ANISOU 445 C ALA A 59 10720 10724 10288 250 -221 -182 C
ATOM 446 O ALA A 59 -29.690 2.297 15.626 1.00 83.36 O
ANISOU 446 O ALA A 59 10676 10690 10308 268 -244 -183 O
ATOM 447 CB ALA A 59 -29.217 -0.661 17.008 1.00 81.67 C
ANISOU 447 CB ALA A 59 10500 10498 10032 263 -180 -200 C
ATOM 448 N ILE A 60 -30.356 0.583 14.331 1.00 84.30 N
ANISOU 448 N ILE A 60 10851 10821 10357 219 -205 -163 N
ATOM 449 CA ILE A 60 -30.136 1.286 13.068 1.00 82.88 C
ANISOU 449 CA ILE A 60 10681 10624 10187 201 -212 -139 C
ATOM 450 C ILE A 60 -31.153 2.426 12.890 1.00 80.21 C
ANISOU 450 C ILE A 60 10318 10292 9866 202 -255 -137 C
ATOM 451 O ILE A 60 -30.771 3.517 12.484 1.00 76.88 O
ANISOU 451 O ILE A 60 9882 9851 9478 206 -276 -125 O
ATOM 452 CB ILE A 60 -30.135 0.327 11.863 1.00 83.02 C
ANISOU 452 CB ILE A 60 10742 10639 10164 165 -182 -122 C
ATOM 453 CG1 ILE A 60 -28.848 -0.503 11.846 1.00 82.24 C
ANISOU 453 CG1 ILE A 60 10663 10524 10062 167 -141 -123 C
ATOM 454 CG2 ILE A 60 -30.295 1.101 10.563 1.00 83.50 C
ANISOU 454 CG2 ILE A 60 10810 10689 10225 140 -197 -97 C
ATOM 455 CD1 ILE A 60 -28.813 -1.587 10.788 1.00 81.85 C
ANISOU 455 CD1 ILE A 60 10655 10472 9971 134 -108 -113 C
ATOM 456 N PRO A 61 -32.449 2.191 13.190 1.00 80.93 N
ANISOU 456 N PRO A 61 10402 10408 9938 197 -270 -147 N
ATOM 457 CA PRO A 61 -33.360 3.344 13.230 1.00 83.73 C
ANISOU 457 CA PRO A 61 10725 10768 10321 205 -313 -150 C
ATOM 458 C PRO A 61 -32.963 4.388 14.278 1.00 86.51 C
ANISOU 458 C PRO A 61 11036 11113 10721 243 -337 -171 C
ATOM 459 O PRO A 61 -33.106 5.590 14.021 1.00 88.68 O
ANISOU 459 O PRO A 61 11288 11373 11033 251 -371 -167 O
ATOM 460 CB PRO A 61 -34.714 2.710 13.552 1.00 82.89 C
ANISOU 460 CB PRO A 61 10617 10693 10184 197 -317 -160 C
ATOM 461 CG PRO A 61 -34.610 1.345 12.978 1.00 80.26 C
ANISOU 461 CG PRO A 61 10327 10365 9802 168 -281 -148 C
ATOM 462 CD PRO A 61 -33.199 0.922 13.240 1.00 79.85 C
ANISOU 462 CD PRO A 61 10289 10296 9756 179 -250 -150 C
ATOM 463 N PHE A 62 -32.458 3.953 15.432 1.00 86.42 N
ANISOU 463 N PHE A 62 11017 11110 10710 266 -320 -194 N
ATOM 464 CA PHE A 62 -31.981 4.902 16.435 1.00 87.05 C
ANISOU 464 CA PHE A 62 11061 11182 10833 301 -341 -215 C
ATOM 465 C PHE A 62 -30.811 5.732 15.914 1.00 88.41 C
ANISOU 465 C PHE A 62 11231 11318 11041 307 -348 -198 C
ATOM 466 O PHE A 62 -30.768 6.944 16.115 1.00 88.04 O
ANISOU 466 O PHE A 62 11155 11258 11038 325 -382 -204 O
ATOM 467 CB PHE A 62 -31.581 4.181 17.725 1.00 89.04 C
ANISOU 467 CB PHE A 62 11309 11450 11073 320 -321 -238 C
ATOM 468 CG PHE A 62 -32.742 3.686 18.537 1.00 90.65 C
ANISOU 468 CG PHE A 62 11501 11692 11251 321 -323 -261 C
ATOM 469 CD1 PHE A 62 -34.028 4.196 18.348 1.00 90.14 C
ANISOU 469 CD1 PHE A 62 11417 11644 11187 318 -349 -268 C
ATOM 470 CD2 PHE A 62 -32.548 2.701 19.505 1.00 90.78 C
ANISOU 470 CD2 PHE A 62 11523 11728 11241 325 -300 -274 C
ATOM 471 CE1 PHE A 62 -35.089 3.727 19.106 1.00 88.64 C
ANISOU 471 CE1 PHE A 62 11214 11493 10973 319 -348 -288 C
ATOM 472 CE2 PHE A 62 -33.610 2.233 20.262 1.00 88.34 C
ANISOU 472 CE2 PHE A 62 11202 11457 10904 323 -302 -293 C
ATOM 473 CZ PHE A 62 -34.875 2.730 20.047 1.00 87.04 C
ANISOU 473 CZ PHE A 62 11019 11312 10740 320 -324 -300 C
ATOM 474 N ALA A 63 -29.877 5.079 15.224 1.00 90.02 N
ANISOU 474 N ALA A 63 11467 11507 11230 289 -316 -176 N
ATOM 475 CA ALA A 63 -28.687 5.767 14.712 1.00 89.36 C
ANISOU 475 CA ALA A 63 11383 11392 11179 291 -318 -158 C
ATOM 476 C ALA A 63 -29.048 6.824 13.669 1.00 88.94 C
ANISOU 476 C ALA A 63 11323 11324 11145 276 -350 -135 C
ATOM 477 O ALA A 63 -28.376 7.847 13.576 1.00 86.73 O
ANISOU 477 O ALA A 63 11027 11022 10907 286 -371 -127 O
ATOM 478 CB ALA A 63 -27.690 4.771 14.147 1.00 90.17 C
ANISOU 478 CB ALA A 63 11519 11485 11257 274 -273 -142 C
ATOM 479 N ILE A 64 -30.104 6.580 12.897 1.00 88.14 N
ANISOU 479 N ILE A 64 11237 11237 11015 249 -355 -124 N
ATOM 480 CA ILE A 64 -30.568 7.574 11.935 1.00 88.10 C
ANISOU 480 CA ILE A 64 11225 11219 11029 232 -391 -101 C
ATOM 481 C ILE A 64 -31.192 8.767 12.666 1.00 90.11 C
ANISOU 481 C ILE A 64 11436 11471 11331 261 -440 -120 C
ATOM 482 O ILE A 64 -30.996 9.919 12.268 1.00 91.98 O
ANISOU 482 O ILE A 64 11654 11684 11608 262 -475 -106 O
ATOM 483 CB ILE A 64 -31.545 6.946 10.926 1.00 86.03 C
ANISOU 483 CB ILE A 64 10991 10972 10723 195 -385 -83 C
ATOM 484 CG1 ILE A 64 -30.828 5.874 10.099 1.00 86.38 C
ANISOU 484 CG1 ILE A 64 11079 11016 10725 166 -338 -66 C
ATOM 485 CG2 ILE A 64 -32.144 8.008 10.015 1.00 86.18 C
ANISOU 485 CG2 ILE A 64 11000 10979 10764 176 -429 -59 C
ATOM 486 CD1 ILE A 64 -31.746 5.047 9.225 1.00 85.49 C
ANISOU 486 CD1 ILE A 64 10999 10920 10563 130 -327 -53 C
ATOM 487 N THR A 65 -31.912 8.498 13.747 1.00 90.74 N
ANISOU 487 N THR A 65 11497 11574 11407 283 -442 -153 N
ATOM 488 CA THR A 65 -32.576 9.570 14.484 1.00 92.75 C
ANISOU 488 CA THR A 65 11708 11828 11704 311 -485 -178 C
ATOM 489 C THR A 65 -31.564 10.476 15.189 1.00 95.08 C
ANISOU 489 C THR A 65 11977 12100 12047 342 -501 -190 C
ATOM 490 O THR A 65 -31.762 11.693 15.254 1.00 97.95 O
ANISOU 490 O THR A 65 12311 12446 12460 358 -545 -195 O
ATOM 491 CB THR A 65 -33.575 8.994 15.491 1.00 92.90 C
ANISOU 491 CB THR A 65 11712 11882 11701 325 -478 -212 C
ATOM 492 OG1 THR A 65 -34.156 7.806 14.948 1.00 94.14 O
ANISOU 492 OG1 THR A 65 11903 12062 11806 295 -450 -199 O
ATOM 493 CG2 THR A 65 -34.674 9.996 15.786 1.00 91.99 C
ANISOU 493 CG2 THR A 65 11558 11772 11623 341 -523 -232 C
ATOM 494 N ILE A 66 -30.483 9.898 15.702 1.00 93.65 N
ANISOU 494 N ILE A 66 11810 11917 11857 352 -469 -195 N
ATOM 495 CA ILE A 66 -29.455 10.697 16.364 1.00 91.73 C
ANISOU 495 CA ILE A 66 11545 11651 11658 380 -483 -205 C
ATOM 496 C ILE A 66 -28.747 11.607 15.356 1.00 92.67 C
ANISOU 496 C ILE A 66 11665 11736 11811 367 -504 -170 C
ATOM 497 O ILE A 66 -28.342 12.723 15.698 1.00 94.57 O
ANISOU 497 O ILE A 66 11878 11954 12102 388 -538 -176 O
ATOM 498 CB ILE A 66 -28.457 9.802 17.116 1.00 87.83 C
ANISOU 498 CB ILE A 66 11064 11161 11145 390 -444 -214 C
ATOM 499 CG1 ILE A 66 -29.199 8.904 18.104 1.00 88.28 C
ANISOU 499 CG1 ILE A 66 11120 11254 11167 398 -426 -244 C
ATOM 500 CG2 ILE A 66 -27.431 10.636 17.866 1.00 85.45 C
ANISOU 500 CG2 ILE A 66 10740 10838 10891 419 -461 -225 C
ATOM 501 CD1 ILE A 66 -28.359 7.773 18.653 1.00 85.61 C
ANISOU 501 CD1 ILE A 66 10803 10923 10802 398 -386 -247 C
ATOM 502 N SER A 67 -28.623 11.151 14.111 1.00 92.03 N
ANISOU 502 N SER A 67 11615 11651 11701 331 -485 -135 N
ATOM 503 CA SER A 67 -27.916 11.926 13.091 1.00 93.13 C
ANISOU 503 CA SER A 67 11758 11762 11865 313 -501 -99 C
ATOM 504 C SER A 67 -28.609 13.250 12.761 1.00 94.42 C
ANISOU 504 C SER A 67 11893 11908 12072 314 -559 -91 C
ATOM 505 O SER A 67 -27.955 14.168 12.273 1.00 96.09 O
ANISOU 505 O SER A 67 12097 12093 12320 309 -584 -67 O
ATOM 506 CB SER A 67 -27.744 11.100 11.821 1.00 94.67 C
ANISOU 506 CB SER A 67 11995 11963 12014 271 -466 -66 C
ATOM 507 OG SER A 67 -29.000 10.676 11.330 1.00 97.97 O
ANISOU 507 OG SER A 67 12424 12400 12399 249 -470 -64 O
ATOM 508 N THR A 68 -29.906 13.351 13.044 1.00 95.94 N
ANISOU 508 N THR A 68 12071 12118 12264 320 -581 -111 N
ATOM 509 CA THR A 68 -30.644 14.583 12.782 1.00 96.52 C
ANISOU 509 CA THR A 68 12115 12174 12384 324 -639 -107 C
ATOM 510 C THR A 68 -30.409 15.653 13.844 1.00 95.43 C
ANISOU 510 C THR A 68 11936 12019 12306 366 -676 -138 C
ATOM 511 O THR A 68 -30.586 16.841 13.569 1.00 97.17 O
ANISOU 511 O THR A 68 12131 12213 12577 370 -727 -129 O
ATOM 512 CB THR A 68 -32.151 14.314 12.649 1.00 95.70 C
ANISOU 512 CB THR A 68 12007 12092 12261 315 -651 -117 C
ATOM 513 OG1 THR A 68 -32.604 13.596 13.799 1.00 96.15 O
ANISOU 513 OG1 THR A 68 12055 12179 12296 339 -627 -159 O
ATOM 514 CG2 THR A 68 -32.445 13.497 11.400 1.00 94.28 C
ANISOU 514 CG2 THR A 68 11868 11924 12030 268 -628 -81 C
ATOM 515 N GLY A 69 -30.017 15.245 15.051 1.00 93.73 N
ANISOU 515 N GLY A 69 11713 11816 12085 396 -652 -174 N
ATOM 516 CA GLY A 69 -29.869 16.189 16.153 1.00 94.86 C
ANISOU 516 CA GLY A 69 11816 11946 12279 436 -685 -209 C
ATOM 517 C GLY A 69 -31.182 16.761 16.647 1.00 96.39 C
ANISOU 517 C GLY A 69 11977 12151 12497 456 -721 -243 C
ATOM 518 O GLY A 69 -31.228 17.908 17.081 1.00 98.47 O
ANISOU 518 O GLY A 69 12205 12393 12817 481 -765 -262 O
ATOM 519 N PHE A 70 -32.246 15.965 16.590 1.00 97.71 N
ANISOU 519 N PHE A 70 12152 12351 12624 444 -702 -252 N
ATOM 520 CA PHE A 70 -33.576 16.425 16.976 1.00100.27 C
ANISOU 520 CA PHE A 70 12442 12687 12967 459 -732 -283 C
ATOM 521 C PHE A 70 -33.630 16.799 18.452 1.00102.70 C
ANISOU 521 C PHE A 70 12716 13007 13299 502 -739 -339 C
ATOM 522 O PHE A 70 -32.849 16.308 19.269 1.00103.10 O
ANISOU 522 O PHE A 70 12775 13068 13329 515 -709 -354 O
ATOM 523 CB PHE A 70 -34.627 15.362 16.653 1.00 98.39 C
ANISOU 523 CB PHE A 70 12223 12485 12676 435 -705 -280 C
ATOM 524 CG PHE A 70 -34.608 14.188 17.583 1.00 95.93 C
ANISOU 524 CG PHE A 70 11924 12212 12313 442 -657 -306 C
ATOM 525 CD1 PHE A 70 -33.546 13.289 17.565 1.00 93.45 C
ANISOU 525 CD1 PHE A 70 11645 11900 11962 431 -614 -289 C
ATOM 526 CD2 PHE A 70 -35.650 13.979 18.482 1.00 96.50 C
ANISOU 526 CD2 PHE A 70 11971 12318 12375 460 -655 -347 C
ATOM 527 CE1 PHE A 70 -33.519 12.204 18.424 1.00 92.76 C
ANISOU 527 CE1 PHE A 70 11569 11845 11830 436 -574 -311 C
ATOM 528 CE2 PHE A 70 -35.638 12.887 19.340 1.00 95.04 C
ANISOU 528 CE2 PHE A 70 11799 12171 12142 462 -613 -368 C
ATOM 529 CZ PHE A 70 -34.568 11.998 19.315 1.00 93.33 C
ANISOU 529 CZ PHE A 70 11618 11953 11890 450 -575 -348 C
ATOM 530 N CYS A 71 -34.554 17.688 18.784 1.00104.57 N
ANISOU 530 N CYS A 71 12912 13241 13578 523 -780 -369 N
ATOM 531 CA CYS A 71 -34.745 18.105 20.169 1.00107.93 C
ANISOU 531 CA CYS A 71 13303 13681 14027 563 -788 -427 C
ATOM 532 C CYS A 71 -35.379 16.983 20.976 1.00105.38 C
ANISOU 532 C CYS A 71 12985 13410 13646 564 -745 -457 C
ATOM 533 O CYS A 71 -36.346 16.362 20.522 1.00108.18 O
ANISOU 533 O CYS A 71 13346 13788 13969 544 -733 -447 O
ATOM 534 CB CYS A 71 -35.613 19.356 20.233 1.00112.82 C
ANISOU 534 CB CYS A 71 13876 14282 14710 585 -843 -453 C
ATOM 535 SG CYS A 71 -34.864 20.814 19.474 1.00116.91 S
ANISOU 535 SG CYS A 71 14381 14735 15305 588 -903 -422 S
ATOM 536 N ALA A 72 -34.832 16.728 22.162 1.00102.29 N
ANISOU 536 N ALA A 72 12589 13037 13241 586 -724 -490 N
ATOM 537 CA ALA A 72 -35.352 15.694 23.050 1.00101.66 C
ANISOU 537 CA ALA A 72 12513 13008 13107 586 -685 -518 C
ATOM 538 C ALA A 72 -34.789 15.891 24.438 1.00100.64 C
ANISOU 538 C ALA A 72 12367 12890 12982 616 -680 -562 C
ATOM 539 O ALA A 72 -33.723 16.490 24.606 1.00 99.88 O
ANISOU 539 O ALA A 72 12270 12761 12918 630 -694 -559 O
ATOM 540 CB ALA A 72 -35.010 14.299 22.531 1.00100.56 C
ANISOU 540 CB ALA A 72 12420 12883 12904 552 -638 -480 C
ATOM 541 N ALA A 73 -35.518 15.393 25.434 1.00 99.72 N
ANISOU 541 N ALA A 73 12236 12821 12833 625 -660 -602 N
ATOM 542 CA ALA A 73 -35.038 15.369 26.813 1.00 98.90 C
ANISOU 542 CA ALA A 73 12120 12737 12719 647 -649 -643 C
ATOM 543 C ALA A 73 -33.741 14.574 26.889 1.00 98.95 C
ANISOU 543 C ALA A 73 12166 12736 12696 633 -620 -612 C
ATOM 544 O ALA A 73 -33.560 13.591 26.160 1.00102.32 O
ANISOU 544 O ALA A 73 12628 13164 13085 604 -592 -571 O
ATOM 545 CB ALA A 73 -36.090 14.770 27.730 1.00 96.06 C
ANISOU 545 CB ALA A 73 11744 12437 12317 648 -627 -683 C
ATOM 546 N CYS A 74 -32.837 15.003 27.767 1.00 95.42 N
ANISOU 546 N CYS A 74 11711 12277 12266 655 -628 -633 N
ATOM 547 CA CYS A 74 -31.495 14.447 27.796 1.00 92.80 C
ANISOU 547 CA CYS A 74 11411 11928 11920 645 -608 -603 C
ATOM 548 C CYS A 74 -31.489 12.940 28.068 1.00 93.89 C
ANISOU 548 C CYS A 74 11580 12103 11992 621 -562 -589 C
ATOM 549 O CYS A 74 -30.679 12.209 27.510 1.00 94.63 O
ANISOU 549 O CYS A 74 11707 12180 12069 602 -540 -549 O
ATOM 550 CB CYS A 74 -30.630 15.178 28.815 1.00 93.22 C
ANISOU 550 CB CYS A 74 11448 11967 12005 673 -627 -632 C
ATOM 551 SG CYS A 74 -28.905 14.658 28.775 1.00 91.63 S
ANISOU 551 SG CYS A 74 11281 11736 11799 663 -609 -592 S
ATOM 552 N HIS A 75 -32.403 12.476 28.911 1.00 94.85 N
ANISOU 552 N HIS A 75 11689 12274 12078 621 -548 -623 N
ATOM 553 CA HIS A 75 -32.481 11.055 29.229 1.00 97.03 C
ANISOU 553 CA HIS A 75 11990 12585 12290 597 -509 -610 C
ATOM 554 C HIS A 75 -33.104 10.247 28.102 1.00 97.79 C
ANISOU 554 C HIS A 75 12111 12687 12359 568 -491 -574 C
ATOM 555 O HIS A 75 -32.694 9.111 27.852 1.00 98.97 O
ANISOU 555 O HIS A 75 12294 12839 12471 544 -461 -543 O
ATOM 556 CB HIS A 75 -33.226 10.842 30.543 1.00 97.73 C
ANISOU 556 CB HIS A 75 12057 12729 12348 604 -501 -657 C
ATOM 557 CG HIS A 75 -32.465 11.305 31.746 1.00 99.48 C
ANISOU 557 CG HIS A 75 12266 12952 12581 626 -511 -688 C
ATOM 558 ND1 HIS A 75 -32.456 12.620 32.161 1.00100.33 N
ANISOU 558 ND1 HIS A 75 12339 13044 12736 657 -544 -727 N
ATOM 559 CD2 HIS A 75 -31.677 10.630 32.616 1.00100.30 C
ANISOU 559 CD2 HIS A 75 12386 13069 12655 619 -494 -686 C
ATOM 560 CE1 HIS A 75 -31.700 12.733 33.239 1.00101.47 C
ANISOU 560 CE1 HIS A 75 12481 13194 12878 668 -547 -748 C
ATOM 561 NE2 HIS A 75 -31.217 11.541 33.536 1.00101.88 N
ANISOU 561 NE2 HIS A 75 12563 13263 12883 646 -517 -723 N
ATOM 562 N GLY A 76 -34.088 10.821 27.417 1.00 98.66 N
ANISOU 562 N GLY A 76 12203 12794 12489 568 -510 -577 N
ATOM 563 CA GLY A 76 -34.646 10.179 26.225 1.00 99.96 C
ANISOU 563 CA GLY A 76 12391 12958 12633 540 -497 -540 C
ATOM 564 C GLY A 76 -33.597 10.013 25.136 1.00 98.07 C
ANISOU 564 C GLY A 76 12185 12674 12402 524 -491 -492 C
ATOM 565 O GLY A 76 -33.485 8.944 24.526 1.00 99.30 O
ANISOU 565 O GLY A 76 12376 12833 12520 497 -463 -460 O
ATOM 566 N CYS A 77 -32.818 11.068 24.902 1.00 94.05 N
ANISOU 566 N CYS A 77 11666 12124 11944 541 -518 -488 N
ATOM 567 CA CYS A 77 -31.686 10.979 23.985 1.00 91.82 C
ANISOU 567 CA CYS A 77 11413 11803 11673 528 -511 -445 C
ATOM 568 C CYS A 77 -30.618 10.016 24.518 1.00 93.25 C
ANISOU 568 C CYS A 77 11619 11985 11825 523 -478 -436 C
ATOM 569 O CYS A 77 -29.894 9.400 23.734 1.00 95.49 O
ANISOU 569 O CYS A 77 11935 12251 12098 503 -456 -400 O
ATOM 570 CB CYS A 77 -31.100 12.371 23.741 1.00 90.86 C
ANISOU 570 CB CYS A 77 11270 11638 11613 548 -550 -444 C
ATOM 571 SG CYS A 77 -29.623 12.434 22.696 1.00 93.04 S
ANISOU 571 SG CYS A 77 11576 11867 11909 533 -544 -394 S
ATOM 572 N LEU A 78 -30.535 9.874 25.841 1.00 90.93 N
ANISOU 572 N LEU A 78 11311 11716 11521 539 -474 -469 N
ATOM 573 CA LEU A 78 -29.534 8.994 26.437 1.00 88.88 C
ANISOU 573 CA LEU A 78 11074 11459 11239 535 -448 -460 C
ATOM 574 C LEU A 78 -29.860 7.521 26.214 1.00 88.26 C
ANISOU 574 C LEU A 78 11025 11405 11105 506 -412 -441 C
ATOM 575 O LEU A 78 -28.949 6.706 26.054 1.00 89.71 O
ANISOU 575 O LEU A 78 11235 11573 11275 494 -388 -417 O
ATOM 576 CB LEU A 78 -29.387 9.287 27.929 1.00 87.34 C
ANISOU 576 CB LEU A 78 10855 11283 11046 557 -458 -500 C
ATOM 577 CG LEU A 78 -28.110 8.807 28.614 1.00 88.66 C
ANISOU 577 CG LEU A 78 11037 11440 11211 560 -445 -492 C
ATOM 578 CD1 LEU A 78 -26.877 9.484 28.026 1.00 88.59 C
ANISOU 578 CD1 LEU A 78 11032 11378 11249 568 -458 -468 C
ATOM 579 CD2 LEU A 78 -28.197 9.055 30.111 1.00 91.32 C
ANISOU 579 CD2 LEU A 78 11352 11806 11542 577 -456 -534 C
ATOM 580 N PHE A 79 -31.149 7.179 26.190 1.00 85.67 N
ANISOU 580 N PHE A 79 10691 11111 10747 495 -408 -453 N
ATOM 581 CA PHE A 79 -31.543 5.783 26.003 1.00 85.44 C
ANISOU 581 CA PHE A 79 10690 11106 10666 467 -377 -435 C
ATOM 582 C PHE A 79 -31.306 5.316 24.569 1.00 84.78 C
ANISOU 582 C PHE A 79 10639 10996 10577 444 -363 -394 C
ATOM 583 O PHE A 79 -30.778 4.225 24.345 1.00 82.60 O
ANISOU 583 O PHE A 79 10393 10715 10274 426 -335 -372 O
ATOM 584 CB PHE A 79 -33.003 5.570 26.399 1.00 85.62 C
ANISOU 584 CB PHE A 79 10696 11177 10660 462 -379 -458 C
ATOM 585 CG PHE A 79 -33.468 4.152 26.253 1.00 86.81 C
ANISOU 585 CG PHE A 79 10874 11353 10757 432 -350 -440 C
ATOM 586 CD1 PHE A 79 -33.238 3.227 27.267 1.00 87.38 C
ANISOU 586 CD1 PHE A 79 10953 11451 10795 425 -333 -446 C
ATOM 587 CD2 PHE A 79 -34.129 3.733 25.096 1.00 85.19 C
ANISOU 587 CD2 PHE A 79 10687 11144 10536 409 -344 -415 C
ATOM 588 CE1 PHE A 79 -33.662 1.910 27.135 1.00 85.25 C
ANISOU 588 CE1 PHE A 79 10709 11204 10479 397 -310 -428 C
ATOM 589 CE2 PHE A 79 -34.553 2.419 24.958 1.00 83.30 C
ANISOU 589 CE2 PHE A 79 10474 10927 10249 381 -320 -399 C
ATOM 590 CZ PHE A 79 -34.321 1.505 25.979 1.00 83.33 C
ANISOU 590 CZ PHE A 79 10484 10955 10221 376 -303 -405 C
ATOM 591 N ILE A 80 -31.699 6.138 23.603 1.00 86.99 N
ANISOU 591 N ILE A 80 10912 11258 10883 443 -382 -385 N
ATOM 592 CA ILE A 80 -31.561 5.765 22.198 1.00 89.46 C
ANISOU 592 CA ILE A 80 11256 11549 11188 418 -370 -347 C
ATOM 593 C ILE A 80 -30.087 5.677 21.796 1.00 86.22 C
ANISOU 593 C ILE A 80 10865 11101 10793 417 -356 -324 C
ATOM 594 O ILE A 80 -29.727 4.906 20.915 1.00 89.01 O
ANISOU 594 O ILE A 80 11251 11443 11127 394 -331 -296 O
ATOM 595 CB ILE A 80 -32.348 6.713 21.279 1.00 89.46 C
ANISOU 595 CB ILE A 80 11241 11537 11211 414 -399 -341 C
ATOM 596 CG1 ILE A 80 -31.902 8.161 21.492 1.00 91.96 C
ANISOU 596 CG1 ILE A 80 11528 11829 11585 442 -434 -353 C
ATOM 597 CG2 ILE A 80 -33.846 6.573 21.537 1.00 87.87 C
ANISOU 597 CG2 ILE A 80 11024 11375 10989 410 -407 -360 C
ATOM 598 CD1 ILE A 80 -32.412 9.119 20.450 1.00 93.02 C
ANISOU 598 CD1 ILE A 80 11652 11942 11750 436 -465 -338 C
ATOM 599 N ALA A 81 -29.233 6.459 22.454 1.00 81.53 N
ANISOU 599 N ALA A 81 10252 10489 10238 442 -371 -336 N
ATOM 600 CA ALA A 81 -27.805 6.441 22.149 1.00 81.35 C
ANISOU 600 CA ALA A 81 10244 10431 10236 443 -360 -314 C
ATOM 601 C ALA A 81 -27.092 5.264 22.815 1.00 84.41 C
ANISOU 601 C ALA A 81 10649 10825 10598 440 -329 -313 C
ATOM 602 O ALA A 81 -26.105 4.754 22.271 1.00 86.48 O
ANISOU 602 O ALA A 81 10934 11063 10862 430 -307 -289 O
ATOM 603 CB ALA A 81 -27.157 7.758 22.547 1.00 79.68 C
ANISOU 603 CB ALA A 81 10003 10195 10076 470 -391 -325 C
ATOM 604 N CYS A 82 -27.579 4.838 23.980 1.00 87.14 N
ANISOU 604 N CYS A 82 10986 11203 10922 447 -329 -338 N
ATOM 605 CA CYS A 82 -26.949 3.761 24.742 1.00 88.14 C
ANISOU 605 CA CYS A 82 11126 11336 11026 443 -306 -337 C
ATOM 606 C CYS A 82 -27.516 2.374 24.457 1.00 86.26 C
ANISOU 606 C CYS A 82 10915 11119 10740 416 -279 -325 C
ATOM 607 O CYS A 82 -26.945 1.383 24.912 1.00 85.38 O
ANISOU 607 O CYS A 82 10820 11007 10613 409 -260 -318 O
ATOM 608 CB CYS A 82 -27.048 4.038 26.240 1.00 87.64 C
ANISOU 608 CB CYS A 82 11039 11297 10964 462 -323 -369 C
ATOM 609 SG CYS A 82 -25.988 5.369 26.814 1.00 91.17 S
ANISOU 609 SG CYS A 82 11459 11713 11467 493 -351 -381 S
ATOM 610 N PHE A 83 -28.635 2.282 23.741 1.00 83.67 N
ANISOU 610 N PHE A 83 10593 10808 10390 400 -279 -322 N
ATOM 611 CA PHE A 83 -29.231 0.975 23.507 1.00 79.68 C
ANISOU 611 CA PHE A 83 10113 10323 9839 374 -256 -311 C
ATOM 612 C PHE A 83 -28.343 0.076 22.656 1.00 77.15 C
ANISOU 612 C PHE A 83 9827 9974 9513 357 -227 -284 C
ATOM 613 O PHE A 83 -28.316 -1.137 22.864 1.00 78.65 O
ANISOU 613 O PHE A 83 10038 10172 9675 342 -208 -278 O
ATOM 614 CB PHE A 83 -30.623 1.091 22.902 1.00 79.95 C
ANISOU 614 CB PHE A 83 10145 10380 9852 360 -264 -313 C
ATOM 615 CG PHE A 83 -31.331 -0.225 22.770 1.00 80.29 C
ANISOU 615 CG PHE A 83 10211 10446 9847 333 -244 -304 C
ATOM 616 CD1 PHE A 83 -31.971 -0.799 23.865 1.00 79.33 C
ANISOU 616 CD1 PHE A 83 10080 10364 9698 331 -244 -320 C
ATOM 617 CD2 PHE A 83 -31.346 -0.902 21.551 1.00 79.34 C
ANISOU 617 CD2 PHE A 83 10124 10311 9710 309 -226 -278 C
ATOM 618 CE1 PHE A 83 -32.620 -2.018 23.746 1.00 78.46 C
ANISOU 618 CE1 PHE A 83 9991 10274 9545 305 -228 -309 C
ATOM 619 CE2 PHE A 83 -31.991 -2.123 21.427 1.00 78.96 C
ANISOU 619 CE2 PHE A 83 10099 10283 9621 284 -210 -270 C
ATOM 620 CZ PHE A 83 -32.629 -2.684 22.526 1.00 78.91 C
ANISOU 620 CZ PHE A 83 10082 10313 9588 282 -212 -284 C
ATOM 621 N VAL A 84 -27.611 0.669 21.718 1.00 74.80 N
ANISOU 621 N VAL A 84 9535 9642 9244 359 -226 -268 N
ATOM 622 CA VAL A 84 -26.688 -0.103 20.891 1.00 73.88 C
ANISOU 622 CA VAL A 84 9448 9497 9125 345 -197 -246 C
ATOM 623 C VAL A 84 -25.551 -0.696 21.732 1.00 74.73 C
ANISOU 623 C VAL A 84 9557 9592 9246 356 -184 -247 C
ATOM 624 O VAL A 84 -24.983 -1.724 21.375 1.00 73.17 O
ANISOU 624 O VAL A 84 9383 9379 9038 343 -157 -235 O
ATOM 625 CB VAL A 84 -26.150 0.732 19.720 1.00 71.88 C
ANISOU 625 CB VAL A 84 9198 9216 8899 343 -198 -229 C
ATOM 626 CG1 VAL A 84 -25.114 1.742 20.190 1.00 71.93 C
ANISOU 626 CG1 VAL A 84 9179 9198 8952 369 -214 -232 C
ATOM 627 CG2 VAL A 84 -25.573 -0.170 18.643 1.00 71.35 C
ANISOU 627 CG2 VAL A 84 9164 9129 8816 321 -163 -208 C
ATOM 628 N LEU A 85 -25.239 -0.056 22.855 1.00 76.68 N
ANISOU 628 N LEU A 85 9777 9841 9515 379 -205 -263 N
ATOM 629 CA LEU A 85 -24.221 -0.577 23.758 1.00 77.30 C
ANISOU 629 CA LEU A 85 9856 9909 9607 388 -198 -264 C
ATOM 630 C LEU A 85 -24.702 -1.828 24.481 1.00 79.20 C
ANISOU 630 C LEU A 85 10108 10175 9809 374 -189 -267 C
ATOM 631 O LEU A 85 -23.886 -2.661 24.887 1.00 80.92 O
ANISOU 631 O LEU A 85 10336 10378 10030 372 -177 -259 O
ATOM 632 CB LEU A 85 -23.780 0.496 24.753 1.00 74.85 C
ANISOU 632 CB LEU A 85 9514 9596 9329 415 -226 -280 C
ATOM 633 CG LEU A 85 -23.134 1.746 24.147 1.00 73.62 C
ANISOU 633 CG LEU A 85 9346 9411 9218 430 -239 -274 C
ATOM 634 CD1 LEU A 85 -22.697 2.703 25.243 1.00 74.61 C
ANISOU 634 CD1 LEU A 85 9442 9533 9374 456 -267 -292 C
ATOM 635 CD2 LEU A 85 -21.964 1.385 23.243 1.00 73.02 C
ANISOU 635 CD2 LEU A 85 9287 9297 9160 423 -214 -249 C
ATOM 636 N VAL A 86 -26.014 -1.962 24.652 1.00 79.00 N
ANISOU 636 N VAL A 86 10081 10187 9750 364 -196 -278 N
ATOM 637 CA VAL A 86 -26.576 -3.171 25.249 1.00 78.89 C
ANISOU 637 CA VAL A 86 10079 10200 9697 346 -188 -278 C
ATOM 638 C VAL A 86 -26.417 -4.349 24.287 1.00 79.96 C
ANISOU 638 C VAL A 86 10248 10317 9815 324 -161 -257 C
ATOM 639 O VAL A 86 -25.980 -5.432 24.685 1.00 78.21 O
ANISOU 639 O VAL A 86 10042 10091 9586 314 -150 -249 O
ATOM 640 CB VAL A 86 -28.049 -2.962 25.639 1.00 79.94 C
ANISOU 640 CB VAL A 86 10197 10379 9798 340 -202 -295 C
ATOM 641 CG1 VAL A 86 -28.667 -4.252 26.148 1.00 77.77 C
ANISOU 641 CG1 VAL A 86 9936 10133 9480 317 -194 -291 C
ATOM 642 CG2 VAL A 86 -28.168 -1.857 26.681 1.00 81.89 C
ANISOU 642 CG2 VAL A 86 10409 10644 10061 363 -227 -321 C
ATOM 643 N LEU A 87 -26.752 -4.132 23.020 1.00 80.60 N
ANISOU 643 N LEU A 87 10342 10389 9892 314 -152 -249 N
ATOM 644 CA LEU A 87 -26.654 -5.192 22.018 1.00 81.21 C
ANISOU 644 CA LEU A 87 10453 10450 9952 292 -126 -232 C
ATOM 645 C LEU A 87 -25.215 -5.613 21.746 1.00 81.39 C
ANISOU 645 C LEU A 87 10488 10433 10004 297 -105 -222 C
ATOM 646 O LEU A 87 -24.950 -6.791 21.510 1.00 81.42 O
ANISOU 646 O LEU A 87 10515 10424 9995 283 -85 -214 O
ATOM 647 CB LEU A 87 -27.340 -4.771 20.722 1.00 80.54 C
ANISOU 647 CB LEU A 87 10379 10366 9856 278 -123 -225 C
ATOM 648 CG LEU A 87 -28.840 -4.515 20.839 1.00 81.18 C
ANISOU 648 CG LEU A 87 10451 10485 9909 270 -141 -233 C
ATOM 649 CD1 LEU A 87 -29.364 -3.885 19.561 1.00 83.72 C
ANISOU 649 CD1 LEU A 87 10780 10802 10229 259 -144 -224 C
ATOM 650 CD2 LEU A 87 -29.584 -5.802 21.165 1.00 80.99 C
ANISOU 650 CD2 LEU A 87 10444 10485 9844 248 -134 -231 C
ATOM 651 N ALA A 88 -24.289 -4.656 21.785 1.00 79.78 N
ANISOU 651 N ALA A 88 10266 10207 9839 318 -111 -223 N
ATOM 652 CA ALA A 88 -22.874 -4.980 21.605 1.00 78.50 C
ANISOU 652 CA ALA A 88 10110 10007 9709 325 -92 -213 C
ATOM 653 C ALA A 88 -22.364 -5.837 22.764 1.00 78.98 C
ANISOU 653 C ALA A 88 10169 10065 9774 329 -94 -215 C
ATOM 654 O ALA A 88 -21.634 -6.806 22.544 1.00 80.08 O
ANISOU 654 O ALA A 88 10325 10180 9922 323 -74 -207 O
ATOM 655 CB ALA A 88 -22.046 -3.716 21.451 1.00 77.18 C
ANISOU 655 CB ALA A 88 9922 9819 9583 345 -101 -212 C
ATOM 656 N GLN A 89 -22.762 -5.495 23.988 1.00 81.09 N
ANISOU 656 N GLN A 89 10416 10358 10037 338 -120 -226 N
ATOM 657 CA GLN A 89 -22.352 -6.274 25.152 1.00 82.69 C
ANISOU 657 CA GLN A 89 10617 10562 10241 339 -126 -226 C
ATOM 658 C GLN A 89 -23.008 -7.652 25.166 1.00 82.35 C
ANISOU 658 C GLN A 89 10596 10533 10161 314 -117 -219 C
ATOM 659 O GLN A 89 -22.423 -8.609 25.676 1.00 83.81 O
ANISOU 659 O GLN A 89 10789 10704 10352 309 -114 -211 O
ATOM 660 CB GLN A 89 -22.659 -5.521 26.443 1.00 80.30 C
ANISOU 660 CB GLN A 89 10286 10287 9936 352 -156 -241 C
ATOM 661 CG GLN A 89 -21.759 -5.910 27.604 1.00 79.34 C
ANISOU 661 CG GLN A 89 10157 10155 9833 358 -166 -237 C
ATOM 662 CD GLN A 89 -20.314 -5.511 27.377 1.00 78.69 C
ANISOU 662 CD GLN A 89 10069 10029 9802 376 -161 -229 C
ATOM 663 OE1 GLN A 89 -20.022 -4.373 27.014 1.00 79.38 O
ANISOU 663 OE1 GLN A 89 10142 10105 9915 392 -167 -234 O
ATOM 664 NE2 GLN A 89 -19.405 -6.451 27.581 1.00 77.29 N
ANISOU 664 NE2 GLN A 89 9901 9824 9643 372 -153 -215 N
ATOM 665 N SER A 90 -24.216 -7.756 24.615 1.00 83.62 N
ANISOU 665 N SER A 90 10767 10720 10285 298 -115 -222 N
ATOM 666 CA SER A 90 -24.864 -9.060 24.484 1.00 85.61 C
ANISOU 666 CA SER A 90 11042 10983 10502 273 -106 -214 C
ATOM 667 C SER A 90 -24.076 -9.976 23.548 1.00 84.45 C
ANISOU 667 C SER A 90 10921 10796 10368 265 -79 -203 C
ATOM 668 O SER A 90 -23.934 -11.171 23.820 1.00 81.86 O
ANISOU 668 O SER A 90 10609 10460 10034 252 -74 -196 O
ATOM 669 CB SER A 90 -26.304 -8.900 24.006 1.00 88.68 C
ANISOU 669 CB SER A 90 11435 11406 10852 258 -109 -219 C
ATOM 670 OG SER A 90 -26.921 -10.161 23.830 1.00 92.17 O
ANISOU 670 OG SER A 90 11902 11858 11262 232 -102 -210 O
ATOM 671 N SER A 91 -23.557 -9.412 22.460 1.00 84.53 N
ANISOU 671 N SER A 91 10937 10782 10399 272 -62 -202 N
ATOM 672 CA SER A 91 -22.794 -10.200 21.496 1.00 82.86 C
ANISOU 672 CA SER A 91 10749 10535 10200 265 -32 -196 C
ATOM 673 C SER A 91 -21.445 -10.648 22.056 1.00 83.18 C
ANISOU 673 C SER A 91 10782 10541 10281 279 -27 -192 C
ATOM 674 O SER A 91 -20.976 -11.738 21.733 1.00 82.32 O
ANISOU 674 O SER A 91 10692 10408 10180 270 -9 -189 O
ATOM 675 CB SER A 91 -22.606 -9.421 20.199 1.00 80.42 C
ANISOU 675 CB SER A 91 10444 10213 9898 266 -15 -196 C
ATOM 676 OG SER A 91 -23.854 -9.147 19.583 1.00 75.71 O
ANISOU 676 OG SER A 91 9857 9644 9264 250 -20 -196 O
ATOM 677 N ILE A 92 -20.833 -9.821 22.898 1.00 82.60 N
ANISOU 677 N ILE A 92 10682 10465 10236 299 -45 -194 N
ATOM 678 CA ILE A 92 -19.548 -10.180 23.494 1.00 82.62 C
ANISOU 678 CA ILE A 92 10676 10435 10281 312 -44 -189 C
ATOM 679 C ILE A 92 -19.719 -11.359 24.452 1.00 84.70 C
ANISOU 679 C ILE A 92 10945 10703 10533 300 -57 -183 C
ATOM 680 O ILE A 92 -18.909 -12.288 24.457 1.00 85.48 O
ANISOU 680 O ILE A 92 11052 10769 10656 299 -47 -177 O
ATOM 681 CB ILE A 92 -18.906 -8.973 24.194 1.00 81.75 C
ANISOU 681 CB ILE A 92 10536 10322 10203 336 -63 -191 C
ATOM 682 CG1 ILE A 92 -18.416 -7.961 23.153 1.00 81.94 C
ANISOU 682 CG1 ILE A 92 10555 10330 10250 347 -48 -191 C
ATOM 683 CG2 ILE A 92 -17.759 -9.418 25.084 1.00 79.40 C
ANISOU 683 CG2 ILE A 92 10228 9997 9944 346 -71 -184 C
ATOM 684 CD1 ILE A 92 -18.207 -6.564 23.700 1.00 80.72 C
ANISOU 684 CD1 ILE A 92 10373 10182 10116 367 -72 -195 C
ATOM 685 N PHE A 93 -20.783 -11.333 25.249 1.00 86.44 N
ANISOU 685 N PHE A 93 11161 10964 10717 290 -79 -186 N
ATOM 686 CA PHE A 93 -21.048 -12.443 26.159 1.00 87.09 C
ANISOU 686 CA PHE A 93 11251 11056 10783 274 -94 -178 C
ATOM 687 C PHE A 93 -21.379 -13.726 25.398 1.00 86.20 C
ANISOU 687 C PHE A 93 11167 10932 10654 253 -77 -172 C
ATOM 688 O PHE A 93 -20.969 -14.813 25.813 1.00 85.92 O
ANISOU 688 O PHE A 93 11139 10876 10630 244 -81 -162 O
ATOM 689 CB PHE A 93 -22.162 -12.081 27.140 1.00 86.94 C
ANISOU 689 CB PHE A 93 11219 11089 10725 265 -119 -183 C
ATOM 690 CG PHE A 93 -21.766 -11.059 28.168 1.00 85.91 C
ANISOU 690 CG PHE A 93 11061 10970 10612 284 -141 -190 C
ATOM 691 CD1 PHE A 93 -20.498 -11.084 28.754 1.00 85.33 C
ANISOU 691 CD1 PHE A 93 10977 10864 10579 297 -148 -183 C
ATOM 692 CD2 PHE A 93 -22.673 -10.081 28.575 1.00 84.29 C
ANISOU 692 CD2 PHE A 93 10838 10807 10381 288 -155 -205 C
ATOM 693 CE1 PHE A 93 -20.140 -10.140 29.706 1.00 83.11 C
ANISOU 693 CE1 PHE A 93 10672 10593 10312 313 -170 -190 C
ATOM 694 CE2 PHE A 93 -22.320 -9.136 29.530 1.00 81.41 C
ANISOU 694 CE2 PHE A 93 10449 10453 10031 306 -176 -215 C
ATOM 695 CZ PHE A 93 -21.052 -9.165 30.095 1.00 80.61 C
ANISOU 695 CZ PHE A 93 10340 10319 9969 317 -183 -207 C
ATOM 696 N SER A 94 -22.097 -13.599 24.284 1.00 84.88 N
ANISOU 696 N SER A 94 11015 10773 10461 244 -59 -177 N
ATOM 697 CA SER A 94 -22.438 -14.772 23.475 1.00 84.69 C
ANISOU 697 CA SER A 94 11021 10737 10421 223 -42 -174 C
ATOM 698 C SER A 94 -21.195 -15.380 22.826 1.00 84.37 C
ANISOU 698 C SER A 94 10990 10645 10421 231 -18 -174 C
ATOM 699 O SER A 94 -21.008 -16.597 22.852 1.00 85.53 O
ANISOU 699 O SER A 94 11153 10771 10574 220 -15 -170 O
ATOM 700 CB SER A 94 -23.480 -14.420 22.417 1.00 84.71 C
ANISOU 700 CB SER A 94 11038 10761 10386 211 -31 -179 C
ATOM 701 OG SER A 94 -24.793 -14.526 22.936 1.00 84.28 O
ANISOU 701 OG SER A 94 10982 10750 10289 195 -51 -177 O
ATOM 702 N LEU A 95 -20.346 -14.534 22.251 1.00 84.14 N
ANISOU 702 N LEU A 95 10951 10596 10422 250 -1 -180 N
ATOM 703 CA LEU A 95 -19.125 -15.021 21.615 1.00 83.29 C
ANISOU 703 CA LEU A 95 10849 10442 10356 259 26 -182 C
ATOM 704 C LEU A 95 -18.180 -15.648 22.635 1.00 84.85 C
ANISOU 704 C LEU A 95 11033 10612 10594 268 12 -175 C
ATOM 705 O LEU A 95 -17.517 -16.641 22.339 1.00 88.01 O
ANISOU 705 O LEU A 95 11444 10976 11021 267 26 -176 O
ATOM 706 CB LEU A 95 -18.430 -13.892 20.861 1.00 81.25 C
ANISOU 706 CB LEU A 95 10578 10172 10120 276 45 -188 C
ATOM 707 CG LEU A 95 -19.059 -13.483 19.532 1.00 80.73 C
ANISOU 707 CG LEU A 95 10530 10120 10023 264 66 -193 C
ATOM 708 CD1 LEU A 95 -18.624 -12.079 19.157 1.00 79.16 C
ANISOU 708 CD1 LEU A 95 10314 9924 9842 279 70 -193 C
ATOM 709 CD2 LEU A 95 -18.679 -14.475 18.449 1.00 81.68 C
ANISOU 709 CD2 LEU A 95 10677 10214 10146 253 101 -201 C
ATOM 710 N LEU A 96 -18.138 -15.080 23.839 1.00 83.72 N
ANISOU 710 N LEU A 96 10868 10485 10456 277 -18 -168 N
ATOM 711 CA LEU A 96 -17.319 -15.642 24.907 1.00 85.46 C
ANISOU 711 CA LEU A 96 11076 10683 10712 282 -37 -157 C
ATOM 712 C LEU A 96 -17.843 -17.000 25.368 1.00 85.87 C
ANISOU 712 C LEU A 96 11145 10736 10746 259 -52 -148 C
ATOM 713 O LEU A 96 -17.058 -17.873 25.738 1.00 86.90 O
ANISOU 713 O LEU A 96 11275 10832 10913 259 -58 -140 O
ATOM 714 CB LEU A 96 -17.235 -14.666 26.081 1.00 84.84 C
ANISOU 714 CB LEU A 96 10972 10627 10637 293 -67 -153 C
ATOM 715 CG LEU A 96 -16.266 -14.977 27.221 1.00 84.27 C
ANISOU 715 CG LEU A 96 10884 10532 10605 300 -90 -141 C
ATOM 716 CD1 LEU A 96 -14.820 -14.964 26.747 1.00 85.18 C
ANISOU 716 CD1 LEU A 96 10989 10595 10781 320 -71 -140 C
ATOM 717 CD2 LEU A 96 -16.455 -13.975 28.351 1.00 82.71 C
ANISOU 717 CD2 LEU A 96 10665 10366 10397 307 -120 -140 C
ATOM 718 N ALA A 97 -19.160 -17.181 25.335 1.00 84.02 N
ANISOU 718 N ALA A 97 10925 10541 10459 239 -59 -149 N
ATOM 719 CA ALA A 97 -19.752 -18.456 25.743 1.00 82.47 C
ANISOU 719 CA ALA A 97 10744 10349 10242 214 -75 -138 C
ATOM 720 C ALA A 97 -19.463 -19.560 24.726 1.00 82.51 C
ANISOU 720 C ALA A 97 10773 10314 10262 207 -51 -142 C
ATOM 721 O ALA A 97 -19.233 -20.708 25.107 1.00 81.91 O
ANISOU 721 O ALA A 97 10705 10215 10202 196 -64 -132 O
ATOM 722 CB ALA A 97 -21.248 -18.307 25.970 1.00 81.05 C
ANISOU 722 CB ALA A 97 10570 10223 10002 194 -89 -136 C
ATOM 723 N ILE A 98 -19.453 -19.210 23.444 1.00 84.11 N
ANISOU 723 N ILE A 98 10988 10510 10461 213 -18 -157 N
ATOM 724 CA ILE A 98 -19.190 -20.202 22.406 1.00 86.67 C
ANISOU 724 CA ILE A 98 11335 10798 10797 207 7 -166 C
ATOM 725 C ILE A 98 -17.750 -20.711 22.509 1.00 89.93 C
ANISOU 725 C ILE A 98 11738 11159 11274 224 16 -168 C
ATOM 726 O ILE A 98 -17.497 -21.910 22.362 1.00 94.36 O
ANISOU 726 O ILE A 98 12312 11686 11853 216 17 -169 O
ATOM 727 CB ILE A 98 -19.498 -19.641 21.009 1.00 84.37 C
ANISOU 727 CB ILE A 98 11059 10516 10484 207 41 -182 C
ATOM 728 CG1 ILE A 98 -20.971 -19.247 20.924 1.00 82.04 C
ANISOU 728 CG1 ILE A 98 10773 10269 10128 188 29 -179 C
ATOM 729 CG2 ILE A 98 -19.181 -20.669 19.934 1.00 83.75 C
ANISOU 729 CG2 ILE A 98 11006 10402 10416 200 70 -195 C
ATOM 730 CD1 ILE A 98 -21.317 -18.357 19.749 1.00 83.22 C
ANISOU 730 CD1 ILE A 98 10930 10433 10255 188 53 -189 C
ATOM 731 N ALA A 99 -16.813 -19.807 22.786 1.00 88.94 N
ANISOU 731 N ALA A 99 11588 11023 11184 247 19 -168 N
ATOM 732 CA ALA A 99 -15.410 -20.205 22.923 1.00 88.33 C
ANISOU 732 CA ALA A 99 11495 10895 11170 264 26 -168 C
ATOM 733 C ALA A 99 -15.219 -21.159 24.104 1.00 90.36 C
ANISOU 733 C ALA A 99 11748 11136 11450 256 -10 -151 C
ATOM 734 O ALA A 99 -14.488 -22.143 23.998 1.00 90.35 O
ANISOU 734 O ALA A 99 11747 11089 11491 259 -6 -152 O
ATOM 735 CB ALA A 99 -14.514 -18.985 23.056 1.00 85.22 C
ANISOU 735 CB ALA A 99 11075 10498 10808 289 32 -169 C
ATOM 736 N ILE A 100 -15.884 -20.876 25.220 1.00 89.82 N
ANISOU 736 N ILE A 100 11671 11104 11351 245 -46 -135 N
ATOM 737 CA ILE A 100 -15.810 -21.760 26.380 1.00 88.99 C
ANISOU 737 CA ILE A 100 11563 10990 11260 232 -84 -114 C
ATOM 738 C ILE A 100 -16.472 -23.107 26.068 1.00 92.56 C
ANISOU 738 C ILE A 100 12042 11434 11695 208 -88 -112 C
ATOM 739 O ILE A 100 -15.973 -24.161 26.470 1.00 91.10 O
ANISOU 739 O ILE A 100 11856 11211 11545 202 -106 -101 O
ATOM 740 CB ILE A 100 -16.430 -21.090 27.618 1.00 84.47 C
ANISOU 740 CB ILE A 100 10978 10466 10653 223 -118 -100 C
ATOM 741 CG1 ILE A 100 -15.644 -19.823 27.956 1.00 84.30 C
ANISOU 741 CG1 ILE A 100 10930 10445 10656 248 -117 -103 C
ATOM 742 CG2 ILE A 100 -16.434 -22.033 28.809 1.00 81.22 C
ANISOU 742 CG2 ILE A 100 10564 10050 10247 203 -159 -76 C
ATOM 743 CD1 ILE A 100 -16.314 -18.914 28.960 1.00 82.81 C
ANISOU 743 CD1 ILE A 100 10728 10307 10428 243 -143 -98 C
ATOM 744 N ASP A 101 -17.581 -23.071 25.335 1.00 95.69 N
ANISOU 744 N ASP A 101 12459 11861 12039 194 -73 -121 N
ATOM 745 CA ASP A 101 -18.287 -24.299 24.986 1.00 99.23 C
ANISOU 745 CA ASP A 101 12934 12303 12468 170 -78 -119 C
ATOM 746 C ASP A 101 -17.412 -25.216 24.126 1.00102.66 C
ANISOU 746 C ASP A 101 13378 12678 12951 179 -55 -134 C
ATOM 747 O ASP A 101 -17.286 -26.407 24.408 1.00106.83 O
ANISOU 747 O ASP A 101 13914 13176 13502 167 -74 -125 O
ATOM 748 CB ASP A 101 -19.596 -23.972 24.272 1.00100.40 C
ANISOU 748 CB ASP A 101 13100 12494 12552 155 -65 -127 C
ATOM 749 CG ASP A 101 -20.373 -25.209 23.896 1.00102.06 C
ANISOU 749 CG ASP A 101 13339 12700 12741 129 -71 -124 C
ATOM 750 OD1 ASP A 101 -20.980 -25.826 24.796 1.00102.86 O
ANISOU 750 OD1 ASP A 101 13441 12818 12822 107 -106 -103 O
ATOM 751 OD2 ASP A 101 -20.370 -25.568 22.701 1.00101.96 O
ANISOU 751 OD2 ASP A 101 13346 12666 12727 129 -42 -143 O
ATOM 752 N ARG A 102 -16.798 -24.656 23.086 1.00102.57 N
ANISOU 752 N ARG A 102 13365 12650 12957 199 -14 -156 N
ATOM 753 CA ARG A 102 -15.903 -25.434 22.236 1.00100.25 C
ANISOU 753 CA ARG A 102 13078 12302 12711 210 14 -175 C
ATOM 754 C ARG A 102 -14.621 -25.834 22.954 1.00 99.64 C
ANISOU 754 C ARG A 102 12976 12178 12705 227 -1 -168 C
ATOM 755 O ARG A 102 -13.990 -26.817 22.573 1.00 96.26 O
ANISOU 755 O ARG A 102 12552 11701 12321 231 8 -179 O
ATOM 756 CB ARG A 102 -15.585 -24.677 20.949 1.00 98.36 C
ANISOU 756 CB ARG A 102 12842 12064 12468 225 62 -201 C
ATOM 757 CG ARG A 102 -16.768 -24.512 20.006 1.00 99.84 C
ANISOU 757 CG ARG A 102 13057 12286 12590 206 79 -211 C
ATOM 758 CD ARG A 102 -17.326 -25.843 19.527 1.00102.77 C
ANISOU 758 CD ARG A 102 13458 12640 12948 186 78 -218 C
ATOM 759 NE ARG A 102 -18.298 -26.422 20.457 1.00105.19 N
ANISOU 759 NE ARG A 102 13772 12969 13226 163 35 -195 N
ATOM 760 CZ ARG A 102 -18.611 -27.714 20.518 1.00110.77 C
ANISOU 760 CZ ARG A 102 14497 13653 13937 145 18 -192 C
ATOM 761 NH1 ARG A 102 -18.033 -28.598 19.712 1.00114.52 N
ANISOU 761 NH1 ARG A 102 14985 14081 14446 150 40 -214 N
ATOM 762 NH2 ARG A 102 -19.512 -28.134 21.390 1.00111.76 N
ANISOU 762 NH2 ARG A 102 14627 13804 14033 122 -21 -167 N
ATOM 763 N TYR A 103 -14.236 -25.084 23.984 1.00100.42 N
ANISOU 763 N TYR A 103 13050 12289 12816 236 -24 -150 N
ATOM 764 CA TYR A 103 -13.078 -25.469 24.784 1.00103.91 C
ANISOU 764 CA TYR A 103 13469 12688 13325 248 -45 -137 C
ATOM 765 C TYR A 103 -13.400 -26.662 25.686 1.00103.96 C
ANISOU 765 C TYR A 103 13482 12681 13338 225 -90 -115 C
ATOM 766 O TYR A 103 -12.553 -27.542 25.875 1.00101.87 O
ANISOU 766 O TYR A 103 13210 12364 13133 231 -101 -111 O
ATOM 767 CB TYR A 103 -12.573 -24.288 25.606 1.00108.45 C
ANISOU 767 CB TYR A 103 14017 13280 13911 263 -59 -124 C
ATOM 768 CG TYR A 103 -11.415 -24.624 26.508 1.00113.98 C
ANISOU 768 CG TYR A 103 14692 13938 14677 273 -85 -108 C
ATOM 769 CD1 TYR A 103 -10.124 -24.772 25.993 1.00117.64 C
ANISOU 769 CD1 TYR A 103 15139 14348 15209 297 -61 -121 C
ATOM 770 CD2 TYR A 103 -11.608 -24.803 27.881 1.00115.76 C
ANISOU 770 CD2 TYR A 103 14909 14176 14897 257 -135 -79 C
ATOM 771 CE1 TYR A 103 -9.058 -25.086 26.820 1.00123.02 C
ANISOU 771 CE1 TYR A 103 15797 14990 15956 307 -87 -105 C
ATOM 772 CE2 TYR A 103 -10.549 -25.116 28.717 1.00120.51 C
ANISOU 772 CE2 TYR A 103 15489 14738 15560 264 -163 -61 C
ATOM 773 CZ TYR A 103 -9.277 -25.255 28.183 1.00124.45 C
ANISOU 773 CZ TYR A 103 15972 15183 16130 290 -140 -74 C
ATOM 774 OH TYR A 103 -8.223 -25.564 29.005 1.00126.72 O
ANISOU 774 OH TYR A 103 16237 15429 16483 297 -169 -55 O
ATOM 775 N ILE A 104 -14.609 -26.696 26.236 1.00104.26 N
ANISOU 775 N ILE A 104 13533 12766 13316 199 -116 -98 N
ATOM 776 CA ILE A 104 -15.011 -27.808 27.090 1.00104.75 C
ANISOU 776 CA ILE A 104 13603 12822 13377 173 -160 -73 C
ATOM 777 C ILE A 104 -15.143 -29.093 26.269 1.00108.30 C
ANISOU 777 C ILE A 104 14075 13233 13842 164 -151 -86 C
ATOM 778 O ILE A 104 -14.749 -30.168 26.726 1.00112.11 O
ANISOU 778 O ILE A 104 14556 13674 14366 155 -180 -72 O
ATOM 779 CB ILE A 104 -16.311 -27.489 27.846 1.00100.94 C
ANISOU 779 CB ILE A 104 13126 12404 12822 146 -187 -54 C
ATOM 780 CG1 ILE A 104 -16.089 -26.333 28.820 1.00 97.24 C
ANISOU 780 CG1 ILE A 104 12634 11969 12345 154 -202 -43 C
ATOM 781 CG2 ILE A 104 -16.793 -28.708 28.618 1.00 99.83 C
ANISOU 781 CG2 ILE A 104 12997 12259 12677 114 -231 -27 C
ATOM 782 CD1 ILE A 104 -17.365 -25.806 29.440 1.00 94.09 C
ANISOU 782 CD1 ILE A 104 12237 11638 11873 133 -219 -33 C
ATOM 783 N ALA A 105 -15.674 -28.977 25.054 1.00109.81 N
ANISOU 783 N ALA A 105 14287 13435 14001 165 -112 -111 N
ATOM 784 CA ALA A 105 -15.909 -30.155 24.223 1.00114.52 C
ANISOU 784 CA ALA A 105 14908 13999 14605 155 -103 -126 C
ATOM 785 C ALA A 105 -14.605 -30.833 23.798 1.00116.25 C
ANISOU 785 C ALA A 105 15118 14148 14903 177 -87 -145 C
ATOM 786 O ALA A 105 -14.577 -32.042 23.583 1.00121.53 O
ANISOU 786 O ALA A 105 15800 14778 15600 168 -98 -149 O
ATOM 787 CB ALA A 105 -16.752 -29.802 23.009 1.00114.38 C
ANISOU 787 CB ALA A 105 14915 14010 14532 151 -65 -150 C
ATOM 788 N ILE A 106 -13.531 -30.058 23.689 1.00115.84 N
ANISOU 788 N ILE A 106 15041 14080 14891 206 -64 -155 N
ATOM 789 CA ILE A 106 -12.253 -30.602 23.240 1.00116.31 C
ANISOU 789 CA ILE A 106 15088 14077 15029 229 -44 -176 C
ATOM 790 C ILE A 106 -11.301 -30.933 24.393 1.00115.85 C
ANISOU 790 C ILE A 106 15000 13980 15037 236 -84 -151 C
ATOM 791 O ILE A 106 -10.369 -31.715 24.206 1.00116.08 O
ANISOU 791 O ILE A 106 15019 13950 15136 250 -81 -162 O
ATOM 792 CB ILE A 106 -11.575 -29.675 22.215 1.00117.37 C
ANISOU 792 CB ILE A 106 15212 14211 15172 256 12 -206 C
ATOM 793 CG1 ILE A 106 -10.734 -30.496 21.236 1.00116.62 C
ANISOU 793 CG1 ILE A 106 15118 14060 15133 272 47 -240 C
ATOM 794 CG2 ILE A 106 -10.727 -28.609 22.909 1.00119.21 C
ANISOU 794 CG2 ILE A 106 15412 14450 15433 276 7 -191 C
ATOM 795 CD1 ILE A 106 -10.620 -29.881 19.865 1.00115.80 C
ANISOU 795 CD1 ILE A 106 15023 13969 15007 283 107 -275 C
ATOM 796 N ALA A 107 -11.515 -30.338 25.567 1.00114.34 N
ANISOU 796 N ALA A 107 14797 13822 14825 227 -120 -118 N
ATOM 797 CA ALA A 107 -10.656 -30.615 26.721 1.00118.45 C
ANISOU 797 CA ALA A 107 15292 14310 15403 230 -162 -91 C
ATOM 798 C ALA A 107 -11.116 -31.864 27.476 1.00123.77 C
ANISOU 798 C ALA A 107 15977 14967 16083 200 -214 -64 C
ATOM 799 O ALA A 107 -10.327 -32.781 27.702 1.00131.57 O
ANISOU 799 O ALA A 107 16953 15896 17140 204 -235 -59 O
ATOM 800 CB ALA A 107 -10.582 -29.412 27.650 1.00118.98 C
ANISOU 800 CB ALA A 107 15339 14417 15449 232 -179 -70 C
ATOM 801 N ILE A 108 -12.386 -31.895 27.861 1.00122.61 N
ANISOU 801 N ILE A 108 15850 14872 15865 170 -236 -47 N
ATOM 802 CA ILE A 108 -12.958 -33.043 28.553 1.00123.04 C
ANISOU 802 CA ILE A 108 15917 14919 15915 137 -286 -18 C
ATOM 803 C ILE A 108 -14.151 -33.561 27.747 1.00124.80 C
ANISOU 803 C ILE A 108 16173 15164 16083 118 -272 -31 C
ATOM 804 O ILE A 108 -15.299 -33.240 28.055 1.00123.64 O
ANISOU 804 O ILE A 108 16039 15076 15865 94 -283 -17 O
ATOM 805 CB ILE A 108 -13.352 -32.697 30.000 1.00123.09 C
ANISOU 805 CB ILE A 108 15913 14969 15888 112 -334 23 C
ATOM 806 CG1 ILE A 108 -13.929 -31.270 30.086 1.00121.75 C
ANISOU 806 CG1 ILE A 108 15740 14867 15651 117 -312 17 C
ATOM 807 CG2 ILE A 108 -12.157 -32.889 30.928 1.00123.98 C
ANISOU 807 CG2 ILE A 108 15999 15037 16071 119 -369 46 C
ATOM 808 CD1 ILE A 108 -14.629 -30.969 31.393 1.00122.37 C
ANISOU 808 CD1 ILE A 108 15815 15002 15680 88 -354 51 C
ATOM 809 N PRO A 109 -13.901 -34.363 26.698 1.00127.86 N
ANISOU 809 N PRO A 109 16574 15505 16505 128 -247 -60 N
ATOM 810 CA PRO A 109 -15.026 -34.838 25.883 1.00131.32 C
ANISOU 810 CA PRO A 109 17044 15961 16889 109 -234 -74 C
ATOM 811 C PRO A 109 -15.967 -35.788 26.631 1.00138.88 C
ANISOU 811 C PRO A 109 18017 16931 17820 69 -287 -39 C
ATOM 812 O PRO A 109 -17.179 -35.735 26.425 1.00142.58 O
ANISOU 812 O PRO A 109 18507 17447 18221 46 -287 -35 O
ATOM 813 CB PRO A 109 -14.342 -35.535 24.707 1.00130.80 C
ANISOU 813 CB PRO A 109 16986 15836 16877 130 -200 -113 C
ATOM 814 CG PRO A 109 -12.996 -35.915 25.220 1.00128.70 C
ANISOU 814 CG PRO A 109 16692 15509 16701 149 -217 -108 C
ATOM 815 CD PRO A 109 -12.607 -34.837 26.178 1.00127.96 C
ANISOU 815 CD PRO A 109 16571 15446 16602 156 -229 -84 C
ATOM 816 N LEU A 110 -15.417 -36.621 27.514 1.00144.70 N
ANISOU 816 N LEU A 110 18741 17627 18611 59 -335 -12 N
ATOM 817 CA LEU A 110 -16.211 -37.575 28.278 1.00144.74 C
ANISOU 817 CA LEU A 110 18758 17639 18596 19 -390 25 C
ATOM 818 C LEU A 110 -16.879 -36.972 29.511 1.00145.81 C
ANISOU 818 C LEU A 110 18885 17840 18674 -8 -423 65 C
ATOM 819 O LEU A 110 -17.379 -37.708 30.360 1.00148.99 O
ANISOU 819 O LEU A 110 19293 18251 19065 -43 -474 102 O
ATOM 820 CB LEU A 110 -15.362 -38.789 28.662 1.00144.26 C
ANISOU 820 CB LEU A 110 18689 17503 18620 17 -430 39 C
ATOM 821 CG LEU A 110 -15.092 -39.777 27.530 1.00144.72 C
ANISOU 821 CG LEU A 110 18762 17499 18725 30 -411 3 C
ATOM 822 CD1 LEU A 110 -13.874 -40.630 27.847 1.00146.53 C
ANISOU 822 CD1 LEU A 110 18971 17647 19056 43 -439 7 C
ATOM 823 CD2 LEU A 110 -16.303 -40.650 27.229 1.00141.49 C
ANISOU 823 CD2 LEU A 110 18385 17102 18271 -3 -430 10 C
ATOM 824 N ARG A 111 -16.875 -35.644 29.614 1.00146.07 N
ANISOU 824 N ARG A 111 18906 17920 18672 8 -396 56 N
ATOM 825 CA ARG A 111 -17.561 -34.940 30.694 1.00145.70 C
ANISOU 825 CA ARG A 111 18851 17942 18566 -14 -420 85 C
ATOM 826 C ARG A 111 -18.452 -33.814 30.182 1.00144.83 C
ANISOU 826 C ARG A 111 18748 17897 18384 -8 -380 65 C
ATOM 827 O ARG A 111 -19.137 -33.176 30.980 1.00143.23 O
ANISOU 827 O ARG A 111 18539 17756 18127 -25 -395 83 O
ATOM 828 CB ARG A 111 -16.549 -34.386 31.703 1.00145.88 C
ANISOU 828 CB ARG A 111 18845 17956 18626 -2 -440 102 C
ATOM 829 CG ARG A 111 -15.962 -35.413 32.652 1.00146.68 C
ANISOU 829 CG ARG A 111 18937 18014 18781 -22 -496 139 C
ATOM 830 CD ARG A 111 -16.454 -35.187 34.070 1.00148.67 C
ANISOU 830 CD ARG A 111 19180 18319 18987 -57 -542 180 C
ATOM 831 NE ARG A 111 -16.085 -33.859 34.561 1.00151.26 N
ANISOU 831 NE ARG A 111 19489 18683 19299 -39 -527 175 N
ATOM 832 CZ ARG A 111 -16.705 -33.214 35.544 1.00153.84 C
ANISOU 832 CZ ARG A 111 19810 19077 19566 -61 -546 194 C
ATOM 833 NH1 ARG A 111 -16.285 -32.010 35.903 1.00151.77 N
ANISOU 833 NH1 ARG A 111 19530 18840 19296 -40 -531 185 N
ATOM 834 NH2 ARG A 111 -17.742 -33.760 36.172 1.00158.55 N
ANISOU 834 NH2 ARG A 111 20417 19716 20109 -104 -579 223 N
ATOM 835 N TYR A 112 -18.448 -33.569 28.870 1.00144.65 N
ANISOU 835 N TYR A 112 18738 17862 18361 14 -332 27 N
ATOM 836 CA TYR A 112 -19.200 -32.455 28.291 1.00141.16 C
ANISOU 836 CA TYR A 112 18302 17476 17858 22 -294 8 C
ATOM 837 C TYR A 112 -20.706 -32.605 28.501 1.00145.30 C
ANISOU 837 C TYR A 112 18842 18058 18307 -13 -311 24 C
ATOM 838 O TYR A 112 -21.374 -31.664 28.938 1.00146.42 O
ANISOU 838 O TYR A 112 18975 18261 18397 -18 -309 29 O
ATOM 839 CB TYR A 112 -18.862 -32.307 26.808 1.00134.53 C
ANISOU 839 CB TYR A 112 17475 16607 17035 49 -243 -33 C
ATOM 840 CG TYR A 112 -19.578 -31.186 26.094 1.00126.93 C
ANISOU 840 CG TYR A 112 16518 15695 16015 56 -205 -53 C
ATOM 841 CD1 TYR A 112 -19.041 -29.900 26.063 1.00122.06 C
ANISOU 841 CD1 TYR A 112 15881 15094 15402 83 -181 -65 C
ATOM 842 CD2 TYR A 112 -20.784 -31.415 25.428 1.00125.23 C
ANISOU 842 CD2 TYR A 112 16329 15509 15745 36 -197 -58 C
ATOM 843 CE1 TYR A 112 -19.688 -28.870 25.400 1.00120.92 C
ANISOU 843 CE1 TYR A 112 15742 14993 15210 89 -150 -81 C
ATOM 844 CE2 TYR A 112 -21.436 -30.397 24.754 1.00123.54 C
ANISOU 844 CE2 TYR A 112 16120 15339 15482 41 -166 -75 C
ATOM 845 CZ TYR A 112 -20.885 -29.125 24.744 1.00121.20 C
ANISOU 845 CZ TYR A 112 15803 15056 15192 68 -143 -86 C
ATOM 846 OH TYR A 112 -21.535 -28.114 24.086 1.00121.22 O
ANISOU 846 OH TYR A 112 15810 15099 15150 72 -116 -100 O
ATOM 847 N ASN A 113 -21.231 -33.793 28.213 1.00147.96 N
ANISOU 847 N ASN A 113 19201 18375 18642 -37 -328 31 N
ATOM 848 CA ASN A 113 -22.658 -34.049 28.365 1.00150.81 C
ANISOU 848 CA ASN A 113 19577 18787 18935 -72 -345 48 C
ATOM 849 C ASN A 113 -23.118 -34.022 29.818 1.00152.05 C
ANISOU 849 C ASN A 113 19719 18991 19062 -102 -389 87 C
ATOM 850 O ASN A 113 -24.290 -33.773 30.089 1.00149.02 O
ANISOU 850 O ASN A 113 19339 18667 18614 -126 -396 99 O
ATOM 851 CB ASN A 113 -23.037 -35.368 27.694 1.00152.54 C
ANISOU 851 CB ASN A 113 19824 18970 19165 -91 -355 48 C
ATOM 852 CG ASN A 113 -22.772 -35.356 26.203 1.00155.96 C
ANISOU 852 CG ASN A 113 20275 19368 19613 -66 -308 6 C
ATOM 853 OD1 ASN A 113 -23.061 -34.376 25.511 1.00154.81 O
ANISOU 853 OD1 ASN A 113 20131 19253 19434 -51 -269 -16 O
ATOM 854 ND2 ASN A 113 -22.211 -36.446 25.696 1.00162.23 N
ANISOU 854 ND2 ASN A 113 21082 20098 20460 -63 -312 -4 N
ATOM 855 N GLY A 114 -22.193 -34.269 30.743 1.00153.68 N
ANISOU 855 N GLY A 114 19909 19169 19315 -101 -419 108 N
ATOM 856 CA GLY A 114 -22.495 -34.191 32.169 1.00156.85 C
ANISOU 856 CA GLY A 114 20294 19613 19688 -130 -461 144 C
ATOM 857 C GLY A 114 -22.330 -32.784 32.712 1.00155.75 C
ANISOU 857 C GLY A 114 20132 19520 19525 -112 -446 136 C
ATOM 858 O GLY A 114 -22.844 -32.467 33.787 1.00157.32 O
ANISOU 858 O GLY A 114 20320 19774 19682 -135 -470 158 O
ATOM 859 N LEU A 115 -21.609 -31.941 31.975 1.00151.67 N
ANISOU 859 N LEU A 115 19609 18983 19037 -71 -405 103 N
ATOM 860 CA LEU A 115 -21.311 -30.590 32.429 1.00148.73 C
ANISOU 860 CA LEU A 115 19214 18644 18652 -50 -391 93 C
ATOM 861 C LEU A 115 -22.346 -29.569 31.948 1.00148.47 C
ANISOU 861 C LEU A 115 19184 18671 18556 -45 -360 72 C
ATOM 862 O LEU A 115 -22.890 -28.813 32.750 1.00149.07 O
ANISOU 862 O LEU A 115 19246 18806 18589 -54 -369 78 O
ATOM 863 CB LEU A 115 -19.900 -30.179 31.999 1.00148.25 C
ANISOU 863 CB LEU A 115 19142 18528 18659 -10 -369 74 C
ATOM 864 CG LEU A 115 -19.418 -28.768 32.364 1.00152.05 C
ANISOU 864 CG LEU A 115 19600 19034 19139 16 -354 62 C
ATOM 865 CD1 LEU A 115 -19.720 -28.362 33.806 1.00148.60 C
ANISOU 865 CD1 LEU A 115 19147 18647 18667 -5 -390 86 C
ATOM 866 CD2 LEU A 115 -17.932 -28.630 32.090 1.00150.39 C
ANISOU 866 CD2 LEU A 115 19377 18762 19004 49 -342 51 C
ATOM 867 N VAL A 116 -22.600 -29.544 30.645 1.00143.65 N
ANISOU 867 N VAL A 116 18590 18046 17943 -31 -324 46 N
ATOM 868 CA VAL A 116 -23.504 -28.567 30.043 1.00138.39 C
ANISOU 868 CA VAL A 116 17927 17429 17226 -24 -294 26 C
ATOM 869 C VAL A 116 -24.779 -29.257 29.582 1.00136.15 C
ANISOU 869 C VAL A 116 17665 17169 16896 -53 -298 31 C
ATOM 870 O VAL A 116 -24.744 -30.395 29.104 1.00135.54 O
ANISOU 870 O VAL A 116 17608 17052 16837 -66 -304 37 O
ATOM 871 CB VAL A 116 -22.834 -27.810 28.874 1.00135.76 C
ANISOU 871 CB VAL A 116 17595 17067 16921 13 -249 -7 C
ATOM 872 CG1 VAL A 116 -21.647 -27.002 29.377 1.00136.78 C
ANISOU 872 CG1 VAL A 116 17699 17179 17092 42 -247 -12 C
ATOM 873 CG2 VAL A 116 -22.399 -28.765 27.773 1.00134.74 C
ANISOU 873 CG2 VAL A 116 17487 16879 16828 18 -232 -20 C
ATOM 874 N THR A 117 -25.902 -28.566 29.742 1.00131.30 N
ANISOU 874 N THR A 117 17046 16619 16222 -64 -294 30 N
ATOM 875 CA THR A 117 -27.208 -29.066 29.315 1.00128.96 C
ANISOU 875 CA THR A 117 16768 16353 15878 -92 -297 36 C
ATOM 876 C THR A 117 -27.996 -27.927 28.692 1.00124.91 C
ANISOU 876 C THR A 117 16252 15883 15325 -80 -268 14 C
ATOM 877 O THR A 117 -27.507 -26.797 28.585 1.00119.05 O
ANISOU 877 O THR A 117 15494 15145 14595 -50 -247 -6 O
ATOM 878 CB THR A 117 -28.012 -29.674 30.488 1.00132.41 C
ANISOU 878 CB THR A 117 17199 16832 16277 -132 -337 69 C
ATOM 879 OG1 THR A 117 -28.075 -28.731 31.563 1.00132.21 O
ANISOU 879 OG1 THR A 117 17147 16857 16230 -130 -345 72 O
ATOM 880 CG2 THR A 117 -27.403 -30.986 30.979 1.00136.61 C
ANISOU 880 CG2 THR A 117 17740 17319 16848 -151 -371 96 C
ATOM 881 N GLY A 118 -29.218 -28.229 28.275 1.00124.21 N
ANISOU 881 N GLY A 118 16177 15826 15193 -103 -268 18 N
ATOM 882 CA GLY A 118 -30.096 -27.232 27.676 1.00125.48 C
ANISOU 882 CA GLY A 118 16334 16028 15315 -96 -246 0 C
ATOM 883 C GLY A 118 -30.596 -26.193 28.670 1.00127.25 C
ANISOU 883 C GLY A 118 16528 16314 15508 -95 -253 0 C
ATOM 884 O GLY A 118 -30.554 -24.986 28.399 1.00127.39 O
ANISOU 884 O GLY A 118 16532 16348 15524 -69 -233 -21 O
ATOM 885 N THR A 119 -31.066 -26.657 29.822 1.00127.72 N
ANISOU 885 N THR A 119 16577 16409 15542 -123 -283 23 N
ATOM 886 CA THR A 119 -31.645 -25.763 30.824 1.00127.02 C
ANISOU 886 CA THR A 119 16460 16386 15418 -126 -291 22 C
ATOM 887 C THR A 119 -30.582 -24.886 31.485 1.00123.11 C
ANISOU 887 C THR A 119 15943 15882 14952 -97 -289 11 C
ATOM 888 O THR A 119 -30.852 -23.734 31.826 1.00114.54 O
ANISOU 888 O THR A 119 14835 14836 13850 -82 -281 -7 O
ATOM 889 CB THR A 119 -32.434 -26.543 31.883 1.00129.53 C
ANISOU 889 CB THR A 119 16772 16747 15696 -168 -323 51 C
ATOM 890 OG1 THR A 119 -33.104 -27.641 31.257 1.00134.66 O
ANISOU 890 OG1 THR A 119 17447 17385 16334 -195 -330 67 O
ATOM 891 CG2 THR A 119 -33.468 -25.643 32.547 1.00126.74 C
ANISOU 891 CG2 THR A 119 16391 16470 15293 -174 -321 43 C
ATOM 892 N ARG A 120 -29.379 -25.427 31.656 1.00124.73 N
ANISOU 892 N ARG A 120 16154 16034 15205 -90 -298 20 N
ATOM 893 CA ARG A 120 -28.276 -24.641 32.206 1.00127.01 C
ANISOU 893 CA ARG A 120 16423 16307 15526 -63 -297 10 C
ATOM 894 C ARG A 120 -27.805 -23.569 31.229 1.00125.71 C
ANISOU 894 C ARG A 120 16256 16121 15387 -24 -263 -19 C
ATOM 895 O ARG A 120 -27.431 -22.472 31.649 1.00124.49 O
ANISOU 895 O ARG A 120 16080 15981 15239 -2 -259 -34 O
ATOM 896 CB ARG A 120 -27.117 -25.545 32.625 1.00131.98 C
ANISOU 896 CB ARG A 120 17059 16884 16204 -66 -317 30 C
ATOM 897 CG ARG A 120 -27.419 -26.420 33.833 1.00137.63 C
ANISOU 897 CG ARG A 120 17772 17624 16899 -105 -357 63 C
ATOM 898 CD ARG A 120 -26.218 -27.261 34.221 1.00142.19 C
ANISOU 898 CD ARG A 120 18354 18143 17531 -107 -380 83 C
ATOM 899 NE ARG A 120 -26.457 -28.049 35.427 1.00147.99 N
ANISOU 899 NE ARG A 120 19084 18900 18245 -147 -422 118 N
ATOM 900 CZ ARG A 120 -25.577 -28.884 35.973 1.00148.42 C
ANISOU 900 CZ ARG A 120 19141 18912 18342 -158 -452 144 C
ATOM 901 NH1 ARG A 120 -25.898 -29.549 37.073 1.00152.82 N
ANISOU 901 NH1 ARG A 120 19694 19496 18874 -198 -492 178 N
ATOM 902 NH2 ARG A 120 -24.376 -29.060 35.432 1.00146.71 N
ANISOU 902 NH2 ARG A 120 18928 18625 18191 -130 -444 136 N
ATOM 903 N ALA A 121 -27.828 -23.877 29.934 1.00119.88 N
ANISOU 903 N ALA A 121 15540 15349 14661 -17 -241 -29 N
ATOM 904 CA ALA A 121 -27.442 -22.889 28.923 1.00112.01 C
ANISOU 904 CA ALA A 121 14542 14334 13682 15 -209 -55 C
ATOM 905 C ALA A 121 -28.485 -21.781 28.806 1.00107.62 C
ANISOU 905 C ALA A 121 13972 13832 13085 19 -200 -69 C
ATOM 906 O ALA A 121 -28.131 -20.605 28.688 1.00106.80 O
ANISOU 906 O ALA A 121 13852 13731 12995 46 -188 -87 O
ATOM 907 CB ALA A 121 -27.206 -23.555 27.579 1.00109.43 C
ANISOU 907 CB ALA A 121 14243 13959 13374 17 -187 -61 C
ATOM 908 N ALA A 122 -29.765 -22.151 28.864 1.00102.40 N
ANISOU 908 N ALA A 122 13317 13213 12379 -8 -209 -61 N
ATOM 909 CA ALA A 122 -30.843 -21.164 28.762 1.00 96.40 C
ANISOU 909 CA ALA A 122 12541 12504 11581 -6 -203 -75 C
ATOM 910 C ALA A 122 -30.776 -20.136 29.886 1.00 95.38 C
ANISOU 910 C ALA A 122 12379 12413 11447 7 -213 -85 C
ATOM 911 O ALA A 122 -31.116 -18.973 29.683 1.00 96.77 O
ANISOU 911 O ALA A 122 12539 12612 11618 26 -203 -105 O
ATOM 912 CB ALA A 122 -32.199 -21.848 28.736 1.00 90.85 C
ANISOU 912 CB ALA A 122 11847 11839 10832 -40 -213 -62 C
ATOM 913 N GLY A 123 -30.326 -20.563 31.064 1.00 95.77 N
ANISOU 913 N GLY A 123 12420 12469 11499 -4 -234 -71 N
ATOM 914 CA GLY A 123 -30.164 -19.636 32.181 1.00 95.65 C
ANISOU 914 CA GLY A 123 12375 12488 11479 8 -245 -81 C
ATOM 915 C GLY A 123 -29.011 -18.673 31.966 1.00 94.01 C
ANISOU 915 C GLY A 123 12158 12244 11317 45 -234 -98 C
ATOM 916 O GLY A 123 -29.098 -17.496 32.333 1.00 93.50 O
ANISOU 916 O GLY A 123 12071 12206 11249 64 -232 -118 O
ATOM 917 N ILE A 124 -27.924 -19.168 31.380 1.00 93.54 N
ANISOU 917 N ILE A 124 12115 12124 11301 56 -226 -91 N
ATOM 918 CA ILE A 124 -26.753 -18.331 31.119 1.00 90.99 C
ANISOU 918 CA ILE A 124 11784 11764 11026 90 -214 -104 C
ATOM 919 C ILE A 124 -27.107 -17.208 30.138 1.00 89.85 C
ANISOU 919 C ILE A 124 11635 11625 10880 112 -192 -127 C
ATOM 920 O ILE A 124 -26.679 -16.065 30.313 1.00 88.17 O
ANISOU 920 O ILE A 124 11403 11414 10685 137 -190 -142 O
ATOM 921 CB ILE A 124 -25.578 -19.179 30.613 1.00 88.87 C
ANISOU 921 CB ILE A 124 11532 11429 10804 95 -208 -93 C
ATOM 922 CG1 ILE A 124 -25.125 -20.135 31.719 1.00 89.59 C
ANISOU 922 CG1 ILE A 124 11624 11514 10904 75 -236 -69 C
ATOM 923 CG2 ILE A 124 -24.426 -18.293 30.162 1.00 88.74 C
ANISOU 923 CG2 ILE A 124 11507 11375 10835 130 -191 -107 C
ATOM 924 CD1 ILE A 124 -24.105 -21.164 31.283 1.00 91.53 C
ANISOU 924 CD1 ILE A 124 11886 11695 11197 77 -234 -57 C
ATOM 925 N ILE A 125 -27.913 -17.529 29.130 1.00 87.84 N
ANISOU 925 N ILE A 125 11398 11374 10605 101 -178 -128 N
ATOM 926 CA ILE A 125 -28.355 -16.523 28.167 1.00 85.87 C
ANISOU 926 CA ILE A 125 11146 11131 10351 116 -160 -145 C
ATOM 927 C ILE A 125 -29.114 -15.400 28.879 1.00 86.22 C
ANISOU 927 C ILE A 125 11161 11227 10373 124 -172 -161 C
ATOM 928 O ILE A 125 -28.908 -14.217 28.586 1.00 87.59 O
ANISOU 928 O ILE A 125 11319 11397 10563 148 -166 -178 O
ATOM 929 CB ILE A 125 -29.205 -17.164 27.056 1.00 83.30 C
ANISOU 929 CB ILE A 125 10846 10804 10001 97 -148 -141 C
ATOM 930 CG1 ILE A 125 -28.349 -18.130 26.237 1.00 81.72 C
ANISOU 930 CG1 ILE A 125 10674 10548 9829 95 -133 -133 C
ATOM 931 CG2 ILE A 125 -29.829 -16.101 26.162 1.00 83.25 C
ANISOU 931 CG2 ILE A 125 10834 10811 9985 108 -136 -156 C
ATOM 932 CD1 ILE A 125 -29.121 -18.891 25.186 1.00 78.52 C
ANISOU 932 CD1 ILE A 125 10296 10139 9399 73 -123 -129 C
ATOM 933 N ALA A 126 -29.971 -15.767 29.826 1.00 84.72 N
ANISOU 933 N ALA A 126 10961 11084 10145 102 -188 -156 N
ATOM 934 CA ALA A 126 -30.738 -14.772 30.571 1.00 83.81 C
ANISOU 934 CA ALA A 126 10816 11021 10006 108 -198 -174 C
ATOM 935 C ALA A 126 -29.824 -13.885 31.421 1.00 83.12 C
ANISOU 935 C ALA A 126 10706 10929 9945 132 -207 -187 C
ATOM 936 O ALA A 126 -30.011 -12.667 31.463 1.00 77.91 O
ANISOU 936 O ALA A 126 10025 10286 9292 154 -207 -209 O
ATOM 937 CB ALA A 126 -31.798 -15.443 31.430 1.00 84.35 C
ANISOU 937 CB ALA A 126 10879 11143 10027 76 -212 -165 C
ATOM 938 N ILE A 127 -28.833 -14.492 32.069 1.00 86.19 N
ANISOU 938 N ILE A 127 11102 11295 10354 129 -216 -172 N
ATOM 939 CA ILE A 127 -27.918 -13.736 32.922 1.00 87.47 C
ANISOU 939 CA ILE A 127 11244 11450 10541 149 -227 -181 C
ATOM 940 C ILE A 127 -27.109 -12.737 32.092 1.00 91.24 C
ANISOU 940 C ILE A 127 11717 11886 11063 183 -214 -195 C
ATOM 941 O ILE A 127 -26.938 -11.580 32.492 1.00 91.50 O
ANISOU 941 O ILE A 127 11728 11930 11107 204 -220 -214 O
ATOM 942 CB ILE A 127 -26.997 -14.682 33.713 1.00 83.06 C
ANISOU 942 CB ILE A 127 10693 10868 9997 135 -243 -159 C
ATOM 943 CG1 ILE A 127 -27.827 -15.582 34.622 1.00 83.96 C
ANISOU 943 CG1 ILE A 127 10809 11028 10064 99 -260 -143 C
ATOM 944 CG2 ILE A 127 -25.994 -13.897 34.545 1.00 78.75 C
ANISOU 944 CG2 ILE A 127 10129 10313 9480 156 -255 -167 C
ATOM 945 CD1 ILE A 127 -27.131 -16.875 34.990 1.00 83.40 C
ANISOU 945 CD1 ILE A 127 10755 10926 10007 78 -274 -113 C
ATOM 946 N CYS A 128 -26.633 -13.176 30.931 1.00 90.29 N
ANISOU 946 N CYS A 128 11619 11721 10967 186 -196 -185 N
ATOM 947 CA CYS A 128 -25.841 -12.296 30.077 1.00 90.02 C
ANISOU 947 CA CYS A 128 11582 11649 10973 214 -181 -194 C
ATOM 948 C CYS A 128 -26.677 -11.134 29.548 1.00 89.79 C
ANISOU 948 C CYS A 128 11539 11644 10932 226 -178 -214 C
ATOM 949 O CYS A 128 -26.203 -9.996 29.502 1.00 91.24 O
ANISOU 949 O CYS A 128 11706 11817 11143 251 -180 -227 O
ATOM 950 CB CYS A 128 -25.215 -13.084 28.936 1.00 91.94 C
ANISOU 950 CB CYS A 128 11852 11843 11240 212 -160 -181 C
ATOM 951 SG CYS A 128 -24.074 -14.354 29.513 1.00 97.40 S
ANISOU 951 SG CYS A 128 12554 12495 11960 203 -167 -160 S
ATOM 952 N TRP A 129 -27.922 -11.409 29.166 1.00 87.03 N
ANISOU 952 N TRP A 129 11196 11326 10544 208 -174 -215 N
ATOM 953 CA TRP A 129 -28.784 -10.351 28.642 1.00 83.22 C
ANISOU 953 CA TRP A 129 10701 10866 10054 218 -173 -232 C
ATOM 954 C TRP A 129 -29.122 -9.320 29.719 1.00 81.88 C
ANISOU 954 C TRP A 129 10498 10734 9879 232 -192 -254 C
ATOM 955 O TRP A 129 -29.167 -8.121 29.433 1.00 80.28 O
ANISOU 955 O TRP A 129 10277 10530 9695 254 -195 -271 O
ATOM 956 CB TRP A 129 -30.053 -10.938 28.037 1.00 83.39 C
ANISOU 956 CB TRP A 129 10735 10912 10036 194 -168 -226 C
ATOM 957 CG TRP A 129 -29.937 -11.243 26.575 1.00 83.06 C
ANISOU 957 CG TRP A 129 10721 10836 10003 189 -149 -216 C
ATOM 958 CD1 TRP A 129 -29.677 -12.456 26.008 1.00 83.74 C
ANISOU 958 CD1 TRP A 129 10837 10896 10085 171 -136 -199 C
ATOM 959 CD2 TRP A 129 -30.086 -10.320 25.495 1.00 83.70 C
ANISOU 959 CD2 TRP A 129 10800 10904 10096 201 -141 -223 C
ATOM 960 NE1 TRP A 129 -29.655 -12.347 24.638 1.00 84.05 N
ANISOU 960 NE1 TRP A 129 10895 10909 10130 171 -119 -197 N
ATOM 961 CE2 TRP A 129 -29.904 -11.047 24.295 1.00 83.81 C
ANISOU 961 CE2 TRP A 129 10846 10888 10110 187 -122 -210 C
ATOM 962 CE3 TRP A 129 -30.356 -8.947 25.421 1.00 83.63 C
ANISOU 962 CE3 TRP A 129 10768 10908 10102 221 -151 -239 C
ATOM 963 CZ2 TRP A 129 -29.981 -10.448 23.036 1.00 83.13 C
ANISOU 963 CZ2 TRP A 129 10770 10785 10032 190 -112 -210 C
ATOM 964 CZ3 TRP A 129 -30.433 -8.351 24.169 1.00 83.80 C
ANISOU 964 CZ3 TRP A 129 10797 10910 10135 224 -143 -237 C
ATOM 965 CH2 TRP A 129 -30.244 -9.103 22.993 1.00 83.45 C
ANISOU 965 CH2 TRP A 129 10785 10837 10085 208 -123 -222 C
ATOM 966 N VAL A 130 -29.348 -9.777 30.948 1.00 83.20 N
ANISOU 966 N VAL A 130 10655 10935 10021 219 -204 -254 N
ATOM 967 CA VAL A 130 -29.605 -8.856 32.058 1.00 82.48 C
ANISOU 967 CA VAL A 130 10533 10881 9923 231 -220 -278 C
ATOM 968 C VAL A 130 -28.365 -8.003 32.336 1.00 81.19 C
ANISOU 968 C VAL A 130 10359 10685 9805 259 -227 -286 C
ATOM 969 O VAL A 130 -28.469 -6.789 32.537 1.00 78.70 O
ANISOU 969 O VAL A 130 10020 10380 9503 282 -236 -311 O
ATOM 970 CB VAL A 130 -30.066 -9.615 33.316 1.00 79.24 C
ANISOU 970 CB VAL A 130 10118 10516 9472 206 -232 -274 C
ATOM 971 CG1 VAL A 130 -30.138 -8.694 34.517 1.00 77.83 C
ANISOU 971 CG1 VAL A 130 9909 10375 9288 219 -247 -301 C
ATOM 972 CG2 VAL A 130 -31.428 -10.240 33.081 1.00 78.89 C
ANISOU 972 CG2 VAL A 130 10078 10512 9384 180 -227 -270 C
ATOM 973 N LEU A 131 -27.195 -8.635 32.335 1.00 80.00 N
ANISOU 973 N LEU A 131 10225 10493 9679 259 -225 -266 N
ATOM 974 CA LEU A 131 -25.951 -7.894 32.506 1.00 78.81 C
ANISOU 974 CA LEU A 131 10065 10307 9574 284 -231 -270 C
ATOM 975 C LEU A 131 -25.676 -6.961 31.330 1.00 81.49 C
ANISOU 975 C LEU A 131 10402 10613 9947 307 -220 -276 C
ATOM 976 O LEU A 131 -25.081 -5.896 31.515 1.00 82.98 O
ANISOU 976 O LEU A 131 10573 10788 10167 331 -230 -288 O
ATOM 977 CB LEU A 131 -24.781 -8.848 32.714 1.00 73.31 C
ANISOU 977 CB LEU A 131 9384 9571 8900 277 -230 -246 C
ATOM 978 CG LEU A 131 -24.780 -9.631 34.023 1.00 67.07 C
ANISOU 978 CG LEU A 131 8592 8806 8084 256 -248 -236 C
ATOM 979 CD1 LEU A 131 -23.706 -10.703 33.980 1.00 66.57 C
ANISOU 979 CD1 LEU A 131 8547 8697 8048 247 -247 -209 C
ATOM 980 CD2 LEU A 131 -24.606 -8.730 35.232 1.00 64.87 C
ANISOU 980 CD2 LEU A 131 8290 8553 7805 267 -269 -255 C
ATOM 981 N SER A 132 -26.116 -7.346 30.133 1.00 80.19 N
ANISOU 981 N SER A 132 10256 10438 9775 297 -202 -266 N
ATOM 982 CA SER A 132 -25.910 -6.500 28.960 1.00 78.48 C
ANISOU 982 CA SER A 132 10040 10193 9586 313 -193 -269 C
ATOM 983 C SER A 132 -26.721 -5.209 29.057 1.00 77.54 C
ANISOU 983 C SER A 132 9894 10102 9464 328 -207 -293 C
ATOM 984 O SER A 132 -26.249 -4.146 28.640 1.00 77.90 O
ANISOU 984 O SER A 132 9929 10125 9545 349 -212 -299 O
ATOM 985 CB SER A 132 -26.236 -7.262 27.682 1.00 77.27 C
ANISOU 985 CB SER A 132 9915 10026 9420 296 -171 -254 C
ATOM 986 OG SER A 132 -25.384 -8.382 27.540 1.00 76.53 O
ANISOU 986 OG SER A 132 9843 9900 9337 286 -158 -235 O
ATOM 987 N PHE A 133 -27.932 -5.292 29.605 1.00 76.92 N
ANISOU 987 N PHE A 133 9806 10072 9348 317 -215 -306 N
ATOM 988 CA PHE A 133 -28.706 -4.080 29.858 1.00 78.17 C
ANISOU 988 CA PHE A 133 9936 10259 9508 333 -230 -333 C
ATOM 989 C PHE A 133 -28.045 -3.220 30.931 1.00 79.09 C
ANISOU 989 C PHE A 133 10028 10376 9647 355 -249 -353 C
ATOM 990 O PHE A 133 -27.986 -1.997 30.796 1.00 80.11 O
ANISOU 990 O PHE A 133 10136 10496 9805 378 -261 -370 O
ATOM 991 CB PHE A 133 -30.140 -4.419 30.254 1.00 80.15 C
ANISOU 991 CB PHE A 133 10178 10563 9713 315 -233 -344 C
ATOM 992 CG PHE A 133 -31.025 -4.750 29.100 1.00 82.20 C
ANISOU 992 CG PHE A 133 10453 10824 9957 300 -222 -333 C
ATOM 993 CD1 PHE A 133 -31.602 -3.741 28.342 1.00 83.05 C
ANISOU 993 CD1 PHE A 133 10546 10929 10079 312 -228 -344 C
ATOM 994 CD2 PHE A 133 -31.294 -6.071 28.770 1.00 86.29 C
ANISOU 994 CD2 PHE A 133 10998 11344 10445 272 -208 -310 C
ATOM 995 CE1 PHE A 133 -32.427 -4.045 27.268 1.00 84.61 C
ANISOU 995 CE1 PHE A 133 10759 11129 10262 295 -220 -331 C
ATOM 996 CE2 PHE A 133 -32.118 -6.387 27.700 1.00 87.38 C
ANISOU 996 CE2 PHE A 133 11151 11483 10566 256 -199 -300 C
ATOM 997 CZ PHE A 133 -32.688 -5.370 26.943 1.00 86.79 C
ANISOU 997 CZ PHE A 133 11063 11407 10505 267 -205 -310 C
ATOM 998 N ALA A 134 -27.531 -3.857 31.981 1.00 77.47 N
ANISOU 998 N ALA A 134 9825 10179 9431 347 -253 -349 N
ATOM 999 CA ALA A 134 -26.926 -3.117 33.090 1.00 76.63 C
ANISOU 999 CA ALA A 134 9697 10077 9341 365 -271 -367 C
ATOM 1000 C ALA A 134 -25.681 -2.356 32.632 1.00 76.98 C
ANISOU 1000 C ALA A 134 9741 10069 9440 389 -276 -361 C
ATOM 1001 O ALA A 134 -25.539 -1.159 32.912 1.00 75.16 O
ANISOU 1001 O ALA A 134 9488 9836 9234 412 -292 -383 O
ATOM 1002 CB ALA A 134 -26.602 -4.053 34.242 1.00 74.13 C
ANISOU 1002 CB ALA A 134 9387 9778 9000 347 -276 -358 C
ATOM 1003 N ILE A 135 -24.797 -3.036 31.908 1.00 77.24 N
ANISOU 1003 N ILE A 135 9795 10059 9491 383 -261 -333 N
ATOM 1004 CA ILE A 135 -23.575 -2.401 31.426 1.00 76.11 C
ANISOU 1004 CA ILE A 135 9652 9868 9400 404 -262 -325 C
ATOM 1005 C ILE A 135 -23.903 -1.336 30.377 1.00 76.39 C
ANISOU 1005 C ILE A 135 9678 9890 9455 418 -262 -332 C
ATOM 1006 O ILE A 135 -23.423 -0.206 30.456 1.00 74.14 O
ANISOU 1006 O ILE A 135 9375 9589 9206 440 -278 -342 O
ATOM 1007 CB ILE A 135 -22.592 -3.444 30.873 1.00 73.73 C
ANISOU 1007 CB ILE A 135 9374 9526 9113 393 -242 -295 C
ATOM 1008 CG1 ILE A 135 -22.143 -4.385 31.989 1.00 72.47 C
ANISOU 1008 CG1 ILE A 135 9220 9373 8943 381 -249 -286 C
ATOM 1009 CG2 ILE A 135 -21.392 -2.761 30.237 1.00 73.14 C
ANISOU 1009 CG2 ILE A 135 9296 9403 9091 413 -240 -286 C
ATOM 1010 CD1 ILE A 135 -21.418 -5.613 31.492 1.00 71.27 C
ANISOU 1010 CD1 ILE A 135 9091 9186 8801 367 -231 -259 C
ATOM 1011 N GLY A 136 -24.738 -1.693 29.409 1.00 77.56 N
ANISOU 1011 N GLY A 136 9840 10047 9582 403 -247 -325 N
ATOM 1012 CA GLY A 136 -25.055 -0.783 28.318 1.00 79.38 C
ANISOU 1012 CA GLY A 136 10066 10265 9831 412 -248 -326 C
ATOM 1013 C GLY A 136 -25.823 0.457 28.739 1.00 81.74 C
ANISOU 1013 C GLY A 136 10334 10586 10136 429 -273 -355 C
ATOM 1014 O GLY A 136 -25.800 1.457 28.027 1.00 85.88 O
ANISOU 1014 O GLY A 136 10850 11092 10690 442 -283 -356 O
ATOM 1015 N LEU A 137 -26.493 0.398 29.889 1.00 80.50 N
ANISOU 1015 N LEU A 137 10163 10472 9953 429 -284 -378 N
ATOM 1016 CA LEU A 137 -27.292 1.522 30.367 1.00 80.36 C
ANISOU 1016 CA LEU A 137 10114 10480 9941 446 -306 -411 C
ATOM 1017 C LEU A 137 -26.731 2.141 31.640 1.00 83.00 C
ANISOU 1017 C LEU A 137 10427 10820 10290 465 -326 -435 C
ATOM 1018 O LEU A 137 -27.453 2.823 32.366 1.00 83.14 O
ANISOU 1018 O LEU A 137 10419 10869 10300 476 -341 -469 O
ATOM 1019 CB LEU A 137 -28.750 1.091 30.561 1.00 76.94 C
ANISOU 1019 CB LEU A 137 9676 10096 9463 430 -302 -425 C
ATOM 1020 CG LEU A 137 -29.438 0.556 29.304 1.00 73.17 C
ANISOU 1020 CG LEU A 137 9218 9615 8969 411 -286 -404 C
ATOM 1021 CD1 LEU A 137 -30.561 -0.398 29.678 1.00 72.84 C
ANISOU 1021 CD1 LEU A 137 9181 9621 8876 387 -276 -406 C
ATOM 1022 CD2 LEU A 137 -29.940 1.686 28.421 1.00 71.29 C
ANISOU 1022 CD2 LEU A 137 8964 9364 8758 424 -300 -411 C
ATOM 1023 N THR A 138 -25.453 1.908 31.919 1.00 87.86 N
ANISOU 1023 N THR A 138 11052 11404 10926 468 -325 -419 N
ATOM 1024 CA THR A 138 -24.801 2.555 33.058 1.00 89.70 C
ANISOU 1024 CA THR A 138 11267 11636 11177 486 -346 -439 C
ATOM 1025 C THR A 138 -24.879 4.096 33.029 1.00 89.31 C
ANISOU 1025 C THR A 138 11191 11578 11167 514 -371 -465 C
ATOM 1026 O THR A 138 -25.140 4.694 34.066 1.00 90.86 O
ANISOU 1026 O THR A 138 11365 11798 11359 526 -390 -498 O
ATOM 1027 CB THR A 138 -23.349 2.081 33.202 1.00 90.24 C
ANISOU 1027 CB THR A 138 11351 11667 11269 485 -342 -412 C
ATOM 1028 OG1 THR A 138 -23.326 0.656 33.276 1.00 93.04 O
ANISOU 1028 OG1 THR A 138 11729 12031 11592 459 -323 -390 O
ATOM 1029 CG2 THR A 138 -22.708 2.645 34.450 1.00 88.53 C
ANISOU 1029 CG2 THR A 138 11117 11452 11067 499 -366 -431 C
ATOM 1030 N PRO A 139 -24.693 4.749 31.857 1.00 85.96 N
ANISOU 1030 N PRO A 139 10767 11118 10778 523 -374 -452 N
ATOM 1031 CA PRO A 139 -24.855 6.214 31.851 1.00 85.20 C
ANISOU 1031 CA PRO A 139 10642 11010 10719 548 -402 -477 C
ATOM 1032 C PRO A 139 -26.248 6.697 32.248 1.00 88.39 C
ANISOU 1032 C PRO A 139 11022 11457 11104 554 -413 -515 C
ATOM 1033 O PRO A 139 -26.385 7.830 32.702 1.00 88.64 O
ANISOU 1033 O PRO A 139 11028 11488 11163 577 -440 -546 O
ATOM 1034 CB PRO A 139 -24.555 6.597 30.403 1.00 84.83 C
ANISOU 1034 CB PRO A 139 10605 10923 10705 548 -400 -449 C
ATOM 1035 CG PRO A 139 -23.670 5.507 29.916 1.00 82.70 C
ANISOU 1035 CG PRO A 139 10364 10632 10427 530 -373 -411 C
ATOM 1036 CD PRO A 139 -24.187 4.270 30.560 1.00 82.98 C
ANISOU 1036 CD PRO A 139 10412 10704 10411 511 -354 -414 C
ATOM 1037 N MET A 140 -27.263 5.849 32.112 1.00 89.98 N
ANISOU 1037 N MET A 140 11232 11694 11261 533 -394 -513 N
ATOM 1038 CA MET A 140 -28.615 6.214 32.539 1.00 87.84 C
ANISOU 1038 CA MET A 140 10937 11468 10970 537 -402 -550 C
ATOM 1039 C MET A 140 -28.700 6.415 34.053 1.00 88.28 C
ANISOU 1039 C MET A 140 10973 11561 11010 546 -412 -588 C
ATOM 1040 O MET A 140 -29.510 7.213 34.529 1.00 86.42 O
ANISOU 1040 O MET A 140 10707 11351 10777 562 -426 -629 O
ATOM 1041 CB MET A 140 -29.617 5.150 32.108 1.00 85.80 C
ANISOU 1041 CB MET A 140 10693 11241 10665 510 -379 -536 C
ATOM 1042 CG MET A 140 -29.625 4.876 30.613 1.00 86.15 C
ANISOU 1042 CG MET A 140 10760 11255 10719 498 -368 -499 C
ATOM 1043 SD MET A 140 -30.784 5.912 29.699 1.00 87.51 S
ANISOU 1043 SD MET A 140 10910 11426 10914 507 -386 -512 S
ATOM 1044 CE MET A 140 -32.358 5.352 30.359 1.00 84.80 C
ANISOU 1044 CE MET A 140 10551 11148 10520 494 -377 -539 C
ATOM 1045 N LEU A 141 -27.845 5.723 34.799 1.00 89.01 N
ANISOU 1045 N LEU A 141 11081 11654 11086 537 -405 -577 N
ATOM 1046 CA LEU A 141 -27.879 5.771 36.255 1.00 90.13 C
ANISOU 1046 CA LEU A 141 11209 11834 11204 539 -413 -609 C
ATOM 1047 C LEU A 141 -27.254 7.027 36.845 1.00 91.08 C
ANISOU 1047 C LEU A 141 11307 11934 11366 568 -441 -638 C
ATOM 1048 O LEU A 141 -27.246 7.189 38.066 1.00 93.67 O
ANISOU 1048 O LEU A 141 11623 12293 11676 571 -450 -669 O
ATOM 1049 CB LEU A 141 -27.215 4.523 36.840 1.00 89.35 C
ANISOU 1049 CB LEU A 141 11135 11742 11072 515 -398 -582 C
ATOM 1050 CG LEU A 141 -27.803 3.180 36.410 1.00 87.71 C
ANISOU 1050 CG LEU A 141 10949 11555 10820 484 -372 -554 C
ATOM 1051 CD1 LEU A 141 -26.901 2.055 36.891 1.00 87.92 C
ANISOU 1051 CD1 LEU A 141 11001 11574 10830 463 -364 -523 C
ATOM 1052 CD2 LEU A 141 -29.235 2.975 36.895 1.00 84.27 C
ANISOU 1052 CD2 LEU A 141 10498 11183 10339 472 -366 -581 C
ATOM 1053 N GLY A 142 -26.733 7.919 36.004 1.00 89.70 N
ANISOU 1053 N GLY A 142 11128 11710 11245 588 -457 -629 N
ATOM 1054 CA GLY A 142 -26.195 9.181 36.497 1.00 90.06 C
ANISOU 1054 CA GLY A 142 11152 11734 11335 616 -487 -657 C
ATOM 1055 C GLY A 142 -24.839 9.558 35.937 1.00 89.71 C
ANISOU 1055 C GLY A 142 11119 11629 11340 626 -499 -625 C
ATOM 1056 O GLY A 142 -24.358 10.666 36.180 1.00 91.11 O
ANISOU 1056 O GLY A 142 11278 11780 11559 649 -527 -644 O
ATOM 1057 N TRP A 143 -24.216 8.646 35.194 1.00 87.96 N
ANISOU 1057 N TRP A 143 10924 11383 11112 607 -477 -579 N
ATOM 1058 CA TRP A 143 -22.917 8.909 34.585 1.00 87.74 C
ANISOU 1058 CA TRP A 143 10907 11300 11131 614 -483 -545 C
ATOM 1059 C TRP A 143 -23.109 9.457 33.169 1.00 90.26 C
ANISOU 1059 C TRP A 143 11225 11588 11481 617 -485 -527 C
ATOM 1060 O TRP A 143 -22.740 8.833 32.173 1.00 92.33 O
ANISOU 1060 O TRP A 143 11509 11829 11743 602 -464 -488 O
ATOM 1061 CB TRP A 143 -22.054 7.651 34.608 1.00 83.75 C
ANISOU 1061 CB TRP A 143 10429 10784 10607 593 -460 -508 C
ATOM 1062 CG TRP A 143 -20.608 7.892 34.303 1.00 82.35 C
ANISOU 1062 CG TRP A 143 10258 10556 10476 601 -466 -480 C
ATOM 1063 CD1 TRP A 143 -20.003 9.095 34.061 1.00 81.06 C
ANISOU 1063 CD1 TRP A 143 10079 10355 10364 622 -492 -482 C
ATOM 1064 CD2 TRP A 143 -19.579 6.906 34.234 1.00 82.14 C
ANISOU 1064 CD2 TRP A 143 10253 10507 10449 587 -448 -444 C
ATOM 1065 NE1 TRP A 143 -18.666 8.913 33.831 1.00 80.32 N
ANISOU 1065 NE1 TRP A 143 9996 10221 10302 622 -489 -450 N
ATOM 1066 CE2 TRP A 143 -18.374 7.581 33.934 1.00 81.17 C
ANISOU 1066 CE2 TRP A 143 10125 10336 10380 601 -462 -427 C
ATOM 1067 CE3 TRP A 143 -19.554 5.514 34.394 1.00 82.00 C
ANISOU 1067 CE3 TRP A 143 10257 10504 10395 564 -423 -425 C
ATOM 1068 CZ2 TRP A 143 -17.155 6.912 33.785 1.00 79.83 C
ANISOU 1068 CZ2 TRP A 143 9970 10135 10228 594 -449 -393 C
ATOM 1069 CZ3 TRP A 143 -18.341 4.849 34.248 1.00 79.96 C
ANISOU 1069 CZ3 TRP A 143 10013 10211 10156 557 -412 -392 C
ATOM 1070 CH2 TRP A 143 -17.158 5.551 33.943 1.00 78.54 C
ANISOU 1070 CH2 TRP A 143 9826 9985 10030 573 -424 -377 C
ATOM 1071 N ASN A 144 -23.689 10.647 33.103 1.00 88.61 N
ANISOU 1071 N ASN A 144 10991 11377 11300 637 -512 -555 N
ATOM 1072 CA ASN A 144 -24.018 11.288 31.838 1.00 89.58 C
ANISOU 1072 CA ASN A 144 11110 11474 11453 640 -521 -540 C
ATOM 1073 C ASN A 144 -23.627 12.754 31.875 1.00 93.79 C
ANISOU 1073 C ASN A 144 11617 11974 12045 666 -560 -555 C
ATOM 1074 O ASN A 144 -23.202 13.278 32.905 1.00 93.99 O
ANISOU 1074 O ASN A 144 11628 11998 12084 684 -580 -583 O
ATOM 1075 CB ASN A 144 -25.513 11.143 31.517 1.00 89.65 C
ANISOU 1075 CB ASN A 144 11111 11519 11433 632 -514 -557 C
ATOM 1076 CG ASN A 144 -26.402 11.605 32.652 1.00 91.56 C
ANISOU 1076 CG ASN A 144 11325 11801 11664 648 -528 -610 C
ATOM 1077 OD1 ASN A 144 -26.384 12.772 33.039 1.00 93.98 O
ANISOU 1077 OD1 ASN A 144 11605 12095 12009 673 -560 -641 O
ATOM 1078 ND2 ASN A 144 -27.185 10.684 33.197 1.00 93.18 N
ANISOU 1078 ND2 ASN A 144 11534 12055 11814 632 -505 -623 N
ATOM 1079 N ASN A 145 -23.788 13.409 30.731 1.00 98.77 N
ANISOU 1079 N ASN A 145 12244 12576 12708 667 -573 -537 N
ATOM 1080 CA ASN A 145 -23.512 14.829 30.577 1.00104.40 C
ANISOU 1080 CA ASN A 145 12932 13253 13480 689 -615 -547 C
ATOM 1081 C ASN A 145 -24.782 15.672 30.583 1.00106.34 C
ANISOU 1081 C ASN A 145 13150 13514 13740 703 -640 -584 C
ATOM 1082 O ASN A 145 -24.787 16.775 30.024 1.00111.25 O
ANISOU 1082 O ASN A 145 13755 14102 14412 715 -674 -582 O
ATOM 1083 CB ASN A 145 -22.727 15.073 29.282 1.00105.95 C
ANISOU 1083 CB ASN A 145 13142 13404 13710 678 -617 -497 C
ATOM 1084 CG ASN A 145 -21.295 14.591 29.365 1.00107.63 C
ANISOU 1084 CG ASN A 145 13372 13593 13928 672 -601 -466 C
ATOM 1085 OD1 ASN A 145 -20.597 14.838 30.349 1.00110.09 O
ANISOU 1085 OD1 ASN A 145 13677 13899 14255 687 -615 -482 O
ATOM 1086 ND2 ASN A 145 -20.845 13.903 28.324 1.00104.68 N
ANISOU 1086 ND2 ASN A 145 13023 13206 13544 650 -573 -423 N
ATOM 1087 N CYS A 146 -25.852 15.179 31.203 1.00104.20 N
ANISOU 1087 N CYS A 146 12872 13291 13427 701 -626 -617 N
ATOM 1088 CA CYS A 146 -27.088 15.959 31.275 1.00105.03 C
ANISOU 1088 CA CYS A 146 12948 13412 13548 716 -648 -656 C
ATOM 1089 C CYS A 146 -26.959 17.170 32.190 1.00110.76 C
ANISOU 1089 C CYS A 146 13641 14127 14315 749 -687 -703 C
ATOM 1090 O CYS A 146 -27.599 18.190 31.961 1.00113.67 O
ANISOU 1090 O CYS A 146 13981 14483 14725 766 -719 -726 O
ATOM 1091 CB CYS A 146 -28.259 15.084 31.704 1.00100.77 C
ANISOU 1091 CB CYS A 146 12407 12930 12951 705 -620 -678 C
ATOM 1092 SG CYS A 146 -28.625 13.731 30.561 1.00 98.19 S
ANISOU 1092 SG CYS A 146 12115 12614 12577 667 -581 -628 S
ATOM 1093 N GLY A 147 -26.108 17.058 33.206 1.00115.67 N
ANISOU 1093 N GLY A 147 14267 14752 14930 756 -685 -716 N
ATOM 1094 CA GLY A 147 -25.854 18.155 34.137 1.00121.13 C
ANISOU 1094 CA GLY A 147 14931 15432 15659 785 -721 -761 C
ATOM 1095 C GLY A 147 -25.204 19.372 33.495 1.00124.40 C
ANISOU 1095 C GLY A 147 15334 15786 16145 801 -763 -746 C
ATOM 1096 O GLY A 147 -25.317 20.480 34.015 1.00128.76 O
ANISOU 1096 O GLY A 147 15859 16326 16740 828 -800 -786 O
ATOM 1097 N GLN A 148 -24.521 19.161 32.371 1.00123.58 N
ANISOU 1097 N GLN A 148 15251 15648 16055 784 -757 -688 N
ATOM 1098 CA GLN A 148 -23.794 20.229 31.678 1.00123.09 C
ANISOU 1098 CA GLN A 148 15182 15530 16059 793 -795 -664 C
ATOM 1099 C GLN A 148 -24.207 20.256 30.207 1.00116.37 C
ANISOU 1099 C GLN A 148 14336 14660 15218 775 -795 -622 C
ATOM 1100 O GLN A 148 -23.400 19.970 29.324 1.00113.79 O
ANISOU 1100 O GLN A 148 14031 14308 14895 757 -784 -570 O
ATOM 1101 CB GLN A 148 -22.284 20.024 31.802 1.00132.16 C
ANISOU 1101 CB GLN A 148 16349 16650 17217 788 -791 -630 C
ATOM 1102 CG GLN A 148 -21.810 19.567 33.174 1.00142.23 C
ANISOU 1102 CG GLN A 148 17629 17949 18464 795 -779 -658 C
ATOM 1103 CD GLN A 148 -20.661 18.566 33.104 1.00149.59 C
ANISOU 1103 CD GLN A 148 18590 18873 19373 775 -748 -613 C
ATOM 1104 OE1 GLN A 148 -19.735 18.711 32.300 1.00157.38 O
ANISOU 1104 OE1 GLN A 148 19586 19820 20390 768 -752 -569 O
ATOM 1105 NE2 GLN A 148 -20.715 17.543 33.957 1.00158.79 N
ANISOU 1105 NE2 GLN A 148 19769 20078 20486 766 -719 -625 N
ATOM 1106 N PRO A 149 -25.473 20.608 29.926 1.00116.59 N
ANISOU 1106 N PRO A 149 14345 14703 15251 780 -807 -645 N
ATOM 1107 CA PRO A 149 -25.948 20.561 28.547 1.00119.58 C
ANISOU 1107 CA PRO A 149 14732 15069 15635 759 -807 -605 C
ATOM 1108 C PRO A 149 -25.402 21.697 27.688 1.00124.81 C
ANISOU 1108 C PRO A 149 15384 15676 16361 762 -851 -575 C
ATOM 1109 O PRO A 149 -25.075 22.775 28.196 1.00130.10 O
ANISOU 1109 O PRO A 149 16031 16319 17084 787 -892 -600 O
ATOM 1110 CB PRO A 149 -27.460 20.683 28.700 1.00116.58 C
ANISOU 1110 CB PRO A 149 14329 14720 15245 767 -813 -645 C
ATOM 1111 CG PRO A 149 -27.638 21.498 29.930 1.00116.56 C
ANISOU 1111 CG PRO A 149 14294 14723 15269 801 -840 -706 C
ATOM 1112 CD PRO A 149 -26.508 21.121 30.843 1.00117.33 C
ANISOU 1112 CD PRO A 149 14407 14824 15349 804 -824 -710 C
ATOM 1113 N LYS A 150 -25.307 21.439 26.388 1.00122.13 N
ANISOU 1113 N LYS A 150 15064 15321 16018 734 -842 -522 N
ATOM 1114 CA LYS A 150 -24.922 22.453 25.418 1.00124.01 C
ANISOU 1114 CA LYS A 150 15294 15511 16312 729 -883 -487 C
ATOM 1115 C LYS A 150 -26.132 23.333 25.121 1.00130.51 C
ANISOU 1115 C LYS A 150 16089 16329 17172 740 -924 -509 C
ATOM 1116 O LYS A 150 -27.010 22.958 24.345 1.00135.10 O
ANISOU 1116 O LYS A 150 16677 16925 17732 720 -914 -493 O
ATOM 1117 CB LYS A 150 -24.379 21.799 24.145 1.00119.47 C
ANISOU 1117 CB LYS A 150 14752 14928 15714 693 -855 -424 C
ATOM 1118 CG LYS A 150 -22.926 21.376 24.237 1.00117.76 C
ANISOU 1118 CG LYS A 150 14556 14697 15490 686 -831 -395 C
ATOM 1119 CD LYS A 150 -22.425 20.829 22.910 1.00118.04 C
ANISOU 1119 CD LYS A 150 14620 14723 15506 650 -805 -336 C
ATOM 1120 CE LYS A 150 -20.913 20.972 22.776 1.00117.24 C
ANISOU 1120 CE LYS A 150 14527 14592 15428 646 -802 -302 C
ATOM 1121 NZ LYS A 150 -20.131 20.191 23.778 1.00121.44 N
ANISOU 1121 NZ LYS A 150 15069 15137 15935 657 -769 -318 N
ATOM 1122 N GLU A 151 -26.185 24.500 25.751 1.00133.39 N
ANISOU 1122 N GLU A 151 16419 16669 17593 770 -972 -546 N
ATOM 1123 CA GLU A 151 -27.340 25.384 25.614 1.00140.25 C
ANISOU 1123 CA GLU A 151 17254 17530 18504 785 -1015 -575 C
ATOM 1124 C GLU A 151 -27.347 26.138 24.293 1.00140.99 C
ANISOU 1124 C GLU A 151 17346 17581 18644 767 -1055 -526 C
ATOM 1125 O GLU A 151 -28.404 26.330 23.693 1.00143.92 O
ANISOU 1125 O GLU A 151 17705 17954 19025 760 -1072 -524 O
ATOM 1126 CB GLU A 151 -27.407 26.355 26.791 1.00145.55 C
ANISOU 1126 CB GLU A 151 17890 18190 19221 826 -1052 -637 C
ATOM 1127 CG GLU A 151 -27.804 25.706 28.108 1.00150.00 C
ANISOU 1127 CG GLU A 151 18450 18806 19739 843 -1017 -695 C
ATOM 1128 CD GLU A 151 -29.278 25.348 28.172 1.00156.52 C
ANISOU 1128 CD GLU A 151 19260 19672 20539 844 -1003 -728 C
ATOM 1129 OE1 GLU A 151 -30.125 26.195 27.818 1.00158.84 O
ANISOU 1129 OE1 GLU A 151 19524 19948 20880 856 -1043 -744 O
ATOM 1130 OE2 GLU A 151 -29.591 24.216 28.583 1.00158.24 O
ANISOU 1130 OE2 GLU A 151 19496 19939 20690 833 -953 -737 O
ATOM 1131 N GLY A 152 -26.172 26.571 23.842 1.00141.28 N
ANISOU 1131 N GLY A 152 17392 17579 18709 757 -1072 -484 N
ATOM 1132 CA GLY A 152 -26.048 27.282 22.568 1.00137.80 C
ANISOU 1132 CA GLY A 152 16950 17098 18309 735 -1111 -431 C
ATOM 1133 C GLY A 152 -26.507 26.443 21.386 1.00134.02 C
ANISOU 1133 C GLY A 152 16500 16639 17783 695 -1079 -385 C
ATOM 1134 O GLY A 152 -27.142 26.945 20.454 1.00130.56 O
ANISOU 1134 O GLY A 152 16053 16183 17369 679 -1112 -360 O
ATOM 1135 N LYS A 153 -26.181 25.156 21.425 1.00131.39 N
ANISOU 1135 N LYS A 153 16200 16341 17382 678 -1017 -373 N
ATOM 1136 CA LYS A 153 -26.633 24.235 20.389 1.00128.17 C
ANISOU 1136 CA LYS A 153 15821 15956 16922 641 -982 -336 C
ATOM 1137 C LYS A 153 -28.129 23.955 20.510 1.00128.44 C
ANISOU 1137 C LYS A 153 15843 16021 16937 645 -979 -368 C
ATOM 1138 O LYS A 153 -28.787 23.667 19.510 1.00129.64 O
ANISOU 1138 O LYS A 153 16007 16179 17070 616 -976 -338 O
ATOM 1139 CB LYS A 153 -25.831 22.940 20.437 1.00125.52 C
ANISOU 1139 CB LYS A 153 15522 15645 16523 624 -917 -318 C
ATOM 1140 CG LYS A 153 -25.986 22.048 19.215 1.00125.09 C
ANISOU 1140 CG LYS A 153 15502 15606 16420 582 -882 -271 C
ATOM 1141 CD LYS A 153 -25.078 20.829 19.285 1.00124.50 C
ANISOU 1141 CD LYS A 153 15461 15551 16292 569 -821 -255 C
ATOM 1142 CE LYS A 153 -23.607 21.211 19.163 1.00123.78 C
ANISOU 1142 CE LYS A 153 15374 15428 16229 567 -825 -226 C
ATOM 1143 NZ LYS A 153 -22.701 20.041 19.287 1.00122.84 N
ANISOU 1143 NZ LYS A 153 15284 15325 16065 557 -768 -214 N
ATOM 1144 N ALA A 154 -28.665 24.031 21.724 1.00124.44 N
ANISOU 1144 N ALA A 154 15312 15535 16434 679 -981 -429 N
ATOM 1145 CA ALA A 154 -30.091 23.773 21.938 1.00126.04 C
ANISOU 1145 CA ALA A 154 15499 15770 16620 685 -977 -463 C
ATOM 1146 C ALA A 154 -30.949 24.913 21.392 1.00129.54 C
ANISOU 1146 C ALA A 154 15910 16183 17126 690 -1037 -465 C
ATOM 1147 O ALA A 154 -31.881 24.679 20.614 1.00127.98 O
ANISOU 1147 O ALA A 154 15715 15996 16916 669 -1039 -447 O
ATOM 1148 CB ALA A 154 -30.379 23.528 23.413 1.00129.35 C
ANISOU 1148 CB ALA A 154 15901 16223 17023 717 -959 -528 C
ATOM 1149 N HIS A 155 -30.632 26.145 21.782 1.00131.38 N
ANISOU 1149 N HIS A 155 16113 16379 17429 718 -1089 -485 N
ATOM 1150 CA HIS A 155 -31.378 27.301 21.294 1.00136.26 C
ANISOU 1150 CA HIS A 155 16697 16962 18115 725 -1152 -487 C
ATOM 1151 C HIS A 155 -31.197 27.533 19.801 1.00136.12 C
ANISOU 1151 C HIS A 155 16696 16913 18110 685 -1176 -415 C
ATOM 1152 O HIS A 155 -32.044 28.168 19.178 1.00140.61 O
ANISOU 1152 O HIS A 155 17245 17463 18719 679 -1220 -407 O
ATOM 1153 CB HIS A 155 -30.996 28.559 22.068 1.00140.32 C
ANISOU 1153 CB HIS A 155 17175 17439 18703 763 -1204 -525 C
ATOM 1154 CG HIS A 155 -31.482 28.563 23.481 1.00146.18 C
ANISOU 1154 CG HIS A 155 17890 18209 19442 803 -1193 -603 C
ATOM 1155 ND1 HIS A 155 -30.731 28.069 24.525 1.00148.37 N
ANISOU 1155 ND1 HIS A 155 18179 18509 19684 818 -1156 -631 N
ATOM 1156 CD2 HIS A 155 -32.644 28.995 24.024 1.00149.69 C
ANISOU 1156 CD2 HIS A 155 18296 18666 19915 830 -1213 -660 C
ATOM 1157 CE1 HIS A 155 -31.407 28.201 25.653 1.00151.82 C
ANISOU 1157 CE1 HIS A 155 18589 18973 20124 850 -1154 -701 C
ATOM 1158 NE2 HIS A 155 -32.572 28.759 25.376 1.00152.42 N
ANISOU 1158 NE2 HIS A 155 18631 19042 20237 859 -1187 -722 N
ATOM 1159 N SER A 156 -30.107 27.017 19.230 1.00132.88 N
ANISOU 1159 N SER A 156 16323 16500 17666 657 -1147 -365 N
ATOM 1160 CA SER A 156 -29.892 27.142 17.790 1.00133.10 C
ANISOU 1160 CA SER A 156 16371 16505 17696 614 -1162 -296 C
ATOM 1161 C SER A 156 -31.005 26.436 17.008 1.00136.05 C
ANISOU 1161 C SER A 156 16758 16906 18027 585 -1145 -279 C
ATOM 1162 O SER A 156 -31.512 26.973 16.024 1.00135.94 O
ANISOU 1162 O SER A 156 16740 16871 18042 562 -1185 -244 O
ATOM 1163 CB SER A 156 -28.521 26.600 17.405 1.00131.94 C
ANISOU 1163 CB SER A 156 16260 16356 17514 590 -1125 -252 C
ATOM 1164 OG SER A 156 -28.321 26.675 16.008 1.00131.94 O
ANISOU 1164 OG SER A 156 16281 16340 17509 546 -1136 -186 O
ATOM 1165 N GLN A 157 -31.387 25.247 17.467 1.00135.49 N
ANISOU 1165 N GLN A 157 16706 16883 17892 586 -1087 -303 N
ATOM 1166 CA GLN A 157 -32.481 24.493 16.870 1.00134.23 C
ANISOU 1166 CA GLN A 157 16558 16752 17689 561 -1067 -293 C
ATOM 1167 C GLN A 157 -33.804 24.698 17.599 1.00131.13 C
ANISOU 1167 C GLN A 157 16130 16378 17316 590 -1083 -348 C
ATOM 1168 O GLN A 157 -34.793 24.034 17.279 1.00133.03 O
ANISOU 1168 O GLN A 157 16377 16647 17521 574 -1065 -347 O
ATOM 1169 CB GLN A 157 -32.127 23.012 16.801 1.00133.46 C
ANISOU 1169 CB GLN A 157 16505 16696 17509 539 -995 -279 C
ATOM 1170 CG GLN A 157 -31.097 22.693 15.735 1.00134.74 C
ANISOU 1170 CG GLN A 157 16705 16843 17645 501 -977 -218 C
ATOM 1171 CD GLN A 157 -30.200 21.540 16.121 1.00137.10 C
ANISOU 1171 CD GLN A 157 17036 17168 17886 497 -912 -218 C
ATOM 1172 OE1 GLN A 157 -29.960 21.287 17.301 1.00137.97 O
ANISOU 1172 OE1 GLN A 157 17137 17293 17990 528 -892 -261 O
ATOM 1173 NE2 GLN A 157 -29.698 20.829 15.122 1.00140.16 N
ANISOU 1173 NE2 GLN A 157 17463 17561 18231 459 -879 -172 N
ATOM 1174 N GLY A 158 -33.830 25.604 18.576 1.00127.34 N
ANISOU 1174 N GLY A 158 15609 15882 16891 632 -1116 -398 N
ATOM 1175 CA GLY A 158 -35.072 25.960 19.256 1.00124.65 C
ANISOU 1175 CA GLY A 158 15228 15555 16578 661 -1136 -454 C
ATOM 1176 C GLY A 158 -35.693 24.851 20.079 1.00124.66 C
ANISOU 1176 C GLY A 158 15234 15614 16516 670 -1080 -495 C
ATOM 1177 O GLY A 158 -36.908 24.661 20.037 1.00126.94 O
ANISOU 1177 O GLY A 158 15506 15925 16800 669 -1082 -513 O
ATOM 1178 N CYS A 159 -34.872 24.119 20.824 1.00121.13 N
ANISOU 1178 N CYS A 159 14809 15192 16023 676 -1033 -507 N
ATOM 1179 CA CYS A 159 -35.387 23.109 21.741 1.00121.89 C
ANISOU 1179 CA CYS A 159 14908 15343 16061 684 -983 -547 C
ATOM 1180 C CYS A 159 -35.993 23.766 22.970 1.00118.98 C
ANISOU 1180 C CYS A 159 14493 14987 15728 727 -1002 -621 C
ATOM 1181 O CYS A 159 -35.519 24.811 23.433 1.00126.92 O
ANISOU 1181 O CYS A 159 15474 15960 16791 755 -1039 -645 O
ATOM 1182 CB CYS A 159 -34.286 22.131 22.152 1.00119.55 C
ANISOU 1182 CB CYS A 159 14650 15066 15707 675 -931 -536 C
ATOM 1183 SG CYS A 159 -33.404 21.341 20.783 1.00116.63 S
ANISOU 1183 SG CYS A 159 14334 14683 15296 627 -903 -456 S
ATOM 1184 N GLY A 160 -37.042 23.145 23.498 1.00119.64 N
ANISOU 1184 N GLY A 160 14564 15117 15776 732 -974 -656 N
ATOM 1185 CA GLY A 160 -37.692 23.626 24.704 1.00124.98 C
ANISOU 1185 CA GLY A 160 15196 15815 16475 770 -983 -730 C
ATOM 1186 C GLY A 160 -36.816 23.489 25.931 1.00131.32 C
ANISOU 1186 C GLY A 160 16003 16635 17258 791 -959 -766 C
ATOM 1187 O GLY A 160 -35.700 22.959 25.879 1.00131.02 O
ANISOU 1187 O GLY A 160 16002 16591 17187 777 -935 -733 O
ATOM 1188 N GLU A 161 -37.327 23.977 27.051 1.00136.46 N
ANISOU 1188 N GLU A 161 16615 17306 17929 826 -967 -835 N
ATOM 1189 CA GLU A 161 -36.630 23.838 28.326 1.00142.16 C
ANISOU 1189 CA GLU A 161 17338 18048 18626 845 -945 -876 C
ATOM 1190 C GLU A 161 -36.517 22.368 28.713 1.00140.45 C
ANISOU 1190 C GLU A 161 17157 17887 18322 821 -883 -864 C
ATOM 1191 O GLU A 161 -37.493 21.622 28.627 1.00140.46 O
ANISOU 1191 O GLU A 161 17157 17929 18282 806 -856 -867 O
ATOM 1192 CB GLU A 161 -37.331 24.632 29.421 1.00149.07 C
ANISOU 1192 CB GLU A 161 18163 18940 19537 885 -964 -957 C
ATOM 1193 CG GLU A 161 -37.043 26.127 29.375 1.00156.31 C
ANISOU 1193 CG GLU A 161 19048 19799 20544 915 -1027 -977 C
ATOM 1194 CD GLU A 161 -37.477 26.859 30.634 1.00163.01 C
ANISOU 1194 CD GLU A 161 19852 20664 21422 956 -1041 -1064 C
ATOM 1195 OE1 GLU A 161 -38.643 26.699 31.061 1.00169.65 O
ANISOU 1195 OE1 GLU A 161 20662 21546 22250 966 -1026 -1110 O
ATOM 1196 OE2 GLU A 161 -36.651 27.614 31.193 1.00169.70 O
ANISOU 1196 OE2 GLU A 161 20692 21481 22304 979 -1066 -1087 O
ATOM 1197 N GLY A 162 -35.313 21.957 29.104 1.00136.93 N
ANISOU 1197 N GLY A 162 16742 17438 17849 816 -863 -848 N
ATOM 1198 CA GLY A 162 -35.040 20.562 29.407 1.00132.38 C
ANISOU 1198 CA GLY A 162 16201 16903 17193 791 -808 -830 C
ATOM 1199 C GLY A 162 -34.677 19.706 28.208 1.00127.25 C
ANISOU 1199 C GLY A 162 15595 16242 16514 754 -787 -759 C
ATOM 1200 O GLY A 162 -34.188 18.591 28.388 1.00128.64 O
ANISOU 1200 O GLY A 162 15804 16442 16632 734 -745 -738 O
ATOM 1201 N GLN A 163 -34.907 20.205 26.996 1.00119.84 N
ANISOU 1201 N GLN A 163 14655 15266 15611 743 -815 -723 N
ATOM 1202 CA GLN A 163 -34.543 19.479 25.780 1.00114.02 C
ANISOU 1202 CA GLN A 163 13959 14516 14847 707 -797 -657 C
ATOM 1203 C GLN A 163 -33.158 19.890 25.301 1.00112.23 C
ANISOU 1203 C GLN A 163 13752 14241 14648 703 -811 -618 C
ATOM 1204 O GLN A 163 -32.742 21.039 25.471 1.00112.05 O
ANISOU 1204 O GLN A 163 13707 14182 14685 726 -853 -631 O
ATOM 1205 CB GLN A 163 -35.564 19.721 24.675 1.00107.16 C
ANISOU 1205 CB GLN A 163 13082 13638 13998 691 -819 -634 C
ATOM 1206 CG GLN A 163 -36.952 19.202 24.992 1.00103.29 C
ANISOU 1206 CG GLN A 163 12574 13195 13477 689 -802 -664 C
ATOM 1207 CD GLN A 163 -37.879 19.284 23.801 1.00105.32 C
ANISOU 1207 CD GLN A 163 12830 13441 13747 668 -821 -632 C
ATOM 1208 OE1 GLN A 163 -37.969 20.316 23.131 1.00106.15 O
ANISOU 1208 OE1 GLN A 163 12917 13503 13912 673 -869 -620 O
ATOM 1209 NE2 GLN A 163 -38.582 18.194 23.532 1.00104.32 N
ANISOU 1209 NE2 GLN A 163 12721 13351 13564 642 -787 -618 N
ATOM 1210 N VAL A 164 -32.456 18.944 24.691 1.00107.71 N
ANISOU 1210 N VAL A 164 13222 13669 14034 674 -777 -570 N
ATOM 1211 CA VAL A 164 -31.109 19.171 24.183 1.00105.37 C
ANISOU 1211 CA VAL A 164 12946 13332 13756 666 -782 -529 C
ATOM 1212 C VAL A 164 -31.011 18.650 22.761 1.00107.84 C
ANISOU 1212 C VAL A 164 13292 13633 14048 628 -768 -470 C
ATOM 1213 O VAL A 164 -31.776 17.768 22.347 1.00109.20 O
ANISOU 1213 O VAL A 164 13480 13834 14176 606 -741 -459 O
ATOM 1214 CB VAL A 164 -30.031 18.497 25.068 1.00100.98 C
ANISOU 1214 CB VAL A 164 12409 12787 13170 671 -748 -536 C
ATOM 1215 CG1 VAL A 164 -29.893 19.222 26.397 1.00 98.72 C
ANISOU 1215 CG1 VAL A 164 12093 12505 12913 707 -770 -590 C
ATOM 1216 CG2 VAL A 164 -30.346 17.022 25.281 1.00 95.37 C
ANISOU 1216 CG2 VAL A 164 11725 12122 12387 651 -696 -532 C
ATOM 1217 N ALA A 165 -30.066 19.207 22.012 1.00107.77 N
ANISOU 1217 N ALA A 165 13293 13583 14073 619 -787 -431 N
ATOM 1218 CA ALA A 165 -29.749 18.711 20.676 1.00107.02 C
ANISOU 1218 CA ALA A 165 13231 13476 13955 581 -770 -374 C
ATOM 1219 C ALA A 165 -29.141 17.318 20.808 1.00106.23 C
ANISOU 1219 C ALA A 165 13168 13401 13793 565 -711 -361 C
ATOM 1220 O ALA A 165 -28.033 17.166 21.329 1.00114.31 O
ANISOU 1220 O ALA A 165 14199 14416 14818 574 -697 -360 O
ATOM 1221 CB ALA A 165 -28.793 19.657 19.964 1.00103.49 C
ANISOU 1221 CB ALA A 165 12783 12982 13556 576 -802 -337 C
ATOM 1222 N CYS A 166 -29.875 16.304 20.357 1.00100.92 N
ANISOU 1222 N CYS A 166 12517 12758 13069 541 -680 -350 N
ATOM 1223 CA CYS A 166 -29.492 14.922 20.593 1.00 96.08 C
ANISOU 1223 CA CYS A 166 11936 12171 12398 527 -627 -345 C
ATOM 1224 C CYS A 166 -28.302 14.516 19.735 1.00 91.47 C
ANISOU 1224 C CYS A 166 11385 11565 11805 505 -603 -300 C
ATOM 1225 O CYS A 166 -28.418 14.417 18.521 1.00 88.74 O
ANISOU 1225 O CYS A 166 11058 11210 11450 476 -601 -263 O
ATOM 1226 CB CYS A 166 -30.679 13.993 20.346 1.00 94.74 C
ANISOU 1226 CB CYS A 166 11779 12038 12179 508 -605 -347 C
ATOM 1227 SG CYS A 166 -30.351 12.283 20.805 1.00 92.80 S
ANISOU 1227 SG CYS A 166 11568 11825 11865 494 -545 -347 S
ATOM 1228 N LEU A 167 -27.155 14.322 20.382 1.00 90.76 N
ANISOU 1228 N LEU A 167 11300 11467 11720 517 -587 -303 N
ATOM 1229 CA LEU A 167 -25.943 13.836 19.727 1.00 91.12 C
ANISOU 1229 CA LEU A 167 11373 11493 11756 499 -559 -266 C
ATOM 1230 C LEU A 167 -25.210 12.909 20.673 1.00 92.61 C
ANISOU 1230 C LEU A 167 11573 11695 11921 509 -524 -280 C
ATOM 1231 O LEU A 167 -25.205 13.129 21.887 1.00 93.18 O
ANISOU 1231 O LEU A 167 11625 11776 12004 535 -535 -314 O
ATOM 1232 CB LEU A 167 -25.030 14.989 19.297 1.00 86.08 C
ANISOU 1232 CB LEU A 167 10722 10814 11172 504 -591 -243 C
ATOM 1233 CG LEU A 167 -25.535 15.973 18.239 1.00 80.70 C
ANISOU 1233 CG LEU A 167 10031 10113 10521 490 -630 -220 C
ATOM 1234 CD1 LEU A 167 -24.560 17.120 18.075 1.00 80.97 C
ANISOU 1234 CD1 LEU A 167 10048 10107 10611 498 -664 -202 C
ATOM 1235 CD2 LEU A 167 -25.780 15.278 16.906 1.00 77.02 C
ANISOU 1235 CD2 LEU A 167 9596 9653 10014 449 -604 -182 C
ATOM 1236 N PHE A 168 -24.589 11.873 20.113 1.00 90.44 N
ANISOU 1236 N PHE A 168 11329 11419 11613 487 -483 -253 N
ATOM 1237 CA PHE A 168 -23.952 10.840 20.926 1.00 89.25 C
ANISOU 1237 CA PHE A 168 11191 11280 11438 492 -449 -263 C
ATOM 1238 C PHE A 168 -22.866 11.424 21.828 1.00 89.12 C
ANISOU 1238 C PHE A 168 11157 11243 11462 518 -464 -273 C
ATOM 1239 O PHE A 168 -22.939 11.306 23.054 1.00 86.46 O
ANISOU 1239 O PHE A 168 10808 10922 11122 537 -468 -304 O
ATOM 1240 CB PHE A 168 -23.385 9.730 20.043 1.00 90.16 C
ANISOU 1240 CB PHE A 168 11342 11394 11522 464 -404 -232 C
ATOM 1241 CG PHE A 168 -22.862 8.556 20.808 1.00 91.41 C
ANISOU 1241 CG PHE A 168 11514 11563 11654 467 -371 -241 C
ATOM 1242 CD1 PHE A 168 -23.717 7.526 21.191 1.00 91.88 C
ANISOU 1242 CD1 PHE A 168 11587 11655 11669 459 -352 -256 C
ATOM 1243 CD2 PHE A 168 -21.510 8.473 21.147 1.00 92.96 C
ANISOU 1243 CD2 PHE A 168 11711 11736 11875 477 -360 -232 C
ATOM 1244 CE1 PHE A 168 -23.236 6.435 21.900 1.00 92.76 C
ANISOU 1244 CE1 PHE A 168 11711 11776 11759 459 -325 -261 C
ATOM 1245 CE2 PHE A 168 -21.025 7.386 21.859 1.00 93.51 C
ANISOU 1245 CE2 PHE A 168 11792 11813 11923 478 -333 -238 C
ATOM 1246 CZ PHE A 168 -21.890 6.366 22.233 1.00 93.35 C
ANISOU 1246 CZ PHE A 168 11786 11825 11859 469 -316 -252 C
ATOM 1247 N GLU A 169 -21.888 12.093 21.229 1.00 89.29 N
ANISOU 1247 N GLU A 169 11176 11231 11520 516 -474 -247 N
ATOM 1248 CA GLU A 169 -20.793 12.667 22.002 1.00 91.82 C
ANISOU 1248 CA GLU A 169 11479 11527 11881 539 -490 -252 C
ATOM 1249 C GLU A 169 -21.249 13.748 22.978 1.00 93.47 C
ANISOU 1249 C GLU A 169 11656 11736 12122 568 -536 -288 C
ATOM 1250 O GLU A 169 -20.496 14.106 23.879 1.00 94.30 O
ANISOU 1250 O GLU A 169 11747 11829 12254 588 -549 -301 O
ATOM 1251 CB GLU A 169 -19.711 13.218 21.082 1.00 95.22 C
ANISOU 1251 CB GLU A 169 11911 11922 12345 529 -494 -214 C
ATOM 1252 CG GLU A 169 -19.041 12.171 20.210 1.00 98.96 C
ANISOU 1252 CG GLU A 169 12415 12395 12792 503 -446 -183 C
ATOM 1253 CD GLU A 169 -17.726 12.654 19.630 1.00104.90 C
ANISOU 1253 CD GLU A 169 13164 13114 13580 498 -446 -151 C
ATOM 1254 OE1 GLU A 169 -17.300 13.779 19.973 1.00108.63 O
ANISOU 1254 OE1 GLU A 169 13612 13563 14099 515 -484 -152 O
ATOM 1255 OE2 GLU A 169 -17.118 11.910 18.832 1.00108.40 O
ANISOU 1255 OE2 GLU A 169 13629 13555 14005 477 -407 -127 O
ATOM 1256 N ASP A 170 -22.470 14.257 22.813 1.00 94.44 N
ANISOU 1256 N ASP A 170 11766 11873 12245 569 -559 -304 N
ATOM 1257 CA ASP A 170 -22.965 15.319 23.689 1.00 97.66 C
ANISOU 1257 CA ASP A 170 12140 12280 12687 598 -602 -342 C
ATOM 1258 C ASP A 170 -23.510 14.794 25.016 1.00 97.91 C
ANISOU 1258 C ASP A 170 12165 12348 12689 613 -592 -386 C
ATOM 1259 O ASP A 170 -23.451 15.496 26.023 1.00 99.18 O
ANISOU 1259 O ASP A 170 12301 12507 12875 639 -619 -420 O
ATOM 1260 CB ASP A 170 -24.032 16.156 22.979 1.00 98.79 C
ANISOU 1260 CB ASP A 170 12268 12419 12850 595 -635 -343 C
ATOM 1261 CG ASP A 170 -23.449 17.125 21.959 1.00 99.12 C
ANISOU 1261 CG ASP A 170 12305 12420 12937 587 -664 -307 C
ATOM 1262 OD1 ASP A 170 -22.211 17.161 21.793 1.00102.96 O
ANISOU 1262 OD1 ASP A 170 12800 12882 13440 583 -657 -281 O
ATOM 1263 OD2 ASP A 170 -24.235 17.856 21.320 1.00 97.48 O
ANISOU 1263 OD2 ASP A 170 12085 12204 12751 582 -696 -302 O
ATOM 1264 N VAL A 171 -24.033 13.575 25.025 1.00 95.70 N
ANISOU 1264 N VAL A 171 11906 12102 12355 596 -555 -386 N
ATOM 1265 CA VAL A 171 -24.695 13.038 26.211 1.00 93.81 C
ANISOU 1265 CA VAL A 171 11660 11903 12082 606 -545 -425 C
ATOM 1266 C VAL A 171 -23.917 11.900 26.875 1.00 91.21 C
ANISOU 1266 C VAL A 171 11352 11584 11721 599 -512 -419 C
ATOM 1267 O VAL A 171 -24.023 11.718 28.084 1.00 91.74 O
ANISOU 1267 O VAL A 171 11408 11675 11773 611 -513 -450 O
ATOM 1268 CB VAL A 171 -26.135 12.591 25.891 1.00 94.66 C
ANISOU 1268 CB VAL A 171 11769 12045 12153 593 -536 -435 C
ATOM 1269 CG1 VAL A 171 -27.037 13.800 25.705 1.00 93.73 C
ANISOU 1269 CG1 VAL A 171 11620 11922 12072 607 -576 -456 C
ATOM 1270 CG2 VAL A 171 -26.161 11.710 24.652 1.00 97.31 C
ANISOU 1270 CG2 VAL A 171 12137 12378 12460 561 -506 -394 C
ATOM 1271 N VAL A 172 -23.150 11.135 26.104 1.00 89.18 N
ANISOU 1271 N VAL A 172 11121 11310 11453 580 -483 -381 N
ATOM 1272 CA VAL A 172 -22.392 10.011 26.641 1.00 88.47 C
ANISOU 1272 CA VAL A 172 11051 11226 11337 572 -452 -372 C
ATOM 1273 C VAL A 172 -20.974 10.496 26.945 1.00 90.91 C
ANISOU 1273 C VAL A 172 11354 11500 11689 586 -464 -361 C
ATOM 1274 O VAL A 172 -20.305 11.013 26.054 1.00 96.19 O
ANISOU 1274 O VAL A 172 12024 12135 12390 583 -469 -334 O
ATOM 1275 CB VAL A 172 -22.365 8.831 25.652 1.00 84.55 C
ANISOU 1275 CB VAL A 172 10587 10732 10808 544 -413 -340 C
ATOM 1276 CG1 VAL A 172 -21.680 7.631 26.275 1.00 83.11 C
ANISOU 1276 CG1 VAL A 172 10421 10555 10601 537 -385 -335 C
ATOM 1277 CG2 VAL A 172 -23.776 8.464 25.225 1.00 82.29 C
ANISOU 1277 CG2 VAL A 172 10305 10477 10483 529 -406 -348 C
ATOM 1278 N PRO A 173 -20.505 10.344 28.197 1.00 87.71 N
ANISOU 1278 N PRO A 173 10941 11101 11282 599 -469 -380 N
ATOM 1279 CA PRO A 173 -19.136 10.768 28.511 1.00 86.23 C
ANISOU 1279 CA PRO A 173 10748 10878 11136 611 -481 -368 C
ATOM 1280 C PRO A 173 -18.105 9.857 27.855 1.00 85.37 C
ANISOU 1280 C PRO A 173 10662 10748 11026 594 -448 -330 C
ATOM 1281 O PRO A 173 -18.297 8.637 27.788 1.00 82.50 O
ANISOU 1281 O PRO A 173 10320 10402 10624 577 -415 -322 O
ATOM 1282 CB PRO A 173 -19.069 10.658 30.035 1.00 85.84 C
ANISOU 1282 CB PRO A 173 10690 10850 11077 624 -493 -400 C
ATOM 1283 CG PRO A 173 -20.489 10.573 30.493 1.00 85.59 C
ANISOU 1283 CG PRO A 173 10651 10863 11008 624 -495 -434 C
ATOM 1284 CD PRO A 173 -21.217 9.875 29.393 1.00 85.53 C
ANISOU 1284 CD PRO A 173 10661 10867 10971 602 -468 -414 C
ATOM 1285 N MET A 174 -17.026 10.453 27.363 1.00 86.57 N
ANISOU 1285 N MET A 174 10809 10861 11222 599 -456 -306 N
ATOM 1286 CA MET A 174 -16.014 9.694 26.643 1.00 88.84 C
ANISOU 1286 CA MET A 174 11114 11126 11514 585 -423 -270 C
ATOM 1287 C MET A 174 -15.197 8.778 27.553 1.00 89.99 C
ANISOU 1287 C MET A 174 11267 11271 11654 586 -408 -269 C
ATOM 1288 O MET A 174 -14.686 7.755 27.098 1.00 90.44 O
ANISOU 1288 O MET A 174 11342 11320 11700 572 -374 -248 O
ATOM 1289 CB MET A 174 -15.104 10.618 25.837 1.00 90.68 C
ANISOU 1289 CB MET A 174 11337 11321 11795 587 -436 -244 C
ATOM 1290 CG MET A 174 -14.792 10.115 24.438 1.00 93.18 C
ANISOU 1290 CG MET A 174 11672 11627 12104 564 -401 -211 C
ATOM 1291 SD MET A 174 -16.154 10.376 23.284 1.00 98.20 S
ANISOU 1291 SD MET A 174 12317 12282 12712 547 -401 -209 S
ATOM 1292 CE MET A 174 -16.869 8.743 23.188 1.00 94.22 C
ANISOU 1292 CE MET A 174 11843 11811 12146 527 -357 -214 C
ATOM 1293 N ASN A 175 -15.076 9.136 28.829 1.00 89.32 N
ANISOU 1293 N ASN A 175 11168 11191 11578 603 -435 -293 N
ATOM 1294 CA ASN A 175 -14.352 8.287 29.781 1.00 87.18 C
ANISOU 1294 CA ASN A 175 10903 10920 11302 602 -427 -291 C
ATOM 1295 C ASN A 175 -15.074 6.957 29.985 1.00 83.93 C
ANISOU 1295 C ASN A 175 10511 10542 10837 584 -399 -296 C
ATOM 1296 O ASN A 175 -14.436 5.908 30.075 1.00 83.96 O
ANISOU 1296 O ASN A 175 10529 10537 10835 574 -376 -278 O
ATOM 1297 CB ASN A 175 -14.151 9.000 31.114 1.00 90.09 C
ANISOU 1297 CB ASN A 175 11252 11291 11686 621 -464 -316 C
ATOM 1298 CG ASN A 175 -15.319 9.895 31.478 1.00 94.39 C
ANISOU 1298 CG ASN A 175 11782 11862 12219 632 -490 -353 C
ATOM 1299 OD1 ASN A 175 -16.424 9.423 31.735 1.00 95.83 O
ANISOU 1299 OD1 ASN A 175 11969 12083 12358 624 -481 -373 O
ATOM 1300 ND2 ASN A 175 -15.078 11.200 31.497 1.00 98.82 N
ANISOU 1300 ND2 ASN A 175 12322 12402 12823 650 -524 -362 N
ATOM 1301 N TYR A 176 -16.404 7.002 30.042 1.00 81.20 N
ANISOU 1301 N TYR A 176 10165 10231 10454 581 -401 -319 N
ATOM 1302 CA TYR A 176 -17.190 5.773 30.065 1.00 80.26 C
ANISOU 1302 CA TYR A 176 10065 10144 10284 561 -375 -320 C
ATOM 1303 C TYR A 176 -16.921 4.936 28.814 1.00 79.58 C
ANISOU 1303 C TYR A 176 10002 10042 10193 543 -339 -290 C
ATOM 1304 O TYR A 176 -16.780 3.718 28.891 1.00 79.16 O
ANISOU 1304 O TYR A 176 9966 9993 10116 529 -315 -279 O
ATOM 1305 CB TYR A 176 -18.682 6.084 30.190 1.00 81.28 C
ANISOU 1305 CB TYR A 176 10188 10314 10381 560 -384 -348 C
ATOM 1306 CG TYR A 176 -19.572 4.886 29.962 1.00 83.22 C
ANISOU 1306 CG TYR A 176 10454 10591 10575 538 -357 -346 C
ATOM 1307 CD1 TYR A 176 -19.832 3.981 30.994 1.00 82.67 C
ANISOU 1307 CD1 TYR A 176 10391 10551 10470 528 -352 -355 C
ATOM 1308 CD2 TYR A 176 -20.152 4.647 28.709 1.00 83.18 C
ANISOU 1308 CD2 TYR A 176 10462 10585 10556 524 -338 -331 C
ATOM 1309 CE1 TYR A 176 -20.643 2.877 30.791 1.00 82.12 C
ANISOU 1309 CE1 TYR A 176 10338 10508 10354 506 -330 -350 C
ATOM 1310 CE2 TYR A 176 -20.964 3.543 28.496 1.00 83.52 C
ANISOU 1310 CE2 TYR A 176 10524 10654 10553 503 -315 -328 C
ATOM 1311 CZ TYR A 176 -21.204 2.662 29.540 1.00 84.16 C
ANISOU 1311 CZ TYR A 176 10611 10764 10603 495 -311 -338 C
ATOM 1312 OH TYR A 176 -22.007 1.570 29.337 1.00 87.70 O
ANISOU 1312 OH TYR A 176 11077 11238 11007 473 -291 -333 O
ATOM 1313 N MET A 177 -16.830 5.597 27.668 1.00 80.00 N
ANISOU 1313 N MET A 177 10053 10075 10267 543 -337 -276 N
ATOM 1314 CA MET A 177 -16.683 4.887 26.409 1.00 80.94 C
ANISOU 1314 CA MET A 177 10194 10183 10377 525 -303 -252 C
ATOM 1315 C MET A 177 -15.282 4.332 26.189 1.00 81.95 C
ANISOU 1315 C MET A 177 10328 10276 10531 523 -282 -228 C
ATOM 1316 O MET A 177 -15.117 3.380 25.433 1.00 83.08 O
ANISOU 1316 O MET A 177 10491 10414 10660 507 -248 -212 O
ATOM 1317 CB MET A 177 -17.067 5.796 25.254 1.00 82.82 C
ANISOU 1317 CB MET A 177 10429 10414 10626 522 -309 -243 C
ATOM 1318 CG MET A 177 -18.529 6.183 25.280 1.00 86.68 C
ANISOU 1318 CG MET A 177 10913 10935 11088 520 -325 -265 C
ATOM 1319 SD MET A 177 -19.596 4.775 24.933 1.00 90.65 S
ANISOU 1319 SD MET A 177 11443 11471 11530 495 -293 -265 S
ATOM 1320 CE MET A 177 -18.780 4.095 23.491 1.00 90.61 C
ANISOU 1320 CE MET A 177 11464 11438 11528 475 -255 -231 C
ATOM 1321 N VAL A 178 -14.281 4.912 26.846 1.00 81.55 N
ANISOU 1321 N VAL A 178 10261 10203 10522 540 -302 -225 N
ATOM 1322 CA VAL A 178 -12.900 4.472 26.668 1.00 81.05 C
ANISOU 1322 CA VAL A 178 10199 10106 10492 540 -284 -202 C
ATOM 1323 C VAL A 178 -12.519 3.491 27.773 1.00 80.81 C
ANISOU 1323 C VAL A 178 10173 10078 10455 540 -282 -206 C
ATOM 1324 O VAL A 178 -12.142 2.349 27.498 1.00 80.84 O
ANISOU 1324 O VAL A 178 10191 10073 10451 529 -253 -193 O
ATOM 1325 CB VAL A 178 -11.930 5.671 26.630 1.00 79.36 C
ANISOU 1325 CB VAL A 178 9962 9860 10330 556 -307 -192 C
ATOM 1326 CG1 VAL A 178 -10.490 5.191 26.660 1.00 78.45 C
ANISOU 1326 CG1 VAL A 178 9844 9712 10251 558 -291 -171 C
ATOM 1327 CG2 VAL A 178 -12.180 6.518 25.392 1.00 78.10 C
ANISOU 1327 CG2 VAL A 178 9800 9694 10179 551 -306 -181 C
ATOM 1328 N TYR A 179 -12.615 3.937 29.024 1.00 78.29 N
ANISOU 1328 N TYR A 179 9840 9770 10138 552 -315 -223 N
ATOM 1329 CA TYR A 179 -12.207 3.111 30.156 1.00 76.17 C
ANISOU 1329 CA TYR A 179 9574 9504 9865 551 -320 -224 C
ATOM 1330 C TYR A 179 -13.220 2.012 30.452 1.00 76.31 C
ANISOU 1330 C TYR A 179 9610 9557 9828 533 -306 -234 C
ATOM 1331 O TYR A 179 -12.877 0.826 30.470 1.00 76.22 O
ANISOU 1331 O TYR A 179 9612 9537 9809 521 -286 -220 O
ATOM 1332 CB TYR A 179 -11.979 3.976 31.394 1.00 75.03 C
ANISOU 1332 CB TYR A 179 9409 9361 9736 566 -360 -240 C
ATOM 1333 CG TYR A 179 -10.894 5.008 31.236 1.00 75.17 C
ANISOU 1333 CG TYR A 179 9409 9342 9810 583 -377 -229 C
ATOM 1334 CD1 TYR A 179 -9.659 4.673 30.684 1.00 74.68 C
ANISOU 1334 CD1 TYR A 179 9347 9242 9787 582 -359 -200 C
ATOM 1335 CD2 TYR A 179 -11.098 6.324 31.652 1.00 75.81 C
ANISOU 1335 CD2 TYR A 179 9471 9425 9907 599 -413 -247 C
ATOM 1336 CE1 TYR A 179 -8.659 5.619 30.543 1.00 75.28 C
ANISOU 1336 CE1 TYR A 179 9405 9285 9915 596 -376 -188 C
ATOM 1337 CE2 TYR A 179 -10.107 7.279 31.517 1.00 76.24 C
ANISOU 1337 CE2 TYR A 179 9509 9444 10013 614 -432 -235 C
ATOM 1338 CZ TYR A 179 -8.892 6.921 30.962 1.00 76.09 C
ANISOU 1338 CZ TYR A 179 9490 9389 10031 611 -413 -204 C
ATOM 1339 OH TYR A 179 -7.914 7.869 30.828 1.00 79.21 O
ANISOU 1339 OH TYR A 179 9868 9751 10479 623 -433 -190 O
ATOM 1340 N PHE A 180 -14.472 2.400 30.678 1.00 77.29 N
ANISOU 1340 N PHE A 180 9732 9718 9917 532 -318 -257 N
ATOM 1341 CA PHE A 180 -15.484 1.441 31.113 1.00 79.03 C
ANISOU 1341 CA PHE A 180 9966 9977 10086 515 -309 -267 C
ATOM 1342 C PHE A 180 -15.933 0.529 29.972 1.00 77.56 C
ANISOU 1342 C PHE A 180 9803 9792 9876 497 -275 -254 C
ATOM 1343 O PHE A 180 -15.946 -0.692 30.116 1.00 76.54 O
ANISOU 1343 O PHE A 180 9689 9666 9726 481 -259 -244 O
ATOM 1344 CB PHE A 180 -16.682 2.170 31.727 1.00 81.89 C
ANISOU 1344 CB PHE A 180 10316 10381 10418 520 -331 -298 C
ATOM 1345 CG PHE A 180 -17.585 1.288 32.532 1.00 82.96 C
ANISOU 1345 CG PHE A 180 10460 10559 10503 503 -329 -310 C
ATOM 1346 CD1 PHE A 180 -18.535 0.476 31.909 1.00 83.88 C
ANISOU 1346 CD1 PHE A 180 10592 10697 10580 484 -307 -306 C
ATOM 1347 CD2 PHE A 180 -17.496 1.276 33.922 1.00 82.57 C
ANISOU 1347 CD2 PHE A 180 10401 10529 10442 503 -351 -324 C
ATOM 1348 CE1 PHE A 180 -19.372 -0.336 32.657 1.00 83.34 C
ANISOU 1348 CE1 PHE A 180 10531 10670 10465 467 -306 -315 C
ATOM 1349 CE2 PHE A 180 -18.333 0.466 34.676 1.00 83.05 C
ANISOU 1349 CE2 PHE A 180 10469 10633 10453 485 -350 -333 C
ATOM 1350 CZ PHE A 180 -19.272 -0.343 34.043 1.00 83.37 C
ANISOU 1350 CZ PHE A 180 10525 10694 10457 466 -327 -327 C
ATOM 1351 N ASN A 181 -16.303 1.114 28.842 1.00 78.45 N
ANISOU 1351 N ASN A 181 9915 9900 9991 498 -266 -252 N
ATOM 1352 CA ASN A 181 -16.868 0.332 27.749 1.00 81.53 C
ANISOU 1352 CA ASN A 181 10328 10296 10355 479 -236 -243 C
ATOM 1353 C ASN A 181 -15.787 -0.381 26.939 1.00 81.88 C
ANISOU 1353 C ASN A 181 10386 10304 10423 473 -206 -219 C
ATOM 1354 O ASN A 181 -15.830 -1.602 26.776 1.00 81.16 O
ANISOU 1354 O ASN A 181 10313 10212 10312 458 -184 -212 O
ATOM 1355 CB ASN A 181 -17.737 1.211 26.845 1.00 85.64 C
ANISOU 1355 CB ASN A 181 10845 10827 10866 479 -239 -249 C
ATOM 1356 CG ASN A 181 -18.572 0.401 25.863 1.00 87.07 C
ANISOU 1356 CG ASN A 181 11051 11023 11010 457 -213 -243 C
ATOM 1357 OD1 ASN A 181 -18.223 0.272 24.687 1.00 87.05 O
ANISOU 1357 OD1 ASN A 181 11060 11000 11015 448 -190 -226 O
ATOM 1358 ND2 ASN A 181 -19.682 -0.151 26.344 1.00 88.07 N
ANISOU 1358 ND2 ASN A 181 11183 11186 11094 446 -215 -255 N
ATOM 1359 N PHE A 182 -14.809 0.371 26.441 1.00 81.77 N
ANISOU 1359 N PHE A 182 10360 10257 10451 485 -206 -208 N
ATOM 1360 CA PHE A 182 -13.825 -0.195 25.524 1.00 80.21 C
ANISOU 1360 CA PHE A 182 10173 10028 10277 480 -174 -188 C
ATOM 1361 C PHE A 182 -12.816 -1.098 26.237 1.00 76.52 C
ANISOU 1361 C PHE A 182 9705 9538 9832 482 -169 -180 C
ATOM 1362 O PHE A 182 -12.681 -2.273 25.900 1.00 74.50 O
ANISOU 1362 O PHE A 182 9466 9274 9566 470 -142 -173 O
ATOM 1363 CB PHE A 182 -13.116 0.923 24.752 1.00 80.69 C
ANISOU 1363 CB PHE A 182 10219 10064 10375 489 -176 -177 C
ATOM 1364 CG PHE A 182 -12.133 0.431 23.742 1.00 80.49 C
ANISOU 1364 CG PHE A 182 10202 10010 10372 482 -140 -159 C
ATOM 1365 CD1 PHE A 182 -12.468 -0.585 22.849 1.00 79.65 C
ANISOU 1365 CD1 PHE A 182 10119 9908 10235 463 -105 -156 C
ATOM 1366 CD2 PHE A 182 -10.869 0.991 23.673 1.00 81.40 C
ANISOU 1366 CD2 PHE A 182 10298 10093 10536 494 -142 -145 C
ATOM 1367 CE1 PHE A 182 -11.559 -1.032 21.911 1.00 80.09 C
ANISOU 1367 CE1 PHE A 182 10181 9939 10311 457 -69 -144 C
ATOM 1368 CE2 PHE A 182 -9.953 0.558 22.729 1.00 82.66 C
ANISOU 1368 CE2 PHE A 182 10462 10228 10716 488 -106 -130 C
ATOM 1369 CZ PHE A 182 -10.297 -0.459 21.845 1.00 82.60 C
ANISOU 1369 CZ PHE A 182 10479 10228 10679 470 -69 -131 C
ATOM 1370 N PHE A 183 -12.114 -0.552 27.220 1.00 74.90 N
ANISOU 1370 N PHE A 183 9480 9320 9658 498 -196 -180 N
ATOM 1371 CA PHE A 183 -11.048 -1.301 27.879 1.00 72.60 C
ANISOU 1371 CA PHE A 183 9186 9004 9396 501 -195 -169 C
ATOM 1372 C PHE A 183 -11.598 -2.487 28.665 1.00 67.99 C
ANISOU 1372 C PHE A 183 8616 8439 8779 487 -197 -173 C
ATOM 1373 O PHE A 183 -11.247 -3.639 28.402 1.00 70.27 O
ANISOU 1373 O PHE A 183 8918 8712 9070 477 -175 -163 O
ATOM 1374 CB PHE A 183 -10.223 -0.378 28.784 1.00 72.28 C
ANISOU 1374 CB PHE A 183 9120 8946 9395 519 -228 -167 C
ATOM 1375 CG PHE A 183 -9.296 0.542 28.045 1.00 71.50 C
ANISOU 1375 CG PHE A 183 9007 8818 9342 531 -224 -155 C
ATOM 1376 CD1 PHE A 183 -9.063 0.388 26.684 1.00 71.60 C
ANISOU 1376 CD1 PHE A 183 9026 8816 9360 524 -189 -144 C
ATOM 1377 CD2 PHE A 183 -8.632 1.558 28.721 1.00 70.91 C
ANISOU 1377 CD2 PHE A 183 8910 8729 9305 548 -256 -153 C
ATOM 1378 CE1 PHE A 183 -8.204 1.234 26.002 1.00 70.93 C
ANISOU 1378 CE1 PHE A 183 8928 8708 9317 532 -185 -130 C
ATOM 1379 CE2 PHE A 183 -7.765 2.411 28.047 1.00 71.02 C
ANISOU 1379 CE2 PHE A 183 8909 8714 9362 557 -254 -139 C
ATOM 1380 CZ PHE A 183 -7.553 2.253 26.683 1.00 70.16 C
ANISOU 1380 CZ PHE A 183 8806 8594 9257 549 -218 -126 C
ATOM 1381 N ALA A 184 -12.486 -2.209 29.612 1.00 64.31 N
ANISOU 1381 N ALA A 184 8147 8009 8281 486 -223 -188 N
ATOM 1382 CA ALA A 184 -12.935 -3.245 30.540 1.00 61.09 C
ANISOU 1382 CA ALA A 184 7749 7621 7841 471 -231 -190 C
ATOM 1383 C ALA A 184 -13.928 -4.206 29.891 1.00 69.41 C
ANISOU 1383 C ALA A 184 8826 8695 8851 451 -207 -191 C
ATOM 1384 O ALA A 184 -13.762 -5.422 29.961 1.00 70.03 O
ANISOU 1384 O ALA A 184 8918 8764 8925 438 -196 -181 O
ATOM 1385 CB ALA A 184 -13.527 -2.615 31.792 1.00 64.16 C
ANISOU 1385 CB ALA A 184 8126 8045 8208 474 -266 -208 C
ATOM 1386 N CYS A 185 -14.957 -3.660 29.247 1.00 72.44 N
ANISOU 1386 N CYS A 185 9213 9105 9206 449 -202 -204 N
ATOM 1387 CA CYS A 185 -16.076 -4.470 28.775 1.00 75.90 C
ANISOU 1387 CA CYS A 185 9672 9569 9597 429 -186 -207 C
ATOM 1388 C CYS A 185 -15.883 -5.059 27.380 1.00 76.49 C
ANISOU 1388 C CYS A 185 9765 9620 9676 420 -150 -196 C
ATOM 1389 O CYS A 185 -16.532 -6.044 27.049 1.00 76.94 O
ANISOU 1389 O CYS A 185 9843 9690 9702 402 -135 -195 O
ATOM 1390 CB CYS A 185 -17.369 -3.660 28.818 1.00 78.05 C
ANISOU 1390 CB CYS A 185 9938 9883 9835 429 -199 -226 C
ATOM 1391 SG CYS A 185 -17.911 -3.237 30.486 1.00 82.98 S
ANISOU 1391 SG CYS A 185 10544 10546 10438 433 -235 -245 S
ATOM 1392 N VAL A 186 -15.017 -4.461 26.565 1.00 76.72 N
ANISOU 1392 N VAL A 186 9788 9619 9742 432 -137 -190 N
ATOM 1393 CA VAL A 186 -14.823 -4.898 25.183 1.00 78.93 C
ANISOU 1393 CA VAL A 186 10085 9881 10023 423 -102 -182 C
ATOM 1394 C VAL A 186 -13.444 -5.525 24.974 1.00 80.59 C
ANISOU 1394 C VAL A 186 10295 10049 10278 428 -82 -170 C
ATOM 1395 O VAL A 186 -13.345 -6.671 24.516 1.00 81.82 O
ANISOU 1395 O VAL A 186 10468 10193 10428 416 -57 -167 O
ATOM 1396 CB VAL A 186 -15.075 -3.743 24.185 1.00 80.72 C
ANISOU 1396 CB VAL A 186 10307 10112 10252 426 -98 -183 C
ATOM 1397 CG1 VAL A 186 -14.599 -4.122 22.793 1.00 81.13 C
ANISOU 1397 CG1 VAL A 186 10374 10142 10310 417 -60 -174 C
ATOM 1398 CG2 VAL A 186 -16.549 -3.390 24.149 1.00 82.81 C
ANISOU 1398 CG2 VAL A 186 10577 10416 10472 417 -111 -195 C
ATOM 1399 N ALEU A 187 -12.389 -4.789 25.314 0.50 80.91 N
ANISOU 1399 N ALEU A 187 10313 10066 10364 446 -93 -164 N
ATOM 1400 N BLEU A 187 -12.385 -4.791 25.306 0.50 80.93 N
ANISOU 1400 N BLEU A 187 10316 10069 10367 446 -93 -164 N
ATOM 1401 CA ALEU A 187 -11.028 -5.255 25.063 0.50 80.98 C
ANISOU 1401 CA ALEU A 187 10315 10033 10419 453 -73 -152 C
ATOM 1402 CA BLEU A 187 -11.030 -5.278 25.059 0.50 81.00 C
ANISOU 1402 CA BLEU A 187 10318 10036 10421 452 -73 -152 C
ATOM 1403 C ALEU A 187 -10.669 -6.464 25.929 0.50 81.54 C
ANISOU 1403 C ALEU A 187 10390 10091 10500 449 -79 -148 C
ATOM 1404 C BLEU A 187 -10.695 -6.489 25.924 0.50 81.49 C
ANISOU 1404 C BLEU A 187 10385 10085 10492 448 -79 -148 C
ATOM 1405 O ALEU A 187 -10.089 -7.432 25.430 0.50 82.43 O
ANISOU 1405 O ALEU A 187 10512 10177 10631 445 -53 -143 O
ATOM 1406 O BLEU A 187 -10.148 -7.476 25.424 0.50 82.43 O
ANISOU 1406 O BLEU A 187 10513 10178 10628 444 -53 -144 O
ATOM 1407 CB ALEU A 187 -10.026 -4.121 25.270 0.50 79.89 C
ANISOU 1407 CB ALEU A 187 10152 9875 10329 472 -88 -145 C
ATOM 1408 CB BLEU A 187 -10.002 -4.174 25.279 0.50 80.17 C
ANISOU 1408 CB BLEU A 187 10188 9910 10365 472 -87 -144 C
ATOM 1409 CG ALEU A 187 -8.564 -4.465 25.012 0.50 79.41 C
ANISOU 1409 CG ALEU A 187 10079 9771 10322 480 -69 -132 C
ATOM 1410 CG BLEU A 187 -9.835 -3.168 24.148 0.50 79.90 C
ANISOU 1410 CG BLEU A 187 10147 9871 10340 474 -73 -141 C
ATOM 1411 CD1ALEU A 187 -8.392 -4.939 23.581 0.50 78.79 C
ANISOU 1411 CD1ALEU A 187 10014 9682 10240 470 -23 -132 C
ATOM 1412 CD1BLEU A 187 -8.675 -2.244 24.463 0.50 79.74 C
ANISOU 1412 CD1BLEU A 187 10100 9824 10372 492 -88 -130 C
ATOM 1413 CD2ALEU A 187 -7.680 -3.260 25.288 0.50 79.65 C
ANISOU 1413 CD2ALEU A 187 10083 9784 10396 498 -88 -123 C
ATOM 1414 CD2BLEU A 187 -9.590 -3.884 22.830 0.50 80.74 C
ANISOU 1414 CD2BLEU A 187 10270 9965 10442 462 -28 -138 C
ATOM 1415 N VAL A 188 -11.032 -6.417 27.209 1.00 81.06 N
ANISOU 1415 N VAL A 188 10324 10049 10427 449 -114 -150 N
ATOM 1416 CA VAL A 188 -10.701 -7.501 28.138 1.00 80.96 C
ANISOU 1416 CA VAL A 188 10314 10025 10423 443 -126 -142 C
ATOM 1417 C VAL A 188 -11.348 -8.845 27.741 1.00 85.04 C
ANISOU 1417 C VAL A 188 10856 10547 10910 423 -107 -143 C
ATOM 1418 O VAL A 188 -10.655 -9.851 27.690 1.00 85.83 O
ANISOU 1418 O VAL A 188 10960 10616 11037 420 -97 -134 O
ATOM 1419 CB VAL A 188 -11.007 -7.107 29.587 1.00 76.75 C
ANISOU 1419 CB VAL A 188 9769 9515 9876 443 -168 -144 C
ATOM 1420 CG1 VAL A 188 -11.118 -8.339 30.467 1.00 74.99 C
ANISOU 1420 CG1 VAL A 188 9556 9294 9642 427 -182 -135 C
ATOM 1421 CG2 VAL A 188 -9.939 -6.167 30.116 1.00 78.00 C
ANISOU 1421 CG2 VAL A 188 9904 9652 10082 463 -187 -138 C
ATOM 1422 N PRO A 189 -12.660 -8.869 27.432 1.00 86.70 N
ANISOU 1422 N PRO A 189 11082 10795 11065 409 -104 -153 N
ATOM 1423 CA PRO A 189 -13.225 -10.142 26.965 1.00 87.26 C
ANISOU 1423 CA PRO A 189 11177 10867 11110 390 -86 -153 C
ATOM 1424 C PRO A 189 -12.689 -10.592 25.608 1.00 86.74 C
ANISOU 1424 C PRO A 189 11123 10771 11064 390 -46 -154 C
ATOM 1425 O PRO A 189 -12.608 -11.800 25.366 1.00 88.90 O
ANISOU 1425 O PRO A 189 11412 11027 11339 379 -32 -152 O
ATOM 1426 CB PRO A 189 -14.725 -9.855 26.889 1.00 87.57 C
ANISOU 1426 CB PRO A 189 11227 10954 11090 376 -93 -163 C
ATOM 1427 CG PRO A 189 -14.936 -8.719 27.830 1.00 86.74 C
ANISOU 1427 CG PRO A 189 11101 10874 10980 387 -123 -168 C
ATOM 1428 CD PRO A 189 -13.719 -7.872 27.652 1.00 86.38 C
ANISOU 1428 CD PRO A 189 11037 10796 10987 409 -121 -164 C
ATOM 1429 N LEU A 190 -12.315 -9.654 24.737 1.00 84.72 N
ANISOU 1429 N LEU A 190 10859 10508 10822 401 -28 -157 N
ATOM 1430 CA LEU A 190 -11.746 -10.037 23.442 1.00 80.49 C
ANISOU 1430 CA LEU A 190 10333 9946 10303 400 13 -160 C
ATOM 1431 C LEU A 190 -10.377 -10.684 23.607 1.00 78.80 C
ANISOU 1431 C LEU A 190 10107 9687 10145 410 23 -154 C
ATOM 1432 O LEU A 190 -10.087 -11.697 22.967 1.00 78.47 O
ANISOU 1432 O LEU A 190 10079 9624 10114 404 51 -158 O
ATOM 1433 CB LEU A 190 -11.661 -8.836 22.504 1.00 79.79 C
ANISOU 1433 CB LEU A 190 10237 9863 10214 405 27 -161 C
ATOM 1434 CG LEU A 190 -12.955 -8.438 21.792 1.00 79.43 C
ANISOU 1434 CG LEU A 190 10210 9855 10117 390 30 -168 C
ATOM 1435 CD1 LEU A 190 -12.797 -7.087 21.107 1.00 82.08 C
ANISOU 1435 CD1 LEU A 190 10533 10194 10459 397 33 -165 C
ATOM 1436 CD2 LEU A 190 -13.413 -9.501 20.802 1.00 80.95 C
ANISOU 1436 CD2 LEU A 190 10432 10047 10280 371 62 -175 C
ATOM 1437 N LEU A 191 -9.542 -10.116 24.474 1.00 79.00 N
ANISOU 1437 N LEU A 191 10108 9698 10211 427 0 -144 N
ATOM 1438 CA LEU A 191 -8.251 -10.732 24.773 1.00 78.84 C
ANISOU 1438 CA LEU A 191 10073 9634 10250 437 4 -136 C
ATOM 1439 C LEU A 191 -8.424 -12.099 25.429 1.00 79.20 C
ANISOU 1439 C LEU A 191 10130 9669 10293 426 -8 -133 C
ATOM 1440 O LEU A 191 -7.606 -12.992 25.217 1.00 80.29 O
ANISOU 1440 O LEU A 191 10266 9770 10472 429 7 -132 O
ATOM 1441 CB LEU A 191 -7.407 -9.815 25.655 1.00 76.43 C
ANISOU 1441 CB LEU A 191 9739 9316 9984 454 -24 -125 C
ATOM 1442 CG LEU A 191 -6.943 -8.489 25.045 1.00 73.86 C
ANISOU 1442 CG LEU A 191 9397 8991 9676 467 -14 -124 C
ATOM 1443 CD1 LEU A 191 -6.345 -7.589 26.115 1.00 73.30 C
ANISOU 1443 CD1 LEU A 191 9301 8913 9635 482 -52 -113 C
ATOM 1444 CD2 LEU A 191 -5.974 -8.677 23.885 1.00 73.45 C
ANISOU 1444 CD2 LEU A 191 9340 8908 9660 472 28 -125 C
ATOM 1445 N LEU A 192 -9.492 -12.267 26.204 1.00 80.10 N
ANISOU 1445 N LEU A 192 10256 9817 10362 412 -37 -132 N
ATOM 1446 CA LEU A 192 -9.769 -13.558 26.830 1.00 81.05 C
ANISOU 1446 CA LEU A 192 10388 9931 10476 397 -52 -126 C
ATOM 1447 C LEU A 192 -10.128 -14.619 25.795 1.00 83.66 C
ANISOU 1447 C LEU A 192 10743 10252 10793 385 -20 -136 C
ATOM 1448 O LEU A 192 -9.696 -15.769 25.909 1.00 84.24 O
ANISOU 1448 O LEU A 192 10820 10293 10893 380 -19 -132 O
ATOM 1449 CB LEU A 192 -10.871 -13.424 27.879 1.00 79.18 C
ANISOU 1449 CB LEU A 192 10157 9739 10190 382 -88 -122 C
ATOM 1450 CG LEU A 192 -10.461 -12.801 29.219 1.00 77.08 C
ANISOU 1450 CG LEU A 192 9870 9478 9940 389 -127 -111 C
ATOM 1451 CD1 LEU A 192 -11.690 -12.377 30.008 1.00 77.38 C
ANISOU 1451 CD1 LEU A 192 9912 9570 9919 376 -153 -115 C
ATOM 1452 CD2 LEU A 192 -9.571 -13.716 30.051 1.00 77.41 C
ANISOU 1452 CD2 LEU A 192 9905 9485 10025 387 -148 -94 C
ATOM 1453 N MET A 193 -10.895 -14.235 24.779 1.00 82.98 N
ANISOU 1453 N MET A 193 10672 10190 10666 379 5 -148 N
ATOM 1454 CA MET A 193 -11.233 -15.174 23.707 1.00 85.76 C
ANISOU 1454 CA MET A 193 11049 10534 11003 366 36 -160 C
ATOM 1455 C MET A 193 -9.982 -15.618 22.958 1.00 87.12 C
ANISOU 1455 C MET A 193 11213 10658 11229 379 70 -166 C
ATOM 1456 O MET A 193 -9.862 -16.791 22.591 1.00 90.88 O
ANISOU 1456 O MET A 193 11704 11111 11717 372 84 -174 O
ATOM 1457 CB MET A 193 -12.239 -14.564 22.740 1.00 89.71 C
ANISOU 1457 CB MET A 193 11567 11069 11451 356 55 -170 C
ATOM 1458 CG MET A 193 -13.586 -14.252 23.360 1.00 92.45 C
ANISOU 1458 CG MET A 193 11921 11463 11743 343 26 -167 C
ATOM 1459 SD MET A 193 -14.689 -13.457 22.184 1.00 94.80 S
ANISOU 1459 SD MET A 193 12234 11796 11987 332 45 -177 S
ATOM 1460 CE MET A 193 -15.839 -12.651 23.291 1.00 96.48 C
ANISOU 1460 CE MET A 193 12437 12058 12161 329 4 -173 C
ATOM 1461 N LEU A 194 -9.049 -14.695 22.739 1.00 86.61 N
ANISOU 1461 N LEU A 194 11127 10581 11200 397 81 -165 N
ATOM 1462 CA LEU A 194 -7.800 -15.043 22.069 1.00 86.96 C
ANISOU 1462 CA LEU A 194 11159 10583 11299 410 114 -172 C
ATOM 1463 C LEU A 194 -7.026 -16.092 22.855 1.00 86.89 C
ANISOU 1463 C LEU A 194 11139 10534 11342 416 98 -165 C
ATOM 1464 O LEU A 194 -6.471 -17.024 22.270 1.00 86.35 O
ANISOU 1464 O LEU A 194 11073 10431 11304 418 124 -177 O
ATOM 1465 CB LEU A 194 -6.950 -13.798 21.843 1.00 87.51 C
ANISOU 1465 CB LEU A 194 11204 10649 11398 427 123 -167 C
ATOM 1466 CG LEU A 194 -5.717 -13.979 20.966 1.00 87.01 C
ANISOU 1466 CG LEU A 194 11126 10550 11385 439 165 -176 C
ATOM 1467 CD1 LEU A 194 -6.106 -14.132 19.502 1.00 86.89 C
ANISOU 1467 CD1 LEU A 194 11132 10546 11335 426 210 -195 C
ATOM 1468 CD2 LEU A 194 -4.792 -12.788 21.151 1.00 86.33 C
ANISOU 1468 CD2 LEU A 194 11009 10456 11336 456 160 -164 C
ATOM 1469 N GLY A 195 -7.004 -15.950 24.177 1.00 87.84 N
ANISOU 1469 N GLY A 195 11247 10657 11471 417 54 -147 N
ATOM 1470 CA GLY A 195 -6.353 -16.945 25.027 1.00 89.50 C
ANISOU 1470 CA GLY A 195 11448 10830 11728 418 30 -136 C
ATOM 1471 C GLY A 195 -7.098 -18.271 25.023 1.00 88.95 C
ANISOU 1471 C GLY A 195 11404 10759 11636 399 25 -139 C
ATOM 1472 O GLY A 195 -6.478 -19.337 25.025 1.00 90.08 O
ANISOU 1472 O GLY A 195 11544 10859 11824 401 27 -140 O
ATOM 1473 N VAL A 196 -8.425 -18.210 25.021 1.00 86.88 N
ANISOU 1473 N VAL A 196 11164 10539 11306 381 16 -141 N
ATOM 1474 CA VAL A 196 -9.230 -19.428 25.006 1.00 86.91 C
ANISOU 1474 CA VAL A 196 11193 10545 11283 360 9 -143 C
ATOM 1475 C VAL A 196 -9.004 -20.199 23.706 1.00 90.46 C
ANISOU 1475 C VAL A 196 11657 10966 11746 361 53 -165 C
ATOM 1476 O VAL A 196 -8.776 -21.413 23.725 1.00 92.06 O
ANISOU 1476 O VAL A 196 11866 11135 11976 356 50 -167 O
ATOM 1477 CB VAL A 196 -10.719 -19.111 25.226 1.00 85.36 C
ANISOU 1477 CB VAL A 196 11017 10404 11012 340 -7 -140 C
ATOM 1478 CG1 VAL A 196 -11.582 -20.318 24.914 1.00 83.44 C
ANISOU 1478 CG1 VAL A 196 10802 10164 10739 318 -6 -144 C
ATOM 1479 CG2 VAL A 196 -10.953 -18.688 26.664 1.00 88.14 C
ANISOU 1479 CG2 VAL A 196 11356 10781 11353 335 -53 -120 C
ATOM 1480 N TYR A 197 -9.041 -19.493 22.581 1.00 91.31 N
ANISOU 1480 N TYR A 197 11769 11088 11835 366 92 -181 N
ATOM 1481 CA TYR A 197 -8.839 -20.156 21.299 1.00 93.08 C
ANISOU 1481 CA TYR A 197 12009 11291 12067 366 136 -205 C
ATOM 1482 C TYR A 197 -7.407 -20.666 21.144 1.00 96.26 C
ANISOU 1482 C TYR A 197 12389 11639 12546 385 155 -213 C
ATOM 1483 O TYR A 197 -7.183 -21.669 20.467 1.00 98.04 O
ANISOU 1483 O TYR A 197 12626 11836 12791 384 179 -233 O
ATOM 1484 CB TYR A 197 -9.223 -19.231 20.146 1.00 91.34 C
ANISOU 1484 CB TYR A 197 11799 11102 11806 363 172 -219 C
ATOM 1485 CG TYR A 197 -10.707 -19.177 19.895 1.00 91.49 C
ANISOU 1485 CG TYR A 197 11847 11165 11752 341 164 -219 C
ATOM 1486 CD1 TYR A 197 -11.367 -20.242 19.281 1.00 93.05 C
ANISOU 1486 CD1 TYR A 197 12073 11358 11922 323 176 -232 C
ATOM 1487 CD2 TYR A 197 -11.458 -18.064 20.267 1.00 91.88 C
ANISOU 1487 CD2 TYR A 197 11894 11257 11760 337 144 -207 C
ATOM 1488 CE1 TYR A 197 -12.735 -20.202 19.051 1.00 94.33 C
ANISOU 1488 CE1 TYR A 197 12262 11561 12019 301 168 -231 C
ATOM 1489 CE2 TYR A 197 -12.827 -18.010 20.040 1.00 94.22 C
ANISOU 1489 CE2 TYR A 197 12214 11593 11993 317 136 -208 C
ATOM 1490 CZ TYR A 197 -13.461 -19.084 19.432 1.00 94.14 C
ANISOU 1490 CZ TYR A 197 12232 11579 11956 298 148 -218 C
ATOM 1491 OH TYR A 197 -14.814 -19.045 19.203 1.00 91.16 O
ANISOU 1491 OH TYR A 197 11878 11241 11518 278 139 -217 O
ATOM 1492 N LEU A 198 -6.446 -20.002 21.783 1.00 96.56 N
ANISOU 1492 N LEU A 198 12395 11662 12630 403 142 -200 N
ATOM 1493 CA LEU A 198 -5.068 -20.487 21.747 1.00 98.19 C
ANISOU 1493 CA LEU A 198 12577 11816 12915 422 156 -205 C
ATOM 1494 C LEU A 198 -4.925 -21.822 22.470 1.00100.33 C
ANISOU 1494 C LEU A 198 12849 12050 13222 418 126 -198 C
ATOM 1495 O LEU A 198 -4.207 -22.709 22.008 1.00101.16 O
ANISOU 1495 O LEU A 198 12948 12111 13378 427 147 -215 O
ATOM 1496 CB LEU A 198 -4.110 -19.450 22.323 1.00 97.21 C
ANISOU 1496 CB LEU A 198 12418 11685 12831 441 144 -189 C
ATOM 1497 CG LEU A 198 -3.663 -18.361 21.349 1.00 99.00 C
ANISOU 1497 CG LEU A 198 12634 11925 13055 451 185 -199 C
ATOM 1498 CD1 LEU A 198 -2.995 -17.216 22.100 1.00 99.19 C
ANISOU 1498 CD1 LEU A 198 12629 11951 13108 466 161 -178 C
ATOM 1499 CD2 LEU A 198 -2.751 -18.900 20.253 1.00 97.87 C
ANISOU 1499 CD2 LEU A 198 12484 11749 12955 462 236 -224 C
ATOM 1500 N ARG A 199 -5.621 -21.979 23.590 1.00100.64 N
ANISOU 1500 N ARG A 199 12896 12107 13236 403 77 -175 N
ATOM 1501 CA ARG A 199 -5.605 -23.262 24.289 1.00103.97 C
ANISOU 1501 CA ARG A 199 13321 12496 13686 393 44 -165 C
ATOM 1502 C ARG A 199 -6.414 -24.317 23.540 1.00102.69 C
ANISOU 1502 C ARG A 199 13190 12333 13494 377 59 -183 C
ATOM 1503 O ARG A 199 -6.114 -25.508 23.645 1.00101.04 O
ANISOU 1503 O ARG A 199 12982 12082 13326 375 49 -186 O
ATOM 1504 CB ARG A 199 -6.107 -23.111 25.719 1.00108.28 C
ANISOU 1504 CB ARG A 199 13866 13066 14211 379 -13 -133 C
ATOM 1505 CG ARG A 199 -5.151 -22.367 26.637 1.00115.28 C
ANISOU 1505 CG ARG A 199 14720 13940 15141 393 -38 -112 C
ATOM 1506 CD ARG A 199 -5.699 -22.265 28.050 1.00125.25 C
ANISOU 1506 CD ARG A 199 15984 15229 16376 375 -93 -83 C
ATOM 1507 NE ARG A 199 -5.201 -21.071 28.733 1.00133.54 N
ANISOU 1507 NE ARG A 199 17012 16293 17435 387 -109 -70 N
ATOM 1508 CZ ARG A 199 -5.594 -20.661 29.937 1.00141.06 C
ANISOU 1508 CZ ARG A 199 17962 17276 18360 374 -153 -49 C
ATOM 1509 NH1 ARG A 199 -6.500 -21.341 30.633 1.00144.92 N
ANISOU 1509 NH1 ARG A 199 18468 17786 18808 348 -185 -35 N
ATOM 1510 NH2 ARG A 199 -5.073 -19.556 30.453 1.00144.64 N
ANISOU 1510 NH2 ARG A 199 18394 17737 18824 387 -165 -41 N
ATOM 1511 N ILE A 200 -7.428 -23.894 22.787 1.00102.00 N
ANISOU 1511 N ILE A 200 13128 12289 13338 365 82 -196 N
ATOM 1512 CA ILE A 200 -8.220 -24.836 21.997 1.00101.59 C
ANISOU 1512 CA ILE A 200 13108 12238 13255 349 98 -214 C
ATOM 1513 C ILE A 200 -7.357 -25.467 20.901 1.00100.20 C
ANISOU 1513 C ILE A 200 12929 12017 13126 363 144 -246 C
ATOM 1514 O ILE A 200 -7.314 -26.693 20.760 1.00102.86 O
ANISOU 1514 O ILE A 200 13276 12319 13488 359 140 -257 O
ATOM 1515 CB ILE A 200 -9.468 -24.162 21.399 1.00100.49 C
ANISOU 1515 CB ILE A 200 12994 12155 13032 333 112 -219 C
ATOM 1516 CG1 ILE A 200 -10.474 -23.823 22.498 1.00103.70 C
ANISOU 1516 CG1 ILE A 200 13405 12604 13391 315 66 -192 C
ATOM 1517 CG2 ILE A 200 -10.121 -25.073 20.366 1.00 99.10 C
ANISOU 1517 CG2 ILE A 200 12851 11975 12828 318 136 -242 C
ATOM 1518 CD1 ILE A 200 -11.669 -23.038 22.015 1.00104.98 C
ANISOU 1518 CD1 ILE A 200 13587 12821 13478 302 76 -195 C
ATOM 1519 N PHE A 201 -6.655 -24.631 20.142 1.00 99.05 N
ANISOU 1519 N PHE A 201 12768 11873 12992 381 185 -261 N
ATOM 1520 CA PHE A 201 -5.810 -25.141 19.069 1.00100.89 C
ANISOU 1520 CA PHE A 201 12997 12070 13268 394 233 -295 C
ATOM 1521 C PHE A 201 -4.568 -25.856 19.592 1.00106.87 C
ANISOU 1521 C PHE A 201 13723 12767 14115 414 223 -294 C
ATOM 1522 O PHE A 201 -4.025 -26.718 18.901 1.00111.11 O
ANISOU 1522 O PHE A 201 14259 13265 14693 422 252 -323 O
ATOM 1523 CB PHE A 201 -5.431 -24.021 18.103 1.00 96.39 C
ANISOU 1523 CB PHE A 201 12419 11523 12682 403 281 -309 C
ATOM 1524 CG PHE A 201 -6.581 -23.503 17.296 1.00 92.89 C
ANISOU 1524 CG PHE A 201 12007 11130 12156 383 299 -316 C
ATOM 1525 CD1 PHE A 201 -7.197 -24.303 16.331 1.00 93.59 C
ANISOU 1525 CD1 PHE A 201 12128 11220 12212 368 324 -342 C
ATOM 1526 CD2 PHE A 201 -7.050 -22.211 17.492 1.00 89.20 C
ANISOU 1526 CD2 PHE A 201 11538 10708 11646 379 288 -296 C
ATOM 1527 CE1 PHE A 201 -8.265 -23.821 15.589 1.00 91.49 C
ANISOU 1527 CE1 PHE A 201 11892 11000 11871 348 338 -345 C
ATOM 1528 CE2 PHE A 201 -8.117 -21.719 16.750 1.00 87.98 C
ANISOU 1528 CE2 PHE A 201 11411 10598 11420 360 301 -301 C
ATOM 1529 CZ PHE A 201 -8.724 -22.525 15.795 1.00 88.34 C
ANISOU 1529 CZ PHE A 201 11488 10644 11432 344 326 -324 C
ATOM 1530 N ALA A 202 -4.129 -25.513 20.802 1.00110.08 N
ANISOU 1530 N ALA A 202 14106 13166 14555 420 181 -263 N
ATOM 1531 CA ALA A 202 -2.974 -26.183 21.406 1.00113.07 C
ANISOU 1531 CA ALA A 202 14454 13486 15022 437 163 -258 C
ATOM 1532 C ALA A 202 -3.327 -27.598 21.866 1.00114.37 C
ANISOU 1532 C ALA A 202 14632 13617 15205 424 128 -254 C
ATOM 1533 O ALA A 202 -2.623 -28.555 21.533 1.00116.80 O
ANISOU 1533 O ALA A 202 14930 13873 15576 436 140 -274 O
ATOM 1534 CB ALA A 202 -2.410 -25.360 22.553 1.00112.05 C
ANISOU 1534 CB ALA A 202 14295 13358 14919 445 126 -224 C
ATOM 1535 N ALA A 203 -4.419 -27.730 22.618 1.00111.96 N
ANISOU 1535 N ALA A 203 14349 13343 14847 400 85 -229 N
ATOM 1536 CA ALA A 203 -4.843 -29.038 23.114 1.00112.56 C
ANISOU 1536 CA ALA A 203 14440 13392 14935 383 46 -219 C
ATOM 1537 C ALA A 203 -5.325 -29.957 21.994 1.00116.17 C
ANISOU 1537 C ALA A 203 14925 13838 15377 376 78 -254 C
ATOM 1538 O ALA A 203 -5.291 -31.176 22.152 1.00121.77 O
ANISOU 1538 O ALA A 203 15638 14505 16122 371 56 -256 O
ATOM 1539 CB ALA A 203 -5.918 -28.886 24.177 1.00113.52 C
ANISOU 1539 CB ALA A 203 14577 13557 14998 356 -5 -183 C
ATOM 1540 N ALA A 204 -5.777 -29.386 20.879 1.00115.97 N
ANISOU 1540 N ALA A 204 14918 13848 15299 376 126 -280 N
ATOM 1541 CA ALA A 204 -6.260 -30.205 19.770 1.00119.07 C
ANISOU 1541 CA ALA A 204 15340 14232 15671 367 158 -314 C
ATOM 1542 C ALA A 204 -5.110 -30.879 19.028 1.00124.95 C
ANISOU 1542 C ALA A 204 16065 14919 16489 391 195 -351 C
ATOM 1543 O ALA A 204 -5.179 -32.067 18.707 1.00129.65 O
ANISOU 1543 O ALA A 204 16674 15477 17110 387 194 -372 O
ATOM 1544 CB ALA A 204 -7.112 -29.382 18.822 1.00117.06 C
ANISOU 1544 CB ALA A 204 15110 14033 15334 356 195 -328 C
ATOM 1545 N ARG A 205 -4.048 -30.124 18.761 1.00128.62 N
ANISOU 1545 N ARG A 205 16501 15377 16993 414 228 -361 N
ATOM 1546 CA ARG A 205 -2.915 -30.670 18.021 1.00135.34 C
ANISOU 1546 CA ARG A 205 17330 16178 17915 438 269 -398 C
ATOM 1547 C ARG A 205 -2.064 -31.601 18.883 1.00139.50 C
ANISOU 1547 C ARG A 205 17829 16640 18535 451 231 -388 C
ATOM 1548 O ARG A 205 -1.452 -32.536 18.357 1.00141.56 O
ANISOU 1548 O ARG A 205 18081 16851 18855 464 251 -422 O
ATOM 1549 CB ARG A 205 -2.073 -29.553 17.428 1.00138.51 C
ANISOU 1549 CB ARG A 205 17707 16596 18326 456 318 -410 C
ATOM 1550 CG ARG A 205 -1.119 -30.002 16.334 1.00145.17 C
ANISOU 1550 CG ARG A 205 18534 17403 19219 476 376 -458 C
ATOM 1551 CD ARG A 205 -0.474 -28.837 15.604 1.00153.85 C
ANISOU 1551 CD ARG A 205 19615 18530 20309 487 429 -469 C
ATOM 1552 NE ARG A 205 0.453 -28.085 16.450 1.00164.98 N
ANISOU 1552 NE ARG A 205 20985 19930 21772 505 409 -440 N
ATOM 1553 CZ ARG A 205 0.147 -26.967 17.108 1.00168.36 C
ANISOU 1553 CZ ARG A 205 21410 20396 22163 499 382 -402 C
ATOM 1554 NH1 ARG A 205 -1.073 -26.446 17.033 1.00174.70 N
ANISOU 1554 NH1 ARG A 205 22247 21252 22880 476 371 -389 N
ATOM 1555 NH2 ARG A 205 1.068 -26.371 17.851 1.00171.50 N
ANISOU 1555 NH2 ARG A 205 21771 20779 22614 516 364 -378 N
ATOM 1556 N ARG A 206 -2.022 -31.360 20.192 1.00141.02 N
ANISOU 1556 N ARG A 206 18008 16833 18743 447 175 -343 N
ATOM 1557 CA ARG A 206 -1.234 -32.213 21.080 1.00144.52 C
ANISOU 1557 CA ARG A 206 18424 17215 19274 456 131 -327 C
ATOM 1558 C ARG A 206 -1.803 -33.627 21.168 1.00141.50 C
ANISOU 1558 C ARG A 206 18064 16799 18901 440 100 -332 C
ATOM 1559 O ARG A 206 -1.049 -34.591 21.295 1.00143.41 O
ANISOU 1559 O ARG A 206 18286 16977 19226 453 87 -342 O
ATOM 1560 CB ARG A 206 -1.126 -31.596 22.471 1.00149.34 C
ANISOU 1560 CB ARG A 206 19017 17837 19888 450 76 -276 C
ATOM 1561 CG ARG A 206 -0.054 -32.229 23.341 1.00158.22 C
ANISOU 1561 CG ARG A 206 20107 18899 21112 463 36 -258 C
ATOM 1562 CD ARG A 206 -0.150 -31.775 24.786 1.00169.57 C
ANISOU 1562 CD ARG A 206 21535 20352 22542 449 -27 -205 C
ATOM 1563 NE ARG A 206 0.776 -32.516 25.640 1.00177.04 N
ANISOU 1563 NE ARG A 206 22452 21235 23581 455 -72 -184 N
ATOM 1564 CZ ARG A 206 0.843 -32.412 26.965 1.00179.84 C
ANISOU 1564 CZ ARG A 206 22797 21589 23947 441 -134 -137 C
ATOM 1565 NH1 ARG A 206 0.038 -31.590 27.630 1.00183.89 N
ANISOU 1565 NH1 ARG A 206 23326 22163 24383 420 -157 -108 N
ATOM 1566 NH2 ARG A 206 1.727 -33.138 27.634 1.00182.12 N
ANISOU 1566 NH2 ARG A 206 23058 21816 24325 447 -175 -119 N
ATOM 1567 N GLN A 207 -3.122 -33.755 21.092 1.00137.06 N
ANISOU 1567 N GLN A 207 17541 16278 18259 412 88 -325 N
ATOM 1568 CA GLN A 207 -3.745 -35.077 21.103 1.00134.74 C
ANISOU 1568 CA GLN A 207 17271 15955 17968 395 59 -329 C
ATOM 1569 C GLN A 207 -3.498 -35.827 19.796 1.00137.13 C
ANISOU 1569 C GLN A 207 17583 16225 18295 408 110 -385 C
ATOM 1570 O GLN A 207 -3.429 -37.057 19.794 1.00141.71 O
ANISOU 1570 O GLN A 207 18167 16754 18923 406 89 -397 O
ATOM 1571 CB GLN A 207 -5.238 -34.966 21.377 1.00127.24 C
ANISOU 1571 CB GLN A 207 16360 15062 16924 361 32 -305 C
ATOM 1572 CG GLN A 207 -5.566 -34.453 22.765 1.00121.99 C
ANISOU 1572 CG GLN A 207 15687 14426 16236 345 -24 -251 C
ATOM 1573 CD GLN A 207 -7.021 -34.057 22.919 1.00120.78 C
ANISOU 1573 CD GLN A 207 15567 14340 15983 315 -37 -232 C
ATOM 1574 OE1 GLN A 207 -7.923 -34.705 22.383 1.00118.07 O
ANISOU 1574 OE1 GLN A 207 15255 14005 15600 296 -34 -245 O
ATOM 1575 NE2 GLN A 207 -7.259 -32.989 23.666 1.00120.82 N
ANISOU 1575 NE2 GLN A 207 15564 14392 15948 309 -53 -203 N
ATOM 1576 N LEU A 208 -3.374 -35.098 18.690 1.00134.91 N
ANISOU 1576 N LEU A 208 17306 15974 17981 419 174 -420 N
ATOM 1577 CA LEU A 208 -3.131 -35.716 17.390 1.00134.57 C
ANISOU 1577 CA LEU A 208 17272 15906 17952 429 229 -476 C
ATOM 1578 C LEU A 208 -1.744 -36.337 17.322 1.00131.14 C
ANISOU 1578 C LEU A 208 16798 15401 17627 460 241 -503 C
ATOM 1579 O LEU A 208 -1.369 -36.948 16.328 1.00127.50 O
ANISOU 1579 O LEU A 208 16339 14912 17195 473 285 -554 O
ATOM 1580 CB LEU A 208 -3.316 -34.691 16.271 1.00136.61 C
ANISOU 1580 CB LEU A 208 17543 16217 18145 430 293 -502 C
ATOM 1581 CG LEU A 208 -4.750 -34.227 16.014 1.00138.70 C
ANISOU 1581 CG LEU A 208 17851 16547 18302 400 290 -489 C
ATOM 1582 CD1 LEU A 208 -4.757 -32.927 15.224 1.00138.91 C
ANISOU 1582 CD1 LEU A 208 17879 16627 18274 402 341 -498 C
ATOM 1583 CD2 LEU A 208 -5.534 -35.310 15.289 1.00140.96 C
ANISOU 1583 CD2 LEU A 208 18175 16821 18562 383 295 -518 C
ATOM 1584 N ALA A1001 0.356 -34.867 19.023 1.00148.50 N
ANISOU 1584 N ALA A1001 18906 17576 19939 498 210 -442 N
ATOM 1585 CA ALA A1001 1.325 -35.893 18.662 1.00148.63 C
ANISOU 1585 CA ALA A1001 18898 17523 20053 521 224 -479 C
ATOM 1586 C ALA A1001 0.969 -37.235 19.296 1.00149.02 C
ANISOU 1586 C ALA A1001 18959 17524 20140 509 164 -466 C
ATOM 1587 O ALA A1001 1.556 -38.260 18.953 1.00152.86 O
ANISOU 1587 O ALA A1001 19431 17949 20702 525 170 -500 O
ATOM 1588 CB ALA A1001 2.728 -35.461 19.068 1.00148.75 C
ANISOU 1588 CB ALA A1001 18860 17504 20153 549 228 -471 C
ATOM 1589 N ASP A1002 0.000 -37.218 20.209 1.00147.90 N
ANISOU 1589 N ASP A1002 18841 17410 19946 480 106 -419 N
ATOM 1590 CA ASP A1002 -0.335 -38.411 20.978 1.00148.25 C
ANISOU 1590 CA ASP A1002 18893 17410 20024 464 40 -396 C
ATOM 1591 C ASP A1002 -0.845 -39.548 20.100 1.00142.75 C
ANISOU 1591 C ASP A1002 18225 16688 19326 458 55 -438 C
ATOM 1592 O ASP A1002 -0.433 -40.697 20.271 1.00140.21 O
ANISOU 1592 O ASP A1002 17892 16300 19083 464 27 -448 O
ATOM 1593 CB ASP A1002 -1.354 -38.081 22.070 1.00151.74 C
ANISOU 1593 CB ASP A1002 19357 17899 20398 430 -18 -338 C
ATOM 1594 CG ASP A1002 -0.712 -37.504 23.312 1.00156.50 C
ANISOU 1594 CG ASP A1002 19927 18498 21036 432 -62 -290 C
ATOM 1595 OD1 ASP A1002 0.342 -38.023 23.740 1.00162.53 O
ANISOU 1595 OD1 ASP A1002 20657 19200 21899 450 -85 -286 O
ATOM 1596 OD2 ASP A1002 -1.272 -36.537 23.869 1.00157.15 O
ANISOU 1596 OD2 ASP A1002 20020 18640 21051 417 -75 -258 O
ATOM 1597 N LEU A1003 -1.723 -39.228 19.151 1.00140.64 N
ANISOU 1597 N LEU A1003 17994 16471 18972 446 99 -464 N
ATOM 1598 CA LEU A1003 -2.284 -40.264 18.285 1.00140.79 C
ANISOU 1598 CA LEU A1003 18043 16469 18980 438 113 -505 C
ATOM 1599 C LEU A1003 -1.214 -40.914 17.414 1.00144.24 C
ANISOU 1599 C LEU A1003 18456 16846 19501 470 159 -564 C
ATOM 1600 O LEU A1003 -1.175 -42.136 17.285 1.00146.72 O
ANISOU 1600 O LEU A1003 18774 17104 19867 472 139 -586 O
ATOM 1601 CB LEU A1003 -3.410 -39.700 17.426 1.00139.23 C
ANISOU 1601 CB LEU A1003 17889 16341 18671 418 152 -519 C
ATOM 1602 CG LEU A1003 -4.804 -39.696 18.057 1.00137.02 C
ANISOU 1602 CG LEU A1003 17645 16105 18310 381 102 -474 C
ATOM 1603 CD1 LEU A1003 -5.752 -38.807 17.263 1.00136.84 C
ANISOU 1603 CD1 LEU A1003 17656 16156 18181 366 143 -483 C
ATOM 1604 CD2 LEU A1003 -5.361 -41.108 18.184 1.00133.04 C
ANISOU 1604 CD2 LEU A1003 17163 15559 17827 364 58 -475 C
ATOM 1605 N GLU A1004 -0.331 -40.104 16.841 1.00149.23 N
ANISOU 1605 N GLU A1004 19062 17490 20150 495 217 -590 N
ATOM 1606 CA GLU A1004 0.739 -40.641 16.008 1.00153.64 C
ANISOU 1606 CA GLU A1004 19593 17996 20788 527 266 -650 C
ATOM 1607 C GLU A1004 1.865 -41.263 16.831 1.00154.71 C
ANISOU 1607 C GLU A1004 19680 18056 21046 550 227 -638 C
ATOM 1608 O GLU A1004 2.623 -42.076 16.299 1.00159.82 O
ANISOU 1608 O GLU A1004 20307 18645 21773 573 250 -686 O
ATOM 1609 CB GLU A1004 1.291 -39.564 15.079 1.00156.42 C
ANISOU 1609 CB GLU A1004 19931 18389 21113 543 344 -681 C
ATOM 1610 CG GLU A1004 1.799 -40.097 13.748 1.00160.91 C
ANISOU 1610 CG GLU A1004 20497 18934 21708 561 414 -756 C
ATOM 1611 CD GLU A1004 0.686 -40.607 12.844 1.00163.41 C
ANISOU 1611 CD GLU A1004 20866 19274 21948 538 432 -788 C
ATOM 1612 OE1 GLU A1004 0.962 -41.518 12.039 1.00168.98 O
ANISOU 1612 OE1 GLU A1004 21574 19940 22692 550 463 -846 O
ATOM 1613 OE2 GLU A1004 -0.460 -40.111 12.936 1.00162.41 O
ANISOU 1613 OE2 GLU A1004 20778 19203 21725 509 416 -757 O
ATOM 1614 N ASP A1005 1.986 -40.889 18.103 1.00154.17 N
ANISOU 1614 N ASP A1005 19595 17989 20994 543 168 -577 N
ATOM 1615 CA ASP A1005 3.027 -41.468 18.953 1.00156.36 C
ANISOU 1615 CA ASP A1005 19827 18194 21387 561 123 -559 C
ATOM 1616 C ASP A1005 2.705 -42.907 19.331 1.00157.29 C
ANISOU 1616 C ASP A1005 19957 18252 21555 550 65 -556 C
ATOM 1617 O ASP A1005 3.562 -43.791 19.219 1.00160.40 O
ANISOU 1617 O ASP A1005 20320 18571 22052 573 60 -585 O
ATOM 1618 CB ASP A1005 3.248 -40.615 20.199 1.00156.58 C
ANISOU 1618 CB ASP A1005 19836 18243 21414 553 76 -494 C
ATOM 1619 CG ASP A1005 4.372 -39.618 20.026 1.00159.87 C
ANISOU 1619 CG ASP A1005 20211 18666 21865 581 121 -502 C
ATOM 1620 OD1 ASP A1005 4.479 -39.008 18.940 1.00165.95 O
ANISOU 1620 OD1 ASP A1005 20984 19471 22598 593 194 -543 O
ATOM 1621 OD2 ASP A1005 5.153 -39.441 20.984 1.00164.84 O
ANISOU 1621 OD2 ASP A1005 20804 19267 22560 590 81 -465 O
ATOM 1622 N ASN A1006 1.475 -43.151 19.778 1.00156.73 N
ANISOU 1622 N ASN A1006 19927 18211 21413 514 19 -522 N
ATOM 1623 CA ASN A1006 1.050 -44.516 20.082 1.00158.93 C
ANISOU 1623 CA ASN A1006 20221 18436 21729 499 -38 -517 C
ATOM 1624 C ASN A1006 1.018 -45.389 18.830 1.00159.58 C
ANISOU 1624 C ASN A1006 20317 18485 21830 513 7 -588 C
ATOM 1625 O ASN A1006 1.284 -46.587 18.909 1.00163.07 O
ANISOU 1625 O ASN A1006 20750 18855 22352 519 -26 -603 O
ATOM 1626 CB ASN A1006 -0.311 -44.516 20.775 1.00155.21 C
ANISOU 1626 CB ASN A1006 19791 18012 21168 456 -92 -464 C
ATOM 1627 CG ASN A1006 -0.230 -44.058 22.220 1.00153.93 C
ANISOU 1627 CG ASN A1006 19613 17863 21010 439 -157 -392 C
ATOM 1628 OD1 ASN A1006 0.608 -44.530 22.992 1.00153.21 O
ANISOU 1628 OD1 ASN A1006 19488 17713 21013 448 -203 -370 O
ATOM 1629 ND2 ASN A1006 -1.111 -43.138 22.595 1.00156.01 N
ANISOU 1629 ND2 ASN A1006 19901 18204 21173 415 -161 -357 N
ATOM 1630 N TRP A1007 0.716 -44.784 17.681 1.00160.14 N
ANISOU 1630 N TRP A1007 20410 18607 21830 517 82 -632 N
ATOM 1631 CA TRP A1007 0.750 -45.513 16.415 1.00162.66 C
ANISOU 1631 CA TRP A1007 20742 18900 22161 530 133 -705 C
ATOM 1632 C TRP A1007 2.180 -45.890 16.030 1.00165.81 C
ANISOU 1632 C TRP A1007 21092 19234 22676 571 168 -754 C
ATOM 1633 O TRP A1007 2.397 -46.930 15.407 1.00169.84 O
ANISOU 1633 O TRP A1007 21602 19690 23242 585 180 -807 O
ATOM 1634 CB TRP A1007 0.080 -44.698 15.309 1.00157.56 C
ANISOU 1634 CB TRP A1007 20132 18329 21405 520 203 -735 C
ATOM 1635 CG TRP A1007 0.045 -45.376 13.967 1.00156.19 C
ANISOU 1635 CG TRP A1007 19977 18138 21232 529 259 -811 C
ATOM 1636 CD1 TRP A1007 0.745 -45.014 12.851 1.00156.28 C
ANISOU 1636 CD1 TRP A1007 19974 18158 21249 553 342 -872 C
ATOM 1637 CD2 TRP A1007 -0.728 -46.523 13.600 1.00154.31 C
ANISOU 1637 CD2 TRP A1007 19775 17872 20985 514 237 -835 C
ATOM 1638 NE1 TRP A1007 0.455 -45.864 11.812 1.00155.26 N
ANISOU 1638 NE1 TRP A1007 19871 18009 21113 553 373 -934 N
ATOM 1639 CE2 TRP A1007 -0.446 -46.798 12.241 1.00153.99 C
ANISOU 1639 CE2 TRP A1007 19741 17823 20944 530 310 -913 C
ATOM 1640 CE3 TRP A1007 -1.635 -47.343 14.283 1.00150.15 C
ANISOU 1640 CE3 TRP A1007 19276 17327 20449 486 163 -797 C
ATOM 1641 CZ2 TRP A1007 -1.033 -47.864 11.553 1.00151.82 C
ANISOU 1641 CZ2 TRP A1007 19500 17521 20662 520 309 -957 C
ATOM 1642 CZ3 TRP A1007 -2.221 -48.400 13.598 1.00147.70 C
ANISOU 1642 CZ3 TRP A1007 18998 16988 20133 476 161 -838 C
ATOM 1643 CH2 TRP A1007 -1.916 -48.651 12.246 1.00148.34 C
ANISOU 1643 CH2 TRP A1007 19086 17060 20216 494 234 -918 C
ATOM 1644 N GLU A1008 3.148 -45.054 16.396 1.00166.90 N
ANISOU 1644 N GLU A1008 21187 19376 22852 592 183 -738 N
ATOM 1645 CA GLU A1008 4.554 -45.391 16.174 1.00169.64 C
ANISOU 1645 CA GLU A1008 21480 19659 23317 631 210 -778 C
ATOM 1646 C GLU A1008 5.082 -46.357 17.228 1.00171.02 C
ANISOU 1646 C GLU A1008 21624 19752 23605 638 131 -748 C
ATOM 1647 O GLU A1008 5.918 -47.207 16.913 1.00169.70 O
ANISOU 1647 O GLU A1008 21424 19512 23541 666 139 -793 O
ATOM 1648 CB GLU A1008 5.417 -44.135 16.127 1.00172.78 C
ANISOU 1648 CB GLU A1008 21842 20092 23715 650 256 -772 C
ATOM 1649 CG GLU A1008 5.280 -43.335 14.841 1.00176.18 C
ANISOU 1649 CG GLU A1008 22290 20585 24067 653 347 -819 C
ATOM 1650 CD GLU A1008 6.190 -42.122 14.796 1.00180.88 C
ANISOU 1650 CD GLU A1008 22847 21211 24670 672 390 -811 C
ATOM 1651 OE1 GLU A1008 7.392 -42.252 15.122 1.00184.37 O
ANISOU 1651 OE1 GLU A1008 23235 21602 25215 700 389 -816 O
ATOM 1652 OE2 GLU A1008 5.714 -41.035 14.411 1.00185.55 O
ANISOU 1652 OE2 GLU A1008 23459 21876 25164 657 426 -801 O
ATOM 1653 N THR A1009 4.613 -46.232 18.468 1.00166.37 N
ANISOU 1653 N THR A1009 21044 19173 22998 612 54 -673 N
ATOM 1654 CA THR A1009 5.001 -47.176 19.513 1.00168.29 C
ANISOU 1654 CA THR A1009 21262 19340 23340 610 -28 -638 C
ATOM 1655 C THR A1009 4.479 -48.584 19.209 1.00170.37 C
ANISOU 1655 C THR A1009 21549 19550 23633 602 -58 -666 C
ATOM 1656 O THR A1009 5.088 -49.575 19.613 1.00173.37 O
ANISOU 1656 O THR A1009 21900 19848 24124 614 -105 -667 O
ATOM 1657 CB THR A1009 4.500 -46.713 20.883 1.00167.60 C
ANISOU 1657 CB THR A1009 21184 19284 23212 578 -102 -551 C
ATOM 1658 OG1 THR A1009 4.692 -45.304 21.002 1.00172.52 O
ANISOU 1658 OG1 THR A1009 21798 19972 23779 581 -68 -531 O
ATOM 1659 CG2 THR A1009 5.263 -47.406 21.999 1.00163.45 C
ANISOU 1659 CG2 THR A1009 20619 18682 22801 581 -180 -511 C
ATOM 1660 N LEU A1010 3.367 -48.666 18.484 1.00169.68 N
ANISOU 1660 N LEU A1010 21514 19508 23450 581 -33 -688 N
ATOM 1661 CA LEU A1010 2.809 -49.955 18.098 1.00168.64 C
ANISOU 1661 CA LEU A1010 21408 19331 23338 572 -57 -718 C
ATOM 1662 C LEU A1010 3.529 -50.559 16.892 1.00167.21 C
ANISOU 1662 C LEU A1010 21210 19101 23223 608 7 -807 C
ATOM 1663 O LEU A1010 3.622 -51.780 16.781 1.00165.34 O
ANISOU 1663 O LEU A1010 20970 18792 23061 615 -24 -835 O
ATOM 1664 CB LEU A1010 1.315 -49.817 17.812 1.00167.94 C
ANISOU 1664 CB LEU A1010 21381 19308 23120 534 -58 -704 C
ATOM 1665 CG LEU A1010 0.459 -51.076 17.957 1.00170.68 C
ANISOU 1665 CG LEU A1010 21761 19617 23473 508 -119 -698 C
ATOM 1666 CD1 LEU A1010 0.157 -51.391 19.418 1.00169.12 C
ANISOU 1666 CD1 LEU A1010 21560 19404 23295 479 -218 -615 C
ATOM 1667 CD2 LEU A1010 -0.837 -50.921 17.175 1.00173.65 C
ANISOU 1667 CD2 LEU A1010 22194 20057 23727 481 -88 -714 C
ATOM 1668 N ASN A1011 4.030 -49.712 15.996 1.00164.34 N
ANISOU 1668 N ASN A1011 20833 18776 22831 631 94 -853 N
ATOM 1669 CA ASN A1011 4.667 -50.178 14.766 1.00163.65 C
ANISOU 1669 CA ASN A1011 20732 18656 22792 663 165 -943 C
ATOM 1670 C ASN A1011 6.161 -50.434 14.918 1.00163.63 C
ANISOU 1670 C ASN A1011 20663 18583 22926 705 174 -968 C
ATOM 1671 O ASN A1011 6.677 -51.415 14.381 1.00164.48 O
ANISOU 1671 O ASN A1011 20752 18623 23119 729 187 -1029 O
ATOM 1672 CB ASN A1011 4.419 -49.187 13.629 1.00162.96 C
ANISOU 1672 CB ASN A1011 20667 18649 22601 663 258 -982 C
ATOM 1673 CG ASN A1011 3.072 -49.385 12.963 1.00162.29 C
ANISOU 1673 CG ASN A1011 20647 18609 22407 631 267 -996 C
ATOM 1674 OD1 ASN A1011 2.685 -50.505 12.637 1.00163.75 O
ANISOU 1674 OD1 ASN A1011 20853 18750 22616 627 248 -1029 O
ATOM 1675 ND2 ASN A1011 2.357 -48.289 12.744 1.00160.23 N
ANISOU 1675 ND2 ASN A1011 20417 18435 22028 608 296 -972 N
ATOM 1676 N ASP A1012 6.860 -49.553 15.627 1.00161.25 N
ANISOU 1676 N ASP A1012 20325 18297 22647 714 167 -923 N
ATOM 1677 CA ASP A1012 8.309 -49.694 15.774 1.00164.89 C
ANISOU 1677 CA ASP A1012 20719 18695 23237 753 177 -944 C
ATOM 1678 C ASP A1012 8.692 -50.908 16.617 1.00165.83 C
ANISOU 1678 C ASP A1012 20811 18716 23480 759 93 -925 C
ATOM 1679 O ASP A1012 9.639 -51.619 16.296 1.00166.93 O
ANISOU 1679 O ASP A1012 20908 18783 23734 794 107 -976 O
ATOM 1680 CB ASP A1012 8.923 -48.418 16.342 1.00165.68 C
ANISOU 1680 CB ASP A1012 20789 18837 23327 758 188 -897 C
ATOM 1681 CG ASP A1012 9.043 -47.314 15.305 1.00164.67 C
ANISOU 1681 CG ASP A1012 20664 18782 23120 766 285 -936 C
ATOM 1682 OD1 ASP A1012 9.688 -47.531 14.257 1.00158.64 O
ANISOU 1682 OD1 ASP A1012 19880 18002 22394 794 357 -1010 O
ATOM 1683 OD2 ASP A1012 8.498 -46.217 15.543 1.00163.88 O
ANISOU 1683 OD2 ASP A1012 20588 18757 22922 744 290 -891 O
ATOM 1684 N ASN A1013 7.941 -51.157 17.683 1.00163.30 N
ANISOU 1684 N ASN A1013 20516 18394 23135 725 5 -853 N
ATOM 1685 CA ASN A1013 8.228 -52.297 18.547 1.00162.85 C
ANISOU 1685 CA ASN A1013 20437 18247 23190 725 -83 -826 C
ATOM 1686 C ASN A1013 7.843 -53.637 17.933 1.00162.63 C
ANISOU 1686 C ASN A1013 20429 18162 23201 727 -94 -879 C
ATOM 1687 O ASN A1013 8.271 -54.675 18.434 1.00156.28 O
ANISOU 1687 O ASN A1013 19599 17270 22509 735 -157 -874 O
ATOM 1688 CB ASN A1013 7.565 -52.119 19.908 1.00161.01 C
ANISOU 1688 CB ASN A1013 20224 18035 22917 683 -174 -729 C
ATOM 1689 CG ASN A1013 8.178 -50.991 20.711 1.00161.04 C
ANISOU 1689 CG ASN A1013 20198 18072 22919 685 -180 -675 C
ATOM 1690 OD1 ASN A1013 8.509 -49.934 20.172 1.00158.40 O
ANISOU 1690 OD1 ASN A1013 19854 17792 22540 701 -107 -696 O
ATOM 1691 ND2 ASN A1013 8.333 -51.210 22.008 1.00163.08 N
ANISOU 1691 ND2 ASN A1013 20440 18298 23226 667 -269 -603 N
ATOM 1692 N LEU A1014 7.040 -53.629 16.869 1.00163.76 N
ANISOU 1692 N LEU A1014 20618 18351 23252 719 -37 -929 N
ATOM 1693 CA LEU A1014 6.806 -54.858 16.114 1.00166.88 C
ANISOU 1693 CA LEU A1014 21029 18690 23688 727 -35 -993 C
ATOM 1694 C LEU A1014 8.067 -55.301 15.382 1.00172.44 C
ANISOU 1694 C LEU A1014 21680 19329 24510 777 19 -1075 C
ATOM 1695 O LEU A1014 8.364 -56.495 15.309 1.00180.84 O
ANISOU 1695 O LEU A1014 22729 20307 25676 793 -13 -1110 O
ATOM 1696 CB LEU A1014 5.650 -54.689 15.134 1.00163.35 C
ANISOU 1696 CB LEU A1014 20645 18311 23111 704 15 -1027 C
ATOM 1697 CG LEU A1014 4.254 -54.977 15.679 1.00162.85 C
ANISOU 1697 CG LEU A1014 20637 18275 22963 656 -53 -968 C
ATOM 1698 CD1 LEU A1014 3.190 -54.571 14.674 1.00164.72 C
ANISOU 1698 CD1 LEU A1014 20931 18589 23065 636 5 -999 C
ATOM 1699 CD2 LEU A1014 4.116 -56.447 16.042 1.00163.45 C
ANISOU 1699 CD2 LEU A1014 20714 18261 23128 651 -131 -968 C
ATOM 1700 N LYS A1015 8.810 -54.340 14.841 1.00173.37 N
ANISOU 1700 N LYS A1015 21770 19488 24615 801 101 -1106 N
ATOM 1701 CA LYS A1015 10.082 -54.641 14.190 1.00172.55 C
ANISOU 1701 CA LYS A1015 21610 19329 24623 849 157 -1181 C
ATOM 1702 C LYS A1015 11.163 -55.032 15.197 1.00171.20 C
ANISOU 1702 C LYS A1015 21375 19075 24598 872 94 -1147 C
ATOM 1703 O LYS A1015 12.128 -55.697 14.824 1.00171.72 O
ANISOU 1703 O LYS A1015 21393 19069 24783 910 113 -1207 O
ATOM 1704 CB LYS A1015 10.542 -53.459 13.341 1.00173.11 C
ANISOU 1704 CB LYS A1015 21669 19473 24633 865 261 -1217 C
ATOM 1705 CG LYS A1015 9.620 -53.147 12.178 1.00174.05 C
ANISOU 1705 CG LYS A1015 21844 19666 24620 847 331 -1263 C
ATOM 1706 CD LYS A1015 10.029 -51.860 11.479 1.00173.83 C
ANISOU 1706 CD LYS A1015 21806 19717 24525 856 424 -1283 C
ATOM 1707 CE LYS A1015 9.115 -51.548 10.304 1.00175.43 C
ANISOU 1707 CE LYS A1015 22065 19993 24596 835 491 -1327 C
ATOM 1708 NZ LYS A1015 9.317 -52.469 9.149 1.00179.16 N
ANISOU 1708 NZ LYS A1015 22539 20428 25105 855 545 -1426 N
ATOM 1709 N VAL A1016 11.012 -54.622 16.456 1.00171.34 N
ANISOU 1709 N VAL A1016 21392 19103 24607 847 19 -1054 N
ATOM 1710 CA VAL A1016 11.924 -55.069 17.508 1.00174.92 C
ANISOU 1710 CA VAL A1016 21790 19475 25195 861 -55 -1012 C
ATOM 1711 C VAL A1016 11.727 -56.567 17.784 1.00181.56 C
ANISOU 1711 C VAL A1016 22634 20223 26128 858 -131 -1019 C
ATOM 1712 O VAL A1016 12.692 -57.284 18.062 1.00188.21 O
ANISOU 1712 O VAL A1016 23422 20974 27114 887 -164 -1034 O
ATOM 1713 CB VAL A1016 11.749 -54.232 18.788 1.00171.74 C
ANISOU 1713 CB VAL A1016 21391 19112 24750 831 -116 -909 C
ATOM 1714 CG1 VAL A1016 12.683 -54.702 19.888 1.00165.96 C
ANISOU 1714 CG1 VAL A1016 20605 18297 24157 842 -196 -863 C
ATOM 1715 CG2 VAL A1016 11.993 -52.762 18.494 1.00172.17 C
ANISOU 1715 CG2 VAL A1016 21441 19253 24724 836 -42 -905 C
ATOM 1716 N ILE A1017 10.491 -57.039 17.685 1.00180.06 N
ANISOU 1716 N ILE A1017 22504 20053 25857 824 -161 -1010 N
ATOM 1717 CA ILE A1017 10.206 -58.457 17.873 1.00178.98 C
ANISOU 1717 CA ILE A1017 22375 19832 25798 818 -233 -1017 C
ATOM 1718 C ILE A1017 10.661 -59.275 16.657 1.00181.60 C
ANISOU 1718 C ILE A1017 22691 20109 26200 857 -173 -1127 C
ATOM 1719 O ILE A1017 11.112 -60.416 16.807 1.00187.70 O
ANISOU 1719 O ILE A1017 23435 20782 27100 875 -223 -1150 O
ATOM 1720 CB ILE A1017 8.715 -58.682 18.177 1.00176.67 C
ANISOU 1720 CB ILE A1017 22151 19580 25394 766 -286 -968 C
ATOM 1721 CG1 ILE A1017 8.298 -57.854 19.397 1.00176.18 C
ANISOU 1721 CG1 ILE A1017 22102 19575 25263 728 -342 -863 C
ATOM 1722 CG2 ILE A1017 8.427 -60.157 18.417 1.00176.59 C
ANISOU 1722 CG2 ILE A1017 22148 19480 25467 757 -367 -971 C
ATOM 1723 CD1 ILE A1017 6.799 -57.755 19.593 1.00175.39 C
ANISOU 1723 CD1 ILE A1017 22070 19542 25029 677 -372 -818 C
ATOM 1724 N GLU A1018 10.564 -58.695 15.461 1.00180.29 N
ANISOU 1724 N GLU A1018 22542 20005 25954 871 -68 -1196 N
ATOM 1725 CA GLU A1018 10.880 -59.423 14.230 1.00184.85 C
ANISOU 1725 CA GLU A1018 23112 20543 26580 904 -4 -1305 C
ATOM 1726 C GLU A1018 12.368 -59.747 14.087 1.00189.86 C
ANISOU 1726 C GLU A1018 23669 21101 27369 956 21 -1358 C
ATOM 1727 O GLU A1018 12.724 -60.681 13.374 1.00196.93 O
ANISOU 1727 O GLU A1018 24548 21933 28346 985 43 -1440 O
ATOM 1728 CB GLU A1018 10.400 -58.648 13.005 1.00181.70 C
ANISOU 1728 CB GLU A1018 22751 20237 26048 900 102 -1360 C
ATOM 1729 CG GLU A1018 8.894 -58.624 12.828 1.00179.76 C
ANISOU 1729 CG GLU A1018 22584 20053 25664 855 86 -1335 C
ATOM 1730 CD GLU A1018 8.446 -57.721 11.693 1.00180.75 C
ANISOU 1730 CD GLU A1018 22747 20276 25656 848 188 -1379 C
ATOM 1731 OE1 GLU A1018 8.858 -57.962 10.536 1.00183.00 O
ANISOU 1731 OE1 GLU A1018 23023 20553 25957 875 267 -1472 O
ATOM 1732 OE2 GLU A1018 7.680 -56.772 11.958 1.00179.88 O
ANISOU 1732 OE2 GLU A1018 22672 20250 25424 815 188 -1320 O
ATOM 1733 N LYS A1019 13.227 -58.988 14.766 1.00194.30 N
ANISOU 1733 N LYS A1019 24183 21669 27973 968 16 -1312 N
ATOM 1734 CA LYS A1019 14.673 -59.177 14.671 1.00200.91 C
ANISOU 1734 CA LYS A1019 24942 22439 28955 1017 42 -1356 C
ATOM 1735 C LYS A1019 15.330 -59.433 16.024 1.00208.47 C
ANISOU 1735 C LYS A1019 25853 23325 30030 1019 -57 -1280 C
ATOM 1736 O LYS A1019 16.556 -59.365 16.132 1.00210.66 O
ANISOU 1736 O LYS A1019 26063 23556 30422 1055 -42 -1298 O
ATOM 1737 CB LYS A1019 15.329 -57.973 13.984 1.00198.00 C
ANISOU 1737 CB LYS A1019 24550 22143 28540 1039 150 -1390 C
ATOM 1738 CG LYS A1019 14.810 -57.678 12.585 1.00193.85 C
ANISOU 1738 CG LYS A1019 24065 21688 27903 1038 253 -1469 C
ATOM 1739 CD LYS A1019 15.258 -56.307 12.108 1.00191.31 C
ANISOU 1739 CD LYS A1019 23728 21452 27508 1045 344 -1475 C
ATOM 1740 CE LYS A1019 14.602 -55.931 10.788 1.00189.87 C
ANISOU 1740 CE LYS A1019 23595 21350 27198 1035 439 -1540 C
ATOM 1741 NZ LYS A1019 14.932 -54.534 10.393 1.00189.35 N
ANISOU 1741 NZ LYS A1019 23520 21373 27051 1034 519 -1533 N
ATOM 1742 N ALA A1020 14.531 -59.730 17.049 1.00208.37 N
ANISOU 1742 N ALA A1020 25875 23304 29991 977 -158 -1195 N
ATOM 1743 CA ALA A1020 15.058 -59.948 18.393 1.00210.28 C
ANISOU 1743 CA ALA A1020 26079 23486 30333 970 -258 -1114 C
ATOM 1744 C ALA A1020 15.928 -61.199 18.461 1.00215.57 C
ANISOU 1744 C ALA A1020 26694 24030 31183 1005 -303 -1154 C
ATOM 1745 O ALA A1020 15.832 -62.091 17.613 1.00220.29 O
ANISOU 1745 O ALA A1020 27297 24583 31820 1024 -278 -1234 O
ATOM 1746 CB ALA A1020 13.935 -60.020 19.417 1.00206.22 C
ANISOU 1746 CB ALA A1020 25618 22996 29740 914 -353 -1018 C
ATOM 1747 N ASP A1021 16.777 -61.248 19.482 1.00216.87 N
ANISOU 1747 N ASP A1021 26806 24136 31458 1011 -370 -1097 N
ATOM 1748 CA ASP A1021 17.678 -62.375 19.713 1.00213.53 C
ANISOU 1748 CA ASP A1021 26325 23589 31219 1043 -424 -1122 C
ATOM 1749 C ASP A1021 17.235 -63.268 20.868 1.00210.66 C
ANISOU 1749 C ASP A1021 25974 23160 30909 1006 -561 -1041 C
ATOM 1750 O ASP A1021 17.191 -64.488 20.727 1.00214.51 O
ANISOU 1750 O ASP A1021 26456 23561 31489 1015 -607 -1075 O
ATOM 1751 CB ASP A1021 19.103 -61.871 19.955 1.00214.58 C
ANISOU 1751 CB ASP A1021 26379 23692 31459 1081 -402 -1124 C
ATOM 1752 CG ASP A1021 19.627 -61.027 18.808 1.00215.84 C
ANISOU 1752 CG ASP A1021 26519 23913 31576 1117 -268 -1204 C
ATOM 1753 OD1 ASP A1021 19.399 -61.395 17.635 1.00220.29 O
ANISOU 1753 OD1 ASP A1021 27099 24484 32116 1136 -194 -1297 O
ATOM 1754 OD2 ASP A1021 20.272 -59.991 19.077 1.00215.73 O
ANISOU 1754 OD2 ASP A1021 26475 23941 31551 1124 -236 -1174 O
ATOM 1755 N ASN A1022 16.905 -62.659 22.005 1.00206.04 N
ANISOU 1755 N ASN A1022 25407 22615 30265 964 -625 -936 N
ATOM 1756 CA ASN A1022 16.558 -63.389 23.219 1.00197.94 C
ANISOU 1756 CA ASN A1022 24390 21534 29286 925 -757 -848 C
ATOM 1757 C ASN A1022 15.098 -63.181 23.591 1.00192.89 C
ANISOU 1757 C ASN A1022 23828 20973 28490 866 -792 -786 C
ATOM 1758 O ASN A1022 14.382 -62.387 22.971 1.00186.37 O
ANISOU 1758 O ASN A1022 23047 20244 27520 856 -716 -806 O
ATOM 1759 CB ASN A1022 17.481 -62.972 24.370 1.00194.42 C
ANISOU 1759 CB ASN A1022 23892 21059 28919 923 -817 -771 C
ATOM 1760 CG ASN A1022 17.610 -61.470 24.493 1.00187.94 C
ANISOU 1760 CG ASN A1022 23075 20340 27993 918 -756 -741 C
ATOM 1761 OD1 ASN A1022 16.796 -60.816 25.140 1.00187.57 O
ANISOU 1761 OD1 ASN A1022 23075 20369 27824 872 -783 -668 O
ATOM 1762 ND2 ASN A1022 18.637 -60.914 23.861 1.00185.28 N
ANISOU 1762 ND2 ASN A1022 22688 20005 27705 965 -671 -799 N
ATOM 1763 N ALA A1023 14.662 -63.912 24.613 1.00189.83 N
ANISOU 1763 N ALA A1023 23454 20539 28134 825 -909 -709 N
ATOM 1764 CA ALA A1023 13.301 -63.803 25.121 1.00189.94 C
ANISOU 1764 CA ALA A1023 23537 20621 28012 765 -955 -641 C
ATOM 1765 C ALA A1023 13.054 -62.491 25.863 1.00189.74 C
ANISOU 1765 C ALA A1023 23528 20694 27869 734 -950 -565 C
ATOM 1766 O ALA A1023 11.916 -62.036 25.943 1.00194.63 O
ANISOU 1766 O ALA A1023 24206 21399 28344 695 -944 -533 O
ATOM 1767 CB ALA A1023 12.969 -64.991 26.011 1.00188.60 C
ANISOU 1767 CB ALA A1023 23372 20371 27916 730 -1084 -581 C
ATOM 1768 N ALA A1024 14.105 -61.896 26.423 1.00190.83 N
ANISOU 1768 N ALA A1024 23615 20819 28073 752 -954 -537 N
ATOM 1769 CA ALA A1024 13.942 -60.656 27.178 1.00187.43 C
ANISOU 1769 CA ALA A1024 23198 20477 27541 723 -953 -465 C
ATOM 1770 C ALA A1024 13.714 -59.457 26.258 1.00185.91 C
ANISOU 1770 C ALA A1024 23027 20386 27224 741 -833 -514 C
ATOM 1771 O ALA A1024 12.998 -58.525 26.627 1.00185.60 O
ANISOU 1771 O ALA A1024 23026 20440 27052 708 -824 -466 O
ATOM 1772 CB ALA A1024 15.129 -60.423 28.098 1.00185.61 C
ANISOU 1772 CB ALA A1024 22907 20196 27420 734 -1002 -416 C
ATOM 1773 N GLN A1025 14.318 -59.475 25.071 1.00187.38 N
ANISOU 1773 N GLN A1025 23187 20555 27453 792 -741 -610 N
ATOM 1774 CA GLN A1025 14.136 -58.377 24.117 1.00186.42 C
ANISOU 1774 CA GLN A1025 23085 20528 27219 808 -626 -660 C
ATOM 1775 C GLN A1025 12.695 -58.288 23.620 1.00187.64 C
ANISOU 1775 C GLN A1025 23314 20759 27222 775 -601 -667 C
ATOM 1776 O GLN A1025 12.164 -57.192 23.435 1.00180.54 O
ANISOU 1776 O GLN A1025 22447 19958 26193 760 -548 -656 O
ATOM 1777 CB GLN A1025 15.090 -58.517 22.942 1.00183.25 C
ANISOU 1777 CB GLN A1025 22639 20089 26900 866 -535 -762 C
ATOM 1778 CG GLN A1025 16.517 -58.106 23.251 1.00182.15 C
ANISOU 1778 CG GLN A1025 22426 19909 26872 902 -526 -759 C
ATOM 1779 CD GLN A1025 17.366 -57.984 22.006 1.00183.60 C
ANISOU 1779 CD GLN A1025 22570 20083 27106 956 -418 -862 C
ATOM 1780 OE1 GLN A1025 18.308 -58.749 21.809 1.00184.87 O
ANISOU 1780 OE1 GLN A1025 22676 20153 27413 994 -423 -907 O
ATOM 1781 NE2 GLN A1025 17.038 -57.016 21.152 1.00177.47 N
ANISOU 1781 NE2 GLN A1025 21821 19400 26209 960 -319 -899 N
ATOM 1782 N VAL A1026 12.062 -59.441 23.430 1.00189.63 N
ANISOU 1782 N VAL A1026 23592 20964 27496 762 -643 -685 N
ATOM 1783 CA VAL A1026 10.653 -59.467 23.049 1.00190.10 C
ANISOU 1783 CA VAL A1026 23723 21089 27419 727 -632 -685 C
ATOM 1784 C VAL A1026 9.786 -58.917 24.187 1.00187.72 C
ANISOU 1784 C VAL A1026 23458 20853 27015 671 -697 -583 C
ATOM 1785 O VAL A1026 8.744 -58.307 23.938 1.00190.83 O
ANISOU 1785 O VAL A1026 23904 21336 27267 645 -664 -573 O
ATOM 1786 CB VAL A1026 10.218 -60.885 22.642 1.00192.47 C
ANISOU 1786 CB VAL A1026 24040 21316 27775 725 -670 -723 C
ATOM 1787 CG1 VAL A1026 8.835 -60.866 22.010 1.00193.97 C
ANISOU 1787 CG1 VAL A1026 24300 21576 27825 696 -641 -739 C
ATOM 1788 CG2 VAL A1026 11.230 -61.488 21.678 1.00194.49 C
ANISOU 1788 CG2 VAL A1026 24249 21495 28153 782 -617 -822 C
ATOM 1789 N LYS A1027 10.226 -59.108 25.430 1.00184.33 N
ANISOU 1789 N LYS A1027 23000 20380 26657 654 -788 -507 N
ATOM 1790 CA LYS A1027 9.465 -58.617 26.576 1.00179.92 C
ANISOU 1790 CA LYS A1027 22473 19881 26006 600 -852 -410 C
ATOM 1791 C LYS A1027 9.487 -57.090 26.646 1.00176.10 C
ANISOU 1791 C LYS A1027 21995 19496 25419 600 -791 -393 C
ATOM 1792 O LYS A1027 8.461 -56.468 26.932 1.00171.08 O
ANISOU 1792 O LYS A1027 21405 18947 24651 562 -792 -352 O
ATOM 1793 CB LYS A1027 9.993 -59.228 27.869 1.00179.38 C
ANISOU 1793 CB LYS A1027 22373 19740 26044 580 -966 -335 C
ATOM 1794 CG LYS A1027 9.062 -59.106 29.061 1.00177.70 C
ANISOU 1794 CG LYS A1027 22197 19574 25745 516 -1049 -237 C
ATOM 1795 CD LYS A1027 9.781 -59.415 30.369 1.00170.75 C
ANISOU 1795 CD LYS A1027 21278 18634 24964 498 -1150 -160 C
ATOM 1796 CE LYS A1027 10.343 -60.830 30.404 1.00165.54 C
ANISOU 1796 CE LYS A1027 20587 17851 24462 510 -1218 -173 C
ATOM 1797 NZ LYS A1027 11.101 -61.090 31.654 1.00162.92 N
ANISOU 1797 NZ LYS A1027 20215 17458 24230 493 -1316 -97 N
ATOM 1798 N ASP A1028 10.643 -56.486 26.380 1.00176.94 N
ANISOU 1798 N ASP A1028 22052 19590 25588 642 -738 -424 N
ATOM 1799 CA ASP A1028 10.744 -55.026 26.414 1.00175.64 C
ANISOU 1799 CA ASP A1028 21889 19513 25334 644 -680 -409 C
ATOM 1800 C ASP A1028 9.961 -54.369 25.282 1.00174.30 C
ANISOU 1800 C ASP A1028 21761 19428 25035 648 -583 -463 C
ATOM 1801 O ASP A1028 9.510 -53.234 25.422 1.00168.60 O
ANISOU 1801 O ASP A1028 21063 18796 24202 632 -553 -436 O
ATOM 1802 CB ASP A1028 12.206 -54.585 26.377 1.00179.44 C
ANISOU 1802 CB ASP A1028 22304 19955 25918 688 -648 -429 C
ATOM 1803 CG ASP A1028 12.894 -54.733 27.719 1.00182.57 C
ANISOU 1803 CG ASP A1028 22664 20301 26404 674 -742 -353 C
ATOM 1804 OD1 ASP A1028 12.384 -54.190 28.723 1.00177.81 O
ANISOU 1804 OD1 ASP A1028 22084 19748 25727 632 -794 -275 O
ATOM 1805 OD2 ASP A1028 13.955 -55.390 27.770 1.00186.18 O
ANISOU 1805 OD2 ASP A1028 23067 20665 27006 704 -766 -371 O
ATOM 1806 N ALA A1029 9.790 -55.082 24.172 1.00175.06 N
ANISOU 1806 N ALA A1029 21869 19498 25149 669 -538 -540 N
ATOM 1807 CA ALA A1029 9.010 -54.553 23.055 1.00173.98 C
ANISOU 1807 CA ALA A1029 21776 19438 24892 670 -450 -592 C
ATOM 1808 C ALA A1029 7.510 -54.747 23.269 1.00174.11 C
ANISOU 1808 C ALA A1029 21856 19505 24792 621 -488 -555 C
ATOM 1809 O ALA A1029 6.718 -53.884 22.884 1.00175.53 O
ANISOU 1809 O ALA A1029 22076 19775 24843 606 -438 -556 O
ATOM 1810 CB ALA A1029 9.457 -55.175 21.744 1.00174.06 C
ANISOU 1810 CB ALA A1029 21771 19403 24960 711 -381 -692 C
ATOM 1811 N LEU A1030 7.116 -55.869 23.870 1.00173.60 N
ANISOU 1811 N LEU A1030 21802 19383 24774 596 -575 -522 N
ATOM 1812 CA LEU A1030 5.699 -56.142 24.101 1.00172.26 C
ANISOU 1812 CA LEU A1030 21692 19259 24502 548 -615 -485 C
ATOM 1813 C LEU A1030 5.127 -55.312 25.247 1.00171.61 C
ANISOU 1813 C LEU A1030 21627 19247 24330 506 -661 -396 C
ATOM 1814 O LEU A1030 3.976 -54.875 25.182 1.00172.03 O
ANISOU 1814 O LEU A1030 21728 19378 24256 474 -649 -377 O
ATOM 1815 CB LEU A1030 5.470 -57.633 24.351 1.00171.35 C
ANISOU 1815 CB LEU A1030 21580 19057 24466 534 -696 -479 C
ATOM 1816 CG LEU A1030 5.510 -58.559 23.133 1.00172.64 C
ANISOU 1816 CG LEU A1030 21749 19166 24679 563 -655 -568 C
ATOM 1817 CD1 LEU A1030 5.574 -60.010 23.574 1.00170.22 C
ANISOU 1817 CD1 LEU A1030 21433 18760 24484 554 -746 -554 C
ATOM 1818 CD2 LEU A1030 4.303 -58.328 22.237 1.00172.94 C
ANISOU 1818 CD2 LEU A1030 21847 19279 24584 546 -600 -601 C
ATOM 1819 N THR A1031 5.919 -55.094 26.293 1.00171.84 N
ANISOU 1819 N THR A1031 21617 19249 24425 505 -712 -342 N
ATOM 1820 CA THR A1031 5.456 -54.293 27.426 1.00165.94 C
ANISOU 1820 CA THR A1031 20885 18568 23597 465 -756 -259 C
ATOM 1821 C THR A1031 5.224 -52.834 27.037 1.00163.53 C
ANISOU 1821 C THR A1031 20593 18361 23178 472 -676 -271 C
ATOM 1822 O THR A1031 4.290 -52.206 27.531 1.00156.40 O
ANISOU 1822 O THR A1031 19726 17537 22164 435 -689 -225 O
ATOM 1823 CB THR A1031 6.428 -54.380 28.602 1.00166.82 C
ANISOU 1823 CB THR A1031 20950 18626 23808 462 -829 -202 C
ATOM 1824 OG1 THR A1031 7.764 -54.209 28.119 1.00174.10 O
ANISOU 1824 OG1 THR A1031 21819 19496 24833 514 -782 -250 O
ATOM 1825 CG2 THR A1031 6.302 -55.732 29.306 1.00157.47 C
ANISOU 1825 CG2 THR A1031 19764 17363 22704 435 -931 -161 C
ATOM 1826 N LYS A1032 6.058 -52.307 26.143 1.00164.12 N
ANISOU 1826 N LYS A1032 20641 18433 23285 518 -593 -333 N
ATOM 1827 CA LYS A1032 5.859 -50.946 25.649 1.00164.26 C
ANISOU 1827 CA LYS A1032 20671 18540 23199 526 -514 -349 C
ATOM 1828 C LYS A1032 4.629 -50.850 24.746 1.00167.19 C
ANISOU 1828 C LYS A1032 21098 18975 23453 511 -465 -383 C
ATOM 1829 O LYS A1032 3.954 -49.818 24.728 1.00167.39 O
ANISOU 1829 O LYS A1032 21150 19087 23363 494 -435 -366 O
ATOM 1830 CB LYS A1032 7.098 -50.436 24.924 1.00162.55 C
ANISOU 1830 CB LYS A1032 20410 18304 23049 576 -440 -404 C
ATOM 1831 CG LYS A1032 8.299 -50.205 25.823 1.00159.59 C
ANISOU 1831 CG LYS A1032 19980 17884 22772 590 -479 -366 C
ATOM 1832 CD LYS A1032 9.501 -49.722 25.031 1.00158.35 C
ANISOU 1832 CD LYS A1032 19777 17708 22680 640 -402 -424 C
ATOM 1833 CE LYS A1032 10.675 -49.426 25.948 1.00157.97 C
ANISOU 1833 CE LYS A1032 19675 17619 22727 653 -441 -382 C
ATOM 1834 NZ LYS A1032 11.855 -48.928 25.189 1.00160.09 N
ANISOU 1834 NZ LYS A1032 19896 17872 23059 701 -365 -436 N
ATOM 1835 N MET A1033 4.336 -51.914 24.004 1.00168.21 N
ANISOU 1835 N MET A1033 21243 19060 23611 516 -461 -430 N
ATOM 1836 CA MET A1033 3.126 -51.945 23.181 1.00168.36 C
ANISOU 1836 CA MET A1033 21315 19132 23521 498 -424 -459 C
ATOM 1837 C MET A1033 1.872 -52.119 24.032 1.00166.12 C
ANISOU 1837 C MET A1033 21073 18888 23155 445 -493 -391 C
ATOM 1838 O MET A1033 0.820 -51.567 23.701 1.00167.59 O
ANISOU 1838 O MET A1033 21301 19152 23222 423 -464 -389 O
ATOM 1839 CB MET A1033 3.204 -53.055 22.141 1.00172.09 C
ANISOU 1839 CB MET A1033 21793 19543 24052 519 -400 -531 C
ATOM 1840 CG MET A1033 4.227 -52.823 21.043 1.00175.79 C
ANISOU 1840 CG MET A1033 22228 19990 24573 568 -312 -612 C
ATOM 1841 SD MET A1033 4.479 -54.278 20.009 1.00177.32 S
ANISOU 1841 SD MET A1033 22419 20096 24859 595 -297 -697 S
ATOM 1842 CE MET A1033 2.838 -54.470 19.316 1.00177.38 C
ANISOU 1842 CE MET A1033 22501 20164 24730 558 -283 -709 C
ATOM 1843 N ARG A1034 1.975 -52.883 25.119 1.00164.20 N
ANISOU 1843 N ARG A1034 20818 18594 22977 423 -586 -335 N
ATOM 1844 CA ARG A1034 0.816 -53.128 25.974 1.00162.74 C
ANISOU 1844 CA ARG A1034 20669 18445 22719 369 -656 -268 C
ATOM 1845 C ARG A1034 0.387 -51.856 26.712 1.00163.99 C
ANISOU 1845 C ARG A1034 20838 18694 22776 346 -654 -214 C
ATOM 1846 O ARG A1034 -0.808 -51.606 26.878 1.00166.81 O
ANISOU 1846 O ARG A1034 21235 19119 23025 310 -663 -187 O
ATOM 1847 CB ARG A1034 1.110 -54.252 26.961 1.00159.93 C
ANISOU 1847 CB ARG A1034 20295 18010 22462 350 -757 -220 C
ATOM 1848 CG ARG A1034 -0.126 -54.842 27.608 1.00157.60 C
ANISOU 1848 CG ARG A1034 20040 17738 22104 295 -828 -164 C
ATOM 1849 CD ARG A1034 0.243 -55.774 28.749 1.00156.69 C
ANISOU 1849 CD ARG A1034 19902 17551 22081 271 -933 -103 C
ATOM 1850 NE ARG A1034 -0.924 -56.501 29.245 1.00157.02 N
ANISOU 1850 NE ARG A1034 19981 17606 22072 218 -1001 -55 N
ATOM 1851 CZ ARG A1034 -1.807 -56.016 30.116 1.00156.38 C
ANISOU 1851 CZ ARG A1034 19926 17602 21891 170 -1036 11 C
ATOM 1852 NH1 ARG A1034 -1.676 -54.789 30.610 1.00158.39 N
ANISOU 1852 NH1 ARG A1034 20172 17924 22085 169 -1010 36 N
ATOM 1853 NH2 ARG A1034 -2.831 -56.760 30.497 1.00157.11 N
ANISOU 1853 NH2 ARG A1034 20049 17701 21944 123 -1096 51 N
ATOM 1854 N ALA A1035 1.358 -51.056 27.144 1.00164.41 N
ANISOU 1854 N ALA A1035 20852 18748 22866 367 -642 -201 N
ATOM 1855 CA ALA A1035 1.049 -49.766 27.758 1.00159.26 C
ANISOU 1855 CA ALA A1035 20207 18181 22122 350 -633 -159 C
ATOM 1856 C ALA A1035 0.522 -48.770 26.727 1.00153.63 C
ANISOU 1856 C ALA A1035 19520 17546 21307 363 -543 -204 C
ATOM 1857 O ALA A1035 -0.346 -47.954 27.042 1.00151.90 O
ANISOU 1857 O ALA A1035 19328 17408 20981 337 -539 -174 O
ATOM 1858 CB ALA A1035 2.259 -49.206 28.489 1.00156.52 C
ANISOU 1858 CB ALA A1035 19813 17811 21846 369 -648 -133 C
ATOM 1859 N ALA A1036 1.044 -48.831 25.504 1.00152.40 N
ANISOU 1859 N ALA A1036 19355 17365 21186 402 -471 -276 N
ATOM 1860 CA ALA A1036 0.569 -47.953 24.435 1.00152.78 C
ANISOU 1860 CA ALA A1036 19427 17482 21141 413 -386 -321 C
ATOM 1861 C ALA A1036 -0.823 -48.351 23.954 1.00155.86 C
ANISOU 1861 C ALA A1036 19870 17910 21440 383 -385 -329 C
ATOM 1862 O ALA A1036 -1.602 -47.492 23.542 1.00153.45 O
ANISOU 1862 O ALA A1036 19594 17683 21029 373 -342 -333 O
ATOM 1863 CB ALA A1036 1.550 -47.930 23.278 1.00152.84 C
ANISOU 1863 CB ALA A1036 19409 17454 21210 460 -310 -395 C
ATOM 1864 N ALA A1037 -1.136 -49.646 23.997 1.00159.09 N
ANISOU 1864 N ALA A1037 20292 18264 21893 369 -433 -329 N
ATOM 1865 CA ALA A1037 -2.469 -50.107 23.608 1.00160.25 C
ANISOU 1865 CA ALA A1037 20488 18442 21958 338 -440 -332 C
ATOM 1866 C ALA A1037 -3.530 -49.636 24.604 1.00159.85 C
ANISOU 1866 C ALA A1037 20462 18462 21812 292 -488 -261 C
ATOM 1867 O ALA A1037 -4.621 -49.226 24.208 1.00163.57 O
ANISOU 1867 O ALA A1037 20972 19001 22179 272 -463 -263 O
ATOM 1868 CB ALA A1037 -2.495 -51.619 23.461 1.00160.98 C
ANISOU 1868 CB ALA A1037 20584 18453 22126 334 -486 -348 C
ATOM 1869 N LEU A1038 -3.202 -49.680 25.892 1.00156.56 N
ANISOU 1869 N LEU A1038 20023 18030 21432 275 -556 -199 N
ATOM 1870 CA LEU A1038 -4.117 -49.191 26.918 1.00156.84 C
ANISOU 1870 CA LEU A1038 20078 18135 21381 232 -601 -133 C
ATOM 1871 C LEU A1038 -4.212 -47.668 26.935 1.00158.80 C
ANISOU 1871 C LEU A1038 20326 18465 21548 239 -550 -129 C
ATOM 1872 O LEU A1038 -5.213 -47.120 27.398 1.00161.20 O
ANISOU 1872 O LEU A1038 20653 18841 21753 207 -562 -93 O
ATOM 1873 CB LEU A1038 -3.707 -49.715 28.293 1.00156.28 C
ANISOU 1873 CB LEU A1038 19984 18023 21373 209 -690 -68 C
ATOM 1874 CG LEU A1038 -3.699 -51.236 28.448 1.00154.20 C
ANISOU 1874 CG LEU A1038 19721 17678 21190 194 -755 -59 C
ATOM 1875 CD1 LEU A1038 -2.866 -51.648 29.653 1.00154.50 C
ANISOU 1875 CD1 LEU A1038 19723 17661 21318 185 -833 -6 C
ATOM 1876 CD2 LEU A1038 -5.104 -51.814 28.532 1.00152.18 C
ANISOU 1876 CD2 LEU A1038 19509 17456 20857 149 -790 -34 C
ATOM 1877 N ASP A1039 -3.184 -46.986 26.432 1.00159.87 N
ANISOU 1877 N ASP A1039 20431 18588 21723 280 -494 -166 N
ATOM 1878 CA ASP A1039 -3.176 -45.526 26.401 1.00158.63 C
ANISOU 1878 CA ASP A1039 20271 18503 21498 290 -446 -165 C
ATOM 1879 C ASP A1039 -3.949 -44.962 25.211 1.00161.83 C
ANISOU 1879 C ASP A1039 20709 18966 21813 295 -373 -210 C
ATOM 1880 O ASP A1039 -4.461 -43.843 25.287 1.00164.40 O
ANISOU 1880 O ASP A1039 21046 19366 22053 287 -349 -197 O
ATOM 1881 CB ASP A1039 -1.738 -45.006 26.393 1.00153.87 C
ANISOU 1881 CB ASP A1039 19623 17865 20977 329 -419 -181 C
ATOM 1882 CG ASP A1039 -1.651 -43.523 26.684 1.00151.62 C
ANISOU 1882 CG ASP A1039 19330 17647 20632 334 -390 -164 C
ATOM 1883 OD1 ASP A1039 -1.988 -43.116 27.816 1.00154.44 O
ANISOU 1883 OD1 ASP A1039 19688 18040 20952 307 -439 -108 O
ATOM 1884 OD2 ASP A1039 -1.240 -42.762 25.783 1.00151.29 O
ANISOU 1884 OD2 ASP A1039 19280 17624 20579 364 -319 -207 O
ATOM 1885 N ALA A1040 -4.037 -45.726 24.123 1.00161.33 N
ANISOU 1885 N ALA A1040 20661 18868 21770 307 -341 -262 N
ATOM 1886 CA ALA A1040 -4.691 -45.246 22.905 1.00159.34 C
ANISOU 1886 CA ALA A1040 20439 18666 21438 312 -271 -308 C
ATOM 1887 C ALA A1040 -6.215 -45.254 23.013 1.00163.29 C
ANISOU 1887 C ALA A1040 20983 19226 21832 271 -292 -282 C
ATOM 1888 O ALA A1040 -6.886 -44.448 22.369 1.00162.84 O
ANISOU 1888 O ALA A1040 20950 19233 21690 267 -245 -298 O
ATOM 1889 CB ALA A1040 -4.235 -46.051 21.700 1.00159.17 C
ANISOU 1889 CB ALA A1040 20418 18587 21471 338 -229 -376 C
ATOM 1890 N GLN A1041 -6.762 -46.163 23.812 1.00162.66 N
ANISOU 1890 N GLN A1041 20915 19126 21762 239 -364 -241 N
ATOM 1891 CA GLN A1041 -8.217 -46.255 23.956 1.00166.42 C
ANISOU 1891 CA GLN A1041 21431 19658 22143 198 -388 -213 C
ATOM 1892 C GLN A1041 -8.782 -45.087 24.774 1.00168.00 C
ANISOU 1892 C GLN A1041 21632 19940 22261 178 -396 -167 C
ATOM 1893 O GLN A1041 -9.845 -44.562 24.454 1.00176.68 O
ANISOU 1893 O GLN A1041 22760 21105 23265 161 -375 -166 O
ATOM 1894 CB GLN A1041 -8.620 -47.597 24.549 1.00165.73 C
ANISOU 1894 CB GLN A1041 21354 19525 22092 168 -462 -182 C
ATOM 1895 CG GLN A1041 -7.985 -47.918 25.891 1.00168.31 C
ANISOU 1895 CG GLN A1041 21650 19815 22485 158 -533 -128 C
ATOM 1896 CD GLN A1041 -8.620 -49.101 26.585 1.00172.04 C
ANISOU 1896 CD GLN A1041 22136 20259 22970 118 -613 -85 C
ATOM 1897 OE1 GLN A1041 -8.844 -50.151 25.982 1.00171.54 O
ANISOU 1897 OE1 GLN A1041 22090 20149 22938 115 -622 -110 O
ATOM 1898 NE2 GLN A1041 -8.899 -48.943 27.872 1.00176.83 N
ANISOU 1898 NE2 GLN A1041 22737 20896 23554 84 -672 -19 N
ATOM 1899 N LYS A1042 -8.065 -44.679 25.817 1.00166.84 N
ANISOU 1899 N LYS A1042 21453 19786 22151 182 -427 -130 N
ATOM 1900 CA LYS A1042 -8.494 -43.569 26.659 1.00163.98 C
ANISOU 1900 CA LYS A1042 21089 19498 21718 165 -437 -89 C
ATOM 1901 C LYS A1042 -8.199 -42.231 25.989 1.00160.48 C
ANISOU 1901 C LYS A1042 20639 19098 21239 195 -366 -122 C
ATOM 1902 O LYS A1042 -8.613 -41.980 24.857 1.00150.28 O
ANISOU 1902 O LYS A1042 19368 17828 19904 204 -310 -163 O
ATOM 1903 CB LYS A1042 -7.819 -43.639 28.031 1.00162.17 C
ANISOU 1903 CB LYS A1042 20829 19245 21541 156 -499 -38 C
ATOM 1904 CG LYS A1042 -8.224 -44.845 28.869 1.00161.94 C
ANISOU 1904 CG LYS A1042 20808 19185 21536 118 -578 6 C
ATOM 1905 CD LYS A1042 -7.513 -44.844 30.216 1.00160.83 C
ANISOU 1905 CD LYS A1042 20639 19025 21447 107 -639 58 C
ATOM 1906 CE LYS A1042 -7.864 -46.075 31.037 1.00160.64 C
ANISOU 1906 CE LYS A1042 20620 18965 21449 67 -721 105 C
ATOM 1907 NZ LYS A1042 -7.179 -46.074 32.360 1.00160.22 N
ANISOU 1907 NZ LYS A1042 20540 18894 21443 52 -783 159 N
ATOM 1908 N LYS A1059 -18.712 -50.654 21.163 1.00186.72 N
ANISOU 1908 N LYS A1059 24323 22427 24196 -77 -518 -165 N
ATOM 1909 CA LYS A1059 -18.803 -52.101 20.975 1.00184.75 C
ANISOU 1909 CA LYS A1059 24089 22108 24000 -90 -562 -171 C
ATOM 1910 C LYS A1059 -17.738 -52.592 20.001 1.00184.37 C
ANISOU 1910 C LYS A1059 24036 21984 24031 -49 -525 -239 C
ATOM 1911 O LYS A1059 -16.950 -53.480 20.334 1.00187.92 O
ANISOU 1911 O LYS A1059 24468 22358 24575 -39 -562 -241 O
ATOM 1912 CB LYS A1059 -20.204 -52.510 20.505 1.00184.74 C
ANISOU 1912 CB LYS A1059 24128 22139 23925 -127 -575 -163 C
ATOM 1913 CG LYS A1059 -21.293 -52.322 21.551 1.00182.58 C
ANISOU 1913 CG LYS A1059 23858 21930 23584 -173 -624 -93 C
ATOM 1914 CD LYS A1059 -22.680 -52.399 20.934 1.00182.74 C
ANISOU 1914 CD LYS A1059 23916 21997 23520 -204 -619 -91 C
ATOM 1915 CE LYS A1059 -23.753 -52.027 21.947 1.00182.04 C
ANISOU 1915 CE LYS A1059 23825 21983 23358 -247 -657 -25 C
ATOM 1916 NZ LYS A1059 -25.110 -51.983 21.332 1.00181.41 N
ANISOU 1916 NZ LYS A1059 23780 21953 23195 -275 -648 -24 N
ATOM 1917 N ASP A1060 -17.715 -52.013 18.804 1.00188.36 N
ANISOU 1917 N ASP A1060 24558 22511 24502 -27 -452 -295 N
ATOM 1918 CA ASP A1060 -16.637 -52.269 17.854 1.00189.90 C
ANISOU 1918 CA ASP A1060 24744 22646 24765 15 -404 -364 C
ATOM 1919 C ASP A1060 -15.299 -51.747 18.375 1.00188.46 C
ANISOU 1919 C ASP A1060 24515 22440 24650 50 -390 -366 C
ATOM 1920 O ASP A1060 -14.254 -52.340 18.111 1.00189.32 O
ANISOU 1920 O ASP A1060 24605 22477 24851 80 -383 -404 O
ATOM 1921 CB ASP A1060 -16.952 -51.644 16.497 1.00189.46 C
ANISOU 1921 CB ASP A1060 24715 22629 24643 26 -328 -419 C
ATOM 1922 CG ASP A1060 -18.189 -52.236 15.856 1.00191.25 C
ANISOU 1922 CG ASP A1060 24988 22869 24810 -6 -340 -424 C
ATOM 1923 OD1 ASP A1060 -19.290 -52.093 16.430 1.00195.53 O
ANISOU 1923 OD1 ASP A1060 25544 23461 25286 -44 -378 -371 O
ATOM 1924 OD2 ASP A1060 -18.065 -52.834 14.767 1.00189.04 O
ANISOU 1924 OD2 ASP A1060 24729 22550 24547 5 -311 -482 O
ATOM 1925 N PHE A1061 -15.341 -50.643 19.115 1.00187.32 N
ANISOU 1925 N PHE A1061 24353 22356 24463 47 -386 -326 N
ATOM 1926 CA PHE A1061 -14.133 -50.044 19.668 1.00187.44 C
ANISOU 1926 CA PHE A1061 24326 22357 24537 78 -375 -322 C
ATOM 1927 C PHE A1061 -13.547 -50.892 20.796 1.00190.79 C
ANISOU 1927 C PHE A1061 24723 22719 25048 72 -448 -282 C
ATOM 1928 O PHE A1061 -12.327 -51.001 20.926 1.00201.36 O
ANISOU 1928 O PHE A1061 26029 24005 26476 103 -443 -300 O
ATOM 1929 CB PHE A1061 -14.416 -48.615 20.136 1.00187.40 C
ANISOU 1929 CB PHE A1061 24311 22434 24457 74 -353 -290 C
ATOM 1930 CG PHE A1061 -13.529 -48.150 21.246 1.00184.66 C
ANISOU 1930 CG PHE A1061 23924 22080 24158 86 -377 -255 C
ATOM 1931 CD1 PHE A1061 -12.220 -47.746 20.992 1.00184.02 C
ANISOU 1931 CD1 PHE A1061 23812 21966 24143 127 -337 -288 C
ATOM 1932 CD2 PHE A1061 -14.002 -48.115 22.556 1.00185.02 C
ANISOU 1932 CD2 PHE A1061 23962 22153 24182 54 -439 -188 C
ATOM 1933 CE1 PHE A1061 -11.400 -47.316 22.023 1.00185.95 C
ANISOU 1933 CE1 PHE A1061 24018 22203 24433 137 -362 -255 C
ATOM 1934 CE2 PHE A1061 -13.187 -47.685 23.593 1.00186.68 C
ANISOU 1934 CE2 PHE A1061 24137 22359 24436 63 -463 -155 C
ATOM 1935 CZ PHE A1061 -11.883 -47.284 23.326 1.00188.69 C
ANISOU 1935 CZ PHE A1061 24361 22577 24757 105 -425 -188 C
ATOM 1936 N ARG A1062 -14.411 -51.483 21.617 1.00189.15 N
ANISOU 1936 N ARG A1062 24529 22521 24818 30 -516 -227 N
ATOM 1937 CA ARG A1062 -13.941 -52.270 22.754 1.00184.04 C
ANISOU 1937 CA ARG A1062 23858 21822 24248 17 -592 -182 C
ATOM 1938 C ARG A1062 -13.434 -53.644 22.319 1.00181.26 C
ANISOU 1938 C ARG A1062 23506 21373 23992 29 -618 -214 C
ATOM 1939 O ARG A1062 -12.420 -54.122 22.836 1.00176.19 O
ANISOU 1939 O ARG A1062 22832 20665 23448 45 -650 -208 O
ATOM 1940 CB ARG A1062 -15.032 -52.396 23.810 1.00182.03 C
ANISOU 1940 CB ARG A1062 23616 21614 23932 -35 -656 -109 C
ATOM 1941 CG ARG A1062 -14.594 -53.117 25.074 1.00181.46 C
ANISOU 1941 CG ARG A1062 23520 21497 23929 -54 -738 -53 C
ATOM 1942 CD ARG A1062 -15.515 -52.799 26.241 1.00184.14 C
ANISOU 1942 CD ARG A1062 23863 21906 24194 -102 -787 20 C
ATOM 1943 NE ARG A1062 -15.395 -51.405 26.669 1.00183.55 N
ANISOU 1943 NE ARG A1062 23773 21902 24066 -93 -751 32 N
ATOM 1944 CZ ARG A1062 -14.545 -50.958 27.590 1.00180.85 C
ANISOU 1944 CZ ARG A1062 23398 21556 23763 -84 -770 60 C
ATOM 1945 NH1 ARG A1062 -13.717 -51.787 28.219 1.00180.21 N
ANISOU 1945 NH1 ARG A1062 23294 21402 23777 -85 -825 81 N
ATOM 1946 NH2 ARG A1062 -14.527 -49.668 27.891 1.00175.04 N
ANISOU 1946 NH2 ARG A1062 22651 20886 22971 -76 -734 66 N
ATOM 1947 N HIS A1063 -14.130 -54.277 21.376 1.00180.88 N
ANISOU 1947 N HIS A1063 23493 21314 23919 20 -605 -249 N
ATOM 1948 CA HIS A1063 -13.727 -55.600 20.906 1.00177.74 C
ANISOU 1948 CA HIS A1063 23098 20825 23610 31 -630 -285 C
ATOM 1949 C HIS A1063 -12.440 -55.578 20.090 1.00173.62 C
ANISOU 1949 C HIS A1063 22552 20247 23168 84 -572 -356 C
ATOM 1950 O HIS A1063 -11.767 -56.599 19.987 1.00173.56 O
ANISOU 1950 O HIS A1063 22530 20153 23260 100 -599 -381 O
ATOM 1951 CB HIS A1063 -14.852 -56.262 20.108 1.00180.02 C
ANISOU 1951 CB HIS A1063 23433 21119 23846 6 -632 -304 C
ATOM 1952 CG HIS A1063 -14.660 -57.734 19.905 1.00183.54 C
ANISOU 1952 CG HIS A1063 23884 21474 24380 4 -680 -323 C
ATOM 1953 ND1 HIS A1063 -14.990 -58.667 20.864 1.00187.93 N
ANISOU 1953 ND1 HIS A1063 24438 21994 24971 -31 -770 -265 N
ATOM 1954 CD2 HIS A1063 -14.168 -58.434 18.854 1.00182.44 C
ANISOU 1954 CD2 HIS A1063 23751 21268 24299 34 -650 -396 C
ATOM 1955 CE1 HIS A1063 -14.710 -59.877 20.414 1.00186.07 C
ANISOU 1955 CE1 HIS A1063 24209 21674 24817 -22 -797 -299 C
ATOM 1956 NE2 HIS A1063 -14.211 -59.764 19.197 1.00182.53 N
ANISOU 1956 NE2 HIS A1063 23765 21205 24384 17 -725 -381 N
ATOM 1957 N GLY A1064 -12.102 -54.428 19.513 1.00170.28 N
ANISOU 1957 N GLY A1064 22123 19873 22704 110 -495 -389 N
ATOM 1958 CA GLY A1064 -10.847 -54.293 18.776 1.00168.02 C
ANISOU 1958 CA GLY A1064 21810 19542 22489 160 -436 -455 C
ATOM 1959 C GLY A1064 -9.633 -54.462 19.675 1.00164.41 C
ANISOU 1959 C GLY A1064 21304 19027 22138 181 -472 -434 C
ATOM 1960 O GLY A1064 -8.696 -55.196 19.351 1.00160.46 O
ANISOU 1960 O GLY A1064 20781 18446 21739 211 -470 -476 O
ATOM 1961 N PHE A1065 -9.652 -53.778 20.814 1.00162.95 N
ANISOU 1961 N PHE A1065 21101 18882 21930 165 -504 -369 N
ATOM 1962 CA PHE A1065 -8.573 -53.908 21.791 1.00162.18 C
ANISOU 1962 CA PHE A1065 20959 18735 21928 179 -546 -339 C
ATOM 1963 C PHE A1065 -8.631 -55.226 22.552 1.00163.92 C
ANISOU 1963 C PHE A1065 21176 18886 22221 155 -638 -301 C
ATOM 1964 O PHE A1065 -7.603 -55.690 23.041 1.00160.30 O
ANISOU 1964 O PHE A1065 20680 18357 21869 173 -671 -296 O
ATOM 1965 CB PHE A1065 -8.583 -52.737 22.768 1.00157.01 C
ANISOU 1965 CB PHE A1065 20288 18147 21221 167 -553 -282 C
ATOM 1966 CG PHE A1065 -8.176 -51.438 22.159 1.00156.05 C
ANISOU 1966 CG PHE A1065 20157 18076 21058 198 -470 -317 C
ATOM 1967 CD1 PHE A1065 -6.832 -51.097 22.055 1.00155.97 C
ANISOU 1967 CD1 PHE A1065 20106 18029 21126 239 -438 -345 C
ATOM 1968 CD2 PHE A1065 -9.136 -50.558 21.671 1.00157.87 C
ANISOU 1968 CD2 PHE A1065 20419 18391 21173 184 -426 -321 C
ATOM 1969 CE1 PHE A1065 -6.449 -49.894 21.480 1.00156.41 C
ANISOU 1969 CE1 PHE A1065 20153 18132 21144 265 -363 -375 C
ATOM 1970 CE2 PHE A1065 -8.761 -49.351 21.098 1.00160.37 C
ANISOU 1970 CE2 PHE A1065 20728 18755 21453 210 -353 -350 C
ATOM 1971 CZ PHE A1065 -7.416 -49.014 21.008 1.00158.64 C
ANISOU 1971 CZ PHE A1065 20468 18499 21310 250 -321 -376 C
ATOM 1972 N ASP A1066 -9.818 -55.826 22.658 1.00167.39 N
ANISOU 1972 N ASP A1066 21651 19342 22606 113 -680 -273 N
ATOM 1973 CA ASP A1066 -9.948 -57.126 23.320 1.00167.62 C
ANISOU 1973 CA ASP A1066 21680 19306 22703 87 -770 -236 C
ATOM 1974 C ASP A1066 -9.115 -58.206 22.633 1.00166.15 C
ANISOU 1974 C ASP A1066 21481 19017 22634 120 -771 -296 C
ATOM 1975 O ASP A1066 -8.576 -59.088 23.294 1.00168.90 O
ANISOU 1975 O ASP A1066 21805 19290 23079 117 -839 -271 O
ATOM 1976 CB ASP A1066 -11.413 -57.549 23.391 1.00167.56 C
ANISOU 1976 CB ASP A1066 21716 19338 22610 37 -807 -202 C
ATOM 1977 CG ASP A1066 -12.102 -57.055 24.647 1.00165.94 C
ANISOU 1977 CG ASP A1066 21513 19201 22337 -8 -857 -117 C
ATOM 1978 OD1 ASP A1066 -11.858 -55.897 25.056 1.00165.29 O
ANISOU 1978 OD1 ASP A1066 21414 19176 22213 1 -826 -101 O
ATOM 1979 OD2 ASP A1066 -12.901 -57.823 25.223 1.00161.04 O
ANISOU 1979 OD2 ASP A1066 20909 18578 21702 -52 -926 -68 O
ATOM 1980 N ILE A1067 -8.989 -58.117 21.314 1.00160.55 N
ANISOU 1980 N ILE A1067 20784 18303 21915 152 -695 -375 N
ATOM 1981 CA ILE A1067 -8.164 -59.061 20.575 1.00160.27 C
ANISOU 1981 CA ILE A1067 20734 18174 21987 187 -685 -442 C
ATOM 1982 C ILE A1067 -6.696 -58.625 20.601 1.00166.27 C
ANISOU 1982 C ILE A1067 21443 18897 22834 235 -648 -471 C
ATOM 1983 O ILE A1067 -5.795 -59.464 20.710 1.00169.31 O
ANISOU 1983 O ILE A1067 21797 19193 23342 258 -679 -491 O
ATOM 1984 CB ILE A1067 -8.679 -59.234 19.139 1.00155.60 C
ANISOU 1984 CB ILE A1067 20180 17593 21348 198 -621 -517 C
ATOM 1985 CG1 ILE A1067 -10.166 -59.605 19.149 1.00152.08 C
ANISOU 1985 CG1 ILE A1067 19784 17187 20812 148 -658 -483 C
ATOM 1986 CG2 ILE A1067 -7.862 -60.281 18.393 1.00154.21 C
ANISOU 1986 CG2 ILE A1067 19990 17319 21285 233 -612 -589 C
ATOM 1987 CD1 ILE A1067 -10.842 -59.525 17.795 1.00151.45 C
ANISOU 1987 CD1 ILE A1067 19747 17140 20659 151 -593 -545 C
ATOM 1988 N LEU A1068 -6.453 -57.320 20.508 1.00167.73 N
ANISOU 1988 N LEU A1068 21619 19151 22961 250 -586 -473 N
ATOM 1989 CA LEU A1068 -5.084 -56.813 20.435 1.00165.20 C
ANISOU 1989 CA LEU A1068 21250 18802 22715 295 -544 -504 C
ATOM 1990 C LEU A1068 -4.339 -56.988 21.760 1.00162.60 C
ANISOU 1990 C LEU A1068 20880 18430 22471 292 -616 -443 C
ATOM 1991 O LEU A1068 -3.267 -57.595 21.798 1.00165.97 O
ANISOU 1991 O LEU A1068 21268 18774 23019 322 -631 -467 O
ATOM 1992 CB LEU A1068 -5.075 -55.347 20.006 1.00166.09 C
ANISOU 1992 CB LEU A1068 21365 19002 22738 308 -462 -517 C
ATOM 1993 CG LEU A1068 -3.685 -54.754 19.763 1.00163.83 C
ANISOU 1993 CG LEU A1068 21032 18694 22522 356 -408 -555 C
ATOM 1994 CD1 LEU A1068 -3.221 -54.996 18.335 1.00162.76 C
ANISOU 1994 CD1 LEU A1068 20897 18531 22413 392 -330 -649 C
ATOM 1995 CD2 LEU A1068 -3.659 -53.270 20.082 1.00163.56 C
ANISOU 1995 CD2 LEU A1068 20990 18742 22411 355 -371 -524 C
ATOM 1996 N VAL A1069 -4.915 -56.477 22.839 1.00153.92 N
ANISOU 1996 N VAL A1069 19787 17385 21309 254 -663 -364 N
ATOM 1997 CA VAL A1069 -4.275 -56.578 24.147 1.00151.25 C
ANISOU 1997 CA VAL A1069 19414 17015 21041 245 -734 -300 C
ATOM 1998 C VAL A1069 -4.194 -58.034 24.599 1.00152.98 C
ANISOU 1998 C VAL A1069 19626 17143 21356 229 -821 -280 C
ATOM 1999 O VAL A1069 -3.236 -58.431 25.268 1.00152.17 O
ANISOU 1999 O VAL A1069 19483 16974 21361 240 -869 -260 O
ATOM 2000 CB VAL A1069 -4.990 -55.692 25.182 1.00150.06 C
ANISOU 2000 CB VAL A1069 19275 16951 20791 205 -762 -224 C
ATOM 2001 CG1 VAL A1069 -4.223 -55.659 26.490 1.00148.91 C
ANISOU 2001 CG1 VAL A1069 19090 16775 20713 197 -828 -162 C
ATOM 2002 CG2 VAL A1069 -5.136 -54.277 24.645 1.00147.05 C
ANISOU 2002 CG2 VAL A1069 18901 16655 20314 221 -677 -248 C
ATOM 2003 N GLY A1070 -5.183 -58.837 24.214 1.00154.57 N
ANISOU 2003 N GLY A1070 19867 17340 21524 203 -844 -287 N
ATOM 2004 CA GLY A1070 -5.151 -60.265 24.534 1.00159.96 C
ANISOU 2004 CA GLY A1070 20546 17933 22299 188 -927 -272 C
ATOM 2005 C GLY A1070 -4.028 -60.994 23.815 1.00162.61 C
ANISOU 2005 C GLY A1070 20850 18169 22766 238 -907 -344 C
ATOM 2006 O GLY A1070 -3.333 -61.821 24.409 1.00162.88 O
ANISOU 2006 O GLY A1070 20852 18118 22916 242 -974 -325 O
ATOM 2007 N GLN A1071 -3.844 -60.689 22.533 1.00163.47 N
ANISOU 2007 N GLN A1071 20966 18289 22856 276 -815 -429 N
ATOM 2008 CA GLN A1071 -2.764 -61.311 21.766 1.00163.20 C
ANISOU 2008 CA GLN A1071 20900 18167 22941 326 -785 -506 C
ATOM 2009 C GLN A1071 -1.390 -60.885 22.276 1.00159.70 C
ANISOU 2009 C GLN A1071 20398 17688 22590 360 -780 -501 C
ATOM 2010 O GLN A1071 -0.430 -61.645 22.161 1.00158.22 O
ANISOU 2010 O GLN A1071 20174 17409 22533 392 -796 -536 O
ATOM 2011 CB GLN A1071 -2.897 -60.994 20.284 1.00166.10 C
ANISOU 2011 CB GLN A1071 21290 18564 23256 355 -683 -597 C
ATOM 2012 CG GLN A1071 -3.941 -61.816 19.551 1.00168.82 C
ANISOU 2012 CG GLN A1071 21684 18903 23558 334 -690 -626 C
ATOM 2013 CD GLN A1071 -4.147 -61.349 18.124 1.00168.63 C
ANISOU 2013 CD GLN A1071 21686 18923 23464 356 -587 -709 C
ATOM 2014 OE1 GLN A1071 -3.987 -60.166 17.808 1.00165.19 O
ANISOU 2014 OE1 GLN A1071 21246 18557 22960 369 -515 -720 O
ATOM 2015 NE2 GLN A1071 -4.491 -62.285 17.248 1.00170.40 N
ANISOU 2015 NE2 GLN A1071 21936 19104 23705 359 -582 -767 N
ATOM 2016 N ILE A1072 -1.297 -59.681 22.838 1.00157.48 N
ANISOU 2016 N ILE A1072 20108 17480 22246 354 -759 -458 N
ATOM 2017 CA ILE A1072 -0.053 -59.241 23.467 1.00157.75 C
ANISOU 2017 CA ILE A1072 20089 17485 22364 380 -765 -441 C
ATOM 2018 C ILE A1072 0.248 -60.112 24.691 1.00159.36 C
ANISOU 2018 C ILE A1072 20268 17617 22663 357 -877 -373 C
ATOM 2019 O ILE A1072 1.390 -60.533 24.897 1.00159.77 O
ANISOU 2019 O ILE A1072 20273 17589 22844 386 -898 -386 O
ATOM 2020 CB ILE A1072 -0.112 -57.750 23.837 1.00153.48 C
ANISOU 2020 CB ILE A1072 19547 17039 21727 374 -724 -406 C
ATOM 2021 CG1 ILE A1072 -0.098 -56.887 22.572 1.00148.15 C
ANISOU 2021 CG1 ILE A1072 18884 16420 20985 405 -611 -479 C
ATOM 2022 CG2 ILE A1072 1.048 -57.375 24.748 1.00153.69 C
ANISOU 2022 CG2 ILE A1072 19522 17035 21838 389 -752 -369 C
ATOM 2023 CD1 ILE A1072 -0.368 -55.417 22.826 1.00149.42 C
ANISOU 2023 CD1 ILE A1072 19053 16681 21038 395 -570 -447 C
ATOM 2024 N ASP A1073 -0.776 -60.396 25.493 1.00159.14 N
ANISOU 2024 N ASP A1073 20273 17618 22574 302 -949 -302 N
ATOM 2025 CA ASP A1073 -0.596 -61.284 26.637 1.00161.49 C
ANISOU 2025 CA ASP A1073 20553 17851 22956 273 -1060 -234 C
ATOM 2026 C ASP A1073 -0.306 -62.717 26.209 1.00163.56 C
ANISOU 2026 C ASP A1073 20805 18003 23336 288 -1100 -274 C
ATOM 2027 O ASP A1073 0.395 -63.437 26.917 1.00166.43 O
ANISOU 2027 O ASP A1073 21134 18285 23817 287 -1175 -243 O
ATOM 2028 CB ASP A1073 -1.823 -61.245 27.546 1.00158.41 C
ANISOU 2028 CB ASP A1073 20201 17524 22464 208 -1124 -150 C
ATOM 2029 CG ASP A1073 -1.931 -59.953 28.317 1.00156.23 C
ANISOU 2029 CG ASP A1073 19923 17339 22099 191 -1109 -97 C
ATOM 2030 OD1 ASP A1073 -0.907 -59.496 28.863 1.00156.83 O
ANISOU 2030 OD1 ASP A1073 19957 17395 22235 210 -1114 -80 O
ATOM 2031 OD2 ASP A1073 -3.043 -59.397 28.382 1.00157.25 O
ANISOU 2031 OD2 ASP A1073 20092 17558 22100 158 -1094 -72 O
ATOM 2032 N ASP A1074 -0.842 -63.131 25.062 1.00163.84 N
ANISOU 2032 N ASP A1074 20872 18037 23343 300 -1053 -342 N
ATOM 2033 CA ASP A1074 -0.551 -64.466 24.547 1.00165.49 C
ANISOU 2033 CA ASP A1074 21072 18141 23665 318 -1084 -390 C
ATOM 2034 C ASP A1074 0.928 -64.613 24.209 1.00166.57 C
ANISOU 2034 C ASP A1074 21152 18198 23940 377 -1054 -449 C
ATOM 2035 O ASP A1074 1.523 -65.665 24.434 1.00165.21 O
ANISOU 2035 O ASP A1074 20950 17923 23899 387 -1116 -453 O
ATOM 2036 CB ASP A1074 -1.420 -64.776 23.330 1.00165.30 C
ANISOU 2036 CB ASP A1074 21095 18138 23573 320 -1031 -456 C
ATOM 2037 CG ASP A1074 -2.761 -65.373 23.704 1.00164.22 C
ANISOU 2037 CG ASP A1074 21007 18023 23367 263 -1099 -402 C
ATOM 2038 OD1 ASP A1074 -3.101 -65.394 24.907 1.00162.20 O
ANISOU 2038 OD1 ASP A1074 20750 17783 23095 218 -1179 -311 O
ATOM 2039 OD2 ASP A1074 -3.476 -65.835 22.788 1.00162.16 O
ANISOU 2039 OD2 ASP A1074 20782 17763 23066 261 -1074 -451 O
ATOM 2040 N ALA A1075 1.529 -63.552 23.680 1.00164.51 N
ANISOU 2040 N ALA A1075 20873 17983 23650 414 -961 -492 N
ATOM 2041 CA ALA A1075 2.958 -63.578 23.385 1.00167.38 C
ANISOU 2041 CA ALA A1075 21179 18280 24139 469 -928 -545 C
ATOM 2042 C ALA A1075 3.787 -63.214 24.614 1.00172.34 C
ANISOU 2042 C ALA A1075 21761 18888 24830 464 -983 -474 C
ATOM 2043 O ALA A1075 4.928 -63.668 24.741 1.00173.32 O
ANISOU 2043 O ALA A1075 21833 18926 25093 498 -1003 -493 O
ATOM 2044 CB ALA A1075 3.289 -62.666 22.214 1.00170.95 C
ANISOU 2044 CB ALA A1075 21629 18784 24539 510 -803 -626 C
ATOM 2045 N LEU A1076 3.231 -62.392 25.506 1.00175.14 N
ANISOU 2045 N LEU A1076 22135 19323 25087 424 -1008 -394 N
ATOM 2046 CA LEU A1076 3.961 -61.969 26.698 1.00175.75 C
ANISOU 2046 CA LEU A1076 22174 19392 25212 416 -1060 -324 C
ATOM 2047 C LEU A1076 4.241 -63.141 27.639 1.00178.28 C
ANISOU 2047 C LEU A1076 22473 19617 25650 393 -1178 -270 C
ATOM 2048 O LEU A1076 5.345 -63.260 28.179 1.00177.63 O
ANISOU 2048 O LEU A1076 22339 19470 25682 413 -1213 -254 O
ATOM 2049 CB LEU A1076 3.202 -60.865 27.431 1.00171.38 C
ANISOU 2049 CB LEU A1076 21650 18948 24519 374 -1061 -254 C
ATOM 2050 CG LEU A1076 3.962 -60.123 28.530 1.00171.03 C
ANISOU 2050 CG LEU A1076 21569 18914 24500 369 -1092 -191 C
ATOM 2051 CD1 LEU A1076 5.028 -59.200 27.953 1.00171.53 C
ANISOU 2051 CD1 LEU A1076 21595 18987 24592 423 -1004 -244 C
ATOM 2052 CD2 LEU A1076 2.992 -59.337 29.397 1.00168.94 C
ANISOU 2052 CD2 LEU A1076 21341 18749 24101 317 -1117 -114 C
ATOM 2053 N LYS A1077 3.252 -64.010 27.825 1.00177.68 N
ANISOU 2053 N LYS A1077 22434 19529 25546 352 -1242 -240 N
ATOM 2054 CA LYS A1077 3.439 -65.184 28.680 1.00177.61 C
ANISOU 2054 CA LYS A1077 22408 19429 25647 326 -1359 -187 C
ATOM 2055 C LYS A1077 4.434 -66.176 28.077 1.00180.57 C
ANISOU 2055 C LYS A1077 22740 19683 26185 375 -1363 -256 C
ATOM 2056 O LYS A1077 5.160 -66.843 28.808 1.00187.11 O
ANISOU 2056 O LYS A1077 23529 20425 27139 374 -1445 -219 O
ATOM 2057 CB LYS A1077 2.105 -65.857 28.995 1.00176.40 C
ANISOU 2057 CB LYS A1077 22306 19297 25422 268 -1425 -138 C
ATOM 2058 CG LYS A1077 1.369 -66.433 27.794 1.00180.08 C
ANISOU 2058 CG LYS A1077 22809 19757 25855 279 -1381 -211 C
ATOM 2059 CD LYS A1077 0.069 -67.093 28.215 1.00183.20 C
ANISOU 2059 CD LYS A1077 23252 20173 26183 217 -1454 -153 C
ATOM 2060 CE LYS A1077 -0.610 -67.777 27.040 1.00185.85 C
ANISOU 2060 CE LYS A1077 23624 20492 26500 228 -1420 -225 C
ATOM 2061 NZ LYS A1077 -1.814 -68.546 27.466 1.00188.95 N
ANISOU 2061 NZ LYS A1077 24058 20891 26843 168 -1500 -167 N
ATOM 2062 N LEU A1078 4.470 -66.262 26.749 1.00177.71 N
ANISOU 2062 N LEU A1078 22386 19315 25821 418 -1276 -355 N
ATOM 2063 CA LEU A1078 5.449 -67.109 26.079 1.00179.16 C
ANISOU 2063 CA LEU A1078 22527 19390 26156 470 -1266 -432 C
ATOM 2064 C LEU A1078 6.862 -66.547 26.186 1.00182.55 C
ANISOU 2064 C LEU A1078 22893 19790 26678 517 -1231 -452 C
ATOM 2065 O LEU A1078 7.830 -67.300 26.072 1.00185.72 O
ANISOU 2065 O LEU A1078 23246 20088 27230 552 -1255 -488 O
ATOM 2066 CB LEU A1078 5.069 -67.334 24.617 1.00173.91 C
ANISOU 2066 CB LEU A1078 21890 18733 25456 500 -1179 -536 C
ATOM 2067 CG LEU A1078 3.760 -68.088 24.360 1.00169.69 C
ANISOU 2067 CG LEU A1078 21413 18207 24853 461 -1215 -530 C
ATOM 2068 CD1 LEU A1078 3.393 -68.061 22.884 1.00163.73 C
ANISOU 2068 CD1 LEU A1078 20689 17479 24043 490 -1116 -632 C
ATOM 2069 CD2 LEU A1078 3.799 -69.518 24.879 1.00169.70 C
ANISOU 2069 CD2 LEU A1078 21403 18099 24977 444 -1329 -502 C
ATOM 2070 N ALA A1079 6.988 -65.237 26.397 1.00184.29 N
ANISOU 2070 N ALA A1079 23112 20098 26811 517 -1177 -429 N
ATOM 2071 CA ALA A1079 8.305 -64.619 26.573 1.00186.87 C
ANISOU 2071 CA ALA A1079 23381 20404 27219 556 -1147 -438 C
ATOM 2072 C ALA A1079 8.842 -64.825 27.988 1.00190.82 C
ANISOU 2072 C ALA A1079 23846 20855 27800 530 -1254 -346 C
ATOM 2073 O ALA A1079 10.049 -65.021 28.169 1.00188.81 O
ANISOU 2073 O ALA A1079 23534 20526 27681 565 -1269 -357 O
ATOM 2074 CB ALA A1079 8.256 -63.142 26.219 1.00187.54 C
ANISOU 2074 CB ALA A1079 23476 20598 27182 567 -1048 -451 C
ATOM 2075 N ASN A1080 7.956 -64.787 28.985 1.00193.83 N
ANISOU 2075 N ASN A1080 24264 21282 28102 469 -1330 -254 N
ATOM 2076 CA ASN A1080 8.373 -65.011 30.371 1.00193.54 C
ANISOU 2076 CA ASN A1080 24200 21203 28132 436 -1438 -160 C
ATOM 2077 C ASN A1080 8.794 -66.458 30.622 1.00193.19 C
ANISOU 2077 C ASN A1080 24127 21031 28244 436 -1532 -154 C
ATOM 2078 O ASN A1080 9.617 -66.716 31.501 1.00197.51 O
ANISOU 2078 O ASN A1080 24632 21515 28899 432 -1606 -104 O
ATOM 2079 CB ASN A1080 7.272 -64.592 31.342 1.00194.82 C
ANISOU 2079 CB ASN A1080 24410 21452 28160 367 -1490 -66 C
ATOM 2080 CG ASN A1080 7.190 -63.088 31.514 1.00195.36 C
ANISOU 2080 CG ASN A1080 24488 21631 28108 365 -1423 -48 C
ATOM 2081 OD1 ASN A1080 8.001 -62.487 32.216 1.00195.68 O
ANISOU 2081 OD1 ASN A1080 24493 21670 28184 369 -1438 -11 O
ATOM 2082 ND2 ASN A1080 6.202 -62.472 30.877 1.00199.13 N
ANISOU 2082 ND2 ASN A1080 25013 22202 28444 357 -1352 -75 N
ATOM 2083 N GLU A1081 8.245 -67.387 29.842 1.00191.35 N
ANISOU 2083 N GLU A1081 23918 20760 28025 442 -1529 -207 N
ATOM 2084 CA GLU A1081 8.664 -68.786 29.911 1.00190.75 C
ANISOU 2084 CA GLU A1081 23815 20557 28105 450 -1611 -217 C
ATOM 2085 C GLU A1081 10.034 -69.022 29.276 1.00190.44 C
ANISOU 2085 C GLU A1081 23711 20429 28218 520 -1568 -298 C
ATOM 2086 O GLU A1081 10.709 -69.995 29.612 1.00194.66 O
ANISOU 2086 O GLU A1081 24205 20852 28906 530 -1645 -291 O
ATOM 2087 CB GLU A1081 7.629 -69.698 29.260 1.00188.57 C
ANISOU 2087 CB GLU A1081 23585 20268 27796 434 -1621 -250 C
ATOM 2088 CG GLU A1081 6.365 -69.896 30.080 1.00182.40 C
ANISOU 2088 CG GLU A1081 22856 19536 26910 359 -1700 -158 C
ATOM 2089 CD GLU A1081 5.379 -70.855 29.434 1.00182.64 C
ANISOU 2089 CD GLU A1081 22931 19547 26918 344 -1716 -190 C
ATOM 2090 OE1 GLU A1081 5.229 -70.837 28.191 1.00179.99 O
ANISOU 2090 OE1 GLU A1081 22610 19221 26557 383 -1627 -286 O
ATOM 2091 OE2 GLU A1081 4.741 -71.629 30.176 1.00181.74 O
ANISOU 2091 OE2 GLU A1081 22837 19408 26809 290 -1820 -119 O
ATOM 2092 N GLY A1082 10.440 -68.142 28.365 1.00186.70 N
ANISOU 2092 N GLY A1082 23227 20005 27705 567 -1448 -373 N
ATOM 2093 CA GLY A1082 11.710 -68.285 27.666 1.00188.45 C
ANISOU 2093 CA GLY A1082 23388 20155 28060 635 -1394 -457 C
ATOM 2094 C GLY A1082 11.592 -68.716 26.217 1.00189.65 C
ANISOU 2094 C GLY A1082 23550 20290 28218 679 -1308 -574 C
ATOM 2095 O GLY A1082 12.576 -68.643 25.483 1.00188.84 O
ANISOU 2095 O GLY A1082 23402 20150 28200 737 -1239 -655 O
ATOM 2096 N LYS A1083 10.411 -69.158 25.794 1.00188.85 N
ANISOU 2096 N LYS A1083 23508 20217 28029 651 -1311 -586 N
ATOM 2097 CA LYS A1083 10.200 -69.589 24.411 1.00189.62 C
ANISOU 2097 CA LYS A1083 23622 20302 28123 686 -1233 -697 C
ATOM 2098 C LYS A1083 10.261 -68.377 23.482 1.00186.83 C
ANISOU 2098 C LYS A1083 23279 20047 27661 715 -1097 -758 C
ATOM 2099 O LYS A1083 9.343 -67.559 23.459 1.00186.75 O
ANISOU 2099 O LYS A1083 23319 20143 27493 683 -1062 -728 O
ATOM 2100 CB LYS A1083 8.864 -70.318 24.282 1.00188.94 C
ANISOU 2100 CB LYS A1083 23600 20227 27963 643 -1278 -682 C
ATOM 2101 CG LYS A1083 8.741 -71.524 25.196 1.00191.18 C
ANISOU 2101 CG LYS A1083 23876 20415 28348 609 -1416 -617 C
ATOM 2102 CD LYS A1083 7.297 -71.978 25.332 1.00195.26 C
ANISOU 2102 CD LYS A1083 24461 20969 28761 552 -1466 -574 C
ATOM 2103 CE LYS A1083 7.170 -73.108 26.341 1.00198.08 C
ANISOU 2103 CE LYS A1083 24810 21238 29213 512 -1609 -497 C
ATOM 2104 NZ LYS A1083 5.756 -73.544 26.508 1.00199.71 N
ANISOU 2104 NZ LYS A1083 25081 21483 29317 453 -1661 -450 N
ATOM 2105 N VAL A1084 11.348 -68.262 22.733 1.00185.72 N
ANISOU 2105 N VAL A1084 23088 19870 27606 775 -1022 -842 N
ATOM 2106 CA VAL A1084 11.590 -67.076 21.927 1.00180.44 C
ANISOU 2106 CA VAL A1084 22419 19289 26849 803 -897 -895 C
ATOM 2107 C VAL A1084 10.799 -67.118 20.619 1.00179.07 C
ANISOU 2107 C VAL A1084 22296 19165 26578 809 -811 -979 C
ATOM 2108 O VAL A1084 10.114 -66.152 20.263 1.00178.23 O
ANISOU 2108 O VAL A1084 22232 19166 26320 792 -746 -974 O
ATOM 2109 CB VAL A1084 13.095 -66.883 21.663 1.00179.58 C
ANISOU 2109 CB VAL A1084 22235 19129 26870 861 -849 -948 C
ATOM 2110 CG1 VAL A1084 13.362 -65.522 21.038 1.00173.28 C
ANISOU 2110 CG1 VAL A1084 21435 18430 25975 882 -730 -981 C
ATOM 2111 CG2 VAL A1084 13.877 -67.031 22.958 1.00176.05 C
ANISOU 2111 CG2 VAL A1084 21737 18618 26537 854 -946 -866 C
ATOM 2112 N LYS A1085 10.891 -68.234 19.904 1.00177.65 N
ANISOU 2112 N LYS A1085 22110 18906 26484 834 -813 -1055 N
ATOM 2113 CA LYS A1085 10.304 -68.323 18.570 1.00177.20 C
ANISOU 2113 CA LYS A1085 22094 18885 26348 847 -726 -1148 C
ATOM 2114 C LYS A1085 8.778 -68.308 18.595 1.00179.32 C
ANISOU 2114 C LYS A1085 22442 19223 26469 792 -750 -1105 C
ATOM 2115 O LYS A1085 8.149 -67.663 17.759 1.00177.99 O
ANISOU 2115 O LYS A1085 22316 19141 26170 787 -667 -1142 O
ATOM 2116 CB LYS A1085 10.822 -69.556 17.834 1.00177.57 C
ANISOU 2116 CB LYS A1085 22113 18824 26531 888 -725 -1243 C
ATOM 2117 CG LYS A1085 12.266 -69.447 17.371 1.00176.79 C
ANISOU 2117 CG LYS A1085 21940 18677 26554 951 -661 -1318 C
ATOM 2118 CD LYS A1085 12.406 -68.540 16.158 1.00173.85 C
ANISOU 2118 CD LYS A1085 21576 18390 26089 978 -520 -1401 C
ATOM 2119 CE LYS A1085 13.833 -68.533 15.643 1.00172.33 C
ANISOU 2119 CE LYS A1085 21309 18146 26024 1040 -455 -1482 C
ATOM 2120 NZ LYS A1085 13.957 -67.798 14.353 1.00172.71 N
ANISOU 2120 NZ LYS A1085 21365 18271 25986 1066 -317 -1573 N
ATOM 2121 N GLU A1086 8.187 -69.001 19.563 1.00186.43 N
ANISOU 2121 N GLU A1086 23360 20086 27389 749 -866 -1024 N
ATOM 2122 CA GLU A1086 6.730 -69.034 19.683 1.00189.19 C
ANISOU 2122 CA GLU A1086 23781 20498 27603 694 -897 -976 C
ATOM 2123 C GLU A1086 6.163 -67.668 20.080 1.00188.97 C
ANISOU 2123 C GLU A1086 23783 20595 27421 662 -864 -911 C
ATOM 2124 O GLU A1086 5.022 -67.349 19.745 1.00187.99 O
ANISOU 2124 O GLU A1086 23718 20549 27160 629 -840 -902 O
ATOM 2125 CB GLU A1086 6.282 -70.123 20.654 1.00193.55 C
ANISOU 2125 CB GLU A1086 24341 20978 28219 654 -1031 -903 C
ATOM 2126 CG GLU A1086 4.814 -70.506 20.507 1.00193.93 C
ANISOU 2126 CG GLU A1086 24460 21067 28156 605 -1062 -880 C
ATOM 2127 CD GLU A1086 4.370 -71.584 21.476 1.00196.40 C
ANISOU 2127 CD GLU A1086 24780 21311 28530 563 -1196 -804 C
ATOM 2128 OE1 GLU A1086 5.154 -72.516 21.758 1.00198.03 O
ANISOU 2128 OE1 GLU A1086 24943 21405 28895 583 -1259 -814 O
ATOM 2129 OE2 GLU A1086 3.216 -71.511 21.944 1.00198.12 O
ANISOU 2129 OE2 GLU A1086 25049 21588 28641 507 -1240 -734 O
ATOM 2130 N ALA A1087 6.961 -66.872 20.792 1.00188.48 N
ANISOU 2130 N ALA A1087 23680 20550 27386 671 -863 -866 N
ATOM 2131 CA ALA A1087 6.566 -65.502 21.125 1.00184.62 C
ANISOU 2131 CA ALA A1087 23212 20175 26759 647 -824 -813 C
ATOM 2132 C ALA A1087 6.628 -64.591 19.901 1.00182.69 C
ANISOU 2132 C ALA A1087 22979 20005 26430 677 -693 -892 C
ATOM 2133 O ALA A1087 5.764 -63.727 19.726 1.00183.56 O
ANISOU 2133 O ALA A1087 23134 20216 26393 651 -653 -872 O
ATOM 2134 CB ALA A1087 7.430 -64.954 22.249 1.00186.72 C
ANISOU 2134 CB ALA A1087 23430 20432 27083 648 -865 -743 C
ATOM 2135 N GLN A1088 7.642 -64.778 19.059 1.00181.99 N
ANISOU 2135 N GLN A1088 22848 19867 26433 731 -629 -982 N
ATOM 2136 CA GLN A1088 7.758 -63.991 17.832 1.00177.55 C
ANISOU 2136 CA GLN A1088 22295 19372 25796 759 -504 -1062 C
ATOM 2137 C GLN A1088 6.620 -64.293 16.858 1.00180.23 C
ANISOU 2137 C GLN A1088 22697 19749 26031 742 -467 -1110 C
ATOM 2138 O GLN A1088 6.201 -63.415 16.108 1.00179.96 O
ANISOU 2138 O GLN A1088 22695 19805 25878 739 -383 -1138 O
ATOM 2139 CB GLN A1088 9.108 -64.231 17.159 1.00173.92 C
ANISOU 2139 CB GLN A1088 21773 18846 25464 820 -445 -1150 C
ATOM 2140 CG GLN A1088 10.308 -63.739 17.951 1.00170.33 C
ANISOU 2140 CG GLN A1088 21252 18365 25101 842 -461 -1112 C
ATOM 2141 CD GLN A1088 11.628 -64.199 17.361 1.00167.48 C
ANISOU 2141 CD GLN A1088 20826 17923 24887 901 -418 -1197 C
ATOM 2142 OE1 GLN A1088 12.000 -65.371 17.475 1.00162.87 O
ANISOU 2142 OE1 GLN A1088 20214 17235 24433 917 -474 -1221 O
ATOM 2143 NE2 GLN A1088 12.347 -63.277 16.734 1.00162.29 N
ANISOU 2143 NE2 GLN A1088 20139 17312 24210 933 -319 -1243 N
ATOM 2144 N ALA A1089 6.120 -65.527 16.879 1.00181.60 N
ANISOU 2144 N ALA A1089 22891 19856 26253 728 -534 -1117 N
ATOM 2145 CA ALA A1089 5.001 -65.902 16.016 1.00184.18 C
ANISOU 2145 CA ALA A1089 23281 20213 26487 708 -510 -1157 C
ATOM 2146 C ALA A1089 3.677 -65.367 16.555 1.00183.21 C
ANISOU 2146 C ALA A1089 23215 20178 26218 650 -545 -1073 C
ATOM 2147 O ALA A1089 2.824 -64.922 15.784 1.00183.72 O
ANISOU 2147 O ALA A1089 23330 20319 26158 634 -487 -1098 O
ATOM 2148 CB ALA A1089 4.947 -67.409 15.833 1.00179.88 C
ANISOU 2148 CB ALA A1089 22735 19562 26048 714 -570 -1197 C
ATOM 2149 N ALA A1090 3.499 -65.410 17.874 1.00180.10 N
ANISOU 2149 N ALA A1090 22815 19775 25839 617 -639 -973 N
ATOM 2150 CA ALA A1090 2.267 -64.907 18.482 1.00178.69 C
ANISOU 2150 CA ALA A1090 22687 19680 25526 561 -675 -890 C
ATOM 2151 C ALA A1090 2.131 -63.393 18.315 1.00178.38 C
ANISOU 2151 C ALA A1090 22659 19754 25365 559 -596 -878 C
ATOM 2152 O ALA A1090 1.018 -62.881 18.215 1.00181.28 O
ANISOU 2152 O ALA A1090 23076 20204 25598 523 -583 -850 O
ATOM 2153 CB ALA A1090 2.190 -65.305 19.946 1.00180.76 C
ANISOU 2153 CB ALA A1090 22936 19907 25838 526 -792 -789 C
ATOM 2154 N ALA A1091 3.262 -62.688 18.273 1.00176.68 N
ANISOU 2154 N ALA A1091 22394 19538 25196 597 -544 -899 N
ATOM 2155 CA ALA A1091 3.260 -61.245 18.031 1.00177.45 C
ANISOU 2155 CA ALA A1091 22498 19736 25189 600 -465 -895 C
ATOM 2156 C ALA A1091 2.933 -60.890 16.581 1.00177.59 C
ANISOU 2156 C ALA A1091 22546 19805 25124 615 -360 -979 C
ATOM 2157 O ALA A1091 2.460 -59.785 16.319 1.00179.00 O
ANISOU 2157 O ALA A1091 22750 20079 25183 602 -306 -968 O
ATOM 2158 CB ALA A1091 4.590 -60.632 18.442 1.00175.29 C
ANISOU 2158 CB ALA A1091 22162 19444 24997 634 -445 -889 C
ATOM 2159 N GLU A1092 3.185 -61.809 15.648 1.00181.55 N
ANISOU 2159 N GLU A1092 23045 20245 25689 641 -334 -1064 N
ATOM 2160 CA GLU A1092 2.858 -61.573 14.246 1.00183.42 C
ANISOU 2160 CA GLU A1092 23314 20528 25849 653 -238 -1147 C
ATOM 2161 C GLU A1092 1.356 -61.526 13.991 1.00180.96 C
ANISOU 2161 C GLU A1092 23073 20281 25401 607 -248 -1124 C
ATOM 2162 O GLU A1092 0.919 -60.892 13.031 1.00176.56 O
ANISOU 2162 O GLU A1092 22549 19795 24742 604 -169 -1165 O
ATOM 2163 CB GLU A1092 3.509 -62.633 13.358 1.00186.68 C
ANISOU 2163 CB GLU A1092 23707 20855 26369 692 -212 -1246 C
ATOM 2164 CG GLU A1092 3.687 -62.223 11.905 1.00189.96 C
ANISOU 2164 CG GLU A1092 24133 21313 26732 716 -95 -1343 C
ATOM 2165 CD GLU A1092 4.716 -61.124 11.723 1.00193.08 C
ANISOU 2165 CD GLU A1092 24483 21747 27132 747 -18 -1360 C
ATOM 2166 OE1 GLU A1092 5.628 -61.010 12.571 1.00200.32 O
ANISOU 2166 OE1 GLU A1092 25345 22623 28143 766 -52 -1323 O
ATOM 2167 OE2 GLU A1092 4.628 -60.386 10.722 1.00199.01 O
ANISOU 2167 OE2 GLU A1092 25251 22567 27795 752 75 -1409 O
ATOM 2168 N GLN A1093 0.575 -62.184 14.845 1.00179.92 N
ANISOU 2168 N GLN A1093 22964 20127 25269 569 -344 -1057 N
ATOM 2169 CA GLN A1093 -0.881 -62.128 14.741 1.00177.67 C
ANISOU 2169 CA GLN A1093 22744 19905 24858 522 -361 -1025 C
ATOM 2170 C GLN A1093 -1.427 -60.725 14.990 1.00174.54 C
ANISOU 2170 C GLN A1093 22366 19620 24329 499 -328 -972 C
ATOM 2171 O GLN A1093 -2.544 -60.418 14.580 1.00169.27 O
ANISOU 2171 O GLN A1093 21750 19020 23544 468 -310 -965 O
ATOM 2172 CB GLN A1093 -1.523 -63.115 15.711 1.00181.03 C
ANISOU 2172 CB GLN A1093 23183 20282 25318 485 -476 -958 C
ATOM 2173 CG GLN A1093 -0.965 -64.521 15.617 1.00186.93 C
ANISOU 2173 CG GLN A1093 23907 20911 26206 507 -523 -1000 C
ATOM 2174 CD GLN A1093 -1.242 -65.170 14.274 1.00196.11 C
ANISOU 2174 CD GLN A1093 25100 22052 27360 522 -473 -1096 C
ATOM 2175 OE1 GLN A1093 -2.387 -65.237 13.824 1.00201.07 O
ANISOU 2175 OE1 GLN A1093 25784 22726 27888 490 -469 -1095 O
ATOM 2176 NE2 GLN A1093 -0.191 -65.652 13.626 1.00205.25 N
ANISOU 2176 NE2 GLN A1093 26220 23140 28626 570 -433 -1180 N
ATOM 2177 N LEU A1094 -0.644 -59.880 15.658 1.00170.99 N
ANISOU 2177 N LEU A1094 21876 19189 23904 513 -320 -936 N
ATOM 2178 CA LEU A1094 -1.064 -58.515 15.955 1.00168.29 C
ANISOU 2178 CA LEU A1094 21547 18948 23448 494 -291 -886 C
ATOM 2179 C LEU A1094 -1.209 -57.651 14.705 1.00171.72 C
ANISOU 2179 C LEU A1094 22003 19453 23790 506 -185 -947 C
ATOM 2180 O LEU A1094 -1.961 -56.681 14.720 1.00169.27 O
ANISOU 2180 O LEU A1094 21722 19231 23363 482 -163 -913 O
ATOM 2181 CB LEU A1094 -0.082 -57.863 16.927 1.00162.10 C
ANISOU 2181 CB LEU A1094 20711 18158 22722 509 -308 -839 C
ATOM 2182 CG LEU A1094 0.021 -58.489 18.319 1.00155.62 C
ANISOU 2182 CG LEU A1094 19870 17283 21976 489 -416 -763 C
ATOM 2183 CD1 LEU A1094 1.337 -58.134 18.983 1.00151.77 C
ANISOU 2183 CD1 LEU A1094 19321 16759 21585 519 -424 -746 C
ATOM 2184 CD2 LEU A1094 -1.147 -58.060 19.186 1.00156.27 C
ANISOU 2184 CD2 LEU A1094 19989 17436 21951 437 -468 -677 C
ATOM 2185 N LYS A1095 -0.504 -58.002 13.632 1.00173.45 N
ANISOU 2185 N LYS A1095 22208 19634 24062 543 -121 -1037 N
ATOM 2186 CA LYS A1095 -0.546 -57.188 12.414 1.00175.43 C
ANISOU 2186 CA LYS A1095 22475 19950 24228 554 -18 -1097 C
ATOM 2187 C LYS A1095 -1.910 -57.244 11.729 1.00174.62 C
ANISOU 2187 C LYS A1095 22439 19902 24006 519 -7 -1105 C
ATOM 2188 O LYS A1095 -2.429 -56.213 11.297 1.00174.77 O
ANISOU 2188 O LYS A1095 22485 20008 23913 504 45 -1099 O
ATOM 2189 CB LYS A1095 0.563 -57.600 11.451 1.00176.47 C
ANISOU 2189 CB LYS A1095 22574 20029 24448 601 48 -1193 C
ATOM 2190 CG LYS A1095 1.953 -57.201 11.910 1.00177.35 C
ANISOU 2190 CG LYS A1095 22618 20109 24657 638 62 -1191 C
ATOM 2191 CD LYS A1095 3.005 -57.584 10.885 1.00178.29 C
ANISOU 2191 CD LYS A1095 22703 20181 24856 683 134 -1291 C
ATOM 2192 CE LYS A1095 4.392 -57.156 11.335 1.00182.00 C
ANISOU 2192 CE LYS A1095 23104 20622 25425 720 149 -1288 C
ATOM 2193 NZ LYS A1095 5.441 -57.598 10.376 1.00180.04 N
ANISOU 2193 NZ LYS A1095 22818 20325 25264 765 217 -1387 N
ATOM 2194 N THR A1096 -2.495 -58.434 11.646 1.00176.25 N
ANISOU 2194 N THR A1096 22672 20057 24237 504 -57 -1117 N
ATOM 2195 CA THR A1096 -3.815 -58.572 11.038 1.00177.06 C
ANISOU 2195 CA THR A1096 22838 20205 24231 468 -54 -1122 C
ATOM 2196 C THR A1096 -4.907 -57.942 11.902 1.00173.12 C
ANISOU 2196 C THR A1096 22367 19776 23634 424 -102 -1029 C
ATOM 2197 O THR A1096 -5.880 -57.403 11.373 1.00175.52 O
ANISOU 2197 O THR A1096 22715 20152 23821 398 -73 -1026 O
ATOM 2198 CB THR A1096 -4.140 -60.038 10.739 1.00181.91 C
ANISOU 2198 CB THR A1096 23472 20742 24902 464 -98 -1159 C
ATOM 2199 OG1 THR A1096 -2.967 -60.685 10.237 1.00186.07 O
ANISOU 2199 OG1 THR A1096 23960 21191 25547 509 -69 -1236 O
ATOM 2200 CG2 THR A1096 -5.244 -60.143 9.708 1.00182.87 C
ANISOU 2200 CG2 THR A1096 23655 20907 24919 438 -66 -1194 C
ATOM 2201 N THR A1097 -4.741 -58.004 13.219 1.00167.70 N
ANISOU 2201 N THR A1097 21655 19068 22995 414 -176 -955 N
ATOM 2202 CA THR A1097 -5.648 -57.298 14.118 1.00165.85 C
ANISOU 2202 CA THR A1097 21440 18905 22672 375 -217 -868 C
ATOM 2203 C THR A1097 -5.482 -55.782 13.991 1.00163.12 C
ANISOU 2203 C THR A1097 21086 18643 22249 382 -152 -858 C
ATOM 2204 O THR A1097 -6.446 -55.034 14.171 1.00164.58 O
ANISOU 2204 O THR A1097 21301 18906 22326 351 -153 -814 O
ATOM 2205 CB THR A1097 -5.432 -57.733 15.569 1.00167.56 C
ANISOU 2205 CB THR A1097 21628 19077 22959 362 -312 -793 C
ATOM 2206 OG1 THR A1097 -5.270 -59.154 15.614 1.00173.50 O
ANISOU 2206 OG1 THR A1097 22376 19735 23809 365 -367 -812 O
ATOM 2207 CG2 THR A1097 -6.617 -57.334 16.430 1.00168.96 C
ANISOU 2207 CG2 THR A1097 21835 19321 23041 313 -364 -709 C
ATOM 2208 N ARG A1098 -4.271 -55.335 13.669 1.00162.75 N
ANISOU 2208 N ARG A1098 20997 18580 22259 422 -96 -899 N
ATOM 2209 CA ARG A1098 -4.011 -53.906 13.509 1.00164.87 C
ANISOU 2209 CA ARG A1098 21255 18923 22464 431 -33 -892 C
ATOM 2210 C ARG A1098 -4.687 -53.350 12.250 1.00168.63 C
ANISOU 2210 C ARG A1098 21773 19467 22831 422 41 -937 C
ATOM 2211 O ARG A1098 -5.242 -52.255 12.275 1.00171.60 O
ANISOU 2211 O ARG A1098 22166 19923 23111 404 64 -905 O
ATOM 2212 CB ARG A1098 -2.505 -53.654 13.472 1.00159.89 C
ANISOU 2212 CB ARG A1098 20567 18254 21930 476 5 -925 C
ATOM 2213 CG ARG A1098 -2.104 -52.201 13.317 1.00156.29 C
ANISOU 2213 CG ARG A1098 20095 17867 21420 487 68 -919 C
ATOM 2214 CD ARG A1098 -0.655 -52.099 12.880 1.00154.65 C
ANISOU 2214 CD ARG A1098 19837 17620 21305 533 123 -973 C
ATOM 2215 NE ARG A1098 -0.456 -52.626 11.530 1.00153.24 N
ANISOU 2215 NE ARG A1098 19668 17420 21135 552 188 -1064 N
ATOM 2216 CZ ARG A1098 0.721 -52.987 11.027 1.00152.37 C
ANISOU 2216 CZ ARG A1098 19517 17257 21121 591 230 -1127 C
ATOM 2217 NH1 ARG A1098 1.832 -52.887 11.749 1.00150.68 N
ANISOU 2217 NH1 ARG A1098 19247 17000 21006 618 213 -1109 N
ATOM 2218 NH2 ARG A1098 0.795 -53.450 9.789 1.00154.67 N
ANISOU 2218 NH2 ARG A1098 19822 17536 21409 604 291 -1211 N
ATOM 2219 N ASN A1099 -4.649 -54.115 11.161 1.00172.00 N
ANISOU 2219 N ASN A1099 22217 19859 23275 433 77 -1012 N
ATOM 2220 CA ASN A1099 -5.215 -53.678 9.889 1.00169.76 C
ANISOU 2220 CA ASN A1099 21973 19633 22894 424 149 -1061 C
ATOM 2221 C ASN A1099 -6.737 -53.792 9.820 1.00166.61 C
ANISOU 2221 C ASN A1099 21632 19279 22392 379 116 -1028 C
ATOM 2222 O ASN A1099 -7.331 -53.351 8.836 1.00167.58 O
ANISOU 2222 O ASN A1099 21792 19457 22424 365 169 -1058 O
ATOM 2223 CB ASN A1099 -4.581 -54.457 8.731 1.00172.98 C
ANISOU 2223 CB ASN A1099 22378 19988 23357 452 202 -1157 C
ATOM 2224 CG ASN A1099 -3.131 -54.085 8.502 1.00174.46 C
ANISOU 2224 CG ASN A1099 22511 20153 23622 496 259 -1200 C
ATOM 2225 OD1 ASN A1099 -2.825 -52.998 8.014 1.00173.11 O
ANISOU 2225 OD1 ASN A1099 22332 20042 23399 503 326 -1211 O
ATOM 2226 ND2 ASN A1099 -2.228 -54.991 8.850 1.00176.15 N
ANISOU 2226 ND2 ASN A1099 22685 20280 23964 525 231 -1223 N
ATOM 2227 N ALA A1100 -7.366 -54.368 10.845 1.00161.23 N
ANISOU 2227 N ALA A1100 20959 18577 21723 353 30 -966 N
ATOM 2228 CA ALA A1100 -8.812 -54.588 10.836 1.00161.70 C
ANISOU 2228 CA ALA A1100 21071 18675 21694 310 -7 -933 C
ATOM 2229 C ALA A1100 -9.570 -53.841 11.933 1.00163.73 C
ANISOU 2229 C ALA A1100 21331 18991 21886 279 -54 -843 C
ATOM 2230 O ALA A1100 -10.791 -53.733 11.851 1.00164.44 O
ANISOU 2230 O ALA A1100 21462 19130 21886 243 -70 -816 O
ATOM 2231 CB ALA A1100 -9.125 -56.078 10.914 1.00154.79 C
ANISOU 2231 CB ALA A1100 20211 17724 20877 300 -68 -944 C
ATOM 2232 N TYR A1101 -8.874 -53.348 12.955 1.00162.92 N
ANISOU 2232 N TYR A1101 21188 18887 21829 291 -76 -799 N
ATOM 2233 CA TYR A1101 -9.540 -52.688 14.077 1.00162.89 C
ANISOU 2233 CA TYR A1101 21185 18937 21770 262 -124 -716 C
ATOM 2234 C TYR A1101 -8.819 -51.421 14.510 1.00160.80 C
ANISOU 2234 C TYR A1101 20884 18713 21500 282 -92 -695 C
ATOM 2235 O TYR A1101 -9.452 -50.384 14.715 1.00160.61 O
ANISOU 2235 O TYR A1101 20872 18765 21388 264 -81 -659 O
ATOM 2236 CB TYR A1101 -9.668 -53.648 15.265 1.00165.74 C
ANISOU 2236 CB TYR A1101 21536 19246 22193 244 -218 -662 C
ATOM 2237 CG TYR A1101 -10.577 -54.825 15.030 1.00166.79 C
ANISOU 2237 CG TYR A1101 21705 19347 22318 216 -263 -665 C
ATOM 2238 CD1 TYR A1101 -11.934 -54.754 15.348 1.00165.97 C
ANISOU 2238 CD1 TYR A1101 21638 19298 22123 172 -300 -615 C
ATOM 2239 CD2 TYR A1101 -10.081 -56.015 14.491 1.00167.34 C
ANISOU 2239 CD2 TYR A1101 21774 19334 22476 235 -270 -720 C
ATOM 2240 CE1 TYR A1101 -12.774 -55.834 15.133 1.00167.11 C
ANISOU 2240 CE1 TYR A1101 21818 19415 22262 145 -343 -616 C
ATOM 2241 CE2 TYR A1101 -10.911 -57.099 14.266 1.00168.35 C
ANISOU 2241 CE2 TYR A1101 21936 19430 22598 209 -313 -724 C
ATOM 2242 CZ TYR A1101 -12.255 -57.005 14.592 1.00169.35 C
ANISOU 2242 CZ TYR A1101 22100 19613 22632 163 -350 -670 C
ATOM 2243 OH TYR A1101 -13.081 -58.077 14.377 1.00171.14 O
ANISOU 2243 OH TYR A1101 22361 19809 22855 136 -396 -671 O
ATOM 2244 N ILE A1102 -7.500 -51.506 14.647 1.00158.48 N
ANISOU 2244 N ILE A1102 20545 18365 21304 318 -79 -718 N
ATOM 2245 CA ILE A1102 -6.723 -50.400 15.199 1.00158.09 C
ANISOU 2245 CA ILE A1102 20458 18345 21265 337 -60 -693 C
ATOM 2246 C ILE A1102 -6.657 -49.223 14.232 1.00164.61 C
ANISOU 2246 C ILE A1102 21291 19236 22020 348 26 -727 C
ATOM 2247 O ILE A1102 -6.921 -48.079 14.618 1.00167.75 O
ANISOU 2247 O ILE A1102 21687 19698 22353 339 34 -688 O
ATOM 2248 CB ILE A1102 -5.319 -50.872 15.618 1.00155.10 C
ANISOU 2248 CB ILE A1102 20027 17888 21017 372 -73 -706 C
ATOM 2249 CG1 ILE A1102 -5.427 -52.006 16.650 1.00153.11 C
ANISOU 2249 CG1 ILE A1102 19768 17572 20834 355 -166 -663 C
ATOM 2250 CG2 ILE A1102 -4.501 -49.715 16.167 1.00154.79 C
ANISOU 2250 CG2 ILE A1102 19949 17877 20989 390 -53 -680 C
ATOM 2251 CD1 ILE A1102 -6.282 -51.714 17.880 1.00151.03 C
ANISOU 2251 CD1 ILE A1102 19517 17353 20516 316 -234 -577 C
ATOM 2252 N GLN A1103 -6.347 -49.501 12.970 1.00168.83 N
ANISOU 2252 N GLN A1103 21833 19753 22560 366 88 -801 N
ATOM 2253 CA GLN A1103 -6.278 -48.440 11.966 1.00168.16 C
ANISOU 2253 CA GLN A1103 21758 19729 22408 374 170 -836 C
ATOM 2254 C GLN A1103 -7.647 -47.818 11.686 1.00164.23 C
ANISOU 2254 C GLN A1103 21308 19310 21784 337 174 -810 C
ATOM 2255 O GLN A1103 -7.718 -46.720 11.145 1.00163.61 O
ANISOU 2255 O GLN A1103 21234 19292 21638 337 227 -816 O
ATOM 2256 CB GLN A1103 -5.634 -48.947 10.677 1.00173.09 C
ANISOU 2256 CB GLN A1103 22381 20318 23067 399 235 -922 C
ATOM 2257 CG GLN A1103 -5.000 -47.850 9.832 1.00175.58 C
ANISOU 2257 CG GLN A1103 22682 20678 23351 417 320 -958 C
ATOM 2258 CD GLN A1103 -4.163 -48.384 8.687 1.00180.16 C
ANISOU 2258 CD GLN A1103 23252 21220 23982 445 385 -1044 C
ATOM 2259 OE1 GLN A1103 -3.162 -49.071 8.897 1.00182.78 O
ANISOU 2259 OE1 GLN A1103 23545 21481 24422 475 378 -1071 O
ATOM 2260 NE2 GLN A1103 -4.561 -48.057 7.465 1.00183.70 N
ANISOU 2260 NE2 GLN A1103 23732 21713 24351 434 448 -1089 N
ATOM 2261 N LYS A1104 -8.723 -48.510 12.055 1.00161.07 N
ANISOU 2261 N LYS A1104 20940 18908 21353 306 116 -780 N
ATOM 2262 CA LYS A1104 -10.052 -47.907 11.985 1.00159.52 C
ANISOU 2262 CA LYS A1104 20783 18786 21041 270 110 -745 C
ATOM 2263 C LYS A1104 -10.218 -46.817 13.042 1.00158.12 C
ANISOU 2263 C LYS A1104 20587 18661 20829 261 86 -679 C
ATOM 2264 O LYS A1104 -10.821 -45.776 12.776 1.00160.44 O
ANISOU 2264 O LYS A1104 20897 19026 21037 248 114 -665 O
ATOM 2265 CB LYS A1104 -11.145 -48.963 12.145 1.00158.88 C
ANISOU 2265 CB LYS A1104 20739 18688 20941 237 53 -728 C
ATOM 2266 CG LYS A1104 -11.461 -49.744 10.882 1.00158.55 C
ANISOU 2266 CG LYS A1104 20733 18624 20885 234 84 -792 C
ATOM 2267 CD LYS A1104 -12.771 -50.504 11.027 1.00156.97 C
ANISOU 2267 CD LYS A1104 20575 18428 20640 195 29 -764 C
ATOM 2268 CE LYS A1104 -13.178 -51.173 9.724 1.00157.61 C
ANISOU 2268 CE LYS A1104 20696 18494 20694 188 62 -827 C
ATOM 2269 NZ LYS A1104 -12.304 -52.329 9.374 1.00157.48 N
ANISOU 2269 NZ LYS A1104 20666 18391 20778 214 63 -884 N
ATOM 2270 N TYR A1105 -9.670 -47.048 14.232 1.00158.29 N
ANISOU 2270 N TYR A1105 20575 18648 20920 269 34 -638 N
ATOM 2271 CA TYR A1105 -9.822 -46.106 15.336 1.00161.08 C
ANISOU 2271 CA TYR A1105 20911 19048 21244 259 4 -575 C
ATOM 2272 C TYR A1105 -8.771 -44.999 15.342 1.00161.43 C
ANISOU 2272 C TYR A1105 20919 19109 21311 289 50 -582 C
ATOM 2273 O TYR A1105 -8.998 -43.959 15.959 1.00164.66 O
ANISOU 2273 O TYR A1105 21319 19570 21673 282 43 -540 O
ATOM 2274 CB TYR A1105 -9.821 -46.852 16.676 1.00161.55 C
ANISOU 2274 CB TYR A1105 20955 19069 21359 246 -79 -522 C
ATOM 2275 CG TYR A1105 -10.022 -45.969 17.886 1.00163.99 C
ANISOU 2275 CG TYR A1105 21248 19425 21635 232 -114 -456 C
ATOM 2276 CD1 TYR A1105 -11.285 -45.456 18.201 1.00165.08 C
ANISOU 2276 CD1 TYR A1105 21413 19633 21676 198 -132 -417 C
ATOM 2277 CD2 TYR A1105 -8.944 -45.633 18.713 1.00165.50 C
ANISOU 2277 CD2 TYR A1105 21396 19592 21895 254 -128 -436 C
ATOM 2278 CE1 TYR A1105 -11.471 -44.643 19.311 1.00164.61 C
ANISOU 2278 CE1 TYR A1105 21339 19619 21587 187 -162 -362 C
ATOM 2279 CE2 TYR A1105 -9.119 -44.818 19.823 1.00163.41 C
ANISOU 2279 CE2 TYR A1105 21117 19371 21599 241 -160 -378 C
ATOM 2280 CZ TYR A1105 -10.382 -44.326 20.119 1.00160.80 C
ANISOU 2280 CZ TYR A1105 20814 19111 21171 207 -176 -343 C
ATOM 2281 OH TYR A1105 -10.559 -43.520 21.217 1.00157.87 O
ANISOU 2281 OH TYR A1105 20430 18786 20769 195 -206 -291 O
ATOM 2282 N LEU A1106 -7.638 -45.214 14.671 1.00158.71 N
ANISOU 2282 N LEU A1106 20550 18717 21034 323 95 -635 N
ATOM 2283 CA LEU A1106 -6.523 -44.257 14.668 1.00160.36 C
ANISOU 2283 CA LEU A1106 20719 18934 21276 353 137 -644 C
ATOM 2284 C LEU A1106 -6.958 -42.852 14.237 1.00161.63 C
ANISOU 2284 C LEU A1106 20892 19177 21342 346 183 -636 C
ATOM 2285 O LEU A1106 -6.422 -41.848 14.696 1.00162.72 O
ANISOU 2285 O LEU A1106 21003 19339 21484 358 192 -613 O
ATOM 2286 CB LEU A1106 -5.387 -44.760 13.771 1.00164.90 C
ANISOU 2286 CB LEU A1106 21273 19454 21929 388 189 -712 C
ATOM 2287 CG LEU A1106 -4.193 -43.819 13.556 1.00166.26 C
ANISOU 2287 CG LEU A1106 21404 19633 22135 419 243 -729 C
ATOM 2288 CD1 LEU A1106 -3.474 -43.486 14.857 1.00161.11 C
ANISOU 2288 CD1 LEU A1106 20709 18962 21544 431 197 -678 C
ATOM 2289 CD2 LEU A1106 -3.224 -44.368 12.524 1.00164.90 C
ANISOU 2289 CD2 LEU A1106 21214 19413 22028 449 300 -803 C
ATOM 2290 N GLU A 219 -8.784 -44.366 12.054 1.00144.54 N
ANISOU 2290 N GLU A 219 18825 17016 19077 306 218 -717 N
ATOM 2291 CA GLU A 219 -8.770 -43.018 11.514 1.00146.30 C
ANISOU 2291 CA GLU A 219 19048 17305 19236 308 273 -721 C
ATOM 2292 C GLU A 219 -10.046 -42.278 11.889 1.00141.18 C
ANISOU 2292 C GLU A 219 18427 16725 18489 276 247 -670 C
ATOM 2293 O GLU A 219 -10.288 -41.165 11.422 1.00140.13 O
ANISOU 2293 O GLU A 219 18300 16650 18291 271 285 -668 O
ATOM 2294 CB GLU A 219 -8.568 -43.051 9.999 1.00149.48 C
ANISOU 2294 CB GLU A 219 19469 17712 19615 315 346 -788 C
ATOM 2295 CG GLU A 219 -7.200 -43.572 9.580 1.00158.06 C
ANISOU 2295 CG GLU A 219 20522 18738 20796 351 384 -843 C
ATOM 2296 CD GLU A 219 -7.027 -43.705 8.078 1.00166.72 C
ANISOU 2296 CD GLU A 219 21637 19840 21868 355 456 -914 C
ATOM 2297 OE1 GLU A 219 -8.023 -43.603 7.324 1.00171.79 O
ANISOU 2297 OE1 GLU A 219 22325 20524 22423 327 472 -924 O
ATOM 2298 OE2 GLU A 219 -5.877 -43.921 7.641 1.00176.90 O
ANISOU 2298 OE2 GLU A 219 22897 21092 23226 385 499 -962 O
ATOM 2299 N ARG A 220 -10.863 -42.898 12.735 1.00136.67 N
ANISOU 2299 N ARG A 220 17870 16149 17911 252 181 -629 N
ATOM 2300 CA ARG A 220 -12.058 -42.233 13.238 1.00139.04 C
ANISOU 2300 CA ARG A 220 18190 16512 18125 222 152 -578 C
ATOM 2301 C ARG A 220 -11.712 -41.132 14.238 1.00139.49 C
ANISOU 2301 C ARG A 220 18214 16602 18183 231 138 -533 C
ATOM 2302 O ARG A 220 -12.410 -40.119 14.314 1.00140.66 O
ANISOU 2302 O ARG A 220 18371 16814 18258 216 143 -508 O
ATOM 2303 CB ARG A 220 -13.026 -43.236 13.856 1.00138.72 C
ANISOU 2303 CB ARG A 220 18173 16459 18077 193 86 -547 C
ATOM 2304 CG ARG A 220 -14.379 -42.644 14.233 1.00141.05 C
ANISOU 2304 CG ARG A 220 18491 16822 18278 159 61 -502 C
ATOM 2305 CD ARG A 220 -15.387 -43.699 14.656 1.00145.31 C
ANISOU 2305 CD ARG A 220 19057 17350 18804 127 2 -476 C
ATOM 2306 NE ARG A 220 -15.869 -44.483 13.519 1.00149.76 N
ANISOU 2306 NE ARG A 220 19659 17896 19349 116 21 -518 N
ATOM 2307 CZ ARG A 220 -16.866 -45.365 13.567 1.00151.03 C
ANISOU 2307 CZ ARG A 220 19850 18051 19485 86 -20 -504 C
ATOM 2308 NH1 ARG A 220 -17.523 -45.598 14.699 1.00152.09 N
ANISOU 2308 NH1 ARG A 220 19981 18199 19609 62 -83 -447 N
ATOM 2309 NH2 ARG A 220 -17.213 -46.020 12.468 1.00151.16 N
ANISOU 2309 NH2 ARG A 220 19900 18049 19485 78 1 -547 N
ATOM 2310 N ALA A 221 -10.650 -41.333 15.013 1.00140.75 N
ANISOU 2310 N ALA A 221 18335 16716 18427 253 118 -524 N
ATOM 2311 CA ALA A 221 -10.211 -40.308 15.963 1.00143.34 C
ANISOU 2311 CA ALA A 221 18631 17071 18762 263 105 -484 C
ATOM 2312 C ALA A 221 -9.669 -39.070 15.249 1.00145.61 C
ANISOU 2312 C ALA A 221 18904 17393 19026 282 169 -506 C
ATOM 2313 O ALA A 221 -9.954 -37.945 15.656 1.00144.87 O
ANISOU 2313 O ALA A 221 18806 17353 18887 277 168 -476 O
ATOM 2314 CB ALA A 221 -9.188 -40.867 16.934 1.00143.40 C
ANISOU 2314 CB ALA A 221 18601 17018 18868 280 67 -467 C
ATOM 2315 N ARG A 222 -8.906 -39.280 14.179 1.00148.83 N
ANISOU 2315 N ARG A 222 19308 17772 19467 303 224 -561 N
ATOM 2316 CA ARG A 222 -8.407 -38.160 13.383 1.00148.58 C
ANISOU 2316 CA ARG A 222 19266 17775 19411 318 287 -584 C
ATOM 2317 C ARG A 222 -9.546 -37.401 12.707 1.00143.15 C
ANISOU 2317 C ARG A 222 18615 17156 18618 292 308 -580 C
ATOM 2318 O ARG A 222 -9.469 -36.182 12.555 1.00143.75 O
ANISOU 2318 O ARG A 222 18683 17278 18658 295 334 -570 O
ATOM 2319 CB ARG A 222 -7.386 -38.632 12.349 1.00156.26 C
ANISOU 2319 CB ARG A 222 20227 18705 20438 342 344 -645 C
ATOM 2320 CG ARG A 222 -5.971 -38.750 12.892 1.00165.35 C
ANISOU 2320 CG ARG A 222 21329 19804 21692 375 343 -649 C
ATOM 2321 CD ARG A 222 -4.934 -38.790 11.783 1.00172.30 C
ANISOU 2321 CD ARG A 222 22192 20662 22612 401 413 -709 C
ATOM 2322 NE ARG A 222 -4.686 -40.146 11.294 1.00179.18 N
ANISOU 2322 NE ARG A 222 23069 21473 23537 408 418 -756 N
ATOM 2323 CZ ARG A 222 -3.804 -40.456 10.345 1.00182.24 C
ANISOU 2323 CZ ARG A 222 23442 21832 23968 431 476 -817 C
ATOM 2324 NH1 ARG A 222 -3.071 -39.515 9.760 1.00186.69 N
ANISOU 2324 NH1 ARG A 222 23984 22423 24525 445 535 -835 N
ATOM 2325 NH2 ARG A 222 -3.652 -41.718 9.972 1.00173.25 N
ANISOU 2325 NH2 ARG A 222 22311 20638 22880 438 475 -860 N
ATOM 2326 N SER A 223 -10.599 -38.115 12.317 1.00141.14 N
ANISOU 2326 N SER A 223 18401 16907 18318 267 294 -587 N
ATOM 2327 CA SER A 223 -11.738 -37.469 11.668 1.00138.34 C
ANISOU 2327 CA SER A 223 18082 16615 17866 241 310 -582 C
ATOM 2328 C SER A 223 -12.523 -36.603 12.655 1.00133.65 C
ANISOU 2328 C SER A 223 17485 16073 17224 225 269 -525 C
ATOM 2329 O SER A 223 -12.891 -35.472 12.329 1.00137.04 O
ANISOU 2329 O SER A 223 17918 16555 17595 219 291 -516 O
ATOM 2330 CB SER A 223 -12.640 -38.512 11.013 1.00138.62 C
ANISOU 2330 CB SER A 223 18160 16640 17869 217 303 -603 C
ATOM 2331 OG SER A 223 -13.705 -37.901 10.311 1.00139.85 O
ANISOU 2331 OG SER A 223 18350 16854 17934 192 319 -600 O
ATOM 2332 N THR A 224 -12.762 -37.120 13.856 1.00128.17 N
ANISOU 2332 N THR A 224 16781 15362 16555 219 209 -487 N
ATOM 2333 CA THR A 224 -13.555 -36.388 14.841 1.00122.91 C
ANISOU 2333 CA THR A 224 16113 14745 15842 202 169 -436 C
ATOM 2334 C THR A 224 -12.804 -35.171 15.379 1.00121.98 C
ANISOU 2334 C THR A 224 15959 14647 15740 223 179 -419 C
ATOM 2335 O THR A 224 -13.409 -34.128 15.630 1.00122.56 O
ANISOU 2335 O THR A 224 16034 14776 15759 214 175 -394 O
ATOM 2336 CB THR A 224 -13.977 -37.310 15.989 1.00122.64 C
ANISOU 2336 CB THR A 224 16079 14690 15830 186 103 -400 C
ATOM 2337 OG1 THR A 224 -14.483 -38.531 15.442 1.00120.57 O
ANISOU 2337 OG1 THR A 224 15847 14398 15567 170 95 -421 O
ATOM 2338 CG2 THR A 224 -15.055 -36.663 16.834 1.00120.00 C
ANISOU 2338 CG2 THR A 224 15750 14415 15431 162 66 -353 C
ATOM 2339 N LEU A 225 -11.492 -35.298 15.551 1.00122.83 N
ANISOU 2339 N LEU A 225 16034 14709 15926 251 191 -432 N
ATOM 2340 CA LEU A 225 -10.700 -34.155 16.002 1.00124.65 C
ANISOU 2340 CA LEU A 225 16230 14954 16176 272 202 -417 C
ATOM 2341 C LEU A 225 -10.611 -33.068 14.939 1.00128.50 C
ANISOU 2341 C LEU A 225 16722 15480 16622 278 259 -440 C
ATOM 2342 O LEU A 225 -10.610 -31.883 15.272 1.00132.51 O
ANISOU 2342 O LEU A 225 17215 16027 17106 281 260 -418 O
ATOM 2343 CB LEU A 225 -9.310 -34.598 16.448 1.00119.44 C
ANISOU 2343 CB LEU A 225 15533 14234 15614 299 198 -424 C
ATOM 2344 CG LEU A 225 -9.121 -34.808 17.953 1.00119.76 C
ANISOU 2344 CG LEU A 225 15551 14258 15695 298 136 -379 C
ATOM 2345 CD1 LEU A 225 -9.929 -35.996 18.464 1.00119.62 C
ANISOU 2345 CD1 LEU A 225 15556 14223 15673 273 84 -362 C
ATOM 2346 CD2 LEU A 225 -7.648 -34.983 18.293 1.00116.89 C
ANISOU 2346 CD2 LEU A 225 15147 13839 15428 328 138 -386 C
ATOM 2347 N GLN A 226 -10.564 -33.464 13.669 1.00129.62 N
ANISOU 2347 N GLN A 226 16884 15613 16753 277 305 -483 N
ATOM 2348 CA GLN A 226 -10.509 -32.481 12.584 1.00131.10 C
ANISOU 2348 CA GLN A 226 17077 15837 16896 278 360 -504 C
ATOM 2349 C GLN A 226 -11.826 -31.723 12.438 1.00127.32 C
ANISOU 2349 C GLN A 226 16627 15421 16328 251 349 -482 C
ATOM 2350 O GLN A 226 -11.819 -30.534 12.124 1.00127.25 O
ANISOU 2350 O GLN A 226 16612 15452 16286 252 372 -475 O
ATOM 2351 CB GLN A 226 -10.122 -33.143 11.268 1.00137.84 C
ANISOU 2351 CB GLN A 226 17947 16666 17759 281 412 -558 C
ATOM 2352 CG GLN A 226 -8.634 -33.438 11.130 1.00145.33 C
ANISOU 2352 CG GLN A 226 18860 17565 18793 312 443 -588 C
ATOM 2353 CD GLN A 226 -8.311 -34.262 9.896 1.00152.22 C
ANISOU 2353 CD GLN A 226 19749 18410 19677 314 491 -646 C
ATOM 2354 OE1 GLN A 226 -8.589 -33.848 8.767 1.00159.57 O
ANISOU 2354 OE1 GLN A 226 20703 19376 20553 302 537 -671 O
ATOM 2355 NE2 GLN A 226 -7.703 -35.427 10.100 1.00154.60 N
ANISOU 2355 NE2 GLN A 226 20038 18650 20052 330 482 -669 N
ATOM 2356 N LYS A 227 -12.947 -32.399 12.679 1.00126.62 N
ANISOU 2356 N LYS A 227 16567 15341 16202 227 314 -468 N
ATOM 2357 CA LYS A 227 -14.252 -31.738 12.593 1.00127.37 C
ANISOU 2357 CA LYS A 227 16686 15495 16216 201 300 -446 C
ATOM 2358 C LYS A 227 -14.479 -30.779 13.757 1.00125.62 C
ANISOU 2358 C LYS A 227 16441 15306 15983 203 265 -402 C
ATOM 2359 O LYS A 227 -15.199 -29.791 13.616 1.00122.67 O
ANISOU 2359 O LYS A 227 16074 14982 15553 192 266 -388 O
ATOM 2360 CB LYS A 227 -15.381 -32.762 12.503 1.00128.08 C
ANISOU 2360 CB LYS A 227 16811 15582 16269 174 273 -444 C
ATOM 2361 CG LYS A 227 -15.528 -33.381 11.124 1.00132.18 C
ANISOU 2361 CG LYS A 227 17363 16090 16768 163 312 -487 C
ATOM 2362 CD LYS A 227 -16.851 -34.113 10.962 1.00134.97 C
ANISOU 2362 CD LYS A 227 17756 16456 17071 132 284 -479 C
ATOM 2363 CE LYS A 227 -17.067 -34.524 9.512 1.00139.22 C
ANISOU 2363 CE LYS A 227 18329 16991 17577 119 326 -522 C
ATOM 2364 NZ LYS A 227 -18.385 -35.180 9.293 1.00145.41 N
ANISOU 2364 NZ LYS A 227 19153 17789 18309 86 298 -514 N
ATOM 2365 N GLU A 228 -13.876 -31.068 14.907 1.00125.00 N
ANISOU 2365 N GLU A 228 16334 15199 15960 217 231 -382 N
ATOM 2366 CA GLU A 228 -13.945 -30.143 16.038 1.00123.87 C
ANISOU 2366 CA GLU A 228 16168 15086 15812 221 199 -345 C
ATOM 2367 C GLU A 228 -13.032 -28.935 15.838 1.00118.24 C
ANISOU 2367 C GLU A 228 15427 14381 15118 244 231 -350 C
ATOM 2368 O GLU A 228 -13.331 -27.850 16.338 1.00121.12 O
ANISOU 2368 O GLU A 228 15780 14785 15455 244 218 -326 O
ATOM 2369 CB GLU A 228 -13.613 -30.854 17.342 1.00127.11 C
ANISOU 2369 CB GLU A 228 16559 15464 16273 224 151 -320 C
ATOM 2370 CG GLU A 228 -14.730 -31.726 17.884 1.00130.76 C
ANISOU 2370 CG GLU A 228 17045 15936 16704 196 106 -299 C
ATOM 2371 CD GLU A 228 -14.360 -32.408 19.191 1.00136.02 C
ANISOU 2371 CD GLU A 228 17691 16572 17419 195 55 -271 C
ATOM 2372 OE1 GLU A 228 -13.257 -32.995 19.281 1.00141.84 O
ANISOU 2372 OE1 GLU A 228 18410 17253 18229 214 57 -282 O
ATOM 2373 OE2 GLU A 228 -15.182 -32.365 20.130 1.00141.02 O
ANISOU 2373 OE2 GLU A 228 18327 17237 18019 175 13 -237 O
ATOM 2374 N VAL A 229 -11.928 -29.115 15.116 1.00111.55 N
ANISOU 2374 N VAL A 229 14568 13498 14317 264 272 -380 N
ATOM 2375 CA VAL A 229 -11.052 -27.990 14.792 1.00108.67 C
ANISOU 2375 CA VAL A 229 14179 13143 13969 283 306 -386 C
ATOM 2376 C VAL A 229 -11.704 -27.101 13.729 1.00108.80 C
ANISOU 2376 C VAL A 229 14216 13206 13917 269 338 -395 C
ATOM 2377 O VAL A 229 -11.581 -25.873 13.771 1.00105.49 O
ANISOU 2377 O VAL A 229 13782 12817 13484 275 344 -381 O
ATOM 2378 CB VAL A 229 -9.661 -28.487 14.358 1.00109.55 C
ANISOU 2378 CB VAL A 229 14269 13203 14154 307 340 -416 C
ATOM 2379 CG1 VAL A 229 -8.839 -27.368 13.740 1.00112.83 C
ANISOU 2379 CG1 VAL A 229 14663 13631 14576 323 384 -426 C
ATOM 2380 CG2 VAL A 229 -8.925 -29.073 15.548 1.00104.66 C
ANISOU 2380 CG2 VAL A 229 13621 12539 13608 323 302 -399 C
ATOM 2381 N HIS A 230 -12.406 -27.718 12.782 1.00111.88 N
ANISOU 2381 N HIS A 230 14641 13602 14266 250 357 -417 N
ATOM 2382 CA HIS A 230 -13.141 -26.955 11.776 1.00114.32 C
ANISOU 2382 CA HIS A 230 14973 13955 14507 231 382 -422 C
ATOM 2383 C HIS A 230 -14.242 -26.110 12.420 1.00112.65 C
ANISOU 2383 C HIS A 230 14766 13792 14244 217 344 -387 C
ATOM 2384 O HIS A 230 -14.499 -24.985 11.987 1.00116.93 O
ANISOU 2384 O HIS A 230 15307 14371 14750 213 357 -380 O
ATOM 2385 CB HIS A 230 -13.721 -27.885 10.714 1.00117.62 C
ANISOU 2385 CB HIS A 230 15431 14368 14891 211 403 -451 C
ATOM 2386 CG HIS A 230 -14.410 -27.167 9.596 1.00121.34 C
ANISOU 2386 CG HIS A 230 15928 14883 15294 189 430 -458 C
ATOM 2387 ND1 HIS A 230 -13.748 -26.742 8.464 1.00125.31 N
ANISOU 2387 ND1 HIS A 230 16430 15388 15792 191 482 -484 N
ATOM 2388 CD2 HIS A 230 -15.702 -26.795 9.437 1.00121.99 C
ANISOU 2388 CD2 HIS A 230 16035 15007 15310 164 411 -440 C
ATOM 2389 CE1 HIS A 230 -14.603 -26.142 7.655 1.00125.61 C
ANISOU 2389 CE1 HIS A 230 16495 15468 15764 167 492 -481 C
ATOM 2390 NE2 HIS A 230 -15.795 -26.160 8.222 1.00124.40 N
ANISOU 2390 NE2 HIS A 230 16356 15337 15574 151 449 -454 N
ATOM 2391 N ALA A 231 -14.885 -26.647 13.454 1.00109.05 N
ANISOU 2391 N ALA A 231 14312 13337 13786 210 297 -364 N
ATOM 2392 CA ALA A 231 -15.917 -25.897 14.166 1.00104.90 C
ANISOU 2392 CA ALA A 231 13786 12857 13215 198 261 -333 C
ATOM 2393 C ALA A 231 -15.312 -24.760 14.987 1.00101.29 C
ANISOU 2393 C ALA A 231 13293 12411 12783 218 250 -313 C
ATOM 2394 O ALA A 231 -15.905 -23.682 15.087 1.00102.12 O
ANISOU 2394 O ALA A 231 13394 12557 12850 214 241 -298 O
ATOM 2395 CB ALA A 231 -16.746 -26.821 15.044 1.00106.30 C
ANISOU 2395 CB ALA A 231 13974 13033 13381 182 216 -315 C
ATOM 2396 N ALA A 232 -14.143 -24.995 15.577 1.00 99.15 N
ANISOU 2396 N ALA A 232 12995 12102 12577 240 248 -313 N
ATOM 2397 CA ALA A 232 -13.476 -23.951 16.358 1.00 96.62 C
ANISOU 2397 CA ALA A 232 12639 11787 12284 260 236 -296 C
ATOM 2398 C ALA A 232 -12.933 -22.848 15.454 1.00 97.10 C
ANISOU 2398 C ALA A 232 12691 11860 12342 270 275 -307 C
ATOM 2399 O ALA A 232 -12.977 -21.673 15.815 1.00 97.01 O
ANISOU 2399 O ALA A 232 12663 11876 12320 276 265 -290 O
ATOM 2400 CB ALA A 232 -12.374 -24.541 17.220 1.00 95.93 C
ANISOU 2400 CB ALA A 232 12526 11654 12268 279 221 -291 C
ATOM 2401 N LYS A 233 -12.433 -23.223 14.279 1.00 99.19 N
ANISOU 2401 N LYS A 233 12966 12106 12614 271 321 -335 N
ATOM 2402 CA LYS A 233 -11.979 -22.228 13.306 1.00100.54 C
ANISOU 2402 CA LYS A 233 13132 12293 12777 274 360 -345 C
ATOM 2403 C LYS A 233 -13.139 -21.346 12.845 1.00 96.49 C
ANISOU 2403 C LYS A 233 12638 11830 12193 254 355 -334 C
ATOM 2404 O LYS A 233 -12.990 -20.129 12.727 1.00 91.75 O
ANISOU 2404 O LYS A 233 12023 11252 11585 258 358 -323 O
ATOM 2405 CB LYS A 233 -11.313 -22.899 12.106 1.00104.43 C
ANISOU 2405 CB LYS A 233 13635 12760 13284 274 411 -381 C
ATOM 2406 CG LYS A 233 -9.882 -23.353 12.339 1.00109.45 C
ANISOU 2406 CG LYS A 233 14241 13347 13997 300 428 -394 C
ATOM 2407 CD LYS A 233 -9.244 -23.835 11.043 1.00115.78 C
ANISOU 2407 CD LYS A 233 15051 14132 14809 300 485 -433 C
ATOM 2408 CE LYS A 233 -7.773 -24.178 11.231 1.00119.71 C
ANISOU 2408 CE LYS A 233 15513 14583 15388 328 505 -448 C
ATOM 2409 NZ LYS A 233 -7.122 -24.578 9.952 1.00123.13 N
ANISOU 2409 NZ LYS A 233 15951 15002 15829 328 565 -489 N
ATOM 2410 N SER A 234 -14.297 -21.959 12.610 1.00 96.56 N
ANISOU 2410 N SER A 234 12679 11854 12154 230 343 -336 N
ATOM 2411 CA SER A 234 -15.469 -21.205 12.175 1.00 98.09 C
ANISOU 2411 CA SER A 234 12892 12095 12284 209 335 -325 C
ATOM 2412 C SER A 234 -15.947 -20.247 13.263 1.00 96.56 C
ANISOU 2412 C SER A 234 12677 11929 12083 216 294 -296 C
ATOM 2413 O SER A 234 -16.331 -19.113 12.969 1.00101.86 O
ANISOU 2413 O SER A 234 13344 12631 12726 211 293 -287 O
ATOM 2414 CB SER A 234 -16.590 -22.149 11.754 1.00101.24 C
ANISOU 2414 CB SER A 234 13328 12502 12637 183 329 -332 C
ATOM 2415 OG SER A 234 -16.146 -23.043 10.751 1.00104.05 O
ANISOU 2415 OG SER A 234 13704 12831 13000 178 367 -362 O
ATOM 2416 N ALA A 235 -15.912 -20.694 14.516 1.00 92.17 N
ANISOU 2416 N ALA A 235 12107 11362 11552 225 260 -283 N
ATOM 2417 CA ALA A 235 -16.325 -19.834 15.623 1.00 89.39 C
ANISOU 2417 CA ALA A 235 11734 11037 11194 231 221 -260 C
ATOM 2418 C ALA A 235 -15.315 -18.716 15.869 1.00 87.88 C
ANISOU 2418 C ALA A 235 11511 10840 11040 254 227 -254 C
ATOM 2419 O ALA A 235 -15.702 -17.608 16.243 1.00 85.00 O
ANISOU 2419 O ALA A 235 11133 10505 10659 257 208 -241 O
ATOM 2420 CB ALA A 235 -16.548 -20.647 16.885 1.00 92.11 C
ANISOU 2420 CB ALA A 235 12073 11373 11551 230 184 -247 C
ATOM 2421 N ALA A 236 -14.031 -18.999 15.659 1.00 89.68 N
ANISOU 2421 N ALA A 236 11725 11031 11320 271 252 -265 N
ATOM 2422 CA ALA A 236 -13.001 -17.974 15.838 1.00 91.65 C
ANISOU 2422 CA ALA A 236 11943 11272 11608 292 258 -259 C
ATOM 2423 C ALA A 236 -13.119 -16.865 14.789 1.00 91.97 C
ANISOU 2423 C ALA A 236 11986 11337 11621 286 282 -261 C
ATOM 2424 O ALA A 236 -12.762 -15.725 15.067 1.00 95.18 O
ANISOU 2424 O ALA A 236 12370 11753 12041 298 273 -249 O
ATOM 2425 CB ALA A 236 -11.612 -18.589 15.811 1.00 92.48 C
ANISOU 2425 CB ALA A 236 12031 11331 11778 310 280 -271 C
ATOM 2426 N ILE A 237 -13.627 -17.193 13.604 1.00 87.22 N
ANISOU 2426 N ILE A 237 11414 10746 10981 266 310 -276 N
ATOM 2427 CA ILE A 237 -13.810 -16.183 12.566 1.00 83.69 C
ANISOU 2427 CA ILE A 237 10973 10324 10503 255 330 -275 C
ATOM 2428 C ILE A 237 -14.899 -15.187 12.979 1.00 83.01 C
ANISOU 2428 C ILE A 237 10885 10276 10380 248 294 -255 C
ATOM 2429 O ILE A 237 -14.776 -13.985 12.720 1.00 81.58 O
ANISOU 2429 O ILE A 237 10690 10110 10197 250 292 -245 O
ATOM 2430 CB ILE A 237 -14.112 -16.836 11.207 1.00 83.20 C
ANISOU 2430 CB ILE A 237 10944 10263 10405 232 367 -295 C
ATOM 2431 CG1 ILE A 237 -12.876 -17.588 10.710 1.00 84.44 C
ANISOU 2431 CG1 ILE A 237 11095 10383 10604 242 409 -318 C
ATOM 2432 CG2 ILE A 237 -14.529 -15.794 10.179 1.00 81.84 C
ANISOU 2432 CG2 ILE A 237 10781 10122 10191 214 380 -289 C
ATOM 2433 CD1 ILE A 237 -13.099 -18.444 9.478 1.00 85.34 C
ANISOU 2433 CD1 ILE A 237 11243 10494 10687 221 447 -344 C
ATOM 2434 N ILE A 238 -15.945 -15.677 13.641 1.00 84.89 N
ANISOU 2434 N ILE A 238 11135 10529 10591 239 263 -250 N
ATOM 2435 CA ILE A 238 -17.032 -14.808 14.087 1.00 87.43 C
ANISOU 2435 CA ILE A 238 11453 10887 10878 233 229 -234 C
ATOM 2436 C ILE A 238 -16.528 -13.774 15.099 1.00 88.05 C
ANISOU 2436 C ILE A 238 11497 10968 10991 256 203 -222 C
ATOM 2437 O ILE A 238 -16.917 -12.604 15.050 1.00 88.02 O
ANISOU 2437 O ILE A 238 11482 10987 10974 257 189 -213 O
ATOM 2438 CB ILE A 238 -18.201 -15.635 14.660 1.00 87.45 C
ANISOU 2438 CB ILE A 238 11474 10907 10849 218 203 -232 C
ATOM 2439 CG1 ILE A 238 -18.545 -16.794 13.720 1.00 88.68 C
ANISOU 2439 CG1 ILE A 238 11663 11052 10978 197 227 -246 C
ATOM 2440 CG2 ILE A 238 -19.426 -14.759 14.888 1.00 86.86 C
ANISOU 2440 CG2 ILE A 238 11396 10872 10734 209 174 -220 C
ATOM 2441 CD1 ILE A 238 -19.258 -16.376 12.447 1.00 90.76 C
ANISOU 2441 CD1 ILE A 238 11951 11338 11195 174 243 -249 C
ATOM 2442 N ALA A 239 -15.648 -14.201 16.002 1.00 87.33 N
ANISOU 2442 N ALA A 239 11386 10849 10944 275 197 -221 N
ATOM 2443 CA ALA A 239 -15.046 -13.274 16.957 1.00 85.58 C
ANISOU 2443 CA ALA A 239 11133 10627 10759 297 173 -210 C
ATOM 2444 C ALA A 239 -14.071 -12.320 16.270 1.00 84.06 C
ANISOU 2444 C ALA A 239 10923 10421 10593 307 196 -209 C
ATOM 2445 O ALA A 239 -13.968 -11.154 16.660 1.00 81.53 O
ANISOU 2445 O ALA A 239 10581 10112 10284 319 176 -199 O
ATOM 2446 CB ALA A 239 -14.368 -14.031 18.088 1.00 86.38 C
ANISOU 2446 CB ALA A 239 11219 10701 10899 310 158 -207 C
ATOM 2447 N GLY A 240 -13.358 -12.807 15.257 1.00 84.09 N
ANISOU 2447 N GLY A 240 10936 10405 10610 304 236 -220 N
ATOM 2448 CA GLY A 240 -12.422 -11.958 14.521 1.00 84.44 C
ANISOU 2448 CA GLY A 240 10965 10440 10678 310 261 -218 C
ATOM 2449 C GLY A 240 -13.127 -10.887 13.703 1.00 83.55 C
ANISOU 2449 C GLY A 240 10860 10358 10526 294 260 -210 C
ATOM 2450 O GLY A 240 -12.665 -9.747 13.628 1.00 82.16 O
ANISOU 2450 O GLY A 240 10663 10185 10368 302 254 -199 O
ATOM 2451 N LEU A 241 -14.250 -11.249 13.092 1.00 82.70 N
ANISOU 2451 N LEU A 241 10783 10273 10367 271 262 -215 N
ATOM 2452 CA LEU A 241 -15.033 -10.269 12.343 1.00 83.81 C
ANISOU 2452 CA LEU A 241 10932 10443 10470 254 255 -206 C
ATOM 2453 C LEU A 241 -15.700 -9.254 13.263 1.00 85.46 C
ANISOU 2453 C LEU A 241 11122 10672 10677 264 209 -192 C
ATOM 2454 O LEU A 241 -15.921 -8.112 12.863 1.00 87.13 O
ANISOU 2454 O LEU A 241 11325 10898 10882 260 198 -181 O
ATOM 2455 CB LEU A 241 -16.068 -10.964 11.461 1.00 81.69 C
ANISOU 2455 CB LEU A 241 10701 10192 10148 225 268 -214 C
ATOM 2456 CG LEU A 241 -15.494 -11.761 10.287 1.00 78.85 C
ANISOU 2456 CG LEU A 241 10362 9817 9781 211 316 -230 C
ATOM 2457 CD1 LEU A 241 -16.590 -12.532 9.569 1.00 78.07 C
ANISOU 2457 CD1 LEU A 241 10301 9733 9627 183 323 -238 C
ATOM 2458 CD2 LEU A 241 -14.715 -10.884 9.320 1.00 78.04 C
ANISOU 2458 CD2 LEU A 241 10251 9715 9686 206 342 -225 C
ATOM 2459 N PHE A 242 -16.015 -9.664 14.492 1.00 83.82 N
ANISOU 2459 N PHE A 242 10906 10465 10477 276 182 -193 N
ATOM 2460 CA PHE A 242 -16.564 -8.728 15.469 1.00 82.22 C
ANISOU 2460 CA PHE A 242 10683 10282 10275 288 140 -185 C
ATOM 2461 C PHE A 242 -15.523 -7.690 15.870 1.00 82.43 C
ANISOU 2461 C PHE A 242 10677 10293 10349 310 131 -177 C
ATOM 2462 O PHE A 242 -15.848 -6.510 16.015 1.00 83.52 O
ANISOU 2462 O PHE A 242 10800 10445 10487 315 106 -170 O
ATOM 2463 CB PHE A 242 -17.089 -9.468 16.697 1.00 82.40 C
ANISOU 2463 CB PHE A 242 10705 10311 10292 293 116 -189 C
ATOM 2464 CG PHE A 242 -17.751 -8.576 17.709 1.00 83.26 C
ANISOU 2464 CG PHE A 242 10793 10444 10396 303 75 -185 C
ATOM 2465 CD1 PHE A 242 -19.117 -8.320 17.639 1.00 82.85 C
ANISOU 2465 CD1 PHE A 242 10750 10426 10302 289 57 -186 C
ATOM 2466 CD2 PHE A 242 -17.012 -8.002 18.747 1.00 83.20 C
ANISOU 2466 CD2 PHE A 242 10757 10427 10427 326 55 -182 C
ATOM 2467 CE1 PHE A 242 -19.734 -7.500 18.570 1.00 82.64 C
ANISOU 2467 CE1 PHE A 242 10702 10423 10273 300 22 -187 C
ATOM 2468 CE2 PHE A 242 -17.622 -7.178 19.679 1.00 82.98 C
ANISOU 2468 CE2 PHE A 242 10711 10423 10395 335 19 -183 C
ATOM 2469 CZ PHE A 242 -18.986 -6.929 19.593 1.00 82.68 C
ANISOU 2469 CZ PHE A 242 10680 10419 10315 323 4 -187 C
ATOM 2470 N ALA A 243 -14.278 -8.125 16.053 1.00 81.46 N
ANISOU 2470 N ALA A 243 10544 10139 10267 323 150 -179 N
ATOM 2471 CA ALA A 243 -13.216 -7.204 16.452 1.00 81.09 C
ANISOU 2471 CA ALA A 243 10467 10076 10269 344 141 -170 C
ATOM 2472 C ALA A 243 -12.863 -6.235 15.322 1.00 82.60 C
ANISOU 2472 C ALA A 243 10653 10268 10462 337 157 -161 C
ATOM 2473 O ALA A 243 -12.655 -5.044 15.570 1.00 82.02 O
ANISOU 2473 O ALA A 243 10559 10197 10409 347 134 -151 O
ATOM 2474 CB ALA A 243 -11.991 -7.969 16.925 1.00 78.94 C
ANISOU 2474 CB ALA A 243 10182 9769 10042 359 156 -173 C
ATOM 2475 N ALEU A 244 -12.818 -6.739 14.092 0.82 83.33 N
ANISOU 2475 N ALEU A 244 10768 10361 10533 317 195 -166 N
ATOM 2476 N BLEU A 244 -12.816 -6.737 14.091 0.18 83.68 N
ANISOU 2476 N BLEU A 244 10813 10405 10578 317 195 -166 N
ATOM 2477 CA ALEU A 244 -12.459 -5.902 12.953 0.82 85.55 C
ANISOU 2477 CA ALEU A 244 11048 10646 10813 305 214 -156 C
ATOM 2478 CA BLEU A 244 -12.450 -5.893 12.954 0.18 85.26 C
ANISOU 2478 CA BLEU A 244 11011 10609 10777 305 214 -156 C
ATOM 2479 C ALEU A 244 -13.524 -4.843 12.668 0.82 86.60 C
ANISOU 2479 C ALEU A 244 11184 10806 10915 292 184 -145 C
ATOM 2480 C BLEU A 244 -13.526 -4.856 12.630 0.18 85.92 C
ANISOU 2480 C BLEU A 244 11099 10720 10827 291 185 -145 C
ATOM 2481 O ALEU A 244 -13.198 -3.714 12.301 0.82 89.94 O
ANISOU 2481 O ALEU A 244 11592 11230 11352 291 175 -130 O
ATOM 2482 O BLEU A 244 -13.208 -3.752 12.193 0.18 86.85 O
ANISOU 2482 O BLEU A 244 11202 10839 10958 289 178 -130 O
ATOM 2483 CB ALEU A 244 -12.205 -6.767 11.717 0.82 86.04 C
ANISOU 2483 CB ALEU A 244 11134 10703 10853 284 263 -167 C
ATOM 2484 CB BLEU A 244 -12.135 -6.746 11.727 0.18 85.40 C
ANISOU 2484 CB BLEU A 244 11052 10622 10775 285 263 -167 C
ATOM 2485 CG ALEU A 244 -11.280 -6.193 10.638 0.82 86.14 C
ANISOU 2485 CG ALEU A 244 11140 10712 10879 274 295 -160 C
ATOM 2486 CG BLEU A 244 -10.838 -7.558 11.779 0.18 84.98 C
ANISOU 2486 CG BLEU A 244 10988 10537 10763 298 298 -178 C
ATOM 2487 CD1ALEU A 244 -9.815 -6.257 11.055 0.82 85.41 C
ANISOU 2487 CD1ALEU A 244 11018 10589 10845 297 311 -160 C
ATOM 2488 CD1BLEU A 244 -10.665 -8.377 10.509 0.18 85.10 C
ANISOU 2488 CD1BLEU A 244 11028 10552 10755 277 348 -193 C
ATOM 2489 CD2ALEU A 244 -11.477 -6.930 9.321 0.82 85.81 C
ANISOU 2489 CD2ALEU A 244 11128 10679 10796 246 338 -172 C
ATOM 2490 CD2BLEU A 244 -9.641 -6.647 12.001 0.18 84.86 C
ANISOU 2490 CD2BLEU A 244 10938 10505 10799 316 296 -165 C
ATOM 2491 N CYS A 245 -14.790 -5.199 12.865 1.00 86.48 N
ANISOU 2491 N CYS A 245 11186 10811 10859 282 166 -151 N
ATOM 2492 CA CYS A 245 -15.884 -4.281 12.554 1.00 88.10 C
ANISOU 2492 CA CYS A 245 11395 11042 11036 269 138 -142 C
ATOM 2493 C CYS A 245 -16.003 -3.135 13.556 1.00 88.39 C
ANISOU 2493 C CYS A 245 11402 11082 11101 291 93 -135 C
ATOM 2494 O CYS A 245 -16.345 -2.017 13.172 1.00 89.16 O
ANISOU 2494 O CYS A 245 11490 11188 11197 286 72 -124 O
ATOM 2495 CB CYS A 245 -17.201 -5.030 12.442 1.00 89.55 C
ANISOU 2495 CB CYS A 245 11606 11247 11171 252 133 -150 C
ATOM 2496 SG CYS A 245 -17.369 -5.988 10.924 1.00 92.80 S
ANISOU 2496 SG CYS A 245 12058 11663 11541 218 178 -155 S
ATOM 2497 N TRP A 246 -15.728 -3.407 14.829 1.00 87.71 N
ANISOU 2497 N TRP A 246 11300 10988 11039 314 78 -143 N
ATOM 2498 CA TRP A 246 -15.988 -2.431 15.888 1.00 85.64 C
ANISOU 2498 CA TRP A 246 11012 10732 10796 335 35 -143 C
ATOM 2499 C TRP A 246 -14.795 -1.572 16.272 1.00 84.89 C
ANISOU 2499 C TRP A 246 10888 10614 10753 355 25 -134 C
ATOM 2500 O TRP A 246 -14.979 -0.440 16.720 1.00 85.72 O
ANISOU 2500 O TRP A 246 10972 10723 10875 367 -10 -131 O
ATOM 2501 CB TRP A 246 -16.535 -3.126 17.131 1.00 85.53 C
ANISOU 2501 CB TRP A 246 10997 10729 10773 345 18 -156 C
ATOM 2502 CG TRP A 246 -17.988 -3.429 17.044 1.00 86.34 C
ANISOU 2502 CG TRP A 246 11116 10861 10827 329 7 -163 C
ATOM 2503 CD1 TRP A 246 -18.554 -4.604 16.651 1.00 87.67 C
ANISOU 2503 CD1 TRP A 246 11313 11038 10960 310 28 -168 C
ATOM 2504 CD2 TRP A 246 -19.065 -2.544 17.351 1.00 87.34 C
ANISOU 2504 CD2 TRP A 246 11232 11012 10940 331 -27 -166 C
ATOM 2505 NE1 TRP A 246 -19.923 -4.508 16.697 1.00 88.96 N
ANISOU 2505 NE1 TRP A 246 11483 11232 11087 299 8 -172 N
ATOM 2506 CE2 TRP A 246 -20.265 -3.255 17.123 1.00 87.73 C
ANISOU 2506 CE2 TRP A 246 11303 11086 10944 311 -25 -171 C
ATOM 2507 CE3 TRP A 246 -19.137 -1.219 17.797 1.00 87.96 C
ANISOU 2507 CE3 TRP A 246 11284 11094 11043 347 -61 -166 C
ATOM 2508 CZ2 TRP A 246 -21.524 -2.686 17.325 1.00 87.41 C
ANISOU 2508 CZ2 TRP A 246 11256 11074 10883 308 -53 -176 C
ATOM 2509 CZ3 TRP A 246 -20.391 -0.653 17.997 1.00 88.93 C
ANISOU 2509 CZ3 TRP A 246 11400 11243 11146 345 -90 -173 C
ATOM 2510 CH2 TRP A 246 -21.568 -1.388 17.761 1.00 88.12 C
ANISOU 2510 CH2 TRP A 246 11318 11166 10999 326 -85 -178 C
ATOM 2511 N LEU A 247 -13.586 -2.101 16.128 1.00 85.47 N
ANISOU 2511 N LEU A 247 10958 10662 10854 360 54 -132 N
ATOM 2512 CA LEU A 247 -12.393 -1.387 16.584 1.00 85.65 C
ANISOU 2512 CA LEU A 247 10953 10662 10930 380 45 -123 C
ATOM 2513 C LEU A 247 -12.167 0.005 15.977 1.00 83.68 C
ANISOU 2513 C LEU A 247 10687 10410 10696 378 30 -106 C
ATOM 2514 O LEU A 247 -11.750 0.902 16.696 1.00 82.46 O
ANISOU 2514 O LEU A 247 10507 10245 10577 397 -1 -102 O
ATOM 2515 CB LEU A 247 -11.152 -2.255 16.434 1.00 86.87 C
ANISOU 2515 CB LEU A 247 11106 10789 11112 384 81 -123 C
ATOM 2516 CG LEU A 247 -10.914 -3.224 17.588 1.00 87.45 C
ANISOU 2516 CG LEU A 247 11177 10851 11199 399 76 -133 C
ATOM 2517 CD1 LEU A 247 -9.860 -4.249 17.209 1.00 90.53 C
ANISOU 2517 CD1 LEU A 247 11570 11215 11613 399 116 -136 C
ATOM 2518 CD2 LEU A 247 -10.513 -2.479 18.847 1.00 86.69 C
ANISOU 2518 CD2 LEU A 247 11053 10746 11139 422 37 -129 C
ATOM 2519 N PRO A 248 -12.445 0.210 14.669 1.00 84.21 N
ANISOU 2519 N PRO A 248 10770 10487 10738 353 49 -97 N
ATOM 2520 CA PRO A 248 -12.304 1.580 14.147 1.00 86.17 C
ANISOU 2520 CA PRO A 248 11003 10735 11004 349 28 -78 C
ATOM 2521 C PRO A 248 -13.185 2.594 14.881 1.00 89.28 C
ANISOU 2521 C PRO A 248 11382 11139 11401 361 -25 -80 C
ATOM 2522 O PRO A 248 -12.712 3.684 15.213 1.00 89.44 O
ANISOU 2522 O PRO A 248 11378 11147 11460 375 -54 -71 O
ATOM 2523 CB PRO A 248 -12.716 1.439 12.683 1.00 84.35 C
ANISOU 2523 CB PRO A 248 10797 10519 10734 316 54 -69 C
ATOM 2524 CG PRO A 248 -12.366 0.036 12.346 1.00 83.20 C
ANISOU 2524 CG PRO A 248 10672 10370 10571 308 102 -82 C
ATOM 2525 CD PRO A 248 -12.674 -0.753 13.578 1.00 83.30 C
ANISOU 2525 CD PRO A 248 10685 10381 10586 328 91 -101 C
ATOM 2526 N LEU A 249 -14.435 2.235 15.164 1.00 90.39 N
ANISOU 2526 N LEU A 249 11536 11302 11505 357 -37 -94 N
ATOM 2527 CA LEU A 249 -15.323 3.129 15.898 1.00 89.73 C
ANISOU 2527 CA LEU A 249 11438 11231 11426 370 -85 -102 C
ATOM 2528 C LEU A 249 -14.841 3.371 17.329 1.00 86.73 C
ANISOU 2528 C LEU A 249 11033 10840 11081 400 -109 -113 C
ATOM 2529 O LEU A 249 -15.093 4.430 17.898 1.00 82.33 O
ANISOU 2529 O LEU A 249 10454 10283 10544 415 -149 -117 O
ATOM 2530 CB LEU A 249 -16.753 2.586 15.896 1.00 91.67 C
ANISOU 2530 CB LEU A 249 11701 11504 11624 358 -89 -115 C
ATOM 2531 CG LEU A 249 -17.883 3.498 16.381 1.00 91.29 C
ANISOU 2531 CG LEU A 249 11639 11474 11574 366 -133 -124 C
ATOM 2532 CD1 LEU A 249 -17.926 4.806 15.599 1.00 92.80 C
ANISOU 2532 CD1 LEU A 249 11819 11658 11785 359 -158 -106 C
ATOM 2533 CD2 LEU A 249 -19.218 2.771 16.293 1.00 89.29 C
ANISOU 2533 CD2 LEU A 249 11406 11248 11272 351 -130 -135 C
ATOM 2534 N HIS A 250 -14.140 2.397 17.904 1.00 87.99 N
ANISOU 2534 N HIS A 250 11195 10989 11247 408 -87 -120 N
ATOM 2535 CA HIS A 250 -13.613 2.554 19.255 1.00 88.11 C
ANISOU 2535 CA HIS A 250 11189 10994 11293 434 -110 -129 C
ATOM 2536 C HIS A 250 -12.336 3.389 19.273 1.00 91.09 C
ANISOU 2536 C HIS A 250 11544 11343 11723 447 -118 -113 C
ATOM 2537 O HIS A 250 -12.123 4.176 20.198 1.00 91.93 O
ANISOU 2537 O HIS A 250 11628 11442 11859 467 -153 -118 O
ATOM 2538 CB HIS A 250 -13.364 1.194 19.895 1.00 85.57 C
ANISOU 2538 CB HIS A 250 10880 10671 10963 436 -89 -138 C
ATOM 2539 CG HIS A 250 -14.589 0.562 20.477 1.00 83.86 C
ANISOU 2539 CG HIS A 250 10677 10484 10704 431 -97 -155 C
ATOM 2540 ND1 HIS A 250 -15.119 0.946 21.688 1.00 83.28 N
ANISOU 2540 ND1 HIS A 250 10588 10425 10628 445 -132 -170 N
ATOM 2541 CD2 HIS A 250 -15.376 -0.442 20.024 1.00 84.26 C
ANISOU 2541 CD2 HIS A 250 10752 10551 10712 412 -76 -160 C
ATOM 2542 CE1 HIS A 250 -16.188 0.217 21.952 1.00 83.71 C
ANISOU 2542 CE1 HIS A 250 10658 10508 10642 435 -130 -181 C
ATOM 2543 NE2 HIS A 250 -16.365 -0.635 20.958 1.00 84.47 N
ANISOU 2543 NE2 HIS A 250 10779 10604 10713 415 -98 -175 N
ATOM 2544 N ILE A 251 -11.487 3.225 18.266 1.00 93.96 N
ANISOU 2544 N ILE A 251 11912 11691 12099 435 -86 -96 N
ATOM 2545 CA ILE A 251 -10.222 3.960 18.233 1.00 95.06 C
ANISOU 2545 CA ILE A 251 12029 11803 12289 445 -90 -80 C
ATOM 2546 C ILE A 251 -10.466 5.449 17.965 1.00 94.06 C
ANISOU 2546 C ILE A 251 11886 11676 12178 446 -128 -68 C
ATOM 2547 O ILE A 251 -9.727 6.300 18.463 1.00 94.67 O
ANISOU 2547 O ILE A 251 11938 11734 12299 462 -153 -60 O
ATOM 2548 CB ILE A 251 -9.249 3.332 17.220 1.00 94.29 C
ANISOU 2548 CB ILE A 251 11938 11691 12197 431 -42 -66 C
ATOM 2549 CG1 ILE A 251 -8.822 1.951 17.707 1.00 95.49 C
ANISOU 2549 CG1 ILE A 251 12098 11835 12349 437 -13 -78 C
ATOM 2550 CG2 ILE A 251 -8.018 4.199 17.043 1.00 92.13 C
ANISOU 2550 CG2 ILE A 251 11638 11393 11973 438 -47 -46 C
ATOM 2551 CD1 ILE A 251 -8.063 1.105 16.714 1.00 91.57 C
ANISOU 2551 CD1 ILE A 251 11612 11328 11852 423 39 -74 C
ATOM 2552 N ILE A 252 -11.513 5.765 17.212 1.00 90.74 N
ANISOU 2552 N ILE A 252 11477 11275 11725 428 -134 -67 N
ATOM 2553 CA ILE A 252 -11.911 7.162 17.038 1.00 86.95 C
ANISOU 2553 CA ILE A 252 10982 10795 11262 429 -176 -58 C
ATOM 2554 C ILE A 252 -12.315 7.767 18.388 1.00 87.89 C
ANISOU 2554 C ILE A 252 11081 10914 11399 456 -221 -78 C
ATOM 2555 O ILE A 252 -12.012 8.932 18.673 1.00 89.79 O
ANISOU 2555 O ILE A 252 11298 11139 11678 469 -258 -72 O
ATOM 2556 CB ILE A 252 -13.025 7.299 15.992 1.00 84.30 C
ANISOU 2556 CB ILE A 252 10664 10479 10886 404 -175 -52 C
ATOM 2557 CG1 ILE A 252 -12.491 6.918 14.611 1.00 84.21 C
ANISOU 2557 CG1 ILE A 252 10669 10467 10860 375 -134 -30 C
ATOM 2558 CG2 ILE A 252 -13.579 8.713 15.982 1.00 83.95 C
ANISOU 2558 CG2 ILE A 252 10602 10434 10863 408 -226 -46 C
ATOM 2559 CD1 ILE A 252 -13.535 6.824 13.524 1.00 85.10 C
ANISOU 2559 CD1 ILE A 252 10806 10601 10927 345 -127 -24 C
ATOM 2560 N ASN A 253 -12.984 6.973 19.220 1.00 88.92 N
ANISOU 2560 N ASN A 253 11220 11062 11502 464 -219 -102 N
ATOM 2561 CA ASN A 253 -13.287 7.405 20.580 1.00 90.33 C
ANISOU 2561 CA ASN A 253 11381 11245 11694 489 -256 -125 C
ATOM 2562 C ASN A 253 -12.024 7.604 21.408 1.00 90.78 C
ANISOU 2562 C ASN A 253 11421 11277 11797 508 -265 -121 C
ATOM 2563 O ASN A 253 -11.972 8.504 22.250 1.00 90.13 O
ANISOU 2563 O ASN A 253 11317 11187 11741 527 -305 -131 O
ATOM 2564 CB ASN A 253 -14.224 6.416 21.266 1.00 90.26 C
ANISOU 2564 CB ASN A 253 11387 11264 11643 488 -247 -148 C
ATOM 2565 CG ASN A 253 -15.646 6.517 20.763 1.00 91.36 C
ANISOU 2565 CG ASN A 253 11537 11431 11746 475 -254 -157 C
ATOM 2566 OD1 ASN A 253 -15.928 7.220 19.790 1.00 94.73 O
ANISOU 2566 OD1 ASN A 253 11964 11855 12176 463 -262 -143 O
ATOM 2567 ND2 ASN A 253 -16.559 5.812 21.426 1.00 90.20 N
ANISOU 2567 ND2 ASN A 253 11399 11311 11563 475 -252 -178 N
ATOM 2568 N CYS A 254 -11.008 6.774 21.175 1.00 92.48 N
ANISOU 2568 N CYS A 254 11642 11476 12020 503 -230 -108 N
ATOM 2569 CA CYS A 254 -9.730 6.950 21.866 1.00 94.69 C
ANISOU 2569 CA CYS A 254 11903 11728 12346 520 -238 -100 C
ATOM 2570 C CYS A 254 -9.024 8.231 21.428 1.00 97.67 C
ANISOU 2570 C CYS A 254 12259 12082 12767 523 -260 -80 C
ATOM 2571 O CYS A 254 -8.373 8.881 22.243 1.00101.02 O
ANISOU 2571 O CYS A 254 12663 12489 13232 542 -290 -80 O
ATOM 2572 CB CYS A 254 -8.827 5.744 21.643 1.00 95.79 C
ANISOU 2572 CB CYS A 254 12052 11854 12488 513 -194 -91 C
ATOM 2573 SG CYS A 254 -9.409 4.242 22.452 1.00 97.27 S
ANISOU 2573 SG CYS A 254 12260 12061 12637 512 -178 -112 S
ATOM 2574 N PHE A 255 -9.151 8.595 20.156 1.00 97.70 N
ANISOU 2574 N PHE A 255 12269 12088 12764 504 -248 -62 N
ATOM 2575 CA PHE A 255 -8.506 9.809 19.669 1.00 95.49 C
ANISOU 2575 CA PHE A 255 11969 11787 12525 504 -270 -38 C
ATOM 2576 C PHE A 255 -9.241 11.057 20.141 1.00 92.83 C
ANISOU 2576 C PHE A 255 11617 11452 12202 516 -326 -49 C
ATOM 2577 O PHE A 255 -8.602 12.055 20.483 1.00 94.61 O
ANISOU 2577 O PHE A 255 11819 11654 12473 529 -359 -40 O
ATOM 2578 CB PHE A 255 -8.400 9.792 18.149 1.00 97.64 C
ANISOU 2578 CB PHE A 255 12253 12063 12783 475 -240 -13 C
ATOM 2579 CG PHE A 255 -7.103 9.253 17.636 1.00 99.27 C
ANISOU 2579 CG PHE A 255 12457 12254 13008 467 -199 6 C
ATOM 2580 CD1 PHE A 255 -5.991 10.085 17.507 1.00 99.35 C
ANISOU 2580 CD1 PHE A 255 12443 12240 13066 470 -211 30 C
ATOM 2581 CD2 PHE A 255 -6.988 7.916 17.258 1.00 99.54 C
ANISOU 2581 CD2 PHE A 255 12511 12296 13012 457 -148 -1 C
ATOM 2582 CE1 PHE A 255 -4.793 9.590 17.017 1.00100.85 C
ANISOU 2582 CE1 PHE A 255 12628 12417 13275 463 -171 46 C
ATOM 2583 CE2 PHE A 255 -5.779 7.420 16.782 1.00100.03 C
ANISOU 2583 CE2 PHE A 255 12568 12343 13094 451 -108 13 C
ATOM 2584 CZ PHE A 255 -4.685 8.255 16.657 1.00101.29 C
ANISOU 2584 CZ PHE A 255 12702 12480 13302 455 -119 37 C
ATOM 2585 N THR A 256 -10.573 11.003 20.162 1.00 89.72 N
ANISOU 2585 N THR A 256 11234 11083 11772 513 -336 -68 N
ATOM 2586 CA THR A 256 -11.359 12.134 20.643 1.00 87.60 C
ANISOU 2586 CA THR A 256 10950 10817 11518 527 -387 -84 C
ATOM 2587 C THR A 256 -11.086 12.399 22.125 1.00 87.15 C
ANISOU 2587 C THR A 256 10875 10752 11485 555 -417 -108 C
ATOM 2588 O THR A 256 -11.045 13.549 22.558 1.00 89.49 O
ANISOU 2588 O THR A 256 11151 11035 11818 571 -461 -113 O
ATOM 2589 CB THR A 256 -12.855 11.893 20.407 1.00 85.86 C
ANISOU 2589 CB THR A 256 10744 10627 11253 518 -388 -102 C
ATOM 2590 OG1 THR A 256 -13.075 11.651 19.017 1.00 88.59 O
ANISOU 2590 OG1 THR A 256 11107 10979 11575 488 -362 -78 O
ATOM 2591 CG2 THR A 256 -13.668 13.100 20.825 1.00 83.92 C
ANISOU 2591 CG2 THR A 256 10478 10381 11027 532 -441 -119 C
ATOM 2592 N PHE A 257 -10.868 11.333 22.886 1.00 88.01 N
ANISOU 2592 N PHE A 257 10994 10870 11576 561 -393 -121 N
ATOM 2593 CA PHE A 257 -10.712 11.437 24.332 1.00 91.00 C
ANISOU 2593 CA PHE A 257 11361 11249 11968 584 -419 -145 C
ATOM 2594 C PHE A 257 -9.279 11.764 24.750 1.00 92.30 C
ANISOU 2594 C PHE A 257 11509 11379 12181 595 -429 -129 C
ATOM 2595 O PHE A 257 -9.053 12.669 25.554 1.00 90.44 O
ANISOU 2595 O PHE A 257 11254 11131 11978 614 -470 -139 O
ATOM 2596 CB PHE A 257 -11.186 10.141 24.999 1.00 93.04 C
ANISOU 2596 CB PHE A 257 11636 11533 12183 581 -393 -164 C
ATOM 2597 CG PHE A 257 -11.108 10.161 26.489 1.00 94.47 C
ANISOU 2597 CG PHE A 257 11807 11718 12368 600 -418 -189 C
ATOM 2598 CD1 PHE A 257 -11.683 11.204 27.215 1.00 95.96 C
ANISOU 2598 CD1 PHE A 257 11979 11914 12568 617 -461 -215 C
ATOM 2599 CD2 PHE A 257 -10.460 9.140 27.175 1.00 94.42 C
ANISOU 2599 CD2 PHE A 257 11808 11710 12357 600 -399 -187 C
ATOM 2600 CE1 PHE A 257 -11.617 11.222 28.599 1.00 97.56 C
ANISOU 2600 CE1 PHE A 257 12173 12125 12771 632 -483 -240 C
ATOM 2601 CE2 PHE A 257 -10.389 9.154 28.557 1.00 96.05 C
ANISOU 2601 CE2 PHE A 257 12007 11923 12565 613 -424 -207 C
ATOM 2602 CZ PHE A 257 -10.968 10.195 29.273 1.00 97.57 C
ANISOU 2602 CZ PHE A 257 12183 12125 12763 629 -465 -235 C
ATOM 2603 N PHE A 258 -8.313 11.032 24.205 1.00 94.78 N
ANISOU 2603 N PHE A 258 11830 11679 12503 584 -392 -104 N
ATOM 2604 CA PHE A 258 -6.933 11.162 24.659 1.00 94.98 C
ANISOU 2604 CA PHE A 258 11840 11674 12575 594 -397 -88 C
ATOM 2605 C PHE A 258 -6.216 12.365 24.057 1.00 98.20 C
ANISOU 2605 C PHE A 258 12228 12055 13029 595 -420 -62 C
ATOM 2606 O PHE A 258 -5.426 13.016 24.736 1.00100.03 O
ANISOU 2606 O PHE A 258 12441 12263 13304 610 -451 -58 O
ATOM 2607 CB PHE A 258 -6.149 9.877 24.397 1.00 91.08 C
ANISOU 2607 CB PHE A 258 11357 11174 12076 585 -350 -74 C
ATOM 2608 CG PHE A 258 -6.467 8.770 25.353 1.00 90.64 C
ANISOU 2608 CG PHE A 258 11314 11134 11991 589 -340 -94 C
ATOM 2609 CD1 PHE A 258 -6.158 8.898 26.709 1.00 91.30 C
ANISOU 2609 CD1 PHE A 258 11387 11211 12091 605 -371 -107 C
ATOM 2610 CD2 PHE A 258 -7.060 7.591 24.908 1.00 89.71 C
ANISOU 2610 CD2 PHE A 258 11220 11037 11829 574 -301 -100 C
ATOM 2611 CE1 PHE A 258 -6.445 7.878 27.600 1.00 89.97 C
ANISOU 2611 CE1 PHE A 258 11231 11059 11896 605 -364 -123 C
ATOM 2612 CE2 PHE A 258 -7.347 6.564 25.796 1.00 89.06 C
ANISOU 2612 CE2 PHE A 258 11149 10968 11722 575 -294 -116 C
ATOM 2613 CZ PHE A 258 -7.043 6.708 27.147 1.00 88.94 C
ANISOU 2613 CZ PHE A 258 11123 10949 11723 590 -326 -126 C
ATOM 2614 N CYS A 259 -6.486 12.659 22.789 1.00101.31 N
ANISOU 2614 N CYS A 259 12626 12452 13414 576 -407 -44 N
ATOM 2615 CA CYS A 259 -5.800 13.743 22.091 1.00107.02 C
ANISOU 2615 CA CYS A 259 13333 13152 14180 571 -426 -15 C
ATOM 2616 C CYS A 259 -6.732 14.940 21.912 1.00111.39 C
ANISOU 2616 C CYS A 259 13878 13709 14738 572 -471 -21 C
ATOM 2617 O CYS A 259 -7.556 14.947 21.001 1.00112.03 O
ANISOU 2617 O CYS A 259 13971 13806 14789 554 -462 -17 O
ATOM 2618 CB CYS A 259 -5.262 13.267 20.736 1.00108.77 C
ANISOU 2618 CB CYS A 259 13563 13374 14393 545 -379 16 C
ATOM 2619 SG CYS A 259 -4.343 14.547 19.846 1.00109.66 S
ANISOU 2619 SG CYS A 259 13652 13460 14554 533 -400 57 S
ATOM 2620 N PRO A 260 -6.607 15.974 22.765 1.00115.15 N
ANISOU 2620 N PRO A 260 14334 14167 15252 593 -523 -32 N
ATOM 2621 CA PRO A 260 -7.409 17.183 22.542 1.00119.46 C
ANISOU 2621 CA PRO A 260 14868 14710 15811 596 -570 -37 C
ATOM 2622 C PRO A 260 -6.823 18.107 21.474 1.00122.26 C
ANISOU 2622 C PRO A 260 15211 15042 16201 579 -585 3 C
ATOM 2623 O PRO A 260 -7.559 18.895 20.884 1.00124.64 O
ANISOU 2623 O PRO A 260 15509 15344 16505 571 -612 8 O
ATOM 2624 CB PRO A 260 -7.394 17.865 23.905 1.00120.81 C
ANISOU 2624 CB PRO A 260 15022 14869 16012 625 -617 -66 C
ATOM 2625 CG PRO A 260 -6.088 17.464 24.492 1.00121.64 C
ANISOU 2625 CG PRO A 260 15121 14955 16141 632 -605 -55 C
ATOM 2626 CD PRO A 260 -5.778 16.085 23.977 1.00117.78 C
ANISOU 2626 CD PRO A 260 14652 14481 15618 615 -544 -41 C
ATOM 2627 N ASP A 261 -5.517 18.015 21.238 1.00123.96 N
ANISOU 2627 N ASP A 261 15418 15237 16444 573 -568 33 N
ATOM 2628 CA ASP A 261 -4.863 18.790 20.196 1.00124.86 C
ANISOU 2628 CA ASP A 261 15521 15333 16588 553 -576 76 C
ATOM 2629 C ASP A 261 -5.219 18.315 18.799 1.00119.09 C
ANISOU 2629 C ASP A 261 14808 14623 15818 520 -536 97 C
ATOM 2630 O ASP A 261 -5.143 19.096 17.844 1.00121.22 O
ANISOU 2630 O ASP A 261 15071 14885 16101 499 -552 129 O
ATOM 2631 CB ASP A 261 -3.348 18.783 20.396 1.00132.39 C
ANISOU 2631 CB ASP A 261 16459 16262 17583 556 -568 100 C
ATOM 2632 CG ASP A 261 -2.918 19.580 21.613 1.00138.15 C
ANISOU 2632 CG ASP A 261 17167 16964 18360 585 -620 87 C
ATOM 2633 OD1 ASP A 261 -3.740 20.357 22.149 1.00145.80 O
ANISOU 2633 OD1 ASP A 261 18130 17930 19336 600 -668 62 O
ATOM 2634 OD2 ASP A 261 -1.752 19.432 22.036 1.00145.33 O
ANISOU 2634 OD2 ASP A 261 18064 17854 19301 592 -614 100 O
ATOM 2635 N CYS A 262 -5.600 17.045 18.673 1.00111.56 N
ANISOU 2635 N CYS A 262 13878 13696 14816 514 -485 82 N
ATOM 2636 CA CYS A 262 -6.015 16.502 17.384 1.00111.13 C
ANISOU 2636 CA CYS A 262 13844 13663 14718 482 -445 98 C
ATOM 2637 C CYS A 262 -7.347 17.103 16.963 1.00114.00 C
ANISOU 2637 C CYS A 262 14214 14039 15061 473 -476 92 C
ATOM 2638 O CYS A 262 -8.226 17.325 17.795 1.00116.90 O
ANISOU 2638 O CYS A 262 14579 14411 15426 494 -508 60 O
ATOM 2639 CB CYS A 262 -6.131 14.982 17.449 1.00107.16 C
ANISOU 2639 CB CYS A 262 13364 13181 14169 480 -387 79 C
ATOM 2640 SG CYS A 262 -4.607 14.117 17.882 1.00104.80 S
ANISOU 2640 SG CYS A 262 13058 12867 13896 490 -347 85 S
ATOM 2641 N SER A 263 -7.489 17.371 15.669 1.00113.40 N
ANISOU 2641 N SER A 263 14146 13970 14971 440 -468 122 N
ATOM 2642 CA SER A 263 -8.783 17.762 15.125 1.00111.70 C
ANISOU 2642 CA SER A 263 13939 13769 14731 427 -492 119 C
ATOM 2643 C SER A 263 -9.714 16.557 15.104 1.00110.84 C
ANISOU 2643 C SER A 263 13858 13691 14564 423 -453 93 C
ATOM 2644 O SER A 263 -9.299 15.443 14.770 1.00115.78 O
ANISOU 2644 O SER A 263 14502 14330 15159 412 -397 94 O
ATOM 2645 CB SER A 263 -8.629 18.356 13.730 1.00112.17 C
ANISOU 2645 CB SER A 263 14001 13827 14790 389 -496 163 C
ATOM 2646 OG SER A 263 -7.965 19.604 13.789 1.00106.87 O
ANISOU 2646 OG SER A 263 13303 13128 14176 392 -543 188 O
ATOM 2647 N HIS A 264 -10.974 16.788 15.466 1.00107.82 N
ANISOU 2647 N HIS A 264 13478 13320 14170 433 -483 68 N
ATOM 2648 CA HIS A 264 -11.950 15.712 15.553 1.00107.24 C
ANISOU 2648 CA HIS A 264 13428 13276 14043 430 -452 42 C
ATOM 2649 C HIS A 264 -12.105 15.016 14.208 1.00103.64 C
ANISOU 2649 C HIS A 264 12999 12839 13541 393 -409 64 C
ATOM 2650 O HIS A 264 -11.945 15.640 13.150 1.00106.74 O
ANISOU 2650 O HIS A 264 13391 13226 13939 365 -418 98 O
ATOM 2651 CB HIS A 264 -13.293 16.244 16.052 1.00108.77 C
ANISOU 2651 CB HIS A 264 13614 13477 14235 444 -495 15 C
ATOM 2652 CG HIS A 264 -14.299 15.172 16.336 1.00111.54 C
ANISOU 2652 CG HIS A 264 13986 13859 14535 446 -468 -14 C
ATOM 2653 ND1 HIS A 264 -15.060 14.587 15.347 1.00115.21 N
ANISOU 2653 ND1 HIS A 264 14476 14346 14954 417 -443 -5 N
ATOM 2654 CD2 HIS A 264 -14.664 14.574 17.494 1.00111.16 C
ANISOU 2654 CD2 HIS A 264 13938 13824 14474 470 -462 -51 C
ATOM 2655 CE1 HIS A 264 -15.849 13.674 15.884 1.00114.96 C
ANISOU 2655 CE1 HIS A 264 14456 14337 14885 424 -424 -34 C
ATOM 2656 NE2 HIS A 264 -15.631 13.648 17.185 1.00111.29 N
ANISOU 2656 NE2 HIS A 264 13977 13870 14439 456 -435 -62 N
ATOM 2657 N ALA A 265 -12.392 13.718 14.255 1.00 99.06 N
ANISOU 2657 N ALA A 265 12442 12280 12916 389 -362 46 N
ATOM 2658 CA ALA A 265 -12.560 12.938 13.038 1.00 97.27 C
ANISOU 2658 CA ALA A 265 12243 12072 12642 354 -318 61 C
ATOM 2659 C ALA A 265 -13.694 13.518 12.190 1.00 95.74 C
ANISOU 2659 C ALA A 265 12057 11890 12429 330 -346 74 C
ATOM 2660 O ALA A 265 -14.742 13.862 12.724 1.00 99.04 O
ANISOU 2660 O ALA A 265 12470 12313 12849 344 -381 54 O
ATOM 2661 CB ALA A 265 -12.820 11.481 13.363 1.00 94.30 C
ANISOU 2661 CB ALA A 265 11890 11715 12225 358 -272 35 C
ATOM 2662 N PRO A 266 -13.482 13.657 10.872 1.00 92.25 N
ANISOU 2662 N PRO A 266 11628 11452 11971 293 -331 107 N
ATOM 2663 CA PRO A 266 -14.503 14.269 10.021 1.00 92.37 C
ANISOU 2663 CA PRO A 266 11649 11475 11970 266 -362 125 C
ATOM 2664 C PRO A 266 -15.797 13.460 9.975 1.00 92.74 C
ANISOU 2664 C PRO A 266 11720 11548 11969 260 -351 102 C
ATOM 2665 O PRO A 266 -15.834 12.292 10.383 1.00 94.74 O
ANISOU 2665 O PRO A 266 11990 11815 12193 270 -310 78 O
ATOM 2666 CB PRO A 266 -13.830 14.331 8.651 1.00 91.94 C
ANISOU 2666 CB PRO A 266 11608 11425 11900 224 -337 164 C
ATOM 2667 CG PRO A 266 -12.777 13.281 8.695 1.00 91.02 C
ANISOU 2667 CG PRO A 266 11501 11313 11770 227 -275 156 C
ATOM 2668 CD PRO A 266 -12.295 13.250 10.106 1.00 89.63 C
ANISOU 2668 CD PRO A 266 11303 11119 11633 272 -285 130 C
ATOM 2669 N LEU A 267 -16.855 14.102 9.498 1.00 92.87 N
ANISOU 2669 N LEU A 267 11736 11568 11980 245 -390 112 N
ATOM 2670 CA LEU A 267 -18.176 13.496 9.493 1.00 90.13 C
ANISOU 2670 CA LEU A 267 11407 11244 11594 240 -388 93 C
ATOM 2671 C LEU A 267 -18.304 12.313 8.536 1.00 90.49 C
ANISOU 2671 C LEU A 267 11491 11313 11579 206 -334 99 C
ATOM 2672 O LEU A 267 -19.052 11.372 8.810 1.00 90.51 O
ANISOU 2672 O LEU A 267 11511 11334 11546 210 -314 75 O
ATOM 2673 CB LEU A 267 -19.253 14.540 9.202 1.00 85.20 C
ANISOU 2673 CB LEU A 267 10771 10616 10987 232 -447 103 C
ATOM 2674 CG LEU A 267 -20.694 14.110 9.493 1.00 79.82 C
ANISOU 2674 CG LEU A 267 10096 9953 10278 237 -456 77 C
ATOM 2675 CD1 LEU A 267 -20.856 13.651 10.935 1.00 77.69 C
ANISOU 2675 CD1 LEU A 267 9815 9690 10016 279 -450 33 C
ATOM 2676 CD2 LEU A 267 -21.643 15.251 9.184 1.00 78.94 C
ANISOU 2676 CD2 LEU A 267 9967 9832 10194 230 -518 90 C
ATOM 2677 N TRP A 268 -17.593 12.359 7.413 1.00 89.86 N
ANISOU 2677 N TRP A 268 11424 11233 11487 172 -312 131 N
ATOM 2678 CA TRP A 268 -17.633 11.246 6.468 1.00 89.59 C
ANISOU 2678 CA TRP A 268 11425 11221 11394 139 -259 135 C
ATOM 2679 C TRP A 268 -16.987 9.988 7.052 1.00 88.64 C
ANISOU 2679 C TRP A 268 11315 11105 11259 159 -204 107 C
ATOM 2680 O TRP A 268 -17.422 8.876 6.764 1.00 86.22 O
ANISOU 2680 O TRP A 268 11037 10816 10907 147 -168 92 O
ATOM 2681 CB TRP A 268 -16.986 11.625 5.140 1.00 91.27 C
ANISOU 2681 CB TRP A 268 11648 11436 11595 97 -246 174 C
ATOM 2682 CG TRP A 268 -15.527 11.958 5.246 1.00 93.91 C
ANISOU 2682 CG TRP A 268 11963 11754 11965 105 -231 187 C
ATOM 2683 CD1 TRP A 268 -14.987 13.188 5.481 1.00 93.97 C
ANISOU 2683 CD1 TRP A 268 11940 11739 12026 114 -273 208 C
ATOM 2684 CD2 TRP A 268 -14.427 11.054 5.124 1.00 95.26 C
ANISOU 2684 CD2 TRP A 268 12143 11928 12124 105 -170 179 C
ATOM 2685 NE1 TRP A 268 -13.616 13.109 5.499 1.00 94.86 N
ANISOU 2685 NE1 TRP A 268 12042 11843 12159 119 -242 216 N
ATOM 2686 CE2 TRP A 268 -13.245 11.809 5.293 1.00 95.58 C
ANISOU 2686 CE2 TRP A 268 12156 11950 12212 114 -178 197 C
ATOM 2687 CE3 TRP A 268 -14.321 9.675 4.889 1.00 96.14 C
ANISOU 2687 CE3 TRP A 268 12281 12055 12192 99 -110 157 C
ATOM 2688 CZ2 TRP A 268 -11.971 11.236 5.233 1.00 95.94 C
ANISOU 2688 CZ2 TRP A 268 12199 11993 12263 117 -127 195 C
ATOM 2689 CZ3 TRP A 268 -13.055 9.104 4.833 1.00 95.05 C
ANISOU 2689 CZ3 TRP A 268 12140 11913 12061 103 -60 153 C
ATOM 2690 CH2 TRP A 268 -11.896 9.886 5.005 1.00 95.35 C
ANISOU 2690 CH2 TRP A 268 12149 11933 12147 112 -68 172 C
ATOM 2691 N LEU A 269 -15.955 10.165 7.873 1.00 88.27 N
ANISOU 2691 N LEU A 269 11246 11040 11255 189 -201 99 N
ATOM 2692 CA LEU A 269 -15.313 9.028 8.517 1.00 88.84 C
ANISOU 2692 CA LEU A 269 11323 11111 11321 210 -156 74 C
ATOM 2693 C LEU A 269 -16.189 8.451 9.623 1.00 91.11 C
ANISOU 2693 C LEU A 269 11611 11406 11599 237 -166 40 C
ATOM 2694 O LEU A 269 -16.251 7.229 9.798 1.00 90.68 O
ANISOU 2694 O LEU A 269 11577 11362 11516 239 -127 21 O
ATOM 2695 CB LEU A 269 -13.942 9.418 9.060 1.00 85.37 C
ANISOU 2695 CB LEU A 269 10857 10648 10930 232 -153 79 C
ATOM 2696 CG LEU A 269 -13.016 8.254 9.401 1.00 84.34 C
ANISOU 2696 CG LEU A 269 10733 10514 10797 244 -100 62 C
ATOM 2697 CD1 LEU A 269 -12.422 7.650 8.138 1.00 83.96 C
ANISOU 2697 CD1 LEU A 269 10706 10476 10719 211 -47 76 C
ATOM 2698 CD2 LEU A 269 -11.919 8.724 10.338 1.00 85.11 C
ANISOU 2698 CD2 LEU A 269 10799 10587 10951 276 -113 62 C
ATOM 2699 N MET A 270 -16.865 9.326 10.366 1.00 91.55 N
ANISOU 2699 N MET A 270 11646 11457 11682 258 -217 33 N
ATOM 2700 CA MET A 270 -17.787 8.881 11.414 1.00 89.59 C
ANISOU 2700 CA MET A 270 11396 11221 11424 281 -229 1 C
ATOM 2701 C MET A 270 -18.929 8.068 10.807 1.00 88.20 C
ANISOU 2701 C MET A 270 11249 11069 11193 257 -213 -4 C
ATOM 2702 O MET A 270 -19.327 7.038 11.361 1.00 86.62 O
ANISOU 2702 O MET A 270 11062 10883 10967 265 -192 -28 O
ATOM 2703 CB MET A 270 -18.352 10.070 12.181 1.00 88.60 C
ANISOU 2703 CB MET A 270 11241 11088 11336 305 -288 -7 C
ATOM 2704 CG MET A 270 -17.337 10.932 12.908 1.00 89.14 C
ANISOU 2704 CG MET A 270 11279 11131 11460 331 -311 -6 C
ATOM 2705 SD MET A 270 -16.761 10.232 14.465 1.00 92.13 S
ANISOU 2705 SD MET A 270 11648 11507 11852 369 -296 -39 S
ATOM 2706 CE MET A 270 -18.250 9.495 15.145 1.00 93.21 C
ANISOU 2706 CE MET A 270 11795 11673 11948 376 -299 -72 C
ATOM 2707 N TYR A 271 -19.459 8.529 9.673 1.00 85.75 N
ANISOU 2707 N TYR A 271 10950 10765 10866 225 -226 19 N
ATOM 2708 CA TYR A 271 -20.471 7.762 8.956 1.00 85.72 C
ANISOU 2708 CA TYR A 271 10976 10783 10809 197 -210 19 C
ATOM 2709 C TYR A 271 -19.935 6.400 8.523 1.00 85.56 C
ANISOU 2709 C TYR A 271 10987 10771 10751 182 -150 13 C
ATOM 2710 O TYR A 271 -20.625 5.389 8.657 1.00 86.53 O
ANISOU 2710 O TYR A 271 11129 10909 10837 179 -131 -5 O
ATOM 2711 CB TYR A 271 -20.978 8.541 7.745 1.00 87.10 C
ANISOU 2711 CB TYR A 271 11159 10961 10975 161 -235 50 C
ATOM 2712 CG TYR A 271 -21.845 9.732 8.068 1.00 89.77 C
ANISOU 2712 CG TYR A 271 11471 11293 11346 172 -297 53 C
ATOM 2713 CD1 TYR A 271 -22.585 9.796 9.252 1.00 89.06 C
ANISOU 2713 CD1 TYR A 271 11362 11207 11272 205 -322 23 C
ATOM 2714 CD2 TYR A 271 -21.954 10.789 7.166 1.00 93.21 C
ANISOU 2714 CD2 TYR A 271 11900 11719 11795 147 -332 87 C
ATOM 2715 CE1 TYR A 271 -23.388 10.890 9.530 1.00 91.93 C
ANISOU 2715 CE1 TYR A 271 11699 11565 11667 216 -378 22 C
ATOM 2716 CE2 TYR A 271 -22.752 11.888 7.432 1.00 95.95 C
ANISOU 2716 CE2 TYR A 271 12222 12058 12178 157 -391 89 C
ATOM 2717 CZ TYR A 271 -23.469 11.934 8.614 1.00 95.89 C
ANISOU 2717 CZ TYR A 271 12193 12052 12187 193 -413 55 C
ATOM 2718 OH TYR A 271 -24.262 13.024 8.877 1.00 97.69 O
ANISOU 2718 OH TYR A 271 12393 12270 12452 205 -471 53 O
ATOM 2719 N LEU A 272 -18.700 6.376 8.030 1.00 85.77 N
ANISOU 2719 N LEU A 272 11014 10786 10788 175 -120 26 N
ATOM 2720 CA LEU A 272 -18.100 5.130 7.564 1.00 88.03 C
ANISOU 2720 CA LEU A 272 11327 11077 11044 162 -62 19 C
ATOM 2721 C LEU A 272 -17.850 4.151 8.709 1.00 87.37 C
ANISOU 2721 C LEU A 272 11241 10990 10967 193 -42 -11 C
ATOM 2722 O LEU A 272 -17.973 2.941 8.526 1.00 81.45 O
ANISOU 2722 O LEU A 272 10516 10248 10183 184 -6 -25 O
ATOM 2723 CB LEU A 272 -16.804 5.420 6.807 1.00 88.86 C
ANISOU 2723 CB LEU A 272 11428 11171 11163 147 -36 39 C
ATOM 2724 CG LEU A 272 -16.193 4.277 5.995 1.00 87.96 C
ANISOU 2724 CG LEU A 272 11342 11065 11016 126 26 33 C
ATOM 2725 CD1 LEU A 272 -17.045 3.918 4.783 1.00 86.44 C
ANISOU 2725 CD1 LEU A 272 11184 10894 10766 84 38 42 C
ATOM 2726 CD2 LEU A 272 -14.783 4.652 5.563 1.00 85.69 C
ANISOU 2726 CD2 LEU A 272 11040 10765 10755 122 50 49 C
ATOM 2727 N ALA A 273 -17.504 4.671 9.885 1.00 88.59 N
ANISOU 2727 N ALA A 273 11364 11130 11164 228 -68 -20 N
ATOM 2728 CA ALA A 273 -17.241 3.809 11.042 1.00 89.70 C
ANISOU 2728 CA ALA A 273 11501 11267 11313 256 -55 -45 C
ATOM 2729 C ALA A 273 -18.532 3.202 11.588 1.00 89.77 C
ANISOU 2729 C ALA A 273 11521 11296 11290 258 -67 -65 C
ATOM 2730 O ALA A 273 -18.550 2.035 11.992 1.00 90.04 O
ANISOU 2730 O ALA A 273 11571 11335 11306 263 -41 -81 O
ATOM 2731 CB ALA A 273 -16.501 4.574 12.129 1.00 88.09 C
ANISOU 2731 CB ALA A 273 11263 11044 11163 289 -82 -48 C
ATOM 2732 N ILE A 274 -19.608 3.986 11.598 1.00 87.59 N
ANISOU 2732 N ILE A 274 11238 11032 11010 256 -106 -62 N
ATOM 2733 CA ILE A 274 -20.878 3.515 12.141 1.00 85.44 C
ANISOU 2733 CA ILE A 274 10972 10781 10710 258 -120 -80 C
ATOM 2734 C ILE A 274 -21.434 2.368 11.291 1.00 86.66 C
ANISOU 2734 C ILE A 274 11163 10951 10813 228 -87 -80 C
ATOM 2735 O ILE A 274 -21.815 1.318 11.821 1.00 84.69 O
ANISOU 2735 O ILE A 274 10926 10712 10541 232 -72 -97 O
ATOM 2736 CB ILE A 274 -21.883 4.667 12.259 1.00 83.37 C
ANISOU 2736 CB ILE A 274 10690 10526 10460 262 -170 -78 C
ATOM 2737 CG1 ILE A 274 -21.376 5.703 13.258 1.00 80.29 C
ANISOU 2737 CG1 ILE A 274 10263 10121 10121 295 -203 -85 C
ATOM 2738 CG2 ILE A 274 -23.240 4.147 12.700 1.00 84.11 C
ANISOU 2738 CG2 ILE A 274 10790 10645 10523 261 -180 -96 C
ATOM 2739 CD1 ILE A 274 -22.144 7.003 13.234 1.00 79.12 C
ANISOU 2739 CD1 ILE A 274 10093 9973 9997 299 -253 -81 C
ATOM 2740 N VAL A 275 -21.452 2.559 9.980 1.00 88.58 N
ANISOU 2740 N VAL A 275 11424 11195 11037 197 -77 -59 N
ATOM 2741 CA VAL A 275 -21.956 1.524 9.079 1.00 87.94 C
ANISOU 2741 CA VAL A 275 11380 11127 10905 166 -47 -59 C
ATOM 2742 C VAL A 275 -21.064 0.282 9.105 1.00 87.67 C
ANISOU 2742 C VAL A 275 11363 11085 10862 168 2 -72 C
ATOM 2743 O VAL A 275 -21.549 -0.835 8.931 1.00 87.11 O
ANISOU 2743 O VAL A 275 11319 11024 10756 156 24 -83 O
ATOM 2744 CB VAL A 275 -22.151 2.050 7.643 1.00 86.24 C
ANISOU 2744 CB VAL A 275 11181 10916 10669 129 -48 -33 C
ATOM 2745 CG1 VAL A 275 -23.242 3.111 7.616 1.00 84.30 C
ANISOU 2745 CG1 VAL A 275 10921 10678 10431 125 -100 -22 C
ATOM 2746 CG2 VAL A 275 -20.847 2.586 7.059 1.00 85.65 C
ANISOU 2746 CG2 VAL A 275 11099 10825 10618 124 -31 -16 C
ATOM 2747 N LEU A 276 -19.766 0.473 9.337 1.00 85.78 N
ANISOU 2747 N LEU A 276 11107 10825 10658 185 18 -70 N
ATOM 2748 CA LEU A 276 -18.869 -0.670 9.451 1.00 84.72 C
ANISOU 2748 CA LEU A 276 10985 10679 10525 191 62 -84 C
ATOM 2749 C LEU A 276 -19.163 -1.476 10.711 1.00 84.18 C
ANISOU 2749 C LEU A 276 10913 10612 10460 214 56 -105 C
ATOM 2750 O LEU A 276 -19.073 -2.705 10.702 1.00 82.89 O
ANISOU 2750 O LEU A 276 10769 10447 10279 210 86 -118 O
ATOM 2751 CB LEU A 276 -17.411 -0.221 9.425 1.00 82.96 C
ANISOU 2751 CB LEU A 276 10741 10434 10344 203 77 -76 C
ATOM 2752 CG LEU A 276 -16.397 -1.365 9.381 1.00 81.65 C
ANISOU 2752 CG LEU A 276 10586 10254 10184 207 125 -89 C
ATOM 2753 CD1 LEU A 276 -16.370 -2.045 8.017 1.00 78.13 C
ANISOU 2753 CD1 LEU A 276 10171 9816 9698 174 167 -89 C
ATOM 2754 CD2 LEU A 276 -15.016 -0.872 9.776 1.00 81.05 C
ANISOU 2754 CD2 LEU A 276 10481 10156 10160 229 131 -84 C
ATOM 2755 N ALA A 277 -19.512 -0.788 11.796 1.00 84.40 N
ANISOU 2755 N ALA A 277 10914 10643 10512 238 17 -109 N
ATOM 2756 CA ALA A 277 -19.908 -1.486 13.019 1.00 84.75 C
ANISOU 2756 CA ALA A 277 10954 10694 10554 256 8 -127 C
ATOM 2757 C ALA A 277 -21.235 -2.221 12.829 1.00 84.88 C
ANISOU 2757 C ALA A 277 10994 10734 10522 237 7 -133 C
ATOM 2758 O ALA A 277 -21.433 -3.297 13.394 1.00 82.59 O
ANISOU 2758 O ALA A 277 10714 10448 10217 239 18 -146 O
ATOM 2759 CB ALA A 277 -19.990 -0.523 14.189 1.00 86.03 C
ANISOU 2759 CB ALA A 277 11083 10857 10748 284 -32 -132 C
ATOM 2760 N HIS A 278 -22.133 -1.649 12.031 1.00 85.46 N
ANISOU 2760 N HIS A 278 11075 10822 10574 217 -9 -123 N
ATOM 2761 CA HIS A 278 -23.430 -2.270 11.787 1.00 84.30 C
ANISOU 2761 CA HIS A 278 10949 10698 10383 197 -13 -127 C
ATOM 2762 C HIS A 278 -23.339 -3.462 10.839 1.00 83.90 C
ANISOU 2762 C HIS A 278 10937 10645 10297 170 26 -127 C
ATOM 2763 O HIS A 278 -24.190 -4.352 10.888 1.00 84.40 O
ANISOU 2763 O HIS A 278 11019 10722 10326 158 29 -134 O
ATOM 2764 CB HIS A 278 -24.428 -1.247 11.248 1.00 85.13 C
ANISOU 2764 CB HIS A 278 11049 10817 10480 184 -46 -114 C
ATOM 2765 CG HIS A 278 -24.768 -0.155 12.215 1.00 85.90 C
ANISOU 2765 CG HIS A 278 11110 10920 10610 210 -87 -120 C
ATOM 2766 ND1 HIS A 278 -25.487 0.961 11.848 1.00 86.15 N
ANISOU 2766 ND1 HIS A 278 11128 10957 10649 204 -122 -110 N
ATOM 2767 CD2 HIS A 278 -24.489 -0.004 13.533 1.00 85.39 C
ANISOU 2767 CD2 HIS A 278 11019 10853 10572 240 -101 -136 C
ATOM 2768 CE1 HIS A 278 -25.643 1.748 12.895 1.00 85.57 C
ANISOU 2768 CE1 HIS A 278 11021 10885 10607 232 -154 -122 C
ATOM 2769 NE2 HIS A 278 -25.044 1.188 13.930 1.00 85.32 N
ANISOU 2769 NE2 HIS A 278 10982 10850 10585 254 -141 -138 N
ATOM 2770 N THR A 279 -22.320 -3.487 9.985 1.00 83.29 N
ANISOU 2770 N THR A 279 10868 10551 10226 161 57 -120 N
ATOM 2771 CA THR A 279 -22.181 -4.566 9.011 1.00 82.95 C
ANISOU 2771 CA THR A 279 10861 10506 10150 136 96 -124 C
ATOM 2772 C THR A 279 -21.972 -5.929 9.672 1.00 83.44 C
ANISOU 2772 C THR A 279 10934 10560 10210 146 117 -143 C
ATOM 2773 O THR A 279 -22.292 -6.957 9.075 1.00 82.42 O
ANISOU 2773 O THR A 279 10836 10433 10048 125 140 -150 O
ATOM 2774 CB THR A 279 -21.041 -4.261 8.033 1.00 82.16 C
ANISOU 2774 CB THR A 279 10765 10392 10062 126 127 -116 C
ATOM 2775 OG1 THR A 279 -21.089 -2.884 7.672 1.00 81.10 O
ANISOU 2775 OG1 THR A 279 10613 10261 9940 121 100 -95 O
ATOM 2776 CG2 THR A 279 -21.180 -5.082 6.764 1.00 81.01 C
ANISOU 2776 CG2 THR A 279 10658 10251 9872 91 162 -118 C
ATOM 2777 N ASN A 280 -21.476 -5.939 10.909 1.00 83.83 N
ANISOU 2777 N ASN A 280 10958 10599 10294 176 106 -150 N
ATOM 2778 CA ASN A 280 -21.271 -7.188 11.633 1.00 85.67 C
ANISOU 2778 CA ASN A 280 11199 10824 10529 185 120 -164 C
ATOM 2779 C ASN A 280 -22.563 -7.998 11.779 1.00 86.34 C
ANISOU 2779 C ASN A 280 11304 10929 10573 169 109 -169 C
ATOM 2780 O ASN A 280 -22.508 -9.221 11.916 1.00 87.81 O
ANISOU 2780 O ASN A 280 11508 11107 10749 165 125 -179 O
ATOM 2781 CB ASN A 280 -20.654 -6.916 13.003 1.00 87.33 C
ANISOU 2781 CB ASN A 280 11376 11023 10780 217 102 -168 C
ATOM 2782 CG ASN A 280 -20.413 -8.183 13.796 1.00 90.91 C
ANISOU 2782 CG ASN A 280 11836 11467 11239 225 111 -179 C
ATOM 2783 OD1 ASN A 280 -19.479 -8.933 13.522 1.00 91.73 O
ANISOU 2783 OD1 ASN A 280 11949 11547 11360 227 141 -185 O
ATOM 2784 ND2 ASN A 280 -21.265 -8.433 14.786 1.00 91.55 N
ANISOU 2784 ND2 ASN A 280 11913 11567 11307 229 84 -182 N
ATOM 2785 N SER A 281 -23.714 -7.330 11.737 1.00 85.30 N
ANISOU 2785 N SER A 281 11169 10823 10420 160 79 -162 N
ATOM 2786 CA SER A 281 -24.986 -8.039 11.836 1.00 86.92 C
ANISOU 2786 CA SER A 281 11391 11049 10586 143 68 -164 C
ATOM 2787 C SER A 281 -25.266 -8.886 10.593 1.00 90.76 C
ANISOU 2787 C SER A 281 11917 11533 11035 112 94 -164 C
ATOM 2788 O SER A 281 -25.909 -9.931 10.686 1.00 91.40 O
ANISOU 2788 O SER A 281 12018 11620 11088 99 96 -169 O
ATOM 2789 CB SER A 281 -26.122 -7.057 12.079 1.00 87.17 C
ANISOU 2789 CB SER A 281 11405 11106 10609 143 30 -157 C
ATOM 2790 OG SER A 281 -25.892 -6.313 13.262 1.00 85.65 O
ANISOU 2790 OG SER A 281 11177 10916 10450 172 6 -162 O
ATOM 2791 N VAL A 282 -24.763 -8.458 9.442 1.00 93.10 N
ANISOU 2791 N VAL A 282 12224 11821 11328 98 113 -158 N
ATOM 2792 CA VAL A 282 -25.011 -9.174 8.197 1.00 93.90 C
ANISOU 2792 CA VAL A 282 12364 11923 11391 66 139 -159 C
ATOM 2793 C VAL A 282 -23.993 -10.301 7.960 1.00 94.78 C
ANISOU 2793 C VAL A 282 12493 12011 11510 67 180 -175 C
ATOM 2794 O VAL A 282 -24.330 -11.325 7.359 1.00 95.00 O
ANISOU 2794 O VAL A 282 12553 12037 11506 46 198 -184 O
ATOM 2795 CB VAL A 282 -25.042 -8.194 7.011 1.00 91.65 C
ANISOU 2795 CB VAL A 282 12086 11645 11094 44 139 -143 C
ATOM 2796 CG1 VAL A 282 -25.442 -8.892 5.724 1.00 91.30 C
ANISOU 2796 CG1 VAL A 282 12082 11605 11002 7 161 -144 C
ATOM 2797 CG2 VAL A 282 -26.009 -7.059 7.296 1.00 90.52 C
ANISOU 2797 CG2 VAL A 282 11921 11520 10951 45 94 -128 C
ATOM 2798 N VAL A 283 -22.771 -10.129 8.449 1.00 94.76 N
ANISOU 2798 N VAL A 283 12468 11987 11550 93 194 -181 N
ATOM 2799 CA VAL A 283 -21.685 -11.039 8.100 1.00 94.33 C
ANISOU 2799 CA VAL A 283 12425 11907 11509 96 235 -197 C
ATOM 2800 C VAL A 283 -21.799 -12.416 8.753 1.00 97.95 C
ANISOU 2800 C VAL A 283 12895 12354 11968 101 239 -211 C
ATOM 2801 O VAL A 283 -21.158 -13.357 8.309 1.00 95.83 O
ANISOU 2801 O VAL A 283 12643 12064 11703 98 272 -227 O
ATOM 2802 CB VAL A 283 -20.308 -10.431 8.413 1.00 93.80 C
ANISOU 2802 CB VAL A 283 12328 11820 11491 121 247 -196 C
ATOM 2803 CG1 VAL A 283 -20.141 -9.107 7.689 1.00 95.59 C
ANISOU 2803 CG1 VAL A 283 12544 12057 11718 112 244 -180 C
ATOM 2804 CG2 VAL A 283 -20.119 -10.269 9.914 1.00 95.84 C
ANISOU 2804 CG2 VAL A 283 12555 12072 11787 152 219 -195 C
ATOM 2805 N ASN A 284 -22.594 -12.535 9.810 1.00100.61 N
ANISOU 2805 N ASN A 284 13221 12702 12302 109 205 -206 N
ATOM 2806 CA ASN A 284 -22.659 -13.799 10.536 1.00105.33 C
ANISOU 2806 CA ASN A 284 13827 13288 12904 114 203 -216 C
ATOM 2807 C ASN A 284 -23.333 -14.935 9.749 1.00107.86 C
ANISOU 2807 C ASN A 284 14188 13610 13186 86 217 -225 C
ATOM 2808 O ASN A 284 -22.749 -16.011 9.630 1.00104.81 O
ANISOU 2808 O ASN A 284 13815 13199 12811 87 240 -240 O
ATOM 2809 CB ASN A 284 -23.268 -13.608 11.923 1.00106.81 C
ANISOU 2809 CB ASN A 284 13992 13493 13099 128 164 -208 C
ATOM 2810 CG ASN A 284 -22.376 -12.803 12.849 1.00105.41 C
ANISOU 2810 CG ASN A 284 13778 13307 12967 158 154 -204 C
ATOM 2811 OD1 ASN A 284 -21.167 -12.678 12.620 1.00100.01 O
ANISOU 2811 OD1 ASN A 284 13086 12598 12317 171 177 -209 O
ATOM 2812 ND2 ASN A 284 -22.967 -12.250 13.907 1.00107.86 N
ANISOU 2812 ND2 ASN A 284 14066 13638 13279 169 119 -197 N
ATOM 2813 N PRO A 285 -24.545 -14.721 9.188 1.00110.42 N
ANISOU 2813 N PRO A 285 14530 13961 13465 61 202 -216 N
ATOM 2814 CA PRO A 285 -25.182 -15.832 8.457 1.00107.48 C
ANISOU 2814 CA PRO A 285 14195 13586 13054 33 213 -224 C
ATOM 2815 C PRO A 285 -24.412 -16.316 7.228 1.00106.02 C
ANISOU 2815 C PRO A 285 14037 13382 12864 20 257 -241 C
ATOM 2816 O PRO A 285 -24.583 -17.461 6.822 1.00101.12 O
ANISOU 2816 O PRO A 285 13445 12750 12226 6 270 -255 O
ATOM 2817 CB PRO A 285 -26.539 -15.259 8.050 1.00108.79 C
ANISOU 2817 CB PRO A 285 14371 13785 13179 10 188 -208 C
ATOM 2818 CG PRO A 285 -26.794 -14.183 9.039 1.00110.26 C
ANISOU 2818 CG PRO A 285 14519 13989 13385 30 156 -195 C
ATOM 2819 CD PRO A 285 -25.457 -13.572 9.298 1.00112.88 C
ANISOU 2819 CD PRO A 285 14826 14301 13761 57 171 -199 C
ATOM 2820 N PHE A 286 -23.567 -15.471 6.647 1.00107.91 N
ANISOU 2820 N PHE A 286 14265 13617 13118 25 278 -241 N
ATOM 2821 CA PHE A 286 -22.769 -15.904 5.506 1.00108.74 C
ANISOU 2821 CA PHE A 286 14392 13707 13218 13 322 -260 C
ATOM 2822 C PHE A 286 -21.652 -16.858 5.925 1.00108.83 C
ANISOU 2822 C PHE A 286 14397 13684 13271 36 348 -282 C
ATOM 2823 O PHE A 286 -21.217 -17.690 5.131 1.00110.08 O
ANISOU 2823 O PHE A 286 14577 13825 13421 25 383 -304 O
ATOM 2824 CB PHE A 286 -22.202 -14.705 4.750 1.00109.57 C
ANISOU 2824 CB PHE A 286 14486 13821 13324 9 337 -251 C
ATOM 2825 CG PHE A 286 -23.198 -14.019 3.866 1.00109.49 C
ANISOU 2825 CG PHE A 286 14495 13840 13267 -23 323 -234 C
ATOM 2826 CD1 PHE A 286 -24.172 -13.179 4.411 1.00110.30 C
ANISOU 2826 CD1 PHE A 286 14582 13964 13363 -22 278 -211 C
ATOM 2827 CD2 PHE A 286 -23.159 -14.200 2.483 1.00107.28 C
ANISOU 2827 CD2 PHE A 286 14247 13565 12949 -55 352 -241 C
ATOM 2828 CE1 PHE A 286 -25.093 -12.538 3.595 1.00110.48 C
ANISOU 2828 CE1 PHE A 286 14620 14009 13347 -52 262 -193 C
ATOM 2829 CE2 PHE A 286 -24.078 -13.561 1.661 1.00107.89 C
ANISOU 2829 CE2 PHE A 286 14342 13667 12983 -88 335 -222 C
ATOM 2830 CZ PHE A 286 -25.046 -12.729 2.218 1.00108.31 C
ANISOU 2830 CZ PHE A 286 14378 13739 13035 -86 289 -197 C
ATOM 2831 N ILE A 287 -21.184 -16.743 7.164 1.00105.37 N
ANISOU 2831 N ILE A 287 13926 13233 12876 66 330 -276 N
ATOM 2832 CA ILE A 287 -20.114 -17.612 7.639 1.00103.78 C
ANISOU 2832 CA ILE A 287 13714 12996 12720 87 349 -294 C
ATOM 2833 C ILE A 287 -20.632 -19.012 7.957 1.00103.72 C
ANISOU 2833 C ILE A 287 13729 12976 12705 80 340 -304 C
ATOM 2834 O ILE A 287 -19.976 -20.007 7.642 1.00103.28 O
ANISOU 2834 O ILE A 287 13684 12890 12668 83 367 -327 O
ATOM 2835 CB ILE A 287 -19.388 -16.981 8.838 1.00102.02 C
ANISOU 2835 CB ILE A 287 13450 12764 12547 119 330 -282 C
ATOM 2836 CG1 ILE A 287 -18.879 -15.586 8.471 1.00 99.19 C
ANISOU 2836 CG1 ILE A 287 13072 12419 12199 125 337 -271 C
ATOM 2837 CG2 ILE A 287 -18.238 -17.862 9.309 1.00102.36 C
ANISOU 2837 CG2 ILE A 287 13481 12768 12642 141 348 -298 C
ATOM 2838 CD1 ILE A 287 -17.960 -15.525 7.256 1.00 96.08 C
ANISOU 2838 CD1 ILE A 287 12685 12014 11807 117 384 -285 C
ATOM 2839 N TYR A 288 -21.808 -19.099 8.573 1.00103.48 N
ANISOU 2839 N TYR A 288 13703 12966 12648 71 302 -288 N
ATOM 2840 CA TYR A 288 -22.385 -20.404 8.889 1.00105.05 C
ANISOU 2840 CA TYR A 288 13922 13154 12837 60 289 -294 C
ATOM 2841 C TYR A 288 -22.664 -21.215 7.628 1.00108.21 C
ANISOU 2841 C TYR A 288 14363 13547 13204 34 316 -314 C
ATOM 2842 O TYR A 288 -22.437 -22.426 7.605 1.00110.34 O
ANISOU 2842 O TYR A 288 14648 13789 13486 33 324 -331 O
ATOM 2843 CB TYR A 288 -23.649 -20.249 9.728 1.00106.01 C
ANISOU 2843 CB TYR A 288 14040 13305 12933 52 245 -272 C
ATOM 2844 CG TYR A 288 -23.477 -19.376 10.944 1.00107.32 C
ANISOU 2844 CG TYR A 288 14168 13484 13127 75 219 -255 C
ATOM 2845 CD1 TYR A 288 -22.395 -19.555 11.816 1.00107.35 C
ANISOU 2845 CD1 TYR A 288 14146 13461 13181 102 219 -258 C
ATOM 2846 CD2 TYR A 288 -24.395 -18.367 11.226 1.00107.90 C
ANISOU 2846 CD2 TYR A 288 14229 13593 13175 71 192 -237 C
ATOM 2847 CE1 TYR A 288 -22.239 -18.755 12.935 1.00108.22 C
ANISOU 2847 CE1 TYR A 288 14222 13582 13313 122 194 -243 C
ATOM 2848 CE2 TYR A 288 -24.248 -17.557 12.342 1.00107.98 C
ANISOU 2848 CE2 TYR A 288 14203 13615 13209 93 168 -226 C
ATOM 2849 CZ TYR A 288 -23.169 -17.753 13.190 1.00109.05 C
ANISOU 2849 CZ TYR A 288 14318 13726 13392 117 170 -229 C
ATOM 2850 OH TYR A 288 -23.028 -16.951 14.294 1.00111.54 O
ANISOU 2850 OH TYR A 288 14600 14053 13728 137 145 -218 O
ATOM 2851 N ALA A 289 -23.125 -20.546 6.575 1.00109.62 N
ANISOU 2851 N ALA A 289 14559 13750 13342 12 327 -311 N
ATOM 2852 CA ALA A 289 -23.411 -21.233 5.316 1.00112.82 C
ANISOU 2852 CA ALA A 289 15005 14152 13709 -16 352 -330 C
ATOM 2853 C ALA A 289 -22.127 -21.703 4.628 1.00115.91 C
ANISOU 2853 C ALA A 289 15400 14513 14127 -7 400 -361 C
ATOM 2854 O ALA A 289 -22.069 -22.826 4.119 1.00113.99 O
ANISOU 2854 O ALA A 289 15184 14249 13877 -17 418 -386 O
ATOM 2855 CB ALA A 289 -24.226 -20.346 4.390 1.00112.46 C
ANISOU 2855 CB ALA A 289 14976 14140 13613 -44 348 -316 C
ATOM 2856 N TYR A 290 -21.099 -20.859 4.634 1.00118.08 N
ANISOU 2856 N TYR A 290 15647 14785 14433 12 420 -361 N
ATOM 2857 CA TYR A 290 -19.850 -21.191 3.958 1.00120.56 C
ANISOU 2857 CA TYR A 290 15961 15075 14772 20 468 -390 C
ATOM 2858 C TYR A 290 -18.976 -22.172 4.733 1.00122.58 C
ANISOU 2858 C TYR A 290 16199 15288 15086 48 474 -408 C
ATOM 2859 O TYR A 290 -18.098 -22.799 4.142 1.00126.49 O
ANISOU 2859 O TYR A 290 16700 15759 15603 53 514 -439 O
ATOM 2860 CB TYR A 290 -19.055 -19.926 3.641 1.00124.80 C
ANISOU 2860 CB TYR A 290 16472 15624 15321 28 488 -381 C
ATOM 2861 CG TYR A 290 -19.335 -19.349 2.283 1.00133.05 C
ANISOU 2861 CG TYR A 290 17541 16696 16315 -4 510 -382 C
ATOM 2862 CD1 TYR A 290 -18.753 -19.902 1.135 1.00138.71 C
ANISOU 2862 CD1 TYR A 290 18280 17405 17018 -19 559 -413 C
ATOM 2863 CD2 TYR A 290 -20.166 -18.238 2.135 1.00134.73 C
ANISOU 2863 CD2 TYR A 290 17754 16942 16494 -21 483 -351 C
ATOM 2864 CE1 TYR A 290 -19.004 -19.371 -0.120 1.00143.45 C
ANISOU 2864 CE1 TYR A 290 18904 18033 17567 -52 580 -412 C
ATOM 2865 CE2 TYR A 290 -20.419 -17.692 0.884 1.00140.73 C
ANISOU 2865 CE2 TYR A 290 18536 17726 17207 -54 500 -348 C
ATOM 2866 CZ TYR A 290 -19.839 -18.266 -0.237 1.00142.81 C
ANISOU 2866 CZ TYR A 290 18824 17984 17453 -71 548 -377 C
ATOM 2867 OH TYR A 290 -20.089 -17.739 -1.476 1.00149.97 O
ANISOU 2867 OH TYR A 290 19754 18918 18310 -107 564 -373 O
ATOM 2868 N ARG A 291 -19.204 -22.308 6.038 1.00116.21 N
ANISOU 2868 N ARG A 291 15373 14475 14306 66 434 -389 N
ATOM 2869 CA ARG A 291 -18.323 -23.119 6.878 1.00111.58 C
ANISOU 2869 CA ARG A 291 14766 13848 13780 92 433 -400 C
ATOM 2870 C ARG A 291 -18.995 -24.317 7.534 1.00109.98 C
ANISOU 2870 C ARG A 291 14579 13630 13579 87 402 -399 C
ATOM 2871 O ARG A 291 -18.340 -25.336 7.737 1.00111.95 O
ANISOU 2871 O ARG A 291 14826 13841 13869 99 410 -419 O
ATOM 2872 CB ARG A 291 -17.643 -22.257 7.938 1.00108.81 C
ANISOU 2872 CB ARG A 291 14373 13496 13474 121 416 -380 C
ATOM 2873 CG ARG A 291 -16.698 -21.211 7.370 1.00108.28 C
ANISOU 2873 CG ARG A 291 14285 13434 13421 130 449 -382 C
ATOM 2874 CD ARG A 291 -15.599 -20.860 8.357 1.00111.67 C
ANISOU 2874 CD ARG A 291 14673 13842 13914 163 442 -374 C
ATOM 2875 NE ARG A 291 -14.731 -22.002 8.642 1.00117.18 N
ANISOU 2875 NE ARG A 291 15363 14495 14663 180 455 -396 N
ATOM 2876 CZ ARG A 291 -13.568 -22.241 8.038 1.00123.59 C
ANISOU 2876 CZ ARG A 291 16165 15281 15511 192 499 -422 C
ATOM 2877 NH1 ARG A 291 -13.104 -21.412 7.109 1.00130.96 N
ANISOU 2877 NH1 ARG A 291 17096 16232 16433 187 534 -427 N
ATOM 2878 NH2 ARG A 291 -12.858 -23.311 8.371 1.00126.15 N
ANISOU 2878 NH2 ARG A 291 16481 15562 15887 208 505 -441 N
ATOM 2879 N ILE A 292 -20.276 -24.208 7.873 1.00107.48 N
ANISOU 2879 N ILE A 292 14275 13343 13220 69 366 -376 N
ATOM 2880 CA ILE A 292 -20.996 -25.313 8.506 1.00109.47 C
ANISOU 2880 CA ILE A 292 14541 13584 13469 60 333 -371 C
ATOM 2881 C ILE A 292 -21.873 -25.983 7.461 1.00114.18 C
ANISOU 2881 C ILE A 292 15181 14187 14016 28 342 -385 C
ATOM 2882 O ILE A 292 -22.678 -25.323 6.800 1.00110.50 O
ANISOU 2882 O ILE A 292 14731 13755 13499 7 342 -376 O
ATOM 2883 CB ILE A 292 -21.829 -24.836 9.710 1.00107.09 C
ANISOU 2883 CB ILE A 292 14222 13311 13157 60 286 -336 C
ATOM 2884 CG1 ILE A 292 -20.935 -24.096 10.709 1.00107.00 C
ANISOU 2884 CG1 ILE A 292 14168 13294 13192 90 278 -324 C
ATOM 2885 CG2 ILE A 292 -22.532 -26.013 10.368 1.00106.43 C
ANISOU 2885 CG2 ILE A 292 14151 13217 13069 48 252 -329 C
ATOM 2886 CD1 ILE A 292 -21.690 -23.212 11.679 1.00108.14 C
ANISOU 2886 CD1 ILE A 292 14293 13476 13320 91 240 -294 C
ATOM 2887 N ARG A 293 -21.709 -27.295 7.307 1.00122.59 N
ANISOU 2887 N ARG A 293 16265 15217 15097 25 347 -406 N
ATOM 2888 CA ARG A 293 -22.446 -28.028 6.288 1.00128.49 C
ANISOU 2888 CA ARG A 293 17055 15965 15800 -4 355 -424 C
ATOM 2889 C ARG A 293 -23.919 -28.195 6.672 1.00126.68 C
ANISOU 2889 C ARG A 293 16842 15764 15527 -29 312 -396 C
ATOM 2890 O ARG A 293 -24.801 -28.088 5.819 1.00127.31 O
ANISOU 2890 O ARG A 293 16952 15867 15553 -57 314 -395 O
ATOM 2891 CB ARG A 293 -21.784 -29.380 6.022 1.00139.06 C
ANISOU 2891 CB ARG A 293 18407 17255 17175 2 373 -458 C
ATOM 2892 CG ARG A 293 -22.507 -30.252 5.007 1.00145.73 C
ANISOU 2892 CG ARG A 293 19297 18095 17977 -28 380 -480 C
ATOM 2893 CD ARG A 293 -21.676 -31.449 4.587 1.00151.14 C
ANISOU 2893 CD ARG A 293 19994 18730 18703 -18 406 -522 C
ATOM 2894 NE ARG A 293 -20.616 -31.085 3.646 1.00155.57 N
ANISOU 2894 NE ARG A 293 20550 19284 19274 -8 462 -557 N
ATOM 2895 CZ ARG A 293 -19.795 -31.949 3.052 1.00157.85 C
ANISOU 2895 CZ ARG A 293 20846 19534 19594 1 497 -602 C
ATOM 2896 NH1 ARG A 293 -18.869 -31.502 2.215 1.00161.66 N
ANISOU 2896 NH1 ARG A 293 21323 20019 20083 9 549 -631 N
ATOM 2897 NH2 ARG A 293 -19.888 -33.255 3.284 1.00155.01 N
ANISOU 2897 NH2 ARG A 293 20500 19134 19262 2 479 -618 N
ATOM 2898 N GLU A 294 -24.185 -28.460 7.947 1.00122.40 N
ANISOU 2898 N GLU A 294 16280 15219 15006 -21 272 -372 N
ATOM 2899 CA GLU A 294 -25.557 -28.673 8.399 1.00118.74 C
ANISOU 2899 CA GLU A 294 15829 14783 14504 -44 231 -345 C
ATOM 2900 C GLU A 294 -26.406 -27.409 8.238 1.00115.04 C
ANISOU 2900 C GLU A 294 15356 14365 13991 -55 222 -323 C
ATOM 2901 O GLU A 294 -27.576 -27.488 7.863 1.00111.02 O
ANISOU 2901 O GLU A 294 14868 13880 13433 -83 206 -312 O
ATOM 2902 CB GLU A 294 -25.585 -29.167 9.839 1.00119.63 C
ANISOU 2902 CB GLU A 294 15919 14887 14649 -34 192 -323 C
ATOM 2903 CG GLU A 294 -26.934 -29.721 10.277 1.00122.01 C
ANISOU 2903 CG GLU A 294 16234 15209 14914 -61 151 -299 C
ATOM 2904 CD GLU A 294 -27.227 -31.100 9.712 1.00123.18 C
ANISOU 2904 CD GLU A 294 16419 15328 15057 -81 148 -315 C
ATOM 2905 OE1 GLU A 294 -26.344 -31.981 9.776 1.00126.51 O
ANISOU 2905 OE1 GLU A 294 16841 15702 15525 -68 156 -335 O
ATOM 2906 OE2 GLU A 294 -28.347 -31.307 9.205 1.00122.02 O
ANISOU 2906 OE2 GLU A 294 16299 15201 14862 -110 135 -308 O
ATOM 2907 N PHE A 295 -25.815 -26.249 8.512 1.00114.98 N
ANISOU 2907 N PHE A 295 15317 14370 13999 -34 232 -316 N
ATOM 2908 CA PHE A 295 -26.514 -24.986 8.297 1.00113.89 C
ANISOU 2908 CA PHE A 295 15172 14276 13826 -43 224 -298 C
ATOM 2909 C PHE A 295 -26.776 -24.732 6.814 1.00113.69 C
ANISOU 2909 C PHE A 295 15178 14260 13760 -66 251 -311 C
ATOM 2910 O PHE A 295 -27.865 -24.281 6.442 1.00111.19 O
ANISOU 2910 O PHE A 295 14873 13974 13398 -88 235 -295 O
ATOM 2911 CB PHE A 295 -25.733 -23.821 8.903 1.00110.02 C
ANISOU 2911 CB PHE A 295 14642 13792 13367 -14 228 -290 C
ATOM 2912 CG PHE A 295 -26.097 -23.516 10.319 1.00107.64 C
ANISOU 2912 CG PHE A 295 14311 13509 13080 -2 190 -266 C
ATOM 2913 CD1 PHE A 295 -27.281 -22.844 10.620 1.00106.63 C
ANISOU 2913 CD1 PHE A 295 14176 13422 12915 -14 162 -244 C
ATOM 2914 CD2 PHE A 295 -25.246 -23.875 11.358 1.00107.02 C
ANISOU 2914 CD2 PHE A 295 14208 13405 13048 21 183 -266 C
ATOM 2915 CE1 PHE A 295 -27.617 -22.553 11.932 1.00106.99 C
ANISOU 2915 CE1 PHE A 295 14193 13487 12971 -4 129 -226 C
ATOM 2916 CE2 PHE A 295 -25.570 -23.582 12.675 1.00106.67 C
ANISOU 2916 CE2 PHE A 295 14137 13381 13013 30 148 -244 C
ATOM 2917 CZ PHE A 295 -26.760 -22.921 12.965 1.00106.43 C
ANISOU 2917 CZ PHE A 295 14100 13394 12943 17 123 -226 C
ATOM 2918 N ARG A 296 -25.788 -25.026 5.972 1.00116.20 N
ANISOU 2918 N ARG A 296 15508 14551 14092 -61 292 -339 N
ATOM 2919 CA ARG A 296 -25.909 -24.759 4.540 1.00118.42 C
ANISOU 2919 CA ARG A 296 15818 14842 14333 -85 321 -353 C
ATOM 2920 C ARG A 296 -27.039 -25.575 3.912 1.00119.86 C
ANISOU 2920 C ARG A 296 16043 15031 14468 -119 308 -355 C
ATOM 2921 O ARG A 296 -27.813 -25.050 3.110 1.00118.44 O
ANISOU 2921 O ARG A 296 15882 14878 14241 -145 305 -345 O
ATOM 2922 CB ARG A 296 -24.583 -25.029 3.835 1.00120.50 C
ANISOU 2922 CB ARG A 296 16084 15076 14623 -73 370 -387 C
ATOM 2923 CG ARG A 296 -24.629 -24.901 2.321 1.00123.48 C
ANISOU 2923 CG ARG A 296 16495 15464 14957 -100 404 -405 C
ATOM 2924 CD ARG A 296 -23.251 -25.042 1.691 1.00129.09 C
ANISOU 2924 CD ARG A 296 17202 16151 15696 -86 455 -440 C
ATOM 2925 NE ARG A 296 -22.650 -26.358 1.914 1.00129.55 N
ANISOU 2925 NE ARG A 296 17265 16167 15793 -72 467 -470 N
ATOM 2926 CZ ARG A 296 -21.701 -26.606 2.814 1.00130.96 C
ANISOU 2926 CZ ARG A 296 17411 16315 16033 -38 468 -475 C
ATOM 2927 NH1 ARG A 296 -21.220 -27.835 2.951 1.00131.69 N
ANISOU 2927 NH1 ARG A 296 17509 16366 16161 -27 477 -503 N
ATOM 2928 NH2 ARG A 296 -21.233 -25.627 3.577 1.00130.66 N
ANISOU 2928 NH2 ARG A 296 17334 16286 16024 -15 459 -453 N
ATOM 2929 N GLN A 297 -27.142 -26.843 4.293 1.00120.99 N
ANISOU 2929 N GLN A 297 16198 15147 14625 -120 297 -365 N
ATOM 2930 CA GLN A 297 -28.197 -27.702 3.756 1.00123.19 C
ANISOU 2930 CA GLN A 297 16516 15428 14862 -152 282 -366 C
ATOM 2931 C GLN A 297 -29.573 -27.267 4.253 1.00117.04 C
ANISOU 2931 C GLN A 297 15734 14687 14050 -169 238 -329 C
ATOM 2932 O GLN A 297 -30.548 -27.345 3.503 1.00114.41 O
ANISOU 2932 O GLN A 297 15430 14372 13670 -201 229 -324 O
ATOM 2933 CB GLN A 297 -27.937 -29.163 4.102 1.00130.07 C
ANISOU 2933 CB GLN A 297 17400 16259 15763 -148 276 -384 C
ATOM 2934 CG GLN A 297 -26.665 -29.730 3.492 1.00136.66 C
ANISOU 2934 CG GLN A 297 18241 17054 16631 -133 320 -426 C
ATOM 2935 CD GLN A 297 -26.176 -30.989 4.192 1.00140.80 C
ANISOU 2935 CD GLN A 297 18760 17532 17204 -117 309 -440 C
ATOM 2936 OE1 GLN A 297 -26.499 -31.244 5.356 1.00142.13 O
ANISOU 2936 OE1 GLN A 297 18909 17699 17393 -110 271 -414 O
ATOM 2937 NE2 GLN A 297 -25.383 -31.782 3.482 1.00143.83 N
ANISOU 2937 NE2 GLN A 297 19161 17880 17609 -112 343 -481 N
ATOM 2938 N THR A 298 -29.653 -26.801 5.496 1.00113.44 N
ANISOU 2938 N THR A 298 15240 14243 13618 -150 212 -306 N
ATOM 2939 CA THR A 298 -30.933 -26.372 6.049 1.00112.95 C
ANISOU 2939 CA THR A 298 15169 14219 13527 -163 172 -274 C
ATOM 2940 C THR A 298 -31.432 -25.081 5.400 1.00118.35 C
ANISOU 2940 C THR A 298 15851 14938 14180 -174 174 -261 C
ATOM 2941 O THR A 298 -32.637 -24.907 5.221 1.00119.79 O
ANISOU 2941 O THR A 298 16042 15147 14324 -198 149 -242 O
ATOM 2942 CB THR A 298 -30.841 -26.195 7.564 1.00110.57 C
ANISOU 2942 CB THR A 298 14828 13924 13259 -140 146 -255 C
ATOM 2943 OG1 THR A 298 -30.145 -27.309 8.125 1.00111.91 O
ANISOU 2943 OG1 THR A 298 14997 14057 13466 -128 146 -267 O
ATOM 2944 CG2 THR A 298 -32.227 -26.121 8.172 1.00106.19 C
ANISOU 2944 CG2 THR A 298 14267 13405 12675 -158 105 -227 C
ATOM 2945 N PHE A 299 -30.512 -24.191 5.040 1.00120.69 N
ANISOU 2945 N PHE A 299 16132 15232 14492 -158 201 -270 N
ATOM 2946 CA PHE A 299 -30.903 -22.949 4.372 1.00120.89 C
ANISOU 2946 CA PHE A 299 16155 15286 14490 -169 201 -257 C
ATOM 2947 C PHE A 299 -31.538 -23.221 3.014 1.00123.95 C
ANISOU 2947 C PHE A 299 16587 15681 14829 -207 210 -261 C
ATOM 2948 O PHE A 299 -32.485 -22.535 2.625 1.00127.12 O
ANISOU 2948 O PHE A 299 16993 16110 15198 -228 190 -241 O
ATOM 2949 CB PHE A 299 -29.708 -22.004 4.224 1.00120.15 C
ANISOU 2949 CB PHE A 299 16039 15187 14427 -146 229 -265 C
ATOM 2950 CG PHE A 299 -29.175 -21.478 5.524 1.00120.24 C
ANISOU 2950 CG PHE A 299 16006 15197 14483 -111 216 -256 C
ATOM 2951 CD1 PHE A 299 -29.952 -21.502 6.682 1.00124.01 C
ANISOU 2951 CD1 PHE A 299 16462 15691 14964 -105 179 -237 C
ATOM 2952 CD2 PHE A 299 -27.897 -20.936 5.588 1.00116.99 C
ANISOU 2952 CD2 PHE A 299 15572 14770 14108 -85 242 -266 C
ATOM 2953 CE1 PHE A 299 -29.462 -21.009 7.878 1.00124.71 C
ANISOU 2953 CE1 PHE A 299 16513 15782 15091 -74 167 -230 C
ATOM 2954 CE2 PHE A 299 -27.399 -20.443 6.785 1.00117.18 C
ANISOU 2954 CE2 PHE A 299 15556 14793 14173 -54 229 -257 C
ATOM 2955 CZ PHE A 299 -28.180 -20.477 7.932 1.00120.70 C
ANISOU 2955 CZ PHE A 299 15985 15256 14621 -49 191 -240 C
ATOM 2956 N ARG A 300 -31.033 -24.228 2.307 1.00126.84 N
ANISOU 2956 N ARG A 300 16984 16018 15190 -217 237 -289 N
ATOM 2957 CA ARG A 300 -31.542 -24.534 0.968 1.00129.24 C
ANISOU 2957 CA ARG A 300 17333 16327 15445 -254 249 -298 C
ATOM 2958 C ARG A 300 -33.018 -24.925 1.004 1.00128.81 C
ANISOU 2958 C ARG A 300 17297 16291 15354 -282 209 -277 C
ATOM 2959 O ARG A 300 -33.809 -24.459 0.184 1.00130.28 O
ANISOU 2959 O ARG A 300 17503 16499 15499 -312 200 -263 O
ATOM 2960 CB ARG A 300 -30.719 -25.637 0.310 1.00132.46 C
ANISOU 2960 CB ARG A 300 17770 16701 15858 -256 286 -337 C
ATOM 2961 CG ARG A 300 -29.286 -25.251 -0.013 1.00134.42 C
ANISOU 2961 CG ARG A 300 18005 16934 16136 -234 330 -361 C
ATOM 2962 CD ARG A 300 -28.585 -26.351 -0.794 1.00135.01 C
ANISOU 2962 CD ARG A 300 18110 16978 16212 -240 369 -403 C
ATOM 2963 NE ARG A 300 -27.194 -26.010 -1.084 1.00138.26 N
ANISOU 2963 NE ARG A 300 18504 17376 16653 -219 414 -427 N
ATOM 2964 CZ ARG A 300 -26.786 -25.257 -2.104 1.00140.92 C
ANISOU 2964 CZ ARG A 300 18849 17729 16965 -233 445 -434 C
ATOM 2965 NH1 ARG A 300 -27.657 -24.736 -2.964 1.00143.52 N
ANISOU 2965 NH1 ARG A 300 19205 18090 17239 -270 435 -417 N
ATOM 2966 NH2 ARG A 300 -25.493 -25.017 -2.261 1.00144.45 N
ANISOU 2966 NH2 ARG A 300 19277 18164 17444 -212 486 -455 N
ATOM 2967 N LYS A 301 -33.391 -25.755 1.971 1.00125.60 N
ANISOU 2967 N LYS A 301 16883 15875 14965 -275 185 -271 N
ATOM 2968 CA LYS A 301 -34.757 -26.264 2.034 1.00121.46 C
ANISOU 2968 CA LYS A 301 16377 15366 14408 -302 148 -251 C
ATOM 2969 C LYS A 301 -35.754 -25.210 2.507 1.00116.17 C
ANISOU 2969 C LYS A 301 15679 14735 13725 -306 115 -217 C
ATOM 2970 O LYS A 301 -36.947 -25.333 2.234 1.00116.71 O
ANISOU 2970 O LYS A 301 15763 14822 13760 -334 88 -199 O
ATOM 2971 CB LYS A 301 -34.826 -27.521 2.895 1.00120.76 C
ANISOU 2971 CB LYS A 301 16289 15255 14340 -296 132 -255 C
ATOM 2972 CG LYS A 301 -34.054 -28.686 2.296 1.00127.38 C
ANISOU 2972 CG LYS A 301 17159 16052 15188 -298 159 -290 C
ATOM 2973 CD LYS A 301 -34.185 -29.961 3.119 1.00131.28 C
ANISOU 2973 CD LYS A 301 17655 16521 15705 -295 137 -290 C
ATOM 2974 CE LYS A 301 -33.429 -31.113 2.471 1.00134.85 C
ANISOU 2974 CE LYS A 301 18138 16929 16170 -296 163 -329 C
ATOM 2975 NZ LYS A 301 -33.553 -32.380 3.245 1.00136.18 N
ANISOU 2975 NZ LYS A 301 18309 17069 16365 -294 137 -328 N
ATOM 2976 N ILE A 302 -35.282 -24.187 3.212 1.00112.44 N
ANISOU 2976 N ILE A 302 15166 14274 13282 -277 115 -209 N
ATOM 2977 CA ILE A 302 -36.158 -23.076 3.567 1.00116.94 C
ANISOU 2977 CA ILE A 302 15708 14880 13844 -278 86 -181 C
ATOM 2978 C ILE A 302 -36.346 -22.144 2.367 1.00120.87 C
ANISOU 2978 C ILE A 302 16221 15391 14314 -299 93 -176 C
ATOM 2979 O ILE A 302 -37.437 -21.601 2.162 1.00121.17 O
ANISOU 2979 O ILE A 302 16257 15455 14328 -318 65 -153 O
ATOM 2980 CB ILE A 302 -35.632 -22.319 4.795 1.00117.45 C
ANISOU 2980 CB ILE A 302 15724 14952 13950 -240 81 -176 C
ATOM 2981 CG1 ILE A 302 -35.334 -23.298 5.934 1.00115.14 C
ANISOU 2981 CG1 ILE A 302 15419 14644 13684 -223 74 -181 C
ATOM 2982 CG2 ILE A 302 -36.655 -21.294 5.264 1.00118.47 C
ANISOU 2982 CG2 ILE A 302 15823 15117 14071 -241 48 -151 C
ATOM 2983 CD1 ILE A 302 -34.493 -22.724 7.057 1.00116.81 C
ANISOU 2983 CD1 ILE A 302 15589 14854 13939 -186 77 -182 C
ATOM 2984 N ILE A 303 -35.293 -21.972 1.572 1.00125.51 N
ANISOU 2984 N ILE A 303 16822 15962 14905 -296 130 -195 N
ATOM 2985 CA ILE A 303 -35.367 -21.116 0.390 1.00129.97 C
ANISOU 2985 CA ILE A 303 17403 16539 15442 -319 138 -189 C
ATOM 2986 C ILE A 303 -36.229 -21.768 -0.698 1.00134.89 C
ANISOU 2986 C ILE A 303 18073 17165 16014 -363 132 -187 C
ATOM 2987 O ILE A 303 -37.022 -21.086 -1.361 1.00138.84 O
ANISOU 2987 O ILE A 303 18582 17687 16485 -390 113 -166 O
ATOM 2988 CB ILE A 303 -33.955 -20.772 -0.121 1.00127.34 C
ANISOU 2988 CB ILE A 303 17068 16189 15125 -305 181 -210 C
ATOM 2989 CG1 ILE A 303 -33.233 -19.880 0.899 1.00122.19 C
ANISOU 2989 CG1 ILE A 303 16367 15538 14522 -265 180 -205 C
ATOM 2990 CG2 ILE A 303 -34.014 -20.064 -1.467 1.00129.43 C
ANISOU 2990 CG2 ILE A 303 17356 16467 15354 -337 192 -204 C
ATOM 2991 CD1 ILE A 303 -31.735 -19.750 0.698 1.00114.18 C
ANISOU 2991 CD1 ILE A 303 15345 14503 13535 -244 222 -227 C
ATOM 2992 N ARG A 304 -36.093 -23.082 -0.860 1.00135.00 N
ANISOU 2992 N ARG A 304 18117 17157 16020 -371 145 -209 N
ATOM 2993 CA ARG A 304 -36.823 -23.799 -1.906 1.00133.82 C
ANISOU 2993 CA ARG A 304 18016 17007 15823 -413 141 -212 C
ATOM 2994 C ARG A 304 -38.331 -23.797 -1.661 1.00132.38 C
ANISOU 2994 C ARG A 304 17834 16846 15618 -435 94 -181 C
ATOM 2995 O ARG A 304 -39.112 -23.489 -2.558 1.00136.01 O
ANISOU 2995 O ARG A 304 18317 17322 16039 -470 80 -166 O
ATOM 2996 CB ARG A 304 -36.294 -25.224 -2.048 1.00135.33 C
ANISOU 2996 CB ARG A 304 18238 17166 16017 -413 164 -245 C
ATOM 2997 CG ARG A 304 -34.959 -25.322 -2.772 1.00141.12 C
ANISOU 2997 CG ARG A 304 18984 17878 16757 -405 215 -280 C
ATOM 2998 CD ARG A 304 -34.301 -26.669 -2.536 1.00148.89 C
ANISOU 2998 CD ARG A 304 19982 18825 17764 -391 235 -314 C
ATOM 2999 NE ARG A 304 -33.002 -26.760 -3.199 1.00155.35 N
ANISOU 2999 NE ARG A 304 20808 19624 18593 -382 285 -351 N
ATOM 3000 CZ ARG A 304 -32.144 -27.767 -3.057 1.00159.66 C
ANISOU 3000 CZ ARG A 304 21359 20134 19168 -363 311 -386 C
ATOM 3001 NH1 ARG A 304 -30.991 -27.741 -3.710 1.00160.84 N
ANISOU 3001 NH1 ARG A 304 21513 20271 19327 -355 359 -419 N
ATOM 3002 NH2 ARG A 304 -32.423 -28.800 -2.267 1.00164.36 N
ANISOU 3002 NH2 ARG A 304 21954 20707 19786 -354 288 -388 N
ATOM 3003 N SER A 305 -38.733 -24.118 -0.435 1.00127.12 N
ANISOU 3003 N SER A 305 17140 16184 14976 -416 70 -170 N
ATOM 3004 CA SER A 305 -40.148 -24.132 -0.076 1.00124.94 C
ANISOU 3004 CA SER A 305 16857 15931 14683 -434 27 -141 C
ATOM 3005 C SER A 305 -40.643 -22.727 0.249 1.00125.60 C
ANISOU 3005 C SER A 305 16902 16045 14776 -425 5 -115 C
ATOM 3006 O SER A 305 -40.236 -22.118 1.241 1.00127.02 O
ANISOU 3006 O SER A 305 17040 16232 14992 -391 4 -114 O
ATOM 3007 CB SER A 305 -40.398 -25.081 1.090 1.00123.88 C
ANISOU 3007 CB SER A 305 16710 15791 14569 -420 10 -140 C
ATOM 3008 OG SER A 305 -40.038 -26.405 0.748 1.00125.41 O
ANISOU 3008 OG SER A 305 16939 15953 14756 -430 25 -162 O
TER 3009 SER A 305
HETATM 3010 C10 9Y2 A1201 -22.397 8.369 16.690 1.00 96.00 C
ANISOU 3010 C10 9Y2 A1201 12154 12110 12211 387 -328 -148 C
HETATM 3011 C13 9Y2 A1201 -22.647 6.174 17.643 1.00 92.29 C
ANISOU 3011 C13 9Y2 A1201 11713 11673 11681 386 -275 -173 C
HETATM 3012 C15 9Y2 A1201 -24.532 7.243 16.607 1.00 98.69 C
ANISOU 3012 C15 9Y2 A1201 12516 12500 12482 367 -319 -167 C
HETATM 3013 C17 9Y2 A1201 -22.041 4.931 18.371 1.00 91.48 C
ANISOU 3013 C17 9Y2 A1201 11624 11575 11561 391 -242 -182 C
HETATM 3014 C20 9Y2 A1201 -20.029 3.858 19.550 1.00 92.87 C
ANISOU 3014 C20 9Y2 A1201 11801 11724 11761 411 -208 -185 C
HETATM 3015 C22 9Y2 A1201 -18.352 2.461 20.580 1.00 96.24 C
ANISOU 3015 C22 9Y2 A1201 12234 12129 12203 424 -174 -185 C
HETATM 3016 C01 9Y2 A1201 -23.570 11.566 13.252 1.00 94.57 C
ANISOU 3016 C01 9Y2 A1201 11958 11892 12080 326 -426 -67 C
HETATM 3017 C02 9Y2 A1201 -23.870 12.635 14.355 1.00 95.75 C
ANISOU 3017 C02 9Y2 A1201 12070 12033 12279 363 -475 -93 C
HETATM 3018 C03 9Y2 A1201 -22.525 13.055 15.043 1.00 98.33 C
ANISOU 3018 C03 9Y2 A1201 12379 12336 12645 387 -476 -95 C
HETATM 3019 C04 9Y2 A1201 -24.526 13.897 13.668 1.00 96.30 C
ANISOU 3019 C04 9Y2 A1201 12121 12088 12381 353 -528 -76 C
HETATM 3020 C05 9Y2 A1201 -24.872 12.056 15.395 1.00 97.50 C
ANISOU 3020 C05 9Y2 A1201 12285 12283 12479 382 -471 -133 C
HETATM 3021 C06 9Y2 A1201 -24.250 10.883 16.179 1.00 98.56 C
ANISOU 3021 C06 9Y2 A1201 12433 12429 12586 392 -427 -149 C
HETATM 3022 C09 9Y2 A1201 -23.739 8.354 16.322 1.00 98.06 C
ANISOU 3022 C09 9Y2 A1201 12420 12393 12447 374 -341 -152 C
HETATM 3023 C12 9Y2 A1201 -21.847 7.270 17.355 1.00 93.57 C
ANISOU 3023 C12 9Y2 A1201 11858 11808 11886 394 -295 -159 C
HETATM 3024 C14 9Y2 A1201 -23.982 6.152 17.266 1.00 94.79 C
ANISOU 3024 C14 9Y2 A1201 12035 12012 11970 372 -286 -177 C
HETATM 3025 C23 9Y2 A1201 -19.557 1.691 20.617 1.00 96.25 C
ANISOU 3025 C23 9Y2 A1201 12251 12160 12158 409 -168 -195 C
HETATM 3026 F11 9Y2 A1201 -21.612 9.453 16.416 1.00 96.61 F
ANISOU 3026 F11 9Y2 A1201 12215 12161 12333 393 -351 -132 F
HETATM 3027 F16 9Y2 A1201 -25.828 7.220 16.247 1.00107.15 F
ANISOU 3027 F16 9Y2 A1201 13590 13591 13530 353 -331 -170 F
HETATM 3028 N08 9Y2 A1201 -24.326 9.500 15.618 1.00 97.85 N
ANISOU 3028 N08 9Y2 A1201 12379 12357 12442 366 -380 -139 N
HETATM 3029 N19 9Y2 A1201 -20.689 4.978 18.880 1.00 90.37 N
ANISOU 3029 N19 9Y2 A1201 11474 11409 11453 407 -235 -179 N
HETATM 3030 N21 9Y2 A1201 -18.668 3.830 19.909 1.00 94.02 N
ANISOU 3030 N21 9Y2 A1201 11939 11844 11940 424 -199 -178 N
HETATM 3031 O07 9Y2 A1201 -23.707 11.078 17.211 1.00 96.61 O
ANISOU 3031 O07 9Y2 A1201 12169 12177 12362 419 -433 -169 O
HETATM 3032 O18 9Y2 A1201 -22.707 3.933 18.462 1.00 94.23 O
ANISOU 3032 O18 9Y2 A1201 11989 11943 11870 379 -224 -190 O
HETATM 3033 S24 9Y2 A1201 -20.641 2.513 19.976 1.00 95.91 S
ANISOU 3033 S24 9Y2 A1201 12205 12132 12103 402 -187 -196 S
HETATM 3034 C1 CLR A1202 -38.805 10.670 22.349 1.00124.65 C
ANISOU 3034 C1 CLR A1202 15502 16081 15777 478 -551 -478 C
HETATM 3035 C2 CLR A1202 -38.391 12.122 22.571 1.00122.53 C
ANISOU 3035 C2 CLR A1202 15202 15780 15575 510 -590 -499 C
HETATM 3036 C3 CLR A1202 -38.552 12.615 23.996 1.00122.12 C
ANISOU 3036 C3 CLR A1202 15110 15751 15537 544 -596 -556 C
HETATM 3037 C4 CLR A1202 -37.931 11.667 25.036 1.00122.74 C
ANISOU 3037 C4 CLR A1202 15206 15861 15568 544 -558 -569 C
HETATM 3038 C5 CLR A1202 -38.216 10.150 24.645 1.00124.20 C
ANISOU 3038 C5 CLR A1202 15429 16073 15687 507 -519 -537 C
HETATM 3039 C6 CLR A1202 -38.391 9.294 25.611 1.00124.86 C
ANISOU 3039 C6 CLR A1202 15515 16199 15726 504 -491 -556 C
HETATM 3040 C7 CLR A1202 -39.055 7.952 25.292 1.00124.79 C
ANISOU 3040 C7 CLR A1202 15532 16222 15660 471 -462 -533 C
HETATM 3041 C8 CLR A1202 -38.223 7.386 24.229 1.00123.43 C
ANISOU 3041 C8 CLR A1202 15405 16015 15477 448 -449 -484 C
HETATM 3042 C9 CLR A1202 -38.690 8.188 23.099 1.00123.94 C
ANISOU 3042 C9 CLR A1202 15462 16051 15577 444 -478 -468 C
HETATM 3043 C10 CLR A1202 -38.103 9.656 23.252 1.00124.65 C
ANISOU 3043 C10 CLR A1202 15524 16106 15732 476 -513 -486 C
HETATM 3044 C11 CLR A1202 -38.165 7.501 21.922 1.00121.37 C
ANISOU 3044 C11 CLR A1202 15183 15702 15232 415 -462 -420 C
HETATM 3045 C12 CLR A1202 -39.058 6.353 21.527 1.00120.19 C
ANISOU 3045 C12 CLR A1202 15054 15580 15032 384 -441 -403 C
HETATM 3046 C13 CLR A1202 -38.673 5.503 22.621 1.00121.14 C
ANISOU 3046 C13 CLR A1202 15181 15729 15118 387 -413 -419 C
HETATM 3047 C14 CLR A1202 -39.017 6.232 23.900 1.00122.10 C
ANISOU 3047 C14 CLR A1202 15257 15876 15259 418 -427 -467 C
HETATM 3048 C15 CLR A1202 -38.830 5.109 24.817 1.00120.49 C
ANISOU 3048 C15 CLR A1202 15067 15706 15008 408 -397 -473 C
HETATM 3049 C16 CLR A1202 -39.556 4.012 24.038 1.00120.67 C
ANISOU 3049 C16 CLR A1202 15118 15742 14989 373 -380 -442 C
HETATM 3050 C17 CLR A1202 -39.610 4.385 22.555 1.00120.07 C
ANISOU 3050 C17 CLR A1202 15059 15628 14933 360 -394 -410 C
HETATM 3051 C18 CLR A1202 -37.202 5.037 22.490 1.00119.67 C
ANISOU 3051 C18 CLR A1202 15029 15513 14927 383 -393 -397 C
HETATM 3052 C19 CLR A1202 -36.584 9.548 23.079 1.00127.64 C
ANISOU 3052 C19 CLR A1202 15931 16450 16115 476 -501 -462 C
HETATM 3053 C20 CLR A1202 -39.178 3.351 21.472 1.00115.98 C
ANISOU 3053 C20 CLR A1202 14592 15091 14384 328 -373 -367 C
HETATM 3054 C21 CLR A1202 -39.873 3.435 20.111 1.00117.39 C
ANISOU 3054 C21 CLR A1202 14784 15254 14563 304 -385 -339 C
HETATM 3055 C22 CLR A1202 -39.336 1.957 22.045 1.00114.21 C
ANISOU 3055 C22 CLR A1202 14388 14899 14108 309 -343 -365 C
HETATM 3056 C23 CLR A1202 -40.737 1.355 21.788 1.00114.23 C
ANISOU 3056 C23 CLR A1202 14389 14935 14079 286 -343 -359 C
HETATM 3057 C24 CLR A1202 -40.794 -0.177 21.632 1.00112.93 C
ANISOU 3057 C24 CLR A1202 14263 14784 13862 254 -316 -336 C
HETATM 3058 C25 CLR A1202 -40.357 -0.712 20.267 1.00109.39 C
ANISOU 3058 C25 CLR A1202 13860 14300 13403 229 -306 -299 C
HETATM 3059 C26 CLR A1202 -39.798 -2.127 20.410 1.00108.15 C
ANISOU 3059 C26 CLR A1202 13741 14145 13208 210 -276 -284 C
HETATM 3060 C27 CLR A1202 -41.510 -0.770 19.274 1.00110.90 C
ANISOU 3060 C27 CLR A1202 14057 14497 13584 205 -318 -282 C
HETATM 3061 O1 CLR A1202 -38.006 13.952 23.972 1.00119.21 O
ANISOU 3061 O1 CLR A1202 14719 15342 15234 570 -635 -567 O
HETATM 3062 C1 CLR A1203 -2.727 8.128 22.357 1.00118.24 C
ANISOU 3062 C1 CLR A1203 14788 14556 15583 559 -232 -3 C
HETATM 3063 C2 CLR A1203 -2.599 9.681 22.356 1.00115.69 C
ANISOU 3063 C2 CLR A1203 14444 14221 15290 565 -277 9 C
HETATM 3064 C3 CLR A1203 -1.770 10.172 21.192 1.00115.12 C
ANISOU 3064 C3 CLR A1203 14360 14136 15245 551 -258 40 C
HETATM 3065 C4 CLR A1203 -2.250 9.576 19.869 1.00116.10 C
ANISOU 3065 C4 CLR A1203 14505 14281 15326 526 -211 44 C
HETATM 3066 C5 CLR A1203 -2.618 8.032 19.994 1.00119.90 C
ANISOU 3066 C5 CLR A1203 15010 14777 15770 523 -170 23 C
HETATM 3067 C6 CLR A1203 -2.375 7.281 18.960 1.00119.34 C
ANISOU 3067 C6 CLR A1203 14950 14712 15682 505 -120 29 C
HETATM 3068 C7 CLR A1203 -2.378 5.756 19.109 1.00121.67 C
ANISOU 3068 C7 CLR A1203 15262 15010 15956 505 -79 12 C
HETATM 3069 C8 CLR A1203 -3.654 5.465 19.737 1.00123.83 C
ANISOU 3069 C8 CLR A1203 15556 15306 16189 509 -100 -12 C
HETATM 3070 C9 CLR A1203 -3.340 5.864 21.106 1.00123.10 C
ANISOU 3070 C9 CLR A1203 15446 15199 16129 531 -142 -16 C
HETATM 3071 C10 CLR A1203 -3.365 7.456 21.133 1.00120.74 C
ANISOU 3071 C10 CLR A1203 15128 14895 15854 537 -187 -4 C
HETATM 3072 C11 CLR A1203 -4.434 5.337 21.917 1.00123.66 C
ANISOU 3072 C11 CLR A1203 15533 15290 16160 536 -157 -41 C
HETATM 3073 C12 CLR A1203 -4.320 3.891 22.178 1.00126.70 C
ANISOU 3073 C12 CLR A1203 15933 15675 16533 534 -126 -50 C
HETATM 3074 C13 CLR A1203 -4.579 3.465 20.854 1.00126.09 C
ANISOU 3074 C13 CLR A1203 15872 15609 16428 514 -84 -47 C
HETATM 3075 C14 CLR A1203 -3.523 4.064 19.948 1.00126.14 C
ANISOU 3075 C14 CLR A1203 15861 15597 16470 509 -67 -24 C
HETATM 3076 C15 CLR A1203 -3.800 3.244 18.779 1.00127.26 C
ANISOU 3076 C15 CLR A1203 16025 15752 16576 488 -18 -27 C
HETATM 3077 C16 CLR A1203 -3.815 1.878 19.455 1.00127.08 C
ANISOU 3077 C16 CLR A1203 16013 15724 16546 495 -3 -44 C
HETATM 3078 C17 CLR A1203 -4.180 2.054 20.939 1.00125.77 C
ANISOU 3078 C17 CLR A1203 15842 15559 16386 512 -50 -54 C
HETATM 3079 C18 CLR A1203 -6.086 3.680 20.541 1.00128.35 C
ANISOU 3079 C18 CLR A1203 16179 15928 16660 502 -95 -60 C
HETATM 3080 C19 CLR A1203 -4.779 7.921 20.754 1.00122.55 C
ANISOU 3080 C19 CLR A1203 15373 15152 16039 527 -203 -16 C
HETATM 3081 C20 CLR A1203 -5.291 1.270 21.703 1.00123.93 C
ANISOU 3081 C20 CLR A1203 15629 15347 16111 511 -61 -74 C
HETATM 3082 C21 CLR A1203 -4.859 0.725 23.064 1.00124.97 C
ANISOU 3082 C21 CLR A1203 15753 15465 16265 526 -82 -78 C
HETATM 3083 C22 CLR A1203 -5.871 0.170 20.839 1.00123.00 C
ANISOU 3083 C22 CLR A1203 15539 15244 15952 493 -20 -83 C
HETATM 3084 C23 CLR A1203 -5.121 -1.167 20.971 1.00123.62 C
ANISOU 3084 C23 CLR A1203 15621 15301 16049 495 10 -86 C
HETATM 3085 C24 CLR A1203 -5.851 -2.390 20.394 1.00122.90 C
ANISOU 3085 C24 CLR A1203 15559 15223 15915 478 42 -100 C
HETATM 3086 C25 CLR A1203 -5.771 -3.692 21.209 1.00122.09 C
ANISOU 3086 C25 CLR A1203 15463 15109 15816 482 43 -108 C
HETATM 3087 C26 CLR A1203 -6.057 -4.893 20.308 1.00117.28 C
ANISOU 3087 C26 CLR A1203 14879 14501 15181 466 85 -119 C
HETATM 3088 C27 CLR A1203 -4.450 -3.915 21.951 1.00125.54 C
ANISOU 3088 C27 CLR A1203 15875 15509 16313 499 36 -99 C
HETATM 3089 O1 CLR A1203 -1.897 11.609 21.276 1.00110.08 O
ANISOU 3089 O1 CLR A1203 13706 13490 14631 555 -308 49 O
HETATM 3090 C1 CLR A1204 -7.670 10.640 14.569 1.00120.48 C
ANISOU 3090 C1 CLR A1204 15156 14958 15662 401 -192 61 C
HETATM 3091 C2 CLR A1204 -7.836 12.146 14.719 1.00118.78 C
ANISOU 3091 C2 CLR A1204 14918 14730 15481 407 -251 75 C
HETATM 3092 C3 CLR A1204 -7.019 12.989 13.758 1.00117.73 C
ANISOU 3092 C3 CLR A1204 14773 14586 15374 385 -254 113 C
HETATM 3093 C4 CLR A1204 -7.187 12.487 12.304 1.00119.13 C
ANISOU 3093 C4 CLR A1204 14973 14784 15506 346 -210 130 C
HETATM 3094 C5 CLR A1204 -6.989 10.906 12.327 1.00121.67 C
ANISOU 3094 C5 CLR A1204 15316 15119 15795 348 -148 108 C
HETATM 3095 C6 CLR A1204 -5.973 10.366 11.691 1.00124.28 C
ANISOU 3095 C6 CLR A1204 15647 15448 16127 334 -100 119 C
HETATM 3096 C7 CLR A1204 -5.704 8.889 11.817 1.00127.68 C
ANISOU 3096 C7 CLR A1204 16094 15884 16537 340 -46 95 C
HETATM 3097 C8 CLR A1204 -7.040 8.320 11.731 1.00126.45 C
ANISOU 3097 C8 CLR A1204 15965 15749 16330 333 -45 75 C
HETATM 3098 C9 CLR A1204 -7.420 8.523 13.126 1.00124.91 C
ANISOU 3098 C9 CLR A1204 15759 15545 16157 366 -87 56 C
HETATM 3099 C10 CLR A1204 -7.852 10.033 13.183 1.00122.41 C
ANISOU 3099 C10 CLR A1204 15425 15222 15862 366 -146 72 C
HETATM 3100 C11 CLR A1204 -8.548 7.634 13.375 1.00125.41 C
ANISOU 3100 C11 CLR A1204 15847 15627 16175 366 -79 30 C
HETATM 3101 C12 CLR A1204 -8.266 6.213 13.437 1.00124.82 C
ANISOU 3101 C12 CLR A1204 15789 15555 16082 367 -31 13 C
HETATM 3102 C13 CLR A1204 -7.874 5.992 12.084 1.00124.10 C
ANISOU 3102 C13 CLR A1204 15709 15471 15971 338 11 28 C
HETATM 3103 C14 CLR A1204 -6.716 6.937 11.809 1.00126.92 C
ANISOU 3103 C14 CLR A1204 16040 15812 16374 337 4 55 C
HETATM 3104 C15 CLR A1204 -6.314 6.411 10.530 1.00129.36 C
ANISOU 3104 C15 CLR A1204 16363 16132 16656 307 56 63 C
HETATM 3105 C16 CLR A1204 -6.338 4.947 10.939 1.00123.99 C
ANISOU 3105 C16 CLR A1204 15699 15451 15960 319 94 34 C
HETATM 3106 C17 CLR A1204 -7.205 4.699 12.170 1.00122.56 C
ANISOU 3106 C17 CLR A1204 15521 15269 15775 343 59 12 C
HETATM 3107 C18 CLR A1204 -9.119 5.956 11.142 1.00123.77 C
ANISOU 3107 C18 CLR A1204 15696 15457 15875 308 12 29 C
HETATM 3108 C19 CLR A1204 -9.268 10.143 12.639 1.00122.05 C
ANISOU 3108 C19 CLR A1204 15401 15201 15774 348 -161 68 C
HETATM 3109 C20 CLR A1204 -8.240 3.533 12.240 1.00117.18 C
ANISOU 3109 C20 CLR A1204 14872 14606 15047 339 76 -13 C
HETATM 3110 C21 CLR A1204 -8.542 3.013 13.658 1.00116.58 C
ANISOU 3110 C21 CLR A1204 14791 14523 14980 367 54 -34 C
HETATM 3111 C22 CLR A1204 -7.814 2.403 11.309 1.00111.38 C
ANISOU 3111 C22 CLR A1204 14156 13875 14288 320 136 -20 C
HETATM 3112 C23 CLR A1204 -8.369 0.990 11.589 1.00106.28 C
ANISOU 3112 C23 CLR A1204 13535 13234 13612 323 159 -47 C
HETATM 3113 C24 CLR A1204 -7.298 -0.040 12.020 1.00104.70 C
ANISOU 3113 C24 CLR A1204 13326 13011 13443 340 192 -60 C
HETATM 3114 C25 CLR A1204 -7.734 -1.505 12.219 1.00103.29 C
ANISOU 3114 C25 CLR A1204 13172 12834 13240 340 215 -85 C
HETATM 3115 C26 CLR A1204 -7.597 -1.958 13.676 1.00102.13 C
ANISOU 3115 C26 CLR A1204 13013 12670 13123 369 191 -95 C
HETATM 3116 C27 CLR A1204 -9.124 -1.851 11.680 1.00104.10 C
ANISOU 3116 C27 CLR A1204 13308 12963 13282 318 214 -94 C
HETATM 3117 O1 CLR A1204 -7.422 14.348 14.031 1.00117.84 O
ANISOU 3117 O1 CLR A1204 14768 14587 15419 393 -317 121 O
HETATM 3118 C1 OLA A1205 -37.314 14.640 13.020 1.00113.44 C
ANISOU 3118 C1 OLA A1205 14180 14398 14523 321 -736 -176 C
HETATM 3119 O1 OLA A1205 -36.821 15.650 12.457 1.00118.64 O
ANISOU 3119 O1 OLA A1205 14830 15021 15225 318 -772 -152 O
HETATM 3120 O2 OLA A1205 -37.944 14.708 14.099 1.00115.21 O
ANISOU 3120 O2 OLA A1205 14372 14642 14759 353 -739 -220 O
HETATM 3121 C2 OLA A1205 -37.153 13.293 12.358 1.00109.79 C
ANISOU 3121 C2 OLA A1205 13768 13957 13991 285 -687 -150 C
HETATM 3122 C3 OLA A1205 -36.813 12.199 13.374 1.00107.35 C
ANISOU 3122 C3 OLA A1205 13470 13677 13640 301 -636 -180 C
HETATM 3123 C4 OLA A1205 -37.215 10.850 12.829 1.00106.05 C
ANISOU 3123 C4 OLA A1205 13345 13538 13409 268 -598 -163 C
HETATM 3124 C5 OLA A1205 -36.188 10.364 11.808 1.00106.17 C
ANISOU 3124 C5 OLA A1205 13406 13538 13396 236 -571 -124 C
HETATM 3125 C6 OLA A1205 -36.660 9.073 11.159 1.00104.36 C
ANISOU 3125 C6 OLA A1205 13216 13330 13104 201 -537 -108 C
HETATM 3126 C7 OLA A1205 -36.899 8.018 12.233 1.00101.77 C
ANISOU 3126 C7 OLA A1205 12890 13035 12743 217 -503 -140 C
HETATM 3127 C8 OLA A1205 -37.159 6.666 11.611 1.00 99.87 C
ANISOU 3127 C8 OLA A1205 12693 12811 12441 183 -467 -124 C
HETATM 3128 C9 OLA A1205 -36.024 6.340 10.670 1.00 99.98 C
ANISOU 3128 C9 OLA A1205 12745 12805 12437 159 -441 -95 C
HETATM 3129 C10 OLA A1205 -36.106 5.323 9.812 1.00100.41 C
ANISOU 3129 C10 OLA A1205 12843 12868 12443 124 -413 -75 C
HETATM 3130 C11 OLA A1205 -37.316 4.412 9.702 1.00100.57 C
ANISOU 3130 C11 OLA A1205 12876 12913 12421 104 -408 -77 C
HETATM 3131 C12 OLA A1205 -36.914 2.946 9.633 1.00 99.16 C
ANISOU 3131 C12 OLA A1205 12739 12746 12192 89 -359 -78 C
HETATM 3132 C13 OLA A1205 -38.158 2.167 9.256 1.00 97.79 C
ANISOU 3132 C13 OLA A1205 12582 12594 11980 61 -361 -71 C
HETATM 3133 C14 OLA A1205 -37.951 0.705 9.585 1.00 94.40 C
ANISOU 3133 C14 OLA A1205 12182 12179 11506 55 -319 -81 C
HETATM 3134 C15 OLA A1205 -37.406 -0.029 8.363 1.00 92.04 C
ANISOU 3134 C15 OLA A1205 11933 11868 11171 19 -291 -59 C
HETATM 3135 C16 OLA A1205 -36.146 -0.803 8.735 1.00 89.85 C
ANISOU 3135 C16 OLA A1205 11673 11582 10885 31 -248 -71 C
HETATM 3136 C17 OLA A1205 -36.375 -2.317 8.687 1.00 88.13 C
ANISOU 3136 C17 OLA A1205 11489 11375 10620 13 -218 -75 C
HETATM 3137 C18 OLA A1205 -37.337 -2.822 9.751 1.00 88.22 C
ANISOU 3137 C18 OLA A1205 11483 11414 10624 25 -226 -92 C
HETATM 3138 C1 OLA A1206 -20.367 12.123 1.153 1.00135.81 C
ANISOU 3138 C1 OLA A1206 17370 17132 17100 -62 -306 260 C
HETATM 3139 O1 OLA A1206 -19.231 11.598 1.090 1.00142.00 O
ANISOU 3139 O1 OLA A1206 18159 17919 17877 -60 -256 254 O
HETATM 3140 O2 OLA A1206 -21.013 12.455 0.131 1.00141.39 O
ANISOU 3140 O2 OLA A1206 18093 17848 17781 -105 -329 290 O
HETATM 3141 C2 OLA A1206 -20.995 12.354 2.517 1.00127.09 C
ANISOU 3141 C2 OLA A1206 16238 16013 16036 -11 -341 228 C
HETATM 3142 C3 OLA A1206 -20.837 11.134 3.423 1.00119.45 C
ANISOU 3142 C3 OLA A1206 15278 15053 15053 22 -294 185 C
HETATM 3143 C4 OLA A1206 -21.575 9.942 2.825 1.00115.48 C
ANISOU 3143 C4 OLA A1206 14814 14576 14486 -4 -258 175 C
HETATM 3144 C5 OLA A1206 -21.678 8.811 3.837 1.00109.57 C
ANISOU 3144 C5 OLA A1206 14071 13833 13727 31 -225 133 C
HETATM 3145 C6 OLA A1206 -20.676 7.701 3.538 1.00105.22 C
ANISOU 3145 C6 OLA A1206 13542 13289 13148 24 -158 123 C
HETATM 3146 C7 OLA A1206 -21.037 6.439 4.318 1.00103.33 C
ANISOU 3146 C7 OLA A1206 13316 13058 12888 47 -129 86 C
HETATM 3147 C8 OLA A1206 -20.568 5.179 3.606 1.00103.70 C
ANISOU 3147 C8 OLA A1206 13397 13116 12889 25 -67 78 C
HETATM 3148 C9 OLA A1206 -21.435 4.967 2.383 1.00104.86 C
ANISOU 3148 C9 OLA A1206 13577 13282 12984 -22 -66 94 C
HETATM 3149 C10 OLA A1206 -21.352 3.866 1.629 1.00105.30 C
ANISOU 3149 C10 OLA A1206 13668 13351 12990 -48 -18 85 C
HETATM 3150 C11 OLA A1206 -20.398 2.717 1.893 1.00104.32 C
ANISOU 3150 C11 OLA A1206 13554 13223 12861 -32 40 58 C
HETATM 3151 C12 OLA A1206 -21.109 1.395 1.625 1.00103.22 C
ANISOU 3151 C12 OLA A1206 13451 13098 12672 -47 68 37 C
HETATM 3152 C13 OLA A1206 -20.118 0.242 1.693 1.00101.30 C
ANISOU 3152 C13 OLA A1206 13219 12848 12424 -36 126 12 C
HETATM 3153 C14 OLA A1206 -20.087 -0.403 3.076 1.00100.46 C
ANISOU 3153 C14 OLA A1206 13097 12729 12345 8 126 -16 C
HETATM 3154 C15 OLA A1206 -18.702 -0.266 3.696 1.00 98.28 C
ANISOU 3154 C15 OLA A1206 12793 12432 12116 38 145 -22 C
HETATM 3155 C16 OLA A1206 -18.009 -1.625 3.784 1.00 94.18 C
ANISOU 3155 C16 OLA A1206 12288 11905 11590 47 197 -49 C
HETATM 3156 C1 OLA A1207 -14.954 14.106 1.190 1.00123.08 C
ANISOU 3156 C1 OLA A1207 15677 15468 15619 -48 -263 326 C
HETATM 3157 O1 OLA A1207 -16.171 14.145 0.891 1.00125.75 O
ANISOU 3157 O1 OLA A1207 16030 15815 15934 -63 -291 328 O
HETATM 3158 O2 OLA A1207 -14.343 15.126 1.591 1.00123.57 O
ANISOU 3158 O2 OLA A1207 15707 15508 15736 -33 -300 344 O
HETATM 3159 C2 OLA A1207 -14.180 12.810 1.069 1.00122.72 C
ANISOU 3159 C2 OLA A1207 15651 15439 15539 -47 -185 302 C
HETATM 3160 C3 OLA A1207 -15.098 11.590 1.044 1.00120.00 C
ANISOU 3160 C3 OLA A1207 15338 15113 15143 -47 -154 270 C
HETATM 3161 C4 OLA A1207 -14.299 10.333 0.742 1.00117.46 C
ANISOU 3161 C4 OLA A1207 15036 14806 14787 -52 -78 249 C
HETATM 3162 C5 OLA A1207 -15.178 9.280 0.074 1.00116.02 C
ANISOU 3162 C5 OLA A1207 14895 14649 14539 -78 -47 234 C
HETATM 3163 C6 OLA A1207 -15.530 8.146 1.034 1.00110.80 C
ANISOU 3163 C6 OLA A1207 14241 13984 13872 -40 -24 189 C
HETATM 3164 C1 OLA A1208 -9.935 -14.490 17.438 1.00112.60 C
ANISOU 3164 C1 OLA A1208 14484 13903 14395 361 234 -220 C
HETATM 3165 O1 OLA A1208 -11.002 -14.489 16.785 1.00118.02 O
ANISOU 3165 O1 OLA A1208 15196 14617 15027 342 239 -225 O
HETATM 3166 O2 OLA A1208 -8.970 -15.225 17.123 1.00115.17 O
ANISOU 3166 O2 OLA A1208 14804 14193 14762 369 260 -231 O
HETATM 3167 C2 OLA A1208 -9.804 -13.586 18.647 1.00109.42 C
ANISOU 3167 C2 OLA A1208 14057 13509 14010 375 193 -202 C
HETATM 3168 C3 OLA A1208 -10.363 -12.190 18.355 1.00102.83 C
ANISOU 3168 C3 OLA A1208 13218 12707 13144 373 184 -195 C
HETATM 3169 C4 OLA A1208 -9.761 -11.163 19.297 1.00100.35 C
ANISOU 3169 C4 OLA A1208 12874 12390 12865 392 155 -180 C
HETATM 3170 C5 OLA A1208 -8.639 -10.387 18.619 1.00 98.59 C
ANISOU 3170 C5 OLA A1208 12630 12149 12679 403 179 -177 C
HETATM 3171 C6 OLA A1208 -8.710 -8.918 19.005 1.00 94.73 C
ANISOU 3171 C6 OLA A1208 12122 11678 12193 412 151 -164 C
HETATM 3172 C7 OLA A1208 -7.544 -8.542 19.910 1.00 97.58 C
ANISOU 3172 C7 OLA A1208 12451 12011 12612 433 132 -153 C
HETATM 3173 NA NA A1209 -23.619 -7.885 16.501 1.00 95.92 NA
ANISOU 3173 NA NA A1209 12443 12182 11822 231 16 -185 NA
HETATM 3174 O HOH A1301 -21.862 12.448 18.257 1.00 99.24 O
ANISOU 3174 O HOH A1301 12465 12464 12777 459 -466 -172 O
HETATM 3175 O HOH A1302 -15.414 3.209 22.910 1.00 93.75 O
ANISOU 3175 O HOH A1302 11870 11757 11994 477 -204 -185 O
HETATM 3176 O HOH A1303 -27.788 3.567 19.936 1.00 86.26 O
ANISOU 3176 O HOH A1303 10956 11054 10766 371 -277 -254 O
HETATM 3177 O HOH A1304 -25.927 8.580 13.672 1.00 65.38 O
ANISOU 3177 O HOH A1304 8313 8272 8257 305 -360 -110 O
HETATM 3178 O HOH A1305 -18.910 6.812 19.476 1.00 86.48 O
ANISOU 3178 O HOH A1305 10938 10870 11050 442 -274 -170 O
HETATM 3179 O HOH A1306 -18.872 -11.701 13.540 1.00 72.21 O
ANISOU 3179 O HOH A1306 9512 9038 8888 218 184 -207 O
HETATM 3180 O HOH A1307 -16.000 0.671 12.955 1.00 81.90 O
ANISOU 3180 O HOH A1307 10529 10264 10327 295 18 -95 O
HETATM 3181 O HOH A1308 -25.046 2.552 16.406 1.00 71.42 O
ANISOU 3181 O HOH A1308 9156 9096 8885 315 -197 -173 O
HETATM 3182 O HOH A1309 -22.997 -5.226 14.813 1.00 80.89 O
ANISOU 3182 O HOH A1309 10517 10264 9951 235 10 -168 O
HETATM 3183 O HOH A1310 -25.040 -14.729 14.440 1.00 79.52 O
ANISOU 3183 O HOH A1310 10522 10074 9620 128 99 -198 O
HETATM 3184 O HOH A1311 -18.087 13.681 26.432 1.00 87.55 O
ANISOU 3184 O HOH A1311 10883 10955 11426 625 -545 -323 O
HETATM 3185 O HOH A1312 -20.410 -22.306 15.277 1.00 67.19 O
ANISOU 3185 O HOH A1312 9015 8283 8231 147 171 -252 O
CONECT 399 3173
CONECT 535 1183
CONECT 551 1092
CONECT 571 1227
CONECT 1092 551
CONECT 1183 535
CONECT 1227 571
CONECT 2619 2640
CONECT 2640 2619
CONECT 3010 3022 3023 3026
CONECT 3011 3013 3023 3024
CONECT 3012 3022 3024 3027
CONECT 3013 3011 3029 3032
CONECT 3014 3029 3030 3033
CONECT 3015 3025 3030
CONECT 3016 3017
CONECT 3017 3016 3018 3019 3020
CONECT 3018 3017
CONECT 3019 3017
CONECT 3020 3017 3021
CONECT 3021 3020 3028 3031
CONECT 3022 3010 3012 3028
CONECT 3023 3010 3011
CONECT 3024 3011 3012
CONECT 3025 3015 3033
CONECT 3026 3010
CONECT 3027 3012
CONECT 3028 3021 3022
CONECT 3029 3013 3014
CONECT 3030 3014 3015
CONECT 3031 3021
CONECT 3032 3013
CONECT 3033 3014 3025
CONECT 3034 3035 3043
CONECT 3035 3034 3036
CONECT 3036 3035 3037 3061
CONECT 3037 3036 3038
CONECT 3038 3037 3039 3043
CONECT 3039 3038 3040
CONECT 3040 3039 3041
CONECT 3041 3040 3042 3047
CONECT 3042 3041 3043 3044
CONECT 3043 3034 3038 3042 3052
CONECT 3044 3042 3045
CONECT 3045 3044 3046
CONECT 3046 3045 3047 3050 3051
CONECT 3047 3041 3046 3048
CONECT 3048 3047 3049
CONECT 3049 3048 3050
CONECT 3050 3046 3049 3053
CONECT 3051 3046
CONECT 3052 3043
CONECT 3053 3050 3054 3055
CONECT 3054 3053
CONECT 3055 3053 3056
CONECT 3056 3055 3057
CONECT 3057 3056 3058
CONECT 3058 3057 3059 3060
CONECT 3059 3058
CONECT 3060 3058
CONECT 3061 3036
CONECT 3062 3063 3071
CONECT 3063 3062 3064
CONECT 3064 3063 3065 3089
CONECT 3065 3064 3066
CONECT 3066 3065 3067 3071
CONECT 3067 3066 3068
CONECT 3068 3067 3069
CONECT 3069 3068 3070 3075
CONECT 3070 3069 3071 3072
CONECT 3071 3062 3066 3070 3080
CONECT 3072 3070 3073
CONECT 3073 3072 3074
CONECT 3074 3073 3075 3078 3079
CONECT 3075 3069 3074 3076
CONECT 3076 3075 3077
CONECT 3077 3076 3078
CONECT 3078 3074 3077 3081
CONECT 3079 3074
CONECT 3080 3071
CONECT 3081 3078 3082 3083
CONECT 3082 3081
CONECT 3083 3081 3084
CONECT 3084 3083 3085
CONECT 3085 3084 3086
CONECT 3086 3085 3087 3088
CONECT 3087 3086
CONECT 3088 3086
CONECT 3089 3064
CONECT 3090 3091 3099
CONECT 3091 3090 3092
CONECT 3092 3091 3093 3117
CONECT 3093 3092 3094
CONECT 3094 3093 3095 3099
CONECT 3095 3094 3096
CONECT 3096 3095 3097
CONECT 3097 3096 3098 3103
CONECT 3098 3097 3099 3100
CONECT 3099 3090 3094 3098 3108
CONECT 3100 3098 3101
CONECT 3101 3100 3102
CONECT 3102 3101 3103 3106 3107
CONECT 3103 3097 3102 3104
CONECT 3104 3103 3105
CONECT 3105 3104 3106
CONECT 3106 3102 3105 3109
CONECT 3107 3102
CONECT 3108 3099
CONECT 3109 3106 3110 3111
CONECT 3110 3109
CONECT 3111 3109 3112
CONECT 3112 3111 3113
CONECT 3113 3112 3114
CONECT 3114 3113 3115 3116
CONECT 3115 3114
CONECT 3116 3114
CONECT 3117 3092
CONECT 3118 3119 3120 3121
CONECT 3119 3118
CONECT 3120 3118
CONECT 3121 3118 3122
CONECT 3122 3121 3123
CONECT 3123 3122 3124
CONECT 3124 3123 3125
CONECT 3125 3124 3126
CONECT 3126 3125 3127
CONECT 3127 3126 3128
CONECT 3128 3127 3129
CONECT 3129 3128 3130
CONECT 3130 3129 3131
CONECT 3131 3130 3132
CONECT 3132 3131 3133
CONECT 3133 3132 3134
CONECT 3134 3133 3135
CONECT 3135 3134 3136
CONECT 3136 3135 3137
CONECT 3137 3136
CONECT 3138 3139 3140 3141
CONECT 3139 3138
CONECT 3140 3138
CONECT 3141 3138 3142
CONECT 3142 3141 3143
CONECT 3143 3142 3144
CONECT 3144 3143 3145
CONECT 3145 3144 3146
CONECT 3146 3145 3147
CONECT 3147 3146 3148
CONECT 3148 3147 3149
CONECT 3149 3148 3150
CONECT 3150 3149 3151
CONECT 3151 3150 3152
CONECT 3152 3151 3153
CONECT 3153 3152 3154
CONECT 3154 3153 3155
CONECT 3155 3154
CONECT 3156 3157 3158 3159
CONECT 3157 3156
CONECT 3158 3156
CONECT 3159 3156 3160
CONECT 3160 3159 3161
CONECT 3161 3160 3162
CONECT 3162 3161 3163
CONECT 3163 3162
CONECT 3164 3165 3166 3167
CONECT 3165 3164
CONECT 3166 3164
CONECT 3167 3164 3168
CONECT 3168 3167 3169
CONECT 3169 3168 3170
CONECT 3170 3169 3171
CONECT 3171 3170 3172
CONECT 3172 3171
CONECT 3173 399
MASTER 341 0 9 19 2 0 0 6 3162 1 173 33
END