HEADER PROTEIN BINDING 15-JUN-20 6ZDR
TITLE CRYSTAL STRUCTURE OF STABILIZED A2A ADENOSINE RECEPTOR A2AR-STAR2-BRIL
TITLE 2 IN COMPLEX WITH CHROMONE 4D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE
COMPND 3 RECEPTOR A2A;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: CYTOCHROME B-562;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: ADORA2A, ADORA2, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS G PROTEIN-COUPLED RECEPTOR, MEMBRANE PROTEIN, RECEPTOR, PROTEIN
KEYWDS 2 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR G.VERDON,W.JESPERS,J.AZUAJE,M.MAJELLARO,H.KERANEN,X.GARCIA-MERA,
AUTHOR 2 M.CONGREVE,F.DEFLORIAN,C.DE GRAAF,A.ZHUKOV,A.DORE,J.MASON,J.AQVIST,
AUTHOR 3 R.COOKE,E.SOTELO,H.GUTIERREZ-DE-TERAN
REVDAT 2 16-DEC-20 6ZDR 1 JRNL
REVDAT 1 16-SEP-20 6ZDR 0
JRNL AUTH W.JESPERS,G.VERDON,J.AZUAJE,M.MAJELLARO,H.KERANEN,
JRNL AUTH 2 X.GARCIA-MERA,M.CONGREVE,F.DEFLORIAN,C.DE GRAAF,A.ZHUKOV,
JRNL AUTH 3 A.S.DORE,J.S.MASON,J.AQVIST,R.M.COOKE,E.SOTELO,
JRNL AUTH 4 H.GUTIERREZ-DE-TERAN
JRNL TITL X-RAY CRYSTALLOGRAPHY AND FREE ENERGY CALCULATIONS REVEAL
JRNL TITL 2 THE BINDING MECHANISM OF A 2A ADENOSINE RECEPTOR
JRNL TITL 3 ANTAGONISTS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 59 16536 2020
JRNL REFN ESSN 1521-3773
JRNL PMID 32542862
JRNL DOI 10.1002/ANIE.202003788
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.4
REMARK 3 NUMBER OF REFLECTIONS : 32710
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1636
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.00
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 14.71
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2334
REMARK 3 BIN FREE R VALUE : 0.2566
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 35
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2958
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 327
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.83270
REMARK 3 B22 (A**2) : 5.93510
REMARK 3 B33 (A**2) : -4.10240
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.270
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.177
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.141
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.178
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.143
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3391 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4572 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1260 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 541 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3365 ; 10.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 445 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3180 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.022
REMARK 3 BOND ANGLES (DEGREES) : 1.47
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.39
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.38
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|0 - A|208 A|219 - A|305 A|1201 - A|1201 }
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8684 -7.3219 17.8996
REMARK 3 T TENSOR
REMARK 3 T11: -0.0004 T22: 0.0487
REMARK 3 T33: -0.0596 T12: -0.0086
REMARK 3 T13: -0.0034 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0 L22: 0.1226
REMARK 3 L33: 0.0132 L12: -0.0065
REMARK 3 L13: 0.139 L23: 0.0072
REMARK 3 S TENSOR
REMARK 3 S11: 0.0025 S12: -0.0426 S13: 0.024
REMARK 3 S21: -0.0426 S22: -0.0153 S23: -0.0622
REMARK 3 S31: 0.024 S32: -0.0622 S33: 0.0128
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1001 - A|1106 }
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1531 -55.1057 20.1162
REMARK 3 T TENSOR
REMARK 3 T11: -0.0224 T22: -0.1852
REMARK 3 T33: 0.1786 T12: 0.0817
REMARK 3 T13: -0.001 T23: -0.0463
REMARK 3 L TENSOR
REMARK 3 L11: 0.8283 L22: 1.3806
REMARK 3 L33: 0 L12: -1.4039
REMARK 3 L13: 0.4463 L23: -0.4284
REMARK 3 S TENSOR
REMARK 3 S11: 0.0885 S12: -0.5015 S13: 0.4264
REMARK 3 S21: -0.5015 S22: 0.1669 S23: -0.1479
REMARK 3 S31: 0.4264 S32: -0.1479 S33: -0.2554
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ZDR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUN-20.
REMARK 100 THE DEPOSITION ID IS D_1292109396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : 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) : 0.96861
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32710
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.918
REMARK 200 RESOLUTION RANGE LOW (A) : 45.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5IU4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400; SODIUM CITRATE; SODIUM
REMARK 280 THIOCYANATE; 2,5 HEXANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.00050
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 70.00050
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 19.63150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.11300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.63150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.11300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.00050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.63150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.11300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.00050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.63150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.11300
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 ASP A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 GLY A -1
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 LYS A 1059
REMARK 465 ASP A 1060
REMARK 465 PHE A 1061
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 ALA A 317
REMARK 465 ALA 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 465 HIS A 327
REMARK 465 HIS A 328
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 SER A 6 CA - C - O ANGL. DEV. = 13.1 DEGREES
REMARK 500 TRP A 29 CA - C - O ANGL. DEV. = 13.7 DEGREES
REMARK 500 TRP A 29 CA - C - O ANGL. DEV. = 14.2 DEGREES
REMARK 500 HIS A 75 CA - C - O ANGL. DEV. = 13.3 DEGREES
REMARK 500 HIS A 75 CA - C - O ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG A 205 CA - C - O ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG A 205 CA - C - O ANGL. DEV. = 12.7 DEGREES
REMARK 500 LEU A 208 O - C - N ANGL. DEV. = -14.0 DEGREES
REMARK 500 CYS A 262 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A1101 -67.02 -135.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER A 6 -10.27
REMARK 500 SER A 6 -11.25
REMARK 500 SER A 7 -10.48
REMARK 500 LEU A 208 -10.55
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
REMARK 610 OLA A 1209
REMARK 610 OLA A 1210
REMARK 610 OLC A 1211
REMARK 610 OLC A 1212
REMARK 610 OLC A 1213
REMARK 610 OLA A 1214
REMARK 610 OLA A 1217
REMARK 610 OLA A 1218
REMARK 610 OLA A 1219
REMARK 610 OLA A 1220
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 OD1
REMARK 620 2 SER A 91 OG 128.0
REMARK 620 3 HOH A1315 O 107.3 121.4
REMARK 620 4 HOH A1334 O 89.2 110.7 85.2
REMARK 620 5 HOH A1377 O 88.6 75.4 89.6 173.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue QGE A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1220
DBREF 6ZDR A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 6ZDR A 1001 1105 UNP P0ABE7 C562_ECOLX 23 127
DBREF 6ZDR A 219 317 UNP P29274 AA2AR_HUMAN 219 317
SEQADV 6ZDR ASP A -8 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR TYR A -7 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR LYS A -6 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR ASP A -5 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR ASP A -4 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR ASP A -3 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR ASP A -2 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR GLY A -1 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION
SEQADV 6ZDR ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION
SEQADV 6ZDR ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION
SEQADV 6ZDR ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION
SEQADV 6ZDR ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION
SEQADV 6ZDR ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION
SEQADV 6ZDR TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 6ZDR ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 6ZDR LEU A 1106 UNP P0ABE7 LINKER
SEQADV 6ZDR ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION
SEQADV 6ZDR ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION
SEQADV 6ZDR ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION
SEQADV 6ZDR ALA A 318 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 326 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 327 UNP P29274 EXPRESSION TAG
SEQADV 6ZDR HIS A 328 UNP P29274 EXPRESSION TAG
SEQRES 1 A 433 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET
SEQRES 2 A 433 GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA
SEQRES 3 A 433 VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA
SEQRES 4 A 433 VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR
SEQRES 5 A 433 PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL GLY
SEQRES 6 A 433 VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY
SEQRES 7 A 433 PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS
SEQRES 8 A 433 PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER LEU
SEQRES 9 A 433 LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA ILE
SEQRES 10 A 433 PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA
SEQRES 11 A 433 ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA
SEQRES 12 A 433 ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY
SEQRES 13 A 433 GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS GLY
SEQRES 14 A 433 GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO
SEQRES 15 A 433 MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL
SEQRES 16 A 433 LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG
SEQRES 17 A 433 ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU
SEQRES 18 A 433 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE
SEQRES 19 A 433 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU
SEQRES 20 A 433 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA
SEQRES 21 A 433 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO
SEQRES 22 A 433 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL
SEQRES 23 A 433 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY
SEQRES 24 A 433 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS
SEQRES 25 A 433 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG
SEQRES 26 A 433 ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS
SEQRES 27 A 433 SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP
SEQRES 28 A 433 LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS
SEQRES 29 A 433 PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU
SEQRES 30 A 433 ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO
SEQRES 31 A 433 PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR
SEQRES 32 A 433 PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN
SEQRES 33 A 433 GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES 34 A 433 HIS HIS HIS HIS
HET QGE A1201 24
HET NA A1202 1
HET CLR A1203 28
HET CLR A1204 28
HET CLR A1205 28
HET OLA A1206 15
HET OLA A1207 5
HET OLA A1208 14
HET OLA A1209 8
HET OLA A1210 16
HET OLC A1211 19
HET OLC A1212 20
HET OLC A1213 18
HET OLA A1214 12
HET OLA A1215 20
HET OLC A1216 25
HET OLA A1217 11
HET OLA A1218 15
HET OLA A1219 11
HET OLA A1220 9
HETNAM QGE [3-(4-METHYL-1,3-THIAZOL-2-YL)-4-OXIDANYLIDENE-6-
HETNAM 2 QGE PROPYL-CHROMEN-7-YL] ETHANOATE
HETNAM NA SODIUM ION
HETNAM CLR CHOLESTEROL
HETNAM OLA OLEIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 QGE C18 H17 N O4 S
FORMUL 3 NA NA 1+
FORMUL 4 CLR 3(C27 H46 O)
FORMUL 7 OLA 11(C18 H34 O2)
FORMUL 12 OLC 4(C21 H40 O4)
FORMUL 22 HOH *104(H2 O)
HELIX 1 AA1 PRO A 1 ASN A 34 1 34
HELIX 2 AA2 SER A 35 GLN A 38 5 4
HELIX 3 AA3 ASN A 39 LEU A 58 1 20
HELIX 4 AA4 LEU A 58 THR A 68 1 11
HELIX 5 AA5 CYS A 74 ILE A 108 1 35
HELIX 6 AA6 ARG A 111 VAL A 116 1 6
HELIX 7 AA7 THR A 117 LEU A 137 1 21
HELIX 8 AA8 THR A 138 GLY A 142 5 5
HELIX 9 AA9 LYS A 150 GLN A 157 1 8
HELIX 10 AB1 LEU A 167 VAL A 172 1 6
HELIX 11 AB2 PRO A 173 PHE A 180 1 8
HELIX 12 AB3 VAL A 186 LYS A 1019 1 42
HELIX 13 AB4 ASN A 1022 GLN A 1041 1 20
HELIX 14 AB5 HIS A 1063 GLU A 1081 1 19
HELIX 15 AB6 LYS A 1083 TYR A 1101 1 19
HELIX 16 AB7 TYR A 1101 CYS A 259 1 47
HELIX 17 AB8 PRO A 266 ILE A 292 1 27
HELIX 18 AB9 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 2.02
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.02
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.08
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03
LINK OD1 ASP A 52 NA NA A1202 1555 1555 2.36
LINK OG SER A 91 NA NA A1202 1555 1555 2.59
LINK NA NA A1202 O HOH A1315 1555 1555 2.56
LINK NA NA A1202 O HOH A1334 1555 1555 2.23
LINK NA NA A1202 O HOH A1377 1555 1555 2.44
SITE 1 AC1 16 LEU A 85 PHE A 168 GLU A 169 MET A 177
SITE 2 AC1 16 LEU A 249 HIS A 250 ASN A 253 HIS A 264
SITE 3 AC1 16 LEU A 267 MET A 270 TYR A 271 ILE A 274
SITE 4 AC1 16 HOH A1319 HOH A1327 HOH A1343 HOH A1362
SITE 1 AC2 5 ASP A 52 SER A 91 HOH A1315 HOH A1334
SITE 2 AC2 5 HOH A1377
SITE 1 AC3 3 LEU A 247 PRO A 248 SER A 263
SITE 1 AC4 7 PHE A 258 CYS A 259 CLR A1205 OLC A1211
SITE 2 AC4 7 OLC A1212 OLC A1213 HOH A1341
SITE 1 AC5 6 ALA A 72 ALA A 73 GLY A 76 ILE A 80
SITE 2 AC5 6 CLR A1204 OLC A1211
SITE 1 AC6 1 PRO A 266
SITE 1 AC7 3 SER A 7 LEU A 19 PHE A 286
SITE 1 AC8 2 SER A 6 THR A 68
SITE 1 AC9 1 VAL A 282
SITE 1 AD1 1 THR A 11
SITE 1 AD2 5 PHE A 258 CLR A1204 CLR A1205 HOH A1335
SITE 2 AD2 5 HOH A1368
SITE 1 AD3 6 PHE A 255 ASP A 261 CLR A1204 OLC A1213
SITE 2 AD3 6 OLA A1217 HOH A1324
SITE 1 AD4 6 THR A 65 PHE A 70 CYS A 71 ASP A 261
SITE 2 AD4 6 CLR A1204 OLC A1212
SITE 1 AD5 6 MET A 140 LEU A 141 TYR A 179 ALA A 184
SITE 2 AD5 6 OLA A1215 HOH A1338
SITE 1 AD6 2 OLA A1214 HOH A1304
SITE 1 AD7 3 TYR A 43 LEU A 54 TRP A 129
SITE 1 AD8 3 THR A 65 THR A 68 OLC A1212
SITE 1 AD9 2 TYR A 271 HOH A1309
SITE 1 AE1 3 CYS A 28 TRP A 32 ALA A 50
SITE 1 AE2 1 VAL A 116
CRYST1 39.263 180.226 140.001 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 0.025469 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005549 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007143 0.00000
ATOM 1 N ALA A 0 -22.231 21.735 0.766 1.00 68.12 N
ANISOU 1 N ALA A 0 8790 8865 8229 76 -246 -63 N
ATOM 2 CA ALA A 0 -23.502 21.233 0.288 1.00 68.15 C
ANISOU 2 CA ALA A 0 8814 8874 8204 67 -246 -80 C
ATOM 3 C ALA A 0 -24.560 20.967 1.337 1.00 66.49 C
ANISOU 3 C ALA A 0 8585 8699 7978 72 -266 -100 C
ATOM 4 O ALA A 0 -24.247 20.716 2.492 1.00 65.90 O
ANISOU 4 O ALA A 0 8483 8644 7912 81 -268 -97 O
ATOM 5 CB ALA A 0 -23.263 19.974 -0.498 1.00 68.43 C
ANISOU 5 CB ALA A 0 8876 8892 8231 58 -202 -63 C
ATOM 6 N PRO A 1 -25.836 20.991 0.917 1.00 65.63 N
ANISOU 6 N PRO A 1 8492 8596 7846 65 -281 -121 N
ATOM 7 CA PRO A 1 -26.960 20.731 1.807 1.00 64.08 C
ANISOU 7 CA PRO A 1 8281 8434 7634 68 -299 -141 C
ATOM 8 C PRO A 1 -26.736 19.400 2.491 1.00 62.19 C
ANISOU 8 C PRO A 1 8031 8206 7391 68 -270 -128 C
ATOM 9 O PRO A 1 -26.404 18.404 1.874 1.00 62.20 O
ANISOU 9 O PRO A 1 8052 8191 7389 61 -235 -111 O
ATOM 10 CB PRO A 1 -28.172 20.650 0.875 1.00 65.74 C
ANISOU 10 CB PRO A 1 8519 8638 7822 57 -305 -158 C
ATOM 11 CG PRO A 1 -27.745 21.214 -0.421 1.00 67.45 C
ANISOU 11 CG PRO A 1 8764 8820 8044 50 -301 -151 C
ATOM 12 CD PRO A 1 -26.252 21.110 -0.492 1.00 66.08 C
ANISOU 12 CD PRO A 1 8587 8629 7893 53 -276 -124 C
ATOM 13 N PRO A 2 -26.898 19.385 3.807 1.00 60.10 N
ANISOU 13 N PRO A 2 7736 7972 7128 78 -285 -135 N
ATOM 14 CA PRO A 2 -26.710 18.183 4.612 1.00 57.55 C
ANISOU 14 CA PRO A 2 7400 7663 6801 78 -262 -124 C
ATOM 15 C PRO A 2 -27.609 17.010 4.240 1.00 55.47 C
ANISOU 15 C PRO A 2 7155 7405 6514 67 -243 -126 C
ATOM 16 O PRO A 2 -27.211 15.908 4.476 1.00 54.91 O
ANISOU 16 O PRO A 2 7085 7335 6443 63 -216 -110 O
ATOM 17 CB PRO A 2 -27.001 18.679 6.023 1.00 58.08 C
ANISOU 17 CB PRO A 2 7433 7765 6871 90 -291 -138 C
ATOM 18 CG PRO A 2 -26.573 20.095 5.997 1.00 59.85 C
ANISOU 18 CG PRO A 2 7647 7981 7112 100 -320 -144 C
ATOM 19 CD PRO A 2 -27.004 20.587 4.646 1.00 59.65 C
ANISOU 19 CD PRO A 2 7651 7933 7079 90 -324 -151 C
ATOM 20 N ILE A 3 -28.792 17.248 3.707 1.00 54.71 N
ANISOU 20 N ILE A 3 7074 7314 6400 61 -259 -145 N
ATOM 21 CA ILE A 3 -29.669 16.189 3.279 1.00 54.39 C
ANISOU 21 CA ILE A 3 7053 7274 6338 50 -244 -147 C
ATOM 22 C ILE A 3 -29.096 15.317 2.154 1.00 53.07 C
ANISOU 22 C ILE A 3 6917 7075 6171 41 -207 -125 C
ATOM 23 O ILE A 3 -29.506 14.208 2.011 1.00 53.01 O
ANISOU 23 O ILE A 3 6922 7069 6149 34 -189 -119 O
ATOM 24 CB ILE A 3 -31.046 16.728 2.869 1.00 55.96 C
ANISOU 24 CB ILE A 3 7262 7481 6519 46 -270 -172 C
ATOM 25 CG1 ILE A 3 -32.041 15.587 2.740 1.00 56.93 C
ANISOU 25 CG1 ILE A 3 7397 7613 6620 37 -258 -175 C
ATOM 26 CG2 ILE A 3 -30.939 17.451 1.551 1.00 57.75 C
ANISOU 26 CG2 ILE A 3 7518 7675 6750 41 -274 -174 C
ATOM 27 CD1 ILE A 3 -33.479 15.963 2.890 1.00 59.22 C
ANISOU 27 CD1 ILE A 3 7684 7923 6893 36 -287 -202 C
ATOM 28 N MET A 4 -28.152 15.802 1.372 1.00 51.56 N
ANISOU 28 N MET A 4 6740 6855 5995 41 -197 -112 N
ATOM 29 CA MET A 4 -27.600 14.968 0.331 1.00 50.29 C
ANISOU 29 CA MET A 4 6609 6665 5834 34 -162 -92 C
ATOM 30 C MET A 4 -26.631 13.930 0.870 1.00 47.73 C
ANISOU 30 C MET A 4 6274 6342 5520 36 -133 -70 C
ATOM 31 O MET A 4 -26.793 12.763 0.614 1.00 47.67 O
ANISOU 31 O MET A 4 6281 6331 5500 30 -110 -61 O
ATOM 32 CB MET A 4 -26.932 15.831 -0.701 1.00 51.69 C
ANISOU 32 CB MET A 4 6805 6812 6024 33 -160 -87 C
ATOM 33 CG MET A 4 -27.916 16.625 -1.510 1.00 54.38 C
ANISOU 33 CG MET A 4 7166 7143 6351 28 -184 -106 C
ATOM 34 SD MET A 4 -27.016 17.706 -2.584 1.00 63.16 S
ANISOU 34 SD MET A 4 8296 8222 7479 26 -184 -98 S
ATOM 35 CE MET A 4 -26.584 16.578 -3.886 1.00 64.60 C
ANISOU 35 CE MET A 4 8518 8371 7655 17 -139 -77 C
ATOM 36 N GLY A 5 -25.655 14.340 1.651 1.00 45.43 N
ANISOU 36 N GLY A 5 5957 6056 5250 44 -135 -63 N
ATOM 37 CA GLY A 5 -24.752 13.383 2.229 1.00 43.48 C
ANISOU 37 CA GLY A 5 5698 5810 5013 46 -110 -44 C
ATOM 38 C GLY A 5 -25.498 12.549 3.252 1.00 41.76 C
ANISOU 38 C GLY A 5 5464 5622 4780 45 -115 -51 C
ATOM 39 O GLY A 5 -25.314 11.369 3.349 1.00 41.71 O
ANISOU 39 O GLY A 5 5463 5616 4769 40 -92 -39 O
ATOM 40 N SER A 6 -26.367 13.196 4.003 1.00 39.84 N
ANISOU 40 N SER A 6 5202 5406 4529 49 -146 -71 N
ATOM 41 CA ASER A 6 -27.269 12.416 4.897 0.54 38.59 C
ANISOU 41 CA ASER A 6 5031 5279 4352 46 -152 -80 C
ATOM 42 CA BSER A 6 -27.217 12.399 4.906 0.46 38.74 C
ANISOU 42 CA BSER A 6 5050 5297 4372 46 -151 -79 C
ATOM 43 C SER A 6 -28.198 11.255 4.310 1.00 37.54 C
ANISOU 43 C SER A 6 4921 5146 4195 34 -137 -79 C
ATOM 44 O SER A 6 -28.381 10.039 4.635 1.00 37.04 O
ANISOU 44 O SER A 6 4860 5093 4122 29 -122 -71 O
ATOM 45 CB ASER A 6 -28.212 13.302 5.705 0.54 39.55 C
ANISOU 45 CB ASER A 6 5130 5430 4466 52 -188 -105 C
ATOM 46 CB BSER A 6 -27.946 13.295 5.908 0.46 40.15 C
ANISOU 46 CB BSER A 6 5201 5507 4547 54 -186 -101 C
ATOM 47 OG ASER A 6 -27.523 13.948 6.737 0.54 40.94 O
ANISOU 47 OG ASER A 6 5277 5618 4660 64 -202 -105 O
ATOM 48 OG BSER A 6 -29.271 13.509 5.520 0.46 43.28 O
ANISOU 48 OG BSER A 6 5609 5914 4923 49 -204 -121 O
ATOM 49 N SER A 7 -28.480 11.542 3.027 1.00 36.50 N
ANISOU 49 N SER A 7 4820 4991 4059 30 -134 -81 N
ATOM 50 CA ASER A 7 -29.285 10.641 2.160 0.71 36.09 C
ANISOU 50 CA ASER A 7 4798 4929 3986 20 -122 -80 C
ATOM 51 CA BSER A 7 -29.315 10.619 2.224 0.29 35.85 C
ANISOU 51 CA BSER A 7 4766 4900 3955 20 -123 -80 C
ATOM 52 C SER A 7 -28.618 9.245 1.698 1.00 34.65 C
ANISOU 52 C SER A 7 4634 4729 3803 14 -86 -56 C
ATOM 53 O SER A 7 -28.998 8.061 1.835 1.00 34.36 O
ANISOU 53 O SER A 7 4602 4699 3752 8 -74 -49 O
ATOM 54 CB ASER A 7 -29.778 11.311 0.896 0.71 39.08 C
ANISOU 54 CB ASER A 7 5206 5284 4359 16 -129 -89 C
ATOM 55 CB BSER A 7 -30.063 11.283 1.078 0.29 37.83 C
ANISOU 55 CB BSER A 7 5044 5133 4197 16 -134 -93 C
ATOM 56 OG ASER A 7 -30.977 11.972 1.148 0.71 42.52 O
ANISOU 56 OG ASER A 7 5634 5739 4783 16 -160 -113 O
ATOM 57 OG BSER A 7 -29.176 11.552 0.024 0.29 40.07 O
ANISOU 57 OG BSER A 7 5350 5382 4492 15 -117 -80 O
ATOM 58 N VAL A 8 -27.328 9.433 1.490 1.00 32.75 N
ANISOU 58 N VAL A 8 4393 4468 3583 18 -69 -41 N
ATOM 59 CA VAL A 8 -26.454 8.364 1.096 1.00 32.05 C
ANISOU 59 CA VAL A 8 4318 4361 3499 16 -37 -19 C
ATOM 60 C VAL A 8 -26.234 7.489 2.349 1.00 30.82 C
ANISOU 60 C VAL A 8 4136 4229 3344 16 -33 -13 C
ATOM 61 O VAL A 8 -26.430 6.324 2.299 1.00 30.81 O
ANISOU 61 O VAL A 8 4145 4230 3332 10 -20 -4 O
ATOM 62 CB VAL A 8 -25.109 8.834 0.561 1.00 32.74 C
ANISOU 62 CB VAL A 8 4409 4420 3609 20 -19 -4 C
ATOM 63 CG1 VAL A 8 -24.159 7.683 0.425 1.00 32.73 C
ANISOU 63 CG1 VAL A 8 4415 4406 3615 19 13 17 C
ATOM 64 CG2 VAL A 8 -25.254 9.571 -0.752 1.00 33.68 C
ANISOU 64 CG2 VAL A 8 4558 4514 3726 18 -19 -8 C
ATOM 65 N TYR A 9 -25.835 8.111 3.450 1.00 28.88 N
ANISOU 65 N TYR A 9 3860 4001 3113 23 -48 -17 N
ATOM 66 CA TYR A 9 -25.644 7.432 4.721 1.00 26.61 C
ANISOU 66 CA TYR A 9 3546 3737 2827 23 -49 -14 C
ATOM 67 C TYR A 9 -26.917 6.687 5.109 1.00 25.37 C
ANISOU 67 C TYR A 9 3389 3606 2645 16 -58 -23 C
ATOM 68 O TYR A 9 -26.875 5.551 5.344 1.00 24.95 O
ANISOU 68 O TYR A 9 3338 3556 2584 10 -45 -13 O
ATOM 69 CB TYR A 9 -25.203 8.416 5.822 1.00 25.93 C
ANISOU 69 CB TYR A 9 3427 3666 2759 34 -69 -21 C
ATOM 70 CG TYR A 9 -25.319 7.864 7.239 1.00 24.58 C
ANISOU 70 CG TYR A 9 3230 3524 2585 34 -76 -23 C
ATOM 71 CD1 TYR A 9 -24.538 6.809 7.647 1.00 23.96 C
ANISOU 71 CD1 TYR A 9 3148 3441 2514 31 -57 -7 C
ATOM 72 CD2 TYR A 9 -26.223 8.385 8.136 1.00 24.51 C
ANISOU 72 CD2 TYR A 9 3200 3547 2566 37 -104 -41 C
ATOM 73 CE1 TYR A 9 -24.644 6.296 8.912 1.00 23.69 C
ANISOU 73 CE1 TYR A 9 3092 3433 2478 30 -64 -8 C
ATOM 74 CE2 TYR A 9 -26.338 7.868 9.391 1.00 24.19 C
ANISOU 74 CE2 TYR A 9 3138 3533 2522 37 -110 -43 C
ATOM 75 CZ TYR A 9 -25.545 6.819 9.768 1.00 25.13 C
ANISOU 75 CZ TYR A 9 3255 3645 2648 32 -90 -26 C
ATOM 76 OH TYR A 9 -25.655 6.297 11.015 1.00 25.11 O
ANISOU 76 OH TYR A 9 3232 3668 2642 31 -97 -27 O
ATOM 77 N ILE A 10 -28.042 7.363 5.118 1.00 25.21 N
ANISOU 77 N ILE A 10 3367 3601 2611 16 -82 -43 N
ATOM 78 CA ILE A 10 -29.302 6.746 5.453 1.00 26.62 C
ANISOU 78 CA ILE A 10 3545 3804 2766 9 -92 -52 C
ATOM 79 C ILE A 10 -29.648 5.568 4.557 1.00 26.86 C
ANISOU 79 C ILE A 10 3605 3819 2781 0 -73 -41 C
ATOM 80 O ILE A 10 -30.046 4.558 5.027 1.00 27.02 O
ANISOU 80 O ILE A 10 3622 3856 2789 -7 -70 -36 O
ATOM 81 CB ILE A 10 -30.469 7.751 5.532 1.00 28.75 C
ANISOU 81 CB ILE A 10 3807 4091 3024 11 -121 -77 C
ATOM 82 CG1 ILE A 10 -30.321 8.631 6.756 1.00 30.76 C
ANISOU 82 CG1 ILE A 10 4028 4371 3289 21 -143 -89 C
ATOM 83 CG2 ILE A 10 -31.800 7.062 5.626 1.00 28.17 C
ANISOU 83 CG2 ILE A 10 3739 4038 2927 3 -128 -85 C
ATOM 84 CD1 ILE A 10 -31.040 9.926 6.683 1.00 33.13 C
ANISOU 84 CD1 ILE A 10 4321 4679 3586 27 -171 -111 C
ATOM 85 N THR A 11 -29.465 5.726 3.253 1.00 27.03 N
ANISOU 85 N THR A 11 3656 3809 2804 -1 -61 -36 N
ATOM 86 CA THR A 11 -29.764 4.683 2.304 1.00 28.23 C
ANISOU 86 CA THR A 11 3839 3943 2942 -9 -44 -25 C
ATOM 87 C THR A 11 -28.938 3.449 2.585 1.00 27.84 C
ANISOU 87 C THR A 11 3790 3891 2897 -11 -22 -5 C
ATOM 88 O THR A 11 -29.458 2.397 2.637 1.00 28.76 O
ANISOU 88 O THR A 11 3913 4014 2998 -18 -18 1 O
ATOM 89 CB THR A 11 -29.604 5.138 0.844 1.00 30.34 C
ANISOU 89 CB THR A 11 4140 4175 3211 -8 -35 -23 C
ATOM 90 OG1 THR A 11 -30.446 6.247 0.601 1.00 32.52 O
ANISOU 90 OG1 THR A 11 4418 4455 3484 -7 -59 -43 O
ATOM 91 CG2 THR A 11 -30.013 4.053 -0.054 1.00 31.51 C
ANISOU 91 CG2 THR A 11 4321 4307 3345 -14 -20 -12 C
ATOM 92 N VAL A 12 -27.648 3.627 2.768 1.00 26.74 N
ANISOU 92 N VAL A 12 3642 3740 2780 -6 -8 6 N
ATOM 93 CA VAL A 12 -26.744 2.569 3.101 1.00 26.30 C
ANISOU 93 CA VAL A 12 3582 3680 2731 -7 12 24 C
ATOM 94 C VAL A 12 -27.138 1.869 4.419 1.00 26.05 C
ANISOU 94 C VAL A 12 3526 3681 2692 -12 1 22 C
ATOM 95 O VAL A 12 -27.117 0.686 4.485 1.00 27.10 O
ANISOU 95 O VAL A 12 3666 3815 2817 -18 11 32 O
ATOM 96 CB VAL A 12 -25.293 3.052 3.126 1.00 27.23 C
ANISOU 96 CB VAL A 12 3691 3779 2876 0 26 33 C
ATOM 97 CG1 VAL A 12 -24.383 1.993 3.691 1.00 26.89 C
ANISOU 97 CG1 VAL A 12 3639 3735 2843 -2 42 49 C
ATOM 98 CG2 VAL A 12 -24.831 3.472 1.742 1.00 29.50 C
ANISOU 98 CG2 VAL A 12 4006 4033 3170 2 42 39 C
ATOM 99 N GLU A 13 -27.512 2.629 5.430 1.00 23.69 N
ANISOU 99 N GLU A 13 3199 3408 2394 -9 -21 7 N
ATOM 100 CA GLU A 13 -27.935 2.074 6.701 1.00 22.69 C
ANISOU 100 CA GLU A 13 3048 3313 2258 -13 -32 4 C
ATOM 101 C GLU A 13 -29.167 1.211 6.500 1.00 23.44 C
ANISOU 101 C GLU A 13 3157 3423 2327 -23 -37 2 C
ATOM 102 O GLU A 13 -29.228 0.130 6.967 1.00 23.25 O
ANISOU 102 O GLU A 13 3129 3409 2294 -30 -32 11 O
ATOM 103 CB GLU A 13 -28.180 3.163 7.738 1.00 22.90 C
ANISOU 103 CB GLU A 13 3045 3366 2290 -6 -55 -13 C
ATOM 104 CG GLU A 13 -26.932 3.834 8.255 1.00 25.43 C
ANISOU 104 CG GLU A 13 3348 3678 2638 3 -53 -8 C
ATOM 105 CD GLU A 13 -26.300 3.119 9.425 1.00 28.52 C
ANISOU 105 CD GLU A 13 3719 4081 3036 1 -50 0 C
ATOM 106 OE1 GLU A 13 -26.126 3.744 10.453 1.00 29.80 O
ANISOU 106 OE1 GLU A 13 3856 4260 3208 8 -65 -8 O
ATOM 107 OE2 GLU A 13 -25.991 1.952 9.302 1.00 28.09 O
ANISOU 107 OE2 GLU A 13 3675 4020 2979 -6 -34 14 O
ATOM 108 N LEU A 14 -30.130 1.713 5.762 1.00 24.34 N
ANISOU 108 N LEU A 14 3285 3533 2428 -23 -47 -10 N
ATOM 109 CA LEU A 14 -31.334 0.974 5.459 1.00 26.20 C
ANISOU 109 CA LEU A 14 3536 3779 2642 -32 -52 -12 C
ATOM 110 C LEU A 14 -31.074 -0.359 4.731 1.00 26.11 C
ANISOU 110 C LEU A 14 3551 3747 2624 -38 -32 8 C
ATOM 111 O LEU A 14 -31.660 -1.330 5.044 1.00 26.04 O
ANISOU 111 O LEU A 14 3541 3752 2599 -47 -35 13 O
ATOM 112 CB LEU A 14 -32.314 1.858 4.712 1.00 28.51 C
ANISOU 112 CB LEU A 14 3840 4066 2925 -30 -67 -28 C
ATOM 113 CG LEU A 14 -32.910 2.971 5.552 1.00 31.38 C
ANISOU 113 CG LEU A 14 4176 4458 3289 -26 -92 -50 C
ATOM 114 CD1 LEU A 14 -33.917 3.789 4.781 1.00 33.73 C
ANISOU 114 CD1 LEU A 14 4488 4749 3578 -25 -107 -67 C
ATOM 115 CD2 LEU A 14 -33.497 2.377 6.792 1.00 32.13 C
ANISOU 115 CD2 LEU A 14 4246 4589 3371 -31 -101 -53 C
ATOM 116 N ALA A 15 -30.173 -0.355 3.773 1.00 25.14 N
ANISOU 116 N ALA A 15 3448 3590 2512 -34 -13 19 N
ATOM 117 CA ALA A 15 -29.795 -1.534 3.045 1.00 25.97 C
ANISOU 117 CA ALA A 15 3580 3675 2614 -38 6 37 C
ATOM 118 C ALA A 15 -29.186 -2.577 3.989 1.00 24.62 C
ANISOU 118 C ALA A 15 3392 3517 2446 -43 12 49 C
ATOM 119 O ALA A 15 -29.497 -3.727 3.905 1.00 25.27 O
ANISOU 119 O ALA A 15 3485 3601 2514 -50 15 59 O
ATOM 120 CB ALA A 15 -28.824 -1.177 1.955 1.00 25.85 C
ANISOU 120 CB ALA A 15 3586 3624 2613 -31 26 45 C
ATOM 121 N ILE A 16 -28.303 -2.119 4.861 1.00 22.92 N
ANISOU 121 N ILE A 16 3151 3310 2249 -38 13 48 N
ATOM 122 CA ILE A 16 -27.672 -2.949 5.887 1.00 22.96 C
ANISOU 122 CA ILE A 16 3137 3327 2260 -43 16 57 C
ATOM 123 C ILE A 16 -28.736 -3.572 6.808 1.00 23.58 C
ANISOU 123 C ILE A 16 3201 3440 2317 -52 -1 52 C
ATOM 124 O ILE A 16 -28.713 -4.739 7.025 1.00 23.61 O
ANISOU 124 O ILE A 16 3209 3448 2313 -60 2 63 O
ATOM 125 CB ILE A 16 -26.560 -2.201 6.667 1.00 22.93 C
ANISOU 125 CB ILE A 16 3108 3323 2281 -35 18 56 C
ATOM 126 CG1 ILE A 16 -25.393 -1.959 5.732 1.00 25.10 C
ANISOU 126 CG1 ILE A 16 3398 3562 2575 -28 40 66 C
ATOM 127 CG2 ILE A 16 -26.080 -2.997 7.873 1.00 21.68 C
ANISOU 127 CG2 ILE A 16 2929 3182 2127 -40 16 62 C
ATOM 128 CD1 ILE A 16 -24.483 -0.868 6.142 1.00 27.17 C
ANISOU 128 CD1 ILE A 16 3641 3819 2863 -19 39 62 C
ATOM 129 N ALA A 17 -29.669 -2.762 7.286 1.00 23.36 N
ANISOU 129 N ALA A 17 3159 3436 2282 -51 -20 36 N
ATOM 130 CA ALA A 17 -30.748 -3.220 8.121 1.00 23.62 C
ANISOU 130 CA ALA A 17 3178 3503 2295 -60 -37 30 C
ATOM 131 C ALA A 17 -31.520 -4.368 7.459 1.00 25.14 C
ANISOU 131 C ALA A 17 3394 3692 2467 -70 -35 39 C
ATOM 132 O ALA A 17 -31.746 -5.358 8.055 1.00 25.96 O
ANISOU 132 O ALA A 17 3492 3812 2560 -79 -38 47 O
ATOM 133 CB ALA A 17 -31.660 -2.096 8.470 1.00 23.13 C
ANISOU 133 CB ALA A 17 3099 3462 2226 -56 -56 9 C
ATOM 134 N VAL A 18 -31.894 -4.203 6.206 1.00 25.73 N
ANISOU 134 N VAL A 18 3496 3743 2537 -67 -31 39 N
ATOM 135 CA VAL A 18 -32.611 -5.231 5.489 1.00 27.23 C
ANISOU 135 CA VAL A 18 3711 3926 2709 -74 -30 49 C
ATOM 136 C VAL A 18 -31.844 -6.536 5.475 1.00 26.17 C
ANISOU 136 C VAL A 18 3586 3781 2576 -79 -16 68 C
ATOM 137 O VAL A 18 -32.360 -7.541 5.821 1.00 26.48 O
ANISOU 137 O VAL A 18 3625 3834 2600 -88 -23 76 O
ATOM 138 CB VAL A 18 -32.952 -4.784 4.054 1.00 29.64 C
ANISOU 138 CB VAL A 18 4049 4201 3013 -69 -25 46 C
ATOM 139 CG1 VAL A 18 -33.507 -5.934 3.249 1.00 31.21 C
ANISOU 139 CG1 VAL A 18 4277 4387 3196 -74 -23 59 C
ATOM 140 CG2 VAL A 18 -33.943 -3.658 4.106 1.00 31.31 C
ANISOU 140 CG2 VAL A 18 4252 4426 3219 -66 -43 26 C
ATOM 141 N LEU A 19 -30.594 -6.464 5.089 1.00 25.07 N
ANISOU 141 N LEU A 19 3455 3617 2455 -72 2 76 N
ATOM 142 CA LEU A 19 -29.735 -7.604 4.997 1.00 25.45 C
ANISOU 142 CA LEU A 19 3511 3651 2507 -75 15 94 C
ATOM 143 C LEU A 19 -29.471 -8.277 6.349 1.00 25.18 C
ANISOU 143 C LEU A 19 3451 3642 2474 -84 8 97 C
ATOM 144 O LEU A 19 -29.429 -9.461 6.423 1.00 25.95 O
ANISOU 144 O LEU A 19 3557 3741 2563 -91 8 109 O
ATOM 145 CB LEU A 19 -28.440 -7.247 4.307 1.00 25.28 C
ANISOU 145 CB LEU A 19 3500 3597 2506 -66 36 100 C
ATOM 146 CG LEU A 19 -28.529 -6.907 2.828 1.00 27.31 C
ANISOU 146 CG LEU A 19 3790 3823 2762 -59 48 101 C
ATOM 147 CD1 LEU A 19 -27.216 -6.397 2.318 1.00 27.61 C
ANISOU 147 CD1 LEU A 19 3833 3834 2822 -49 69 105 C
ATOM 148 CD2 LEU A 19 -29.049 -8.070 2.034 1.00 28.64 C
ANISOU 148 CD2 LEU A 19 3988 3981 2913 -63 49 113 C
ATOM 149 N ALA A 20 -29.334 -7.491 7.396 1.00 24.66 N
ANISOU 149 N ALA A 20 3356 3598 2417 -82 0 86 N
ATOM 150 CA ALA A 20 -29.089 -8.020 8.731 1.00 24.71 C
ANISOU 150 CA ALA A 20 3337 3628 2424 -90 -8 88 C
ATOM 151 C ALA A 20 -30.292 -8.821 9.203 1.00 26.09 C
ANISOU 151 C ALA A 20 3510 3831 2574 -103 -25 89 C
ATOM 152 O ALA A 20 -30.147 -9.883 9.704 1.00 26.14 O
ANISOU 152 O ALA A 20 3513 3845 2574 -112 -27 99 O
ATOM 153 CB ALA A 20 -28.777 -6.906 9.680 1.00 23.91 C
ANISOU 153 CB ALA A 20 3207 3541 2336 -84 -15 75 C
ATOM 154 N ILE A 21 -31.477 -8.282 8.994 1.00 26.14 N
ANISOU 154 N ILE A 21 3516 3851 2565 -103 -36 78 N
ATOM 155 CA ILE A 21 -32.715 -8.922 9.359 1.00 27.92 C
ANISOU 155 CA ILE A 21 3739 4103 2768 -114 -51 78 C
ATOM 156 C ILE A 21 -32.921 -10.239 8.603 1.00 29.77 C
ANISOU 156 C ILE A 21 3999 4322 2989 -121 -48 95 C
ATOM 157 O ILE A 21 -33.101 -11.253 9.186 1.00 30.80 O
ANISOU 157 O ILE A 21 4125 4469 3110 -133 -55 104 O
ATOM 158 CB ILE A 21 -33.908 -7.979 9.178 1.00 29.78 C
ANISOU 158 CB ILE A 21 3971 4353 2993 -111 -64 61 C
ATOM 159 CG1 ILE A 21 -33.841 -6.876 10.196 1.00 30.00 C
ANISOU 159 CG1 ILE A 21 3967 4403 3029 -106 -72 44 C
ATOM 160 CG2 ILE A 21 -35.219 -8.708 9.307 1.00 32.19 C
ANISOU 160 CG2 ILE A 21 4277 4679 3274 -122 -78 63 C
ATOM 161 CD1 ILE A 21 -34.678 -5.679 9.893 1.00 32.31 C
ANISOU 161 CD1 ILE A 21 4256 4702 3318 -98 -82 26 C
ATOM 162 N LEU A 22 -32.838 -10.190 7.291 1.00 29.57 N
ANISOU 162 N LEU A 22 4004 4266 2966 -114 -38 99 N
ATOM 163 CA LEU A 22 -33.024 -11.343 6.452 1.00 30.23 C
ANISOU 163 CA LEU A 22 4116 4332 3039 -118 -36 115 C
ATOM 164 C LEU A 22 -32.094 -12.496 6.764 1.00 29.26 C
ANISOU 164 C LEU A 22 3994 4203 2920 -123 -29 130 C
ATOM 165 O LEU A 22 -32.523 -13.566 6.976 1.00 29.59 O
ANISOU 165 O LEU A 22 4040 4255 2948 -134 -39 141 O
ATOM 166 CB LEU A 22 -32.883 -10.947 4.986 1.00 31.87 C
ANISOU 166 CB LEU A 22 4355 4504 3252 -107 -23 116 C
ATOM 167 CG LEU A 22 -33.998 -10.112 4.383 1.00 35.59 C
ANISOU 167 CG LEU A 22 4834 4973 3713 -104 -32 103 C
ATOM 168 CD1 LEU A 22 -33.692 -9.732 2.961 1.00 36.88 C
ANISOU 168 CD1 LEU A 22 5031 5099 3883 -93 -18 105 C
ATOM 169 CD2 LEU A 22 -35.298 -10.853 4.447 1.00 37.05 C
ANISOU 169 CD2 LEU A 22 5025 5175 3878 -113 -49 106 C
ATOM 170 N GLY A 23 -30.810 -12.245 6.767 1.00 27.78 N
ANISOU 170 N GLY A 23 3803 3998 2753 -116 -14 132 N
ATOM 171 CA GLY A 23 -29.860 -13.273 7.007 1.00 27.48 C
ANISOU 171 CA GLY A 23 3767 3951 2722 -121 -8 145 C
ATOM 172 C GLY A 23 -29.989 -13.869 8.381 1.00 27.06 C
ANISOU 172 C GLY A 23 3690 3930 2663 -134 -23 146 C
ATOM 173 O GLY A 23 -29.919 -15.042 8.538 1.00 28.07 O
ANISOU 173 O GLY A 23 3823 4059 2783 -143 -28 158 O
ATOM 174 N ASN A 24 -30.200 -13.027 9.370 1.00 25.81 N
ANISOU 174 N ASN A 24 3503 3795 2508 -135 -30 133 N
ATOM 175 CA ASN A 24 -30.299 -13.515 10.721 1.00 26.44 C
ANISOU 175 CA ASN A 24 3559 3905 2582 -147 -44 133 C
ATOM 176 C ASN A 24 -31.606 -14.223 11.047 1.00 29.16 C
ANISOU 176 C ASN A 24 3902 4277 2900 -161 -62 136 C
ATOM 177 O ASN A 24 -31.599 -15.141 11.787 1.00 30.71 O
ANISOU 177 O ASN A 24 4091 4489 3089 -174 -71 144 O
ATOM 178 CB ASN A 24 -29.848 -12.475 11.710 1.00 24.42 C
ANISOU 178 CB ASN A 24 3275 3663 2341 -143 -44 120 C
ATOM 179 CG ASN A 24 -28.365 -12.236 11.613 1.00 24.22 C
ANISOU 179 CG ASN A 24 3250 3610 2343 -134 -28 123 C
ATOM 180 OD1 ASN A 24 -27.580 -13.035 12.014 1.00 23.96 O
ANISOU 180 OD1 ASN A 24 3216 3572 2318 -140 -27 131 O
ATOM 181 ND2 ASN A 24 -28.009 -11.177 10.998 1.00 22.75 N
ANISOU 181 ND2 ASN A 24 3067 3406 2170 -120 -17 116 N
ATOM 182 N VAL A 25 -32.699 -13.812 10.439 1.00 29.60 N
ANISOU 182 N VAL A 25 3966 4337 2943 -158 -67 131 N
ATOM 183 CA VAL A 25 -33.960 -14.501 10.607 1.00 32.02 C
ANISOU 183 CA VAL A 25 4274 4667 3226 -171 -83 135 C
ATOM 184 C VAL A 25 -33.783 -15.922 10.046 1.00 33.31 C
ANISOU 184 C VAL A 25 4461 4814 3382 -177 -84 155 C
ATOM 185 O VAL A 25 -34.234 -16.862 10.603 1.00 34.43 O
ANISOU 185 O VAL A 25 4598 4974 3509 -191 -98 163 O
ATOM 186 CB VAL A 25 -35.094 -13.761 9.912 1.00 32.62 C
ANISOU 186 CB VAL A 25 4358 4744 3293 -165 -87 125 C
ATOM 187 CG1 VAL A 25 -36.252 -14.673 9.603 1.00 34.38 C
ANISOU 187 CG1 VAL A 25 4594 4976 3494 -175 -101 135 C
ATOM 188 CG2 VAL A 25 -35.512 -12.558 10.709 1.00 32.58 C
ANISOU 188 CG2 VAL A 25 4325 4765 3290 -162 -93 106 C
ATOM 189 N LEU A 26 -33.063 -16.032 8.949 1.00 32.95 N
ANISOU 189 N LEU A 26 4441 4732 3347 -167 -70 161 N
ATOM 190 CA LEU A 26 -32.775 -17.292 8.337 1.00 33.79 C
ANISOU 190 CA LEU A 26 4571 4820 3448 -170 -70 179 C
ATOM 191 C LEU A 26 -31.928 -18.183 9.246 1.00 33.18 C
ANISOU 191 C LEU A 26 4481 4750 3376 -181 -74 187 C
ATOM 192 O LEU A 26 -32.141 -19.347 9.312 1.00 34.61 O
ANISOU 192 O LEU A 26 4670 4934 3544 -191 -86 199 O
ATOM 193 CB LEU A 26 -32.099 -17.076 7.011 1.00 35.06 C
ANISOU 193 CB LEU A 26 4759 4941 3620 -155 -52 182 C
ATOM 194 CG LEU A 26 -31.930 -18.265 6.074 1.00 39.27 C
ANISOU 194 CG LEU A 26 5324 5450 4148 -155 -52 199 C
ATOM 195 CD1 LEU A 26 -33.238 -18.897 5.636 1.00 40.97 C
ANISOU 195 CD1 LEU A 26 5556 5672 4340 -161 -69 206 C
ATOM 196 CD2 LEU A 26 -31.035 -17.928 4.906 1.00 40.26 C
ANISOU 196 CD2 LEU A 26 5473 5538 4287 -139 -30 200 C
ATOM 197 N VAL A 27 -30.953 -17.622 9.928 1.00 31.64 N
ANISOU 197 N VAL A 27 4267 4555 3199 -177 -65 179 N
ATOM 198 CA VAL A 27 -30.177 -18.394 10.864 1.00 31.53 C
ANISOU 198 CA VAL A 27 4241 4549 3192 -188 -70 185 C
ATOM 199 C VAL A 27 -31.113 -18.950 11.949 1.00 33.00 C
ANISOU 199 C VAL A 27 4409 4771 3357 -206 -92 186 C
ATOM 200 O VAL A 27 -31.071 -20.094 12.214 1.00 34.36 O
ANISOU 200 O VAL A 27 4586 4947 3520 -218 -103 198 O
ATOM 201 CB VAL A 27 -29.050 -17.573 11.528 1.00 30.31 C
ANISOU 201 CB VAL A 27 4067 4389 3062 -181 -59 175 C
ATOM 202 CG1 VAL A 27 -28.540 -18.260 12.766 1.00 29.96 C
ANISOU 202 CG1 VAL A 27 4004 4359 3020 -195 -69 178 C
ATOM 203 CG2 VAL A 27 -27.922 -17.332 10.579 1.00 29.99 C
ANISOU 203 CG2 VAL A 27 4042 4311 3042 -167 -38 177 C
ATOM 204 N CYS A 28 -31.956 -18.104 12.530 1.00 33.03 N
ANISOU 204 N CYS A 28 4395 4803 3354 -207 -98 174 N
ATOM 205 CA CYS A 28 -32.895 -18.447 13.590 1.00 34.13 C
ANISOU 205 CA CYS A 28 4514 4980 3474 -223 -116 174 C
ATOM 206 C CYS A 28 -33.854 -19.507 13.126 1.00 36.26 C
ANISOU 206 C CYS A 28 4800 5256 3722 -233 -130 187 C
ATOM 207 O CYS A 28 -34.140 -20.436 13.824 1.00 36.53 O
ANISOU 207 O CYS A 28 4827 5309 3742 -250 -145 196 O
ATOM 208 CB CYS A 28 -33.641 -17.242 14.087 1.00 33.70 C
ANISOU 208 CB CYS A 28 4439 4951 3416 -219 -118 157 C
ATOM 209 SG CYS A 28 -32.616 -16.085 14.966 1.00 34.73 S
ANISOU 209 SG CYS A 28 4544 5082 3569 -209 -108 142 S
ATOM 210 N TRP A 29 -34.327 -19.392 11.879 1.00 37.22 N
ANISOU 210 N TRP A 29 4945 5357 3840 -224 -125 190 N
ATOM 211 CA ATRP A 29 -35.231 -20.390 11.264 0.48 39.64 C
ANISOU 211 CA ATRP A 29 5271 5662 4127 -231 -139 204 C
ATOM 212 CA BTRP A 29 -35.228 -20.379 11.248 0.52 39.28 C
ANISOU 212 CA BTRP A 29 5226 5616 4081 -231 -139 204 C
ATOM 213 C TRP A 29 -34.701 -21.873 10.987 1.00 39.97 C
ANISOU 213 C TRP A 29 5333 5689 4166 -239 -146 224 C
ATOM 214 O TRP A 29 -35.160 -23.044 11.247 1.00 40.84 O
ANISOU 214 O TRP A 29 5447 5811 4260 -253 -165 238 O
ATOM 215 CB ATRP A 29 -35.832 -19.832 9.972 0.48 40.86 C
ANISOU 215 CB ATRP A 29 5449 5796 4281 -217 -132 202 C
ATOM 216 CB BTRP A 29 -35.735 -19.757 9.944 0.52 39.93 C
ANISOU 216 CB BTRP A 29 5331 5676 4164 -216 -130 201 C
ATOM 217 CG ATRP A 29 -37.194 -19.237 10.137 0.48 43.38 C
ANISOU 217 CG ATRP A 29 5757 6139 4586 -220 -142 192 C
ATOM 218 CG BTRP A 29 -36.971 -20.338 9.348 0.52 42.01 C
ANISOU 218 CG BTRP A 29 5610 5942 4409 -221 -145 210 C
ATOM 219 CD1ATRP A 29 -37.552 -17.942 9.913 0.48 44.47 C
ANISOU 219 CD1ATRP A 29 5889 6278 4730 -209 -134 175 C
ATOM 220 CD1BTRP A 29 -37.623 -21.464 9.734 0.52 43.88 C
ANISOU 220 CD1BTRP A 29 5847 6197 4629 -236 -164 224 C
ATOM 221 CD2ATRP A 29 -38.383 -19.913 10.562 0.48 45.33 C
ANISOU 221 CD2ATRP A 29 5997 6414 4813 -235 -162 200 C
ATOM 222 CD2BTRP A 29 -37.693 -19.821 8.225 0.52 42.90 C
ANISOU 222 CD2BTRP A 29 5743 6036 4519 -210 -142 207 C
ATOM 223 NE1ATRP A 29 -38.885 -17.767 10.169 0.48 46.01 N
ANISOU 223 NE1ATRP A 29 6073 6498 4910 -216 -148 170 N
ATOM 224 NE1BTRP A 29 -38.711 -21.681 8.926 0.52 45.16 N
ANISOU 224 NE1BTRP A 29 6028 6354 4778 -235 -174 230 N
ATOM 225 CE2ATRP A 29 -39.420 -18.961 10.576 0.48 46.93 C
ANISOU 225 CE2ATRP A 29 6189 6632 5009 -232 -164 185 C
ATOM 226 CE2BTRP A 29 -38.776 -20.684 7.992 0.52 44.66 C
ANISOU 226 CE2BTRP A 29 5978 6268 4724 -219 -160 219 C
ATOM 227 CE3ATRP A 29 -38.671 -21.227 10.937 0.48 46.85 C
ANISOU 227 CE3ATRP A 29 6192 6619 4991 -251 -178 217 C
ATOM 228 CE3BTRP A 29 -37.530 -18.704 7.398 0.52 43.26 C
ANISOU 228 CE3BTRP A 29 5800 6060 4576 -194 -127 194 C
ATOM 229 CZ2ATRP A 29 -40.723 -19.284 10.945 0.48 49.12 C
ANISOU 229 CZ2ATRP A 29 6457 6937 5269 -244 -181 188 C
ATOM 230 CZ2BTRP A 29 -39.693 -20.471 6.971 0.52 46.01 C
ANISOU 230 CZ2BTRP A 29 6171 6423 4889 -212 -164 219 C
ATOM 231 CZ3ATRP A 29 -39.963 -21.543 11.305 0.48 49.23 C
ANISOU 231 CZ3ATRP A 29 6484 6949 5274 -263 -195 220 C
ATOM 232 CZ3BTRP A 29 -38.441 -18.495 6.383 0.52 44.82 C
ANISOU 232 CZ3BTRP A 29 6020 6243 4767 -187 -130 194 C
ATOM 233 CH2ATRP A 29 -40.972 -20.578 11.306 0.48 49.98 C
ANISOU 233 CH2ATRP A 29 6568 7059 5364 -259 -196 206 C
ATOM 234 CH2BTRP A 29 -39.509 -19.374 6.179 0.52 45.92 C
ANISOU 234 CH2BTRP A 29 6170 6389 4889 -196 -149 206 C
ATOM 235 N ALA A 30 -33.421 -21.849 10.672 1.00 39.28 N
ANISOU 235 N ALA A 30 5253 5574 4097 -229 -132 224 N
ATOM 236 CA ALA A 30 -32.627 -23.012 10.399 1.00 39.89 C
ANISOU 236 CA ALA A 30 5347 5632 4176 -232 -135 238 C
ATOM 237 C ALA A 30 -32.425 -23.763 11.703 1.00 41.07 C
ANISOU 237 C ALA A 30 5477 5807 4322 -251 -151 242 C
ATOM 238 O ALA A 30 -32.561 -24.947 11.738 1.00 41.45 O
ANISOU 238 O ALA A 30 5534 5857 4359 -263 -167 256 O
ATOM 239 CB ALA A 30 -31.303 -22.630 9.811 1.00 38.86 C
ANISOU 239 CB ALA A 30 5227 5470 4070 -217 -113 234 C
ATOM 240 N VAL A 31 -32.087 -23.042 12.764 1.00 40.59 N
ANISOU 240 N VAL A 31 5388 5763 4270 -254 -147 229 N
ATOM 241 CA VAL A 31 -31.888 -23.664 14.056 1.00 41.83 C
ANISOU 241 CA VAL A 31 5526 5943 4423 -273 -161 232 C
ATOM 242 C VAL A 31 -33.210 -24.202 14.574 1.00 45.21 C
ANISOU 242 C VAL A 31 5947 6405 4825 -290 -183 238 C
ATOM 243 O VAL A 31 -33.267 -25.289 15.039 1.00 45.33 O
ANISOU 243 O VAL A 31 5962 6430 4829 -306 -200 250 O
ATOM 244 CB VAL A 31 -31.226 -22.752 15.096 1.00 40.87 C
ANISOU 244 CB VAL A 31 5378 5832 4318 -271 -153 217 C
ATOM 245 CG1 VAL A 31 -31.116 -23.483 16.411 1.00 41.37 C
ANISOU 245 CG1 VAL A 31 5425 5919 4375 -291 -170 220 C
ATOM 246 CG2 VAL A 31 -29.839 -22.337 14.662 1.00 39.85 C
ANISOU 246 CG2 VAL A 31 5256 5670 4217 -256 -134 213 C
ATOM 247 N TRP A 32 -34.266 -23.435 14.441 1.00 47.42 N
ANISOU 247 N TRP A 32 6220 6702 5095 -286 -181 231 N
ATOM 248 CA TRP A 32 -35.555 -23.862 14.884 1.00 51.28 C
ANISOU 248 CA TRP A 32 6701 7222 5561 -301 -200 237 C
ATOM 249 C TRP A 32 -36.047 -25.115 14.146 1.00 53.09 C
ANISOU 249 C TRP A 32 6954 7442 5776 -308 -215 256 C
ATOM 250 O TRP A 32 -36.573 -26.007 14.745 1.00 54.14 O
ANISOU 250 O TRP A 32 7081 7597 5892 -326 -235 267 O
ATOM 251 CB TRP A 32 -36.558 -22.755 14.731 1.00 52.95 C
ANISOU 251 CB TRP A 32 6903 7449 5767 -293 -194 224 C
ATOM 252 CG TRP A 32 -37.941 -23.170 15.043 1.00 57.09 C
ANISOU 252 CG TRP A 32 7420 8004 6268 -307 -212 230 C
ATOM 253 CD1 TRP A 32 -38.750 -23.951 14.290 1.00 59.67 C
ANISOU 253 CD1 TRP A 32 7766 8326 6582 -311 -224 244 C
ATOM 254 CD2 TRP A 32 -38.688 -22.850 16.219 1.00 59.05 C
ANISOU 254 CD2 TRP A 32 7639 8293 6503 -319 -220 222 C
ATOM 255 NE1 TRP A 32 -39.945 -24.135 14.906 1.00 61.60 N
ANISOU 255 NE1 TRP A 32 7995 8605 6807 -325 -239 246 N
ATOM 256 CE2 TRP A 32 -39.935 -23.473 16.098 1.00 61.59 C
ANISOU 256 CE2 TRP A 32 7963 8633 6805 -330 -236 233 C
ATOM 257 CE3 TRP A 32 -38.419 -22.105 17.367 1.00 59.47 C
ANISOU 257 CE3 TRP A 32 7665 8370 6562 -321 -216 207 C
ATOM 258 CZ2 TRP A 32 -40.909 -23.359 17.073 1.00 63.44 C
ANISOU 258 CZ2 TRP A 32 8173 8909 7023 -344 -246 229 C
ATOM 259 CZ3 TRP A 32 -39.389 -21.984 18.314 1.00 61.66 C
ANISOU 259 CZ3 TRP A 32 7919 8688 6822 -333 -226 203 C
ATOM 260 CH2 TRP A 32 -40.616 -22.604 18.169 1.00 63.13 C
ANISOU 260 CH2 TRP A 32 8107 8892 6987 -345 -240 214 C
ATOM 261 N LEU A 33 -35.819 -25.192 12.849 1.00 53.27 N
ANISOU 261 N LEU A 33 7004 7431 5804 -293 -207 261 N
ATOM 262 CA LEU A 33 -36.277 -26.314 12.054 1.00 54.58 C
ANISOU 262 CA LEU A 33 7195 7584 5957 -296 -222 280 C
ATOM 263 C LEU A 33 -35.449 -27.571 12.108 1.00 54.66 C
ANISOU 263 C LEU A 33 7218 7582 5969 -304 -233 294 C
ATOM 264 O LEU A 33 -35.991 -28.631 12.128 1.00 55.86 O
ANISOU 264 O LEU A 33 7377 7742 6105 -316 -255 309 O
ATOM 265 CB LEU A 33 -36.437 -25.920 10.597 1.00 55.09 C
ANISOU 265 CB LEU A 33 7288 7617 6027 -276 -210 280 C
ATOM 266 CG LEU A 33 -37.534 -24.948 10.188 1.00 57.62 C
ANISOU 266 CG LEU A 33 7607 7945 6342 -269 -206 270 C
ATOM 267 CD1 LEU A 33 -37.487 -24.699 8.704 1.00 58.06 C
ANISOU 267 CD1 LEU A 33 7694 7963 6404 -250 -194 272 C
ATOM 268 CD2 LEU A 33 -38.917 -25.401 10.602 1.00 59.61 C
ANISOU 268 CD2 LEU A 33 7850 8226 6573 -284 -227 278 C
ATOM 269 N ASN A 34 -34.141 -27.445 12.113 1.00 53.28 N
ANISOU 269 N ASN A 34 7044 7387 5814 -297 -219 288 N
ATOM 270 CA ASN A 34 -33.263 -28.585 12.097 1.00 52.90 C
ANISOU 270 CA ASN A 34 7008 7323 5769 -302 -229 299 C
ATOM 271 C ASN A 34 -32.693 -29.064 13.422 1.00 52.18 C
ANISOU 271 C ASN A 34 6895 7250 5680 -320 -240 298 C
ATOM 272 O ASN A 34 -31.807 -28.471 13.988 1.00 50.39 O
ANISOU 272 O ASN A 34 6654 7021 5471 -318 -227 286 O
ATOM 273 CB ASN A 34 -32.139 -28.329 11.124 1.00 53.14 C
ANISOU 273 CB ASN A 34 7056 7314 5819 -282 -208 296 C
ATOM 274 CG ASN A 34 -31.292 -29.540 10.884 1.00 56.10 C
ANISOU 274 CG ASN A 34 7448 7669 6198 -285 -218 307 C
ATOM 275 OD1 ASN A 34 -31.409 -30.544 11.566 1.00 57.95 O
ANISOU 275 OD1 ASN A 34 7678 7919 6422 -303 -241 316 O
ATOM 276 ND2 ASN A 34 -30.406 -29.439 9.932 1.00 55.87 N
ANISOU 276 ND2 ASN A 34 7437 7606 6184 -268 -200 306 N
ATOM 277 N SER A 35 -33.183 -30.208 13.865 1.00 52.84 N
ANISOU 277 N SER A 35 6980 7351 5746 -340 -267 312 N
ATOM 278 CA SER A 35 -32.732 -30.792 15.115 1.00 53.11 C
ANISOU 278 CA SER A 35 6997 7403 5780 -360 -282 312 C
ATOM 279 C SER A 35 -31.223 -31.118 15.169 1.00 52.35 C
ANISOU 279 C SER A 35 6906 7280 5705 -356 -276 309 C
ATOM 280 O SER A 35 -30.657 -31.119 16.237 1.00 52.54 O
ANISOU 280 O SER A 35 6912 7314 5736 -367 -280 302 O
ATOM 281 CB SER A 35 -33.621 -31.967 15.536 1.00 55.45 C
ANISOU 281 CB SER A 35 7294 7722 6051 -382 -313 329 C
ATOM 282 OG SER A 35 -33.171 -33.164 14.977 1.00 58.59 O
ANISOU 282 OG SER A 35 7714 8099 6448 -384 -329 343 O
ATOM 283 N ASN A 36 -30.554 -31.349 14.034 1.00 51.73 N
ANISOU 283 N ASN A 36 6851 7166 5637 -339 -267 312 N
ATOM 284 CA ASN A 36 -29.094 -31.513 14.023 1.00 51.85 C
ANISOU 284 CA ASN A 36 6869 7154 5675 -333 -257 307 C
ATOM 285 C ASN A 36 -28.339 -30.164 14.316 1.00 50.42 C
ANISOU 285 C ASN A 36 6672 6967 5519 -321 -229 289 C
ATOM 286 O ASN A 36 -27.172 -30.182 14.614 1.00 51.21 O
ANISOU 286 O ASN A 36 6767 7050 5639 -319 -222 283 O
ATOM 287 CB ASN A 36 -28.572 -32.111 12.721 1.00 54.03 C
ANISOU 287 CB ASN A 36 7175 7396 5957 -318 -253 315 C
ATOM 288 CG ASN A 36 -29.106 -33.514 12.436 1.00 59.64 C
ANISOU 288 CG ASN A 36 7904 8109 6648 -329 -284 333 C
ATOM 289 OD1 ASN A 36 -29.171 -34.356 13.304 1.00 62.24 O
ANISOU 289 OD1 ASN A 36 8225 8456 6969 -350 -309 339 O
ATOM 290 ND2 ASN A 36 -29.482 -33.748 11.204 1.00 60.27 N
ANISOU 290 ND2 ASN A 36 8008 8170 6720 -315 -282 342 N
ATOM 291 N LEU A 37 -29.057 -29.052 14.236 1.00 48.12 N
ANISOU 291 N LEU A 37 6371 6688 5224 -313 -215 281 N
ATOM 292 CA LEU A 37 -28.504 -27.729 14.508 1.00 46.52 C
ANISOU 292 CA LEU A 37 6152 6482 5041 -300 -192 265 C
ATOM 293 C LEU A 37 -28.881 -27.298 15.905 1.00 46.30 C
ANISOU 293 C LEU A 37 6096 6488 5009 -315 -200 257 C
ATOM 294 O LEU A 37 -28.486 -26.275 16.353 1.00 45.14 O
ANISOU 294 O LEU A 37 5932 6342 4876 -307 -186 244 O
ATOM 295 CB LEU A 37 -28.996 -26.687 13.513 1.00 45.53 C
ANISOU 295 CB LEU A 37 6036 6348 4917 -281 -172 260 C
ATOM 296 CG LEU A 37 -28.414 -26.763 12.121 1.00 46.27 C
ANISOU 296 CG LEU A 37 6155 6404 5020 -263 -157 264 C
ATOM 297 CD1 LEU A 37 -29.066 -25.787 11.192 1.00 46.25 C
ANISOU 297 CD1 LEU A 37 6162 6395 5015 -247 -141 259 C
ATOM 298 CD2 LEU A 37 -26.927 -26.569 12.180 1.00 46.28 C
ANISOU 298 CD2 LEU A 37 6154 6382 5050 -255 -141 257 C
ATOM 299 N GLN A 38 -29.676 -28.091 16.583 1.00 46.66 N
ANISOU 299 N GLN A 38 6135 6560 5032 -335 -224 265 N
ATOM 300 CA GLN A 38 -30.068 -27.763 17.932 1.00 47.21 C
ANISOU 300 CA GLN A 38 6180 6664 5095 -350 -232 258 C
ATOM 301 C GLN A 38 -29.108 -28.318 18.980 1.00 46.90 C
ANISOU 301 C GLN A 38 6131 6623 5066 -364 -243 257 C
ATOM 302 O GLN A 38 -29.212 -29.423 19.400 1.00 48.51 O
ANISOU 302 O GLN A 38 6338 6835 5258 -382 -265 267 O
ATOM 303 CB GLN A 38 -31.480 -28.212 18.187 1.00 49.68 C
ANISOU 303 CB GLN A 38 6489 7009 5378 -365 -251 267 C
ATOM 304 CG GLN A 38 -32.479 -27.450 17.371 1.00 53.41 C
ANISOU 304 CG GLN A 38 6965 7485 5842 -351 -240 265 C
ATOM 305 CD GLN A 38 -33.836 -28.057 17.409 1.00 59.65 C
ANISOU 305 CD GLN A 38 7757 8303 6606 -365 -260 276 C
ATOM 306 OE1 GLN A 38 -34.213 -28.686 18.368 1.00 62.13 O
ANISOU 306 OE1 GLN A 38 8058 8642 6905 -386 -278 282 O
ATOM 307 NE2 GLN A 38 -34.569 -27.867 16.373 1.00 60.00 N
ANISOU 307 NE2 GLN A 38 7816 8339 6644 -354 -256 280 N
ATOM 308 N ASN A 39 -28.144 -27.514 19.346 1.00 45.34 N
ANISOU 308 N ASN A 39 5923 6413 4893 -354 -227 244 N
ATOM 309 CA ASN A 39 -27.147 -27.850 20.333 1.00 44.57 C
ANISOU 309 CA ASN A 39 5815 6309 4809 -364 -235 240 C
ATOM 310 C ASN A 39 -26.757 -26.573 21.078 1.00 43.64 C
ANISOU 310 C ASN A 39 5677 6197 4709 -355 -220 225 C
ATOM 311 O ASN A 39 -27.114 -25.495 20.674 1.00 43.25 O
ANISOU 311 O ASN A 39 5623 6150 4662 -339 -203 217 O
ATOM 312 CB ASN A 39 -25.943 -28.543 19.711 1.00 44.73 C
ANISOU 312 CB ASN A 39 5854 6293 4850 -359 -232 244 C
ATOM 313 CG ASN A 39 -25.387 -27.813 18.512 1.00 46.51 C
ANISOU 313 CG ASN A 39 6090 6487 5094 -334 -206 240 C
ATOM 314 OD1 ASN A 39 -24.862 -26.737 18.623 1.00 46.52 O
ANISOU 314 OD1 ASN A 39 6080 6480 5114 -320 -187 229 O
ATOM 315 ND2 ASN A 39 -25.491 -28.422 17.367 1.00 46.67 N
ANISOU 315 ND2 ASN A 39 6134 6492 5109 -327 -205 250 N
ATOM 316 N VAL A 40 -26.010 -26.708 22.157 1.00 43.17 N
ANISOU 316 N VAL A 40 5605 6136 4661 -365 -228 220 N
ATOM 317 CA VAL A 40 -25.619 -25.566 22.968 1.00 42.25 C
ANISOU 317 CA VAL A 40 5469 6024 4560 -358 -217 205 C
ATOM 318 C VAL A 40 -24.886 -24.486 22.207 1.00 40.92 C
ANISOU 318 C VAL A 40 5302 5829 4418 -332 -192 197 C
ATOM 319 O VAL A 40 -25.180 -23.356 22.375 1.00 40.79 O
ANISOU 319 O VAL A 40 5273 5823 4404 -321 -181 188 O
ATOM 320 CB VAL A 40 -24.838 -25.978 24.223 1.00 43.21 C
ANISOU 320 CB VAL A 40 5581 6145 4692 -373 -231 202 C
ATOM 321 CG1 VAL A 40 -24.177 -24.779 24.843 1.00 43.53 C
ANISOU 321 CG1 VAL A 40 5605 6178 4756 -359 -218 188 C
ATOM 322 CG2 VAL A 40 -25.787 -26.581 25.208 1.00 45.21 C
ANISOU 322 CG2 VAL A 40 5825 6435 4916 -397 -253 207 C
ATOM 323 N THR A 41 -23.940 -24.869 21.375 1.00 39.95 N
ANISOU 323 N THR A 41 5195 5671 4314 -323 -183 201 N
ATOM 324 CA THR A 41 -23.179 -23.934 20.580 1.00 38.48 C
ANISOU 324 CA THR A 41 5012 5456 4153 -300 -159 195 C
ATOM 325 C THR A 41 -24.116 -23.043 19.780 1.00 36.31 C
ANISOU 325 C THR A 41 4738 5191 3866 -286 -146 193 C
ATOM 326 O THR A 41 -24.005 -21.869 19.795 1.00 36.09 O
ANISOU 326 O THR A 41 4700 5162 3850 -272 -132 183 O
ATOM 327 CB THR A 41 -22.237 -24.657 19.609 1.00 41.31 C
ANISOU 327 CB THR A 41 5391 5779 4527 -294 -152 202 C
ATOM 328 OG1 THR A 41 -21.617 -25.755 20.256 1.00 44.44 O
ANISOU 328 OG1 THR A 41 5789 6169 4928 -311 -169 205 O
ATOM 329 CG2 THR A 41 -21.205 -23.755 19.120 1.00 40.93 C
ANISOU 329 CG2 THR A 41 5341 5702 4510 -274 -128 195 C
ATOM 330 N ASN A 42 -25.086 -23.654 19.151 1.00 35.06 N
ANISOU 330 N ASN A 42 4594 5045 3683 -292 -153 202 N
ATOM 331 CA ASN A 42 -26.029 -22.971 18.338 1.00 33.75 C
ANISOU 331 CA ASN A 42 4432 4887 3504 -280 -144 200 C
ATOM 332 C ASN A 42 -27.043 -22.121 19.081 1.00 32.55 C
ANISOU 332 C ASN A 42 4261 4770 3339 -283 -148 191 C
ATOM 333 O ASN A 42 -27.617 -21.258 18.512 1.00 32.21 O
ANISOU 333 O ASN A 42 4217 4729 3292 -270 -138 186 O
ATOM 334 CB ASN A 42 -26.633 -23.922 17.323 1.00 34.25 C
ANISOU 334 CB ASN A 42 4519 4945 3550 -284 -150 214 C
ATOM 335 CG ASN A 42 -25.674 -24.240 16.199 1.00 37.51 C
ANISOU 335 CG ASN A 42 4953 5319 3979 -271 -136 219 C
ATOM 336 OD1 ASN A 42 -24.601 -23.706 16.121 1.00 38.72 O
ANISOU 336 OD1 ASN A 42 5104 5450 4159 -259 -120 212 O
ATOM 337 ND2 ASN A 42 -26.087 -25.087 15.313 1.00 38.17 N
ANISOU 337 ND2 ASN A 42 5059 5395 4049 -272 -142 230 N
ATOM 338 N TYR A 43 -27.251 -22.370 20.359 1.00 32.43 N
ANISOU 338 N TYR A 43 4228 4780 3314 -299 -164 189 N
ATOM 339 CA TYR A 43 -28.122 -21.502 21.112 1.00 32.93 C
ANISOU 339 CA TYR A 43 4271 4876 3366 -299 -166 179 C
ATOM 340 C TYR A 43 -27.450 -20.120 21.266 1.00 30.04 C
ANISOU 340 C TYR A 43 3892 4499 3024 -280 -151 165 C
ATOM 341 O TYR A 43 -28.103 -19.140 21.239 1.00 29.50 O
ANISOU 341 O TYR A 43 3814 4445 2950 -271 -146 156 O
ATOM 342 CB TYR A 43 -28.530 -22.121 22.438 1.00 35.63 C
ANISOU 342 CB TYR A 43 4599 5249 3691 -322 -186 181 C
ATOM 343 CG TYR A 43 -29.245 -23.442 22.254 1.00 40.33 C
ANISOU 343 CG TYR A 43 5205 5856 4261 -340 -203 196 C
ATOM 344 CD1 TYR A 43 -29.929 -23.737 21.076 1.00 42.22 C
ANISOU 344 CD1 TYR A 43 5462 6090 4489 -336 -201 204 C
ATOM 345 CD2 TYR A 43 -29.215 -24.392 23.230 1.00 43.08 C
ANISOU 345 CD2 TYR A 43 5549 6219 4600 -363 -223 202 C
ATOM 346 CE1 TYR A 43 -30.555 -24.935 20.894 1.00 45.17 C
ANISOU 346 CE1 TYR A 43 5847 6472 4842 -352 -218 219 C
ATOM 347 CE2 TYR A 43 -29.847 -25.593 23.061 1.00 45.89 C
ANISOU 347 CE2 TYR A 43 5916 6586 4934 -380 -240 217 C
ATOM 348 CZ TYR A 43 -30.511 -25.867 21.903 1.00 47.57 C
ANISOU 348 CZ TYR A 43 6145 6793 5136 -375 -238 225 C
ATOM 349 OH TYR A 43 -31.114 -27.072 21.778 1.00 51.34 O
ANISOU 349 OH TYR A 43 6634 7281 5593 -392 -258 241 O
ATOM 350 N PHE A 44 -26.140 -20.092 21.421 1.00 27.86 N
ANISOU 350 N PHE A 44 3617 4195 2775 -275 -144 164 N
ATOM 351 CA PHE A 44 -25.403 -18.853 21.486 1.00 27.60 C
ANISOU 351 CA PHE A 44 3573 4146 2766 -257 -130 153 C
ATOM 352 C PHE A 44 -25.394 -18.192 20.097 1.00 26.96 C
ANISOU 352 C PHE A 44 3506 4045 2694 -238 -112 152 C
ATOM 353 O PHE A 44 -25.431 -17.022 20.003 1.00 27.37 O
ANISOU 353 O PHE A 44 3548 4096 2754 -223 -103 142 O
ATOM 354 CB PHE A 44 -23.996 -19.076 21.985 1.00 27.56 C
ANISOU 354 CB PHE A 44 3566 4117 2790 -257 -129 153 C
ATOM 355 CG PHE A 44 -23.924 -19.462 23.439 1.00 29.34 C
ANISOU 355 CG PHE A 44 3776 4359 3010 -273 -147 151 C
ATOM 356 CD1 PHE A 44 -24.182 -18.543 24.418 1.00 30.93 C
ANISOU 356 CD1 PHE A 44 3958 4582 3212 -269 -151 140 C
ATOM 357 CD2 PHE A 44 -23.595 -20.735 23.806 1.00 30.34 C
ANISOU 357 CD2 PHE A 44 3911 4483 3134 -291 -160 159 C
ATOM 358 CE1 PHE A 44 -24.137 -18.890 25.737 1.00 32.53 C
ANISOU 358 CE1 PHE A 44 4148 4801 3409 -284 -166 138 C
ATOM 359 CE2 PHE A 44 -23.536 -21.091 25.119 1.00 32.31 C
ANISOU 359 CE2 PHE A 44 4148 4748 3379 -307 -177 157 C
ATOM 360 CZ PHE A 44 -23.809 -20.171 26.077 1.00 32.83 C
ANISOU 360 CZ PHE A 44 4196 4835 3445 -304 -179 146 C
ATOM 361 N VAL A 45 -25.349 -19.000 19.045 1.00 26.58 N
ANISOU 361 N VAL A 45 3479 3978 2641 -238 -107 163 N
ATOM 362 CA VAL A 45 -25.421 -18.527 17.666 1.00 26.21 C
ANISOU 362 CA VAL A 45 3450 3912 2599 -222 -91 164 C
ATOM 363 C VAL A 45 -26.746 -17.804 17.470 1.00 25.83 C
ANISOU 363 C VAL A 45 3397 3888 2529 -219 -93 158 C
ATOM 364 O VAL A 45 -26.786 -16.768 16.886 1.00 24.40 O
ANISOU 364 O VAL A 45 3216 3698 2356 -204 -81 150 O
ATOM 365 CB VAL A 45 -25.279 -19.660 16.655 1.00 27.24 C
ANISOU 365 CB VAL A 45 3606 4022 2723 -226 -89 177 C
ATOM 366 CG1 VAL A 45 -25.734 -19.217 15.290 1.00 26.18 C
ANISOU 366 CG1 VAL A 45 3489 3873 2584 -212 -76 178 C
ATOM 367 CG2 VAL A 45 -23.860 -20.131 16.592 1.00 28.88 C
ANISOU 367 CG2 VAL A 45 3819 4199 2956 -223 -82 181 C
ATOM 368 N VAL A 46 -27.824 -18.367 18.000 1.00 26.81 N
ANISOU 368 N VAL A 46 3516 4043 2627 -235 -110 160 N
ATOM 369 CA VAL A 46 -29.125 -17.748 17.928 1.00 27.45 C
ANISOU 369 CA VAL A 46 3591 4150 2689 -233 -114 154 C
ATOM 370 C VAL A 46 -29.175 -16.457 18.743 1.00 26.77 C
ANISOU 370 C VAL A 46 3480 4080 2610 -225 -113 138 C
ATOM 371 O VAL A 46 -29.749 -15.511 18.329 1.00 26.37 O
ANISOU 371 O VAL A 46 3427 4034 2557 -214 -109 128 O
ATOM 372 CB VAL A 46 -30.262 -18.716 18.282 1.00 29.55 C
ANISOU 372 CB VAL A 46 3857 4445 2926 -252 -132 162 C
ATOM 373 CG1 VAL A 46 -31.555 -17.982 18.516 1.00 30.72 C
ANISOU 373 CG1 VAL A 46 3991 4624 3056 -252 -138 152 C
ATOM 374 CG2 VAL A 46 -30.413 -19.772 17.208 1.00 30.64 C
ANISOU 374 CG2 VAL A 46 4022 4565 3055 -256 -133 177 C
ATOM 375 N SER A 47 -28.555 -16.434 19.910 1.00 26.33 N
ANISOU 375 N SER A 47 3407 4032 2564 -230 -119 134 N
ATOM 376 CA SER A 47 -28.506 -15.218 20.711 1.00 25.98 C
ANISOU 376 CA SER A 47 3340 4001 2528 -220 -119 119 C
ATOM 377 C SER A 47 -27.805 -14.100 19.900 1.00 24.89 C
ANISOU 377 C SER A 47 3208 3836 2415 -198 -103 113 C
ATOM 378 O SER A 47 -28.237 -13.002 19.860 1.00 24.60 O
ANISOU 378 O SER A 47 3162 3808 2379 -187 -102 101 O
ATOM 379 CB SER A 47 -27.771 -15.449 22.029 1.00 26.07 C
ANISOU 379 CB SER A 47 3337 4019 2549 -228 -127 118 C
ATOM 380 OG SER A 47 -27.810 -14.320 22.821 1.00 27.52 O
ANISOU 380 OG SER A 47 3500 4217 2739 -219 -130 104 O
ATOM 381 N LEU A 48 -26.725 -14.469 19.246 1.00 23.96 N
ANISOU 381 N LEU A 48 3104 3683 2317 -194 -91 121 N
ATOM 382 CA LEU A 48 -25.935 -13.594 18.406 1.00 23.63 C
ANISOU 382 CA LEU A 48 3069 3610 2299 -175 -74 118 C
ATOM 383 C LEU A 48 -26.774 -13.131 17.218 1.00 22.54 C
ANISOU 383 C LEU A 48 2945 3471 2150 -167 -68 116 C
ATOM 384 O LEU A 48 -26.822 -11.985 16.928 1.00 21.42 O
ANISOU 384 O LEU A 48 2798 3325 2015 -153 -62 106 O
ATOM 385 CB LEU A 48 -24.680 -14.316 17.979 1.00 24.48 C
ANISOU 385 CB LEU A 48 3190 3684 2427 -175 -64 128 C
ATOM 386 CG LEU A 48 -23.563 -13.583 17.313 1.00 27.17 C
ANISOU 386 CG LEU A 48 3536 3991 2798 -158 -46 127 C
ATOM 387 CD1 LEU A 48 -23.088 -12.407 18.118 1.00 26.47 C
ANISOU 387 CD1 LEU A 48 3425 3905 2728 -148 -47 116 C
ATOM 388 CD2 LEU A 48 -22.464 -14.571 17.064 1.00 28.84 C
ANISOU 388 CD2 LEU A 48 3759 4174 3024 -162 -39 138 C
ATOM 389 N ALA A 49 -27.491 -14.048 16.598 1.00 22.68 N
ANISOU 389 N ALA A 49 2980 3491 2146 -176 -71 125 N
ATOM 390 CA ALA A 49 -28.386 -13.707 15.516 1.00 23.07 C
ANISOU 390 CA ALA A 49 3044 3539 2184 -170 -67 123 C
ATOM 391 C ALA A 49 -29.481 -12.745 15.990 1.00 23.50 C
ANISOU 391 C ALA A 49 3080 3623 2224 -168 -77 109 C
ATOM 392 O ALA A 49 -29.826 -11.869 15.295 1.00 23.71 O
ANISOU 392 O ALA A 49 3112 3644 2252 -157 -72 101 O
ATOM 393 CB ALA A 49 -28.984 -14.938 14.880 1.00 23.05 C
ANISOU 393 CB ALA A 49 3062 3535 2161 -181 -71 136 C
ATOM 394 N ALA A 50 -29.992 -12.927 17.193 1.00 23.13 N
ANISOU 394 N ALA A 50 3014 3609 2165 -179 -91 105 N
ATOM 395 CA ALA A 50 -31.019 -12.052 17.734 1.00 24.12 C
ANISOU 395 CA ALA A 50 3121 3767 2277 -177 -101 90 C
ATOM 396 C ALA A 50 -30.507 -10.619 17.907 1.00 23.65 C
ANISOU 396 C ALA A 50 3048 3701 2237 -159 -97 76 C
ATOM 397 O ALA A 50 -31.178 -9.664 17.632 1.00 24.87 O
ANISOU 397 O ALA A 50 3198 3864 2388 -150 -99 64 O
ATOM 398 CB ALA A 50 -31.547 -12.588 19.038 1.00 24.90 C
ANISOU 398 CB ALA A 50 3201 3901 2359 -192 -116 90 C
ATOM 399 N ALA A 51 -29.277 -10.526 18.341 1.00 21.89 N
ANISOU 399 N ALA A 51 2819 3460 2037 -155 -91 78 N
ATOM 400 CA ALA A 51 -28.615 -9.270 18.526 1.00 21.40 C
ANISOU 400 CA ALA A 51 2746 3389 1997 -139 -88 68 C
ATOM 401 C ALA A 51 -28.483 -8.569 17.175 1.00 21.15 C
ANISOU 401 C ALA A 51 2731 3331 1976 -125 -75 66 C
ATOM 402 O ALA A 51 -28.702 -7.424 17.081 1.00 21.94 O
ANISOU 402 O ALA A 51 2823 3434 2080 -113 -78 54 O
ATOM 403 CB ALA A 51 -27.276 -9.478 19.150 1.00 20.25 C
ANISOU 403 CB ALA A 51 2593 3225 1874 -138 -84 73 C
ATOM 404 N ASP A 52 -28.131 -9.316 16.155 1.00 20.24 N
ANISOU 404 N ASP A 52 2639 3189 1862 -127 -63 79 N
ATOM 405 CA ASP A 52 -28.015 -8.755 14.833 1.00 20.49 C
ANISOU 405 CA ASP A 52 2689 3194 1901 -116 -51 79 C
ATOM 406 C ASP A 52 -29.367 -8.317 14.242 1.00 22.16 C
ANISOU 406 C ASP A 52 2907 3420 2093 -115 -58 70 C
ATOM 407 O ASP A 52 -29.457 -7.291 13.647 1.00 22.35 O
ANISOU 407 O ASP A 52 2935 3435 2124 -103 -55 61 O
ATOM 408 CB ASP A 52 -27.149 -9.636 13.953 1.00 20.97 C
ANISOU 408 CB ASP A 52 2773 3222 1972 -117 -35 94 C
ATOM 409 CG ASP A 52 -25.691 -9.650 14.430 1.00 27.18 C
ANISOU 409 CG ASP A 52 3551 3989 2786 -113 -27 99 C
ATOM 410 OD1 ASP A 52 -25.247 -8.657 14.965 1.00 26.83 O
ANISOU 410 OD1 ASP A 52 3490 3947 2759 -104 -28 90 O
ATOM 411 OD2 ASP A 52 -25.005 -10.634 14.296 1.00 30.22 O
ANISOU 411 OD2 ASP A 52 3947 4359 3177 -119 -20 110 O
ATOM 412 N ILE A 53 -30.413 -9.085 14.488 1.00 22.41 N
ANISOU 412 N ILE A 53 2940 3476 2100 -128 -68 72 N
ATOM 413 CA ILE A 53 -31.745 -8.734 14.051 1.00 23.64 C
ANISOU 413 CA ILE A 53 3099 3647 2236 -128 -77 64 C
ATOM 414 C ILE A 53 -32.127 -7.388 14.649 1.00 23.62 C
ANISOU 414 C ILE A 53 3074 3664 2236 -119 -86 44 C
ATOM 415 O ILE A 53 -32.608 -6.551 13.962 1.00 24.01 O
ANISOU 415 O ILE A 53 3129 3708 2286 -110 -87 34 O
ATOM 416 CB ILE A 53 -32.796 -9.815 14.364 1.00 25.47 C
ANISOU 416 CB ILE A 53 3332 3904 2443 -144 -88 70 C
ATOM 417 CG1 ILE A 53 -32.515 -11.069 13.558 1.00 27.05 C
ANISOU 417 CG1 ILE A 53 3558 4081 2639 -151 -81 89 C
ATOM 418 CG2 ILE A 53 -34.185 -9.288 14.145 1.00 26.98 C
ANISOU 418 CG2 ILE A 53 3520 4114 2616 -144 -99 58 C
ATOM 419 CD1 ILE A 53 -33.414 -12.228 13.817 1.00 28.91 C
ANISOU 419 CD1 ILE A 53 3796 4337 2852 -168 -92 98 C
ATOM 420 N LEU A 54 -31.858 -7.195 15.941 1.00 22.64 N
ANISOU 420 N LEU A 54 2925 3562 2116 -120 -94 39 N
ATOM 421 CA LEU A 54 -32.147 -5.959 16.664 1.00 22.09 C
ANISOU 421 CA LEU A 54 2831 3513 2049 -111 -105 21 C
ATOM 422 C LEU A 54 -31.324 -4.755 16.211 1.00 20.33 C
ANISOU 422 C LEU A 54 2609 3266 1850 -93 -99 14 C
ATOM 423 O LEU A 54 -31.711 -3.661 16.394 1.00 19.17 O
ANISOU 423 O LEU A 54 2449 3130 1704 -84 -109 -1 O
ATOM 424 CB LEU A 54 -32.043 -6.167 18.165 1.00 22.47 C
ANISOU 424 CB LEU A 54 2854 3589 2093 -117 -115 19 C
ATOM 425 CG LEU A 54 -33.087 -7.078 18.790 1.00 25.82 C
ANISOU 425 CG LEU A 54 3272 4047 2491 -133 -125 21 C
ATOM 426 CD1 LEU A 54 -32.727 -7.455 20.200 1.00 26.71 C
ANISOU 426 CD1 LEU A 54 3365 4180 2602 -141 -131 22 C
ATOM 427 CD2 LEU A 54 -34.419 -6.422 18.757 1.00 27.04 C
ANISOU 427 CD2 LEU A 54 3417 4228 2628 -131 -136 6 C
ATOM 428 N VAL A 55 -30.164 -5.020 15.648 1.00 19.37 N
ANISOU 428 N VAL A 55 2502 3111 1748 -90 -84 26 N
ATOM 429 CA VAL A 55 -29.357 -3.974 15.060 1.00 18.90 C
ANISOU 429 CA VAL A 55 2445 3024 1711 -75 -77 23 C
ATOM 430 C VAL A 55 -30.164 -3.408 13.879 1.00 20.25 C
ANISOU 430 C VAL A 55 2633 3187 1874 -70 -77 15 C
ATOM 431 O VAL A 55 -30.303 -2.260 13.735 1.00 20.76 O
ANISOU 431 O VAL A 55 2692 3251 1944 -60 -84 3 O
ATOM 432 CB VAL A 55 -27.969 -4.479 14.596 1.00 18.19 C
ANISOU 432 CB VAL A 55 2368 2899 1643 -73 -59 38 C
ATOM 433 CG1 VAL A 55 -27.325 -3.527 13.622 1.00 17.62 C
ANISOU 433 CG1 VAL A 55 2307 2797 1591 -60 -48 37 C
ATOM 434 CG2 VAL A 55 -27.064 -4.694 15.784 1.00 18.18 C
ANISOU 434 CG2 VAL A 55 2348 2902 1657 -74 -61 42 C
ATOM 435 N GLY A 56 -30.721 -4.269 13.073 1.00 20.97 N
ANISOU 435 N GLY A 56 2746 3272 1950 -79 -71 24 N
ATOM 436 CA GLY A 56 -31.529 -3.836 11.959 1.00 22.04 C
ANISOU 436 CA GLY A 56 2901 3398 2077 -76 -72 17 C
ATOM 437 C GLY A 56 -32.846 -3.212 12.325 1.00 22.91 C
ANISOU 437 C GLY A 56 2996 3538 2169 -76 -91 0 C
ATOM 438 O GLY A 56 -33.203 -2.220 11.828 1.00 23.31 O
ANISOU 438 O GLY A 56 3050 3584 2223 -68 -97 -13 O
ATOM 439 N VAL A 57 -33.547 -3.829 13.239 1.00 23.17 N
ANISOU 439 N VAL A 57 3014 3603 2185 -86 -101 -1 N
ATOM 440 CA VAL A 57 -34.833 -3.354 13.657 1.00 25.55 C
ANISOU 440 CA VAL A 57 3302 3936 2470 -88 -118 -18 C
ATOM 441 C VAL A 57 -34.764 -2.069 14.492 1.00 25.07 C
ANISOU 441 C VAL A 57 3215 3894 2418 -76 -130 -36 C
ATOM 442 O VAL A 57 -35.527 -1.199 14.308 1.00 25.15 O
ANISOU 442 O VAL A 57 3220 3913 2423 -70 -142 -53 O
ATOM 443 CB VAL A 57 -35.624 -4.466 14.378 1.00 28.25 C
ANISOU 443 CB VAL A 57 3636 4308 2790 -103 -124 -12 C
ATOM 444 CG1 VAL A 57 -36.902 -3.948 14.955 1.00 30.96 C
ANISOU 444 CG1 VAL A 57 3960 4687 3117 -105 -141 -29 C
ATOM 445 CG2 VAL A 57 -35.915 -5.614 13.451 1.00 29.58 C
ANISOU 445 CG2 VAL A 57 3831 4459 2949 -113 -117 5 C
ATOM 446 N LEU A 58 -33.794 -1.977 15.383 1.00 23.67 N
ANISOU 446 N LEU A 58 3021 3719 2254 -73 -129 -33 N
ATOM 447 CA LEU A 58 -33.667 -0.855 16.292 1.00 24.37 C
ANISOU 447 CA LEU A 58 3085 3825 2351 -61 -142 -49 C
ATOM 448 C LEU A 58 -32.394 0.023 16.233 1.00 22.88 C
ANISOU 448 C LEU A 58 2893 3611 2189 -47 -138 -48 C
ATOM 449 O LEU A 58 -32.490 1.205 16.078 1.00 22.91 O
ANISOU 449 O LEU A 58 2890 3613 2200 -35 -148 -62 O
ATOM 450 CB LEU A 58 -33.898 -1.355 17.719 1.00 25.41 C
ANISOU 450 CB LEU A 58 3193 3992 2471 -69 -150 -49 C
ATOM 451 CG LEU A 58 -35.307 -1.792 18.122 1.00 27.68 C
ANISOU 451 CG LEU A 58 3471 4315 2730 -80 -160 -56 C
ATOM 452 CD1 LEU A 58 -35.310 -2.362 19.517 1.00 27.62 C
ANISOU 452 CD1 LEU A 58 3443 4338 2714 -88 -165 -54 C
ATOM 453 CD2 LEU A 58 -36.281 -0.652 18.024 1.00 27.89 C
ANISOU 453 CD2 LEU A 58 3488 4359 2750 -70 -175 -79 C
ATOM 454 N ALA A 59 -31.228 -0.572 16.366 1.00 20.81 N
ANISOU 454 N ALA A 59 2636 3329 1944 -49 -125 -32 N
ATOM 455 CA ALA A 59 -29.995 0.171 16.348 1.00 20.58 C
ANISOU 455 CA ALA A 59 2602 3275 1941 -36 -120 -30 C
ATOM 456 C ALA A 59 -29.805 1.033 15.094 1.00 20.53 C
ANISOU 456 C ALA A 59 2613 3241 1947 -27 -116 -33 C
ATOM 457 O ALA A 59 -29.414 2.132 15.192 1.00 20.92 O
ANISOU 457 O ALA A 59 2652 3285 2010 -14 -123 -41 O
ATOM 458 CB ALA A 59 -28.819 -0.729 16.564 1.00 20.13 C
ANISOU 458 CB ALA A 59 2550 3199 1899 -41 -106 -12 C
ATOM 459 N ILE A 60 -30.085 0.499 13.928 1.00 20.47 N
ANISOU 459 N ILE A 60 2631 3216 1932 -33 -104 -25 N
ATOM 460 CA ILE A 60 -29.945 1.281 12.710 1.00 20.33 C
ANISOU 460 CA ILE A 60 2632 3171 1923 -25 -99 -28 C
ATOM 461 C ILE A 60 -30.910 2.457 12.631 1.00 20.71 C
ANISOU 461 C ILE A 60 2671 3234 1962 -18 -119 -49 C
ATOM 462 O ILE A 60 -30.494 3.520 12.400 1.00 20.29 O
ANISOU 462 O ILE A 60 2616 3169 1925 -7 -124 -56 O
ATOM 463 CB ILE A 60 -29.882 0.429 11.464 1.00 19.87 C
ANISOU 463 CB ILE A 60 2604 3086 1860 -32 -80 -14 C
ATOM 464 CG1 ILE A 60 -28.511 -0.234 11.418 1.00 20.51 C
ANISOU 464 CG1 ILE A 60 2691 3143 1960 -33 -61 4 C
ATOM 465 CG2 ILE A 60 -30.127 1.276 10.239 1.00 20.94 C
ANISOU 465 CG2 ILE A 60 2759 3200 1997 -26 -80 -21 C
ATOM 466 CD1 ILE A 60 -28.360 -1.358 10.436 1.00 21.68 C
ANISOU 466 CD1 ILE A 60 2867 3268 2102 -41 -42 20 C
ATOM 467 N PRO A 61 -32.207 2.239 12.832 1.00 22.08 N
ANISOU 467 N PRO A 61 2841 3434 2113 -25 -131 -60 N
ATOM 468 CA PRO A 61 -33.144 3.362 12.901 1.00 23.54 C
ANISOU 468 CA PRO A 61 3017 3638 2292 -18 -152 -82 C
ATOM 469 C PRO A 61 -32.716 4.397 13.982 1.00 23.81 C
ANISOU 469 C PRO A 61 3022 3688 2338 -5 -168 -94 C
ATOM 470 O PRO A 61 -32.873 5.544 13.784 1.00 24.18 O
ANISOU 470 O PRO A 61 3064 3733 2391 5 -182 -108 O
ATOM 471 CB PRO A 61 -34.448 2.709 13.281 1.00 24.41 C
ANISOU 471 CB PRO A 61 3121 3778 2375 -29 -160 -89 C
ATOM 472 CG PRO A 61 -34.340 1.344 12.800 1.00 24.88 C
ANISOU 472 CG PRO A 61 3201 3824 2428 -41 -142 -69 C
ATOM 473 CD PRO A 61 -32.907 0.967 12.717 1.00 22.54 C
ANISOU 473 CD PRO A 61 2911 3502 2152 -39 -125 -51 C
ATOM 474 N PHE A 62 -32.175 3.934 15.097 1.00 22.96 N
ANISOU 474 N PHE A 62 2896 3594 2234 -6 -166 -87 N
ATOM 475 CA PHE A 62 -31.686 4.809 16.137 1.00 22.17 C
ANISOU 475 CA PHE A 62 2771 3506 2146 6 -180 -95 C
ATOM 476 C PHE A 62 -30.485 5.629 15.643 1.00 21.17 C
ANISOU 476 C PHE A 62 2649 3346 2048 18 -176 -90 C
ATOM 477 O PHE A 62 -30.419 6.785 15.891 1.00 20.58 O
ANISOU 477 O PHE A 62 2562 3276 1982 31 -193 -102 O
ATOM 478 CB PHE A 62 -31.270 4.048 17.403 1.00 21.62 C
ANISOU 478 CB PHE A 62 2685 3455 2077 1 -178 -87 C
ATOM 479 CG PHE A 62 -32.407 3.527 18.251 1.00 22.86 C
ANISOU 479 CG PHE A 62 2828 3651 2207 -8 -187 -96 C
ATOM 480 CD1 PHE A 62 -33.720 3.669 17.890 1.00 24.55 C
ANISOU 480 CD1 PHE A 62 3044 3884 2401 -11 -196 -109 C
ATOM 481 CD2 PHE A 62 -32.131 2.845 19.408 1.00 23.16 C
ANISOU 481 CD2 PHE A 62 2852 3707 2242 -13 -186 -89 C
ATOM 482 CE1 PHE A 62 -34.720 3.150 18.672 1.00 26.42 C
ANISOU 482 CE1 PHE A 62 3266 4157 2614 -20 -203 -115 C
ATOM 483 CE2 PHE A 62 -33.125 2.339 20.193 1.00 24.40 C
ANISOU 483 CE2 PHE A 62 2995 3900 2375 -22 -194 -95 C
ATOM 484 CZ PHE A 62 -34.418 2.482 19.825 1.00 25.84 C
ANISOU 484 CZ PHE A 62 3179 4102 2537 -26 -202 -108 C
ATOM 485 N ALA A 63 -29.541 4.983 14.970 1.00 20.04 N
ANISOU 485 N ALA A 63 2525 3173 1918 13 -154 -71 N
ATOM 486 CA ALA A 63 -28.357 5.628 14.414 1.00 20.47 C
ANISOU 486 CA ALA A 63 2585 3193 1998 23 -147 -63 C
ATOM 487 C ALA A 63 -28.729 6.724 13.389 1.00 21.92 C
ANISOU 487 C ALA A 63 2781 3364 2184 30 -156 -74 C
ATOM 488 O ALA A 63 -28.173 7.756 13.356 1.00 21.50 O
ANISOU 488 O ALA A 63 2721 3300 2149 41 -165 -77 O
ATOM 489 CB ALA A 63 -27.438 4.605 13.784 1.00 19.89 C
ANISOU 489 CB ALA A 63 2531 3091 1936 15 -120 -41 C
ATOM 490 N ILE A 64 -29.720 6.435 12.579 1.00 22.73 N
ANISOU 490 N ILE A 64 2901 3468 2268 22 -154 -79 N
ATOM 491 CA ILE A 64 -30.194 7.366 11.586 1.00 24.50 C
ANISOU 491 CA ILE A 64 3138 3680 2490 25 -163 -91 C
ATOM 492 C ILE A 64 -30.753 8.585 12.318 1.00 25.48 C
ANISOU 492 C ILE A 64 3239 3830 2614 36 -193 -113 C
ATOM 493 O ILE A 64 -30.424 9.675 12.021 1.00 25.66 O
ANISOU 493 O ILE A 64 3260 3840 2650 46 -205 -120 O
ATOM 494 CB ILE A 64 -31.229 6.713 10.655 1.00 25.33 C
ANISOU 494 CB ILE A 64 3267 3782 2574 14 -157 -92 C
ATOM 495 CG1 ILE A 64 -30.563 5.776 9.652 1.00 26.11 C
ANISOU 495 CG1 ILE A 64 3394 3849 2677 7 -129 -71 C
ATOM 496 CG2 ILE A 64 -32.034 7.758 9.945 1.00 27.12 C
ANISOU 496 CG2 ILE A 64 3501 4006 2795 18 -175 -111 C
ATOM 497 CD1 ILE A 64 -31.499 4.757 9.082 1.00 26.49 C
ANISOU 497 CD1 ILE A 64 3462 3900 2704 -5 -122 -68 C
ATOM 498 N THR A 65 -31.550 8.325 13.330 1.00 25.14 N
ANISOU 498 N THR A 65 3177 3822 2555 34 -205 -123 N
ATOM 499 CA THR A 65 -32.175 9.319 14.144 1.00 26.19 C
ANISOU 499 CA THR A 65 3285 3983 2682 44 -233 -145 C
ATOM 500 C THR A 65 -31.176 10.258 14.819 1.00 26.32 C
ANISOU 500 C THR A 65 3283 3995 2721 60 -244 -145 C
ATOM 501 O THR A 65 -31.306 11.438 14.749 1.00 27.46 O
ANISOU 501 O THR A 65 3421 4140 2872 71 -266 -160 O
ATOM 502 CB THR A 65 -33.070 8.656 15.191 1.00 28.77 C
ANISOU 502 CB THR A 65 3595 4349 2988 38 -238 -152 C
ATOM 503 OG1 THR A 65 -34.217 8.137 14.577 1.00 31.38 O
ANISOU 503 OG1 THR A 65 3939 4687 3297 27 -236 -158 O
ATOM 504 CG2 THR A 65 -33.511 9.608 16.166 1.00 30.08 C
ANISOU 504 CG2 THR A 65 3734 4543 3151 50 -264 -172 C
ATOM 505 N ILE A 66 -30.157 9.700 15.444 1.00 24.72 N
ANISOU 505 N ILE A 66 3075 3786 2533 60 -231 -129 N
ATOM 506 CA ILE A 66 -29.160 10.479 16.142 1.00 25.06 C
ANISOU 506 CA ILE A 66 3100 3823 2599 74 -242 -127 C
ATOM 507 C ILE A 66 -28.257 11.310 15.237 1.00 25.60 C
ANISOU 507 C ILE A 66 3180 3857 2691 82 -240 -120 C
ATOM 508 O ILE A 66 -27.737 12.279 15.648 1.00 26.30 O
ANISOU 508 O ILE A 66 3255 3943 2796 95 -257 -124 O
ATOM 509 CB ILE A 66 -28.372 9.638 17.161 1.00 24.89 C
ANISOU 509 CB ILE A 66 3068 3805 2585 72 -231 -112 C
ATOM 510 CG1 ILE A 66 -27.942 10.506 18.344 1.00 27.04 C
ANISOU 510 CG1 ILE A 66 3314 4090 2871 88 -253 -119 C
ATOM 511 CG2 ILE A 66 -27.220 8.934 16.509 1.00 23.70 C
ANISOU 511 CG2 ILE A 66 2934 3619 2453 66 -204 -89 C
ATOM 512 CD1 ILE A 66 -27.453 9.742 19.548 1.00 28.14 C
ANISOU 512 CD1 ILE A 66 3440 4240 3012 86 -248 -110 C
ATOM 513 N SER A 67 -28.129 10.892 13.989 1.00 24.70 N
ANISOU 513 N SER A 67 3091 3716 2576 73 -220 -110 N
ATOM 514 CA SER A 67 -27.370 11.594 12.975 1.00 25.49 C
ANISOU 514 CA SER A 67 3206 3783 2696 77 -216 -103 C
ATOM 515 C SER A 67 -28.008 12.945 12.618 1.00 27.44 C
ANISOU 515 C SER A 67 3451 4034 2940 85 -244 -123 C
ATOM 516 O SER A 67 -27.344 13.782 12.139 1.00 28.57 O
ANISOU 516 O SER A 67 3598 4156 3102 92 -249 -120 O
ATOM 517 CB SER A 67 -27.179 10.749 11.727 1.00 24.18 C
ANISOU 517 CB SER A 67 3070 3590 2527 65 -187 -88 C
ATOM 518 OG SER A 67 -28.319 10.679 10.940 1.00 26.16 O
ANISOU 518 OG SER A 67 3338 3845 2756 57 -190 -99 O
ATOM 519 N THR A 68 -29.289 13.085 12.883 1.00 28.03 N
ANISOU 519 N THR A 68 3520 4137 2992 84 -261 -143 N
ATOM 520 CA THR A 68 -30.001 14.314 12.632 1.00 30.13 C
ANISOU 520 CA THR A 68 3783 4411 3255 91 -290 -165 C
ATOM 521 C THR A 68 -29.771 15.388 13.693 1.00 31.68 C
ANISOU 521 C THR A 68 3950 4624 3461 108 -319 -177 C
ATOM 522 O THR A 68 -29.969 16.542 13.444 1.00 32.85 O
ANISOU 522 O THR A 68 4096 4770 3614 117 -344 -191 O
ATOM 523 CB THR A 68 -31.522 14.092 12.501 1.00 31.86 C
ANISOU 523 CB THR A 68 4006 4654 3447 84 -300 -184 C
ATOM 524 OG1 THR A 68 -32.095 13.828 13.767 1.00 33.03 O
ANISOU 524 OG1 THR A 68 4129 4839 3581 86 -310 -194 O
ATOM 525 CG2 THR A 68 -31.856 12.991 11.566 1.00 30.82 C
ANISOU 525 CG2 THR A 68 3900 4507 3302 68 -274 -174 C
ATOM 526 N GLY A 69 -29.364 14.988 14.888 1.00 31.25 N
ANISOU 526 N GLY A 69 3876 4586 3411 113 -318 -171 N
ATOM 527 CA GLY A 69 -29.183 15.922 15.969 1.00 31.98 C
ANISOU 527 CA GLY A 69 3942 4696 3512 130 -346 -182 C
ATOM 528 C GLY A 69 -30.491 16.542 16.451 1.00 33.63 C
ANISOU 528 C GLY A 69 4136 4939 3700 135 -375 -210 C
ATOM 529 O GLY A 69 -30.510 17.633 16.941 1.00 34.31 O
ANISOU 529 O GLY A 69 4207 5036 3794 150 -404 -223 O
ATOM 530 N PHE A 70 -31.580 15.803 16.328 1.00 33.24 N
ANISOU 530 N PHE A 70 4093 4909 3626 123 -367 -218 N
ATOM 531 CA PHE A 70 -32.900 16.248 16.719 1.00 34.82 C
ANISOU 531 CA PHE A 70 4281 5144 3806 126 -391 -244 C
ATOM 532 C PHE A 70 -33.029 16.587 18.195 1.00 35.68 C
ANISOU 532 C PHE A 70 4360 5287 3912 139 -410 -256 C
ATOM 533 O PHE A 70 -32.398 16.008 19.016 1.00 34.78 O
ANISOU 533 O PHE A 70 4236 5176 3802 140 -399 -242 O
ATOM 534 CB PHE A 70 -33.969 15.217 16.334 1.00 35.02 C
ANISOU 534 CB PHE A 70 4318 5182 3807 109 -375 -247 C
ATOM 535 CG PHE A 70 -34.066 14.076 17.266 1.00 35.85 C
ANISOU 535 CG PHE A 70 4412 5309 3901 102 -359 -238 C
ATOM 536 CD1 PHE A 70 -33.013 13.215 17.440 1.00 35.53 C
ANISOU 536 CD1 PHE A 70 4377 5252 3872 97 -334 -213 C
ATOM 537 CD2 PHE A 70 -35.210 13.856 17.977 1.00 37.63 C
ANISOU 537 CD2 PHE A 70 4623 5573 4104 99 -368 -254 C
ATOM 538 CE1 PHE A 70 -33.087 12.187 18.333 1.00 36.15 C
ANISOU 538 CE1 PHE A 70 4446 5351 3940 89 -322 -205 C
ATOM 539 CE2 PHE A 70 -35.305 12.814 18.840 1.00 37.97 C
ANISOU 539 CE2 PHE A 70 4656 5636 4134 92 -354 -245 C
ATOM 540 CZ PHE A 70 -34.238 11.975 19.020 1.00 36.67 C
ANISOU 540 CZ PHE A 70 4497 5454 3981 86 -332 -220 C
ATOM 541 N CYS A 71 -33.888 17.536 18.495 1.00 37.14 N
ANISOU 541 N CYS A 71 4530 5495 4087 149 -441 -281 N
ATOM 542 CA CYS A 71 -34.134 17.964 19.847 1.00 38.91 C
ANISOU 542 CA CYS A 71 4726 5753 4305 164 -462 -295 C
ATOM 543 C CYS A 71 -34.779 16.840 20.642 1.00 38.74 C
ANISOU 543 C CYS A 71 4695 5762 4262 153 -447 -294 C
ATOM 544 O CYS A 71 -35.707 16.222 20.190 1.00 39.64 O
ANISOU 544 O CYS A 71 4819 5886 4358 140 -436 -299 O
ATOM 545 CB CYS A 71 -35.044 19.182 19.855 1.00 41.50 C
ANISOU 545 CB CYS A 71 5042 6099 4625 176 -498 -325 C
ATOM 546 SG CYS A 71 -34.382 20.670 19.163 1.00 50.70 S
ANISOU 546 SG CYS A 71 6214 7236 5815 190 -526 -330 S
ATOM 547 N ALA A 72 -34.255 16.592 21.823 1.00 36.92 N
ANISOU 547 N ALA A 72 4448 5544 4034 160 -446 -287 N
ATOM 548 CA ALA A 72 -34.762 15.566 22.699 1.00 36.86 C
ANISOU 548 CA ALA A 72 4431 5567 4008 151 -433 -285 C
ATOM 549 C ALA A 72 -34.344 15.770 24.133 1.00 36.13 C
ANISOU 549 C ALA A 72 4316 5494 3917 164 -445 -287 C
ATOM 550 O ALA A 72 -33.402 16.442 24.413 1.00 35.09 O
ANISOU 550 O ALA A 72 4180 5346 3808 179 -456 -281 O
ATOM 551 CB ALA A 72 -34.308 14.197 22.243 1.00 36.14 C
ANISOU 551 CB ALA A 72 4359 5456 3917 131 -398 -260 C
ATOM 552 N ALA A 73 -35.067 15.130 25.025 1.00 36.74 N
ANISOU 552 N ALA A 73 4380 5606 3972 159 -441 -292 N
ATOM 553 CA ALA A 73 -34.722 15.130 26.420 1.00 36.79 C
ANISOU 553 CA ALA A 73 4367 5632 3978 169 -449 -292 C
ATOM 554 C ALA A 73 -33.434 14.329 26.493 1.00 35.63 C
ANISOU 554 C ALA A 73 4232 5455 3851 162 -427 -264 C
ATOM 555 O ALA A 73 -33.352 13.291 25.910 1.00 35.48 O
ANISOU 555 O ALA A 73 4229 5423 3829 143 -401 -248 O
ATOM 556 CB ALA A 73 -35.791 14.460 27.210 1.00 38.26 C
ANISOU 556 CB ALA A 73 4541 5861 4136 160 -445 -302 C
ATOM 557 N CYS A 74 -32.450 14.825 27.212 1.00 35.02 N
ANISOU 557 N CYS A 74 4145 5366 3793 177 -438 -258 N
ATOM 558 CA CYS A 74 -31.168 14.180 27.280 1.00 34.13 C
ANISOU 558 CA CYS A 74 4043 5222 3703 172 -419 -232 C
ATOM 559 C CYS A 74 -31.154 12.694 27.578 1.00 33.09 C
ANISOU 559 C CYS A 74 3918 5096 3559 151 -392 -217 C
ATOM 560 O CYS A 74 -30.471 11.979 26.941 1.00 30.87 O
ANISOU 560 O CYS A 74 3654 4786 3291 140 -371 -198 O
ATOM 561 CB CYS A 74 -30.193 14.938 28.154 1.00 35.83 C
ANISOU 561 CB CYS A 74 4247 5428 3941 193 -438 -230 C
ATOM 562 SG CYS A 74 -28.523 14.338 27.939 1.00 39.15 S
ANISOU 562 SG CYS A 74 4681 5800 4395 188 -417 -199 S
ATOM 563 N HIS A 75 -31.974 12.205 28.496 1.00 34.04 N
ANISOU 563 N HIS A 75 4026 5253 3654 146 -394 -226 N
ATOM 564 CA AHIS A 75 -32.019 10.766 28.800 0.64 34.57 C
ANISOU 564 CA AHIS A 75 4100 5327 3709 124 -370 -211 C
ATOM 565 CA BHIS A 75 -32.000 10.762 28.801 0.36 34.38 C
ANISOU 565 CA BHIS A 75 4076 5302 3685 124 -370 -211 C
ATOM 566 C HIS A 75 -32.579 9.671 27.776 1.00 33.80 C
ANISOU 566 C HIS A 75 4020 5225 3597 101 -346 -202 C
ATOM 567 O HIS A 75 -32.270 8.455 27.535 1.00 32.02 O
ANISOU 567 O HIS A 75 3808 4987 3370 82 -323 -183 O
ATOM 568 CB AHIS A 75 -32.638 10.534 30.174 0.64 37.54 C
ANISOU 568 CB AHIS A 75 4457 5744 4063 125 -379 -221 C
ATOM 569 CB BHIS A 75 -32.562 10.523 30.203 0.36 36.87 C
ANISOU 569 CB BHIS A 75 4372 5657 3979 125 -379 -220 C
ATOM 570 CG AHIS A 75 -31.769 10.996 31.292 0.64 41.03 C
ANISOU 570 CG AHIS A 75 4887 6181 4520 141 -393 -219 C
ATOM 571 CG BHIS A 75 -31.741 11.150 31.284 0.36 39.85 C
ANISOU 571 CG BHIS A 75 4738 6031 4374 144 -396 -221 C
ATOM 572 ND1AHIS A 75 -30.890 10.165 31.939 0.64 42.90 N
ANISOU 572 ND1AHIS A 75 5129 6405 4768 134 -382 -201 N
ATOM 573 ND1BHIS A 75 -32.006 12.403 31.783 0.36 42.76 N
ANISOU 573 ND1BHIS A 75 5089 6415 4742 167 -424 -240 N
ATOM 574 CD2AHIS A 75 -31.602 12.218 31.838 0.64 42.85 C
ANISOU 574 CD2AHIS A 75 5104 6417 4761 166 -419 -233 C
ATOM 575 CD2BHIS A 75 -30.631 10.722 31.923 0.36 40.65 C
ANISOU 575 CD2BHIS A 75 4841 6112 4493 144 -390 -204 C
ATOM 576 CE1AHIS A 75 -30.238 10.847 32.855 0.64 43.68 C
ANISOU 576 CE1AHIS A 75 5217 6499 4881 152 -399 -204 C
ATOM 577 CE1BHIS A 75 -31.113 12.704 32.704 0.36 43.33 C
ANISOU 577 CE1BHIS A 75 5154 6477 4830 181 -434 -235 C
ATOM 578 NE2AHIS A 75 -30.648 12.097 32.812 0.64 44.07 N
ANISOU 578 NE2AHIS A 75 5255 6559 4930 172 -423 -222 N
ATOM 579 NE2BHIS A 75 -30.272 11.696 32.814 0.36 42.42 N
ANISOU 579 NE2BHIS A 75 5051 6340 4727 167 -414 -213 N
ATOM 580 N GLY A 76 -33.467 10.253 26.989 1.00 34.28 N
ANISOU 580 N GLY A 76 4083 5294 3648 103 -354 -217 N
ATOM 581 CA GLY A 76 -34.142 9.601 25.898 1.00 33.78 C
ANISOU 581 CA GLY A 76 4036 5226 3572 86 -338 -214 C
ATOM 582 C GLY A 76 -33.092 9.541 24.812 1.00 32.15 C
ANISOU 582 C GLY A 76 3851 4973 3390 84 -324 -196 C
ATOM 583 O GLY A 76 -32.916 8.547 24.195 1.00 32.01 O
ANISOU 583 O GLY A 76 3851 4940 3372 69 -302 -180 O
ATOM 584 N CYS A 77 -32.387 10.633 24.628 1.00 30.47 N
ANISOU 584 N CYS A 77 3636 4740 3200 102 -337 -200 N
ATOM 585 CA CYS A 77 -31.294 10.721 23.720 1.00 29.12 C
ANISOU 585 CA CYS A 77 3483 4527 3056 103 -326 -183 C
ATOM 586 C CYS A 77 -30.219 9.675 24.055 1.00 26.73 C
ANISOU 586 C CYS A 77 3187 4204 2766 94 -305 -160 C
ATOM 587 O CYS A 77 -29.740 9.019 23.203 1.00 25.20 O
ANISOU 587 O CYS A 77 3011 3984 2579 83 -284 -144 O
ATOM 588 CB CYS A 77 -30.702 12.115 23.733 1.00 30.57 C
ANISOU 588 CB CYS A 77 3658 4696 3260 124 -347 -191 C
ATOM 589 SG CYS A 77 -29.260 12.248 22.695 1.00 34.87 S
ANISOU 589 SG CYS A 77 4222 5189 3839 126 -332 -169 S
ATOM 590 N LEU A 78 -29.899 9.520 25.332 1.00 25.94 N
ANISOU 590 N LEU A 78 3070 4118 2666 98 -311 -159 N
ATOM 591 CA LEU A 78 -28.952 8.541 25.810 1.00 24.56 C
ANISOU 591 CA LEU A 78 2901 3929 2504 89 -295 -139 C
ATOM 592 C LEU A 78 -29.358 7.145 25.397 1.00 23.28 C
ANISOU 592 C LEU A 78 2752 3769 2323 66 -273 -128 C
ATOM 593 O LEU A 78 -28.531 6.395 24.981 1.00 22.76 O
ANISOU 593 O LEU A 78 2701 3676 2272 57 -254 -110 O
ATOM 594 CB LEU A 78 -28.798 8.594 27.349 1.00 24.10 C
ANISOU 594 CB LEU A 78 2823 3892 2444 97 -309 -143 C
ATOM 595 CG LEU A 78 -27.792 9.538 27.949 1.00 25.09 C
ANISOU 595 CG LEU A 78 2938 3999 2595 117 -326 -143 C
ATOM 596 CD1 LEU A 78 -27.842 9.572 29.464 1.00 25.25 C
ANISOU 596 CD1 LEU A 78 2940 4044 2609 124 -341 -149 C
ATOM 597 CD2 LEU A 78 -26.401 9.283 27.448 1.00 24.17 C
ANISOU 597 CD2 LEU A 78 2835 3839 2512 116 -311 -122 C
ATOM 598 N PHE A 79 -30.632 6.812 25.506 1.00 23.77 N
ANISOU 598 N PHE A 79 2810 3865 2356 57 -275 -139 N
ATOM 599 CA PHE A 79 -31.086 5.492 25.155 1.00 24.69 C
ANISOU 599 CA PHE A 79 2940 3987 2456 35 -257 -128 C
ATOM 600 C PHE A 79 -30.856 5.207 23.676 1.00 23.10 C
ANISOU 600 C PHE A 79 2763 3753 2263 29 -240 -118 C
ATOM 601 O PHE A 79 -30.366 4.201 23.333 1.00 22.85 O
ANISOU 601 O PHE A 79 2746 3703 2234 16 -222 -101 O
ATOM 602 CB PHE A 79 -32.540 5.228 25.539 1.00 26.71 C
ANISOU 602 CB PHE A 79 3186 4284 2678 27 -263 -142 C
ATOM 603 CG PHE A 79 -32.983 3.831 25.252 1.00 28.49 C
ANISOU 603 CG PHE A 79 3423 4514 2886 4 -246 -129 C
ATOM 604 CD1 PHE A 79 -32.659 2.809 26.089 1.00 30.36 C
ANISOU 604 CD1 PHE A 79 3658 4759 3118 -8 -240 -117 C
ATOM 605 CD2 PHE A 79 -33.677 3.535 24.123 1.00 29.14 C
ANISOU 605 CD2 PHE A 79 3522 4592 2959 -4 -238 -129 C
ATOM 606 CE1 PHE A 79 -33.043 1.530 25.828 1.00 31.05 C
ANISOU 606 CE1 PHE A 79 3756 4850 3190 -29 -226 -105 C
ATOM 607 CE2 PHE A 79 -34.065 2.258 23.844 1.00 29.91 C
ANISOU 607 CE2 PHE A 79 3631 4692 3041 -24 -225 -116 C
ATOM 608 CZ PHE A 79 -33.745 1.251 24.699 1.00 30.78 C
ANISOU 608 CZ PHE A 79 3738 4812 3146 -36 -219 -104 C
ATOM 609 N ILE A 80 -31.257 6.148 22.852 1.00 23.17 N
ANISOU 609 N ILE A 80 2776 3756 2273 38 -248 -129 N
ATOM 610 CA ILE A 80 -31.087 6.128 21.400 1.00 23.91 C
ANISOU 610 CA ILE A 80 2892 3818 2374 35 -235 -122 C
ATOM 611 C ILE A 80 -29.586 5.987 21.048 1.00 20.89 C
ANISOU 611 C ILE A 80 2521 3395 2021 38 -220 -103 C
ATOM 612 O ILE A 80 -29.251 5.314 20.138 1.00 20.77 O
ANISOU 612 O ILE A 80 2525 3356 2009 28 -201 -89 O
ATOM 613 CB ILE A 80 -31.649 7.429 20.796 1.00 27.21 C
ANISOU 613 CB ILE A 80 3309 4237 2792 47 -252 -141 C
ATOM 614 CG1 ILE A 80 -33.157 7.477 20.874 1.00 31.44 C
ANISOU 614 CG1 ILE A 80 3838 4807 3300 43 -263 -159 C
ATOM 615 CG2 ILE A 80 -31.199 7.667 19.398 1.00 28.32 C
ANISOU 615 CG2 ILE A 80 3472 4340 2947 48 -241 -133 C
ATOM 616 CD1 ILE A 80 -33.833 6.271 20.350 1.00 33.99 C
ANISOU 616 CD1 ILE A 80 4177 5134 3605 24 -247 -150 C
ATOM 617 N ALA A 81 -28.720 6.658 21.785 1.00 19.59 N
ANISOU 617 N ALA A 81 2341 3224 1876 51 -230 -103 N
ATOM 618 CA ALA A 81 -27.300 6.602 21.591 1.00 19.72 C
ANISOU 618 CA ALA A 81 2365 3204 1923 55 -219 -86 C
ATOM 619 C ALA A 81 -26.642 5.277 22.008 1.00 18.90 C
ANISOU 619 C ALA A 81 2267 3093 1823 42 -201 -68 C
ATOM 620 O ALA A 81 -25.870 4.765 21.285 1.00 19.32 O
ANISOU 620 O ALA A 81 2335 3116 1890 37 -183 -53 O
ATOM 621 CB ALA A 81 -26.634 7.776 22.259 1.00 20.07 C
ANISOU 621 CB ALA A 81 2392 3244 1988 75 -238 -92 C
ATOM 622 N CYS A 82 -27.034 4.735 23.155 1.00 18.59 N
ANISOU 622 N CYS A 82 2214 3081 1768 36 -208 -72 N
ATOM 623 CA CYS A 82 -26.438 3.562 23.758 1.00 18.58 C
ANISOU 623 CA CYS A 82 2215 3075 1770 24 -196 -57 C
ATOM 624 C CYS A 82 -27.016 2.193 23.521 1.00 18.94 C
ANISOU 624 C CYS A 82 2273 3130 1794 3 -183 -49 C
ATOM 625 O CYS A 82 -26.384 1.243 23.875 1.00 19.05 O
ANISOU 625 O CYS A 82 2290 3133 1813 -7 -173 -36 O
ATOM 626 CB CYS A 82 -26.333 3.760 25.288 1.00 20.11 C
ANISOU 626 CB CYS A 82 2388 3289 1964 29 -213 -64 C
ATOM 627 SG CYS A 82 -25.466 5.215 25.814 1.00 24.91 S
ANISOU 627 SG CYS A 82 2980 3883 2601 55 -232 -70 S
ATOM 628 N PHE A 83 -28.216 2.113 22.986 1.00 19.28 N
ANISOU 628 N PHE A 83 2321 3194 1812 -4 -184 -57 N
ATOM 629 CA PHE A 83 -28.814 0.829 22.772 1.00 20.44 C
ANISOU 629 CA PHE A 83 2478 3350 1937 -23 -173 -49 C
ATOM 630 C PHE A 83 -27.934 -0.105 21.934 1.00 20.11 C
ANISOU 630 C PHE A 83 2459 3274 1909 -32 -152 -30 C
ATOM 631 O PHE A 83 -27.842 -1.227 22.251 1.00 20.69 O
ANISOU 631 O PHE A 83 2536 3350 1975 -46 -146 -19 O
ATOM 632 CB PHE A 83 -30.245 0.875 22.271 1.00 21.01 C
ANISOU 632 CB PHE A 83 2553 3447 1982 -28 -178 -60 C
ATOM 633 CG PHE A 83 -30.877 -0.478 22.155 1.00 22.48 C
ANISOU 633 CG PHE A 83 2749 3644 2146 -49 -169 -51 C
ATOM 634 CD1 PHE A 83 -31.136 -1.242 23.272 1.00 24.10 C
ANISOU 634 CD1 PHE A 83 2944 3877 2338 -60 -174 -48 C
ATOM 635 CD2 PHE A 83 -31.158 -1.019 20.934 1.00 21.71 C
ANISOU 635 CD2 PHE A 83 2675 3531 2044 -56 -157 -43 C
ATOM 636 CE1 PHE A 83 -31.706 -2.484 23.168 1.00 24.94 C
ANISOU 636 CE1 PHE A 83 3059 3994 2424 -79 -168 -38 C
ATOM 637 CE2 PHE A 83 -31.730 -2.261 20.824 1.00 22.82 C
ANISOU 637 CE2 PHE A 83 2824 3681 2164 -74 -151 -33 C
ATOM 638 CZ PHE A 83 -31.996 -3.003 21.942 1.00 24.06 C
ANISOU 638 CZ PHE A 83 2969 3865 2307 -86 -157 -30 C
ATOM 639 N VAL A 84 -27.218 0.435 20.959 1.00 18.87 N
ANISOU 639 N VAL A 84 2314 3084 1773 -22 -143 -25 N
ATOM 640 CA VAL A 84 -26.310 -0.337 20.119 1.00 17.72 C
ANISOU 640 CA VAL A 84 2188 2903 1642 -28 -123 -8 C
ATOM 641 C VAL A 84 -25.156 -0.995 20.936 1.00 17.21 C
ANISOU 641 C VAL A 84 2117 2825 1596 -32 -118 4 C
ATOM 642 O VAL A 84 -24.675 -2.022 20.607 1.00 16.38 O
ANISOU 642 O VAL A 84 2026 2704 1494 -42 -105 17 O
ATOM 643 CB VAL A 84 -25.765 0.491 18.937 1.00 16.60 C
ANISOU 643 CB VAL A 84 2058 2730 1519 -16 -114 -7 C
ATOM 644 CG1 VAL A 84 -24.998 1.691 19.383 1.00 16.33 C
ANISOU 644 CG1 VAL A 84 2008 2686 1509 1 -124 -12 C
ATOM 645 CG2 VAL A 84 -24.988 -0.369 17.970 1.00 16.75 C
ANISOU 645 CG2 VAL A 84 2100 2717 1549 -23 -92 11 C
ATOM 646 N LEU A 85 -24.772 -0.335 22.012 1.00 16.25 N
ANISOU 646 N LEU A 85 1977 2712 1487 -22 -132 -3 N
ATOM 647 CA LEU A 85 -23.761 -0.807 22.919 1.00 16.18 C
ANISOU 647 CA LEU A 85 1961 2692 1496 -24 -132 6 C
ATOM 648 C LEU A 85 -24.270 -2.051 23.642 1.00 16.04 C
ANISOU 648 C LEU A 85 1943 2696 1455 -43 -134 9 C
ATOM 649 O LEU A 85 -23.537 -2.925 23.916 1.00 16.18 O
ANISOU 649 O LEU A 85 1965 2699 1482 -52 -128 20 O
ATOM 650 CB LEU A 85 -23.359 0.276 23.893 1.00 17.22 C
ANISOU 650 CB LEU A 85 2072 2827 1643 -8 -149 -3 C
ATOM 651 CG LEU A 85 -22.902 1.568 23.256 1.00 18.51 C
ANISOU 651 CG LEU A 85 2235 2971 1828 10 -151 -7 C
ATOM 652 CD1 LEU A 85 -22.537 2.645 24.235 1.00 17.68 C
ANISOU 652 CD1 LEU A 85 2109 2869 1738 27 -170 -15 C
ATOM 653 CD2 LEU A 85 -21.809 1.323 22.258 1.00 19.09 C
ANISOU 653 CD2 LEU A 85 2323 3003 1926 11 -131 8 C
ATOM 654 N VAL A 86 -25.554 -2.098 23.920 1.00 15.63 N
ANISOU 654 N VAL A 86 1885 2680 1373 -49 -143 -1 N
ATOM 655 CA VAL A 86 -26.152 -3.263 24.530 1.00 16.74 C
ANISOU 655 CA VAL A 86 2026 2845 1491 -68 -145 3 C
ATOM 656 C VAL A 86 -26.029 -4.444 23.557 1.00 16.69 C
ANISOU 656 C VAL A 86 2041 2819 1480 -83 -129 18 C
ATOM 657 O VAL A 86 -25.608 -5.495 23.897 1.00 17.47 O
ANISOU 657 O VAL A 86 2145 2913 1579 -96 -126 29 O
ATOM 658 CB VAL A 86 -27.631 -3.049 24.855 1.00 18.62 C
ANISOU 658 CB VAL A 86 2253 3124 1696 -72 -157 -10 C
ATOM 659 CG1 VAL A 86 -28.262 -4.329 25.340 1.00 20.01 C
ANISOU 659 CG1 VAL A 86 2431 3323 1848 -93 -158 -3 C
ATOM 660 CG2 VAL A 86 -27.831 -1.898 25.811 1.00 18.35 C
ANISOU 660 CG2 VAL A 86 2198 3111 1664 -57 -174 -26 C
ATOM 661 N LEU A 87 -26.382 -4.193 22.313 1.00 16.24 N
ANISOU 661 N LEU A 87 1999 2752 1420 -79 -121 18 N
ATOM 662 CA LEU A 87 -26.317 -5.204 21.283 1.00 16.50 C
ANISOU 662 CA LEU A 87 2054 2766 1448 -89 -106 31 C
ATOM 663 C LEU A 87 -24.873 -5.692 21.063 1.00 16.49 C
ANISOU 663 C LEU A 87 2062 2728 1475 -89 -93 45 C
ATOM 664 O LEU A 87 -24.649 -6.853 20.961 1.00 18.33 O
ANISOU 664 O LEU A 87 2306 2954 1704 -102 -87 56 O
ATOM 665 CB LEU A 87 -27.008 -4.734 19.991 1.00 16.30 C
ANISOU 665 CB LEU A 87 2043 2735 1414 -84 -100 28 C
ATOM 666 CG LEU A 87 -28.493 -4.352 20.042 1.00 17.32 C
ANISOU 666 CG LEU A 87 2165 2899 1517 -85 -112 14 C
ATOM 667 CD1 LEU A 87 -29.043 -3.956 18.685 1.00 16.24 C
ANISOU 667 CD1 LEU A 87 2045 2749 1374 -80 -106 12 C
ATOM 668 CD2 LEU A 87 -29.352 -5.409 20.688 1.00 17.03 C
ANISOU 668 CD2 LEU A 87 2125 2892 1454 -103 -119 17 C
ATOM 669 N ALA A 88 -23.923 -4.785 21.000 1.00 14.75 N
ANISOU 669 N ALA A 88 1837 2486 1283 -73 -90 43 N
ATOM 670 CA ALA A 88 -22.541 -5.136 20.815 1.00 15.17 C
ANISOU 670 CA ALA A 88 1897 2504 1365 -71 -78 55 C
ATOM 671 C ALA A 88 -22.039 -5.959 22.001 1.00 16.06 C
ANISOU 671 C ALA A 88 2001 2620 1481 -82 -85 59 C
ATOM 672 O ALA A 88 -21.348 -6.911 21.811 1.00 17.41 O
ANISOU 672 O ALA A 88 2182 2771 1661 -91 -76 70 O
ATOM 673 CB ALA A 88 -21.675 -3.915 20.643 1.00 14.20 C
ANISOU 673 CB ALA A 88 1766 2357 1270 -53 -75 52 C
ATOM 674 N GLN A 89 -22.406 -5.555 23.207 1.00 15.47 N
ANISOU 674 N GLN A 89 1908 2571 1400 -81 -102 50 N
ATOM 675 CA GLN A 89 -21.985 -6.261 24.406 1.00 15.38 C
ANISOU 675 CA GLN A 89 1888 2564 1392 -92 -111 53 C
ATOM 676 C GLN A 89 -22.501 -7.691 24.450 1.00 17.67 C
ANISOU 676 C GLN A 89 2189 2867 1658 -114 -111 60 C
ATOM 677 O GLN A 89 -21.783 -8.561 24.790 1.00 18.43 O
ANISOU 677 O GLN A 89 2290 2949 1764 -123 -110 68 O
ATOM 678 CB GLN A 89 -22.337 -5.521 25.669 1.00 13.99 C
ANISOU 678 CB GLN A 89 1691 2413 1211 -86 -129 41 C
ATOM 679 CG GLN A 89 -21.452 -5.900 26.833 1.00 17.50 C
ANISOU 679 CG GLN A 89 2129 2849 1672 -90 -137 44 C
ATOM 680 CD GLN A 89 -19.989 -5.650 26.575 1.00 18.83 C
ANISOU 680 CD GLN A 89 2300 2974 1880 -79 -129 51 C
ATOM 681 OE1 GLN A 89 -19.613 -4.632 26.129 1.00 18.14 O
ANISOU 681 OE1 GLN A 89 2209 2871 1810 -62 -125 48 O
ATOM 682 NE2 GLN A 89 -19.192 -6.604 26.874 1.00 20.90 N
ANISOU 682 NE2 GLN A 89 2569 3218 2155 -90 -126 60 N
ATOM 683 N SER A 90 -23.755 -7.885 24.079 1.00 17.54 N
ANISOU 683 N SER A 90 2175 2877 1611 -120 -113 57 N
ATOM 684 CA SER A 90 -24.370 -9.182 24.022 1.00 18.62 C
ANISOU 684 CA SER A 90 2323 3028 1724 -141 -114 65 C
ATOM 685 C SER A 90 -23.642 -10.079 23.040 1.00 18.51 C
ANISOU 685 C SER A 90 2330 2982 1721 -145 -100 79 C
ATOM 686 O SER A 90 -23.435 -11.213 23.305 1.00 18.87 O
ANISOU 686 O SER A 90 2383 3026 1763 -161 -103 87 O
ATOM 687 CB SER A 90 -25.851 -9.061 23.720 1.00 20.76 C
ANISOU 687 CB SER A 90 2593 3332 1964 -144 -119 59 C
ATOM 688 OG SER A 90 -26.435 -10.274 23.424 1.00 22.13 O
ANISOU 688 OG SER A 90 2780 3514 2116 -162 -119 68 O
ATOM 689 N SER A 91 -23.276 -9.504 21.904 1.00 17.90 N
ANISOU 689 N SER A 91 2263 2880 1658 -132 -86 80 N
ATOM 690 CA SER A 91 -22.539 -10.185 20.884 1.00 18.21 C
ANISOU 690 CA SER A 91 2322 2887 1710 -133 -70 91 C
ATOM 691 C SER A 91 -21.203 -10.696 21.431 1.00 20.37 C
ANISOU 691 C SER A 91 2593 3136 2010 -136 -69 98 C
ATOM 692 O SER A 91 -20.856 -11.795 21.188 1.00 22.21 O
ANISOU 692 O SER A 91 2839 3357 2243 -147 -65 107 O
ATOM 693 CB SER A 91 -22.352 -9.280 19.674 1.00 18.29 C
ANISOU 693 CB SER A 91 2341 2876 1732 -116 -56 90 C
ATOM 694 OG SER A 91 -23.565 -8.996 19.074 1.00 20.85 O
ANISOU 694 OG SER A 91 2671 3219 2032 -116 -58 85 O
ATOM 695 N ILE A 92 -20.498 -9.862 22.177 1.00 19.39 N
ANISOU 695 N ILE A 92 2454 3005 1909 -125 -73 92 N
ATOM 696 CA ILE A 92 -19.232 -10.191 22.787 1.00 20.49 C
ANISOU 696 CA ILE A 92 2589 3120 2077 -126 -73 96 C
ATOM 697 C ILE A 92 -19.392 -11.379 23.745 1.00 21.53 C
ANISOU 697 C ILE A 92 2720 3266 2194 -147 -87 99 C
ATOM 698 O ILE A 92 -18.643 -12.268 23.717 1.00 21.79 O
ANISOU 698 O ILE A 92 2761 3279 2239 -155 -84 107 O
ATOM 699 CB ILE A 92 -18.614 -8.969 23.471 1.00 21.37 C
ANISOU 699 CB ILE A 92 2683 3223 2212 -110 -78 89 C
ATOM 700 CG1 ILE A 92 -18.041 -8.028 22.418 1.00 23.52 C
ANISOU 700 CG1 ILE A 92 2960 3470 2508 -92 -62 90 C
ATOM 701 CG2 ILE A 92 -17.568 -9.347 24.505 1.00 21.34 C
ANISOU 701 CG2 ILE A 92 2672 3203 2232 -115 -85 91 C
ATOM 702 CD1 ILE A 92 -17.929 -6.610 22.849 1.00 26.47 C
ANISOU 702 CD1 ILE A 92 3316 3846 2895 -75 -70 81 C
ATOM 703 N PHE A 93 -20.421 -11.343 24.559 1.00 21.52 N
ANISOU 703 N PHE A 93 2709 3301 2167 -155 -101 93 N
ATOM 704 CA PHE A 93 -20.701 -12.405 25.490 1.00 23.63 C
ANISOU 704 CA PHE A 93 2975 3586 2418 -175 -116 95 C
ATOM 705 C PHE A 93 -20.981 -13.714 24.724 1.00 23.54 C
ANISOU 705 C PHE A 93 2982 3572 2390 -190 -112 106 C
ATOM 706 O PHE A 93 -20.460 -14.723 25.047 1.00 23.84 O
ANISOU 706 O PHE A 93 3027 3600 2432 -204 -117 113 O
ATOM 707 CB PHE A 93 -21.850 -12.021 26.400 1.00 24.83 C
ANISOU 707 CB PHE A 93 3112 3779 2542 -179 -130 86 C
ATOM 708 CG PHE A 93 -21.489 -11.039 27.499 1.00 27.19 C
ANISOU 708 CG PHE A 93 3393 4083 2857 -168 -140 77 C
ATOM 709 CD1 PHE A 93 -20.280 -11.096 28.143 1.00 30.69 C
ANISOU 709 CD1 PHE A 93 3833 4499 3329 -166 -143 78 C
ATOM 710 CD2 PHE A 93 -22.383 -10.092 27.902 1.00 27.75 C
ANISOU 710 CD2 PHE A 93 3450 4183 2912 -159 -147 65 C
ATOM 711 CE1 PHE A 93 -19.979 -10.215 29.158 1.00 32.45 C
ANISOU 711 CE1 PHE A 93 4040 4725 3564 -155 -153 70 C
ATOM 712 CE2 PHE A 93 -22.091 -9.216 28.901 1.00 29.31 C
ANISOU 712 CE2 PHE A 93 3631 4385 3121 -148 -157 56 C
ATOM 713 CZ PHE A 93 -20.894 -9.279 29.538 1.00 30.60 C
ANISOU 713 CZ PHE A 93 3792 4521 3313 -146 -160 59 C
ATOM 714 N SER A 94 -21.796 -13.647 23.688 1.00 22.42 N
ANISOU 714 N SER A 94 2850 3438 2230 -187 -104 108 N
ATOM 715 CA SER A 94 -22.085 -14.803 22.863 1.00 23.94 C
ANISOU 715 CA SER A 94 3062 3626 2408 -199 -101 119 C
ATOM 716 C SER A 94 -20.821 -15.353 22.207 1.00 23.21 C
ANISOU 716 C SER A 94 2983 3494 2341 -196 -89 127 C
ATOM 717 O SER A 94 -20.599 -16.509 22.214 1.00 24.11 O
ANISOU 717 O SER A 94 3108 3602 2451 -210 -94 135 O
ATOM 718 CB SER A 94 -23.111 -14.492 21.806 1.00 25.69 C
ANISOU 718 CB SER A 94 3293 3858 2609 -193 -94 119 C
ATOM 719 OG SER A 94 -24.372 -14.359 22.343 1.00 29.06 O
ANISOU 719 OG SER A 94 3710 4323 3008 -201 -106 113 O
ATOM 720 N LEU A 95 -20.007 -14.488 21.650 1.00 21.83 N
ANISOU 720 N LEU A 95 2808 3293 2193 -178 -74 125 N
ATOM 721 CA LEU A 95 -18.766 -14.892 21.040 1.00 22.45 C
ANISOU 721 CA LEU A 95 2898 3333 2298 -174 -61 131 C
ATOM 722 C LEU A 95 -17.851 -15.596 22.051 1.00 23.39 C
ANISOU 722 C LEU A 95 3011 3441 2435 -185 -72 133 C
ATOM 723 O LEU A 95 -17.285 -16.593 21.752 1.00 24.32 O
ANISOU 723 O LEU A 95 3140 3541 2558 -192 -70 140 O
ATOM 724 CB LEU A 95 -18.069 -13.717 20.409 1.00 21.55 C
ANISOU 724 CB LEU A 95 2781 3196 2210 -153 -44 128 C
ATOM 725 CG LEU A 95 -18.683 -13.243 19.101 1.00 22.14 C
ANISOU 725 CG LEU A 95 2869 3270 2273 -143 -30 129 C
ATOM 726 CD1 LEU A 95 -18.191 -11.886 18.682 1.00 22.01 C
ANISOU 726 CD1 LEU A 95 2846 3238 2279 -124 -18 125 C
ATOM 727 CD2 LEU A 95 -18.510 -14.260 18.019 1.00 21.81 C
ANISOU 727 CD2 LEU A 95 2850 3211 2227 -147 -19 140 C
ATOM 728 N LEU A 96 -17.737 -15.039 23.235 1.00 22.59 N
ANISOU 728 N LEU A 96 2892 3350 2340 -184 -83 125 N
ATOM 729 CA LEU A 96 -16.933 -15.627 24.280 1.00 24.40 C
ANISOU 729 CA LEU A 96 3116 3569 2586 -195 -95 125 C
ATOM 730 C LEU A 96 -17.461 -17.001 24.700 1.00 25.24 C
ANISOU 730 C LEU A 96 3230 3692 2667 -219 -111 130 C
ATOM 731 O LEU A 96 -16.711 -17.919 24.912 1.00 26.29 O
ANISOU 731 O LEU A 96 3370 3807 2812 -229 -117 134 O
ATOM 732 CB LEU A 96 -16.862 -14.701 25.473 1.00 25.43 C
ANISOU 732 CB LEU A 96 3227 3709 2725 -189 -106 116 C
ATOM 733 CG LEU A 96 -15.921 -15.031 26.627 1.00 28.02 C
ANISOU 733 CG LEU A 96 3548 4021 3075 -196 -119 115 C
ATOM 734 CD1 LEU A 96 -14.563 -15.487 26.176 1.00 27.89 C
ANISOU 734 CD1 LEU A 96 3541 3964 3094 -193 -109 120 C
ATOM 735 CD2 LEU A 96 -15.871 -13.889 27.616 1.00 28.07 C
ANISOU 735 CD2 LEU A 96 3537 4036 3093 -185 -127 106 C
ATOM 736 N ALA A 97 -18.764 -17.109 24.809 1.00 24.84 N
ANISOU 736 N ALA A 97 3178 3677 2582 -227 -119 130 N
ATOM 737 CA ALA A 97 -19.402 -18.340 25.171 1.00 26.75 C
ANISOU 737 CA ALA A 97 3427 3939 2798 -249 -135 136 C
ATOM 738 C ALA A 97 -19.103 -19.434 24.142 1.00 27.52 C
ANISOU 738 C ALA A 97 3545 4016 2894 -255 -130 146 C
ATOM 739 O ALA A 97 -18.809 -20.526 24.479 1.00 28.49 O
ANISOU 739 O ALA A 97 3675 4135 3016 -271 -143 151 O
ATOM 740 CB ALA A 97 -20.885 -18.144 25.319 1.00 26.70 C
ANISOU 740 CB ALA A 97 3415 3974 2756 -255 -142 134 C
ATOM 741 N ILE A 98 -19.171 -19.091 22.877 1.00 26.78 N
ANISOU 741 N ILE A 98 3462 3911 2803 -241 -112 149 N
ATOM 742 CA ILE A 98 -18.901 -20.033 21.815 1.00 26.84 C
ANISOU 742 CA ILE A 98 3490 3899 2810 -243 -106 158 C
ATOM 743 C ILE A 98 -17.462 -20.515 21.883 1.00 28.13 C
ANISOU 743 C ILE A 98 3657 4028 3005 -243 -103 159 C
ATOM 744 O ILE A 98 -17.231 -21.662 21.738 1.00 29.63 O
ANISOU 744 O ILE A 98 3859 4209 3191 -254 -111 166 O
ATOM 745 CB ILE A 98 -19.256 -19.449 20.440 1.00 26.35 C
ANISOU 745 CB ILE A 98 3439 3830 2743 -226 -87 160 C
ATOM 746 CG1 ILE A 98 -20.756 -19.337 20.317 1.00 27.18 C
ANISOU 746 CG1 ILE A 98 3544 3969 2814 -231 -94 160 C
ATOM 747 CG2 ILE A 98 -18.687 -20.299 19.333 1.00 26.91 C
ANISOU 747 CG2 ILE A 98 3531 3873 2820 -224 -77 169 C
ATOM 748 CD1 ILE A 98 -21.258 -18.430 19.250 1.00 28.09 C
ANISOU 748 CD1 ILE A 98 3666 4082 2926 -214 -78 158 C
ATOM 749 N ALA A 99 -16.517 -19.635 22.148 1.00 27.62 N
ANISOU 749 N ALA A 99 3581 3942 2971 -229 -93 153 N
ATOM 750 CA ALA A 99 -15.135 -20.029 22.241 1.00 28.97 C
ANISOU 750 CA ALA A 99 3754 4078 3175 -228 -90 154 C
ATOM 751 C ALA A 99 -14.919 -21.001 23.386 1.00 31.51 C
ANISOU 751 C ALA A 99 4073 4404 3495 -249 -114 153 C
ATOM 752 O ALA A 99 -14.247 -21.975 23.234 1.00 32.22 O
ANISOU 752 O ALA A 99 4172 4474 3594 -257 -119 156 O
ATOM 753 CB ALA A 99 -14.226 -18.843 22.374 1.00 27.91 C
ANISOU 753 CB ALA A 99 3607 3923 3075 -210 -77 148 C
ATOM 754 N ILE A 100 -15.540 -20.709 24.514 1.00 32.04 N
ANISOU 754 N ILE A 100 4127 4499 3549 -258 -129 148 N
ATOM 755 CA ILE A 100 -15.442 -21.538 25.700 1.00 33.47 C
ANISOU 755 CA ILE A 100 4305 4686 3725 -279 -153 147 C
ATOM 756 C ILE A 100 -16.091 -22.900 25.491 1.00 34.44 C
ANISOU 756 C ILE A 100 4442 4824 3819 -299 -168 155 C
ATOM 757 O ILE A 100 -15.571 -23.881 25.895 1.00 34.42 O
ANISOU 757 O ILE A 100 4445 4810 3822 -314 -182 157 O
ATOM 758 CB ILE A 100 -15.980 -20.839 26.955 1.00 33.78 C
ANISOU 758 CB ILE A 100 4327 4752 3755 -282 -165 140 C
ATOM 759 CG1 ILE A 100 -15.126 -19.631 27.294 1.00 34.65 C
ANISOU 759 CG1 ILE A 100 4424 4841 3899 -263 -155 132 C
ATOM 760 CG2 ILE A 100 -15.978 -21.778 28.136 1.00 33.98 C
ANISOU 760 CG2 ILE A 100 4352 4787 3772 -306 -190 140 C
ATOM 761 CD1 ILE A 100 -15.708 -18.771 28.350 1.00 35.35 C
ANISOU 761 CD1 ILE A 100 4497 4956 3978 -261 -164 125 C
ATOM 762 N ASP A 101 -17.230 -22.904 24.839 1.00 34.47 N
ANISOU 762 N ASP A 101 4451 4853 3793 -299 -164 160 N
ATOM 763 CA ASP A 101 -17.942 -24.091 24.535 1.00 36.03 C
ANISOU 763 CA ASP A 101 4662 5065 3963 -315 -178 169 C
ATOM 764 C ASP A 101 -17.080 -25.015 23.682 1.00 37.03 C
ANISOU 764 C ASP A 101 4806 5160 4104 -315 -175 175 C
ATOM 765 O ASP A 101 -16.995 -26.161 23.944 1.00 37.85 O
ANISOU 765 O ASP A 101 4918 5263 4200 -332 -193 179 O
ATOM 766 CB ASP A 101 -19.254 -23.743 23.864 1.00 37.07 C
ANISOU 766 CB ASP A 101 4797 5224 4065 -311 -172 173 C
ATOM 767 CG ASP A 101 -20.037 -24.940 23.493 1.00 42.27 C
ANISOU 767 CG ASP A 101 5470 5898 4695 -327 -186 183 C
ATOM 768 OD1 ASP A 101 -20.679 -25.509 24.339 1.00 44.14 O
ANISOU 768 OD1 ASP A 101 5701 6160 4910 -346 -207 186 O
ATOM 769 OD2 ASP A 101 -19.991 -25.335 22.358 1.00 44.02 O
ANISOU 769 OD2 ASP A 101 5707 6104 4915 -320 -178 190 O
ATOM 770 N ARG A 102 -16.411 -24.481 22.681 1.00 37.35 N
ANISOU 770 N ARG A 102 4851 5173 4166 -294 -152 174 N
ATOM 771 CA ARG A 102 -15.552 -25.251 21.820 1.00 39.00 C
ANISOU 771 CA ARG A 102 5076 5352 4390 -291 -146 178 C
ATOM 772 C ARG A 102 -14.286 -25.728 22.550 1.00 41.20 C
ANISOU 772 C ARG A 102 5352 5605 4699 -298 -155 174 C
ATOM 773 O ARG A 102 -13.780 -26.769 22.256 1.00 42.29 O
ANISOU 773 O ARG A 102 5501 5726 4841 -305 -163 177 O
ATOM 774 CB ARG A 102 -15.246 -24.497 20.529 1.00 39.49 C
ANISOU 774 CB ARG A 102 5145 5394 4465 -267 -117 179 C
ATOM 775 CG ARG A 102 -16.424 -24.351 19.578 1.00 41.51 C
ANISOU 775 CG ARG A 102 5412 5670 4692 -262 -110 185 C
ATOM 776 CD ARG A 102 -16.978 -25.678 19.074 1.00 44.94 C
ANISOU 776 CD ARG A 102 5865 6110 5101 -274 -125 195 C
ATOM 777 NE ARG A 102 -18.005 -26.257 19.939 1.00 47.51 N
ANISOU 777 NE ARG A 102 6186 6469 5397 -295 -150 198 N
ATOM 778 CZ ARG A 102 -18.232 -27.552 20.089 1.00 51.12 C
ANISOU 778 CZ ARG A 102 6653 6932 5838 -313 -173 206 C
ATOM 779 NH1 ARG A 102 -17.532 -28.426 19.423 1.00 52.57 N
ANISOU 779 NH1 ARG A 102 6853 7091 6031 -312 -174 210 N
ATOM 780 NH2 ARG A 102 -19.164 -27.978 20.892 1.00 51.20 N
ANISOU 780 NH2 ARG A 102 6658 6974 5822 -332 -195 209 N
ATOM 781 N TYR A 103 -13.796 -24.951 23.495 1.00 41.90 N
ANISOU 781 N TYR A 103 5423 5688 4807 -296 -155 165 N
ATOM 782 CA TYR A 103 -12.664 -25.348 24.283 1.00 44.56 C
ANISOU 782 CA TYR A 103 5756 6001 5173 -303 -166 160 C
ATOM 783 C TYR A 103 -13.047 -26.531 25.187 1.00 45.36 C
ANISOU 783 C TYR A 103 5861 6118 5254 -330 -198 162 C
ATOM 784 O TYR A 103 -12.294 -27.436 25.380 1.00 45.97 O
ANISOU 784 O TYR A 103 5945 6175 5345 -341 -211 161 O
ATOM 785 CB TYR A 103 -12.125 -24.218 25.142 1.00 45.84 C
ANISOU 785 CB TYR A 103 5900 6155 5361 -294 -162 152 C
ATOM 786 CG TYR A 103 -10.958 -24.670 25.966 1.00 49.71 C
ANISOU 786 CG TYR A 103 6388 6618 5882 -302 -175 146 C
ATOM 787 CD1 TYR A 103 -9.795 -25.036 25.373 1.00 52.22 C
ANISOU 787 CD1 TYR A 103 6712 6899 6230 -295 -166 146 C
ATOM 788 CD2 TYR A 103 -11.058 -24.821 27.316 1.00 52.08 C
ANISOU 788 CD2 TYR A 103 6681 6929 6179 -318 -197 142 C
ATOM 789 CE1 TYR A 103 -8.731 -25.486 26.099 1.00 54.58 C
ANISOU 789 CE1 TYR A 103 7010 7171 6558 -304 -179 140 C
ATOM 790 CE2 TYR A 103 -10.001 -25.274 28.061 1.00 54.52 C
ANISOU 790 CE2 TYR A 103 6989 7210 6517 -327 -211 136 C
ATOM 791 CZ TYR A 103 -8.833 -25.596 27.440 1.00 56.43 C
ANISOU 791 CZ TYR A 103 7236 7414 6790 -319 -202 135 C
ATOM 792 OH TYR A 103 -7.766 -26.046 28.152 1.00 60.26 O
ANISOU 792 OH TYR A 103 7721 7870 7306 -328 -216 129 O
ATOM 793 N ILE A 104 -14.237 -26.504 25.735 1.00 45.33 N
ANISOU 793 N ILE A 104 5854 6152 5219 -342 -210 164 N
ATOM 794 CA ILE A 104 -14.678 -27.587 26.581 1.00 47.15 C
ANISOU 794 CA ILE A 104 6088 6401 5428 -369 -239 167 C
ATOM 795 C ILE A 104 -14.855 -28.867 25.769 1.00 48.49 C
ANISOU 795 C ILE A 104 6276 6568 5581 -378 -249 176 C
ATOM 796 O ILE A 104 -14.509 -29.926 26.216 1.00 49.66 O
ANISOU 796 O ILE A 104 6430 6708 5730 -397 -272 177 O
ATOM 797 CB ILE A 104 -15.931 -27.225 27.367 1.00 47.89 C
ANISOU 797 CB ILE A 104 6171 6536 5489 -379 -249 167 C
ATOM 798 CG1 ILE A 104 -15.629 -26.107 28.349 1.00 48.08 C
ANISOU 798 CG1 ILE A 104 6177 6560 5530 -371 -244 157 C
ATOM 799 CG2 ILE A 104 -16.460 -28.433 28.115 1.00 49.81 C
ANISOU 799 CG2 ILE A 104 6419 6799 5707 -408 -279 172 C
ATOM 800 CD1 ILE A 104 -16.839 -25.468 28.931 1.00 48.40 C
ANISOU 800 CD1 ILE A 104 6206 6641 5543 -374 -247 156 C
ATOM 801 N ALA A 105 -15.341 -28.735 24.552 1.00 48.54 N
ANISOU 801 N ALA A 105 6291 6577 5576 -365 -233 182 N
ATOM 802 CA ALA A 105 -15.526 -29.858 23.668 1.00 50.56 C
ANISOU 802 CA ALA A 105 6566 6829 5817 -370 -241 191 C
ATOM 803 C ALA A 105 -14.229 -30.527 23.287 1.00 53.33 C
ANISOU 803 C ALA A 105 6926 7142 6196 -367 -241 189 C
ATOM 804 O ALA A 105 -14.189 -31.713 23.178 1.00 54.77 O
ANISOU 804 O ALA A 105 7121 7321 6369 -381 -262 194 O
ATOM 805 CB ALA A 105 -16.263 -29.446 22.424 1.00 49.78 C
ANISOU 805 CB ALA A 105 6475 6738 5702 -353 -221 198 C
ATOM 806 N ILE A 106 -13.175 -29.770 23.074 1.00 54.43 N
ANISOU 806 N ILE A 106 7059 7253 6370 -349 -220 182 N
ATOM 807 CA ILE A 106 -11.922 -30.360 22.697 1.00 57.14 C
ANISOU 807 CA ILE A 106 7410 7559 6742 -346 -219 178 C
ATOM 808 C ILE A 106 -11.037 -30.816 23.862 1.00 59.10 C
ANISOU 808 C ILE A 106 7652 7791 7013 -361 -240 170 C
ATOM 809 O ILE A 106 -10.330 -31.775 23.735 1.00 60.48 O
ANISOU 809 O ILE A 106 7835 7945 7199 -368 -252 169 O
ATOM 810 CB ILE A 106 -11.140 -29.487 21.707 1.00 58.25 C
ANISOU 810 CB ILE A 106 7550 7673 6910 -319 -185 176 C
ATOM 811 CG1 ILE A 106 -10.053 -30.297 21.038 1.00 61.31 C
ANISOU 811 CG1 ILE A 106 7948 8026 7319 -314 -183 175 C
ATOM 812 CG2 ILE A 106 -10.450 -28.345 22.393 1.00 58.41 C
ANISOU 812 CG2 ILE A 106 7552 7681 6961 -309 -172 167 C
ATOM 813 CD1 ILE A 106 -9.831 -29.964 19.591 1.00 63.27 C
ANISOU 813 CD1 ILE A 106 8207 8260 7573 -292 -153 178 C
ATOM 814 N ALA A 107 -11.117 -30.153 24.998 1.00 59.41 N
ANISOU 814 N ALA A 107 7676 7841 7058 -367 -245 164 N
ATOM 815 CA ALA A 107 -10.297 -30.472 26.137 1.00 61.53 C
ANISOU 815 CA ALA A 107 7939 8092 7348 -381 -264 156 C
ATOM 816 C ALA A 107 -10.822 -31.648 26.927 1.00 64.02 C
ANISOU 816 C ALA A 107 8261 8426 7639 -410 -300 159 C
ATOM 817 O ALA A 107 -10.092 -32.544 27.276 1.00 65.52 O
ANISOU 817 O ALA A 107 8457 8595 7842 -424 -320 155 O
ATOM 818 CB ALA A 107 -10.172 -29.270 27.036 1.00 60.88 C
ANISOU 818 CB ALA A 107 7838 8012 7280 -374 -257 149 C
ATOM 819 N ILE A 108 -12.107 -31.640 27.205 1.00 64.43 N
ANISOU 819 N ILE A 108 8311 8516 7653 -421 -308 165 N
ATOM 820 CA ILE A 108 -12.724 -32.684 27.974 1.00 66.35 C
ANISOU 820 CA ILE A 108 8559 8781 7869 -449 -341 169 C
ATOM 821 C ILE A 108 -13.999 -33.191 27.358 1.00 67.09 C
ANISOU 821 C ILE A 108 8662 8908 7923 -455 -347 182 C
ATOM 822 O ILE A 108 -15.052 -33.005 27.888 1.00 66.73 O
ANISOU 822 O ILE A 108 8610 8896 7849 -466 -354 186 O
ATOM 823 CB ILE A 108 -13.043 -32.169 29.361 1.00 67.49 C
ANISOU 823 CB ILE A 108 8690 8944 8008 -462 -352 164 C
ATOM 824 CG1 ILE A 108 -13.772 -30.847 29.269 1.00 67.54 C
ANISOU 824 CG1 ILE A 108 8684 8973 8006 -444 -328 164 C
ATOM 825 CG2 ILE A 108 -11.786 -31.960 30.162 1.00 68.90 C
ANISOU 825 CG2 ILE A 108 8863 9090 8226 -462 -356 153 C
ATOM 826 CD1 ILE A 108 -14.277 -30.382 30.601 1.00 69.31 C
ANISOU 826 CD1 ILE A 108 8895 9222 8219 -456 -339 160 C
ATOM 827 N PRO A 109 -13.895 -33.873 26.227 1.00 68.45 N
ANISOU 827 N PRO A 109 8849 9067 8092 -449 -345 188 N
ATOM 828 CA PRO A 109 -15.051 -34.391 25.509 1.00 69.47 C
ANISOU 828 CA PRO A 109 8988 9222 8184 -453 -350 201 C
ATOM 829 C PRO A 109 -15.878 -35.431 26.257 1.00 72.11 C
ANISOU 829 C PRO A 109 9327 9584 8488 -482 -386 209 C
ATOM 830 O PRO A 109 -17.033 -35.574 25.963 1.00 72.07 O
ANISOU 830 O PRO A 109 9324 9608 8451 -487 -390 219 O
ATOM 831 CB PRO A 109 -14.444 -34.997 24.258 1.00 70.19 C
ANISOU 831 CB PRO A 109 9096 9286 8287 -440 -344 204 C
ATOM 832 CG PRO A 109 -13.033 -35.198 24.561 1.00 71.06 C
ANISOU 832 CG PRO A 109 9205 9360 8433 -439 -346 193 C
ATOM 833 CD PRO A 109 -12.650 -34.136 25.517 1.00 68.76 C
ANISOU 833 CD PRO A 109 8896 9067 8164 -436 -336 183 C
ATOM 834 N LEU A 110 -15.272 -36.150 27.195 1.00 74.30 N
ANISOU 834 N LEU A 110 9604 9851 8774 -503 -412 203 N
ATOM 835 CA LEU A 110 -15.954 -37.152 27.989 1.00 76.48 C
ANISOU 835 CA LEU A 110 9884 10152 9022 -534 -448 210 C
ATOM 836 C LEU A 110 -16.910 -36.517 28.963 1.00 76.93 C
ANISOU 836 C LEU A 110 9927 10246 9059 -544 -448 211 C
ATOM 837 O LEU A 110 -17.914 -37.092 29.275 1.00 77.87 O
ANISOU 837 O LEU A 110 10047 10395 9145 -563 -468 221 O
ATOM 838 CB LEU A 110 -14.942 -38.026 28.731 1.00 78.13 C
ANISOU 838 CB LEU A 110 10098 10337 9251 -552 -475 203 C
ATOM 839 CG LEU A 110 -14.015 -38.854 27.841 1.00 80.76 C
ANISOU 839 CG LEU A 110 10446 10635 9603 -546 -481 201 C
ATOM 840 CD1 LEU A 110 -12.944 -39.577 28.636 1.00 82.09 C
ANISOU 840 CD1 LEU A 110 10618 10777 9795 -563 -507 191 C
ATOM 841 CD2 LEU A 110 -14.771 -39.794 26.924 1.00 81.87 C
ANISOU 841 CD2 LEU A 110 10602 10790 9714 -549 -495 215 C
ATOM 842 N ARG A 111 -16.591 -35.322 29.428 1.00 76.15 N
ANISOU 842 N ARG A 111 9813 10143 8978 -531 -426 201 N
ATOM 843 CA ARG A 111 -17.443 -34.623 30.371 1.00 76.37 C
ANISOU 843 CA ARG A 111 9827 10205 8988 -538 -425 200 C
ATOM 844 C ARG A 111 -18.285 -33.462 29.801 1.00 73.82 C
ANISOU 844 C ARG A 111 9493 9902 8653 -516 -396 202 C
ATOM 845 O ARG A 111 -19.010 -32.831 30.532 1.00 73.49 O
ANISOU 845 O ARG A 111 9439 9889 8596 -520 -394 200 O
ATOM 846 CB ARG A 111 -16.602 -34.138 31.550 1.00 79.85 C
ANISOU 846 CB ARG A 111 10257 10630 9453 -542 -428 187 C
ATOM 847 CG ARG A 111 -16.043 -35.243 32.414 1.00 86.60 C
ANISOU 847 CG ARG A 111 11119 11472 10311 -569 -462 185 C
ATOM 848 CD ARG A 111 -15.255 -34.709 33.603 1.00 92.63 C
ANISOU 848 CD ARG A 111 11874 12219 11100 -572 -465 173 C
ATOM 849 NE ARG A 111 -14.661 -35.797 34.388 1.00 98.82 N
ANISOU 849 NE ARG A 111 12668 12988 11890 -599 -498 170 N
ATOM 850 CZ ARG A 111 -13.822 -35.644 35.420 1.00102.99 C
ANISOU 850 CZ ARG A 111 13195 13495 12443 -606 -509 158 C
ATOM 851 NH1 ARG A 111 -13.455 -34.441 35.813 1.00102.84 N
ANISOU 851 NH1 ARG A 111 13163 13467 12445 -588 -488 150 N
ATOM 852 NH2 ARG A 111 -13.349 -36.706 36.059 1.00104.32 N
ANISOU 852 NH2 ARG A 111 13373 13649 12614 -632 -541 156 N
ATOM 853 N TYR A 112 -18.193 -33.214 28.497 1.00 71.66 N
ANISOU 853 N TYR A 112 9227 9614 8386 -494 -375 205 N
ATOM 854 CA TYR A 112 -18.918 -32.131 27.840 1.00 69.57 C
ANISOU 854 CA TYR A 112 8955 9365 8113 -473 -348 206 C
ATOM 855 C TYR A 112 -20.422 -32.221 27.978 1.00 69.78 C
ANISOU 855 C TYR A 112 8978 9435 8101 -484 -356 215 C
ATOM 856 O TYR A 112 -21.065 -31.295 28.430 1.00 68.90 O
ANISOU 856 O TYR A 112 8853 9347 7980 -480 -346 211 O
ATOM 857 CB TYR A 112 -18.542 -32.018 26.354 1.00 67.92 C
ANISOU 857 CB TYR A 112 8758 9130 7917 -450 -327 209 C
ATOM 858 CG TYR A 112 -19.287 -30.929 25.606 1.00 66.32 C
ANISOU 858 CG TYR A 112 8551 8942 7706 -429 -301 209 C
ATOM 859 CD1 TYR A 112 -18.792 -29.659 25.511 1.00 65.83 C
ANISOU 859 CD1 TYR A 112 8479 8867 7668 -407 -275 200 C
ATOM 860 CD2 TYR A 112 -20.486 -31.186 25.014 1.00 66.69 C
ANISOU 860 CD2 TYR A 112 8604 9013 7722 -431 -304 219 C
ATOM 861 CE1 TYR A 112 -19.485 -28.668 24.864 1.00 65.59 C
ANISOU 861 CE1 TYR A 112 8443 8848 7628 -389 -254 199 C
ATOM 862 CE2 TYR A 112 -21.190 -30.213 24.359 1.00 66.55 C
ANISOU 862 CE2 TYR A 112 8583 9007 7697 -413 -282 219 C
ATOM 863 CZ TYR A 112 -20.679 -28.951 24.282 1.00 66.43 C
ANISOU 863 CZ TYR A 112 8557 8978 7704 -392 -257 209 C
ATOM 864 OH TYR A 112 -21.391 -28.012 23.615 1.00 66.49 O
ANISOU 864 OH TYR A 112 8562 8997 7704 -376 -238 208 O
ATOM 865 N ASN A 113 -20.997 -33.351 27.607 1.00 70.91 N
ANISOU 865 N ASN A 113 9133 9588 8220 -499 -376 227 N
ATOM 866 CA ASN A 113 -22.444 -33.484 27.681 1.00 72.18 C
ANISOU 866 CA ASN A 113 9292 9789 8345 -510 -384 237 C
ATOM 867 C ASN A 113 -23.039 -33.283 29.071 1.00 72.99 C
ANISOU 867 C ASN A 113 9377 9924 8430 -530 -397 234 C
ATOM 868 O ASN A 113 -24.101 -32.734 29.200 1.00 73.48 O
ANISOU 868 O ASN A 113 9429 10018 8471 -528 -390 236 O
ATOM 869 CB ASN A 113 -22.918 -34.785 27.041 1.00 74.36 C
ANISOU 869 CB ASN A 113 9585 10068 8600 -523 -406 252 C
ATOM 870 CG ASN A 113 -22.830 -34.750 25.538 1.00 77.83 C
ANISOU 870 CG ASN A 113 10039 10487 9045 -500 -390 257 C
ATOM 871 OD1 ASN A 113 -23.051 -33.712 24.911 1.00 78.20 O
ANISOU 871 OD1 ASN A 113 10082 10533 9098 -478 -362 253 O
ATOM 872 ND2 ASN A 113 -22.499 -35.882 24.947 1.00 79.50 N
ANISOU 872 ND2 ASN A 113 10269 10681 9257 -506 -407 265 N
ATOM 873 N GLY A 114 -22.349 -33.726 30.102 1.00 73.04 N
ANISOU 873 N GLY A 114 9382 9923 8446 -547 -414 229 N
ATOM 874 CA GLY A 114 -22.859 -33.549 31.432 1.00 73.95 C
ANISOU 874 CA GLY A 114 9484 10068 8546 -565 -426 226 C
ATOM 875 C GLY A 114 -22.611 -32.155 31.953 1.00 73.09 C
ANISOU 875 C GLY A 114 9359 9960 8453 -547 -404 212 C
ATOM 876 O GLY A 114 -23.293 -31.691 32.842 1.00 74.40 O
ANISOU 876 O GLY A 114 9511 10156 8602 -555 -405 209 O
ATOM 877 N LEU A 115 -21.630 -31.480 31.391 1.00 70.75 N
ANISOU 877 N LEU A 115 9063 9629 8189 -524 -383 204 N
ATOM 878 CA LEU A 115 -21.278 -30.158 31.855 1.00 69.58 C
ANISOU 878 CA LEU A 115 8900 9477 8060 -505 -364 191 C
ATOM 879 C LEU A 115 -22.050 -29.054 31.156 1.00 66.97 C
ANISOU 879 C LEU A 115 8562 9163 7722 -483 -339 190 C
ATOM 880 O LEU A 115 -22.605 -28.209 31.799 1.00 67.01 O
ANISOU 880 O LEU A 115 8552 9192 7718 -479 -334 184 O
ATOM 881 CB LEU A 115 -19.768 -29.951 31.748 1.00 70.14 C
ANISOU 881 CB LEU A 115 8976 9502 8173 -492 -357 183 C
ATOM 882 CG LEU A 115 -19.132 -28.569 31.815 1.00 71.84 C
ANISOU 882 CG LEU A 115 9179 9699 8416 -467 -334 171 C
ATOM 883 CD1 LEU A 115 -19.657 -27.733 32.949 1.00 73.00 C
ANISOU 883 CD1 LEU A 115 9309 9874 8553 -468 -335 164 C
ATOM 884 CD2 LEU A 115 -17.634 -28.665 31.897 1.00 72.82 C
ANISOU 884 CD2 LEU A 115 9308 9780 8581 -461 -333 164 C
ATOM 885 N VAL A 116 -22.074 -29.094 29.835 1.00 64.57 N
ANISOU 885 N VAL A 116 8268 8845 7421 -468 -326 195 N
ATOM 886 CA VAL A 116 -22.723 -28.094 29.030 1.00 62.24 C
ANISOU 886 CA VAL A 116 7968 8560 7121 -446 -303 194 C
ATOM 887 C VAL A 116 -24.049 -28.580 28.520 1.00 61.18 C
ANISOU 887 C VAL A 116 7838 8455 6952 -455 -309 205 C
ATOM 888 O VAL A 116 -24.095 -29.330 27.592 1.00 61.77 O
ANISOU 888 O VAL A 116 7929 8519 7023 -455 -312 214 O
ATOM 889 CB VAL A 116 -21.824 -27.699 27.854 1.00 61.86 C
ANISOU 889 CB VAL A 116 7929 8473 7101 -422 -282 192 C
ATOM 890 CG1 VAL A 116 -22.337 -26.478 27.139 1.00 61.33 C
ANISOU 890 CG1 VAL A 116 7855 8413 7033 -399 -258 187 C
ATOM 891 CG2 VAL A 116 -20.419 -27.436 28.315 1.00 62.18 C
ANISOU 891 CG2 VAL A 116 7966 8480 7178 -416 -278 183 C
ATOM 892 N THR A 117 -25.124 -28.122 29.137 1.00 59.54 N
ANISOU 892 N THR A 117 7617 8286 6721 -461 -311 203 N
ATOM 893 CA THR A 117 -26.457 -28.507 28.764 1.00 58.59 C
ANISOU 893 CA THR A 117 7498 8196 6568 -469 -318 213 C
ATOM 894 C THR A 117 -27.259 -27.341 28.255 1.00 57.57 C
ANISOU 894 C THR A 117 7359 8082 6433 -450 -298 207 C
ATOM 895 O THR A 117 -26.918 -26.210 28.465 1.00 57.21 O
ANISOU 895 O THR A 117 7302 8031 6403 -433 -282 195 O
ATOM 896 CB THR A 117 -27.242 -29.086 29.964 1.00 60.16 C
ANISOU 896 CB THR A 117 7687 8433 6740 -497 -340 218 C
ATOM 897 OG1 THR A 117 -27.414 -28.084 30.959 1.00 61.07 O
ANISOU 897 OG1 THR A 117 7782 8567 6854 -493 -333 205 O
ATOM 898 CG2 THR A 117 -26.561 -30.302 30.564 1.00 60.31 C
ANISOU 898 CG2 THR A 117 7715 8439 6761 -520 -364 223 C
ATOM 899 N GLY A 118 -28.377 -27.644 27.634 1.00 57.32 N
ANISOU 899 N GLY A 118 7332 8070 6377 -453 -300 217 N
ATOM 900 CA GLY A 118 -29.286 -26.662 27.113 1.00 56.79 C
ANISOU 900 CA GLY A 118 7257 8019 6301 -437 -285 212 C
ATOM 901 C GLY A 118 -29.868 -25.770 28.168 1.00 56.88 C
ANISOU 901 C GLY A 118 7246 8064 6303 -438 -283 200 C
ATOM 902 O GLY A 118 -30.083 -24.605 27.943 1.00 56.37 O
ANISOU 902 O GLY A 118 7172 8002 6245 -419 -267 190 O
ATOM 903 N THR A 119 -30.122 -26.314 29.334 1.00 57.42 N
ANISOU 903 N THR A 119 7305 8157 6356 -460 -300 203 N
ATOM 904 CA THR A 119 -30.697 -25.511 30.399 1.00 58.33 C
ANISOU 904 CA THR A 119 7398 8305 6459 -462 -299 192 C
ATOM 905 C THR A 119 -29.691 -24.541 30.986 1.00 56.17 C
ANISOU 905 C THR A 119 7115 8014 6212 -446 -289 177 C
ATOM 906 O THR A 119 -30.025 -23.437 31.266 1.00 56.69 O
ANISOU 906 O THR A 119 7166 8095 6278 -432 -279 165 O
ATOM 907 CB THR A 119 -31.343 -26.369 31.487 1.00 62.40 C
ANISOU 907 CB THR A 119 7906 8854 6947 -491 -320 199 C
ATOM 908 OG1 THR A 119 -32.403 -27.107 30.903 1.00 64.89 O
ANISOU 908 OG1 THR A 119 8228 9189 7239 -503 -329 213 O
ATOM 909 CG2 THR A 119 -31.936 -25.483 32.505 1.00 64.20 C
ANISOU 909 CG2 THR A 119 8113 9117 7164 -490 -317 188 C
ATOM 910 N ARG A 120 -28.461 -24.978 31.158 1.00 53.92 N
ANISOU 910 N ARG A 120 6841 7698 5950 -449 -293 178 N
ATOM 911 CA ARG A 120 -27.406 -24.125 31.647 1.00 52.16 C
ANISOU 911 CA ARG A 120 6611 7453 5756 -434 -285 165 C
ATOM 912 C ARG A 120 -27.154 -23.006 30.616 1.00 49.03 C
ANISOU 912 C ARG A 120 6215 7036 5379 -404 -262 158 C
ATOM 913 O ARG A 120 -26.989 -21.884 30.969 1.00 49.54 O
ANISOU 913 O ARG A 120 6266 7102 5455 -388 -253 146 O
ATOM 914 CB ARG A 120 -26.136 -24.923 31.895 1.00 53.78 C
ANISOU 914 CB ARG A 120 6827 7623 5982 -443 -295 169 C
ATOM 915 CG ARG A 120 -26.026 -25.505 33.291 1.00 59.99 C
ANISOU 915 CG ARG A 120 7609 8424 6760 -467 -315 169 C
ATOM 916 CD ARG A 120 -24.945 -26.560 33.415 1.00 63.55 C
ANISOU 916 CD ARG A 120 8074 8843 7228 -481 -329 174 C
ATOM 917 NE ARG A 120 -25.392 -27.660 34.232 1.00 69.25 N
ANISOU 917 NE ARG A 120 8799 9587 7925 -512 -354 182 N
ATOM 918 CZ ARG A 120 -24.679 -28.730 34.544 1.00 71.96 C
ANISOU 918 CZ ARG A 120 9154 9911 8276 -531 -373 187 C
ATOM 919 NH1 ARG A 120 -25.216 -29.658 35.294 1.00 73.34 N
ANISOU 919 NH1 ARG A 120 9331 10111 8426 -560 -395 194 N
ATOM 920 NH2 ARG A 120 -23.456 -28.890 34.117 1.00 71.16 N
ANISOU 920 NH2 ARG A 120 9064 9768 8207 -522 -370 184 N
ATOM 921 N ALA A 121 -27.178 -23.349 29.343 1.00 46.08 N
ANISOU 921 N ALA A 121 5856 6645 5008 -398 -255 166 N
ATOM 922 CA ALA A 121 -26.972 -22.407 28.259 1.00 43.22 C
ANISOU 922 CA ALA A 121 5497 6262 4663 -372 -234 161 C
ATOM 923 C ALA A 121 -27.993 -21.289 28.227 1.00 42.01 C
ANISOU 923 C ALA A 121 5329 6136 4496 -359 -225 152 C
ATOM 924 O ALA A 121 -27.631 -20.167 28.136 1.00 40.74 O
ANISOU 924 O ALA A 121 5162 5966 4353 -340 -213 141 O
ATOM 925 CB ALA A 121 -26.943 -23.138 26.948 1.00 42.51 C
ANISOU 925 CB ALA A 121 5428 6151 4572 -371 -230 172 C
ATOM 926 N ALA A 122 -29.269 -21.617 28.332 1.00 42.61 N
ANISOU 926 N ALA A 122 5402 6248 4541 -372 -234 156 N
ATOM 927 CA ALA A 122 -30.344 -20.640 28.333 1.00 43.22 C
ANISOU 927 CA ALA A 122 5464 6353 4603 -362 -228 147 C
ATOM 928 C ALA A 122 -30.257 -19.648 29.499 1.00 44.44 C
ANISOU 928 C ALA A 122 5598 6526 4762 -355 -228 132 C
ATOM 929 O ALA A 122 -30.587 -18.498 29.364 1.00 44.75 O
ANISOU 929 O ALA A 122 5627 6573 4804 -337 -219 120 O
ATOM 930 CB ALA A 122 -31.682 -21.332 28.336 1.00 43.70 C
ANISOU 930 CB ALA A 122 5524 6448 4631 -379 -239 155 C
ATOM 931 N GLY A 123 -29.812 -20.146 30.641 1.00 44.31 N
ANISOU 931 N GLY A 123 5577 6515 4746 -371 -240 133 N
ATOM 932 CA GLY A 123 -29.637 -19.351 31.825 1.00 44.06 C
ANISOU 932 CA GLY A 123 5527 6497 4717 -366 -243 120 C
ATOM 933 C GLY A 123 -28.466 -18.430 31.613 1.00 41.62 C
ANISOU 933 C GLY A 123 5218 6153 4443 -343 -232 112 C
ATOM 934 O GLY A 123 -28.530 -17.294 31.938 1.00 41.65 O
ANISOU 934 O GLY A 123 5208 6164 4453 -326 -227 99 O
ATOM 935 N ILE A 124 -27.396 -18.948 31.059 1.00 39.43 N
ANISOU 935 N ILE A 124 4956 5837 4189 -342 -229 119 N
ATOM 936 CA ILE A 124 -26.258 -18.128 30.771 1.00 37.31 C
ANISOU 936 CA ILE A 124 4689 5533 3955 -321 -217 113 C
ATOM 937 C ILE A 124 -26.616 -17.000 29.794 1.00 34.12 C
ANISOU 937 C ILE A 124 4282 5127 3556 -297 -202 106 C
ATOM 938 O ILE A 124 -26.267 -15.893 30.014 1.00 32.92 O
ANISOU 938 O ILE A 124 4120 4969 3420 -279 -197 95 O
ATOM 939 CB ILE A 124 -25.113 -18.967 30.291 1.00 38.52 C
ANISOU 939 CB ILE A 124 4859 5647 4130 -325 -216 122 C
ATOM 940 CG1 ILE A 124 -24.595 -19.767 31.467 1.00 42.13 C
ANISOU 940 CG1 ILE A 124 5316 6104 4589 -345 -233 124 C
ATOM 941 CG2 ILE A 124 -24.018 -18.102 29.730 1.00 37.88 C
ANISOU 941 CG2 ILE A 124 4780 5529 4085 -302 -201 117 C
ATOM 942 CD1 ILE A 124 -23.557 -20.770 31.079 1.00 44.81 C
ANISOU 942 CD1 ILE A 124 5672 6408 4947 -353 -236 133 C
ATOM 943 N ILE A 125 -27.362 -17.314 28.749 1.00 32.72 N
ANISOU 943 N ILE A 125 4114 4954 3363 -299 -196 112 N
ATOM 944 CA ILE A 125 -27.786 -16.351 27.760 1.00 31.06 C
ANISOU 944 CA ILE A 125 3905 4742 3155 -279 -183 106 C
ATOM 945 C ILE A 125 -28.602 -15.238 28.397 1.00 29.66 C
ANISOU 945 C ILE A 125 3707 4596 2965 -270 -186 92 C
ATOM 946 O ILE A 125 -28.403 -14.106 28.120 1.00 27.53 O
ANISOU 946 O ILE A 125 3432 4318 2711 -250 -178 82 O
ATOM 947 CB ILE A 125 -28.572 -17.035 26.628 1.00 31.82 C
ANISOU 947 CB ILE A 125 4017 4840 3233 -285 -180 116 C
ATOM 948 CG1 ILE A 125 -27.647 -17.974 25.858 1.00 32.21 C
ANISOU 948 CG1 ILE A 125 4088 4853 3298 -289 -176 128 C
ATOM 949 CG2 ILE A 125 -29.296 -16.015 25.773 1.00 31.37 C
ANISOU 949 CG2 ILE A 125 3958 4788 3172 -268 -170 108 C
ATOM 950 CD1 ILE A 125 -28.332 -18.839 24.839 1.00 32.98 C
ANISOU 950 CD1 ILE A 125 4202 4951 3377 -297 -176 140 C
ATOM 951 N ALA A 126 -29.504 -15.614 29.287 1.00 30.96 N
ANISOU 951 N ALA A 126 3860 4798 3103 -286 -198 91 N
ATOM 952 CA ALA A 126 -30.352 -14.688 30.007 1.00 32.34 C
ANISOU 952 CA ALA A 126 4016 5009 3265 -279 -202 77 C
ATOM 953 C ALA A 126 -29.515 -13.703 30.825 1.00 32.47 C
ANISOU 953 C ALA A 126 4020 5016 3303 -263 -203 66 C
ATOM 954 O ALA A 126 -29.721 -12.525 30.776 1.00 31.30 O
ANISOU 954 O ALA A 126 3861 4874 3160 -245 -200 53 O
ATOM 955 CB ALA A 126 -31.313 -15.448 30.890 1.00 33.72 C
ANISOU 955 CB ALA A 126 4182 5223 3408 -302 -215 81 C
ATOM 956 N ILE A 127 -28.576 -14.248 31.574 1.00 33.06 N
ANISOU 956 N ILE A 127 4096 5074 3390 -272 -209 71 N
ATOM 957 CA ILE A 127 -27.666 -13.495 32.409 1.00 33.32 C
ANISOU 957 CA ILE A 127 4120 5094 3445 -260 -212 62 C
ATOM 958 C ILE A 127 -26.843 -12.535 31.558 1.00 30.62 C
ANISOU 958 C ILE A 127 3783 4718 3135 -235 -200 58 C
ATOM 959 O ILE A 127 -26.692 -11.419 31.887 1.00 30.41 O
ANISOU 959 O ILE A 127 3744 4692 3120 -217 -201 47 O
ATOM 960 CB ILE A 127 -26.737 -14.431 33.203 1.00 34.74 C
ANISOU 960 CB ILE A 127 4307 5257 3637 -276 -221 70 C
ATOM 961 CG1 ILE A 127 -27.491 -15.059 34.378 1.00 38.34 C
ANISOU 961 CG1 ILE A 127 4755 5751 4063 -297 -235 70 C
ATOM 962 CG2 ILE A 127 -25.507 -13.704 33.684 1.00 33.86 C
ANISOU 962 CG2 ILE A 127 4191 5115 3558 -260 -221 64 C
ATOM 963 CD1 ILE A 127 -26.772 -16.226 34.996 1.00 41.37 C
ANISOU 963 CD1 ILE A 127 5149 6120 4451 -319 -246 80 C
ATOM 964 N CYS A 128 -26.349 -13.016 30.441 1.00 28.45 N
ANISOU 964 N CYS A 128 3524 4413 2873 -235 -190 68 N
ATOM 965 CA CYS A 128 -25.555 -12.196 29.562 1.00 27.12 C
ANISOU 965 CA CYS A 128 3360 4211 2733 -214 -177 66 C
ATOM 966 C CYS A 128 -26.332 -11.011 28.966 1.00 25.23 C
ANISOU 966 C CYS A 128 3114 3986 2487 -196 -172 55 C
ATOM 967 O CYS A 128 -25.800 -9.971 28.848 1.00 23.27 O
ANISOU 967 O CYS A 128 2859 3721 2260 -177 -168 48 O
ATOM 968 CB CYS A 128 -24.844 -13.041 28.525 1.00 28.12 C
ANISOU 968 CB CYS A 128 3508 4304 2874 -219 -166 79 C
ATOM 969 SG CYS A 128 -23.581 -14.089 29.206 1.00 34.14 S
ANISOU 969 SG CYS A 128 4277 5039 3656 -233 -173 87 S
ATOM 970 N TRP A 129 -27.603 -11.189 28.649 1.00 25.00 N
ANISOU 970 N TRP A 129 3083 3985 2428 -203 -173 54 N
ATOM 971 CA TRP A 129 -28.419 -10.108 28.149 1.00 25.14 C
ANISOU 971 CA TRP A 129 3095 4019 2439 -188 -171 42 C
ATOM 972 C TRP A 129 -28.632 -9.063 29.246 1.00 25.51 C
ANISOU 972 C TRP A 129 3120 4089 2485 -177 -181 27 C
ATOM 973 O TRP A 129 -28.564 -7.910 29.002 1.00 25.41 O
ANISOU 973 O TRP A 129 3099 4071 2483 -157 -180 17 O
ATOM 974 CB TRP A 129 -29.733 -10.603 27.589 1.00 25.96 C
ANISOU 974 CB TRP A 129 3203 4148 2513 -199 -171 44 C
ATOM 975 CG TRP A 129 -29.644 -11.030 26.186 1.00 26.46 C
ANISOU 975 CG TRP A 129 3288 4186 2582 -199 -159 54 C
ATOM 976 CD1 TRP A 129 -29.503 -12.271 25.740 1.00 27.64 C
ANISOU 976 CD1 TRP A 129 3454 4323 2726 -214 -157 69 C
ATOM 977 CD2 TRP A 129 -29.653 -10.183 25.032 1.00 25.96 C
ANISOU 977 CD2 TRP A 129 3231 4103 2528 -182 -149 50 C
ATOM 978 NE1 TRP A 129 -29.444 -12.287 24.385 1.00 27.67 N
ANISOU 978 NE1 TRP A 129 3476 4303 2735 -207 -145 74 N
ATOM 979 CE2 TRP A 129 -29.525 -11.009 23.921 1.00 26.60 C
ANISOU 979 CE2 TRP A 129 3336 4162 2610 -188 -140 62 C
ATOM 980 CE3 TRP A 129 -29.759 -8.813 24.838 1.00 25.29 C
ANISOU 980 CE3 TRP A 129 3137 4018 2452 -162 -149 36 C
ATOM 981 CZ2 TRP A 129 -29.502 -10.506 22.635 1.00 26.37 C
ANISOU 981 CZ2 TRP A 129 3320 4110 2589 -175 -129 62 C
ATOM 982 CZ3 TRP A 129 -29.722 -8.327 23.584 1.00 25.91 C
ANISOU 982 CZ3 TRP A 129 3229 4075 2540 -151 -138 35 C
ATOM 983 CH2 TRP A 129 -29.608 -9.166 22.490 1.00 26.09 C
ANISOU 983 CH2 TRP A 129 3275 4075 2562 -157 -128 48 C
ATOM 984 N VAL A 130 -28.886 -9.515 30.464 1.00 26.46 N
ANISOU 984 N VAL A 130 3229 4234 2590 -190 -192 26 N
ATOM 985 CA VAL A 130 -29.054 -8.608 31.590 1.00 28.08 C
ANISOU 985 CA VAL A 130 3414 4461 2792 -179 -203 13 C
ATOM 986 C VAL A 130 -27.771 -7.788 31.774 1.00 26.31 C
ANISOU 986 C VAL A 130 3188 4204 2603 -160 -203 10 C
ATOM 987 O VAL A 130 -27.838 -6.617 31.829 1.00 26.26 O
ANISOU 987 O VAL A 130 3172 4202 2605 -141 -206 -2 O
ATOM 988 CB VAL A 130 -29.479 -9.318 32.908 1.00 31.09 C
ANISOU 988 CB VAL A 130 3786 4874 3151 -198 -215 13 C
ATOM 989 CG1 VAL A 130 -29.406 -8.349 34.062 1.00 32.63 C
ANISOU 989 CG1 VAL A 130 3964 5085 3349 -184 -225 -1 C
ATOM 990 CG2 VAL A 130 -30.864 -9.919 32.814 1.00 32.41 C
ANISOU 990 CG2 VAL A 130 3952 5080 3284 -214 -216 14 C
ATOM 991 N LEU A 131 -26.618 -8.442 31.789 1.00 24.95 N
ANISOU 991 N LEU A 131 3028 3999 2454 -166 -200 21 N
ATOM 992 CA LEU A 131 -25.334 -7.789 31.916 1.00 24.55 C
ANISOU 992 CA LEU A 131 2976 3912 2438 -149 -199 20 C
ATOM 993 C LEU A 131 -25.049 -6.784 30.787 1.00 23.24 C
ANISOU 993 C LEU A 131 2814 3725 2293 -128 -189 17 C
ATOM 994 O LEU A 131 -24.469 -5.774 31.013 1.00 23.35 O
ANISOU 994 O LEU A 131 2819 3725 2327 -110 -193 11 O
ATOM 995 CB LEU A 131 -24.224 -8.790 31.983 1.00 25.32 C
ANISOU 995 CB LEU A 131 3087 3978 2556 -162 -196 33 C
ATOM 996 CG LEU A 131 -24.141 -9.661 33.224 1.00 30.01 C
ANISOU 996 CG LEU A 131 3680 4584 3140 -180 -208 36 C
ATOM 997 CD1 LEU A 131 -23.023 -10.671 33.126 1.00 30.55 C
ANISOU 997 CD1 LEU A 131 3762 4616 3228 -192 -206 48 C
ATOM 998 CD2 LEU A 131 -24.010 -8.814 34.461 1.00 31.66 C
ANISOU 998 CD2 LEU A 131 3872 4803 3353 -169 -221 25 C
ATOM 999 N SER A 132 -25.496 -7.125 29.594 1.00 21.21 N
ANISOU 999 N SER A 132 2568 3464 2025 -133 -178 22 N
ATOM 1000 CA SER A 132 -25.357 -6.313 28.396 1.00 20.04 C
ANISOU 1000 CA SER A 132 2427 3297 1892 -117 -167 21 C
ATOM 1001 C SER A 132 -26.126 -4.999 28.531 1.00 19.87 C
ANISOU 1001 C SER A 132 2389 3298 1861 -100 -176 4 C
ATOM 1002 O SER A 132 -25.640 -3.976 28.169 1.00 18.54 O
ANISOU 1002 O SER A 132 2218 3112 1714 -81 -175 0 O
ATOM 1003 CB SER A 132 -25.781 -7.091 27.171 1.00 20.64 C
ANISOU 1003 CB SER A 132 2520 3366 1955 -127 -155 30 C
ATOM 1004 OG SER A 132 -24.923 -8.140 26.928 1.00 22.13 O
ANISOU 1004 OG SER A 132 2724 3529 2157 -138 -147 43 O
ATOM 1005 N PHE A 133 -27.342 -5.071 29.051 1.00 21.01 N
ANISOU 1005 N PHE A 133 2524 3483 1976 -107 -185 -4 N
ATOM 1006 CA PHE A 133 -28.140 -3.900 29.307 1.00 23.52 C
ANISOU 1006 CA PHE A 133 2827 3828 2284 -92 -195 -21 C
ATOM 1007 C PHE A 133 -27.448 -3.007 30.349 1.00 24.68 C
ANISOU 1007 C PHE A 133 2958 3971 2448 -76 -207 -29 C
ATOM 1008 O PHE A 133 -27.344 -1.852 30.187 1.00 25.42 O
ANISOU 1008 O PHE A 133 3044 4059 2554 -57 -213 -38 O
ATOM 1009 CB PHE A 133 -29.549 -4.274 29.724 1.00 24.40 C
ANISOU 1009 CB PHE A 133 2930 3984 2359 -105 -201 -28 C
ATOM 1010 CG PHE A 133 -30.487 -4.450 28.581 1.00 24.81 C
ANISOU 1010 CG PHE A 133 2991 4042 2394 -110 -194 -28 C
ATOM 1011 CD1 PHE A 133 -31.136 -3.384 28.044 1.00 25.77 C
ANISOU 1011 CD1 PHE A 133 3107 4172 2513 -96 -198 -42 C
ATOM 1012 CD2 PHE A 133 -30.698 -5.673 28.043 1.00 25.55 C
ANISOU 1012 CD2 PHE A 133 3100 4132 2477 -129 -186 -14 C
ATOM 1013 CE1 PHE A 133 -31.992 -3.536 26.992 1.00 26.63 C
ANISOU 1013 CE1 PHE A 133 3226 4283 2607 -100 -192 -42 C
ATOM 1014 CE2 PHE A 133 -31.556 -5.842 26.990 1.00 26.87 C
ANISOU 1014 CE2 PHE A 133 3277 4302 2629 -133 -180 -13 C
ATOM 1015 CZ PHE A 133 -32.207 -4.771 26.463 1.00 26.42 C
ANISOU 1015 CZ PHE A 133 3215 4252 2570 -119 -183 -27 C
ATOM 1016 N ALA A 134 -26.926 -3.608 31.388 1.00 24.24 N
ANISOU 1016 N ALA A 134 2900 3915 2395 -85 -212 -24 N
ATOM 1017 CA ALA A 134 -26.214 -2.907 32.440 1.00 25.00 C
ANISOU 1017 CA ALA A 134 2984 4005 2509 -71 -225 -29 C
ATOM 1018 C ALA A 134 -24.985 -2.172 31.929 1.00 24.22 C
ANISOU 1018 C ALA A 134 2890 3864 2449 -53 -222 -25 C
ATOM 1019 O ALA A 134 -24.783 -1.045 32.218 1.00 24.08 O
ANISOU 1019 O ALA A 134 2861 3844 2444 -33 -232 -34 O
ATOM 1020 CB ALA A 134 -25.802 -3.879 33.509 1.00 26.14 C
ANISOU 1020 CB ALA A 134 3130 4151 2652 -87 -229 -22 C
ATOM 1021 N ILE A 135 -24.176 -2.863 31.163 1.00 23.03 N
ANISOU 1021 N ILE A 135 2755 3680 2316 -60 -207 -11 N
ATOM 1022 CA ILE A 135 -22.965 -2.312 30.619 1.00 22.32 C
ANISOU 1022 CA ILE A 135 2670 3548 2263 -46 -202 -5 C
ATOM 1023 C ILE A 135 -23.253 -1.219 29.576 1.00 20.82 C
ANISOU 1023 C ILE A 135 2479 3354 2077 -29 -198 -12 C
ATOM 1024 O ILE A 135 -22.789 -0.135 29.683 1.00 20.24 O
ANISOU 1024 O ILE A 135 2397 3269 2023 -10 -207 -17 O
ATOM 1025 CB ILE A 135 -22.066 -3.409 30.053 1.00 23.34 C
ANISOU 1025 CB ILE A 135 2815 3644 2408 -59 -186 11 C
ATOM 1026 CG1 ILE A 135 -21.494 -4.253 31.173 1.00 26.20 C
ANISOU 1026 CG1 ILE A 135 3177 4002 2775 -72 -193 16 C
ATOM 1027 CG2 ILE A 135 -20.944 -2.826 29.223 1.00 23.55 C
ANISOU 1027 CG2 ILE A 135 2848 3630 2471 -45 -177 17 C
ATOM 1028 CD1 ILE A 135 -21.040 -5.607 30.763 1.00 28.01 C
ANISOU 1028 CD1 ILE A 135 3423 4213 3008 -91 -182 29 C
ATOM 1029 N GLY A 136 -24.074 -1.559 28.605 1.00 19.62 N
ANISOU 1029 N GLY A 136 2337 3212 1905 -38 -188 -12 N
ATOM 1030 CA GLY A 136 -24.444 -0.658 27.542 1.00 19.74 C
ANISOU 1030 CA GLY A 136 2355 3224 1922 -25 -185 -18 C
ATOM 1031 C GLY A 136 -25.184 0.587 27.954 1.00 20.70 C
ANISOU 1031 C GLY A 136 2459 3371 2033 -10 -203 -35 C
ATOM 1032 O GLY A 136 -24.984 1.598 27.399 1.00 21.79 O
ANISOU 1032 O GLY A 136 2596 3497 2185 6 -205 -40 O
ATOM 1033 N LEU A 137 -26.044 0.467 28.937 1.00 20.07 N
ANISOU 1033 N LEU A 137 2367 3329 1929 -14 -215 -45 N
ATOM 1034 CA LEU A 137 -26.816 1.566 29.431 1.00 20.76 C
ANISOU 1034 CA LEU A 137 2438 3446 2006 0 -232 -63 C
ATOM 1035 C LEU A 137 -26.257 2.227 30.696 1.00 21.44 C
ANISOU 1035 C LEU A 137 2508 3534 2105 15 -249 -69 C
ATOM 1036 O LEU A 137 -26.907 2.999 31.312 1.00 22.71 O
ANISOU 1036 O LEU A 137 2653 3721 2252 26 -265 -84 O
ATOM 1037 CB LEU A 137 -28.274 1.178 29.587 1.00 20.41 C
ANISOU 1037 CB LEU A 137 2388 3443 1924 -12 -235 -73 C
ATOM 1038 CG LEU A 137 -28.963 0.580 28.366 1.00 21.04 C
ANISOU 1038 CG LEU A 137 2483 3522 1988 -25 -221 -68 C
ATOM 1039 CD1 LEU A 137 -30.419 0.316 28.648 1.00 22.09 C
ANISOU 1039 CD1 LEU A 137 2608 3699 2087 -35 -226 -78 C
ATOM 1040 CD2 LEU A 137 -28.787 1.459 27.152 1.00 19.88 C
ANISOU 1040 CD2 LEU A 137 2345 3352 1857 -12 -217 -71 C
ATOM 1041 N THR A 138 -25.000 1.949 30.990 1.00 20.36 N
ANISOU 1041 N THR A 138 2376 3365 1995 16 -246 -56 N
ATOM 1042 CA THR A 138 -24.277 2.555 32.095 1.00 20.41 C
ANISOU 1042 CA THR A 138 2371 3364 2020 30 -262 -59 C
ATOM 1043 C THR A 138 -24.382 4.071 32.047 1.00 20.86 C
ANISOU 1043 C THR A 138 2415 3424 2086 55 -278 -72 C
ATOM 1044 O THR A 138 -24.606 4.665 33.031 1.00 22.84 O
ANISOU 1044 O THR A 138 2653 3694 2332 67 -296 -83 O
ATOM 1045 CB THR A 138 -22.813 2.082 32.224 1.00 21.36 C
ANISOU 1045 CB THR A 138 2499 3442 2173 29 -255 -43 C
ATOM 1046 OG1 THR A 138 -22.779 0.845 32.886 1.00 21.88 O
ANISOU 1046 OG1 THR A 138 2570 3514 2228 8 -250 -36 O
ATOM 1047 CG2 THR A 138 -21.981 3.059 32.978 1.00 21.44 C
ANISOU 1047 CG2 THR A 138 2499 3435 2211 50 -272 -46 C
ATOM 1048 N PRO A 139 -24.296 4.695 30.872 1.00 20.43 N
ANISOU 1048 N PRO A 139 2367 3352 2043 64 -273 -72 N
ATOM 1049 CA PRO A 139 -24.502 6.130 30.828 1.00 20.58 C
ANISOU 1049 CA PRO A 139 2375 3377 2068 86 -292 -86 C
ATOM 1050 C PRO A 139 -25.865 6.621 31.405 1.00 21.28 C
ANISOU 1050 C PRO A 139 2449 3513 2124 91 -308 -106 C
ATOM 1051 O PRO A 139 -25.881 7.659 31.979 1.00 21.32 O
ANISOU 1051 O PRO A 139 2440 3527 2134 110 -329 -118 O
ATOM 1052 CB PRO A 139 -24.296 6.485 29.362 1.00 20.54 C
ANISOU 1052 CB PRO A 139 2382 3347 2075 88 -281 -81 C
ATOM 1053 CG PRO A 139 -23.427 5.418 28.863 1.00 20.61 C
ANISOU 1053 CG PRO A 139 2407 3326 2100 73 -258 -62 C
ATOM 1054 CD PRO A 139 -23.818 4.186 29.592 1.00 19.30 C
ANISOU 1054 CD PRO A 139 2242 3180 1912 54 -252 -59 C
ATOM 1055 N MET A 140 -26.911 5.820 31.289 1.00 21.43 N
ANISOU 1055 N MET A 140 2470 3560 2112 73 -299 -110 N
ATOM 1056 CA MET A 140 -28.226 6.135 31.821 1.00 24.05 C
ANISOU 1056 CA MET A 140 2788 3938 2412 75 -312 -129 C
ATOM 1057 C MET A 140 -28.255 6.146 33.351 1.00 25.78 C
ANISOU 1057 C MET A 140 2992 4180 2623 79 -326 -134 C
ATOM 1058 O MET A 140 -29.067 6.770 33.921 1.00 26.48 O
ANISOU 1058 O MET A 140 3066 4301 2694 89 -341 -151 O
ATOM 1059 CB MET A 140 -29.314 5.256 31.226 1.00 25.10 C
ANISOU 1059 CB MET A 140 2928 4093 2517 54 -298 -129 C
ATOM 1060 CG MET A 140 -29.401 5.365 29.708 1.00 26.86 C
ANISOU 1060 CG MET A 140 3166 4294 2745 51 -286 -126 C
ATOM 1061 SD MET A 140 -30.789 4.531 29.000 1.00 33.96 S
ANISOU 1061 SD MET A 140 4073 5219 3612 31 -274 -128 S
ATOM 1062 CE MET A 140 -32.020 5.724 29.393 1.00 33.29 C
ANISOU 1062 CE MET A 140 3967 5173 3507 46 -297 -156 C
ATOM 1063 N LEU A 141 -27.331 5.432 33.960 1.00 26.59 N
ANISOU 1063 N LEU A 141 3099 4263 2739 72 -321 -120 N
ATOM 1064 CA LEU A 141 -27.160 5.421 35.399 1.00 29.48 C
ANISOU 1064 CA LEU A 141 3455 4643 3102 77 -334 -123 C
ATOM 1065 C LEU A 141 -26.453 6.691 35.941 1.00 29.82 C
ANISOU 1065 C LEU A 141 3489 4672 3171 105 -356 -130 C
ATOM 1066 O LEU A 141 -26.376 6.864 37.119 1.00 31.11 O
ANISOU 1066 O LEU A 141 3643 4848 3330 113 -370 -135 O
ATOM 1067 CB LEU A 141 -26.489 4.144 35.876 1.00 31.05 C
ANISOU 1067 CB LEU A 141 3665 4827 3306 57 -322 -107 C
ATOM 1068 CG LEU A 141 -27.067 2.823 35.407 1.00 34.20 C
ANISOU 1068 CG LEU A 141 4074 5238 3683 29 -303 -99 C
ATOM 1069 CD1 LEU A 141 -26.370 1.629 35.966 1.00 34.99 C
ANISOU 1069 CD1 LEU A 141 4183 5322 3788 11 -295 -83 C
ATOM 1070 CD2 LEU A 141 -28.548 2.709 35.560 1.00 35.76 C
ANISOU 1070 CD2 LEU A 141 4262 5483 3842 21 -305 -111 C
ATOM 1071 N GLY A 142 -25.993 7.564 35.063 1.00 28.12 N
ANISOU 1071 N GLY A 142 3275 4431 2977 120 -359 -129 N
ATOM 1072 CA GLY A 142 -25.376 8.779 35.502 1.00 29.11 C
ANISOU 1072 CA GLY A 142 3391 4542 3125 146 -381 -134 C
ATOM 1073 C GLY A 142 -24.078 9.217 34.888 1.00 28.01 C
ANISOU 1073 C GLY A 142 3260 4355 3026 157 -380 -121 C
ATOM 1074 O GLY A 142 -23.689 10.338 35.034 1.00 29.09 O
ANISOU 1074 O GLY A 142 3389 4482 3181 179 -400 -126 O
ATOM 1075 N TRP A 143 -23.399 8.316 34.193 1.00 25.29 N
ANISOU 1075 N TRP A 143 2931 3982 2696 140 -357 -103 N
ATOM 1076 CA TRP A 143 -22.153 8.653 33.530 1.00 23.23 C
ANISOU 1076 CA TRP A 143 2678 3675 2474 148 -353 -89 C
ATOM 1077 C TRP A 143 -22.520 9.221 32.164 1.00 21.90 C
ANISOU 1077 C TRP A 143 2515 3503 2305 150 -347 -93 C
ATOM 1078 O TRP A 143 -22.479 8.536 31.206 1.00 20.20 O
ANISOU 1078 O TRP A 143 2312 3275 2088 135 -325 -84 O
ATOM 1079 CB TRP A 143 -21.251 7.435 33.426 1.00 22.74 C
ANISOU 1079 CB TRP A 143 2630 3584 2427 130 -331 -70 C
ATOM 1080 CG TRP A 143 -19.815 7.627 33.103 1.00 23.34 C
ANISOU 1080 CG TRP A 143 2712 3612 2546 138 -327 -55 C
ATOM 1081 CD1 TRP A 143 -19.191 8.763 32.761 1.00 23.95 C
ANISOU 1081 CD1 TRP A 143 2784 3666 2650 158 -339 -54 C
ATOM 1082 CD2 TRP A 143 -18.809 6.617 33.142 1.00 21.84 C
ANISOU 1082 CD2 TRP A 143 2532 3390 2376 124 -311 -38 C
ATOM 1083 NE1 TRP A 143 -17.883 8.532 32.564 1.00 23.74 N
ANISOU 1083 NE1 TRP A 143 2764 3597 2659 158 -330 -37 N
ATOM 1084 CE2 TRP A 143 -17.618 7.217 32.779 1.00 22.38 C
ANISOU 1084 CE2 TRP A 143 2601 3418 2483 138 -313 -28 C
ATOM 1085 CE3 TRP A 143 -18.816 5.257 33.414 1.00 21.30 C
ANISOU 1085 CE3 TRP A 143 2472 3324 2296 102 -297 -32 C
ATOM 1086 CZ2 TRP A 143 -16.439 6.508 32.685 1.00 22.03 C
ANISOU 1086 CZ2 TRP A 143 2566 3337 2469 130 -299 -12 C
ATOM 1087 CZ3 TRP A 143 -17.645 4.569 33.331 1.00 21.75 C
ANISOU 1087 CZ3 TRP A 143 2539 3344 2381 94 -285 -16 C
ATOM 1088 CH2 TRP A 143 -16.479 5.188 32.963 1.00 21.65 C
ANISOU 1088 CH2 TRP A 143 2526 3291 2408 109 -285 -7 C
ATOM 1089 N ASN A 144 -22.909 10.473 32.157 1.00 22.41 N
ANISOU 1089 N ASN A 144 2569 3579 2369 170 -369 -107 N
ATOM 1090 CA ASN A 144 -23.317 11.169 30.967 1.00 23.67 C
ANISOU 1090 CA ASN A 144 2731 3736 2526 174 -369 -112 C
ATOM 1091 C ASN A 144 -23.020 12.657 31.041 1.00 24.82 C
ANISOU 1091 C ASN A 144 2866 3874 2690 200 -396 -120 C
ATOM 1092 O ASN A 144 -22.568 13.151 32.023 1.00 24.17 O
ANISOU 1092 O ASN A 144 2773 3790 2620 216 -415 -122 O
ATOM 1093 CB ASN A 144 -24.798 10.939 30.712 1.00 24.00 C
ANISOU 1093 CB ASN A 144 2772 3818 2530 164 -366 -128 C
ATOM 1094 CG ASN A 144 -25.662 11.451 31.824 1.00 27.90 C
ANISOU 1094 CG ASN A 144 3248 4352 3002 175 -389 -148 C
ATOM 1095 OD1 ASN A 144 -25.639 12.592 32.133 1.00 28.91 O
ANISOU 1095 OD1 ASN A 144 3365 4484 3137 196 -414 -158 O
ATOM 1096 ND2 ASN A 144 -26.395 10.588 32.426 1.00 28.00 N
ANISOU 1096 ND2 ASN A 144 3258 4394 2987 160 -382 -151 N
ATOM 1097 N ASN A 145 -23.297 13.355 29.958 1.00 26.33 N
ANISOU 1097 N ASN A 145 3062 4060 2883 204 -398 -125 N
ATOM 1098 CA ASN A 145 -23.086 14.761 29.907 1.00 28.80 C
ANISOU 1098 CA ASN A 145 3365 4366 3211 227 -425 -133 C
ATOM 1099 C ASN A 145 -24.412 15.508 29.980 1.00 32.30 C
ANISOU 1099 C ASN A 145 3798 4849 3626 235 -446 -158 C
ATOM 1100 O ASN A 145 -24.473 16.624 29.631 1.00 33.35 O
ANISOU 1100 O ASN A 145 3926 4978 3766 250 -467 -167 O
ATOM 1101 CB ASN A 145 -22.303 15.156 28.671 1.00 28.71 C
ANISOU 1101 CB ASN A 145 3366 4318 3226 228 -417 -120 C
ATOM 1102 CG ASN A 145 -20.880 14.657 28.682 1.00 31.50 C
ANISOU 1102 CG ASN A 145 3725 4630 3612 225 -401 -97 C
ATOM 1103 OD1 ASN A 145 -20.298 14.427 29.703 1.00 34.03 O
ANISOU 1103 OD1 ASN A 145 4040 4945 3945 230 -406 -91 O
ATOM 1104 ND2 ASN A 145 -20.337 14.490 27.537 1.00 31.52 N
ANISOU 1104 ND2 ASN A 145 3742 4605 3630 217 -381 -84 N
ATOM 1105 N CYS A 146 -25.461 14.885 30.487 1.00 33.68 N
ANISOU 1105 N CYS A 146 3968 5060 3768 224 -442 -170 N
ATOM 1106 CA CYS A 146 -26.768 15.518 30.607 1.00 36.61 C
ANISOU 1106 CA CYS A 146 4329 5471 4112 231 -461 -194 C
ATOM 1107 C CYS A 146 -26.790 16.670 31.591 1.00 39.87 C
ANISOU 1107 C CYS A 146 4722 5897 4528 257 -496 -209 C
ATOM 1108 O CYS A 146 -27.520 17.593 31.422 1.00 40.48 O
ANISOU 1108 O CYS A 146 4792 5993 4595 269 -518 -228 O
ATOM 1109 CB CYS A 146 -27.860 14.521 30.912 1.00 37.69 C
ANISOU 1109 CB CYS A 146 4464 5643 4214 213 -446 -202 C
ATOM 1110 SG CYS A 146 -28.127 13.299 29.627 1.00 40.25 S
ANISOU 1110 SG CYS A 146 4810 5955 4529 184 -410 -189 S
ATOM 1111 N GLY A 147 -25.923 16.618 32.590 1.00 41.74 N
ANISOU 1111 N GLY A 147 4954 6122 4782 267 -503 -199 N
ATOM 1112 CA GLY A 147 -25.733 17.683 33.541 1.00 44.40 C
ANISOU 1112 CA GLY A 147 5277 6467 5128 293 -536 -209 C
ATOM 1113 C GLY A 147 -25.034 18.922 33.002 1.00 46.20 C
ANISOU 1113 C GLY A 147 5504 6666 5385 313 -559 -207 C
ATOM 1114 O GLY A 147 -25.032 19.912 33.634 1.00 48.28 O
ANISOU 1114 O GLY A 147 5755 6938 5653 336 -590 -217 O
ATOM 1115 N GLN A 148 -24.431 18.856 31.833 1.00 46.08 N
ANISOU 1115 N GLN A 148 5501 6617 5388 304 -543 -192 N
ATOM 1116 CA GLN A 148 -23.770 19.975 31.211 1.00 47.06 C
ANISOU 1116 CA GLN A 148 5626 6714 5540 320 -562 -188 C
ATOM 1117 C GLN A 148 -24.247 20.126 29.765 1.00 46.45 C
ANISOU 1117 C GLN A 148 5560 6632 5456 308 -551 -192 C
ATOM 1118 O GLN A 148 -23.484 19.970 28.845 1.00 45.94 O
ANISOU 1118 O GLN A 148 5509 6534 5412 299 -534 -175 O
ATOM 1119 CB GLN A 148 -22.276 19.754 31.223 1.00 49.78 C
ANISOU 1119 CB GLN A 148 5977 7015 5922 321 -552 -162 C
ATOM 1120 CG GLN A 148 -21.633 19.712 32.602 1.00 57.16 C
ANISOU 1120 CG GLN A 148 6903 7946 6870 335 -565 -157 C
ATOM 1121 CD GLN A 148 -21.348 18.307 33.096 1.00 65.19 C
ANISOU 1121 CD GLN A 148 7926 8959 7882 316 -536 -145 C
ATOM 1122 OE1 GLN A 148 -21.026 17.408 32.320 1.00 66.24 O
ANISOU 1122 OE1 GLN A 148 8073 9074 8020 295 -505 -131 O
ATOM 1123 NE2 GLN A 148 -21.455 18.116 34.400 1.00 67.96 N
ANISOU 1123 NE2 GLN A 148 8269 9328 8225 323 -547 -150 N
ATOM 1124 N PRO A 149 -25.518 20.463 29.567 1.00 46.44 N
ANISOU 1124 N PRO A 149 5554 6664 5426 307 -562 -215 N
ATOM 1125 CA PRO A 149 -26.064 20.595 28.224 1.00 45.77 C
ANISOU 1125 CA PRO A 149 5482 6576 5334 295 -554 -220 C
ATOM 1126 C PRO A 149 -25.457 21.708 27.425 1.00 46.25 C
ANISOU 1126 C PRO A 149 5546 6608 5419 307 -572 -217 C
ATOM 1127 O PRO A 149 -25.083 22.710 27.983 1.00 47.17 O
ANISOU 1127 O PRO A 149 5651 6723 5551 328 -604 -221 O
ATOM 1128 CB PRO A 149 -27.534 20.912 28.475 1.00 47.19 C
ANISOU 1128 CB PRO A 149 5651 6799 5480 297 -571 -249 C
ATOM 1129 CG PRO A 149 -27.615 21.377 29.854 1.00 48.67 C
ANISOU 1129 CG PRO A 149 5819 7009 5663 317 -597 -260 C
ATOM 1130 CD PRO A 149 -26.533 20.701 30.593 1.00 46.92 C
ANISOU 1130 CD PRO A 149 5599 6768 5460 317 -583 -238 C
ATOM 1131 N LYS A 150 -25.332 21.514 26.128 1.00 45.65 N
ANISOU 1131 N LYS A 150 5487 6510 5348 292 -553 -208 N
ATOM 1132 CA LYS A 150 -24.835 22.558 25.275 1.00 46.60 C
ANISOU 1132 CA LYS A 150 5612 6604 5489 300 -569 -205 C
ATOM 1133 C LYS A 150 -26.050 23.429 24.967 1.00 47.94 C
ANISOU 1133 C LYS A 150 5778 6800 5637 306 -597 -233 C
ATOM 1134 O LYS A 150 -26.758 23.170 24.041 1.00 47.26 O
ANISOU 1134 O LYS A 150 5703 6717 5534 291 -584 -240 O
ATOM 1135 CB LYS A 150 -24.250 21.992 24.000 1.00 47.60 C
ANISOU 1135 CB LYS A 150 5761 6697 5628 282 -537 -186 C
ATOM 1136 CG LYS A 150 -23.056 21.104 24.210 1.00 51.43 C
ANISOU 1136 CG LYS A 150 6250 7155 6134 276 -509 -159 C
ATOM 1137 CD LYS A 150 -22.220 21.046 22.975 1.00 56.66 C
ANISOU 1137 CD LYS A 150 6930 7779 6818 266 -488 -140 C
ATOM 1138 CE LYS A 150 -20.763 21.019 23.353 1.00 61.95 C
ANISOU 1138 CE LYS A 150 7597 8418 7524 274 -483 -117 C
ATOM 1139 NZ LYS A 150 -20.082 19.782 22.938 1.00 64.91 N
ANISOU 1139 NZ LYS A 150 7986 8771 7908 256 -443 -96 N
ATOM 1140 N GLU A 151 -26.281 24.452 25.780 1.00 49.66 N
ANISOU 1140 N GLU A 151 5978 7036 5855 328 -636 -250 N
ATOM 1141 CA GLU A 151 -27.441 25.319 25.626 1.00 51.79 C
ANISOU 1141 CA GLU A 151 6240 7333 6104 335 -665 -279 C
ATOM 1142 C GLU A 151 -27.364 26.217 24.414 1.00 52.89 C
ANISOU 1142 C GLU A 151 6391 7451 6255 334 -680 -281 C
ATOM 1143 O GLU A 151 -28.365 26.572 23.873 1.00 54.53 O
ANISOU 1143 O GLU A 151 6602 7675 6444 330 -692 -302 O
ATOM 1144 CB GLU A 151 -27.747 26.092 26.894 1.00 55.71 C
ANISOU 1144 CB GLU A 151 6714 7857 6595 359 -703 -296 C
ATOM 1145 CG GLU A 151 -28.128 25.233 28.080 1.00 62.41 C
ANISOU 1145 CG GLU A 151 7552 8735 7425 358 -690 -300 C
ATOM 1146 CD GLU A 151 -29.442 24.523 27.901 1.00 72.09 C
ANISOU 1146 CD GLU A 151 8780 9994 8617 341 -673 -316 C
ATOM 1147 OE1 GLU A 151 -29.987 24.527 26.802 1.00 75.01 O
ANISOU 1147 OE1 GLU A 151 9161 10359 8979 328 -666 -323 O
ATOM 1148 OE2 GLU A 151 -29.947 23.945 28.851 1.00 75.55 O
ANISOU 1148 OE2 GLU A 151 9208 10462 9036 341 -667 -323 O
ATOM 1149 N GLY A 152 -26.181 26.575 23.976 1.00 51.97 N
ANISOU 1149 N GLY A 152 6281 7298 6169 338 -680 -260 N
ATOM 1150 CA GLY A 152 -26.069 27.353 22.773 1.00 52.25 C
ANISOU 1150 CA GLY A 152 6328 7310 6213 335 -691 -260 C
ATOM 1151 C GLY A 152 -26.615 26.555 21.598 1.00 51.34 C
ANISOU 1151 C GLY A 152 6234 7189 6082 309 -658 -260 C
ATOM 1152 O GLY A 152 -27.428 27.035 20.849 1.00 52.58 O
ANISOU 1152 O GLY A 152 6399 7353 6227 305 -671 -277 O
ATOM 1153 N LYS A 153 -26.148 25.325 21.441 1.00 49.14 N
ANISOU 1153 N LYS A 153 5966 6897 5806 294 -616 -239 N
ATOM 1154 CA LYS A 153 -26.604 24.443 20.383 1.00 47.75 C
ANISOU 1154 CA LYS A 153 5812 6715 5615 270 -582 -236 C
ATOM 1155 C LYS A 153 -28.101 24.146 20.483 1.00 47.49 C
ANISOU 1155 C LYS A 153 5777 6718 5548 263 -585 -261 C
ATOM 1156 O LYS A 153 -28.781 24.106 19.497 1.00 47.20 O
ANISOU 1156 O LYS A 153 5756 6679 5499 251 -580 -270 O
ATOM 1157 CB LYS A 153 -25.784 23.155 20.378 1.00 47.91 C
ANISOU 1157 CB LYS A 153 5842 6718 5645 257 -540 -210 C
ATOM 1158 CG LYS A 153 -25.884 22.330 19.128 1.00 50.03 C
ANISOU 1158 CG LYS A 153 6136 6968 5907 235 -505 -200 C
ATOM 1159 CD LYS A 153 -25.012 21.102 19.217 1.00 53.84 C
ANISOU 1159 CD LYS A 153 6624 7432 6399 224 -467 -174 C
ATOM 1160 CE LYS A 153 -23.542 21.439 19.109 1.00 57.40 C
ANISOU 1160 CE LYS A 153 7076 7849 6886 232 -463 -151 C
ATOM 1161 NZ LYS A 153 -22.637 20.270 19.060 1.00 58.02 N
ANISOU 1161 NZ LYS A 153 7162 7906 6976 221 -426 -127 N
ATOM 1162 N ALA A 154 -28.604 23.954 21.680 1.00 47.53 N
ANISOU 1162 N ALA A 154 5764 6756 5540 272 -595 -273 N
ATOM 1163 CA ALA A 154 -30.008 23.684 21.859 1.00 49.04 C
ANISOU 1163 CA ALA A 154 5950 6983 5700 266 -598 -297 C
ATOM 1164 C ALA A 154 -30.871 24.897 21.465 1.00 51.37 C
ANISOU 1164 C ALA A 154 6242 7291 5987 274 -635 -324 C
ATOM 1165 O ALA A 154 -31.891 24.740 20.859 1.00 51.22 O
ANISOU 1165 O ALA A 154 6231 7283 5949 263 -633 -340 O
ATOM 1166 CB ALA A 154 -30.302 23.268 23.278 1.00 48.70 C
ANISOU 1166 CB ALA A 154 5887 6973 5643 273 -601 -303 C
ATOM 1167 N HIS A 155 -30.434 26.098 21.810 1.00 53.27 N
ANISOU 1167 N HIS A 155 6470 7526 6242 295 -671 -330 N
ATOM 1168 CA HIS A 155 -31.181 27.307 21.482 1.00 56.32 C
ANISOU 1168 CA HIS A 155 6852 7923 6623 304 -711 -357 C
ATOM 1169 C HIS A 155 -31.149 27.627 20.030 1.00 56.74 C
ANISOU 1169 C HIS A 155 6928 7948 6683 292 -709 -354 C
ATOM 1170 O HIS A 155 -32.121 28.047 19.484 1.00 58.22 O
ANISOU 1170 O HIS A 155 7120 8145 6856 288 -725 -377 O
ATOM 1171 CB HIS A 155 -30.742 28.480 22.314 1.00 59.51 C
ANISOU 1171 CB HIS A 155 7237 8333 7042 331 -753 -363 C
ATOM 1172 CG HIS A 155 -31.172 28.361 23.725 1.00 65.67 C
ANISOU 1172 CG HIS A 155 7994 9149 7807 345 -764 -376 C
ATOM 1173 ND1 HIS A 155 -30.428 28.831 24.770 1.00 69.02 N
ANISOU 1173 ND1 HIS A 155 8403 9575 8248 366 -784 -370 N
ATOM 1174 CD2 HIS A 155 -32.255 27.769 24.267 1.00 68.22 C
ANISOU 1174 CD2 HIS A 155 8309 9509 8103 340 -755 -393 C
ATOM 1175 CE1 HIS A 155 -31.050 28.560 25.898 1.00 70.69 C
ANISOU 1175 CE1 HIS A 155 8598 9823 8440 374 -788 -383 C
ATOM 1176 NE2 HIS A 155 -32.155 27.906 25.620 1.00 70.44 N
ANISOU 1176 NE2 HIS A 155 8569 9813 8382 358 -770 -397 N
ATOM 1177 N SER A 156 -30.035 27.363 19.387 1.00 55.51 N
ANISOU 1177 N SER A 156 6787 7755 6549 284 -686 -327 N
ATOM 1178 CA SER A 156 -29.948 27.585 17.976 1.00 56.13 C
ANISOU 1178 CA SER A 156 6889 7804 6633 271 -680 -323 C
ATOM 1179 C SER A 156 -30.872 26.675 17.174 1.00 56.50 C
ANISOU 1179 C SER A 156 6955 7855 6657 249 -652 -328 C
ATOM 1180 O SER A 156 -31.350 27.056 16.153 1.00 57.25 O
ANISOU 1180 O SER A 156 7066 7939 6748 241 -659 -338 O
ATOM 1181 CB SER A 156 -28.511 27.492 17.508 1.00 56.63 C
ANISOU 1181 CB SER A 156 6963 7829 6724 269 -661 -291 C
ATOM 1182 OG SER A 156 -28.248 26.267 16.908 1.00 58.54 O
ANISOU 1182 OG SER A 156 7224 8055 6964 249 -615 -272 O
ATOM 1183 N GLN A 157 -31.128 25.466 17.637 1.00 55.66 N
ANISOU 1183 N GLN A 157 6847 7764 6538 240 -622 -322 N
ATOM 1184 CA GLN A 157 -32.017 24.572 16.956 1.00 55.81 C
ANISOU 1184 CA GLN A 157 6883 7787 6536 221 -597 -326 C
ATOM 1185 C GLN A 157 -33.449 24.716 17.415 1.00 57.03 C
ANISOU 1185 C GLN A 157 7025 7980 6665 223 -617 -357 C
ATOM 1186 O GLN A 157 -34.284 23.978 17.008 1.00 57.84 O
ANISOU 1186 O GLN A 157 7138 8090 6749 208 -600 -362 O
ATOM 1187 CB GLN A 157 -31.603 23.148 17.191 1.00 56.49 C
ANISOU 1187 CB GLN A 157 6975 7871 6620 209 -555 -303 C
ATOM 1188 CG GLN A 157 -30.243 22.835 16.709 1.00 60.07 C
ANISOU 1188 CG GLN A 157 7441 8287 7097 205 -531 -274 C
ATOM 1189 CD GLN A 157 -30.038 21.371 16.662 1.00 65.37 C
ANISOU 1189 CD GLN A 157 8123 8954 7762 189 -489 -254 C
ATOM 1190 OE1 GLN A 157 -30.954 20.608 16.883 1.00 66.93 O
ANISOU 1190 OE1 GLN A 157 8320 9175 7937 180 -479 -263 O
ATOM 1191 NE2 GLN A 157 -28.832 20.968 16.371 1.00 66.50 N
ANISOU 1191 NE2 GLN A 157 8275 9067 7926 186 -466 -228 N
ATOM 1192 N GLY A 158 -33.736 25.643 18.290 1.00 57.57 N
ANISOU 1192 N GLY A 158 7070 8072 6732 242 -653 -376 N
ATOM 1193 CA GLY A 158 -35.083 25.822 18.733 1.00 58.95 C
ANISOU 1193 CA GLY A 158 7232 8284 6883 245 -673 -406 C
ATOM 1194 C GLY A 158 -35.572 24.758 19.664 1.00 59.12 C
ANISOU 1194 C GLY A 158 7240 8336 6885 240 -651 -405 C
ATOM 1195 O GLY A 158 -36.753 24.546 19.765 1.00 60.68 O
ANISOU 1195 O GLY A 158 7434 8561 7062 235 -654 -425 O
ATOM 1196 N CYS A 159 -34.663 24.083 20.349 1.00 57.18 N
ANISOU 1196 N CYS A 159 6990 8087 6649 242 -630 -382 N
ATOM 1197 CA CYS A 159 -35.066 23.050 21.269 1.00 56.93 C
ANISOU 1197 CA CYS A 159 6946 8083 6599 236 -610 -380 C
ATOM 1198 C CYS A 159 -35.782 23.628 22.455 1.00 59.38 C
ANISOU 1198 C CYS A 159 7230 8435 6896 253 -639 -404 C
ATOM 1199 O CYS A 159 -35.499 24.711 22.879 1.00 60.60 O
ANISOU 1199 O CYS A 159 7371 8592 7061 273 -671 -414 O
ATOM 1200 CB CYS A 159 -33.882 22.217 21.755 1.00 54.41 C
ANISOU 1200 CB CYS A 159 6629 7750 6295 234 -582 -350 C
ATOM 1201 SG CYS A 159 -33.003 21.302 20.500 1.00 50.96 S
ANISOU 1201 SG CYS A 159 6223 7268 5873 214 -542 -319 S
ATOM 1202 N GLY A 160 -36.685 22.853 23.014 1.00 59.71 N
ANISOU 1202 N GLY A 160 7263 8510 6915 245 -626 -413 N
ATOM 1203 CA GLY A 160 -37.421 23.268 24.164 1.00 61.28 C
ANISOU 1203 CA GLY A 160 7435 8750 7097 260 -650 -436 C
ATOM 1204 C GLY A 160 -36.657 23.192 25.457 1.00 61.65 C
ANISOU 1204 C GLY A 160 7466 8807 7150 274 -651 -425 C
ATOM 1205 O GLY A 160 -35.547 22.732 25.520 1.00 60.16 O
ANISOU 1205 O GLY A 160 7286 8594 6979 271 -633 -399 O
ATOM 1206 N GLU A 161 -37.285 23.642 26.527 1.00 63.29 N
ANISOU 1206 N GLU A 161 7651 9053 7345 289 -674 -446 N
ATOM 1207 CA GLU A 161 -36.611 23.616 27.784 1.00 63.68 C
ANISOU 1207 CA GLU A 161 7685 9112 7398 304 -678 -438 C
ATOM 1208 C GLU A 161 -36.501 22.209 28.270 1.00 62.04 C
ANISOU 1208 C GLU A 161 7480 8911 7180 287 -641 -419 C
ATOM 1209 O GLU A 161 -37.416 21.443 28.186 1.00 63.12 O
ANISOU 1209 O GLU A 161 7617 9070 7295 271 -624 -424 O
ATOM 1210 CB GLU A 161 -37.264 24.534 28.801 1.00 69.36 C
ANISOU 1210 CB GLU A 161 8380 9869 8106 327 -713 -466 C
ATOM 1211 CG GLU A 161 -36.335 25.632 29.264 1.00 77.68 C
ANISOU 1211 CG GLU A 161 9426 10908 9181 352 -745 -464 C
ATOM 1212 CD GLU A 161 -35.790 26.464 28.124 1.00 87.96 C
ANISOU 1212 CD GLU A 161 10742 12173 10506 354 -761 -461 C
ATOM 1213 OE1 GLU A 161 -34.674 26.973 28.229 1.00 90.37 O
ANISOU 1213 OE1 GLU A 161 11049 12452 10837 367 -773 -446 O
ATOM 1214 OE2 GLU A 161 -36.470 26.611 27.108 1.00 91.70 O
ANISOU 1214 OE2 GLU A 161 11225 12642 10973 343 -762 -473 O
ATOM 1215 N GLY A 162 -35.315 21.871 28.730 1.00 59.46 N
ANISOU 1215 N GLY A 162 7156 8564 6872 289 -630 -395 N
ATOM 1216 CA GLY A 162 -35.018 20.539 29.203 1.00 57.68 C
ANISOU 1216 CA GLY A 162 6935 8340 6640 273 -597 -374 C
ATOM 1217 C GLY A 162 -34.561 19.617 28.088 1.00 55.00 C
ANISOU 1217 C GLY A 162 6620 7968 6310 250 -564 -351 C
ATOM 1218 O GLY A 162 -34.367 18.450 28.309 1.00 55.25 O
ANISOU 1218 O GLY A 162 6658 7999 6337 235 -536 -334 O
ATOM 1219 N GLN A 163 -34.407 20.158 26.891 1.00 51.87 N
ANISOU 1219 N GLN A 163 6237 7543 5926 249 -568 -351 N
ATOM 1220 CA GLN A 163 -33.997 19.396 25.735 1.00 48.46 C
ANISOU 1220 CA GLN A 163 5831 7080 5504 229 -539 -331 C
ATOM 1221 C GLN A 163 -32.649 19.830 25.230 1.00 44.99 C
ANISOU 1221 C GLN A 163 5401 6597 5095 236 -539 -312 C
ATOM 1222 O GLN A 163 -32.238 20.931 25.457 1.00 45.61 O
ANISOU 1222 O GLN A 163 5471 6670 5189 255 -567 -319 O
ATOM 1223 CB GLN A 163 -34.998 19.569 24.599 1.00 49.78 C
ANISOU 1223 CB GLN A 163 6009 7247 5658 219 -540 -346 C
ATOM 1224 CG GLN A 163 -36.339 18.972 24.855 1.00 54.06 C
ANISOU 1224 CG GLN A 163 6544 7827 6171 208 -535 -361 C
ATOM 1225 CD GLN A 163 -37.219 19.019 23.660 1.00 58.78 C
ANISOU 1225 CD GLN A 163 7157 8419 6759 197 -533 -373 C
ATOM 1226 OE1 GLN A 163 -37.076 19.851 22.809 1.00 59.22 O
ANISOU 1226 OE1 GLN A 163 7222 8453 6827 202 -548 -379 O
ATOM 1227 NE2 GLN A 163 -38.135 18.119 23.605 1.00 60.69 N
ANISOU 1227 NE2 GLN A 163 7400 8680 6979 181 -517 -375 N
ATOM 1228 N VAL A 164 -31.998 18.923 24.527 1.00 41.35 N
ANISOU 1228 N VAL A 164 4960 6107 4645 219 -507 -288 N
ATOM 1229 CA VAL A 164 -30.735 19.150 23.890 1.00 39.01 C
ANISOU 1229 CA VAL A 164 4676 5768 4377 221 -500 -268 C
ATOM 1230 C VAL A 164 -30.786 18.621 22.478 1.00 36.62 C
ANISOU 1230 C VAL A 164 4399 5441 4075 203 -476 -258 C
ATOM 1231 O VAL A 164 -31.635 17.862 22.152 1.00 36.58 O
ANISOU 1231 O VAL A 164 4401 5450 4049 188 -461 -262 O
ATOM 1232 CB VAL A 164 -29.597 18.384 24.575 1.00 39.34 C
ANISOU 1232 CB VAL A 164 4717 5795 4436 220 -481 -244 C
ATOM 1233 CG1 VAL A 164 -29.415 18.854 25.992 1.00 40.37 C
ANISOU 1233 CG1 VAL A 164 4825 5944 4568 239 -504 -251 C
ATOM 1234 CG2 VAL A 164 -29.844 16.900 24.522 1.00 39.36 C
ANISOU 1234 CG2 VAL A 164 4729 5802 4422 198 -448 -232 C
ATOM 1235 N ALA A 165 -29.857 19.061 21.664 1.00 34.52 N
ANISOU 1235 N ALA A 165 4145 5139 3833 205 -474 -245 N
ATOM 1236 CA ALA A 165 -29.711 18.534 20.337 1.00 34.01 C
ANISOU 1236 CA ALA A 165 4106 5047 3771 188 -448 -232 C
ATOM 1237 C ALA A 165 -29.132 17.126 20.570 1.00 32.93 C
ANISOU 1237 C ALA A 165 3975 4900 3635 175 -413 -209 C
ATOM 1238 O ALA A 165 -28.133 16.981 21.196 1.00 33.04 O
ANISOU 1238 O ALA A 165 3983 4903 3667 181 -409 -195 O
ATOM 1239 CB ALA A 165 -28.768 19.381 19.541 1.00 34.11 C
ANISOU 1239 CB ALA A 165 4127 5023 3809 195 -455 -223 C
ATOM 1240 N CYS A 166 -29.803 16.102 20.102 1.00 31.92 N
ANISOU 1240 N CYS A 166 3861 4779 3487 157 -391 -207 N
ATOM 1241 CA CYS A 166 -29.356 14.752 20.340 1.00 30.82 C
ANISOU 1241 CA CYS A 166 3728 4635 3348 144 -361 -188 C
ATOM 1242 C CYS A 166 -28.236 14.305 19.435 1.00 30.19 C
ANISOU 1242 C CYS A 166 3668 4514 3289 136 -336 -164 C
ATOM 1243 O CYS A 166 -28.477 13.850 18.346 1.00 30.81 O
ANISOU 1243 O CYS A 166 3767 4578 3361 124 -318 -159 O
ATOM 1244 CB CYS A 166 -30.503 13.762 20.316 1.00 31.42 C
ANISOU 1244 CB CYS A 166 3809 4736 3394 127 -349 -194 C
ATOM 1245 SG CYS A 166 -30.019 12.119 20.768 1.00 35.92 S
ANISOU 1245 SG CYS A 166 4384 5304 3961 111 -318 -171 S
ATOM 1246 N LEU A 167 -27.022 14.464 19.932 1.00 28.78 N
ANISOU 1246 N LEU A 167 3483 4318 3136 145 -335 -150 N
ATOM 1247 CA LEU A 167 -25.791 14.110 19.268 1.00 28.22 C
ANISOU 1247 CA LEU A 167 3425 4207 3088 141 -312 -127 C
ATOM 1248 C LEU A 167 -24.927 13.191 20.128 1.00 26.97 C
ANISOU 1248 C LEU A 167 3262 4045 2942 139 -297 -110 C
ATOM 1249 O LEU A 167 -24.666 13.525 21.244 1.00 27.43 O
ANISOU 1249 O LEU A 167 3301 4114 3007 150 -313 -113 O
ATOM 1250 CB LEU A 167 -25.032 15.371 18.931 1.00 28.90 C
ANISOU 1250 CB LEU A 167 3509 4271 3201 156 -329 -125 C
ATOM 1251 CG LEU A 167 -25.821 16.273 17.989 1.00 31.91 C
ANISOU 1251 CG LEU A 167 3899 4654 3572 158 -345 -141 C
ATOM 1252 CD1 LEU A 167 -25.350 17.697 18.039 1.00 32.56 C
ANISOU 1252 CD1 LEU A 167 3971 4727 3674 175 -374 -147 C
ATOM 1253 CD2 LEU A 167 -25.848 15.702 16.583 1.00 33.07 C
ANISOU 1253 CD2 LEU A 167 4072 4777 3714 142 -318 -132 C
ATOM 1254 N PHE A 168 -24.489 12.064 19.572 1.00 25.70 N
ANISOU 1254 N PHE A 168 3117 3864 2783 124 -267 -93 N
ATOM 1255 CA PHE A 168 -23.708 11.052 20.268 1.00 25.19 C
ANISOU 1255 CA PHE A 168 3050 3794 2729 118 -251 -77 C
ATOM 1256 C PHE A 168 -22.618 11.578 21.168 1.00 25.75 C
ANISOU 1256 C PHE A 168 3105 3852 2828 133 -263 -70 C
ATOM 1257 O PHE A 168 -22.640 11.346 22.338 1.00 25.90 O
ANISOU 1257 O PHE A 168 3110 3887 2843 135 -272 -73 O
ATOM 1258 CB PHE A 168 -23.092 10.017 19.342 1.00 24.21 C
ANISOU 1258 CB PHE A 168 2947 3641 2611 104 -218 -58 C
ATOM 1259 CG PHE A 168 -22.522 8.839 20.062 1.00 22.79 C
ANISOU 1259 CG PHE A 168 2765 3458 2435 95 -204 -45 C
ATOM 1260 CD1 PHE A 168 -21.264 8.885 20.611 1.00 23.23 C
ANISOU 1260 CD1 PHE A 168 2813 3492 2520 102 -202 -33 C
ATOM 1261 CD2 PHE A 168 -23.253 7.710 20.222 1.00 23.09 C
ANISOU 1261 CD2 PHE A 168 2809 3516 2448 80 -193 -46 C
ATOM 1262 CE1 PHE A 168 -20.739 7.817 21.273 1.00 23.37 C
ANISOU 1262 CE1 PHE A 168 2830 3506 2542 94 -190 -22 C
ATOM 1263 CE2 PHE A 168 -22.744 6.630 20.905 1.00 23.64 C
ANISOU 1263 CE2 PHE A 168 2877 3584 2521 71 -182 -34 C
ATOM 1264 CZ PHE A 168 -21.480 6.689 21.427 1.00 22.50 C
ANISOU 1264 CZ PHE A 168 2726 3416 2406 78 -181 -23 C
ATOM 1265 N GLU A 169 -21.730 12.368 20.611 1.00 25.11 N
ANISOU 1265 N GLU A 169 3026 3741 2773 142 -265 -63 N
ATOM 1266 CA GLU A 169 -20.621 12.928 21.341 1.00 25.58 C
ANISOU 1266 CA GLU A 169 3072 3784 2863 157 -276 -54 C
ATOM 1267 C GLU A 169 -20.960 14.055 22.322 1.00 26.88 C
ANISOU 1267 C GLU A 169 3216 3970 3028 176 -312 -70 C
ATOM 1268 O GLU A 169 -20.143 14.442 23.094 1.00 27.30 O
ANISOU 1268 O GLU A 169 3258 4012 3104 188 -324 -64 O
ATOM 1269 CB GLU A 169 -19.475 13.295 20.409 1.00 27.47 C
ANISOU 1269 CB GLU A 169 3322 3984 3134 160 -264 -38 C
ATOM 1270 CG GLU A 169 -18.842 12.115 19.699 1.00 29.46 C
ANISOU 1270 CG GLU A 169 3591 4211 3392 144 -228 -20 C
ATOM 1271 CD GLU A 169 -17.621 12.445 18.862 1.00 34.54 C
ANISOU 1271 CD GLU A 169 4241 4815 4067 148 -215 -3 C
ATOM 1272 OE1 GLU A 169 -16.929 13.405 19.117 1.00 35.50 O
ANISOU 1272 OE1 GLU A 169 4351 4923 4213 162 -231 1 O
ATOM 1273 OE2 GLU A 169 -17.344 11.708 17.955 1.00 35.54 O
ANISOU 1273 OE2 GLU A 169 4386 4925 4194 136 -187 8 O
ATOM 1274 N ASP A 170 -22.173 14.569 22.285 1.00 27.06 N
ANISOU 1274 N ASP A 170 3235 4022 3025 178 -330 -90 N
ATOM 1275 CA ASP A 170 -22.580 15.581 23.214 1.00 27.77 C
ANISOU 1275 CA ASP A 170 3305 4134 3112 196 -364 -107 C
ATOM 1276 C ASP A 170 -23.114 14.951 24.491 1.00 27.37 C
ANISOU 1276 C ASP A 170 3242 4115 3042 194 -368 -115 C
ATOM 1277 O ASP A 170 -22.957 15.496 25.525 1.00 29.42 O
ANISOU 1277 O ASP A 170 3486 4384 3308 209 -391 -120 O
ATOM 1278 CB ASP A 170 -23.659 16.475 22.623 1.00 30.65 C
ANISOU 1278 CB ASP A 170 3670 4517 3457 199 -383 -128 C
ATOM 1279 CG ASP A 170 -23.124 17.510 21.679 1.00 36.69 C
ANISOU 1279 CG ASP A 170 4441 5255 4243 207 -393 -124 C
ATOM 1280 OD1 ASP A 170 -21.929 17.563 21.467 1.00 36.74 O
ANISOU 1280 OD1 ASP A 170 4452 5230 4279 210 -384 -105 O
ATOM 1281 OD2 ASP A 170 -23.925 18.267 21.150 1.00 38.56 O
ANISOU 1281 OD2 ASP A 170 4680 5504 4468 210 -410 -140 O
ATOM 1282 N VAL A 171 -23.763 13.809 24.384 1.00 25.22 N
ANISOU 1282 N VAL A 171 2979 3858 2747 175 -348 -115 N
ATOM 1283 CA VAL A 171 -24.344 13.135 25.527 1.00 24.68 C
ANISOU 1283 CA VAL A 171 2899 3821 2657 171 -350 -121 C
ATOM 1284 C VAL A 171 -23.552 11.965 26.118 1.00 23.53 C
ANISOU 1284 C VAL A 171 2757 3663 2521 160 -330 -104 C
ATOM 1285 O VAL A 171 -23.619 11.737 27.308 1.00 22.87 O
ANISOU 1285 O VAL A 171 2662 3597 2432 163 -340 -107 O
ATOM 1286 CB VAL A 171 -25.816 12.730 25.274 1.00 25.89 C
ANISOU 1286 CB VAL A 171 3055 4009 2774 158 -347 -137 C
ATOM 1287 CG1 VAL A 171 -26.641 13.920 24.879 1.00 27.83 C
ANISOU 1287 CG1 VAL A 171 3296 4269 3010 170 -370 -157 C
ATOM 1288 CG2 VAL A 171 -25.959 11.641 24.240 1.00 24.88 C
ANISOU 1288 CG2 VAL A 171 2947 3868 2636 137 -317 -125 C
ATOM 1289 N VAL A 172 -22.841 11.204 25.306 1.00 22.01 N
ANISOU 1289 N VAL A 172 2581 3440 2341 148 -304 -86 N
ATOM 1290 CA VAL A 172 -22.057 10.091 25.792 1.00 21.42 C
ANISOU 1290 CA VAL A 172 2511 3352 2278 137 -287 -70 C
ATOM 1291 C VAL A 172 -20.616 10.549 26.035 1.00 20.88 C
ANISOU 1291 C VAL A 172 2438 3247 2248 150 -290 -56 C
ATOM 1292 O VAL A 172 -19.974 10.987 25.138 1.00 20.24 O
ANISOU 1292 O VAL A 172 2364 3138 2187 154 -284 -48 O
ATOM 1293 CB VAL A 172 -22.094 8.838 24.868 1.00 21.54 C
ANISOU 1293 CB VAL A 172 2546 3356 2284 115 -256 -58 C
ATOM 1294 CG1 VAL A 172 -21.261 7.724 25.450 1.00 20.56 C
ANISOU 1294 CG1 VAL A 172 2424 3217 2171 105 -242 -43 C
ATOM 1295 CG2 VAL A 172 -23.500 8.359 24.578 1.00 22.06 C
ANISOU 1295 CG2 VAL A 172 2616 3454 2312 102 -253 -69 C
ATOM 1296 N PRO A 173 -20.127 10.455 27.280 1.00 21.07 N
ANISOU 1296 N PRO A 173 2451 3273 2283 156 -302 -54 N
ATOM 1297 CA PRO A 173 -18.754 10.850 27.579 1.00 21.20 C
ANISOU 1297 CA PRO A 173 2464 3254 2338 169 -306 -41 C
ATOM 1298 C PRO A 173 -17.747 9.922 26.900 1.00 20.56 C
ANISOU 1298 C PRO A 173 2397 3137 2278 156 -277 -21 C
ATOM 1299 O PRO A 173 -17.967 8.750 26.922 1.00 20.84 O
ANISOU 1299 O PRO A 173 2441 3179 2298 138 -260 -18 O
ATOM 1300 CB PRO A 173 -18.661 10.687 29.092 1.00 22.15 C
ANISOU 1300 CB PRO A 173 2572 3387 2458 174 -322 -45 C
ATOM 1301 CG PRO A 173 -20.013 10.440 29.565 1.00 22.72 C
ANISOU 1301 CG PRO A 173 2639 3504 2491 168 -329 -61 C
ATOM 1302 CD PRO A 173 -20.777 9.866 28.443 1.00 20.71 C
ANISOU 1302 CD PRO A 173 2397 3258 2214 151 -308 -63 C
ATOM 1303 N MET A 174 -16.693 10.463 26.318 1.00 19.65 N
ANISOU 1303 N MET A 174 2284 2987 2196 164 -274 -9 N
ATOM 1304 CA MET A 174 -15.675 9.677 25.647 1.00 20.62 C
ANISOU 1304 CA MET A 174 2419 3075 2341 154 -247 9 C
ATOM 1305 C MET A 174 -14.830 8.827 26.599 1.00 20.40 C
ANISOU 1305 C MET A 174 2388 3031 2330 149 -243 19 C
ATOM 1306 O MET A 174 -14.284 7.871 26.191 1.00 21.14 O
ANISOU 1306 O MET A 174 2493 3106 2432 136 -220 30 O
ATOM 1307 CB MET A 174 -14.765 10.517 24.790 1.00 23.28 C
ANISOU 1307 CB MET A 174 2757 3378 2708 165 -244 20 C
ATOM 1308 CG MET A 174 -15.277 10.823 23.412 1.00 29.89 C
ANISOU 1308 CG MET A 174 3607 4217 3533 160 -232 17 C
ATOM 1309 SD MET A 174 -15.784 9.439 22.381 1.00 37.65 S
ANISOU 1309 SD MET A 174 4611 5203 4490 136 -198 21 S
ATOM 1310 CE MET A 174 -17.542 9.660 22.559 1.00 34.81 C
ANISOU 1310 CE MET A 174 4249 4890 4086 133 -215 -1 C
ATOM 1311 N ASN A 175 -14.722 9.221 27.859 1.00 19.97 N
ANISOU 1311 N ASN A 175 2321 2985 2283 161 -266 14 N
ATOM 1312 CA ASN A 175 -13.988 8.412 28.821 1.00 20.69 C
ANISOU 1312 CA ASN A 175 2411 3062 2389 156 -265 21 C
ATOM 1313 C ASN A 175 -14.724 7.076 29.039 1.00 19.65 C
ANISOU 1313 C ASN A 175 2287 2953 2225 133 -251 18 C
ATOM 1314 O ASN A 175 -14.101 6.090 29.136 1.00 19.10 O
ANISOU 1314 O ASN A 175 2225 2866 2166 121 -237 27 O
ATOM 1315 CB ASN A 175 -13.596 9.149 30.121 1.00 22.28 C
ANISOU 1315 CB ASN A 175 2598 3261 2608 174 -294 18 C
ATOM 1316 CG ASN A 175 -14.745 9.867 30.802 1.00 24.58 C
ANISOU 1316 CG ASN A 175 2878 3592 2870 184 -319 -1 C
ATOM 1317 OD1 ASN A 175 -15.879 9.656 30.529 1.00 25.24 O
ANISOU 1317 OD1 ASN A 175 2964 3708 2919 175 -315 -12 O
ATOM 1318 ND2 ASN A 175 -14.409 10.703 31.735 1.00 25.37 N
ANISOU 1318 ND2 ASN A 175 2965 3687 2985 204 -345 -4 N
ATOM 1319 N TYR A 176 -16.052 7.107 29.072 1.00 18.69 N
ANISOU 1319 N TYR A 176 2165 2872 2066 129 -257 3 N
ATOM 1320 CA TYR A 176 -16.870 5.917 29.153 1.00 18.30 C
ANISOU 1320 CA TYR A 176 2123 2848 1984 108 -244 0 C
ATOM 1321 C TYR A 176 -16.633 5.066 27.926 1.00 17.66 C
ANISOU 1321 C TYR A 176 2059 2749 1904 92 -216 12 C
ATOM 1322 O TYR A 176 -16.400 3.930 28.042 1.00 18.63 O
ANISOU 1322 O TYR A 176 2190 2866 2025 76 -203 19 O
ATOM 1323 CB TYR A 176 -18.387 6.187 29.265 1.00 18.18 C
ANISOU 1323 CB TYR A 176 2102 2878 1929 106 -255 -17 C
ATOM 1324 CG TYR A 176 -19.221 4.984 28.935 1.00 18.38 C
ANISOU 1324 CG TYR A 176 2138 2924 1923 83 -238 -17 C
ATOM 1325 CD1 TYR A 176 -19.512 4.034 29.881 1.00 18.57 C
ANISOU 1325 CD1 TYR A 176 2161 2966 1930 70 -239 -18 C
ATOM 1326 CD2 TYR A 176 -19.666 4.760 27.655 1.00 17.67 C
ANISOU 1326 CD2 TYR A 176 2061 2833 1821 75 -221 -15 C
ATOM 1327 CE1 TYR A 176 -20.236 2.923 29.585 1.00 18.61 C
ANISOU 1327 CE1 TYR A 176 2175 2989 1907 49 -226 -16 C
ATOM 1328 CE2 TYR A 176 -20.390 3.647 27.343 1.00 18.72 C
ANISOU 1328 CE2 TYR A 176 2204 2983 1927 55 -207 -14 C
ATOM 1329 CZ TYR A 176 -20.681 2.723 28.310 1.00 19.85 C
ANISOU 1329 CZ TYR A 176 2344 3145 2054 42 -210 -14 C
ATOM 1330 OH TYR A 176 -21.378 1.644 27.980 1.00 20.18 O
ANISOU 1330 OH TYR A 176 2396 3202 2070 22 -198 -12 O
ATOM 1331 N MET A 177 -16.682 5.683 26.760 1.00 16.29 N
ANISOU 1331 N MET A 177 1890 2565 1734 98 -209 13 N
ATOM 1332 CA MET A 177 -16.518 5.018 25.490 1.00 15.40 C
ANISOU 1332 CA MET A 177 1794 2436 1621 86 -182 22 C
ATOM 1333 C MET A 177 -15.167 4.345 25.321 1.00 16.79 C
ANISOU 1333 C MET A 177 1977 2573 1829 81 -165 39 C
ATOM 1334 O MET A 177 -15.101 3.256 24.868 1.00 17.69 O
ANISOU 1334 O MET A 177 2104 2681 1936 66 -146 46 O
ATOM 1335 CB MET A 177 -16.746 5.989 24.342 1.00 15.40 C
ANISOU 1335 CB MET A 177 1799 2431 1622 95 -180 20 C
ATOM 1336 CG MET A 177 -18.197 6.302 24.005 1.00 19.03 C
ANISOU 1336 CG MET A 177 2260 2926 2046 93 -188 4 C
ATOM 1337 SD MET A 177 -19.306 4.915 23.955 1.00 19.85 S
ANISOU 1337 SD MET A 177 2373 3057 2110 70 -175 1 S
ATOM 1338 CE MET A 177 -18.690 4.072 22.529 1.00 16.46 C
ANISOU 1338 CE MET A 177 1968 2596 1691 58 -144 18 C
ATOM 1339 N VAL A 178 -14.111 5.031 25.711 1.00 16.82 N
ANISOU 1339 N VAL A 178 1972 2551 1868 96 -174 45 N
ATOM 1340 CA VAL A 178 -12.755 4.518 25.590 1.00 17.34 C
ANISOU 1340 CA VAL A 178 2042 2577 1968 94 -159 60 C
ATOM 1341 C VAL A 178 -12.313 3.555 26.709 1.00 17.93 C
ANISOU 1341 C VAL A 178 2115 2648 2050 84 -163 62 C
ATOM 1342 O VAL A 178 -11.985 2.458 26.430 1.00 17.07 O
ANISOU 1342 O VAL A 178 2017 2528 1942 70 -146 70 O
ATOM 1343 CB VAL A 178 -11.743 5.643 25.413 1.00 18.01 C
ANISOU 1343 CB VAL A 178 2118 2632 2091 112 -166 67 C
ATOM 1344 CG1 VAL A 178 -10.335 5.144 25.480 1.00 19.20 C
ANISOU 1344 CG1 VAL A 178 2271 2743 2281 111 -154 81 C
ATOM 1345 CG2 VAL A 178 -11.988 6.393 24.138 1.00 18.21 C
ANISOU 1345 CG2 VAL A 178 2150 2655 2114 118 -157 67 C
ATOM 1346 N TYR A 179 -12.326 4.003 27.954 1.00 18.64 N
ANISOU 1346 N TYR A 179 2192 2747 2144 93 -187 56 N
ATOM 1347 CA TYR A 179 -11.899 3.189 29.081 1.00 20.99 C
ANISOU 1347 CA TYR A 179 2488 3038 2448 85 -194 58 C
ATOM 1348 C TYR A 179 -12.848 2.080 29.517 1.00 21.28 C
ANISOU 1348 C TYR A 179 2531 3106 2448 65 -192 52 C
ATOM 1349 O TYR A 179 -12.418 0.990 29.739 1.00 22.03 O
ANISOU 1349 O TYR A 179 2633 3190 2547 51 -184 58 O
ATOM 1350 CB TYR A 179 -11.562 4.043 30.290 1.00 21.75 C
ANISOU 1350 CB TYR A 179 2571 3132 2563 103 -220 54 C
ATOM 1351 CG TYR A 179 -10.429 5.026 30.160 1.00 24.52 C
ANISOU 1351 CG TYR A 179 2915 3447 2957 122 -226 62 C
ATOM 1352 CD1 TYR A 179 -9.226 4.673 29.624 1.00 26.90 C
ANISOU 1352 CD1 TYR A 179 3221 3708 3293 120 -210 76 C
ATOM 1353 CD2 TYR A 179 -10.573 6.309 30.589 1.00 25.50 C
ANISOU 1353 CD2 TYR A 179 3026 3577 3086 143 -250 56 C
ATOM 1354 CE1 TYR A 179 -8.212 5.571 29.510 1.00 28.95 C
ANISOU 1354 CE1 TYR A 179 3473 3935 3591 137 -215 85 C
ATOM 1355 CE2 TYR A 179 -9.553 7.208 30.492 1.00 27.98 C
ANISOU 1355 CE2 TYR A 179 3334 3859 3440 161 -258 65 C
ATOM 1356 CZ TYR A 179 -8.379 6.827 29.949 1.00 30.55 C
ANISOU 1356 CZ TYR A 179 3664 4145 3800 157 -240 80 C
ATOM 1357 OH TYR A 179 -7.395 7.722 29.836 1.00 34.81 O
ANISOU 1357 OH TYR A 179 4196 4653 4378 175 -247 89 O
ATOM 1358 N PHE A 180 -14.118 2.397 29.653 1.00 19.99 N
ANISOU 1358 N PHE A 180 2363 2982 2249 65 -201 39 N
ATOM 1359 CA PHE A 180 -15.106 1.443 30.105 1.00 20.51 C
ANISOU 1359 CA PHE A 180 2432 3081 2278 47 -201 33 C
ATOM 1360 C PHE A 180 -15.600 0.534 29.000 1.00 21.02 C
ANISOU 1360 C PHE A 180 2512 3152 2322 30 -180 37 C
ATOM 1361 O PHE A 180 -15.475 -0.630 29.089 1.00 22.31 O
ANISOU 1361 O PHE A 180 2684 3312 2480 12 -171 43 O
ATOM 1362 CB PHE A 180 -16.256 2.148 30.811 1.00 20.86 C
ANISOU 1362 CB PHE A 180 2465 3167 2295 54 -221 18 C
ATOM 1363 CG PHE A 180 -17.160 1.241 31.608 1.00 22.01 C
ANISOU 1363 CG PHE A 180 2610 3346 2406 37 -226 12 C
ATOM 1364 CD1 PHE A 180 -18.216 0.584 31.026 1.00 22.06 C
ANISOU 1364 CD1 PHE A 180 2624 3380 2378 21 -215 9 C
ATOM 1365 CD2 PHE A 180 -16.969 1.077 32.949 1.00 23.57 C
ANISOU 1365 CD2 PHE A 180 2801 3548 2605 37 -242 9 C
ATOM 1366 CE1 PHE A 180 -19.066 -0.213 31.757 1.00 22.73 C
ANISOU 1366 CE1 PHE A 180 2708 3497 2432 5 -220 4 C
ATOM 1367 CE2 PHE A 180 -17.807 0.265 33.676 1.00 24.62 C
ANISOU 1367 CE2 PHE A 180 2934 3714 2706 20 -246 4 C
ATOM 1368 CZ PHE A 180 -18.854 -0.382 33.083 1.00 23.04 C
ANISOU 1368 CZ PHE A 180 2740 3542 2473 4 -235 2 C
ATOM 1369 N ASN A 181 -16.134 1.111 27.959 1.00 19.89 N
ANISOU 1369 N ASN A 181 2373 3016 2170 35 -172 35 N
ATOM 1370 CA ASN A 181 -16.630 0.347 26.858 1.00 20.21 C
ANISOU 1370 CA ASN A 181 2428 3061 2191 21 -153 39 C
ATOM 1371 C ASN A 181 -15.553 -0.329 26.004 1.00 21.31 C
ANISOU 1371 C ASN A 181 2581 3162 2355 16 -131 53 C
ATOM 1372 O ASN A 181 -15.559 -1.512 25.914 1.00 22.26 O
ANISOU 1372 O ASN A 181 2712 3282 2466 -1 -121 59 O
ATOM 1373 CB ASN A 181 -17.585 1.143 25.995 1.00 21.20 C
ANISOU 1373 CB ASN A 181 2554 3204 2296 28 -153 30 C
ATOM 1374 CG ASN A 181 -18.480 0.251 25.162 1.00 25.14 C
ANISOU 1374 CG ASN A 181 3068 3719 2765 11 -139 31 C
ATOM 1375 OD1 ASN A 181 -19.522 -0.170 25.585 1.00 27.23 O
ANISOU 1375 OD1 ASN A 181 3331 4016 3000 2 -145 24 O
ATOM 1376 ND2 ASN A 181 -18.036 -0.056 24.016 1.00 23.68 N
ANISOU 1376 ND2 ASN A 181 2897 3509 2590 9 -119 41 N
ATOM 1377 N PHE A 182 -14.654 0.425 25.401 1.00 19.53 N
ANISOU 1377 N PHE A 182 2355 2906 2160 29 -125 59 N
ATOM 1378 CA PHE A 182 -13.642 -0.153 24.547 1.00 19.91 C
ANISOU 1378 CA PHE A 182 2415 2919 2231 25 -103 72 C
ATOM 1379 C PHE A 182 -12.618 -1.055 25.249 1.00 21.35 C
ANISOU 1379 C PHE A 182 2598 3079 2437 17 -101 80 C
ATOM 1380 O PHE A 182 -12.577 -2.205 24.976 1.00 21.70 O
ANISOU 1380 O PHE A 182 2653 3119 2472 2 -90 85 O
ATOM 1381 CB PHE A 182 -12.961 0.900 23.665 1.00 20.00 C
ANISOU 1381 CB PHE A 182 2426 2906 2270 41 -95 77 C
ATOM 1382 CG PHE A 182 -11.956 0.354 22.675 1.00 21.60 C
ANISOU 1382 CG PHE A 182 2640 3073 2494 38 -70 91 C
ATOM 1383 CD1 PHE A 182 -12.195 -0.784 21.957 1.00 21.71 C
ANISOU 1383 CD1 PHE A 182 2670 3087 2491 23 -52 95 C
ATOM 1384 CD2 PHE A 182 -10.789 1.039 22.424 1.00 22.43 C
ANISOU 1384 CD2 PHE A 182 2740 3145 2638 51 -65 99 C
ATOM 1385 CE1 PHE A 182 -11.284 -1.250 21.036 1.00 22.30 C
ANISOU 1385 CE1 PHE A 182 2757 3131 2586 21 -29 106 C
ATOM 1386 CE2 PHE A 182 -9.884 0.582 21.512 1.00 23.68 C
ANISOU 1386 CE2 PHE A 182 2908 3272 2816 48 -41 110 C
ATOM 1387 CZ PHE A 182 -10.133 -0.572 20.820 1.00 23.16 C
ANISOU 1387 CZ PHE A 182 2859 3208 2732 33 -23 114 C
ATOM 1388 N PHE A 183 -11.822 -0.495 26.141 1.00 21.58 N
ANISOU 1388 N PHE A 183 2614 3091 2494 29 -115 80 N
ATOM 1389 CA PHE A 183 -10.764 -1.215 26.840 1.00 22.49 C
ANISOU 1389 CA PHE A 183 2729 3181 2636 23 -116 87 C
ATOM 1390 C PHE A 183 -11.273 -2.370 27.701 1.00 22.02 C
ANISOU 1390 C PHE A 183 2673 3141 2553 4 -124 83 C
ATOM 1391 O PHE A 183 -10.911 -3.476 27.502 1.00 21.91 O
ANISOU 1391 O PHE A 183 2669 3114 2540 -10 -113 89 O
ATOM 1392 CB PHE A 183 -9.889 -0.274 27.677 1.00 23.92 C
ANISOU 1392 CB PHE A 183 2895 3340 2852 40 -132 88 C
ATOM 1393 CG PHE A 183 -9.025 0.690 26.896 1.00 24.66 C
ANISOU 1393 CG PHE A 183 2986 3405 2980 57 -124 95 C
ATOM 1394 CD1 PHE A 183 -8.968 0.684 25.530 1.00 25.17 C
ANISOU 1394 CD1 PHE A 183 3059 3460 3043 56 -102 101 C
ATOM 1395 CD2 PHE A 183 -8.279 1.623 27.565 1.00 25.93 C
ANISOU 1395 CD2 PHE A 183 3134 3547 3173 74 -140 97 C
ATOM 1396 CE1 PHE A 183 -8.185 1.574 24.850 1.00 26.06 C
ANISOU 1396 CE1 PHE A 183 3169 3547 3186 70 -94 109 C
ATOM 1397 CE2 PHE A 183 -7.488 2.515 26.901 1.00 27.17 C
ANISOU 1397 CE2 PHE A 183 3287 3677 3361 89 -134 105 C
ATOM 1398 CZ PHE A 183 -7.437 2.491 25.535 1.00 26.70 C
ANISOU 1398 CZ PHE A 183 3236 3610 3299 87 -111 111 C
ATOM 1399 N ALA A 184 -12.138 -2.060 28.642 1.00 20.88 N
ANISOU 1399 N ALA A 184 2519 3028 2385 5 -143 73 N
ATOM 1400 CA ALA A 184 -12.666 -3.034 29.556 1.00 21.08 C
ANISOU 1400 CA ALA A 184 2547 3075 2387 -13 -153 69 C
ATOM 1401 C ALA A 184 -13.656 -4.063 29.013 1.00 20.93 C
ANISOU 1401 C ALA A 184 2540 3082 2331 -32 -143 69 C
ATOM 1402 O ALA A 184 -13.463 -5.220 29.186 1.00 21.65 O
ANISOU 1402 O ALA A 184 2640 3169 2419 -49 -140 73 O
ATOM 1403 CB ALA A 184 -13.250 -2.338 30.756 1.00 20.33 C
ANISOU 1403 CB ALA A 184 2439 3006 2280 -5 -176 58 C
ATOM 1404 N CYS A 185 -14.692 -3.605 28.339 1.00 19.03 N
ANISOU 1404 N CYS A 185 2299 2866 2063 -29 -139 64 N
ATOM 1405 CA CYS A 185 -15.748 -4.468 27.875 1.00 19.76 C
ANISOU 1405 CA CYS A 185 2402 2986 2120 -46 -133 63 C
ATOM 1406 C CYS A 185 -15.663 -5.053 26.458 1.00 20.04 C
ANISOU 1406 C CYS A 185 2454 3007 2153 -52 -111 71 C
ATOM 1407 O CYS A 185 -16.341 -5.968 26.155 1.00 20.74 O
ANISOU 1407 O CYS A 185 2553 3112 2217 -67 -107 73 O
ATOM 1408 CB CYS A 185 -17.091 -3.792 28.100 1.00 21.14 C
ANISOU 1408 CB CYS A 185 2568 3202 2263 -42 -144 51 C
ATOM 1409 SG CYS A 185 -17.434 -3.218 29.762 1.00 25.45 S
ANISOU 1409 SG CYS A 185 3095 3773 2802 -36 -170 40 S
ATOM 1410 N VAL A 186 -14.821 -4.495 25.619 1.00 18.70 N
ANISOU 1410 N VAL A 186 2287 2806 2011 -39 -98 77 N
ATOM 1411 CA VAL A 186 -14.656 -4.999 24.273 1.00 18.50 C
ANISOU 1411 CA VAL A 186 2278 2764 1985 -43 -76 85 C
ATOM 1412 C VAL A 186 -13.275 -5.592 24.073 1.00 19.69 C
ANISOU 1412 C VAL A 186 2434 2876 2169 -45 -64 95 C
ATOM 1413 O VAL A 186 -13.129 -6.750 23.797 1.00 19.63 O
ANISOU 1413 O VAL A 186 2440 2863 2157 -59 -56 101 O
ATOM 1414 CB VAL A 186 -14.899 -3.938 23.205 1.00 19.14 C
ANISOU 1414 CB VAL A 186 2361 2843 2068 -29 -67 84 C
ATOM 1415 CG1 VAL A 186 -14.494 -4.474 21.839 1.00 18.81 C
ANISOU 1415 CG1 VAL A 186 2337 2778 2031 -32 -43 93 C
ATOM 1416 CG2 VAL A 186 -16.342 -3.515 23.219 1.00 19.02 C
ANISOU 1416 CG2 VAL A 186 2344 2866 2018 -29 -77 73 C
ATOM 1417 N LEU A 187 -12.258 -4.771 24.282 1.00 20.34 N
ANISOU 1417 N LEU A 187 2508 2933 2288 -30 -65 97 N
ATOM 1418 CA ALEU A 187 -10.869 -5.222 24.146 0.58 21.91 C
ANISOU 1418 CA ALEU A 187 2709 3092 2523 -30 -54 106 C
ATOM 1419 CA BLEU A 187 -10.871 -5.216 24.146 0.42 22.45 C
ANISOU 1419 CA BLEU A 187 2778 3160 2591 -30 -54 106 C
ATOM 1420 C LEU A 187 -10.351 -6.513 24.940 1.00 23.71 C
ANISOU 1420 C LEU A 187 2940 3310 2757 -46 -60 109 C
ATOM 1421 O LEU A 187 -9.827 -7.602 24.530 1.00 24.61 O
ANISOU 1421 O LEU A 187 3066 3407 2877 -57 -49 115 O
ATOM 1422 CB ALEU A 187 -9.871 -4.101 24.381 0.58 21.73 C
ANISOU 1422 CB ALEU A 187 2673 3043 2539 -11 -57 108 C
ATOM 1423 CB BLEU A 187 -9.903 -4.063 24.381 0.42 23.33 C
ANISOU 1423 CB BLEU A 187 2876 3246 2741 -11 -57 108 C
ATOM 1424 CG ALEU A 187 -9.285 -3.415 23.164 0.58 21.81 C
ANISOU 1424 CG ALEU A 187 2687 3030 2569 1 -38 115 C
ATOM 1425 CG BLEU A 187 -8.774 -3.888 23.378 0.42 25.59 C
ANISOU 1425 CG BLEU A 187 3167 3496 3061 -3 -36 118 C
ATOM 1426 CD1ALEU A 187 -8.021 -2.654 23.507 0.58 21.76 C
ANISOU 1426 CD1ALEU A 187 2669 2991 2609 16 -40 121 C
ATOM 1427 CD1BLEU A 187 -9.224 -4.187 21.959 0.42 26.27 C
ANISOU 1427 CD1BLEU A 187 3269 3586 3128 -7 -14 122 C
ATOM 1428 CD2ALEU A 187 -9.058 -4.375 22.012 0.58 22.33 C
ANISOU 1428 CD2ALEU A 187 2770 3082 2631 -8 -13 123 C
ATOM 1429 CD2BLEU A 187 -8.141 -2.514 23.469 0.42 26.55 C
ANISOU 1429 CD2BLEU A 187 3275 3601 3213 17 -41 120 C
ATOM 1430 N VAL A 188 -10.651 -6.436 26.223 1.00 23.63 N
ANISOU 1430 N VAL A 188 2920 3316 2741 -49 -81 102 N
ATOM 1431 CA VAL A 188 -10.299 -7.493 27.160 1.00 25.03 C
ANISOU 1431 CA VAL A 188 3100 3489 2922 -65 -92 102 C
ATOM 1432 C VAL A 188 -10.999 -8.807 26.811 1.00 25.85 C
ANISOU 1432 C VAL A 188 3219 3611 2994 -86 -88 104 C
ATOM 1433 O VAL A 188 -10.349 -9.777 26.674 1.00 27.01 O
ANISOU 1433 O VAL A 188 3374 3738 3152 -96 -84 109 O
ATOM 1434 CB VAL A 188 -10.436 -7.086 28.642 1.00 25.36 C
ANISOU 1434 CB VAL A 188 3129 3543 2964 -63 -117 95 C
ATOM 1435 CG1 VAL A 188 -10.362 -8.295 29.545 1.00 25.68 C
ANISOU 1435 CG1 VAL A 188 3174 3585 2997 -83 -129 95 C
ATOM 1436 CG2 VAL A 188 -9.371 -6.084 29.024 1.00 24.87 C
ANISOU 1436 CG2 VAL A 188 3055 3450 2943 -44 -121 96 C
ATOM 1437 N PRO A 189 -12.326 -8.795 26.613 1.00 25.32 N
ANISOU 1437 N PRO A 189 3153 3581 2887 -91 -91 100 N
ATOM 1438 CA PRO A 189 -12.989 -10.024 26.209 1.00 24.98 C
ANISOU 1438 CA PRO A 189 3124 3554 2815 -110 -88 103 C
ATOM 1439 C PRO A 189 -12.459 -10.531 24.874 1.00 24.16 C
ANISOU 1439 C PRO A 189 3034 3424 2720 -109 -66 112 C
ATOM 1440 O PRO A 189 -12.313 -11.688 24.743 1.00 24.15 O
ANISOU 1440 O PRO A 189 3045 3418 2714 -123 -65 116 O
ATOM 1441 CB PRO A 189 -14.450 -9.622 26.100 1.00 25.75 C
ANISOU 1441 CB PRO A 189 3219 3692 2874 -110 -92 97 C
ATOM 1442 CG PRO A 189 -14.591 -8.494 27.019 1.00 26.55 C
ANISOU 1442 CG PRO A 189 3303 3804 2980 -98 -106 89 C
ATOM 1443 CD PRO A 189 -13.303 -7.748 26.948 1.00 24.60 C
ANISOU 1443 CD PRO A 189 3051 3521 2776 -81 -101 92 C
ATOM 1444 N LEU A 190 -12.191 -9.672 23.914 1.00 23.03 N
ANISOU 1444 N LEU A 190 2892 3267 2590 -93 -50 114 N
ATOM 1445 CA LEU A 190 -11.647 -10.123 22.657 1.00 23.57 C
ANISOU 1445 CA LEU A 190 2975 3312 2669 -92 -29 122 C
ATOM 1446 C LEU A 190 -10.263 -10.814 22.841 1.00 25.51 C
ANISOU 1446 C LEU A 190 3223 3521 2949 -95 -25 127 C
ATOM 1447 O LEU A 190 -10.003 -11.798 22.252 1.00 25.71 O
ANISOU 1447 O LEU A 190 3261 3535 2972 -103 -16 132 O
ATOM 1448 CB LEU A 190 -11.593 -9.003 21.640 1.00 23.28 C
ANISOU 1448 CB LEU A 190 2938 3266 2640 -74 -13 123 C
ATOM 1449 CG LEU A 190 -12.893 -8.488 21.032 1.00 24.03 C
ANISOU 1449 CG LEU A 190 3039 3391 2703 -71 -12 119 C
ATOM 1450 CD1 LEU A 190 -12.697 -7.241 20.203 1.00 25.24 C
ANISOU 1450 CD1 LEU A 190 3189 3532 2869 -53 0 119 C
ATOM 1451 CD2 LEU A 190 -13.678 -9.524 20.284 1.00 24.20 C
ANISOU 1451 CD2 LEU A 190 3077 3424 2692 -84 -6 122 C
ATOM 1452 N LEU A 191 -9.411 -10.262 23.677 1.00 26.40 N
ANISOU 1452 N LEU A 191 3321 3616 3092 -87 -33 125 N
ATOM 1453 CA LEU A 191 -8.113 -10.823 23.974 1.00 29.47 C
ANISOU 1453 CA LEU A 191 3710 3970 3516 -90 -31 128 C
ATOM 1454 C LEU A 191 -8.259 -12.191 24.647 1.00 30.34 C
ANISOU 1454 C LEU A 191 3828 4088 3613 -111 -46 127 C
ATOM 1455 O LEU A 191 -7.542 -13.086 24.361 1.00 31.65 O
ANISOU 1455 O LEU A 191 4002 4232 3793 -118 -40 130 O
ATOM 1456 CB LEU A 191 -7.308 -9.868 24.834 1.00 31.46 C
ANISOU 1456 CB LEU A 191 3946 4204 3804 -77 -41 126 C
ATOM 1457 CG LEU A 191 -6.885 -8.575 24.171 1.00 34.95 C
ANISOU 1457 CG LEU A 191 4380 4631 4268 -56 -27 129 C
ATOM 1458 CD1 LEU A 191 -6.154 -7.592 25.044 1.00 36.50 C
ANISOU 1458 CD1 LEU A 191 4561 4811 4498 -43 -40 128 C
ATOM 1459 CD2 LEU A 191 -6.201 -8.774 22.846 1.00 36.86 C
ANISOU 1459 CD2 LEU A 191 4632 4848 4525 -52 -1 137 C
ATOM 1460 N LEU A 192 -9.232 -12.318 25.523 1.00 29.70 N
ANISOU 1460 N LEU A 192 3742 4038 3502 -121 -64 122 N
ATOM 1461 CA LEU A 192 -9.531 -13.546 26.192 1.00 31.45 C
ANISOU 1461 CA LEU A 192 3971 4272 3706 -143 -80 121 C
ATOM 1462 C LEU A 192 -9.932 -14.572 25.167 1.00 31.00 C
ANISOU 1462 C LEU A 192 3931 4220 3627 -153 -70 126 C
ATOM 1463 O LEU A 192 -9.484 -15.655 25.203 1.00 31.34 O
ANISOU 1463 O LEU A 192 3983 4250 3674 -166 -74 128 O
ATOM 1464 CB LEU A 192 -10.655 -13.353 27.187 1.00 32.30 C
ANISOU 1464 CB LEU A 192 4071 4418 3783 -151 -99 114 C
ATOM 1465 CG LEU A 192 -10.315 -12.611 28.467 1.00 35.53 C
ANISOU 1465 CG LEU A 192 4465 4824 4209 -144 -116 108 C
ATOM 1466 CD1 LEU A 192 -11.514 -12.541 29.366 1.00 36.44 C
ANISOU 1466 CD1 LEU A 192 4576 4981 4290 -153 -133 102 C
ATOM 1467 CD2 LEU A 192 -9.164 -13.258 29.179 1.00 37.24 C
ANISOU 1467 CD2 LEU A 192 4683 5009 4457 -152 -125 109 C
ATOM 1468 N MET A 193 -10.783 -14.175 24.245 1.00 30.59 N
ANISOU 1468 N MET A 193 3884 4187 3552 -147 -58 128 N
ATOM 1469 CA MET A 193 -11.234 -15.009 23.160 1.00 31.74 C
ANISOU 1469 CA MET A 193 4047 4338 3676 -153 -48 133 C
ATOM 1470 C MET A 193 -10.036 -15.496 22.361 1.00 33.45 C
ANISOU 1470 C MET A 193 4272 4516 3921 -149 -31 139 C
ATOM 1471 O MET A 193 -9.981 -16.618 22.003 1.00 34.00 O
ANISOU 1471 O MET A 193 4355 4581 3982 -160 -32 143 O
ATOM 1472 CB MET A 193 -12.143 -14.247 22.225 1.00 31.30 C
ANISOU 1472 CB MET A 193 3995 4300 3599 -143 -35 134 C
ATOM 1473 CG MET A 193 -13.594 -14.225 22.595 1.00 33.00 C
ANISOU 1473 CG MET A 193 4208 4556 3775 -151 -49 130 C
ATOM 1474 SD MET A 193 -14.457 -13.325 21.339 1.00 36.31 S
ANISOU 1474 SD MET A 193 4634 4987 4177 -137 -33 130 S
ATOM 1475 CE MET A 193 -15.468 -12.278 22.344 1.00 32.96 C
ANISOU 1475 CE MET A 193 4191 4598 3736 -134 -49 120 C
ATOM 1476 N LEU A 194 -9.088 -14.620 22.089 1.00 33.89 N
ANISOU 1476 N LEU A 194 4320 4545 4010 -133 -17 139 N
ATOM 1477 CA LEU A 194 -7.878 -14.999 21.375 1.00 36.22 C
ANISOU 1477 CA LEU A 194 4622 4804 4336 -127 -1 144 C
ATOM 1478 C LEU A 194 -7.138 -16.094 22.146 1.00 36.89 C
ANISOU 1478 C LEU A 194 4708 4873 4437 -142 -15 142 C
ATOM 1479 O LEU A 194 -6.722 -17.047 21.587 1.00 37.69 O
ANISOU 1479 O LEU A 194 4821 4959 4541 -147 -9 146 O
ATOM 1480 CB LEU A 194 -6.985 -13.800 21.148 1.00 37.55 C
ANISOU 1480 CB LEU A 194 4779 4947 4540 -108 14 145 C
ATOM 1481 CG LEU A 194 -5.651 -14.002 20.468 1.00 41.89 C
ANISOU 1481 CG LEU A 194 5331 5458 5126 -101 33 149 C
ATOM 1482 CD1 LEU A 194 -5.824 -14.514 19.071 1.00 42.94 C
ANISOU 1482 CD1 LEU A 194 5482 5589 5244 -99 53 155 C
ATOM 1483 CD2 LEU A 194 -4.828 -12.746 20.454 1.00 43.28 C
ANISOU 1483 CD2 LEU A 194 5493 5613 5338 -83 43 151 C
ATOM 1484 N GLY A 195 -7.016 -15.924 23.447 1.00 36.31 N
ANISOU 1484 N GLY A 195 4623 4802 4373 -147 -35 137 N
ATOM 1485 CA GLY A 195 -6.386 -16.878 24.314 1.00 37.06 C
ANISOU 1485 CA GLY A 195 4718 4882 4481 -162 -52 135 C
ATOM 1486 C GLY A 195 -7.050 -18.239 24.277 1.00 37.20 C
ANISOU 1486 C GLY A 195 4750 4918 4467 -183 -64 136 C
ATOM 1487 O GLY A 195 -6.387 -19.237 24.226 1.00 38.70 O
ANISOU 1487 O GLY A 195 4948 5088 4669 -192 -68 136 O
ATOM 1488 N VAL A 196 -8.363 -18.261 24.304 1.00 35.06 N
ANISOU 1488 N VAL A 196 4482 4684 4155 -189 -71 136 N
ATOM 1489 CA VAL A 196 -9.109 -19.484 24.233 1.00 34.60 C
ANISOU 1489 CA VAL A 196 4437 4646 4065 -208 -84 139 C
ATOM 1490 C VAL A 196 -8.893 -20.182 22.891 1.00 35.01 C
ANISOU 1490 C VAL A 196 4504 4683 4113 -205 -68 145 C
ATOM 1491 O VAL A 196 -8.692 -21.358 22.848 1.00 35.31 O
ANISOU 1491 O VAL A 196 4553 4715 4147 -219 -77 147 O
ATOM 1492 CB VAL A 196 -10.590 -19.269 24.546 1.00 33.55 C
ANISOU 1492 CB VAL A 196 4302 4556 3890 -215 -94 138 C
ATOM 1493 CG1 VAL A 196 -11.388 -20.518 24.305 1.00 34.27 C
ANISOU 1493 CG1 VAL A 196 4407 4667 3948 -233 -105 143 C
ATOM 1494 CG2 VAL A 196 -10.766 -18.841 25.977 1.00 33.53 C
ANISOU 1494 CG2 VAL A 196 4285 4567 3888 -221 -113 132 C
ATOM 1495 N TYR A 197 -8.917 -19.430 21.808 1.00 34.46 N
ANISOU 1495 N TYR A 197 4438 4609 4047 -188 -44 148 N
ATOM 1496 CA TYR A 197 -8.708 -20.010 20.511 1.00 35.91 C
ANISOU 1496 CA TYR A 197 4638 4779 4228 -183 -27 154 C
ATOM 1497 C TYR A 197 -7.322 -20.620 20.423 1.00 39.76 C
ANISOU 1497 C TYR A 197 5127 5230 4751 -183 -23 153 C
ATOM 1498 O TYR A 197 -7.182 -21.691 19.942 1.00 41.10 O
ANISOU 1498 O TYR A 197 5311 5393 4914 -190 -25 156 O
ATOM 1499 CB TYR A 197 -9.035 -19.044 19.373 1.00 34.35 C
ANISOU 1499 CB TYR A 197 4443 4583 4025 -165 -3 157 C
ATOM 1500 CG TYR A 197 -10.516 -19.014 19.128 1.00 33.37 C
ANISOU 1500 CG TYR A 197 4326 4494 3859 -170 -9 159 C
ATOM 1501 CD1 TYR A 197 -11.186 -20.159 18.774 1.00 33.25 C
ANISOU 1501 CD1 TYR A 197 4326 4492 3815 -182 -18 164 C
ATOM 1502 CD2 TYR A 197 -11.254 -17.868 19.331 1.00 32.76 C
ANISOU 1502 CD2 TYR A 197 4239 4438 3772 -162 -8 156 C
ATOM 1503 CE1 TYR A 197 -12.530 -20.170 18.595 1.00 33.04 C
ANISOU 1503 CE1 TYR A 197 4306 4497 3752 -187 -24 166 C
ATOM 1504 CE2 TYR A 197 -12.611 -17.865 19.164 1.00 32.87 C
ANISOU 1504 CE2 TYR A 197 4257 4483 3749 -167 -14 156 C
ATOM 1505 CZ TYR A 197 -13.245 -19.024 18.800 1.00 34.13 C
ANISOU 1505 CZ TYR A 197 4433 4654 3881 -180 -22 162 C
ATOM 1506 OH TYR A 197 -14.573 -19.039 18.630 1.00 36.26 O
ANISOU 1506 OH TYR A 197 4708 4954 4116 -185 -29 163 O
ATOM 1507 N LEU A 198 -6.319 -19.935 20.934 1.00 41.23 N
ANISOU 1507 N LEU A 198 5299 5393 4974 -174 -19 150 N
ATOM 1508 CA LEU A 198 -4.977 -20.443 20.945 1.00 44.28 C
ANISOU 1508 CA LEU A 198 5685 5743 5397 -174 -16 148 C
ATOM 1509 C LEU A 198 -4.910 -21.763 21.681 1.00 46.03 C
ANISOU 1509 C LEU A 198 5912 5964 5612 -195 -41 145 C
ATOM 1510 O LEU A 198 -4.298 -22.661 21.222 1.00 47.43 O
ANISOU 1510 O LEU A 198 6100 6124 5799 -199 -40 145 O
ATOM 1511 CB LEU A 198 -4.016 -19.442 21.561 1.00 45.53 C
ANISOU 1511 CB LEU A 198 5825 5877 5596 -163 -12 144 C
ATOM 1512 CG LEU A 198 -3.658 -18.236 20.738 1.00 48.69 C
ANISOU 1512 CG LEU A 198 6220 6266 6015 -141 15 148 C
ATOM 1513 CD1 LEU A 198 -2.647 -17.372 21.445 1.00 50.44 C
ANISOU 1513 CD1 LEU A 198 6424 6462 6279 -131 15 146 C
ATOM 1514 CD2 LEU A 198 -3.217 -18.592 19.336 1.00 50.84 C
ANISOU 1514 CD2 LEU A 198 6505 6522 6291 -133 40 153 C
ATOM 1515 N ARG A 199 -5.570 -21.871 22.813 1.00 46.31 N
ANISOU 1515 N ARG A 199 5943 6022 5630 -210 -66 141 N
ATOM 1516 CA ARG A 199 -5.583 -23.094 23.568 1.00 48.13 C
ANISOU 1516 CA ARG A 199 6180 6255 5853 -232 -92 139 C
ATOM 1517 C ARG A 199 -6.342 -24.199 22.867 1.00 48.39 C
ANISOU 1517 C ARG A 199 6230 6306 5850 -243 -98 144 C
ATOM 1518 O ARG A 199 -6.002 -25.342 22.998 1.00 50.72 O
ANISOU 1518 O ARG A 199 6534 6591 6146 -256 -114 143 O
ATOM 1519 CB ARG A 199 -6.157 -22.856 24.937 1.00 50.41 C
ANISOU 1519 CB ARG A 199 6458 6565 6129 -244 -116 134 C
ATOM 1520 CG ARG A 199 -5.186 -22.140 25.824 1.00 56.84 C
ANISOU 1520 CG ARG A 199 7259 7355 6983 -237 -118 128 C
ATOM 1521 CD ARG A 199 -5.874 -21.398 26.925 1.00 62.50 C
ANISOU 1521 CD ARG A 199 7964 8095 7687 -240 -132 125 C
ATOM 1522 NE ARG A 199 -6.582 -22.265 27.834 1.00 69.52 N
ANISOU 1522 NE ARG A 199 8858 9007 8547 -264 -159 124 N
ATOM 1523 CZ ARG A 199 -6.054 -22.754 28.953 1.00 75.81 C
ANISOU 1523 CZ ARG A 199 9653 9791 9359 -278 -182 118 C
ATOM 1524 NH1 ARG A 199 -4.806 -22.454 29.262 1.00 77.48 N
ANISOU 1524 NH1 ARG A 199 9859 9964 9615 -270 -180 114 N
ATOM 1525 NH2 ARG A 199 -6.760 -23.537 29.757 1.00 76.20 N
ANISOU 1525 NH2 ARG A 199 9707 9864 9380 -301 -206 117 N
ATOM 1526 N ILE A 200 -7.363 -23.844 22.119 1.00 46.51 N
ANISOU 1526 N ILE A 200 5997 6093 5582 -236 -87 150 N
ATOM 1527 CA ILE A 200 -8.141 -24.800 21.386 1.00 45.80 C
ANISOU 1527 CA ILE A 200 5924 6018 5458 -244 -91 156 C
ATOM 1528 C ILE A 200 -7.306 -25.408 20.275 1.00 46.79 C
ANISOU 1528 C ILE A 200 6062 6116 5599 -236 -77 158 C
ATOM 1529 O ILE A 200 -7.271 -26.587 20.111 1.00 48.11 O
ANISOU 1529 O ILE A 200 6242 6281 5757 -247 -91 160 O
ATOM 1530 CB ILE A 200 -9.390 -24.183 20.772 1.00 43.89 C
ANISOU 1530 CB ILE A 200 5686 5806 5184 -237 -81 161 C
ATOM 1531 CG1 ILE A 200 -10.482 -23.990 21.813 1.00 43.07 C
ANISOU 1531 CG1 ILE A 200 5573 5737 5053 -250 -101 160 C
ATOM 1532 CG2 ILE A 200 -9.910 -25.055 19.662 1.00 44.19 C
ANISOU 1532 CG2 ILE A 200 5743 5849 5197 -238 -79 169 C
ATOM 1533 CD1 ILE A 200 -11.719 -23.325 21.285 1.00 42.77 C
ANISOU 1533 CD1 ILE A 200 5537 5729 4986 -243 -92 163 C
ATOM 1534 N PHE A 201 -6.622 -24.585 19.527 1.00 46.54 N
ANISOU 1534 N PHE A 201 6027 6063 5592 -215 -49 158 N
ATOM 1535 CA PHE A 201 -5.818 -25.075 18.451 1.00 48.32 C
ANISOU 1535 CA PHE A 201 6264 6262 5833 -206 -32 160 C
ATOM 1536 C PHE A 201 -4.605 -25.866 18.947 1.00 50.49 C
ANISOU 1536 C PHE A 201 6536 6508 6139 -213 -44 154 C
ATOM 1537 O PHE A 201 -4.200 -26.781 18.321 1.00 51.81 O
ANISOU 1537 O PHE A 201 6716 6662 6308 -214 -43 155 O
ATOM 1538 CB PHE A 201 -5.461 -23.956 17.486 1.00 48.23 C
ANISOU 1538 CB PHE A 201 6250 6238 5837 -183 1 163 C
ATOM 1539 CG PHE A 201 -6.644 -23.371 16.759 1.00 48.28 C
ANISOU 1539 CG PHE A 201 6264 6270 5811 -176 12 169 C
ATOM 1540 CD1 PHE A 201 -7.493 -24.162 16.034 1.00 49.22 C
ANISOU 1540 CD1 PHE A 201 6402 6404 5896 -180 8 175 C
ATOM 1541 CD2 PHE A 201 -6.897 -22.038 16.800 1.00 48.42 C
ANISOU 1541 CD2 PHE A 201 6269 6294 5832 -164 25 168 C
ATOM 1542 CE1 PHE A 201 -8.560 -23.636 15.369 1.00 49.14 C
ANISOU 1542 CE1 PHE A 201 6399 6415 5858 -174 17 179 C
ATOM 1543 CE2 PHE A 201 -7.967 -21.496 16.135 1.00 48.29 C
ANISOU 1543 CE2 PHE A 201 6261 6300 5788 -158 34 172 C
ATOM 1544 CZ PHE A 201 -8.803 -22.294 15.420 1.00 48.18 C
ANISOU 1544 CZ PHE A 201 6265 6299 5741 -163 30 178 C
ATOM 1545 N ALA A 202 -4.086 -25.523 20.105 1.00 51.71 N
ANISOU 1545 N ALA A 202 6676 6654 6318 -219 -56 148 N
ATOM 1546 CA ALA A 202 -2.967 -26.225 20.688 1.00 55.08 C
ANISOU 1546 CA ALA A 202 7100 7053 6776 -227 -69 140 C
ATOM 1547 C ALA A 202 -3.379 -27.594 21.204 1.00 57.03 C
ANISOU 1547 C ALA A 202 7357 7311 7000 -251 -101 139 C
ATOM 1548 O ALA A 202 -2.663 -28.532 21.059 1.00 58.69 O
ANISOU 1548 O ALA A 202 7575 7501 7224 -256 -110 135 O
ATOM 1549 CB ALA A 202 -2.338 -25.415 21.794 1.00 55.04 C
ANISOU 1549 CB ALA A 202 7077 7033 6803 -226 -74 134 C
ATOM 1550 N ALA A 203 -4.543 -27.682 21.814 1.00 57.19 N
ANISOU 1550 N ALA A 203 7379 7365 6986 -265 -120 142 N
ATOM 1551 CA ALA A 203 -5.069 -28.910 22.321 1.00 58.67 C
ANISOU 1551 CA ALA A 203 7576 7567 7148 -288 -152 142 C
ATOM 1552 C ALA A 203 -5.361 -29.866 21.185 1.00 60.95 C
ANISOU 1552 C ALA A 203 7884 7859 7415 -287 -150 148 C
ATOM 1553 O ALA A 203 -5.116 -31.031 21.304 1.00 62.19 O
ANISOU 1553 O ALA A 203 8050 8009 7570 -301 -172 146 O
ATOM 1554 CB ALA A 203 -6.311 -28.652 23.122 1.00 57.66 C
ANISOU 1554 CB ALA A 203 7444 7477 6987 -300 -167 145 C
ATOM 1555 N ALA A 204 -5.880 -29.351 20.088 1.00 61.44 N
ANISOU 1555 N ALA A 204 7951 7930 7462 -270 -126 155 N
ATOM 1556 CA ALA A 204 -6.214 -30.142 18.946 1.00 63.44 C
ANISOU 1556 CA ALA A 204 8223 8186 7693 -267 -123 162 C
ATOM 1557 C ALA A 204 -4.962 -30.686 18.318 1.00 66.64 C
ANISOU 1557 C ALA A 204 8635 8557 8129 -258 -114 157 C
ATOM 1558 O ALA A 204 -4.891 -31.828 17.971 1.00 67.97 O
ANISOU 1558 O ALA A 204 8817 8722 8288 -265 -129 158 O
ATOM 1559 CB ALA A 204 -6.976 -29.323 17.936 1.00 62.27 C
ANISOU 1559 CB ALA A 204 8080 8053 7527 -250 -97 169 C
ATOM 1560 N ARG A 205 -3.970 -29.843 18.183 1.00 68.12 N
ANISOU 1560 N ARG A 205 8810 8719 8353 -243 -89 153 N
ATOM 1561 CA AARG A 205 -2.663 -30.231 17.614 0.50 71.59 C
ANISOU 1561 CA AARG A 205 9251 9123 8825 -233 -77 148 C
ATOM 1562 CA BARG A 205 -2.673 -30.242 17.606 0.50 71.58 C
ANISOU 1562 CA BARG A 205 9250 9122 8823 -233 -77 148 C
ATOM 1563 C ARG A 205 -1.709 -31.308 18.318 1.00 73.54 C
ANISOU 1563 C ARG A 205 9499 9348 9097 -248 -103 138 C
ATOM 1564 O ARG A 205 -0.948 -32.241 17.861 1.00 75.70 O
ANISOU 1564 O ARG A 205 9780 9600 9383 -247 -108 133 O
ATOM 1565 CB AARG A 205 -1.850 -28.954 17.338 0.50 74.26 C
ANISOU 1565 CB AARG A 205 9575 9441 9198 -213 -44 146 C
ATOM 1566 CB BARG A 205 -1.873 -28.975 17.261 0.50 74.27 C
ANISOU 1566 CB BARG A 205 9578 9443 9199 -212 -43 146 C
ATOM 1567 CG AARG A 205 -0.561 -29.154 16.565 0.50 80.41 C
ANISOU 1567 CG AARG A 205 10355 10185 10011 -199 -24 142 C
ATOM 1568 CG BARG A 205 -0.509 -29.220 16.647 0.50 80.46 C
ANISOU 1568 CG BARG A 205 10362 10191 10020 -201 -26 141 C
ATOM 1569 CD AARG A 205 0.655 -28.701 17.363 0.50 85.52 C
ANISOU 1569 CD AARG A 205 10985 10804 10707 -198 -22 133 C
ATOM 1570 CD BARG A 205 -0.405 -28.629 15.249 0.50 85.02 C
ANISOU 1570 CD BARG A 205 10945 10762 10596 -178 11 148 C
ATOM 1571 NE AARG A 205 0.806 -27.249 17.399 0.50 88.22 N
ANISOU 1571 NE AARG A 205 11312 11143 11066 -184 2 136 N
ATOM 1572 NE BARG A 205 -1.310 -27.502 15.052 0.50 86.80 N
ANISOU 1572 NE BARG A 205 11168 11010 10802 -170 26 155 N
ATOM 1573 CZ AARG A 205 0.689 -26.521 18.501 0.50 90.08 C
ANISOU 1573 CZ AARG A 205 11532 11383 11311 -189 -9 134 C
ATOM 1574 CZ BARG A 205 -1.818 -27.138 13.880 0.50 89.23 C
ANISOU 1574 CZ BARG A 205 11487 11326 11090 -156 49 163 C
ATOM 1575 NH1AARG A 205 0.827 -25.211 18.453 0.50 89.52 N
ANISOU 1575 NH1AARG A 205 11449 11309 11257 -175 11 137 N
ATOM 1576 NH1BARG A 205 -2.631 -26.090 13.810 0.50 87.80 N
ANISOU 1576 NH1BARG A 205 11302 11164 10893 -151 59 167 N
ATOM 1577 NH2AARG A 205 0.421 -27.106 19.652 0.50 90.15 N
ANISOU 1577 NH2AARG A 205 11539 11399 11312 -209 -42 129 N
ATOM 1578 NH2BARG A 205 -1.514 -27.818 12.780 0.50 90.82 N
ANISOU 1578 NH2BARG A 205 11704 11515 11287 -148 61 165 N
ATOM 1579 N ARG A 206 -2.031 -31.251 19.593 1.00 72.99 N
ANISOU 1579 N ARG A 206 9419 9289 9023 -265 -128 134 N
ATOM 1580 CA ARG A 206 -1.424 -32.085 20.600 1.00 74.49 C
ANISOU 1580 CA ARG A 206 9608 9465 9231 -284 -158 125 C
ATOM 1581 C ARG A 206 -2.098 -33.437 20.658 1.00 74.89 C
ANISOU 1581 C ARG A 206 9674 9532 9247 -304 -191 128 C
ATOM 1582 O ARG A 206 -1.472 -34.437 20.877 1.00 76.40 O
ANISOU 1582 O ARG A 206 9871 9706 9451 -315 -212 121 O
ATOM 1583 CB ARG A 206 -1.590 -31.437 21.943 1.00 75.92 C
ANISOU 1583 CB ARG A 206 9775 9653 9419 -295 -172 122 C
ATOM 1584 CG ARG A 206 -0.987 -32.174 23.108 1.00 82.23 C
ANISOU 1584 CG ARG A 206 10571 10436 10236 -316 -204 112 C
ATOM 1585 CD ARG A 206 -1.123 -31.436 24.429 1.00 87.37 C
ANISOU 1585 CD ARG A 206 11209 11093 10895 -324 -215 109 C
ATOM 1586 NE ARG A 206 -0.529 -32.110 25.579 1.00 93.44 N
ANISOU 1586 NE ARG A 206 11977 11843 11682 -344 -247 99 N
ATOM 1587 CZ ARG A 206 -0.360 -31.577 26.786 1.00 95.44 C
ANISOU 1587 CZ ARG A 206 12220 12092 11951 -351 -259 94 C
ATOM 1588 NH1 ARG A 206 -0.735 -30.330 27.034 1.00 93.50 N
ANISOU 1588 NH1 ARG A 206 11962 11858 11704 -339 -242 97 N
ATOM 1589 NH2 ARG A 206 0.184 -32.300 27.749 1.00 96.06 N
ANISOU 1589 NH2 ARG A 206 12301 12153 12046 -371 -289 85 N
ATOM 1590 N GLN A 207 -3.395 -33.450 20.485 1.00 73.39 N
ANISOU 1590 N GLN A 207 9491 9377 9016 -308 -195 137 N
ATOM 1591 CA GLN A 207 -4.124 -34.664 20.525 1.00 73.20 C
ANISOU 1591 CA GLN A 207 9482 9371 8959 -326 -226 142 C
ATOM 1592 C GLN A 207 -3.892 -35.413 19.257 1.00 74.45 C
ANISOU 1592 C GLN A 207 9656 9518 9112 -315 -219 145 C
ATOM 1593 O GLN A 207 -3.704 -36.592 19.287 1.00 75.49 O
ANISOU 1593 O GLN A 207 9799 9645 9239 -327 -245 143 O
ATOM 1594 CB GLN A 207 -5.585 -34.385 20.714 1.00 72.18 C
ANISOU 1594 CB GLN A 207 9354 9282 8789 -334 -232 152 C
ATOM 1595 CG GLN A 207 -5.911 -34.038 22.124 1.00 73.10 C
ANISOU 1595 CG GLN A 207 9457 9413 8903 -351 -250 149 C
ATOM 1596 CD GLN A 207 -7.342 -33.684 22.317 1.00 74.86 C
ANISOU 1596 CD GLN A 207 9680 9675 9087 -357 -253 158 C
ATOM 1597 OE1 GLN A 207 -8.206 -34.177 21.639 1.00 75.94 O
ANISOU 1597 OE1 GLN A 207 9829 9831 9192 -358 -257 167 O
ATOM 1598 NE2 GLN A 207 -7.593 -32.815 23.252 1.00 73.81 N
ANISOU 1598 NE2 GLN A 207 9532 9554 8957 -361 -252 155 N
ATOM 1599 N LEU A 208 -3.910 -34.704 18.133 1.00 74.56 N
ANISOU 1599 N LEU A 208 9673 9530 9127 -292 -184 150 N
ATOM 1600 CA LEU A 208 -3.697 -35.326 16.831 1.00 76.58 C
ANISOU 1600 CA LEU A 208 9945 9774 9376 -278 -174 153 C
ATOM 1601 C LEU A 208 -2.264 -35.829 16.688 1.00 78.67 C
ANISOU 1601 C LEU A 208 10208 10003 9679 -273 -172 142 C
ATOM 1602 O LEU A 208 -2.036 -36.983 16.326 1.00 80.40 O
ANISOU 1602 O LEU A 208 10441 10215 9893 -277 -191 140 O
ATOM 1603 CB LEU A 208 -4.023 -34.341 15.707 1.00 76.85 C
ANISOU 1603 CB LEU A 208 9983 9813 9405 -254 -135 161 C
ATOM 1604 CG LEU A 208 -3.735 -34.818 14.282 1.00 80.96 C
ANISOU 1604 CG LEU A 208 10521 10320 9921 -236 -118 164 C
ATOM 1605 CD1 LEU A 208 -4.430 -36.142 14.007 1.00 82.66 C
ANISOU 1605 CD1 LEU A 208 10756 10549 10103 -247 -149 170 C
ATOM 1606 CD2 LEU A 208 -4.156 -33.765 13.267 1.00 81.26 C
ANISOU 1606 CD2 LEU A 208 10561 10363 9949 -215 -81 172 C
ATOM 1607 N ALA A1001 -1.093 -35.290 17.238 1.00 59.76 N
ANISOU 1607 N ALA A1001 4720 5302 12685 1071 836 -1631 N
ATOM 1608 CA ALA A1001 0.272 -35.784 17.389 1.00 64.67 C
ANISOU 1608 CA ALA A1001 5323 5813 13435 1170 909 -1664 C
ATOM 1609 C ALA A1001 0.312 -37.028 18.270 1.00 59.91 C
ANISOU 1609 C ALA A1001 4813 5373 12578 1163 785 -1674 C
ATOM 1610 O ALA A1001 0.962 -38.025 18.006 1.00 57.78 O
ANISOU 1610 O ALA A1001 4723 5020 12209 1184 841 -1594 O
ATOM 1611 CB ALA A1001 1.169 -34.697 17.960 1.00 77.42 C
ANISOU 1611 CB ALA A1001 6593 7381 15442 1276 922 -1850 C
ATOM 1612 N ASP A1002 -0.455 -36.981 19.369 1.00 91.18 N
ANISOU 1612 N ASP A1002 8650 9581 16414 1137 610 -1768 N
ATOM 1613 CA ASP A1002 -0.512 -38.085 20.282 1.00 89.53 C
ANISOU 1613 CA ASP A1002 8506 9546 15967 1139 492 -1775 C
ATOM 1614 C ASP A1002 -1.137 -39.311 19.611 1.00 79.90 C
ANISOU 1614 C ASP A1002 7624 8311 14423 1036 495 -1566 C
ATOM 1615 O ASP A1002 -0.735 -40.413 19.856 1.00 77.13 O
ANISOU 1615 O ASP A1002 7404 7980 13920 1047 474 -1523 O
ATOM 1616 CB ASP A1002 -1.293 -37.712 21.526 1.00 95.61 C
ANISOU 1616 CB ASP A1002 9079 10583 16667 1150 319 -1897 C
ATOM 1617 CG ASP A1002 -0.448 -37.043 22.577 1.00114.85 C
ANISOU 1617 CG ASP A1002 11216 13074 19346 1289 259 -2126 C
ATOM 1618 OD1 ASP A1002 0.553 -36.410 22.230 1.00123.32 O
ANISOU 1618 OD1 ASP A1002 12170 13962 20726 1358 353 -2203 O
ATOM 1619 OD2 ASP A1002 -0.790 -37.119 23.766 1.00122.49 O
ANISOU 1619 OD2 ASP A1002 12062 14268 20211 1342 112 -2229 O
ATOM 1620 N LEU A1003 -2.145 -39.117 18.790 1.00 75.42 N
ANISOU 1620 N LEU A1003 7193 7708 13754 939 506 -1442 N
ATOM 1621 CA LEU A1003 -2.732 -40.239 18.115 1.00 68.92 C
ANISOU 1621 CA LEU A1003 6688 6847 12651 851 490 -1252 C
ATOM 1622 C LEU A1003 -1.704 -40.866 17.211 1.00 68.93 C
ANISOU 1622 C LEU A1003 6894 6623 12675 901 627 -1169 C
ATOM 1623 O LEU A1003 -1.568 -42.057 17.181 1.00 65.31 O
ANISOU 1623 O LEU A1003 6635 6163 12018 886 595 -1080 O
ATOM 1624 CB LEU A1003 -3.898 -39.822 17.236 1.00 66.62 C
ANISOU 1624 CB LEU A1003 6515 6511 12286 753 488 -1141 C
ATOM 1625 CG LEU A1003 -5.332 -39.779 17.730 1.00 66.92 C
ANISOU 1625 CG LEU A1003 6523 6749 12156 652 337 -1107 C
ATOM 1626 CD1 LEU A1003 -6.124 -39.115 16.632 1.00 66.99 C
ANISOU 1626 CD1 LEU A1003 6632 6639 12184 584 385 -1023 C
ATOM 1627 CD2 LEU A1003 -5.879 -41.157 17.987 1.00 63.93 C
ANISOU 1627 CD2 LEU A1003 6339 6460 11492 584 222 -977 C
ATOM 1628 N GLU A1004 -0.975 -40.062 16.458 1.00 74.17 N
ANISOU 1628 N GLU A1004 7505 7091 13584 969 786 -1188 N
ATOM 1629 CA GLU A1004 0.019 -40.608 15.550 1.00 77.02 C
ANISOU 1629 CA GLU A1004 8061 7231 13972 1037 936 -1094 C
ATOM 1630 C GLU A1004 1.162 -41.248 16.320 1.00 79.85 C
ANISOU 1630 C GLU A1004 8349 7614 14376 1114 934 -1174 C
ATOM 1631 O GLU A1004 1.719 -42.220 15.881 1.00 79.20 O
ANISOU 1631 O GLU A1004 8484 7433 14176 1139 986 -1078 O
ATOM 1632 CB GLU A1004 0.569 -39.560 14.586 1.00 87.13 C
ANISOU 1632 CB GLU A1004 9282 8295 15528 1109 1125 -1081 C
ATOM 1633 CG GLU A1004 0.079 -39.612 13.133 1.00 92.17 C
ANISOU 1633 CG GLU A1004 10204 8760 16058 1093 1225 -904 C
ATOM 1634 CD GLU A1004 0.177 -40.969 12.455 1.00 96.23 C
ANISOU 1634 CD GLU A1004 11080 9184 16301 1098 1230 -747 C
ATOM 1635 OE1 GLU A1004 1.284 -41.490 12.271 1.00101.33 O
ANISOU 1635 OE1 GLU A1004 11795 9716 16991 1190 1331 -720 O
ATOM 1636 OE2 GLU A1004 -0.868 -41.512 12.092 1.00 93.51 O
ANISOU 1636 OE2 GLU A1004 10953 8876 15703 1014 1125 -649 O
ATOM 1637 N ASP A1005 1.513 -40.709 17.468 1.00 83.90 N
ANISOU 1637 N ASP A1005 8564 8256 15056 1159 867 -1354 N
ATOM 1638 CA ASP A1005 2.576 -41.294 18.216 1.00 87.86 C
ANISOU 1638 CA ASP A1005 8998 8780 15603 1237 856 -1441 C
ATOM 1639 C ASP A1005 2.219 -42.696 18.635 1.00 79.81 C
ANISOU 1639 C ASP A1005 8182 7894 14249 1183 745 -1367 C
ATOM 1640 O ASP A1005 2.980 -43.598 18.415 1.00 80.10 O
ANISOU 1640 O ASP A1005 8375 7845 14216 1217 796 -1310 O
ATOM 1641 CB ASP A1005 2.949 -40.444 19.398 1.00 98.28 C
ANISOU 1641 CB ASP A1005 9968 10217 17157 1309 779 -1660 C
ATOM 1642 CG ASP A1005 4.131 -41.007 20.133 1.00110.88 C
ANISOU 1642 CG ASP A1005 11492 11813 18825 1403 770 -1761 C
ATOM 1643 OD1 ASP A1005 4.666 -42.045 19.710 1.00108.78 O
ANISOU 1643 OD1 ASP A1005 11444 11459 18427 1405 834 -1654 O
ATOM 1644 OD2 ASP A1005 4.513 -40.419 21.171 1.00122.63 O
ANISOU 1644 OD2 ASP A1005 12705 13393 20495 1482 686 -1954 O
ATOM 1645 N ASN A1006 1.049 -42.881 19.218 1.00 73.51 N
ANISOU 1645 N ASN A1006 7380 7300 13249 1101 595 -1356 N
ATOM 1646 CA ASN A1006 0.612 -44.185 19.653 1.00 67.23 C
ANISOU 1646 CA ASN A1006 6756 6636 12152 1046 482 -1271 C
ATOM 1647 C ASN A1006 0.641 -45.209 18.512 1.00 61.23 C
ANISOU 1647 C ASN A1006 6345 5709 11211 1001 540 -1080 C
ATOM 1648 O ASN A1006 1.085 -46.321 18.688 1.00 58.99 O
ANISOU 1648 O ASN A1006 6201 5431 10780 1011 516 -1035 O
ATOM 1649 CB ASN A1006 -0.773 -44.090 20.273 1.00 66.25 C
ANISOU 1649 CB ASN A1006 6571 6731 11868 963 333 -1254 C
ATOM 1650 CG ASN A1006 -0.730 -43.686 21.727 1.00 76.06 C
ANISOU 1650 CG ASN A1006 7531 8199 13171 1034 233 -1429 C
ATOM 1651 OD1 ASN A1006 0.309 -43.650 22.337 1.00 83.13 O
ANISOU 1651 OD1 ASN A1006 8294 9094 14196 1138 250 -1564 O
ATOM 1652 ND2 ASN A1006 -1.863 -43.406 22.280 1.00 77.37 N
ANISOU 1652 ND2 ASN A1006 7609 8552 13236 987 123 -1423 N
ATOM 1653 N TRP A1007 0.175 -44.791 17.354 1.00 59.46 N
ANISOU 1653 N TRP A1007 6256 5335 11000 963 610 -975 N
ATOM 1654 CA TRP A1007 0.154 -45.604 16.186 1.00 57.48 C
ANISOU 1654 CA TRP A1007 6339 4911 10590 944 659 -803 C
ATOM 1655 C TRP A1007 1.568 -45.951 15.805 1.00 62.67 C
ANISOU 1655 C TRP A1007 7067 5401 11345 1053 801 -804 C
ATOM 1656 O TRP A1007 1.875 -47.081 15.539 1.00 61.65 O
ANISOU 1656 O TRP A1007 7167 5220 11039 1059 789 -713 O
ATOM 1657 CB TRP A1007 -0.495 -44.829 15.067 1.00 57.67 C
ANISOU 1657 CB TRP A1007 6449 4801 10662 918 725 -725 C
ATOM 1658 CG TRP A1007 -0.530 -45.478 13.747 1.00 59.02 C
ANISOU 1658 CG TRP A1007 6966 4771 10688 929 781 -557 C
ATOM 1659 CD1 TRP A1007 0.139 -45.090 12.647 1.00 65.91 C
ANISOU 1659 CD1 TRP A1007 7946 5420 11677 1025 959 -503 C
ATOM 1660 CD2 TRP A1007 -1.329 -46.595 13.351 1.00 56.14 C
ANISOU 1660 CD2 TRP A1007 6890 4401 10038 855 652 -416 C
ATOM 1661 NE1 TRP A1007 -0.160 -45.891 11.600 1.00 67.38 N
ANISOU 1661 NE1 TRP A1007 8480 5469 11653 1029 949 -346 N
ATOM 1662 CE2 TRP A1007 -1.066 -46.830 12.007 1.00 61.65 C
ANISOU 1662 CE2 TRP A1007 7872 4869 10684 921 751 -296 C
ATOM 1663 CE3 TRP A1007 -2.223 -47.427 14.010 1.00 52.25 C
ANISOU 1663 CE3 TRP A1007 6440 4072 9341 749 461 -375 C
ATOM 1664 CZ2 TRP A1007 -1.664 -47.859 11.305 1.00 62.82 C
ANISOU 1664 CZ2 TRP A1007 8348 4939 10581 887 646 -152 C
ATOM 1665 CZ3 TRP A1007 -2.828 -48.433 13.306 1.00 53.54 C
ANISOU 1665 CZ3 TRP A1007 6912 4151 9278 701 362 -223 C
ATOM 1666 CH2 TRP A1007 -2.546 -48.641 11.968 1.00 58.43 C
ANISOU 1666 CH2 TRP A1007 7816 4535 9850 770 445 -121 C
ATOM 1667 N GLU A1008 2.431 -44.965 15.778 1.00 69.19 N
ANISOU 1667 N GLU A1008 7688 6137 12465 1142 934 -904 N
ATOM 1668 CA GLU A1008 3.804 -45.210 15.409 1.00 76.92 C
ANISOU 1668 CA GLU A1008 8709 6946 13572 1253 1084 -897 C
ATOM 1669 C GLU A1008 4.483 -46.155 16.372 1.00 76.46 C
ANISOU 1669 C GLU A1008 8627 6993 13433 1275 1013 -964 C
ATOM 1670 O GLU A1008 5.270 -46.966 15.964 1.00 79.37 O
ANISOU 1670 O GLU A1008 9172 7247 13736 1327 1083 -893 O
ATOM 1671 CB GLU A1008 4.591 -43.919 15.285 1.00 88.95 C
ANISOU 1671 CB GLU A1008 9976 8351 15470 1343 1231 -991 C
ATOM 1672 CG GLU A1008 4.660 -43.407 13.868 1.00 99.42 C
ANISOU 1672 CG GLU A1008 11442 9449 16883 1391 1408 -858 C
ATOM 1673 CD GLU A1008 4.720 -41.902 13.805 1.00114.22 C
ANISOU 1673 CD GLU A1008 13037 11271 19091 1423 1493 -943 C
ATOM 1674 OE1 GLU A1008 5.431 -41.304 14.630 1.00121.65 O
ANISOU 1674 OE1 GLU A1008 13679 12243 20298 1473 1493 -1096 O
ATOM 1675 OE2 GLU A1008 4.052 -41.318 12.933 1.00117.11 O
ANISOU 1675 OE2 GLU A1008 13481 11559 19456 1403 1552 -859 O
ATOM 1676 N THR A1009 4.163 -46.049 17.642 1.00 73.66 N
ANISOU 1676 N THR A1009 8059 6856 13073 1246 874 -1099 N
ATOM 1677 CA THR A1009 4.670 -46.906 18.673 1.00 73.86 C
ANISOU 1677 CA THR A1009 8047 7011 13006 1270 789 -1174 C
ATOM 1678 C THR A1009 4.197 -48.373 18.509 1.00 67.26 C
ANISOU 1678 C THR A1009 7511 6222 11824 1198 702 -1026 C
ATOM 1679 O THR A1009 4.885 -49.295 18.853 1.00 67.73 O
ANISOU 1679 O THR A1009 7646 6293 11795 1230 692 -1030 O
ATOM 1680 CB THR A1009 4.270 -46.323 20.029 1.00 76.30 C
ANISOU 1680 CB THR A1009 8060 7551 13379 1274 657 -1346 C
ATOM 1681 OG1 THR A1009 5.070 -45.168 20.284 1.00 87.24 O
ANISOU 1681 OG1 THR A1009 9169 8868 15110 1369 728 -1505 O
ATOM 1682 CG2 THR A1009 4.463 -47.291 21.113 1.00 75.56 C
ANISOU 1682 CG2 THR A1009 7959 7629 13121 1289 546 -1400 C
ATOM 1683 N LEU A1010 3.024 -48.576 17.953 1.00 61.78 N
ANISOU 1683 N LEU A1010 6985 5542 10947 1101 634 -896 N
ATOM 1684 CA LEU A1010 2.527 -49.894 17.747 1.00 57.58 C
ANISOU 1684 CA LEU A1010 6724 5033 10122 1033 536 -754 C
ATOM 1685 C LEU A1010 3.248 -50.531 16.568 1.00 60.40 C
ANISOU 1685 C LEU A1010 7369 5157 10424 1084 646 -634 C
ATOM 1686 O LEU A1010 3.489 -51.708 16.557 1.00 59.47 O
ANISOU 1686 O LEU A1010 7443 5032 10120 1078 598 -563 O
ATOM 1687 CB LEU A1010 1.046 -49.812 17.461 1.00 54.00 C
ANISOU 1687 CB LEU A1010 6347 4640 9530 920 424 -654 C
ATOM 1688 CG LEU A1010 0.243 -51.075 17.266 1.00 53.01 C
ANISOU 1688 CG LEU A1010 6477 4542 9124 830 284 -497 C
ATOM 1689 CD1 LEU A1010 -1.204 -50.708 17.469 1.00 51.88 C
ANISOU 1689 CD1 LEU A1010 6267 4523 8922 725 162 -454 C
ATOM 1690 CD2 LEU A1010 0.431 -51.606 15.869 1.00 56.07 C
ANISOU 1690 CD2 LEU A1010 7194 4690 9419 848 340 -357 C
ATOM 1691 N ASN A1011 3.585 -49.741 15.576 1.00 64.76 N
ANISOU 1691 N ASN A1011 7949 5520 11135 1144 796 -607 N
ATOM 1692 CA ASN A1011 4.243 -50.252 14.405 1.00 70.37 C
ANISOU 1692 CA ASN A1011 8936 6008 11793 1219 916 -483 C
ATOM 1693 C ASN A1011 5.724 -50.497 14.585 1.00 76.87 C
ANISOU 1693 C ASN A1011 9713 6752 12741 1330 1041 -535 C
ATOM 1694 O ASN A1011 6.231 -51.485 14.136 1.00 79.74 O
ANISOU 1694 O ASN A1011 10316 7025 12956 1370 1064 -444 O
ATOM 1695 CB ASN A1011 3.972 -49.360 13.219 1.00 76.15 C
ANISOU 1695 CB ASN A1011 9739 6569 12628 1256 1036 -410 C
ATOM 1696 CG ASN A1011 2.538 -49.435 12.774 1.00 75.55 C
ANISOU 1696 CG ASN A1011 9813 6524 12369 1153 905 -319 C
ATOM 1697 OD1 ASN A1011 1.815 -50.307 13.195 1.00 71.81 O
ANISOU 1697 OD1 ASN A1011 9434 6168 11682 1061 732 -279 O
ATOM 1698 ND2 ASN A1011 2.120 -48.514 11.929 1.00 79.32 N
ANISOU 1698 ND2 ASN A1011 10304 6893 12942 1171 986 -282 N
ATOM 1699 N ASP A1012 6.401 -49.613 15.276 1.00 80.19 N
ANISOU 1699 N ASP A1012 9824 7208 13438 1380 1110 -686 N
ATOM 1700 CA ASP A1012 7.835 -49.750 15.518 1.00 88.54 C
ANISOU 1700 CA ASP A1012 10799 8183 14659 1487 1225 -749 C
ATOM 1701 C ASP A1012 8.134 -50.883 16.475 1.00 84.88 C
ANISOU 1701 C ASP A1012 10365 7862 14023 1465 1107 -799 C
ATOM 1702 O ASP A1012 9.113 -51.603 16.279 1.00 90.20 O
ANISOU 1702 O ASP A1012 11161 8441 14670 1532 1180 -764 O
ATOM 1703 CB ASP A1012 8.441 -48.443 16.051 1.00 97.19 C
ANISOU 1703 CB ASP A1012 11531 9269 16129 1548 1303 -909 C
ATOM 1704 CG ASP A1012 8.352 -47.272 15.090 1.00107.59 C
ANISOU 1704 CG ASP A1012 12793 10421 17665 1588 1450 -858 C
ATOM 1705 OD1 ASP A1012 8.032 -47.501 13.899 1.00108.18 O
ANISOU 1705 OD1 ASP A1012 13136 10361 17608 1597 1526 -691 O
ATOM 1706 OD2 ASP A1012 8.582 -46.128 15.532 1.00115.78 O
ANISOU 1706 OD2 ASP A1012 13524 11465 19004 1617 1481 -987 O
ATOM 1707 N ASN A1013 7.309 -51.040 17.512 1.00 76.71 N
ANISOU 1707 N ASN A1013 9216 7056 12873 1380 932 -875 N
ATOM 1708 CA ASN A1013 7.499 -52.125 18.464 1.00 73.85 C
ANISOU 1708 CA ASN A1013 8878 6845 12335 1362 817 -914 C
ATOM 1709 C ASN A1013 7.191 -53.505 17.847 1.00 69.72 C
ANISOU 1709 C ASN A1013 8710 6281 11500 1312 760 -741 C
ATOM 1710 O ASN A1013 7.760 -54.498 18.288 1.00 69.77 O
ANISOU 1710 O ASN A1013 8794 6328 11387 1328 726 -746 O
ATOM 1711 CB ASN A1013 6.741 -51.876 19.751 1.00 70.77 C
ANISOU 1711 CB ASN A1013 8262 6711 11918 1313 663 -1033 C
ATOM 1712 CG ASN A1013 7.527 -51.058 20.741 1.00 80.68 C
ANISOU 1712 CG ASN A1013 9191 8028 13435 1404 683 -1243 C
ATOM 1713 OD1 ASN A1013 8.684 -51.355 21.034 1.00 87.85 O
ANISOU 1713 OD1 ASN A1013 10060 8882 14436 1486 739 -1316 O
ATOM 1714 ND2 ASN A1013 6.917 -50.017 21.283 1.00 81.82 N
ANISOU 1714 ND2 ASN A1013 9096 8285 13707 1398 627 -1348 N
ATOM 1715 N LEU A1014 6.401 -53.526 16.795 1.00 67.83 N
ANISOU 1715 N LEU A1014 8682 5940 11150 1266 755 -596 N
ATOM 1716 CA LEU A1014 6.108 -54.740 16.103 1.00 67.54 C
ANISOU 1716 CA LEU A1014 8986 5833 10844 1233 690 -437 C
ATOM 1717 C LEU A1014 7.386 -55.173 15.414 1.00 76.58 C
ANISOU 1717 C LEU A1014 10294 6789 12013 1348 837 -393 C
ATOM 1718 O LEU A1014 7.812 -56.303 15.566 1.00 77.20 O
ANISOU 1718 O LEU A1014 10529 6877 11927 1355 791 -356 O
ATOM 1719 CB LEU A1014 5.027 -54.515 15.079 1.00 66.61 C
ANISOU 1719 CB LEU A1014 9047 5624 10637 1182 652 -309 C
ATOM 1720 CG LEU A1014 3.695 -55.119 15.442 1.00 62.12 C
ANISOU 1720 CG LEU A1014 8542 5198 9863 1051 444 -243 C
ATOM 1721 CD1 LEU A1014 2.597 -54.468 14.637 1.00 62.40 C
ANISOU 1721 CD1 LEU A1014 8644 5167 9897 1000 415 -168 C
ATOM 1722 CD2 LEU A1014 3.675 -56.616 15.234 1.00 63.24 C
ANISOU 1722 CD2 LEU A1014 8968 5311 9751 1027 333 -126 C
ATOM 1723 N LYS A1015 8.000 -54.257 14.675 1.00 84.21 N
ANISOU 1723 N LYS A1015 11215 7587 13195 1443 1020 -392 N
ATOM 1724 CA LYS A1015 9.240 -54.500 13.941 1.00 95.34 C
ANISOU 1724 CA LYS A1015 12759 8801 14666 1573 1194 -335 C
ATOM 1725 C LYS A1015 10.341 -54.941 14.892 1.00 97.78 C
ANISOU 1725 C LYS A1015 12929 9175 15046 1612 1211 -446 C
ATOM 1726 O LYS A1015 11.082 -55.863 14.563 1.00103.14 O
ANISOU 1726 O LYS A1015 13810 9769 15608 1670 1253 -377 O
ATOM 1727 CB LYS A1015 9.679 -53.242 13.180 1.00106.63 C
ANISOU 1727 CB LYS A1015 14079 10060 16375 1670 1397 -326 C
ATOM 1728 CG LYS A1015 8.780 -52.895 12.004 1.00112.21 C
ANISOU 1728 CG LYS A1015 14983 10656 16996 1668 1415 -194 C
ATOM 1729 CD LYS A1015 9.258 -51.639 11.295 1.00127.82 C
ANISOU 1729 CD LYS A1015 16834 12469 19261 1773 1630 -180 C
ATOM 1730 CE LYS A1015 8.315 -51.195 10.203 1.00133.56 C
ANISOU 1730 CE LYS A1015 17734 13101 19911 1775 1645 -66 C
ATOM 1731 NZ LYS A1015 8.225 -52.201 9.109 1.00142.56 N
ANISOU 1731 NZ LYS A1015 19291 14106 20770 1844 1639 104 N
ATOM 1732 N VAL A1016 10.429 -54.311 16.080 1.00 94.62 N
ANISOU 1732 N VAL A1016 12197 8928 14826 1587 1168 -621 N
ATOM 1733 CA VAL A1016 11.416 -54.662 17.104 1.00 97.86 C
ANISOU 1733 CA VAL A1016 12452 9416 15315 1628 1162 -752 C
ATOM 1734 C VAL A1016 11.235 -56.140 17.524 1.00 92.21 C
ANISOU 1734 C VAL A1016 11940 8816 14281 1572 1022 -706 C
ATOM 1735 O VAL A1016 12.218 -56.861 17.664 1.00 96.94 O
ANISOU 1735 O VAL A1016 12608 9372 14850 1629 1066 -715 O
ATOM 1736 CB VAL A1016 11.346 -53.673 18.302 1.00 97.71 C
ANISOU 1736 CB VAL A1016 12051 9549 15524 1622 1106 -955 C
ATOM 1737 CG1 VAL A1016 12.021 -54.227 19.552 1.00 99.37 C
ANISOU 1737 CG1 VAL A1016 12129 9898 15730 1649 1031 -1099 C
ATOM 1738 CG2 VAL A1016 11.942 -52.323 17.927 1.00108.21 C
ANISOU 1738 CG2 VAL A1016 13165 10728 17222 1705 1263 -1012 C
ATOM 1739 N ILE A1017 9.997 -56.577 17.630 1.00 83.45 N
ANISOU 1739 N ILE A1017 10932 7829 12947 1463 864 -641 N
ATOM 1740 CA ILE A1017 9.661 -57.939 18.002 1.00 79.03 C
ANISOU 1740 CA ILE A1017 10553 7376 12099 1399 718 -579 C
ATOM 1741 C ILE A1017 10.089 -58.933 16.916 1.00 84.49 C
ANISOU 1741 C ILE A1017 11599 7889 12614 1437 760 -424 C
ATOM 1742 O ILE A1017 10.609 -59.975 17.221 1.00 85.45 O
ANISOU 1742 O ILE A1017 11832 8038 12596 1446 721 -414 O
ATOM 1743 CB ILE A1017 8.174 -58.061 18.353 1.00 70.47 C
ANISOU 1743 CB ILE A1017 9464 6453 10859 1276 541 -533 C
ATOM 1744 CG1 ILE A1017 7.921 -57.386 19.682 1.00 68.44 C
ANISOU 1744 CG1 ILE A1017 8869 6411 10724 1262 484 -695 C
ATOM 1745 CG2 ILE A1017 7.754 -59.503 18.474 1.00 67.56 C
ANISOU 1745 CG2 ILE A1017 9319 6147 10203 1208 394 -425 C
ATOM 1746 CD1 ILE A1017 6.486 -57.432 20.094 1.00 63.32 C
ANISOU 1746 CD1 ILE A1017 8186 5929 9944 1154 327 -644 C
ATOM 1747 N GLU A1018 9.880 -58.576 15.662 1.00 89.01 N
ANISOU 1747 N GLU A1018 12346 8280 13194 1473 840 -308 N
ATOM 1748 CA GLU A1018 10.265 -59.364 14.510 1.00 97.45 C
ANISOU 1748 CA GLU A1018 13762 9161 14104 1542 890 -159 C
ATOM 1749 C GLU A1018 11.766 -59.569 14.355 1.00108.92 C
ANISOU 1749 C GLU A1018 15238 10496 15652 1669 1058 -176 C
ATOM 1750 O GLU A1018 12.181 -60.581 13.844 1.00114.43 O
ANISOU 1750 O GLU A1018 16205 11108 16165 1716 1054 -80 O
ATOM 1751 CB GLU A1018 9.780 -58.713 13.224 1.00104.05 C
ANISOU 1751 CB GLU A1018 14746 9826 14965 1586 964 -48 C
ATOM 1752 CG GLU A1018 8.308 -58.816 12.919 1.00102.32 C
ANISOU 1752 CG GLU A1018 14643 9648 14584 1480 793 29 C
ATOM 1753 CD GLU A1018 7.912 -57.810 11.858 1.00113.25 C
ANISOU 1753 CD GLU A1018 16073 10885 16070 1532 895 89 C
ATOM 1754 OE1 GLU A1018 6.719 -57.655 11.562 1.00110.59 O
ANISOU 1754 OE1 GLU A1018 15801 10568 15651 1453 775 139 O
ATOM 1755 OE2 GLU A1018 8.807 -57.161 11.317 1.00123.39 O
ANISOU 1755 OE2 GLU A1018 17324 12030 17529 1657 1101 90 O
ATOM 1756 N LYS A1019 12.561 -58.581 14.733 1.00114.09 N
ANISOU 1756 N LYS A1019 15613 11131 16605 1732 1204 -290 N
ATOM 1757 CA LYS A1019 14.024 -58.621 14.634 1.00127.04 C
ANISOU 1757 CA LYS A1019 17224 12649 18398 1856 1376 -311 C
ATOM 1758 C LYS A1019 14.722 -59.042 15.930 1.00126.38 C
ANISOU 1758 C LYS A1019 16953 12707 18358 1839 1322 -463 C
ATOM 1759 O LYS A1019 15.949 -59.049 15.970 1.00137.18 O
ANISOU 1759 O LYS A1019 18265 13982 19877 1935 1453 -498 O
ATOM 1760 CB LYS A1019 14.569 -57.242 14.206 1.00138.62 C
ANISOU 1760 CB LYS A1019 18482 13973 20213 1949 1577 -336 C
ATOM 1761 CG LYS A1019 13.912 -56.657 12.962 1.00144.97 C
ANISOU 1761 CG LYS A1019 19437 14638 21006 1982 1652 -198 C
ATOM 1762 CD LYS A1019 14.235 -57.447 11.714 1.00159.43 C
ANISOU 1762 CD LYS A1019 21649 16290 22636 2087 1733 -11 C
ATOM 1763 CE LYS A1019 13.464 -56.939 10.522 1.00166.59 C
ANISOU 1763 CE LYS A1019 22728 17074 23494 2126 1778 119 C
ATOM 1764 NZ LYS A1019 13.730 -55.499 10.266 1.00175.86 N
ANISOU 1764 NZ LYS A1019 23653 18156 25008 2190 1962 93 N
ATOM 1765 N ALA A1020 13.971 -59.346 16.996 1.00115.45 N
ANISOU 1765 N ALA A1020 15461 11544 16860 1731 1137 -553 N
ATOM 1766 CA ALA A1020 14.566 -59.731 18.273 1.00115.54 C
ANISOU 1766 CA ALA A1020 15296 11704 16898 1729 1078 -704 C
ATOM 1767 C ALA A1020 15.222 -61.117 18.215 1.00118.97 C
ANISOU 1767 C ALA A1020 15972 12118 17115 1749 1060 -641 C
ATOM 1768 O ALA A1020 14.857 -61.941 17.379 1.00118.05 O
ANISOU 1768 O ALA A1020 16165 11928 16759 1729 1023 -483 O
ATOM 1769 CB ALA A1020 13.513 -59.690 19.369 1.00104.59 C
ANISOU 1769 CB ALA A1020 13748 10563 15428 1627 896 -793 C
ATOM 1770 N ASP A1021 16.163 -61.305 19.124 1.00123.88 N
ANISOU 1770 N ASP A1021 16438 12800 17831 1792 1076 -776 N
ATOM 1771 CA ASP A1021 16.918 -62.523 19.253 1.00128.50 C
ANISOU 1771 CA ASP A1021 17198 13379 18246 1817 1066 -751 C
ATOM 1772 C ASP A1021 16.567 -63.287 20.511 1.00120.37 C
ANISOU 1772 C ASP A1021 16102 12586 17049 1747 895 -843 C
ATOM 1773 O ASP A1021 16.681 -64.486 20.521 1.00119.51 O
ANISOU 1773 O ASP A1021 16200 12504 16704 1723 831 -776 O
ATOM 1774 CB ASP A1021 18.444 -62.249 19.149 1.00146.03 C
ANISOU 1774 CB ASP A1021 19331 15447 20706 1941 1245 -809 C
ATOM 1775 CG ASP A1021 18.901 -61.870 17.735 1.00163.02 C
ANISOU 1775 CG ASP A1021 21639 17347 22953 2032 1434 -657 C
ATOM 1776 OD1 ASP A1021 18.108 -62.097 16.798 1.00159.90 O
ANISOU 1776 OD1 ASP A1021 21486 16896 22371 2005 1410 -502 O
ATOM 1777 OD2 ASP A1021 20.040 -61.353 17.560 1.00179.65 O
ANISOU 1777 OD2 ASP A1021 23626 19309 25325 2139 1604 -686 O
ATOM 1778 N ASN A1022 16.111 -62.614 21.559 1.00115.41 N
ANISOU 1778 N ASN A1022 15191 12127 16531 1722 818 -988 N
ATOM 1779 CA ASN A1022 15.761 -63.334 22.770 1.00109.49 C
ANISOU 1779 CA ASN A1022 14379 11608 15615 1678 667 -1063 C
ATOM 1780 C ASN A1022 14.397 -62.970 23.276 1.00100.04 C
ANISOU 1780 C ASN A1022 13070 10588 14354 1597 536 -1063 C
ATOM 1781 O ASN A1022 13.773 -62.069 22.770 1.00 98.00 O
ANISOU 1781 O ASN A1022 12754 10279 14202 1574 560 -1032 O
ATOM 1782 CB ASN A1022 16.788 -63.102 23.880 1.00118.26 C
ANISOU 1782 CB ASN A1022 15248 12788 16899 1769 689 -1271 C
ATOM 1783 CG ASN A1022 16.931 -61.652 24.261 1.00126.58 C
ANISOU 1783 CG ASN A1022 15985 13831 18276 1830 734 -1428 C
ATOM 1784 OD1 ASN A1022 15.977 -61.014 24.630 1.00122.33 O
ANISOU 1784 OD1 ASN A1022 15310 13414 17757 1793 657 -1461 O
ATOM 1785 ND2 ASN A1022 18.137 -61.140 24.204 1.00139.26 N
ANISOU 1785 ND2 ASN A1022 17470 15294 20149 1929 853 -1525 N
ATOM 1786 N ALA A1023 13.964 -63.680 24.306 1.00 95.31 N
ANISOU 1786 N ALA A1023 12432 10199 13582 1563 405 -1095 N
ATOM 1787 CA ALA A1023 12.677 -63.451 24.909 1.00 88.77 C
ANISOU 1787 CA ALA A1023 11491 9559 12678 1497 281 -1082 C
ATOM 1788 C ALA A1023 12.638 -62.079 25.547 1.00 91.58 C
ANISOU 1788 C ALA A1023 11530 9984 13281 1559 303 -1254 C
ATOM 1789 O ALA A1023 11.682 -61.358 25.391 1.00 88.35 O
ANISOU 1789 O ALA A1023 11045 9612 12913 1513 271 -1221 O
ATOM 1790 CB ALA A1023 12.353 -64.530 25.914 1.00 86.63 C
ANISOU 1790 CB ALA A1023 11237 9494 12184 1471 156 -1072 C
ATOM 1791 N ALA A1024 13.700 -61.688 26.220 1.00 98.67 N
ANISOU 1791 N ALA A1024 12246 10884 14360 1669 354 -1439 N
ATOM 1792 CA ALA A1024 13.709 -60.404 26.891 1.00103.42 C
ANISOU 1792 CA ALA A1024 12541 11547 15207 1744 351 -1618 C
ATOM 1793 C ALA A1024 13.465 -59.213 25.990 1.00102.52 C
ANISOU 1793 C ALA A1024 12365 11280 15308 1728 434 -1592 C
ATOM 1794 O ALA A1024 12.864 -58.257 26.404 1.00103.11 O
ANISOU 1794 O ALA A1024 12238 11443 15497 1739 391 -1672 O
ATOM 1795 CB ALA A1024 14.984 -60.220 27.684 1.00114.91 C
ANISOU 1795 CB ALA A1024 13823 12994 16843 1874 381 -1825 C
ATOM 1796 N GLN A1025 13.912 -59.263 24.752 1.00101.96 N
ANISOU 1796 N GLN A1025 12471 10983 15286 1711 556 -1473 N
ATOM 1797 CA GLN A1025 13.705 -58.132 23.883 1.00102.55 C
ANISOU 1797 CA GLN A1025 12487 10910 15567 1708 647 -1441 C
ATOM 1798 C GLN A1025 12.261 -58.085 23.493 1.00 91.74 C
ANISOU 1798 C GLN A1025 11213 9613 14032 1599 568 -1309 C
ATOM 1799 O GLN A1025 11.677 -57.037 23.376 1.00 91.20 O
ANISOU 1799 O GLN A1025 11002 9548 14103 1587 572 -1337 O
ATOM 1800 CB GLN A1025 14.518 -58.268 22.631 1.00109.23 C
ANISOU 1800 CB GLN A1025 13521 11500 16483 1737 806 -1325 C
ATOM 1801 CG GLN A1025 15.959 -57.900 22.812 1.00126.15 C
ANISOU 1801 CG GLN A1025 15515 13516 18899 1852 921 -1449 C
ATOM 1802 CD GLN A1025 16.775 -58.321 21.637 1.00137.07 C
ANISOU 1802 CD GLN A1025 17124 14668 20289 1890 1078 -1305 C
ATOM 1803 OE1 GLN A1025 16.571 -57.859 20.530 1.00140.03 O
ANISOU 1803 OE1 GLN A1025 17596 14888 20721 1890 1181 -1178 O
ATOM 1804 NE2 GLN A1025 17.696 -59.220 21.868 1.00142.68 N
ANISOU 1804 NE2 GLN A1025 17926 15358 20928 1931 1098 -1319 N
ATOM 1805 N VAL A1026 11.696 -59.258 23.294 1.00 83.94 N
ANISOU 1805 N VAL A1026 10468 8676 12751 1520 489 -1163 N
ATOM 1806 CA VAL A1026 10.311 -59.392 22.924 1.00 75.36 C
ANISOU 1806 CA VAL A1026 9491 7648 11495 1410 395 -1021 C
ATOM 1807 C VAL A1026 9.471 -58.924 24.084 1.00 72.88 C
ANISOU 1807 C VAL A1026 8936 7572 11184 1396 282 -1116 C
ATOM 1808 O VAL A1026 8.528 -58.203 23.901 1.00 70.12 O
ANISOU 1808 O VAL A1026 8516 7254 10872 1347 252 -1085 O
ATOM 1809 CB VAL A1026 9.983 -60.831 22.523 1.00 71.65 C
ANISOU 1809 CB VAL A1026 9324 7169 10732 1338 317 -850 C
ATOM 1810 CG1 VAL A1026 8.495 -61.013 22.378 1.00 65.87 C
ANISOU 1810 CG1 VAL A1026 8663 6521 9843 1224 186 -718 C
ATOM 1811 CG2 VAL A1026 10.684 -61.188 21.227 1.00 75.44 C
ANISOU 1811 CG2 VAL A1026 10066 7402 11198 1367 426 -742 C
ATOM 1812 N LYS A1027 9.858 -59.282 25.292 1.00 75.20 N
ANISOU 1812 N LYS A1027 9096 8032 11445 1454 226 -1238 N
ATOM 1813 CA LYS A1027 9.111 -58.862 26.448 1.00 76.11 C
ANISOU 1813 CA LYS A1027 8986 8383 11549 1472 124 -1327 C
ATOM 1814 C LYS A1027 9.156 -57.362 26.622 1.00 80.83 C
ANISOU 1814 C LYS A1027 9326 8970 12416 1537 162 -1478 C
ATOM 1815 O LYS A1027 8.255 -56.781 27.185 1.00 80.98 O
ANISOU 1815 O LYS A1027 9192 9144 12433 1531 87 -1510 O
ATOM 1816 CB LYS A1027 9.610 -59.541 27.711 1.00 82.02 C
ANISOU 1816 CB LYS A1027 9652 9306 12208 1553 64 -1436 C
ATOM 1817 CG LYS A1027 9.256 -58.792 28.974 1.00 91.55 C
ANISOU 1817 CG LYS A1027 10576 10728 13483 1644 -9 -1597 C
ATOM 1818 CD LYS A1027 9.771 -59.506 30.203 1.00101.75 C
ANISOU 1818 CD LYS A1027 11803 12188 14668 1744 -66 -1703 C
ATOM 1819 CE LYS A1027 8.691 -59.619 31.253 1.00106.97 C
ANISOU 1819 CE LYS A1027 12355 13119 15170 1767 -177 -1682 C
ATOM 1820 NZ LYS A1027 9.214 -59.569 32.637 1.00119.63 N
ANISOU 1820 NZ LYS A1027 13774 14899 16780 1936 -226 -1878 N
ATOM 1821 N ASP A1028 10.209 -56.734 26.136 1.00 85.81 N
ANISOU 1821 N ASP A1028 9903 9414 13288 1602 279 -1566 N
ATOM 1822 CA ASP A1028 10.357 -55.297 26.288 1.00 91.95 C
ANISOU 1822 CA ASP A1028 10422 10157 14357 1669 312 -1715 C
ATOM 1823 C ASP A1028 9.406 -54.584 25.396 1.00 85.22 C
ANISOU 1823 C ASP A1028 9604 9237 13537 1583 337 -1604 C
ATOM 1824 O ASP A1028 8.707 -53.716 25.825 1.00 86.20 O
ANISOU 1824 O ASP A1028 9547 9470 13736 1587 280 -1672 O
ATOM 1825 CB ASP A1028 11.766 -54.841 25.900 1.00103.83 C
ANISOU 1825 CB ASP A1028 11861 11449 16143 1758 441 -1811 C
ATOM 1826 CG ASP A1028 12.827 -55.265 26.896 1.00119.09 C
ANISOU 1826 CG ASP A1028 13692 13436 18119 1866 412 -1974 C
ATOM 1827 OD1 ASP A1028 12.477 -55.661 28.023 1.00120.56 O
ANISOU 1827 OD1 ASP A1028 13807 13844 18155 1898 290 -2052 O
ATOM 1828 OD2 ASP A1028 14.017 -55.213 26.539 1.00129.94 O
ANISOU 1828 OD2 ASP A1028 15062 14629 19680 1927 516 -2016 O
ATOM 1829 N ALA A1029 9.405 -54.963 24.136 1.00 79.57 N
ANISOU 1829 N ALA A1029 9133 8338 12760 1517 421 -1433 N
ATOM 1830 CA ALA A1029 8.577 -54.323 23.153 1.00 75.04 C
ANISOU 1830 CA ALA A1029 8625 7672 12216 1445 455 -1321 C
ATOM 1831 C ALA A1029 7.067 -54.512 23.311 1.00 67.36 C
ANISOU 1831 C ALA A1029 7699 6858 11036 1338 326 -1219 C
ATOM 1832 O ALA A1029 6.301 -53.710 22.825 1.00 65.79 O
ANISOU 1832 O ALA A1029 7463 6631 10901 1292 332 -1181 O
ATOM 1833 CB ALA A1029 9.018 -54.729 21.780 1.00 74.67 C
ANISOU 1833 CB ALA A1029 8843 7385 12142 1430 574 -1169 C
ATOM 1834 N LEU A1030 6.658 -55.561 23.991 1.00 63.55 N
ANISOU 1834 N LEU A1030 7289 6538 10319 1302 214 -1169 N
ATOM 1835 CA LEU A1030 5.249 -55.834 24.187 1.00 58.59 C
ANISOU 1835 CA LEU A1030 6697 6058 9507 1204 92 -1053 C
ATOM 1836 C LEU A1030 4.696 -55.124 25.404 1.00 61.78 C
ANISOU 1836 C LEU A1030 6820 6693 9962 1248 15 -1178 C
ATOM 1837 O LEU A1030 3.542 -54.754 25.442 1.00 59.54 O
ANISOU 1837 O LEU A1030 6490 6501 9631 1184 -50 -1113 O
ATOM 1838 CB LEU A1030 5.013 -57.330 24.313 1.00 55.69 C
ANISOU 1838 CB LEU A1030 6538 5747 8875 1146 7 -916 C
ATOM 1839 CG LEU A1030 5.143 -58.223 23.084 1.00 53.65 C
ANISOU 1839 CG LEU A1030 6605 5286 8492 1084 29 -747 C
ATOM 1840 CD1 LEU A1030 5.364 -59.636 23.576 1.00 53.82 C
ANISOU 1840 CD1 LEU A1030 6756 5385 8308 1072 -45 -687 C
ATOM 1841 CD2 LEU A1030 3.905 -58.155 22.240 1.00 50.77 C
ANISOU 1841 CD2 LEU A1030 6377 4864 8049 975 -33 -585 C
ATOM 1842 N THR A1031 5.544 -54.931 26.400 1.00 68.46 N
ANISOU 1842 N THR A1031 7480 7628 10904 1369 18 -1361 N
ATOM 1843 CA THR A1031 5.167 -54.244 27.622 1.00 75.79 C
ANISOU 1843 CA THR A1031 8142 8775 11881 1451 -59 -1505 C
ATOM 1844 C THR A1031 4.913 -52.778 27.303 1.00 78.16 C
ANISOU 1844 C THR A1031 8271 9016 12411 1464 -25 -1589 C
ATOM 1845 O THR A1031 4.021 -52.164 27.848 1.00 80.83 O
ANISOU 1845 O THR A1031 8460 9511 12740 1470 -97 -1617 O
ATOM 1846 CB THR A1031 6.263 -54.343 28.673 1.00 86.36 C
ANISOU 1846 CB THR A1031 9337 10187 13290 1599 -68 -1700 C
ATOM 1847 OG1 THR A1031 7.518 -54.263 28.017 1.00 89.50 O
ANISOU 1847 OG1 THR A1031 9784 10360 13862 1631 42 -1758 O
ATOM 1848 CG2 THR A1031 6.184 -55.642 29.401 1.00 86.43 C
ANISOU 1848 CG2 THR A1031 9443 10350 13046 1606 -136 -1637 C
ATOM 1849 N LYS A1032 5.710 -52.257 26.398 1.00 77.82 N
ANISOU 1849 N LYS A1032 8254 8743 12572 1471 90 -1619 N
ATOM 1850 CA LYS A1032 5.565 -50.914 25.943 1.00 80.26 C
ANISOU 1850 CA LYS A1032 8417 8961 13115 1478 140 -1682 C
ATOM 1851 C LYS A1032 4.275 -50.874 25.166 1.00 72.72 C
ANISOU 1851 C LYS A1032 7598 8002 12030 1345 121 -1502 C
ATOM 1852 O LYS A1032 3.485 -49.966 25.325 1.00 74.61 O
ANISOU 1852 O LYS A1032 7695 8320 12334 1331 82 -1534 O
ATOM 1853 CB LYS A1032 6.706 -50.545 25.003 1.00 84.58 C
ANISOU 1853 CB LYS A1032 9001 9242 13895 1512 288 -1703 C
ATOM 1854 CG LYS A1032 7.993 -50.054 25.661 1.00 99.69 C
ANISOU 1854 CG LYS A1032 10698 11112 16068 1652 317 -1913 C
ATOM 1855 CD LYS A1032 9.122 -50.036 24.641 1.00107.16 C
ANISOU 1855 CD LYS A1032 11734 11784 17196 1675 478 -1872 C
ATOM 1856 CE LYS A1032 10.276 -49.149 25.061 1.00124.52 C
ANISOU 1856 CE LYS A1032 13671 13887 19754 1803 518 -2070 C
ATOM 1857 NZ LYS A1032 11.093 -48.678 23.912 1.00131.41 N
ANISOU 1857 NZ LYS A1032 14574 14480 20876 1820 695 -2006 N
ATOM 1858 N MET A1033 4.059 -51.870 24.318 1.00 65.11 N
ANISOU 1858 N MET A1033 6916 6939 10883 1252 139 -1314 N
ATOM 1859 CA MET A1033 2.866 -51.932 23.483 1.00 58.92 C
ANISOU 1859 CA MET A1033 6291 6121 9976 1128 108 -1137 C
ATOM 1860 C MET A1033 1.595 -52.020 24.270 1.00 58.43 C
ANISOU 1860 C MET A1033 6146 6289 9766 1075 -25 -1092 C
ATOM 1861 O MET A1033 0.604 -51.463 23.876 1.00 57.06 O
ANISOU 1861 O MET A1033 5965 6122 9595 1004 -51 -1025 O
ATOM 1862 CB MET A1033 2.910 -53.108 22.516 1.00 54.67 C
ANISOU 1862 CB MET A1033 6080 5435 9257 1058 122 -954 C
ATOM 1863 CG MET A1033 3.593 -52.850 21.204 1.00 56.47 C
ANISOU 1863 CG MET A1033 6463 5396 9597 1077 261 -909 C
ATOM 1864 SD MET A1033 4.026 -54.384 20.396 1.00 55.79 S
ANISOU 1864 SD MET A1033 6742 5164 9292 1053 266 -744 S
ATOM 1865 CE MET A1033 2.747 -54.459 19.175 1.00 49.07 C
ANISOU 1865 CE MET A1033 6131 4203 8311 944 212 -550 C
ATOM 1866 N ARG A1034 1.623 -52.734 25.368 1.00 60.73 N
ANISOU 1866 N ARG A1034 6380 6768 9927 1117 -104 -1120 N
ATOM 1867 CA ARG A1034 0.446 -52.869 26.149 1.00 63.64 C
ANISOU 1867 CA ARG A1034 6667 7359 10156 1084 -217 -1057 C
ATOM 1868 C ARG A1034 0.083 -51.549 26.782 1.00 70.95 C
ANISOU 1868 C ARG A1034 7321 8409 11227 1152 -234 -1200 C
ATOM 1869 O ARG A1034 -1.060 -51.226 26.893 1.00 72.49 O
ANISOU 1869 O ARG A1034 7466 8712 11366 1097 -294 -1125 O
ATOM 1870 CB ARG A1034 0.631 -53.924 27.207 1.00 67.57 C
ANISOU 1870 CB ARG A1034 7159 8030 10487 1137 -283 -1052 C
ATOM 1871 CG ARG A1034 -0.632 -54.261 27.945 1.00 73.12 C
ANISOU 1871 CG ARG A1034 7804 8953 11024 1103 -389 -935 C
ATOM 1872 CD ARG A1034 -0.442 -55.497 28.762 1.00 78.68 C
ANISOU 1872 CD ARG A1034 8556 9790 11549 1140 -439 -883 C
ATOM 1873 NE ARG A1034 -1.706 -55.945 29.282 1.00 86.25 N
ANISOU 1873 NE ARG A1034 9490 10928 12355 1091 -529 -718 N
ATOM 1874 CZ ARG A1034 -2.361 -55.307 30.226 1.00 97.81 C
ANISOU 1874 CZ ARG A1034 10739 12605 13819 1170 -567 -763 C
ATOM 1875 NH1 ARG A1034 -1.852 -54.214 30.735 1.00102.24 N
ANISOU 1875 NH1 ARG A1034 11104 13220 14522 1299 -537 -981 N
ATOM 1876 NH2 ARG A1034 -3.521 -55.757 30.653 1.00104.13 N
ANISOU 1876 NH2 ARG A1034 11520 13557 14486 1127 -637 -586 N
ATOM 1877 N ALA A1035 1.065 -50.779 27.192 1.00 76.66 N
ANISOU 1877 N ALA A1035 7866 9112 12148 1276 -187 -1408 N
ATOM 1878 CA ALA A1035 0.785 -49.504 27.807 1.00 84.74 C
ANISOU 1878 CA ALA A1035 8630 10246 13323 1355 -218 -1560 C
ATOM 1879 C ALA A1035 0.164 -48.591 26.798 1.00 81.07 C
ANISOU 1879 C ALA A1035 8178 9654 12971 1262 -174 -1504 C
ATOM 1880 O ALA A1035 -0.808 -47.958 27.081 1.00 84.02 O
ANISOU 1880 O ALA A1035 8440 10153 13332 1244 -231 -1497 O
ATOM 1881 CB ALA A1035 2.047 -48.902 28.364 1.00 93.02 C
ANISOU 1881 CB ALA A1035 9494 11259 14590 1508 -190 -1796 C
ATOM 1882 N ALA A1036 0.705 -48.565 25.597 1.00 75.46 N
ANISOU 1882 N ALA A1036 7616 8697 12359 1208 -68 -1451 N
ATOM 1883 CA ALA A1036 0.187 -47.733 24.513 1.00 72.68 C
ANISOU 1883 CA ALA A1036 7303 8200 12113 1128 -9 -1389 C
ATOM 1884 C ALA A1036 -1.143 -48.168 23.884 1.00 68.16 C
ANISOU 1884 C ALA A1036 6914 7640 11346 984 -62 -1180 C
ATOM 1885 O ALA A1036 -1.685 -47.453 23.060 1.00 66.29 O
ANISOU 1885 O ALA A1036 6703 7302 11182 922 -26 -1134 O
ATOM 1886 CB ALA A1036 1.216 -47.588 23.417 1.00 70.61 C
ANISOU 1886 CB ALA A1036 7149 7667 12012 1141 134 -1386 C
ATOM 1887 N ALA A1037 -1.625 -49.358 24.207 1.00 66.93 N
ANISOU 1887 N ALA A1037 6891 7584 10957 933 -145 -1051 N
ATOM 1888 CA ALA A1037 -2.880 -49.818 23.687 1.00 64.96 C
ANISOU 1888 CA ALA A1037 6799 7340 10545 801 -215 -854 C
ATOM 1889 C ALA A1037 -3.924 -49.276 24.634 1.00 72.10 C
ANISOU 1889 C ALA A1037 7495 8480 11419 805 -304 -872 C
ATOM 1890 O ALA A1037 -4.954 -48.836 24.229 1.00 71.89 O
ANISOU 1890 O ALA A1037 7475 8456 11382 721 -337 -788 O
ATOM 1891 CB ALA A1037 -2.926 -51.327 23.652 1.00 62.85 C
ANISOU 1891 CB ALA A1037 6746 7067 10067 750 -274 -702 C
ATOM 1892 N LEU A1038 -3.636 -49.326 25.912 1.00 79.62 N
ANISOU 1892 N LEU A1038 8267 9634 12351 915 -344 -983 N
ATOM 1893 CA LEU A1038 -4.542 -48.832 26.913 1.00 89.60 C
ANISOU 1893 CA LEU A1038 9330 11139 13575 954 -423 -1005 C
ATOM 1894 C LEU A1038 -4.724 -47.328 26.901 1.00 94.65 C
ANISOU 1894 C LEU A1038 9774 11789 14400 994 -403 -1144 C
ATOM 1895 O LEU A1038 -5.816 -46.832 27.111 1.00 99.42 O
ANISOU 1895 O LEU A1038 10291 12514 14968 959 -457 -1092 O
ATOM 1896 CB LEU A1038 -4.054 -49.263 28.256 1.00 97.72 C
ANISOU 1896 CB LEU A1038 10230 12367 14533 1095 -464 -1102 C
ATOM 1897 CG LEU A1038 -4.027 -50.761 28.374 1.00 97.40 C
ANISOU 1897 CG LEU A1038 10366 12346 14296 1053 -495 -949 C
ATOM 1898 CD1 LEU A1038 -4.289 -51.121 29.817 1.00108.83 C
ANISOU 1898 CD1 LEU A1038 11665 14069 15615 1172 -562 -967 C
ATOM 1899 CD2 LEU A1038 -5.084 -51.346 27.469 1.00 93.63 C
ANISOU 1899 CD2 LEU A1038 10083 11780 13711 879 -531 -708 C
ATOM 1900 N ASP A1039 -3.657 -46.605 26.629 1.00 94.46 N
ANISOU 1900 N ASP A1039 9676 11628 14585 1065 -325 -1313 N
ATOM 1901 CA ASP A1039 -3.675 -45.167 26.558 1.00 99.47 C
ANISOU 1901 CA ASP A1039 10120 12242 15430 1108 -302 -1455 C
ATOM 1902 C ASP A1039 -4.625 -44.768 25.489 1.00 94.95 C
ANISOU 1902 C ASP A1039 9653 11566 14859 967 -279 -1320 C
ATOM 1903 O ASP A1039 -5.482 -43.942 25.701 1.00 99.64 O
ANISOU 1903 O ASP A1039 10117 12263 15478 954 -322 -1337 O
ATOM 1904 CB ASP A1039 -2.328 -44.659 26.144 1.00100.93 C
ANISOU 1904 CB ASP A1039 10260 12232 15856 1179 -205 -1605 C
ATOM 1905 CG ASP A1039 -1.671 -43.870 27.194 1.00117.23 C
ANISOU 1905 CG ASP A1039 12057 14398 18087 1342 -245 -1840 C
ATOM 1906 OD1 ASP A1039 -2.366 -43.207 27.970 1.00125.96 O
ANISOU 1906 OD1 ASP A1039 12988 15690 19182 1397 -331 -1911 O
ATOM 1907 OD2 ASP A1039 -0.439 -43.900 27.236 1.00121.88 O
ANISOU 1907 OD2 ASP A1039 12611 14872 18827 1425 -195 -1957 O
ATOM 1908 N ALA A1040 -4.502 -45.387 24.327 1.00 86.82 N
ANISOU 1908 N ALA A1040 8871 10330 13787 867 -217 -1182 N
ATOM 1909 CA ALA A1040 -5.374 -45.119 23.192 1.00 83.05 C
ANISOU 1909 CA ALA A1040 8534 9725 13295 740 -199 -1045 C
ATOM 1910 C ALA A1040 -6.840 -45.530 23.390 1.00 85.78 C
ANISOU 1910 C ALA A1040 8927 10213 13451 637 -311 -882 C
ATOM 1911 O ALA A1040 -7.712 -45.020 22.722 1.00 85.16 O
ANISOU 1911 O ALA A1040 8889 10081 13387 548 -319 -808 O
ATOM 1912 CB ALA A1040 -4.816 -45.776 21.949 1.00 76.11 C
ANISOU 1912 CB ALA A1040 7927 8593 12399 691 -117 -942 C
ATOM 1913 N GLN A1041 -7.092 -46.457 24.301 1.00 89.76 N
ANISOU 1913 N GLN A1041 9424 10891 13791 653 -394 -820 N
ATOM 1914 CA GLN A1041 -8.412 -46.931 24.620 1.00 95.13 C
ANISOU 1914 CA GLN A1041 10123 11712 14309 571 -497 -651 C
ATOM 1915 C GLN A1041 -8.930 -46.237 25.871 1.00106.07 C
ANISOU 1915 C GLN A1041 11241 13364 15697 661 -549 -736 C
ATOM 1916 O GLN A1041 -9.822 -46.737 26.536 1.00113.60 O
ANISOU 1916 O GLN A1041 12161 14493 16510 646 -628 -612 O
ATOM 1917 CB GLN A1041 -8.314 -48.429 24.879 1.00 96.27 C
ANISOU 1917 CB GLN A1041 10418 11881 14278 549 -548 -517 C
ATOM 1918 CG GLN A1041 -9.572 -49.126 25.319 1.00106.45 C
ANISOU 1918 CG GLN A1041 11719 13315 15411 475 -656 -321 C
ATOM 1919 CD GLN A1041 -9.267 -50.282 26.216 1.00114.43 C
ANISOU 1919 CD GLN A1041 12736 14456 16287 532 -695 -268 C
ATOM 1920 OE1 GLN A1041 -9.861 -51.337 26.109 1.00118.64 O
ANISOU 1920 OE1 GLN A1041 13398 14982 16699 447 -766 -74 O
ATOM 1921 NE2 GLN A1041 -8.318 -50.095 27.095 1.00116.56 N
ANISOU 1921 NE2 GLN A1041 12866 14834 16587 679 -654 -442 N
ATOM 1922 N LYS A1042 -8.370 -45.092 26.219 1.00 56.72 N
ANISOU 1922 N LYS A1042 4796 7145 9610 769 -509 -944 N
ATOM 1923 CA LYS A1042 -8.833 -44.404 27.406 1.00 68.54 C
ANISOU 1923 CA LYS A1042 6048 8893 11103 878 -570 -1037 C
ATOM 1924 C LYS A1042 -9.917 -43.373 27.114 1.00 71.91 C
ANISOU 1924 C LYS A1042 6389 9354 11580 814 -591 -1011 C
ATOM 1925 O LYS A1042 -10.873 -43.232 27.886 1.00 82.31 O
ANISOU 1925 O LYS A1042 7591 10884 12800 841 -660 -956 O
ATOM 1926 CB LYS A1042 -7.666 -43.758 28.147 1.00 73.32 C
ANISOU 1926 CB LYS A1042 6466 9539 11854 1056 -550 -1292 C
ATOM 1927 CG LYS A1042 -7.183 -44.578 29.326 1.00 80.35 C
ANISOU 1927 CG LYS A1042 7308 10598 12621 1189 -595 -1331 C
ATOM 1928 CD LYS A1042 -5.971 -43.955 30.005 1.00 86.45 C
ANISOU 1928 CD LYS A1042 7908 11384 13556 1370 -591 -1596 C
ATOM 1929 CE LYS A1042 -6.110 -44.006 31.523 1.00101.93 C
ANISOU 1929 CE LYS A1042 9700 13625 15405 1556 -680 -1681 C
ATOM 1930 NZ LYS A1042 -4.901 -43.549 32.251 1.00109.99 N
ANISOU 1930 NZ LYS A1042 10567 14653 16572 1747 -701 -1942 N
ATOM 1931 N ARG A1062 -14.116 -51.001 20.823 1.00102.49 N
ANISOU 1931 N ARG A1062 12091 12121 14731 -183 -1036 535 N
ATOM 1932 CA ARG A1062 -14.116 -51.592 22.156 1.00108.36 C
ANISOU 1932 CA ARG A1062 12669 13099 15406 -132 -1062 573 C
ATOM 1933 C ARG A1062 -13.698 -53.048 22.002 1.00107.48 C
ANISOU 1933 C ARG A1062 12751 12891 15196 -152 -1125 681 C
ATOM 1934 O ARG A1062 -12.754 -53.493 22.629 1.00104.45 O
ANISOU 1934 O ARG A1062 12333 12584 14768 -64 -1073 606 O
ATOM 1935 CB ARG A1062 -15.491 -51.468 22.807 1.00 76.82 C
ANISOU 1935 CB ARG A1062 8512 9276 11401 -188 -1146 715 C
ATOM 1936 CG ARG A1062 -16.025 -50.048 22.967 1.00 78.92 C
ANISOU 1936 CG ARG A1062 8589 9644 11752 -173 -1098 621 C
ATOM 1937 CD ARG A1062 -16.623 -49.865 24.359 1.00 91.22 C
ANISOU 1937 CD ARG A1062 9883 11501 13275 -107 -1111 659 C
ATOM 1938 NE ARG A1062 -17.764 -48.948 24.413 1.00 99.93 N
ANISOU 1938 NE ARG A1062 10853 12689 14428 -152 -1135 702 N
ATOM 1939 CZ ARG A1062 -18.591 -48.839 25.451 1.00114.46 C
ANISOU 1939 CZ ARG A1062 12491 14766 16231 -113 -1162 795 C
ATOM 1940 NH1 ARG A1062 -18.414 -49.593 26.521 1.00122.11 N
ANISOU 1940 NH1 ARG A1062 13371 15914 17113 -22 -1166 857 N
ATOM 1941 NH2 ARG A1062 -19.600 -47.979 25.420 1.00122.53 N
ANISOU 1941 NH2 ARG A1062 13405 15851 17300 -155 -1180 831 N
ATOM 1942 N HIS A1063 -14.381 -53.775 21.130 1.00110.54 N
ANISOU 1942 N HIS A1063 13348 13099 15553 -264 -1244 850 N
ATOM 1943 CA HIS A1063 -14.029 -55.151 20.862 1.00110.68 C
ANISOU 1943 CA HIS A1063 13570 13000 15485 -286 -1324 955 C
ATOM 1944 C HIS A1063 -12.585 -55.214 20.376 1.00 97.60 C
ANISOU 1944 C HIS A1063 12055 11217 13813 -199 -1216 803 C
ATOM 1945 O HIS A1063 -11.797 -56.013 20.842 1.00 95.78 O
ANISOU 1945 O HIS A1063 11850 11027 13515 -146 -1200 789 O
ATOM 1946 CB HIS A1063 -14.918 -55.741 19.763 1.00 75.76 C
ANISOU 1946 CB HIS A1063 9378 8349 11057 -407 -1480 1126 C
ATOM 1947 CG HIS A1063 -16.386 -55.745 20.078 1.00 89.62 C
ANISOU 1947 CG HIS A1063 11017 10184 12853 -506 -1600 1299 C
ATOM 1948 ND1 HIS A1063 -16.947 -56.549 21.047 1.00100.91 N
ANISOU 1948 ND1 HIS A1063 12317 11770 14255 -530 -1678 1458 N
ATOM 1949 CD2 HIS A1063 -17.399 -54.991 19.588 1.00 95.18 C
ANISOU 1949 CD2 HIS A1063 11697 10838 13630 -579 -1645 1339 C
ATOM 1950 CE1 HIS A1063 -18.247 -56.323 21.106 1.00113.66 C
ANISOU 1950 CE1 HIS A1063 13837 13416 15933 -617 -1767 1601 C
ATOM 1951 NE2 HIS A1063 -18.547 -55.379 20.234 1.00110.13 N
ANISOU 1951 NE2 HIS A1063 13453 12847 15544 -651 -1753 1527 N
ATOM 1952 N GLY A1064 -12.257 -54.382 19.403 1.00 89.36 N
ANISOU 1952 N GLY A1064 11106 10012 12834 -183 -1139 702 N
ATOM 1953 CA GLY A1064 -10.935 -54.341 18.826 1.00 78.98 C
ANISOU 1953 CA GLY A1064 9926 8557 11527 -95 -1022 576 C
ATOM 1954 C GLY A1064 -9.813 -54.109 19.797 1.00 71.55 C
ANISOU 1954 C GLY A1064 8802 7771 10612 18 -898 416 C
ATOM 1955 O GLY A1064 -8.761 -54.655 19.634 1.00 67.04 O
ANISOU 1955 O GLY A1064 8345 7120 10007 79 -845 370 O
ATOM 1956 N PHE A1065 -10.035 -53.294 20.803 1.00 71.76 N
ANISOU 1956 N PHE A1065 8548 8016 10700 54 -858 330 N
ATOM 1957 CA PHE A1065 -9.003 -53.006 21.770 1.00 68.32 C
ANISOU 1957 CA PHE A1065 7928 7727 10302 177 -760 161 C
ATOM 1958 C PHE A1065 -8.890 -54.108 22.802 1.00 71.91 C
ANISOU 1958 C PHE A1065 8343 8342 10640 202 -820 224 C
ATOM 1959 O PHE A1065 -7.835 -54.328 23.346 1.00 69.17 O
ANISOU 1959 O PHE A1065 7950 8046 10287 299 -756 111 O
ATOM 1960 CB PHE A1065 -9.219 -51.653 22.429 1.00 70.01 C
ANISOU 1960 CB PHE A1065 7866 8103 10631 231 -704 24 C
ATOM 1961 CG PHE A1065 -8.432 -50.544 21.800 1.00 64.70 C
ANISOU 1961 CG PHE A1065 7168 7300 10114 288 -577 -141 C
ATOM 1962 CD1 PHE A1065 -7.094 -50.449 21.993 1.00 61.55 C
ANISOU 1962 CD1 PHE A1065 6732 6869 9786 396 -477 -291 C
ATOM 1963 CD2 PHE A1065 -9.048 -49.608 21.013 1.00 64.99 C
ANISOU 1963 CD2 PHE A1065 7214 7244 10237 234 -558 -137 C
ATOM 1964 CE1 PHE A1065 -6.382 -49.441 21.420 1.00 58.96 C
ANISOU 1964 CE1 PHE A1065 6364 6413 9627 451 -359 -425 C
ATOM 1965 CE2 PHE A1065 -8.343 -48.590 20.434 1.00 61.34 C
ANISOU 1965 CE2 PHE A1065 6718 6659 9930 290 -436 -274 C
ATOM 1966 CZ PHE A1065 -7.008 -48.511 20.635 1.00 58.23 C
ANISOU 1966 CZ PHE A1065 6276 6228 9620 398 -334 -412 C
ATOM 1967 N ASP A1066 -9.993 -54.806 23.039 1.00 78.76 N
ANISOU 1967 N ASP A1066 9227 9276 11424 116 -944 413 N
ATOM 1968 CA ASP A1066 -10.051 -55.920 23.963 1.00 84.06 C
ANISOU 1968 CA ASP A1066 9863 10091 11984 130 -1008 512 C
ATOM 1969 C ASP A1066 -9.209 -57.008 23.345 1.00 76.94 C
ANISOU 1969 C ASP A1066 9209 9012 11012 121 -1021 542 C
ATOM 1970 O ASP A1066 -8.429 -57.635 24.019 1.00 76.41 O
ANISOU 1970 O ASP A1066 9119 9028 10884 193 -994 497 O
ATOM 1971 CB ASP A1066 -11.493 -56.431 24.116 1.00 98.47 C
ANISOU 1971 CB ASP A1066 11672 11974 13769 24 -1141 742 C
ATOM 1972 CG ASP A1066 -12.301 -55.693 25.196 1.00114.53 C
ANISOU 1972 CG ASP A1066 13423 14266 15827 66 -1132 747 C
ATOM 1973 OD1 ASP A1066 -11.715 -54.978 26.049 1.00114.41 O
ANISOU 1973 OD1 ASP A1066 13218 14421 15833 195 -1040 574 O
ATOM 1974 OD2 ASP A1066 -13.544 -55.850 25.193 1.00127.35 O
ANISOU 1974 OD2 ASP A1066 15017 15919 17453 -24 -1224 930 O
ATOM 1975 N ILE A1067 -9.381 -57.204 22.049 1.00 72.32 N
ANISOU 1975 N ILE A1067 8866 8181 10431 43 -1065 613 N
ATOM 1976 CA ILE A1067 -8.654 -58.186 21.300 1.00 67.37 C
ANISOU 1976 CA ILE A1067 8504 7362 9731 40 -1087 648 C
ATOM 1977 C ILE A1067 -7.168 -57.850 21.284 1.00 57.85 C
ANISOU 1977 C ILE A1067 7302 6121 8559 157 -934 458 C
ATOM 1978 O ILE A1067 -6.345 -58.695 21.515 1.00 56.28 O
ANISOU 1978 O ILE A1067 7181 5916 8288 201 -923 445 O
ATOM 1979 CB ILE A1067 -9.113 -58.250 19.855 1.00 68.25 C
ANISOU 1979 CB ILE A1067 8875 7211 9846 -34 -1157 737 C
ATOM 1980 CG1 ILE A1067 -10.451 -58.932 19.731 1.00 80.14 C
ANISOU 1980 CG1 ILE A1067 10439 8694 11318 -154 -1343 945 C
ATOM 1981 CG2 ILE A1067 -8.138 -59.051 19.051 1.00 65.39 C
ANISOU 1981 CG2 ILE A1067 8785 6650 9411 7 -1147 731 C
ATOM 1982 CD1 ILE A1067 -11.275 -58.489 18.554 1.00 84.69 C
ANISOU 1982 CD1 ILE A1067 11164 9075 11939 -224 -1415 1007 C
ATOM 1983 N LEU A1068 -6.844 -56.594 21.033 1.00 52.05 N
ANISOU 1983 N LEU A1068 6467 5361 7948 208 -817 314 N
ATOM 1984 CA LEU A1068 -5.473 -56.169 20.955 1.00 45.01 C
ANISOU 1984 CA LEU A1068 5558 4413 7129 317 -670 143 C
ATOM 1985 C LEU A1068 -4.699 -56.400 22.220 1.00 43.56 C
ANISOU 1985 C LEU A1068 5196 4420 6934 408 -631 32 C
ATOM 1986 O LEU A1068 -3.626 -56.922 22.183 1.00 40.72 O
ANISOU 1986 O LEU A1068 4922 3997 6552 469 -576 -23 O
ATOM 1987 CB LEU A1068 -5.376 -54.711 20.557 1.00 42.35 C
ANISOU 1987 CB LEU A1068 5105 4028 6957 352 -560 18 C
ATOM 1988 CG LEU A1068 -3.968 -54.352 20.131 1.00 39.58 C
ANISOU 1988 CG LEU A1068 4789 3543 6705 456 -409 -118 C
ATOM 1989 CD1 LEU A1068 -3.676 -54.876 18.752 1.00 39.25 C
ANISOU 1989 CD1 LEU A1068 5065 3239 6610 444 -391 -23 C
ATOM 1990 CD2 LEU A1068 -3.757 -52.867 20.178 1.00 39.34 C
ANISOU 1990 CD2 LEU A1068 4548 3527 6871 511 -300 -270 C
ATOM 1991 N VAL A1069 -5.251 -55.990 23.339 1.00 47.08 N
ANISOU 1991 N VAL A1069 5396 5100 7394 429 -659 -1 N
ATOM 1992 CA VAL A1069 -4.579 -56.140 24.601 1.00 49.24 C
ANISOU 1992 CA VAL A1069 5492 5567 7651 539 -630 -116 C
ATOM 1993 C VAL A1069 -4.472 -57.597 24.951 1.00 51.44 C
ANISOU 1993 C VAL A1069 5892 5881 7771 520 -701 3 C
ATOM 1994 O VAL A1069 -3.458 -58.043 25.411 1.00 50.83 O
ANISOU 1994 O VAL A1069 5814 5833 7668 601 -657 -87 O
ATOM 1995 CB VAL A1069 -5.256 -55.328 25.703 1.00 56.60 C
ANISOU 1995 CB VAL A1069 6141 6744 8620 590 -648 -175 C
ATOM 1996 CG1 VAL A1069 -4.635 -55.615 27.037 1.00 61.78 C
ANISOU 1996 CG1 VAL A1069 6638 7606 9231 720 -638 -280 C
ATOM 1997 CG2 VAL A1069 -5.136 -53.857 25.401 1.00 55.49 C
ANISOU 1997 CG2 VAL A1069 5869 6561 8653 626 -572 -326 C
ATOM 1998 N GLY A1070 -5.519 -58.348 24.682 1.00 54.63 N
ANISOU 1998 N GLY A1070 6407 6268 8082 408 -818 209 N
ATOM 1999 CA GLY A1070 -5.525 -59.769 24.917 1.00 57.45 C
ANISOU 1999 CA GLY A1070 6888 6638 8302 376 -901 346 C
ATOM 2000 C GLY A1070 -4.437 -60.458 24.145 1.00 50.79 C
ANISOU 2000 C GLY A1070 6283 5596 7419 388 -869 317 C
ATOM 2001 O GLY A1070 -3.759 -61.296 24.653 1.00 51.38 O
ANISOU 2001 O GLY A1070 6387 5721 7413 433 -866 305 O
ATOM 2002 N GLN A1071 -4.266 -60.076 22.908 1.00 45.32 N
ANISOU 2002 N GLN A1071 5761 4679 6779 358 -837 308 N
ATOM 2003 CA GLN A1071 -3.251 -60.666 22.090 1.00 41.52 C
ANISOU 2003 CA GLN A1071 5517 4000 6258 386 -797 291 C
ATOM 2004 C GLN A1071 -1.844 -60.360 22.536 1.00 37.85 C
ANISOU 2004 C GLN A1071 4963 3567 5851 509 -655 102 C
ATOM 2005 O GLN A1071 -0.970 -61.155 22.351 1.00 36.91 O
ANISOU 2005 O GLN A1071 4992 3367 5665 543 -635 97 O
ATOM 2006 CB GLN A1071 -3.432 -60.226 20.657 1.00 41.17 C
ANISOU 2006 CB GLN A1071 5672 3714 6258 352 -784 328 C
ATOM 2007 CG GLN A1071 -4.590 -60.913 19.981 1.00 49.53 C
ANISOU 2007 CG GLN A1071 6915 4669 7234 238 -952 526 C
ATOM 2008 CD GLN A1071 -4.834 -60.373 18.620 1.00 52.49 C
ANISOU 2008 CD GLN A1071 7474 4817 7650 224 -942 549 C
ATOM 2009 OE1 GLN A1071 -4.818 -59.182 18.423 1.00 50.77 O
ANISOU 2009 OE1 GLN A1071 7144 4596 7551 253 -838 453 O
ATOM 2010 NE2 GLN A1071 -5.039 -61.245 17.672 1.00 55.67 N
ANISOU 2010 NE2 GLN A1071 8167 5029 7958 191 -1054 673 N
ATOM 2011 N ILE A1072 -1.641 -59.178 23.098 1.00 36.50 N
ANISOU 2011 N ILE A1072 4548 3504 5818 577 -566 -55 N
ATOM 2012 CA ILE A1072 -0.357 -58.754 23.589 1.00 35.31 C
ANISOU 2012 CA ILE A1072 4274 3380 5763 699 -446 -248 C
ATOM 2013 C ILE A1072 -0.050 -59.575 24.815 1.00 38.54 C
ANISOU 2013 C ILE A1072 4593 3981 6068 750 -487 -273 C
ATOM 2014 O ILE A1072 1.051 -59.994 25.004 1.00 37.75 O
ANISOU 2014 O ILE A1072 4530 3853 5962 821 -432 -358 O
ATOM 2015 CB ILE A1072 -0.342 -57.256 23.911 1.00 36.21 C
ANISOU 2015 CB ILE A1072 4135 3558 6063 760 -370 -407 C
ATOM 2016 CG1 ILE A1072 -0.150 -56.475 22.638 1.00 34.18 C
ANISOU 2016 CG1 ILE A1072 3980 3073 5932 746 -281 -415 C
ATOM 2017 CG2 ILE A1072 0.764 -56.922 24.887 1.00 38.85 C
ANISOU 2017 CG2 ILE A1072 4274 3995 6491 895 -300 -609 C
ATOM 2018 CD1 ILE A1072 -0.569 -55.051 22.734 1.00 35.76 C
ANISOU 2018 CD1 ILE A1072 3968 3320 6301 762 -241 -512 C
ATOM 2019 N ASP A1073 -1.064 -59.803 25.633 1.00 43.32 N
ANISOU 2019 N ASP A1073 5083 4781 6595 717 -582 -189 N
ATOM 2020 CA ASP A1073 -0.947 -60.617 26.829 1.00 48.84 C
ANISOU 2020 CA ASP A1073 5696 5680 7180 771 -625 -183 C
ATOM 2021 C ASP A1073 -0.576 -62.059 26.471 1.00 47.59 C
ANISOU 2021 C ASP A1073 5776 5424 6880 723 -673 -63 C
ATOM 2022 O ASP A1073 0.174 -62.689 27.168 1.00 49.56 O
ANISOU 2022 O ASP A1073 6009 5757 7066 794 -656 -122 O
ATOM 2023 CB ASP A1073 -2.250 -60.625 27.609 1.00 58.29 C
ANISOU 2023 CB ASP A1073 6746 7083 8320 741 -713 -65 C
ATOM 2024 CG ASP A1073 -2.479 -59.362 28.389 1.00 68.62 C
ANISOU 2024 CG ASP A1073 7783 8560 9731 834 -674 -207 C
ATOM 2025 OD1 ASP A1073 -1.560 -58.563 28.574 1.00 67.48 O
ANISOU 2025 OD1 ASP A1073 7534 8404 9702 938 -592 -415 O
ATOM 2026 OD2 ASP A1073 -3.612 -59.186 28.826 1.00 78.50 O
ANISOU 2026 OD2 ASP A1073 8923 9951 10951 807 -733 -103 O
ATOM 2027 N ASP A1074 -1.140 -62.579 25.391 1.00 45.33 N
ANISOU 2027 N ASP A1074 5716 4963 6545 607 -744 103 N
ATOM 2028 CA ASP A1074 -0.846 -63.913 24.923 1.00 45.12 C
ANISOU 2028 CA ASP A1074 5935 4819 6389 561 -808 221 C
ATOM 2029 C ASP A1074 0.628 -63.988 24.620 1.00 41.24 C
ANISOU 2029 C ASP A1074 5540 4214 5917 646 -697 81 C
ATOM 2030 O ASP A1074 1.290 -64.903 25.024 1.00 42.14 O
ANISOU 2030 O ASP A1074 5714 4360 5937 678 -703 76 O
ATOM 2031 CB ASP A1074 -1.577 -64.205 23.619 1.00 45.83 C
ANISOU 2031 CB ASP A1074 6264 4694 6455 449 -900 383 C
ATOM 2032 CG ASP A1074 -2.992 -64.585 23.813 1.00 55.80 C
ANISOU 2032 CG ASP A1074 7494 6027 7680 346 -1045 568 C
ATOM 2033 OD1 ASP A1074 -3.472 -64.568 24.938 1.00 62.16 O
ANISOU 2033 OD1 ASP A1074 8085 7055 8478 361 -1061 587 O
ATOM 2034 OD2 ASP A1074 -3.640 -64.887 22.824 1.00 58.93 O
ANISOU 2034 OD2 ASP A1074 8080 6250 8061 257 -1145 700 O
ATOM 2035 N ALA A1075 1.113 -63.008 23.868 1.00 37.85 N
ANISOU 2035 N ALA A1075 5123 3641 5616 682 -592 -20 N
ATOM 2036 CA ALA A1075 2.499 -62.939 23.442 1.00 36.53 C
ANISOU 2036 CA ALA A1075 5041 3337 5503 767 -469 -138 C
ATOM 2037 C ALA A1075 3.441 -62.739 24.591 1.00 38.59 C
ANISOU 2037 C ALA A1075 5093 3749 5821 878 -396 -318 C
ATOM 2038 O ALA A1075 4.496 -63.290 24.612 1.00 38.87 O
ANISOU 2038 O ALA A1075 5210 3730 5828 933 -345 -372 O
ATOM 2039 CB ALA A1075 2.710 -61.863 22.398 1.00 33.99 C
ANISOU 2039 CB ALA A1075 4754 2831 5330 787 -365 -185 C
ATOM 2040 N LEU A1076 3.035 -61.949 25.549 1.00 41.23 N
ANISOU 2040 N LEU A1076 5162 4271 6232 917 -399 -411 N
ATOM 2041 CA LEU A1076 3.856 -61.683 26.706 1.00 46.22 C
ANISOU 2041 CA LEU A1076 5585 5054 6923 1042 -350 -598 C
ATOM 2042 C LEU A1076 4.055 -62.916 27.558 1.00 49.65 C
ANISOU 2042 C LEU A1076 6054 5625 7186 1063 -410 -560 C
ATOM 2043 O LEU A1076 5.110 -63.141 28.071 1.00 52.03 O
ANISOU 2043 O LEU A1076 6319 5950 7499 1156 -361 -688 O
ATOM 2044 CB LEU A1076 3.235 -60.567 27.533 1.00 50.69 C
ANISOU 2044 CB LEU A1076 5871 5797 7590 1093 -362 -696 C
ATOM 2045 CG LEU A1076 3.922 -59.245 27.304 1.00 53.44 C
ANISOU 2045 CG LEU A1076 6079 6055 8171 1169 -261 -879 C
ATOM 2046 CD1 LEU A1076 3.005 -58.116 27.684 1.00 57.09 C
ANISOU 2046 CD1 LEU A1076 6330 6637 8723 1177 -290 -922 C
ATOM 2047 CD2 LEU A1076 5.160 -59.240 28.144 1.00 58.98 C
ANISOU 2047 CD2 LEU A1076 6659 6809 8943 1307 -215 -1073 C
ATOM 2048 N LYS A1077 3.016 -63.708 27.712 1.00 50.85 N
ANISOU 2048 N LYS A1077 6269 5863 7190 977 -519 -378 N
ATOM 2049 CA LYS A1077 3.114 -64.900 28.503 1.00 55.09 C
ANISOU 2049 CA LYS A1077 6834 6529 7567 993 -576 -318 C
ATOM 2050 C LYS A1077 4.077 -65.862 27.857 1.00 53.30 C
ANISOU 2050 C LYS A1077 6847 6135 7268 977 -557 -297 C
ATOM 2051 O LYS A1077 4.838 -66.501 28.537 1.00 55.96 O
ANISOU 2051 O LYS A1077 7175 6549 7537 1045 -541 -363 O
ATOM 2052 CB LYS A1077 1.772 -65.564 28.628 1.00 59.75 C
ANISOU 2052 CB LYS A1077 7453 7205 8043 892 -697 -96 C
ATOM 2053 CG LYS A1077 1.848 -66.883 29.340 1.00 67.67 C
ANISOU 2053 CG LYS A1077 8502 8321 8888 899 -756 -5 C
ATOM 2054 CD LYS A1077 0.489 -67.314 29.827 1.00 79.07 C
ANISOU 2054 CD LYS A1077 9873 9908 10263 836 -859 196 C
ATOM 2055 CE LYS A1077 0.568 -68.647 30.530 1.00 88.63 C
ANISOU 2055 CE LYS A1077 11122 11225 11328 847 -911 301 C
ATOM 2056 NZ LYS A1077 0.908 -69.713 29.558 1.00 87.79 N
ANISOU 2056 NZ LYS A1077 11295 10908 11152 748 -971 404 N
ATOM 2057 N LEU A1078 4.010 -65.975 26.538 1.00 49.28 N
ANISOU 2057 N LEU A1078 6561 5398 6764 895 -561 -201 N
ATOM 2058 CA LEU A1078 4.913 -66.850 25.802 1.00 48.30 C
ANISOU 2058 CA LEU A1078 6688 5099 6565 891 -542 -172 C
ATOM 2059 C LEU A1078 6.346 -66.373 25.964 1.00 49.21 C
ANISOU 2059 C LEU A1078 6739 5171 6790 1010 -402 -372 C
ATOM 2060 O LEU A1078 7.231 -67.194 26.215 1.00 50.88 O
ANISOU 2060 O LEU A1078 7032 5378 6923 1051 -385 -405 O
ATOM 2061 CB LEU A1078 4.527 -66.901 24.319 1.00 46.33 C
ANISOU 2061 CB LEU A1078 6688 4610 6305 811 -571 -40 C
ATOM 2062 CG LEU A1078 3.253 -67.663 24.020 1.00 49.78 C
ANISOU 2062 CG LEU A1078 7248 5040 6628 691 -737 171 C
ATOM 2063 CD1 LEU A1078 2.810 -67.440 22.575 1.00 50.13 C
ANISOU 2063 CD1 LEU A1078 7511 4849 6689 635 -769 270 C
ATOM 2064 CD2 LEU A1078 3.426 -69.148 24.325 1.00 53.33 C
ANISOU 2064 CD2 LEU A1078 7834 5517 6911 664 -832 270 C
ATOM 2065 N ALA A1079 6.568 -65.043 25.871 1.00 48.88 N
ANISOU 2065 N ALA A1079 6533 5098 6942 1066 -307 -505 N
ATOM 2066 CA ALA A1079 7.882 -64.430 26.041 1.00 52.49 C
ANISOU 2066 CA ALA A1079 6887 5500 7557 1181 -179 -698 C
ATOM 2067 C ALA A1079 8.427 -64.572 27.479 1.00 58.62 C
ANISOU 2067 C ALA A1079 7462 6480 8329 1282 -188 -854 C
ATOM 2068 O ALA A1079 9.637 -64.652 27.652 1.00 62.46 O
ANISOU 2068 O ALA A1079 7938 6913 8881 1367 -114 -980 O
ATOM 2069 CB ALA A1079 7.849 -62.968 25.626 1.00 52.34 C
ANISOU 2069 CB ALA A1079 6724 5401 7764 1211 -96 -788 C
ATOM 2070 N ASN A1080 7.566 -64.674 28.486 1.00 60.89 N
ANISOU 2070 N ASN A1080 7608 6995 8533 1283 -277 -836 N
ATOM 2071 CA ASN A1080 7.997 -64.852 29.867 1.00 67.85 C
ANISOU 2071 CA ASN A1080 8315 8081 9384 1399 -292 -974 C
ATOM 2072 C ASN A1080 8.430 -66.307 30.134 1.00 69.27 C
ANISOU 2072 C ASN A1080 8656 8292 9371 1388 -327 -903 C
ATOM 2073 O ASN A1080 9.170 -66.582 31.056 1.00 75.10 O
ANISOU 2073 O ASN A1080 9308 9138 10088 1494 -314 -1032 O
ATOM 2074 CB ASN A1080 6.891 -64.445 30.818 1.00 73.03 C
ANISOU 2074 CB ASN A1080 8771 8970 10006 1423 -365 -961 C
ATOM 2075 CG ASN A1080 6.800 -62.953 30.998 1.00 79.33 C
ANISOU 2075 CG ASN A1080 9347 9789 11006 1494 -330 -1115 C
ATOM 2076 OD1 ASN A1080 7.764 -62.253 30.859 1.00 82.20 O
ANISOU 2076 OD1 ASN A1080 9641 10046 11546 1568 -257 -1284 O
ATOM 2077 ND2 ASN A1080 5.618 -62.469 31.295 1.00 81.69 N
ANISOU 2077 ND2 ASN A1080 9532 10220 11288 1470 -386 -1047 N
ATOM 2078 N GLU A1081 7.906 -67.230 29.350 1.00 64.69 N
ANISOU 2078 N GLU A1081 8307 7621 8653 1264 -383 -697 N
ATOM 2079 CA GLU A1081 8.297 -68.640 29.401 1.00 65.33 C
ANISOU 2079 CA GLU A1081 8571 7696 8556 1238 -423 -610 C
ATOM 2080 C GLU A1081 9.595 -68.934 28.590 1.00 64.20 C
ANISOU 2080 C GLU A1081 8612 7340 8442 1259 -339 -666 C
ATOM 2081 O GLU A1081 10.026 -70.087 28.535 1.00 65.65 O
ANISOU 2081 O GLU A1081 8966 7498 8481 1240 -367 -604 O
ATOM 2082 CB GLU A1081 7.160 -69.524 28.869 1.00 65.44 C
ANISOU 2082 CB GLU A1081 8756 7684 8425 1099 -542 -361 C
ATOM 2083 CG GLU A1081 5.908 -69.501 29.724 1.00 74.48 C
ANISOU 2083 CG GLU A1081 9733 9041 9523 1078 -625 -267 C
ATOM 2084 CD GLU A1081 4.667 -70.061 29.048 1.00 81.99 C
ANISOU 2084 CD GLU A1081 10820 9929 10403 934 -744 -22 C
ATOM 2085 OE1 GLU A1081 4.694 -70.257 27.811 1.00 79.20 O
ANISOU 2085 OE1 GLU A1081 10691 9353 10049 854 -767 57 O
ATOM 2086 OE2 GLU A1081 3.659 -70.287 29.756 1.00 89.76 O
ANISOU 2086 OE2 GLU A1081 11684 11081 11339 911 -817 93 O
ATOM 2087 N GLY A1082 10.176 -67.917 27.954 1.00 62.73 N
ANISOU 2087 N GLY A1082 8391 7002 8441 1299 -235 -769 N
ATOM 2088 CA GLY A1082 11.390 -68.051 27.158 1.00 63.74 C
ANISOU 2088 CA GLY A1082 8671 6923 8625 1335 -134 -810 C
ATOM 2089 C GLY A1082 11.173 -68.484 25.718 1.00 60.68 C
ANISOU 2089 C GLY A1082 8575 6319 8162 1253 -138 -632 C
ATOM 2090 O GLY A1082 12.132 -68.542 24.946 1.00 64.43 O
ANISOU 2090 O GLY A1082 9190 6611 8680 1296 -42 -645 O
ATOM 2091 N LYS A1083 9.923 -68.782 25.333 1.00 55.62 N
ANISOU 2091 N LYS A1083 8030 5691 7414 1148 -251 -464 N
ATOM 2092 CA LYS A1083 9.595 -69.236 23.987 1.00 54.16 C
ANISOU 2092 CA LYS A1083 8134 5302 7144 1081 -289 -295 C
ATOM 2093 C LYS A1083 9.561 -68.060 22.999 1.00 53.31 C
ANISOU 2093 C LYS A1083 8028 5028 7200 1101 -192 -309 C
ATOM 2094 O LYS A1083 8.504 -67.477 22.767 1.00 51.07 O
ANISOU 2094 O LYS A1083 7692 4758 6954 1041 -243 -250 O
ATOM 2095 CB LYS A1083 8.251 -69.980 24.000 1.00 54.02 C
ANISOU 2095 CB LYS A1083 8198 5351 6976 965 -465 -116 C
ATOM 2096 CG LYS A1083 8.165 -71.056 25.076 1.00 57.84 C
ANISOU 2096 CG LYS A1083 8638 6019 7318 948 -555 -89 C
ATOM 2097 CD LYS A1083 6.748 -71.566 25.270 1.00 61.11 C
ANISOU 2097 CD LYS A1083 9051 6522 7645 840 -716 86 C
ATOM 2098 CE LYS A1083 6.687 -72.614 26.353 1.00 65.55 C
ANISOU 2098 CE LYS A1083 9556 7268 8081 835 -788 125 C
ATOM 2099 NZ LYS A1083 5.362 -73.286 26.399 1.00 69.84 N
ANISOU 2099 NZ LYS A1083 10129 7858 8550 726 -950 332 N
ATOM 2100 N VAL A1084 10.707 -67.739 22.394 1.00 56.06 N
ANISOU 2100 N VAL A1084 8440 5214 7646 1188 -49 -375 N
ATOM 2101 CA VAL A1084 10.826 -66.607 21.475 1.00 57.53 C
ANISOU 2101 CA VAL A1084 8614 5236 8007 1228 70 -388 C
ATOM 2102 C VAL A1084 10.000 -66.766 20.183 1.00 56.88 C
ANISOU 2102 C VAL A1084 8790 4993 7828 1174 13 -211 C
ATOM 2103 O VAL A1084 9.186 -65.892 19.883 1.00 54.56 O
ANISOU 2103 O VAL A1084 8417 4689 7624 1139 7 -193 O
ATOM 2104 CB VAL A1084 12.291 -66.237 21.137 1.00 65.57 C
ANISOU 2104 CB VAL A1084 9628 6110 9176 1347 251 -482 C
ATOM 2105 CG1 VAL A1084 12.371 -64.816 20.591 1.00 68.19 C
ANISOU 2105 CG1 VAL A1084 9825 6330 9754 1396 382 -531 C
ATOM 2106 CG2 VAL A1084 13.221 -66.413 22.339 1.00 68.93 C
ANISOU 2106 CG2 VAL A1084 9865 6666 9658 1406 280 -645 C
ATOM 2107 N LYS A1085 10.214 -67.854 19.417 1.00 59.71 N
ANISOU 2107 N LYS A1085 9458 5222 8006 1175 -36 -88 N
ATOM 2108 CA LYS A1085 9.522 -68.081 18.147 1.00 62.21 C
ANISOU 2108 CA LYS A1085 10050 5366 8220 1151 -106 70 C
ATOM 2109 C LYS A1085 8.012 -68.111 18.280 1.00 57.00 C
ANISOU 2109 C LYS A1085 9361 4790 7505 1030 -281 158 C
ATOM 2110 O LYS A1085 7.317 -67.617 17.393 1.00 58.12 O
ANISOU 2110 O LYS A1085 9598 4815 7669 1016 -302 232 O
ATOM 2111 CB LYS A1085 10.011 -69.376 17.483 1.00 70.70 C
ANISOU 2111 CB LYS A1085 11457 6313 9092 1183 -163 174 C
ATOM 2112 CG LYS A1085 11.498 -69.363 17.183 1.00 80.74 C
ANISOU 2112 CG LYS A1085 12790 7475 10412 1312 19 114 C
ATOM 2113 CD LYS A1085 11.844 -68.481 16.010 1.00 90.90 C
ANISOU 2113 CD LYS A1085 14168 8559 11813 1415 177 144 C
ATOM 2114 CE LYS A1085 13.339 -68.348 15.906 1.00102.53 C
ANISOU 2114 CE LYS A1085 15629 9944 13383 1543 376 80 C
ATOM 2115 NZ LYS A1085 13.766 -68.055 14.517 1.00117.36 N
ANISOU 2115 NZ LYS A1085 17733 11586 15272 1670 508 180 N
ATOM 2116 N GLU A1086 7.505 -68.697 19.366 1.00 52.74 N
ANISOU 2116 N GLU A1086 8694 4448 6897 951 -402 159 N
ATOM 2117 CA GLU A1086 6.071 -68.772 19.571 1.00 51.47 C
ANISOU 2117 CA GLU A1086 8485 4373 6699 838 -565 258 C
ATOM 2118 C GLU A1086 5.509 -67.377 19.873 1.00 47.59 C
ANISOU 2118 C GLU A1086 7731 3964 6385 827 -499 180 C
ATOM 2119 O GLU A1086 4.479 -67.011 19.320 1.00 47.77 O
ANISOU 2119 O GLU A1086 7794 3935 6424 766 -573 266 O
ATOM 2120 CB GLU A1086 5.725 -69.780 20.662 1.00 53.62 C
ANISOU 2120 CB GLU A1086 8681 4831 6859 773 -693 297 C
ATOM 2121 CG GLU A1086 4.438 -70.517 20.364 1.00 64.25 C
ANISOU 2121 CG GLU A1086 10154 6154 8104 661 -901 480 C
ATOM 2122 CD GLU A1086 3.994 -71.438 21.477 1.00 74.30 C
ANISOU 2122 CD GLU A1086 11318 7616 9294 598 -1018 541 C
ATOM 2123 OE1 GLU A1086 4.870 -71.928 22.227 1.00 75.98 O
ANISOU 2123 OE1 GLU A1086 11478 7931 9459 649 -961 462 O
ATOM 2124 OE2 GLU A1086 2.769 -71.676 21.601 1.00 79.12 O
ANISOU 2124 OE2 GLU A1086 11895 8272 9895 503 -1164 673 O
ATOM 2125 N ALA A1087 6.218 -66.581 20.693 1.00 45.08 N
ANISOU 2125 N ALA A1087 7156 3762 6211 894 -365 12 N
ATOM 2126 CA ALA A1087 5.796 -65.212 21.025 1.00 42.88 C
ANISOU 2126 CA ALA A1087 6617 3563 6112 900 -302 -82 C
ATOM 2127 C ALA A1087 5.808 -64.332 19.771 1.00 44.07 C
ANISOU 2127 C ALA A1087 6869 3507 6370 928 -209 -62 C
ATOM 2128 O ALA A1087 4.895 -63.539 19.581 1.00 42.31 O
ANISOU 2128 O ALA A1087 6561 3297 6218 881 -234 -41 O
ATOM 2129 CB ALA A1087 6.706 -64.616 22.088 1.00 42.35 C
ANISOU 2129 CB ALA A1087 6281 3629 6182 989 -191 -277 C
ATOM 2130 N GLN A1088 6.803 -64.489 18.920 1.00 47.81 N
ANISOU 2130 N GLN A1088 7527 3793 6847 1009 -102 -58 N
ATOM 2131 CA GLN A1088 6.871 -63.736 17.697 1.00 51.21 C
ANISOU 2131 CA GLN A1088 8073 4022 7365 1058 -1 -22 C
ATOM 2132 C GLN A1088 5.709 -64.087 16.774 1.00 53.12 C
ANISOU 2132 C GLN A1088 8547 4163 7473 987 -140 140 C
ATOM 2133 O GLN A1088 5.119 -63.221 16.197 1.00 53.67 O
ANISOU 2133 O GLN A1088 8597 4167 7628 978 -115 158 O
ATOM 2134 CB GLN A1088 8.180 -63.979 16.997 1.00 58.99 C
ANISOU 2134 CB GLN A1088 9224 4831 8359 1176 142 -25 C
ATOM 2135 CG GLN A1088 9.355 -63.267 17.605 1.00 63.61 C
ANISOU 2135 CG GLN A1088 9569 5447 9152 1264 312 -185 C
ATOM 2136 CD GLN A1088 10.630 -63.606 16.891 1.00 76.65 C
ANISOU 2136 CD GLN A1088 11396 6919 10810 1380 453 -162 C
ATOM 2137 OE1 GLN A1088 10.894 -64.754 16.613 1.00 81.18 O
ANISOU 2137 OE1 GLN A1088 12210 7444 11189 1388 395 -80 O
ATOM 2138 NE2 GLN A1088 11.405 -62.610 16.574 1.00 81.73 N
ANISOU 2138 NE2 GLN A1088 11918 7456 11681 1475 638 -225 N
ATOM 2139 N ALA A1089 5.397 -65.355 16.605 1.00 54.79 N
ANISOU 2139 N ALA A1089 8982 4350 7485 941 -294 255 N
ATOM 2140 CA ALA A1089 4.282 -65.713 15.773 1.00 58.20 C
ANISOU 2140 CA ALA A1089 9626 4677 7809 878 -453 400 C
ATOM 2141 C ALA A1089 2.997 -65.145 16.356 1.00 53.55 C
ANISOU 2141 C ALA A1089 8824 4234 7288 765 -549 410 C
ATOM 2142 O ALA A1089 2.098 -64.773 15.643 1.00 55.72 O
ANISOU 2142 O ALA A1089 9180 4419 7571 727 -615 483 O
ATOM 2143 CB ALA A1089 4.181 -67.215 15.655 1.00 62.62 C
ANISOU 2143 CB ALA A1089 10429 5198 8165 845 -623 512 C
ATOM 2144 N ALA A1090 2.928 -65.096 17.673 1.00 48.09 N
ANISOU 2144 N ALA A1090 7864 3770 6640 722 -557 336 N
ATOM 2145 CA ALA A1090 1.764 -64.603 18.379 1.00 46.10 C
ANISOU 2145 CA ALA A1090 7389 3684 6444 630 -640 348 C
ATOM 2146 C ALA A1090 1.608 -63.108 18.235 1.00 43.96 C
ANISOU 2146 C ALA A1090 6936 3415 6351 655 -520 254 C
ATOM 2147 O ALA A1090 0.517 -62.607 18.219 1.00 43.99 O
ANISOU 2147 O ALA A1090 6861 3462 6392 583 -590 300 O
ATOM 2148 CB ALA A1090 1.845 -64.982 19.831 1.00 44.04 C
ANISOU 2148 CB ALA A1090 6903 3666 6163 614 -666 295 C
ATOM 2149 N ALA A1091 2.729 -62.421 18.115 1.00 43.00 N
ANISOU 2149 N ALA A1091 6749 3239 6349 759 -340 128 N
ATOM 2150 CA ALA A1091 2.759 -60.998 17.940 1.00 42.51 C
ANISOU 2150 CA ALA A1091 6513 3158 6480 797 -213 32 C
ATOM 2151 C ALA A1091 2.353 -60.665 16.533 1.00 46.91 C
ANISOU 2151 C ALA A1091 7289 3500 7034 801 -199 127 C
ATOM 2152 O ALA A1091 1.878 -59.592 16.296 1.00 45.85 O
ANISOU 2152 O ALA A1091 7041 3356 7024 792 -151 97 O
ATOM 2153 CB ALA A1091 4.120 -60.436 18.231 1.00 42.56 C
ANISOU 2153 CB ALA A1091 6380 3152 6640 911 -34 -120 C
ATOM 2154 N GLU A1092 2.516 -61.600 15.613 1.00 52.48 N
ANISOU 2154 N GLU A1092 8315 4036 7590 824 -250 241 N
ATOM 2155 CA GLU A1092 2.154 -61.378 14.221 1.00 59.24 C
ANISOU 2155 CA GLU A1092 9417 4675 8416 856 -247 335 C
ATOM 2156 C GLU A1092 0.652 -61.284 14.021 1.00 60.07 C
ANISOU 2156 C GLU A1092 9545 4797 8482 743 -417 425 C
ATOM 2157 O GLU A1092 0.190 -60.612 13.133 1.00 63.09 O
ANISOU 2157 O GLU A1092 10010 5054 8906 760 -393 456 O
ATOM 2158 CB GLU A1092 2.745 -62.444 13.304 1.00 70.15 C
ANISOU 2158 CB GLU A1092 11151 5870 9632 933 -271 429 C
ATOM 2159 CG GLU A1092 4.171 -62.181 12.884 1.00 79.28 C
ANISOU 2159 CG GLU A1092 12353 6912 10858 1082 -56 373 C
ATOM 2160 CD GLU A1092 4.282 -60.993 11.969 1.00 90.13 C
ANISOU 2160 CD GLU A1092 13728 8145 12373 1169 107 365 C
ATOM 2161 OE1 GLU A1092 3.616 -60.993 10.939 1.00 98.41 O
ANISOU 2161 OE1 GLU A1092 15001 9051 13341 1186 46 463 O
ATOM 2162 OE2 GLU A1092 5.019 -60.058 12.275 1.00 90.11 O
ANISOU 2162 OE2 GLU A1092 13501 8167 12569 1225 290 262 O
ATOM 2163 N GLN A1093 -0.106 -61.921 14.895 1.00 58.16 N
ANISOU 2163 N GLN A1093 9211 4714 8173 632 -580 467 N
ATOM 2164 CA GLN A1093 -1.556 -61.894 14.824 1.00 61.16 C
ANISOU 2164 CA GLN A1093 9585 5121 8533 518 -749 564 C
ATOM 2165 C GLN A1093 -2.116 -60.520 15.139 1.00 57.31 C
ANISOU 2165 C GLN A1093 8835 4734 8206 487 -673 488 C
ATOM 2166 O GLN A1093 -3.243 -60.242 14.822 1.00 60.24 O
ANISOU 2166 O GLN A1093 9218 5084 8584 411 -776 559 O
ATOM 2167 CB GLN A1093 -2.170 -62.888 15.786 1.00 63.66 C
ANISOU 2167 CB GLN A1093 9830 5595 8764 417 -920 639 C
ATOM 2168 CG GLN A1093 -1.559 -64.272 15.764 1.00 71.25 C
ANISOU 2168 CG GLN A1093 10992 6502 9576 439 -995 697 C
ATOM 2169 CD GLN A1093 -1.533 -64.880 14.398 1.00 84.11 C
ANISOU 2169 CD GLN A1093 12989 7872 11096 482 -1076 792 C
ATOM 2170 OE1 GLN A1093 -2.564 -65.060 13.783 1.00 92.65 O
ANISOU 2170 OE1 GLN A1093 14203 8852 12147 423 -1237 898 O
ATOM 2171 NE2 GLN A1093 -0.352 -65.205 13.920 1.00 86.01 N
ANISOU 2171 NE2 GLN A1093 13399 8001 11278 597 -971 754 N
ATOM 2172 N LEU A1094 -1.298 -59.697 15.783 1.00 51.48 N
ANISOU 2172 N LEU A1094 7860 4100 7599 550 -504 340 N
ATOM 2173 CA LEU A1094 -1.640 -58.346 16.149 1.00 48.34 C
ANISOU 2173 CA LEU A1094 7198 3802 7369 542 -422 243 C
ATOM 2174 C LEU A1094 -1.885 -57.536 14.907 1.00 52.10 C
ANISOU 2174 C LEU A1094 7800 4087 7909 570 -357 268 C
ATOM 2175 O LEU A1094 -2.760 -56.715 14.888 1.00 51.51 O
ANISOU 2175 O LEU A1094 7609 4055 7908 514 -379 264 O
ATOM 2176 CB LEU A1094 -0.549 -57.704 16.991 1.00 43.78 C
ANISOU 2176 CB LEU A1094 6369 3335 6931 626 -265 72 C
ATOM 2177 CG LEU A1094 -0.514 -58.109 18.448 1.00 42.04 C
ANISOU 2177 CG LEU A1094 5934 3356 6682 608 -323 14 C
ATOM 2178 CD1 LEU A1094 0.771 -57.622 19.043 1.00 40.84 C
ANISOU 2178 CD1 LEU A1094 5605 3250 6662 717 -176 -157 C
ATOM 2179 CD2 LEU A1094 -1.690 -57.558 19.206 1.00 42.04 C
ANISOU 2179 CD2 LEU A1094 5714 3546 6713 533 -408 17 C
ATOM 2180 N LYS A1095 -1.157 -57.817 13.834 1.00 57.30 N
ANISOU 2180 N LYS A1095 8715 4532 8523 662 -282 304 N
ATOM 2181 CA LYS A1095 -1.345 -57.112 12.573 1.00 62.97 C
ANISOU 2181 CA LYS A1095 9586 5055 9285 715 -211 340 C
ATOM 2182 C LYS A1095 -2.773 -57.209 12.062 1.00 67.45 C
ANISOU 2182 C LYS A1095 10275 5579 9773 620 -388 449 C
ATOM 2183 O LYS A1095 -3.340 -56.263 11.599 1.00 68.34 O
ANISOU 2183 O LYS A1095 10344 5649 9971 610 -352 439 O
ATOM 2184 CB LYS A1095 -0.343 -57.571 11.534 1.00 71.85 C
ANISOU 2184 CB LYS A1095 10992 5964 10342 852 -112 384 C
ATOM 2185 CG LYS A1095 0.987 -56.868 11.670 1.00 76.08 C
ANISOU 2185 CG LYS A1095 11379 6483 11045 967 125 276 C
ATOM 2186 CD LYS A1095 2.012 -57.363 10.683 1.00 90.73 C
ANISOU 2186 CD LYS A1095 13508 8132 12832 1114 236 337 C
ATOM 2187 CE LYS A1095 3.428 -57.201 11.226 1.00 95.56 C
ANISOU 2187 CE LYS A1095 13958 8773 13578 1200 416 239 C
ATOM 2188 NZ LYS A1095 4.385 -58.195 10.650 1.00106.95 N
ANISOU 2188 NZ LYS A1095 15671 10077 14887 1311 460 310 N
ATOM 2189 N THR A1096 -3.380 -58.360 12.172 1.00 71.17 N
ANISOU 2189 N THR A1096 10889 6057 10094 545 -588 553 N
ATOM 2190 CA THR A1096 -4.742 -58.519 11.771 1.00 77.26 C
ANISOU 2190 CA THR A1096 11758 6784 10813 448 -776 659 C
ATOM 2191 C THR A1096 -5.663 -57.629 12.596 1.00 72.39 C
ANISOU 2191 C THR A1096 10832 6358 10315 343 -792 620 C
ATOM 2192 O THR A1096 -6.580 -57.085 12.078 1.00 76.14 O
ANISOU 2192 O THR A1096 11332 6776 10822 297 -847 657 O
ATOM 2193 CB THR A1096 -5.153 -59.994 11.886 1.00 85.11 C
ANISOU 2193 CB THR A1096 12927 7759 11653 386 -997 780 C
ATOM 2194 OG1 THR A1096 -4.337 -60.769 10.999 1.00 92.75 O
ANISOU 2194 OG1 THR A1096 14208 8532 12500 498 -990 816 O
ATOM 2195 CG2 THR A1096 -6.598 -60.181 11.532 1.00 93.16 C
ANISOU 2195 CG2 THR A1096 14023 8724 12648 279 -1211 895 C
ATOM 2196 N THR A1097 -5.423 -57.478 13.888 1.00 65.41 N
ANISOU 2196 N THR A1097 9661 5702 9490 314 -748 542 N
ATOM 2197 CA THR A1097 -6.258 -56.624 14.699 1.00 62.69 C
ANISOU 2197 CA THR A1097 9026 5546 9247 237 -760 503 C
ATOM 2198 C THR A1097 -6.053 -55.160 14.369 1.00 59.10 C
ANISOU 2198 C THR A1097 8440 5067 8948 288 -596 390 C
ATOM 2199 O THR A1097 -6.958 -54.376 14.499 1.00 59.45 O
ANISOU 2199 O THR A1097 8345 5182 9061 225 -624 386 O
ATOM 2200 CB THR A1097 -5.998 -56.813 16.183 1.00 60.02 C
ANISOU 2200 CB THR A1097 8422 5461 8922 226 -752 441 C
ATOM 2201 OG1 THR A1097 -6.018 -58.200 16.479 1.00 64.93 O
ANISOU 2201 OG1 THR A1097 9166 6098 9406 192 -881 545 O
ATOM 2202 CG2 THR A1097 -7.066 -56.153 16.980 1.00 61.03 C
ANISOU 2202 CG2 THR A1097 8295 5781 9114 148 -805 442 C
ATOM 2203 N ARG A1098 -4.850 -54.808 13.961 1.00 56.37 N
ANISOU 2203 N ARG A1098 8131 4620 8666 405 -423 304 N
ATOM 2204 CA ARG A1098 -4.523 -53.457 13.607 1.00 54.68 C
ANISOU 2204 CA ARG A1098 7792 4362 8622 467 -255 203 C
ATOM 2205 C ARG A1098 -5.198 -53.117 12.295 1.00 60.85 C
ANISOU 2205 C ARG A1098 8790 4949 9382 464 -273 287 C
ATOM 2206 O ARG A1098 -5.866 -52.119 12.177 1.00 60.98 O
ANISOU 2206 O ARG A1098 8686 4989 9493 428 -253 259 O
ATOM 2207 CB ARG A1098 -3.022 -53.307 13.501 1.00 53.44 C
ANISOU 2207 CB ARG A1098 7626 4130 8551 597 -69 114 C
ATOM 2208 CG ARG A1098 -2.570 -51.969 13.013 1.00 54.38 C
ANISOU 2208 CG ARG A1098 7629 4164 8867 675 115 29 C
ATOM 2209 CD ARG A1098 -1.150 -52.024 12.529 1.00 58.16 C
ANISOU 2209 CD ARG A1098 8190 4495 9413 813 292 1 C
ATOM 2210 NE ARG A1098 -1.015 -52.814 11.321 1.00 64.72 N
ANISOU 2210 NE ARG A1098 9388 5115 10089 873 286 132 N
ATOM 2211 CZ ARG A1098 0.131 -53.266 10.860 1.00 70.32 C
ANISOU 2211 CZ ARG A1098 10245 5693 10782 993 403 151 C
ATOM 2212 NH1 ARG A1098 1.249 -53.009 11.490 1.00 68.56 N
ANISOU 2212 NH1 ARG A1098 9827 5518 10704 1055 535 50 N
ATOM 2213 NH2 ARG A1098 0.159 -53.980 9.771 1.00 77.42 N
ANISOU 2213 NH2 ARG A1098 11487 6409 11522 1059 380 272 N
ATOM 2214 N ASN A1099 -5.059 -53.972 11.310 1.00 66.88 N
ANISOU 2214 N ASN A1099 9883 5518 10009 510 -322 389 N
ATOM 2215 CA ASN A1099 -5.653 -53.689 10.035 1.00 74.65 C
ANISOU 2215 CA ASN A1099 11096 6307 10959 535 -345 462 C
ATOM 2216 C ASN A1099 -7.149 -53.498 10.052 1.00 77.80 C
ANISOU 2216 C ASN A1099 11465 6752 11342 405 -516 521 C
ATOM 2217 O ASN A1099 -7.639 -52.584 9.450 1.00 80.58 O
ANISOU 2217 O ASN A1099 11815 7039 11764 409 -471 510 O
ATOM 2218 CB ASN A1099 -5.309 -54.764 9.021 1.00 84.52 C
ANISOU 2218 CB ASN A1099 12727 7346 12041 621 -405 564 C
ATOM 2219 CG ASN A1099 -3.849 -54.822 8.720 1.00 89.02 C
ANISOU 2219 CG ASN A1099 13366 7827 12631 773 -210 524 C
ATOM 2220 OD1 ASN A1099 -3.128 -53.889 8.988 1.00 86.29 O
ANISOU 2220 OD1 ASN A1099 12810 7526 12451 827 -15 427 O
ATOM 2221 ND2 ASN A1099 -3.401 -55.929 8.171 1.00 96.62 N
ANISOU 2221 ND2 ASN A1099 14619 8658 13434 846 -269 601 N
ATOM 2222 N ALA A1100 -7.877 -54.334 10.757 1.00 78.30 N
ANISOU 2222 N ALA A1100 11495 6930 11327 291 -705 588 N
ATOM 2223 CA ALA A1100 -9.316 -54.243 10.712 1.00 83.57 C
ANISOU 2223 CA ALA A1100 12148 7619 11986 170 -876 667 C
ATOM 2224 C ALA A1100 -10.026 -53.590 11.856 1.00 79.31 C
ANISOU 2224 C ALA A1100 11269 7322 11543 65 -891 628 C
ATOM 2225 O ALA A1100 -11.233 -53.529 11.855 1.00 85.06 O
ANISOU 2225 O ALA A1100 11974 8073 12272 -36 -1030 704 O
ATOM 2226 CB ALA A1100 -9.889 -55.614 10.493 1.00 92.79 C
ANISOU 2226 CB ALA A1100 13541 8701 13013 115 -1107 807 C
ATOM 2227 N TYR A1101 -9.297 -53.126 12.844 1.00 70.99 N
ANISOU 2227 N TYR A1101 9954 6447 10572 98 -759 512 N
ATOM 2228 CA TYR A1101 -9.916 -52.462 13.970 1.00 68.94 C
ANISOU 2228 CA TYR A1101 9372 6428 10395 28 -768 465 C
ATOM 2229 C TYR A1101 -9.190 -51.180 14.369 1.00 62.00 C
ANISOU 2229 C TYR A1101 8247 5638 9672 103 -577 294 C
ATOM 2230 O TYR A1101 -9.720 -50.101 14.260 1.00 61.88 O
ANISOU 2230 O TYR A1101 8104 5651 9756 81 -538 249 O
ATOM 2231 CB TYR A1101 -9.976 -53.376 15.178 1.00 69.80 C
ANISOU 2231 CB TYR A1101 9359 6728 10434 -13 -861 506 C
ATOM 2232 CG TYR A1101 -10.950 -54.512 15.112 1.00 79.68 C
ANISOU 2232 CG TYR A1101 10752 7948 11576 -113 -1072 682 C
ATOM 2233 CD1 TYR A1101 -12.277 -54.328 15.432 1.00 87.59 C
ANISOU 2233 CD1 TYR A1101 11639 9040 12600 -220 -1192 773 C
ATOM 2234 CD2 TYR A1101 -10.533 -55.785 14.777 1.00 83.62 C
ANISOU 2234 CD2 TYR A1101 11484 8328 11959 -98 -1154 763 C
ATOM 2235 CE1 TYR A1101 -13.169 -55.378 15.412 1.00 98.55 C
ANISOU 2235 CE1 TYR A1101 13133 10392 13921 -312 -1390 946 C
ATOM 2236 CE2 TYR A1101 -11.413 -56.830 14.742 1.00 94.02 C
ANISOU 2236 CE2 TYR A1101 12914 9607 13202 -188 -1360 926 C
ATOM 2237 CZ TYR A1101 -12.727 -56.618 15.069 1.00102.42 C
ANISOU 2237 CZ TYR A1101 13849 10755 14312 -296 -1477 1019 C
ATOM 2238 OH TYR A1101 -13.606 -57.655 15.028 1.00115.90 O
ANISOU 2238 OH TYR A1101 15654 12409 15976 -386 -1686 1191 O
ATOM 2239 N ILE A1102 -7.981 -51.319 14.863 1.00 56.96 N
ANISOU 2239 N ILE A1102 7534 5043 9065 192 -468 200 N
ATOM 2240 CA ILE A1102 -7.233 -50.181 15.311 1.00 52.86 C
ANISOU 2240 CA ILE A1102 6770 4599 8717 268 -308 35 C
ATOM 2241 C ILE A1102 -7.072 -49.080 14.285 1.00 53.17 C
ANISOU 2241 C ILE A1102 6845 4474 8884 316 -177 -9 C
ATOM 2242 O ILE A1102 -7.187 -47.945 14.626 1.00 51.87 O
ANISOU 2242 O ILE A1102 6451 4393 8865 322 -112 -109 O
ATOM 2243 CB ILE A1102 -5.867 -50.586 15.798 1.00 50.37 C
ANISOU 2243 CB ILE A1102 6414 4301 8424 366 -215 -51 C
ATOM 2244 CG1 ILE A1102 -5.976 -51.845 16.646 1.00 51.72 C
ANISOU 2244 CG1 ILE A1102 6606 4602 8443 327 -343 13 C
ATOM 2245 CG2 ILE A1102 -5.252 -49.458 16.575 1.00 48.64 C
ANISOU 2245 CG2 ILE A1102 5883 4200 8395 435 -100 -229 C
ATOM 2246 CD1 ILE A1102 -7.049 -51.789 17.694 1.00 54.64 C
ANISOU 2246 CD1 ILE A1102 6776 5204 8782 247 -463 38 C
ATOM 2247 N GLN A1103 -6.797 -49.409 13.039 1.00 55.79 N
ANISOU 2247 N GLN A1103 7464 4573 9163 362 -137 68 N
ATOM 2248 CA GLN A1103 -6.631 -48.382 12.023 1.00 58.06 C
ANISOU 2248 CA GLN A1103 7795 4698 9568 424 3 41 C
ATOM 2249 C GLN A1103 -7.906 -47.606 11.772 1.00 59.38 C
ANISOU 2249 C GLN A1103 7911 4891 9759 336 -65 64 C
ATOM 2250 O GLN A1103 -7.872 -46.459 11.415 1.00 59.43 O
ANISOU 2250 O GLN A1103 7815 4858 9909 368 50 0 O
ATOM 2251 CB GLN A1103 -6.115 -48.966 10.730 1.00 65.30 C
ANISOU 2251 CB GLN A1103 9054 5363 10394 516 55 133 C
ATOM 2252 CG GLN A1103 -5.229 -48.016 9.969 1.00 72.05 C
ANISOU 2252 CG GLN A1103 9899 6069 11408 644 279 81 C
ATOM 2253 CD GLN A1103 -5.131 -48.335 8.503 1.00 85.50 C
ANISOU 2253 CD GLN A1103 11955 7519 13010 740 322 192 C
ATOM 2254 OE1 GLN A1103 -5.691 -49.302 8.036 1.00 92.26 O
ANISOU 2254 OE1 GLN A1103 13078 8302 13676 713 169 297 O
ATOM 2255 NE2 GLN A1103 -4.409 -47.524 7.778 1.00 89.77 N
ANISOU 2255 NE2 GLN A1103 12498 7923 13686 864 528 173 N
ATOM 2256 N LYS A1104 -9.029 -48.265 11.933 1.00 61.45 N
ANISOU 2256 N LYS A1104 8249 5209 9888 225 -255 165 N
ATOM 2257 CA LYS A1104 -10.329 -47.627 11.782 1.00 64.63 C
ANISOU 2257 CA LYS A1104 8599 5649 10309 129 -341 198 C
ATOM 2258 C LYS A1104 -10.606 -46.665 12.944 1.00 61.28 C
ANISOU 2258 C LYS A1104 7809 5465 10009 89 -316 88 C
ATOM 2259 O LYS A1104 -11.206 -45.611 12.730 1.00 62.37 O
ANISOU 2259 O LYS A1104 7843 5616 10238 60 -287 52 O
ATOM 2260 CB LYS A1104 -11.443 -48.670 11.619 1.00 72.69 C
ANISOU 2260 CB LYS A1104 9802 6644 11172 24 -562 351 C
ATOM 2261 CG LYS A1104 -11.495 -49.250 10.215 1.00 83.89 C
ANISOU 2261 CG LYS A1104 11593 7793 12488 68 -608 448 C
ATOM 2262 CD LYS A1104 -11.971 -50.696 10.214 1.00 95.15 C
ANISOU 2262 CD LYS A1104 13216 9175 13760 9 -819 582 C
ATOM 2263 CE LYS A1104 -11.609 -51.406 8.930 1.00106.43 C
ANISOU 2263 CE LYS A1104 15023 10338 15076 102 -849 650 C
ATOM 2264 NZ LYS A1104 -11.921 -52.861 8.994 1.00115.65 N
ANISOU 2264 NZ LYS A1104 16372 11461 16108 55 -1059 768 N
ATOM 2265 N TYR A1105 -10.148 -47.008 14.164 1.00 57.99 N
ANISOU 2265 N TYR A1105 7203 5238 9593 102 -327 31 N
ATOM 2266 CA TYR A1105 -10.292 -46.117 15.308 1.00 57.17 C
ANISOU 2266 CA TYR A1105 6761 5362 9598 100 -307 -88 C
ATOM 2267 C TYR A1105 -9.439 -44.860 15.065 1.00 53.80 C
ANISOU 2267 C TYR A1105 6192 4877 9373 193 -130 -239 C
ATOM 2268 O TYR A1105 -9.940 -43.763 15.245 1.00 54.93 O
ANISOU 2268 O TYR A1105 6151 5096 9624 173 -112 -307 O
ATOM 2269 CB TYR A1105 -9.892 -46.789 16.639 1.00 57.29 C
ANISOU 2269 CB TYR A1105 6624 5580 9562 124 -354 -123 C
ATOM 2270 CG TYR A1105 -9.902 -45.809 17.795 1.00 60.15 C
ANISOU 2270 CG TYR A1105 6648 6168 10039 163 -328 -266 C
ATOM 2271 CD1 TYR A1105 -11.096 -45.363 18.345 1.00 66.31 C
ANISOU 2271 CD1 TYR A1105 7279 7115 10800 94 -419 -235 C
ATOM 2272 CD2 TYR A1105 -8.721 -45.257 18.277 1.00 59.36 C
ANISOU 2272 CD2 TYR A1105 6378 6096 10079 277 -215 -435 C
ATOM 2273 CE1 TYR A1105 -11.115 -44.416 19.362 1.00 70.21 C
ANISOU 2273 CE1 TYR A1105 7474 7810 11391 149 -401 -372 C
ATOM 2274 CE2 TYR A1105 -8.728 -44.308 19.293 1.00 63.42 C
ANISOU 2274 CE2 TYR A1105 6590 6800 10707 329 -210 -580 C
ATOM 2275 CZ TYR A1105 -9.930 -43.895 19.840 1.00 69.37 C
ANISOU 2275 CZ TYR A1105 7210 7728 11418 270 -305 -550 C
ATOM 2276 OH TYR A1105 -9.954 -42.953 20.843 1.00 75.88 O
ANISOU 2276 OH TYR A1105 7747 8743 12341 339 -310 -695 O
ATOM 2277 N LEU A1106 -8.174 -45.031 14.644 1.00 51.00 N
ANISOU 2277 N LEU A1106 5920 4380 9075 295 -3 -281 N
ATOM 2278 CA LEU A1106 -7.262 -43.933 14.354 1.00 51.13 C
ANISOU 2278 CA LEU A1106 5807 4312 9310 392 173 -403 C
ATOM 2279 C LEU A1106 -7.874 -42.965 13.320 1.00 53.20 C
ANISOU 2279 C LEU A1106 6123 4444 9645 371 231 -376 C
ATOM 2280 O LEU A1106 -7.921 -41.770 13.576 1.00 53.28 O
ANISOU 2280 O LEU A1106 5901 4513 9830 383 291 -482 O
ATOM 2281 CB LEU A1106 -5.896 -44.477 13.880 1.00 51.66 C
ANISOU 2281 CB LEU A1106 6013 4214 9403 500 297 -401 C
ATOM 2282 CG LEU A1106 -4.945 -43.499 13.148 1.00 56.82 C
ANISOU 2282 CG LEU A1106 6617 4693 10279 610 501 -464 C
ATOM 2283 CD1 LEU A1106 -4.286 -42.528 14.123 1.00 58.51 C
ANISOU 2283 CD1 LEU A1106 6475 5024 10734 663 562 -642 C
ATOM 2284 CD2 LEU A1106 -3.872 -44.258 12.351 1.00 60.31 C
ANISOU 2284 CD2 LEU A1106 7297 4934 10683 709 611 -393 C
ATOM 2285 N GLU A 219 -8.377 -43.493 12.193 1.00 82.04 N
ANISOU 2285 N GLU A 219 10793 10538 9841 -298 -345 218 N
ATOM 2286 CA GLU A 219 -8.984 -42.677 11.145 1.00 81.75 C
ANISOU 2286 CA GLU A 219 10765 10507 9791 -276 -311 228 C
ATOM 2287 C GLU A 219 -10.226 -41.925 11.609 1.00 79.65 C
ANISOU 2287 C GLU A 219 10491 10270 9502 -286 -308 237 C
ATOM 2288 O GLU A 219 -10.382 -40.761 11.244 1.00 79.33 O
ANISOU 2288 O GLU A 219 10444 10230 9466 -271 -272 238 O
ATOM 2289 CB GLU A 219 -9.263 -43.514 9.892 1.00 85.90 C
ANISOU 2289 CB GLU A 219 11317 11026 10295 -261 -318 237 C
ATOM 2290 CG GLU A 219 -7.994 -43.846 9.134 1.00 94.77 C
ANISOU 2290 CG GLU A 219 12447 12118 11443 -242 -304 227 C
ATOM 2291 CD GLU A 219 -8.078 -45.038 8.206 1.00107.53 C
ANISOU 2291 CD GLU A 219 14089 13727 13041 -233 -326 233 C
ATOM 2292 OE1 GLU A 219 -9.100 -45.762 8.247 1.00110.11 O
ANISOU 2292 OE1 GLU A 219 14429 14073 13337 -244 -359 246 O
ATOM 2293 OE2 GLU A 219 -7.100 -45.267 7.457 1.00112.52 O
ANISOU 2293 OE2 GLU A 219 14727 14334 13691 -215 -311 225 O
ATOM 2294 N ARG A 220 -11.079 -42.546 12.439 1.00 78.58 N
ANISOU 2294 N ARG A 220 10355 10159 9344 -310 -345 244 N
ATOM 2295 CA ARG A 220 -12.269 -41.869 12.956 1.00 77.37 C
ANISOU 2295 CA ARG A 220 10193 10036 9169 -320 -344 253 C
ATOM 2296 C ARG A 220 -11.921 -40.823 13.997 1.00 75.69 C
ANISOU 2296 C ARG A 220 9954 9826 8977 -328 -327 242 C
ATOM 2297 O ARG A 220 -12.553 -39.764 14.027 1.00 74.53 O
ANISOU 2297 O ARG A 220 9799 9694 8824 -322 -305 245 O
ATOM 2298 CB ARG A 220 -13.285 -42.850 13.539 1.00 80.12 C
ANISOU 2298 CB ARG A 220 10546 10409 9485 -345 -388 264 C
ATOM 2299 CG ARG A 220 -14.223 -43.443 12.503 1.00 86.44 C
ANISOU 2299 CG ARG A 220 11371 11218 10256 -336 -399 280 C
ATOM 2300 CD ARG A 220 -15.236 -44.383 13.141 1.00 92.10 C
ANISOU 2300 CD ARG A 220 12091 11961 10942 -362 -444 292 C
ATOM 2301 NE ARG A 220 -15.625 -45.461 12.229 1.00 97.92 N
ANISOU 2301 NE ARG A 220 12853 12694 11659 -355 -468 305 N
ATOM 2302 CZ ARG A 220 -16.619 -46.314 12.456 1.00101.90 C
ANISOU 2302 CZ ARG A 220 13365 13219 12133 -372 -506 319 C
ATOM 2303 NH1 ARG A 220 -17.351 -46.215 13.561 1.00101.04 N
ANISOU 2303 NH1 ARG A 220 13241 13138 12011 -397 -523 323 N
ATOM 2304 NH2 ARG A 220 -16.891 -47.274 11.579 1.00103.75 N
ANISOU 2304 NH2 ARG A 220 13623 13447 12351 -364 -528 331 N
ATOM 2305 N ALA A 221 -10.935 -41.106 14.863 1.00 75.21 N
ANISOU 2305 N ALA A 221 9883 9752 8943 -340 -339 230 N
ATOM 2306 CA ALA A 221 -10.539 -40.144 15.893 1.00 74.35 C
ANISOU 2306 CA ALA A 221 9750 9643 8856 -346 -326 220 C
ATOM 2307 C ALA A 221 -9.899 -38.906 15.259 1.00 73.91 C
ANISOU 2307 C ALA A 221 9688 9570 8826 -321 -280 214 C
ATOM 2308 O ALA A 221 -10.144 -37.792 15.714 1.00 72.46 O
ANISOU 2308 O ALA A 221 9488 9396 8647 -319 -261 212 O
ATOM 2309 CB ALA A 221 -9.580 -40.784 16.882 1.00 75.31 C
ANISOU 2309 CB ALA A 221 9864 9750 9001 -364 -351 208 C
ATOM 2310 N ARG A 222 -9.104 -39.110 14.195 1.00 74.93 N
ANISOU 2310 N ARG A 222 9827 9672 8969 -301 -262 211 N
ATOM 2311 CA ARG A 222 -8.446 -38.043 13.451 1.00 75.46 C
ANISOU 2311 CA ARG A 222 9890 9721 9060 -276 -218 207 C
ATOM 2312 C ARG A 222 -9.488 -37.198 12.706 1.00 73.90 C
ANISOU 2312 C ARG A 222 9699 9541 8840 -263 -195 217 C
ATOM 2313 O ARG A 222 -9.388 -35.972 12.666 1.00 73.16 O
ANISOU 2313 O ARG A 222 9593 9445 8759 -252 -165 214 O
ATOM 2314 CB ARG A 222 -7.461 -38.661 12.456 1.00 79.01 C
ANISOU 2314 CB ARG A 222 10353 10142 9526 -260 -210 203 C
ATOM 2315 CG ARG A 222 -6.546 -37.658 11.785 1.00 83.82 C
ANISOU 2315 CG ARG A 222 10956 10728 10165 -236 -166 197 C
ATOM 2316 CD ARG A 222 -5.808 -38.312 10.632 1.00 90.11 C
ANISOU 2316 CD ARG A 222 11768 11500 10968 -219 -156 195 C
ATOM 2317 NE ARG A 222 -4.869 -39.338 11.085 1.00 95.61 N
ANISOU 2317 NE ARG A 222 12464 12180 11684 -229 -181 185 N
ATOM 2318 CZ ARG A 222 -4.327 -40.259 10.292 1.00101.02 C
ANISOU 2318 CZ ARG A 222 13163 12847 12371 -219 -186 183 C
ATOM 2319 NH1 ARG A 222 -4.654 -40.318 9.006 1.00101.58 N
ANISOU 2319 NH1 ARG A 222 13254 12917 12423 -199 -169 191 N
ATOM 2320 NH2 ARG A 222 -3.466 -41.141 10.783 1.00102.85 N
ANISOU 2320 NH2 ARG A 222 13393 13064 12622 -229 -210 172 N
ATOM 2321 N SER A 223 -10.501 -37.862 12.137 1.00 73.29 N
ANISOU 2321 N SER A 223 9640 9479 8728 -264 -212 229 N
ATOM 2322 CA SER A 223 -11.588 -37.216 11.413 1.00 71.92 C
ANISOU 2322 CA SER A 223 9475 9321 8530 -254 -195 239 C
ATOM 2323 C SER A 223 -12.435 -36.373 12.363 1.00 68.96 C
ANISOU 2323 C SER A 223 9083 8974 8146 -266 -197 240 C
ATOM 2324 O SER A 223 -12.853 -35.277 11.992 1.00 68.52 O
ANISOU 2324 O SER A 223 9024 8924 8088 -254 -170 241 O
ATOM 2325 CB SER A 223 -12.437 -38.263 10.695 1.00 74.97 C
ANISOU 2325 CB SER A 223 9886 9716 8884 -254 -218 252 C
ATOM 2326 OG SER A 223 -13.606 -37.685 10.141 1.00 78.59 O
ANISOU 2326 OG SER A 223 10353 10192 9318 -247 -208 262 O
ATOM 2327 N THR A 224 -12.648 -36.850 13.595 1.00 67.02 N
ANISOU 2327 N THR A 224 8825 8743 7894 -290 -227 238 N
ATOM 2328 CA THR A 224 -13.398 -36.088 14.587 1.00 65.13 C
ANISOU 2328 CA THR A 224 8569 8532 7648 -303 -230 238 C
ATOM 2329 C THR A 224 -12.597 -34.849 15.013 1.00 63.77 C
ANISOU 2329 C THR A 224 8376 8346 7506 -294 -202 226 C
ATOM 2330 O THR A 224 -13.168 -33.778 15.137 1.00 62.33 O
ANISOU 2330 O THR A 224 8184 8179 7320 -288 -185 226 O
ATOM 2331 CB THR A 224 -13.816 -36.984 15.752 1.00 66.31 C
ANISOU 2331 CB THR A 224 8712 8700 7781 -331 -270 239 C
ATOM 2332 OG1 THR A 224 -14.501 -38.116 15.222 1.00 68.74 O
ANISOU 2332 OG1 THR A 224 9040 9016 8062 -337 -295 251 O
ATOM 2333 CG2 THR A 224 -14.716 -36.279 16.738 1.00 65.15 C
ANISOU 2333 CG2 THR A 224 8549 8584 7622 -344 -273 240 C
ATOM 2334 N LEU A 225 -11.291 -34.972 15.163 1.00 64.12 N
ANISOU 2334 N LEU A 225 8415 8363 7583 -290 -196 216 N
ATOM 2335 CA LEU A 225 -10.456 -33.850 15.522 1.00 63.93 C
ANISOU 2335 CA LEU A 225 8374 8325 7593 -280 -171 206 C
ATOM 2336 C LEU A 225 -10.403 -32.780 14.432 1.00 62.97 C
ANISOU 2336 C LEU A 225 8255 8194 7478 -255 -132 208 C
ATOM 2337 O LEU A 225 -10.475 -31.625 14.725 1.00 62.04 O
ANISOU 2337 O LEU A 225 8123 8082 7369 -249 -114 205 O
ATOM 2338 CB LEU A 225 -9.049 -34.290 15.865 1.00 65.94 C
ANISOU 2338 CB LEU A 225 8622 8550 7882 -282 -175 196 C
ATOM 2339 CG LEU A 225 -8.836 -34.971 17.194 1.00 68.60 C
ANISOU 2339 CG LEU A 225 8951 8890 8224 -307 -208 190 C
ATOM 2340 CD1 LEU A 225 -7.428 -35.500 17.265 1.00 70.83 C
ANISOU 2340 CD1 LEU A 225 9231 9139 8540 -306 -211 180 C
ATOM 2341 CD2 LEU A 225 -9.084 -34.023 18.345 1.00 68.50 C
ANISOU 2341 CD2 LEU A 225 8917 8892 8216 -315 -208 186 C
ATOM 2342 N GLN A 226 -10.247 -33.181 13.186 1.00 63.10 N
ANISOU 2342 N GLN A 226 8290 8196 7489 -241 -120 213 N
ATOM 2343 CA GLN A 226 -10.207 -32.254 12.053 1.00 62.69 C
ANISOU 2343 CA GLN A 226 8243 8134 7441 -217 -84 215 C
ATOM 2344 C GLN A 226 -11.498 -31.463 11.956 1.00 60.15 C
ANISOU 2344 C GLN A 226 7922 7838 7093 -216 -79 221 C
ATOM 2345 O GLN A 226 -11.456 -30.263 11.662 1.00 59.11 O
ANISOU 2345 O GLN A 226 7783 7704 6972 -203 -52 219 O
ATOM 2346 CB GLN A 226 -9.967 -33.002 10.731 1.00 66.28 C
ANISOU 2346 CB GLN A 226 8723 8572 7889 -203 -77 220 C
ATOM 2347 CG GLN A 226 -8.547 -33.520 10.564 1.00 73.99 C
ANISOU 2347 CG GLN A 226 9699 9518 8897 -198 -71 213 C
ATOM 2348 CD GLN A 226 -8.432 -34.549 9.453 1.00 82.96 C
ANISOU 2348 CD GLN A 226 10859 10642 10021 -188 -75 218 C
ATOM 2349 OE1 GLN A 226 -9.315 -34.696 8.591 1.00 85.93 O
ANISOU 2349 OE1 GLN A 226 11255 11027 10368 -181 -73 228 O
ATOM 2350 NE2 GLN A 226 -7.338 -35.286 9.443 1.00 85.30 N
ANISOU 2350 NE2 GLN A 226 11156 10916 10338 -187 -80 211 N
ATOM 2351 N LYS A 227 -12.647 -32.131 12.205 1.00 58.65 N
ANISOU 2351 N LYS A 227 7740 7675 6871 -231 -106 229 N
ATOM 2352 CA LYS A 227 -13.951 -31.471 12.201 1.00 56.59 C
ANISOU 2352 CA LYS A 227 7478 7440 6584 -232 -105 234 C
ATOM 2353 C LYS A 227 -14.015 -30.451 13.313 1.00 54.86 C
ANISOU 2353 C LYS A 227 7234 7235 6376 -238 -102 226 C
ATOM 2354 O LYS A 227 -14.575 -29.380 13.109 1.00 54.45 O
ANISOU 2354 O LYS A 227 7176 7192 6318 -229 -85 225 O
ATOM 2355 CB LYS A 227 -15.101 -32.474 12.337 1.00 58.05 C
ANISOU 2355 CB LYS A 227 7674 7648 6734 -248 -137 244 C
ATOM 2356 CG LYS A 227 -15.392 -33.217 11.045 1.00 63.77 C
ANISOU 2356 CG LYS A 227 8426 8363 7441 -237 -137 254 C
ATOM 2357 CD LYS A 227 -16.483 -34.248 11.228 1.00 69.22 C
ANISOU 2357 CD LYS A 227 9127 9075 8099 -253 -171 265 C
ATOM 2358 CE LYS A 227 -16.619 -35.116 10.001 1.00 75.42 C
ANISOU 2358 CE LYS A 227 9940 9846 8869 -242 -176 275 C
ATOM 2359 NZ LYS A 227 -17.634 -36.191 10.190 1.00 79.24 N
ANISOU 2359 NZ LYS A 227 10435 10350 9323 -258 -212 287 N
ATOM 2360 N GLU A 228 -13.447 -30.754 14.456 1.00 53.95 N
ANISOU 2360 N GLU A 228 7104 7119 6275 -253 -118 220 N
ATOM 2361 CA GLU A 228 -13.407 -29.815 15.542 1.00 52.76 C
ANISOU 2361 CA GLU A 228 6930 6979 6137 -258 -117 212 C
ATOM 2362 C GLU A 228 -12.514 -28.616 15.190 1.00 52.12 C
ANISOU 2362 C GLU A 228 6840 6877 6088 -238 -84 205 C
ATOM 2363 O GLU A 228 -12.845 -27.512 15.496 1.00 51.27 O
ANISOU 2363 O GLU A 228 6719 6780 5982 -233 -73 202 O
ATOM 2364 CB GLU A 228 -12.936 -30.485 16.808 1.00 54.80 C
ANISOU 2364 CB GLU A 228 7177 7238 6405 -278 -143 207 C
ATOM 2365 CG GLU A 228 -14.012 -31.233 17.527 1.00 58.06 C
ANISOU 2365 CG GLU A 228 7591 7682 6785 -300 -174 213 C
ATOM 2366 CD GLU A 228 -13.536 -31.772 18.843 1.00 61.36 C
ANISOU 2366 CD GLU A 228 7998 8101 7214 -321 -199 207 C
ATOM 2367 OE1 GLU A 228 -12.971 -32.864 18.872 1.00 63.64 O
ANISOU 2367 OE1 GLU A 228 8297 8376 7509 -330 -217 207 O
ATOM 2368 OE2 GLU A 228 -13.741 -31.093 19.849 1.00 60.40 O
ANISOU 2368 OE2 GLU A 228 7860 7995 7095 -328 -202 202 O
ATOM 2369 N VAL A 229 -11.381 -28.847 14.549 1.00 52.44 N
ANISOU 2369 N VAL A 229 6887 6886 6153 -226 -69 203 N
ATOM 2370 CA VAL A 229 -10.514 -27.744 14.130 1.00 52.69 C
ANISOU 2370 CA VAL A 229 6909 6895 6214 -207 -38 198 C
ATOM 2371 C VAL A 229 -11.255 -26.862 13.098 1.00 51.09 C
ANISOU 2371 C VAL A 229 6716 6701 5997 -191 -15 203 C
ATOM 2372 O VAL A 229 -11.260 -25.649 13.239 1.00 49.60 O
ANISOU 2372 O VAL A 229 6514 6514 5818 -183 0 200 O
ATOM 2373 CB VAL A 229 -9.147 -28.236 13.609 1.00 55.41 C
ANISOU 2373 CB VAL A 229 7259 7205 6588 -199 -26 196 C
ATOM 2374 CG1 VAL A 229 -8.329 -27.093 13.022 1.00 56.27 C
ANISOU 2374 CG1 VAL A 229 7360 7292 6726 -178 8 193 C
ATOM 2375 CG2 VAL A 229 -8.372 -28.933 14.714 1.00 56.66 C
ANISOU 2375 CG2 VAL A 229 7407 7355 6767 -214 -49 189 C
ATOM 2376 N HIS A 230 -11.952 -27.476 12.127 1.00 50.85 N
ANISOU 2376 N HIS A 230 6708 6675 5940 -189 -17 211 N
ATOM 2377 CA HIS A 230 -12.741 -26.741 11.137 1.00 50.70 C
ANISOU 2377 CA HIS A 230 6699 6661 5902 -175 1 216 C
ATOM 2378 C HIS A 230 -13.838 -25.898 11.825 1.00 47.72 C
ANISOU 2378 C HIS A 230 6309 6314 5509 -182 -6 214 C
ATOM 2379 O HIS A 230 -14.003 -24.717 11.498 1.00 46.47 O
ANISOU 2379 O HIS A 230 6146 6156 5356 -170 13 212 O
ATOM 2380 CB HIS A 230 -13.379 -27.705 10.121 1.00 53.70 C
ANISOU 2380 CB HIS A 230 7106 7042 6255 -174 -5 226 C
ATOM 2381 CG HIS A 230 -14.018 -27.009 8.954 1.00 58.97 C
ANISOU 2381 CG HIS A 230 7788 7708 6908 -158 15 230 C
ATOM 2382 ND1 HIS A 230 -13.339 -26.834 7.755 1.00 62.30 N
ANISOU 2382 ND1 HIS A 230 8225 8103 7341 -140 42 232 N
ATOM 2383 CD2 HIS A 230 -15.256 -26.469 8.834 1.00 60.03 C
ANISOU 2383 CD2 HIS A 230 7926 7864 7019 -159 12 233 C
ATOM 2384 CE1 HIS A 230 -14.173 -26.182 6.959 1.00 62.65 C
ANISOU 2384 CE1 HIS A 230 8282 8153 7369 -131 54 235 C
ATOM 2385 NE2 HIS A 230 -15.337 -25.944 7.558 1.00 61.65 N
ANISOU 2385 NE2 HIS A 230 8148 8054 7221 -142 36 236 N
ATOM 2386 N ALA A 231 -14.573 -26.500 12.778 1.00 45.97 N
ANISOU 2386 N ALA A 231 6081 6117 5268 -201 -35 215 N
ATOM 2387 CA ALA A 231 -15.625 -25.766 13.484 1.00 44.77 C
ANISOU 2387 CA ALA A 231 5916 5995 5100 -208 -43 213 C
ATOM 2388 C ALA A 231 -15.031 -24.654 14.358 1.00 43.26 C
ANISOU 2388 C ALA A 231 5700 5802 4934 -204 -34 203 C
ATOM 2389 O ALA A 231 -15.630 -23.574 14.462 1.00 42.61 O
ANISOU 2389 O ALA A 231 5608 5734 4847 -198 -27 200 O
ATOM 2390 CB ALA A 231 -16.455 -26.718 14.329 1.00 45.01 C
ANISOU 2390 CB ALA A 231 5945 6052 5105 -230 -75 217 C
ATOM 2391 N ALA A 232 -13.859 -24.871 14.916 1.00 42.11 N
ANISOU 2391 N ALA A 232 5545 5637 4816 -206 -35 199 N
ATOM 2392 CA ALA A 232 -13.226 -23.862 15.747 1.00 40.85 C
ANISOU 2392 CA ALA A 232 5363 5473 4684 -202 -29 190 C
ATOM 2393 C ALA A 232 -12.729 -22.690 14.915 1.00 39.91 C
ANISOU 2393 C ALA A 232 5244 5336 4585 -181 1 188 C
ATOM 2394 O ALA A 232 -12.769 -21.580 15.358 1.00 38.95 O
ANISOU 2394 O ALA A 232 5106 5219 4472 -175 7 183 O
ATOM 2395 CB ALA A 232 -12.115 -24.434 16.585 1.00 41.03 C
ANISOU 2395 CB ALA A 232 5378 5478 4733 -211 -40 186 C
ATOM 2396 N LYS A 233 -12.242 -22.978 13.721 1.00 40.22 N
ANISOU 2396 N LYS A 233 5300 5353 4630 -170 19 193 N
ATOM 2397 CA LYS A 233 -11.785 -21.959 12.790 1.00 40.82 C
ANISOU 2397 CA LYS A 233 5378 5411 4722 -150 48 193 C
ATOM 2398 C LYS A 233 -12.979 -21.125 12.319 1.00 39.41 C
ANISOU 2398 C LYS A 233 5204 5253 4519 -144 53 194 C
ATOM 2399 O LYS A 233 -12.864 -19.911 12.205 1.00 38.94 O
ANISOU 2399 O LYS A 233 5134 5189 4471 -133 67 190 O
ATOM 2400 CB LYS A 233 -11.089 -22.585 11.583 1.00 44.74 C
ANISOU 2400 CB LYS A 233 5893 5881 5226 -140 66 198 C
ATOM 2401 CG LYS A 233 -9.665 -23.019 11.854 1.00 52.08 C
ANISOU 2401 CG LYS A 233 6816 6783 6189 -140 70 195 C
ATOM 2402 CD LYS A 233 -8.968 -23.442 10.566 1.00 58.91 C
ANISOU 2402 CD LYS A 233 7699 7623 7062 -127 92 199 C
ATOM 2403 CE LYS A 233 -7.673 -24.173 10.826 1.00 64.12 C
ANISOU 2403 CE LYS A 233 8354 8259 7752 -129 91 196 C
ATOM 2404 NZ LYS A 233 -7.174 -24.862 9.594 1.00 67.06 N
ANISOU 2404 NZ LYS A 233 8746 8610 8123 -118 107 200 N
ATOM 2405 N SER A 234 -14.119 -21.769 12.035 1.00 38.45 N
ANISOU 2405 N SER A 234 5096 5150 4363 -152 40 199 N
ATOM 2406 CA SER A 234 -15.333 -21.054 11.641 1.00 37.29 C
ANISOU 2406 CA SER A 234 4953 5023 4192 -149 41 199 C
ATOM 2407 C SER A 234 -15.779 -20.077 12.745 1.00 35.94 C
ANISOU 2407 C SER A 234 4758 4874 4022 -152 32 191 C
ATOM 2408 O SER A 234 -16.038 -18.912 12.456 1.00 36.10 O
ANISOU 2408 O SER A 234 4774 4898 4046 -141 43 187 O
ATOM 2409 CB SER A 234 -16.452 -22.042 11.344 1.00 38.47 C
ANISOU 2409 CB SER A 234 5120 5190 4307 -159 24 206 C
ATOM 2410 OG SER A 234 -16.071 -22.809 10.216 1.00 41.92 O
ANISOU 2410 OG SER A 234 5580 5604 4742 -152 34 213 O
ATOM 2411 N ALA A 235 -15.753 -20.513 13.990 1.00 33.93 N
ANISOU 2411 N ALA A 235 4489 4634 3769 -167 11 188 N
ATOM 2412 CA ALA A 235 -16.111 -19.671 15.083 1.00 32.23 C
ANISOU 2412 CA ALA A 235 4252 4439 3554 -170 2 180 C
ATOM 2413 C ALA A 235 -15.108 -18.532 15.262 1.00 31.35 C
ANISOU 2413 C ALA A 235 4125 4309 3477 -156 17 174 C
ATOM 2414 O ALA A 235 -15.513 -17.430 15.456 1.00 30.36 O
ANISOU 2414 O ALA A 235 3989 4196 3352 -149 19 169 O
ATOM 2415 CB ALA A 235 -16.259 -20.483 16.333 1.00 32.65 C
ANISOU 2415 CB ALA A 235 4295 4510 3600 -189 -23 179 C
ATOM 2416 N ALA A 236 -13.829 -18.807 15.103 1.00 31.62 N
ANISOU 2416 N ALA A 236 4161 4314 3541 -151 27 176 N
ATOM 2417 CA ALA A 236 -12.796 -17.808 15.239 1.00 31.85 C
ANISOU 2417 CA ALA A 236 4176 4323 3604 -138 42 172 C
ATOM 2418 C ALA A 236 -12.888 -16.709 14.187 1.00 31.56 C
ANISOU 2418 C ALA A 236 4143 4277 3570 -121 64 172 C
ATOM 2419 O ALA A 236 -12.581 -15.588 14.436 1.00 31.04 O
ANISOU 2419 O ALA A 236 4063 4207 3522 -111 69 168 O
ATOM 2420 CB ALA A 236 -11.431 -18.440 15.217 1.00 32.55 C
ANISOU 2420 CB ALA A 236 4265 4379 3722 -138 48 173 C
ATOM 2421 N ILE A 237 -13.301 -17.086 13.004 1.00 31.11 N
ANISOU 2421 N ILE A 237 4108 4217 3495 -118 75 178 N
ATOM 2422 CA ILE A 237 -13.454 -16.161 11.917 1.00 31.13 C
ANISOU 2422 CA ILE A 237 4119 4210 3497 -103 95 179 C
ATOM 2423 C ILE A 237 -14.540 -15.136 12.253 1.00 29.22 C
ANISOU 2423 C ILE A 237 3868 3995 3239 -102 85 172 C
ATOM 2424 O ILE A 237 -14.365 -13.995 12.035 1.00 28.35 O
ANISOU 2424 O ILE A 237 3751 3879 3141 -91 95 169 O
ATOM 2425 CB ILE A 237 -13.735 -16.887 10.608 1.00 32.95 C
ANISOU 2425 CB ILE A 237 4377 4432 3710 -101 106 186 C
ATOM 2426 CG1 ILE A 237 -12.446 -17.470 10.044 1.00 35.18 C
ANISOU 2426 CG1 ILE A 237 4667 4683 4016 -95 123 191 C
ATOM 2427 CG2 ILE A 237 -14.365 -15.966 9.598 1.00 33.96 C
ANISOU 2427 CG2 ILE A 237 4516 4560 3826 -90 119 186 C
ATOM 2428 CD1 ILE A 237 -12.681 -18.466 8.951 1.00 37.75 C
ANISOU 2428 CD1 ILE A 237 5021 5001 4323 -95 129 198 C
ATOM 2429 N ILE A 238 -15.646 -15.610 12.804 1.00 28.19 N
ANISOU 2429 N ILE A 238 3738 3894 3081 -114 65 171 N
ATOM 2430 CA ILE A 238 -16.765 -14.808 13.240 1.00 27.67 C
ANISOU 2430 CA ILE A 238 3662 3856 2997 -115 53 164 C
ATOM 2431 C ILE A 238 -16.314 -13.765 14.282 1.00 26.64 C
ANISOU 2431 C ILE A 238 3505 3729 2887 -110 48 155 C
ATOM 2432 O ILE A 238 -16.658 -12.619 14.227 1.00 26.06 O
ANISOU 2432 O ILE A 238 3424 3662 2815 -101 50 149 O
ATOM 2433 CB ILE A 238 -17.858 -15.709 13.819 1.00 29.39 C
ANISOU 2433 CB ILE A 238 3881 4103 3183 -132 31 165 C
ATOM 2434 CG1 ILE A 238 -18.402 -16.663 12.757 1.00 32.39 C
ANISOU 2434 CG1 ILE A 238 4287 4479 3541 -135 34 173 C
ATOM 2435 CG2 ILE A 238 -18.957 -14.908 14.443 1.00 29.33 C
ANISOU 2435 CG2 ILE A 238 3860 4126 3158 -134 18 156 C
ATOM 2436 CD1 ILE A 238 -19.092 -16.012 11.615 1.00 33.27 C
ANISOU 2436 CD1 ILE A 238 4413 4588 3639 -125 46 173 C
ATOM 2437 N ALA A 239 -15.524 -14.210 15.221 1.00 25.91 N
ANISOU 2437 N ALA A 239 3401 3630 2813 -117 40 155 N
ATOM 2438 CA ALA A 239 -15.003 -13.346 16.245 1.00 25.56 C
ANISOU 2438 CA ALA A 239 3335 3587 2792 -112 34 149 C
ATOM 2439 C ALA A 239 -14.012 -12.330 15.662 1.00 25.43 C
ANISOU 2439 C ALA A 239 3314 3542 2805 -95 53 149 C
ATOM 2440 O ALA A 239 -14.012 -11.215 16.018 1.00 24.33 O
ANISOU 2440 O ALA A 239 3160 3406 2676 -86 51 144 O
ATOM 2441 CB ALA A 239 -14.377 -14.162 17.339 1.00 24.74 C
ANISOU 2441 CB ALA A 239 3221 3479 2699 -124 20 149 C
ATOM 2442 N GLY A 240 -13.201 -12.773 14.718 1.00 26.68 N
ANISOU 2442 N GLY A 240 3487 3673 2978 -90 72 156 N
ATOM 2443 CA GLY A 240 -12.231 -11.937 14.074 1.00 27.41 C
ANISOU 2443 CA GLY A 240 3577 3738 3099 -75 92 159 C
ATOM 2444 C GLY A 240 -12.918 -10.858 13.282 1.00 27.11 C
ANISOU 2444 C GLY A 240 3544 3707 3050 -65 100 156 C
ATOM 2445 O GLY A 240 -12.498 -9.752 13.288 1.00 27.23 O
ANISOU 2445 O GLY A 240 3548 3713 3084 -54 105 154 O
ATOM 2446 N LEU A 241 -13.982 -11.233 12.608 1.00 25.68 N
ANISOU 2446 N LEU A 241 3379 3540 2836 -69 99 157 N
ATOM 2447 CA LEU A 241 -14.784 -10.328 11.809 1.00 25.41 C
ANISOU 2447 CA LEU A 241 3354 3514 2788 -62 104 154 C
ATOM 2448 C LEU A 241 -15.453 -9.234 12.653 1.00 23.12 C
ANISOU 2448 C LEU A 241 3044 3247 2493 -59 86 144 C
ATOM 2449 O LEU A 241 -15.540 -8.136 12.241 1.00 23.35 O
ANISOU 2449 O LEU A 241 3072 3274 2528 -49 91 140 O
ATOM 2450 CB LEU A 241 -15.824 -11.078 11.018 1.00 25.73 C
ANISOU 2450 CB LEU A 241 3416 3564 2794 -68 103 157 C
ATOM 2451 CG LEU A 241 -15.354 -11.793 9.750 1.00 29.49 C
ANISOU 2451 CG LEU A 241 3918 4016 3271 -65 124 166 C
ATOM 2452 CD1 LEU A 241 -16.474 -12.538 9.107 1.00 28.95 C
ANISOU 2452 CD1 LEU A 241 3872 3960 3170 -72 119 169 C
ATOM 2453 CD2 LEU A 241 -14.635 -10.891 8.770 1.00 31.40 C
ANISOU 2453 CD2 LEU A 241 4165 4232 3532 -51 147 169 C
ATOM 2454 N PHE A 242 -15.915 -9.603 13.831 1.00 21.04 N
ANISOU 2454 N PHE A 242 2767 3007 2219 -69 66 139 N
ATOM 2455 CA PHE A 242 -16.501 -8.670 14.774 1.00 19.65 C
ANISOU 2455 CA PHE A 242 2572 2856 2040 -67 48 129 C
ATOM 2456 C PHE A 242 -15.453 -7.626 15.153 1.00 19.59 C
ANISOU 2456 C PHE A 242 2546 2829 2066 -54 51 127 C
ATOM 2457 O PHE A 242 -15.720 -6.478 15.159 1.00 18.90 O
ANISOU 2457 O PHE A 242 2451 2748 1981 -44 47 121 O
ATOM 2458 CB PHE A 242 -17.048 -9.396 16.007 1.00 18.14 C
ANISOU 2458 CB PHE A 242 2370 2691 1832 -81 28 126 C
ATOM 2459 CG PHE A 242 -17.588 -8.481 17.058 1.00 18.63 C
ANISOU 2459 CG PHE A 242 2410 2777 1890 -78 10 115 C
ATOM 2460 CD1 PHE A 242 -16.756 -7.853 17.925 1.00 19.97 C
ANISOU 2460 CD1 PHE A 242 2563 2939 2087 -71 4 112 C
ATOM 2461 CD2 PHE A 242 -18.926 -8.244 17.155 1.00 18.76 C
ANISOU 2461 CD2 PHE A 242 2426 2825 1877 -81 -2 107 C
ATOM 2462 CE1 PHE A 242 -17.248 -7.015 18.882 1.00 20.24 C
ANISOU 2462 CE1 PHE A 242 2577 2995 2116 -66 -13 102 C
ATOM 2463 CE2 PHE A 242 -19.428 -7.400 18.104 1.00 19.45 C
ANISOU 2463 CE2 PHE A 242 2494 2937 1961 -77 -19 96 C
ATOM 2464 CZ PHE A 242 -18.581 -6.791 18.976 1.00 19.40 C
ANISOU 2464 CZ PHE A 242 2470 2922 1980 -70 -24 94 C
ATOM 2465 N ALA A 243 -14.252 -8.080 15.441 1.00 20.45 N
ANISOU 2465 N ALA A 243 2652 2915 2202 -54 58 133 N
ATOM 2466 CA ALA A 243 -13.153 -7.210 15.790 1.00 22.22 C
ANISOU 2466 CA ALA A 243 2862 3120 2463 -42 61 134 C
ATOM 2467 C ALA A 243 -12.810 -6.267 14.633 1.00 23.65 C
ANISOU 2467 C ALA A 243 3049 3282 2657 -29 79 137 C
ATOM 2468 O ALA A 243 -12.678 -5.113 14.807 1.00 23.63 O
ANISOU 2468 O ALA A 243 3035 3278 2667 -18 74 133 O
ATOM 2469 CB ALA A 243 -11.951 -8.011 16.206 1.00 23.10 C
ANISOU 2469 CB ALA A 243 2969 3207 2600 -46 66 140 C
ATOM 2470 N LEU A 244 -12.720 -6.807 13.445 1.00 24.29 N
ANISOU 2470 N LEU A 244 3151 3348 2731 -30 98 143 N
ATOM 2471 CA LEU A 244 -12.412 -6.035 12.267 1.00 25.75 C
ANISOU 2471 CA LEU A 244 3345 3514 2925 -19 117 147 C
ATOM 2472 C LEU A 244 -13.463 -4.956 11.964 1.00 24.77 C
ANISOU 2472 C LEU A 244 3222 3409 2782 -14 108 139 C
ATOM 2473 O LEU A 244 -13.138 -3.872 11.605 1.00 25.07 O
ANISOU 2473 O LEU A 244 3255 3436 2834 -3 112 139 O
ATOM 2474 CB LEU A 244 -12.286 -6.976 11.090 1.00 28.32 C
ANISOU 2474 CB LEU A 244 3695 3824 3240 -23 137 155 C
ATOM 2475 CG LEU A 244 -11.750 -6.432 9.773 1.00 34.79 C
ANISOU 2475 CG LEU A 244 4528 4620 4071 -13 162 161 C
ATOM 2476 CD1 LEU A 244 -10.312 -6.016 9.969 1.00 37.73 C
ANISOU 2476 CD1 LEU A 244 4886 4965 4483 -5 173 167 C
ATOM 2477 CD2 LEU A 244 -11.894 -7.404 8.617 1.00 37.03 C
ANISOU 2477 CD2 LEU A 244 4839 4894 4338 -16 179 168 C
ATOM 2478 N CYS A 245 -14.724 -5.300 12.109 1.00 22.36 N
ANISOU 2478 N CYS A 245 2922 3130 2443 -22 95 133 N
ATOM 2479 CA CYS A 245 -15.794 -4.381 11.845 1.00 21.91 C
ANISOU 2479 CA CYS A 245 2867 3092 2368 -18 85 124 C
ATOM 2480 C CYS A 245 -15.949 -3.273 12.880 1.00 20.46 C
ANISOU 2480 C CYS A 245 2658 2924 2192 -12 64 114 C
ATOM 2481 O CYS A 245 -16.303 -2.204 12.557 1.00 19.94 O
ANISOU 2481 O CYS A 245 2590 2861 2125 -4 59 108 O
ATOM 2482 CB CYS A 245 -17.108 -5.109 11.668 1.00 22.68 C
ANISOU 2482 CB CYS A 245 2977 3213 2428 -29 77 120 C
ATOM 2483 SG CYS A 245 -17.222 -6.091 10.177 1.00 27.73 S
ANISOU 2483 SG CYS A 245 3650 3834 3052 -33 98 130 S
ATOM 2484 N TRP A 246 -15.672 -3.570 14.129 1.00 18.60 N
ANISOU 2484 N TRP A 246 2405 2698 1964 -15 51 112 N
ATOM 2485 CA TRP A 246 -15.819 -2.613 15.202 1.00 18.83 C
ANISOU 2485 CA TRP A 246 2411 2743 2001 -8 30 103 C
ATOM 2486 C TRP A 246 -14.601 -1.780 15.540 1.00 20.01 C
ANISOU 2486 C TRP A 246 2546 2869 2188 4 31 106 C
ATOM 2487 O TRP A 246 -14.745 -0.689 15.986 1.00 19.55 O
ANISOU 2487 O TRP A 246 2473 2819 2135 14 16 99 O
ATOM 2488 CB TRP A 246 -16.336 -3.293 16.456 1.00 17.87 C
ANISOU 2488 CB TRP A 246 2278 2647 1864 -18 13 98 C
ATOM 2489 CG TRP A 246 -17.789 -3.540 16.461 1.00 18.06 C
ANISOU 2489 CG TRP A 246 2308 2704 1851 -27 2 90 C
ATOM 2490 CD1 TRP A 246 -18.392 -4.668 16.139 1.00 19.41 C
ANISOU 2490 CD1 TRP A 246 2493 2883 1998 -40 6 93 C
ATOM 2491 CD2 TRP A 246 -18.806 -2.627 16.815 1.00 17.83 C
ANISOU 2491 CD2 TRP A 246 2268 2702 1806 -22 -15 77 C
ATOM 2492 NE1 TRP A 246 -19.720 -4.549 16.261 1.00 19.89 N
ANISOU 2492 NE1 TRP A 246 2554 2975 2030 -44 -7 84 N
ATOM 2493 CE2 TRP A 246 -20.011 -3.288 16.668 1.00 19.21 C
ANISOU 2493 CE2 TRP A 246 2452 2901 1947 -33 -20 73 C
ATOM 2494 CE3 TRP A 246 -18.821 -1.307 17.222 1.00 17.56 C
ANISOU 2494 CE3 TRP A 246 2217 2673 1781 -9 -29 67 C
ATOM 2495 CZ2 TRP A 246 -21.220 -2.686 16.933 1.00 18.64 C
ANISOU 2495 CZ2 TRP A 246 2372 2858 1852 -32 -36 60 C
ATOM 2496 CZ3 TRP A 246 -20.020 -0.710 17.480 1.00 18.03 C
ANISOU 2496 CZ3 TRP A 246 2271 2763 1818 -7 -46 54 C
ATOM 2497 CH2 TRP A 246 -21.203 -1.399 17.332 1.00 18.14 C
ANISOU 2497 CH2 TRP A 246 2292 2800 1799 -19 -48 50 C
ATOM 2498 N LEU A 247 -13.418 -2.331 15.351 1.00 20.85 N
ANISOU 2498 N LEU A 247 2655 2947 2319 4 47 117 N
ATOM 2499 CA LEU A 247 -12.191 -1.630 15.675 1.00 22.10 C
ANISOU 2499 CA LEU A 247 2800 3081 2516 15 48 122 C
ATOM 2500 C LEU A 247 -12.006 -0.211 15.132 1.00 22.35 C
ANISOU 2500 C LEU A 247 2827 3104 2562 29 48 121 C
ATOM 2501 O LEU A 247 -11.614 0.625 15.856 1.00 23.38 O
ANISOU 2501 O LEU A 247 2940 3232 2712 39 34 119 O
ATOM 2502 CB LEU A 247 -10.965 -2.462 15.394 1.00 24.35 C
ANISOU 2502 CB LEU A 247 3090 3335 2825 12 68 134 C
ATOM 2503 CG LEU A 247 -10.484 -3.373 16.491 1.00 28.74 C
ANISOU 2503 CG LEU A 247 3637 3890 3392 4 60 134 C
ATOM 2504 CD1 LEU A 247 -9.425 -4.318 15.973 1.00 30.49 C
ANISOU 2504 CD1 LEU A 247 3868 4083 3633 0 81 145 C
ATOM 2505 CD2 LEU A 247 -9.938 -2.560 17.620 1.00 29.76 C
ANISOU 2505 CD2 LEU A 247 3745 4015 3547 13 42 132 C
ATOM 2506 N PRO A 248 -12.289 0.030 13.854 1.00 21.78 N
ANISOU 2506 N PRO A 248 2772 3026 2479 30 63 123 N
ATOM 2507 CA PRO A 248 -12.140 1.368 13.292 1.00 21.66 C
ANISOU 2507 CA PRO A 248 2753 3001 2475 42 62 123 C
ATOM 2508 C PRO A 248 -12.905 2.427 14.094 1.00 19.78 C
ANISOU 2508 C PRO A 248 2499 2787 2229 49 33 110 C
ATOM 2509 O PRO A 248 -12.364 3.432 14.388 1.00 20.08 O
ANISOU 2509 O PRO A 248 2523 2816 2289 61 23 110 O
ATOM 2510 CB PRO A 248 -12.672 1.211 11.878 1.00 22.64 C
ANISOU 2510 CB PRO A 248 2902 3121 2578 38 79 124 C
ATOM 2511 CG PRO A 248 -12.486 -0.193 11.572 1.00 23.10 C
ANISOU 2511 CG PRO A 248 2975 3173 2630 28 97 131 C
ATOM 2512 CD PRO A 248 -12.722 -0.921 12.841 1.00 21.78 C
ANISOU 2512 CD PRO A 248 2795 3024 2456 21 81 127 C
ATOM 2513 N LEU A 249 -14.149 2.150 14.433 1.00 19.41 N
ANISOU 2513 N LEU A 249 2454 2771 2150 43 19 99 N
ATOM 2514 CA LEU A 249 -14.975 3.053 15.218 1.00 19.09 C
ANISOU 2514 CA LEU A 249 2398 2757 2098 49 -8 85 C
ATOM 2515 C LEU A 249 -14.367 3.288 16.614 1.00 18.44 C
ANISOU 2515 C LEU A 249 2293 2677 2037 55 -25 84 C
ATOM 2516 O LEU A 249 -14.277 4.373 17.044 1.00 18.55 O
ANISOU 2516 O LEU A 249 2292 2692 2062 67 -43 79 O
ATOM 2517 CB LEU A 249 -16.409 2.571 15.320 1.00 18.68 C
ANISOU 2517 CB LEU A 249 2353 2739 2008 39 -17 74 C
ATOM 2518 CG LEU A 249 -17.430 3.533 15.896 1.00 20.16 C
ANISOU 2518 CG LEU A 249 2527 2955 2179 45 -43 57 C
ATOM 2519 CD1 LEU A 249 -17.345 4.921 15.320 1.00 21.81 C
ANISOU 2519 CD1 LEU A 249 2733 3154 2398 58 -51 53 C
ATOM 2520 CD2 LEU A 249 -18.848 3.013 15.842 1.00 19.93 C
ANISOU 2520 CD2 LEU A 249 2505 2956 2112 35 -49 47 C
ATOM 2521 N HIS A 250 -13.956 2.236 17.268 1.00 17.46 N
ANISOU 2521 N HIS A 250 2166 2549 1917 47 -21 89 N
ATOM 2522 CA HIS A 250 -13.324 2.378 18.553 1.00 18.55 C
ANISOU 2522 CA HIS A 250 2286 2686 2077 52 -36 89 C
ATOM 2523 C HIS A 250 -12.027 3.187 18.472 1.00 19.93 C
ANISOU 2523 C HIS A 250 2452 2829 2293 66 -33 98 C
ATOM 2524 O HIS A 250 -11.785 4.007 19.290 1.00 20.88 O
ANISOU 2524 O HIS A 250 2556 2950 2428 77 -53 95 O
ATOM 2525 CB HIS A 250 -13.070 1.035 19.162 1.00 18.22 C
ANISOU 2525 CB HIS A 250 2247 2644 2033 39 -30 93 C
ATOM 2526 CG HIS A 250 -14.291 0.369 19.684 1.00 18.73 C
ANISOU 2526 CG HIS A 250 2313 2743 2061 27 -41 84 C
ATOM 2527 ND1 HIS A 250 -15.042 0.886 20.701 1.00 20.42 N
ANISOU 2527 ND1 HIS A 250 2512 2986 2260 31 -65 72 N
ATOM 2528 CD2 HIS A 250 -14.890 -0.777 19.327 1.00 19.62 C
ANISOU 2528 CD2 HIS A 250 2440 2867 2148 12 -31 86 C
ATOM 2529 CE1 HIS A 250 -16.052 0.092 20.946 1.00 20.47 C
ANISOU 2529 CE1 HIS A 250 2523 3019 2234 18 -68 67 C
ATOM 2530 NE2 HIS A 250 -15.979 -0.931 20.129 1.00 20.61 N
ANISOU 2530 NE2 HIS A 250 2558 3026 2245 6 -49 75 N
ATOM 2531 N ILE A 251 -11.232 2.938 17.449 1.00 19.61 N
ANISOU 2531 N ILE A 251 2423 2759 2268 65 -9 110 N
ATOM 2532 CA ILE A 251 -9.983 3.644 17.219 1.00 20.15 C
ANISOU 2532 CA ILE A 251 2485 2796 2376 76 -3 120 C
ATOM 2533 C ILE A 251 -10.231 5.129 17.011 1.00 20.02 C
ANISOU 2533 C ILE A 251 2460 2784 2364 90 -19 116 C
ATOM 2534 O ILE A 251 -9.532 5.930 17.532 1.00 20.24 O
ANISOU 2534 O ILE A 251 2473 2799 2419 102 -31 119 O
ATOM 2535 CB ILE A 251 -9.131 3.009 16.098 1.00 22.63 C
ANISOU 2535 CB ILE A 251 2813 3081 2704 71 29 134 C
ATOM 2536 CG1 ILE A 251 -8.578 1.678 16.574 1.00 23.77 C
ANISOU 2536 CG1 ILE A 251 2959 3216 2856 61 38 138 C
ATOM 2537 CG2 ILE A 251 -8.006 3.937 15.653 1.00 24.00 C
ANISOU 2537 CG2 ILE A 251 2979 3224 2914 84 36 144 C
ATOM 2538 CD1 ILE A 251 -8.295 0.697 15.492 1.00 25.56 C
ANISOU 2538 CD1 ILE A 251 3205 3428 3077 52 67 146 C
ATOM 2539 N ILE A 252 -11.262 5.463 16.257 1.00 19.85 N
ANISOU 2539 N ILE A 252 2449 2779 2312 87 -19 108 N
ATOM 2540 CA ILE A 252 -11.649 6.826 16.025 1.00 20.84 C
ANISOU 2540 CA ILE A 252 2569 2912 2438 99 -37 101 C
ATOM 2541 C ILE A 252 -12.012 7.493 17.355 1.00 20.75 C
ANISOU 2541 C ILE A 252 2536 2921 2425 108 -69 90 C
ATOM 2542 O ILE A 252 -11.624 8.564 17.596 1.00 22.13 O
ANISOU 2542 O ILE A 252 2700 3089 2621 121 -85 91 O
ATOM 2543 CB ILE A 252 -12.752 6.975 14.980 1.00 22.05 C
ANISOU 2543 CB ILE A 252 2740 3080 2559 93 -32 93 C
ATOM 2544 CG1 ILE A 252 -12.232 6.629 13.588 1.00 24.35 C
ANISOU 2544 CG1 ILE A 252 3051 3346 2855 88 -2 105 C
ATOM 2545 CG2 ILE A 252 -13.285 8.373 15.011 1.00 22.66 C
ANISOU 2545 CG2 ILE A 252 2808 3169 2632 104 -57 83 C
ATOM 2546 CD1 ILE A 252 -13.320 6.486 12.570 1.00 26.12 C
ANISOU 2546 CD1 ILE A 252 3296 3582 3046 80 5 98 C
ATOM 2547 N ASN A 253 -12.751 6.800 18.198 1.00 19.34 N
ANISOU 2547 N ASN A 253 2355 2768 2224 101 -78 81 N
ATOM 2548 CA ASN A 253 -13.097 7.300 19.502 1.00 19.27 C
ANISOU 2548 CA ASN A 253 2328 2780 2214 109 -107 71 C
ATOM 2549 C ASN A 253 -11.807 7.572 20.315 1.00 20.98 C
ANISOU 2549 C ASN A 253 2530 2971 2470 120 -114 81 C
ATOM 2550 O ASN A 253 -11.718 8.530 20.992 1.00 22.66 O
ANISOU 2550 O ASN A 253 2728 3187 2695 134 -138 76 O
ATOM 2551 CB ASN A 253 -14.047 6.350 20.225 1.00 18.43 C
ANISOU 2551 CB ASN A 253 2222 2704 2076 97 -111 62 C
ATOM 2552 CG ASN A 253 -15.460 6.345 19.634 1.00 20.03 C
ANISOU 2552 CG ASN A 253 2435 2935 2240 90 -113 49 C
ATOM 2553 OD1 ASN A 253 -15.830 7.215 18.919 1.00 21.46 O
ANISOU 2553 OD1 ASN A 253 2620 3118 2418 97 -117 44 O
ATOM 2554 ND2 ASN A 253 -16.217 5.355 19.962 1.00 18.60 N
ANISOU 2554 ND2 ASN A 253 2259 2777 2033 77 -110 45 N
ATOM 2555 N CYS A 254 -10.826 6.707 20.220 1.00 20.28 N
ANISOU 2555 N CYS A 254 2447 2857 2403 113 -94 94 N
ATOM 2556 CA CYS A 254 -9.561 6.901 20.895 1.00 21.06 C
ANISOU 2556 CA CYS A 254 2533 2928 2542 122 -99 104 C
ATOM 2557 C CYS A 254 -8.868 8.223 20.455 1.00 22.88 C
ANISOU 2557 C CYS A 254 2755 3136 2801 139 -105 110 C
ATOM 2558 O CYS A 254 -8.422 8.962 21.255 1.00 24.03 O
ANISOU 2558 O CYS A 254 2886 3275 2968 152 -127 111 O
ATOM 2559 CB CYS A 254 -8.685 5.640 20.781 1.00 21.00 C
ANISOU 2559 CB CYS A 254 2533 2896 2549 111 -74 115 C
ATOM 2560 SG CYS A 254 -9.258 4.164 21.646 1.00 23.12 S
ANISOU 2560 SG CYS A 254 2806 3186 2792 93 -75 109 S
ATOM 2561 N PHE A 255 -8.844 8.491 19.163 1.00 22.87 N
ANISOU 2561 N PHE A 255 2766 3126 2798 137 -88 115 N
ATOM 2562 CA PHE A 255 -8.267 9.708 18.611 1.00 24.35 C
ANISOU 2562 CA PHE A 255 2948 3295 3010 149 -93 122 C
ATOM 2563 C PHE A 255 -8.999 10.952 19.135 1.00 24.64 C
ANISOU 2563 C PHE A 255 2972 3353 3036 163 -128 110 C
ATOM 2564 O PHE A 255 -8.391 11.847 19.600 1.00 26.70 O
ANISOU 2564 O PHE A 255 3220 3602 3324 177 -147 114 O
ATOM 2565 CB PHE A 255 -8.230 9.660 17.081 1.00 24.74 C
ANISOU 2565 CB PHE A 255 3014 3332 3052 142 -67 129 C
ATOM 2566 CG PHE A 255 -7.005 8.998 16.516 1.00 26.78 C
ANISOU 2566 CG PHE A 255 3279 3558 3339 138 -37 146 C
ATOM 2567 CD1 PHE A 255 -5.858 9.717 16.308 1.00 28.85 C
ANISOU 2567 CD1 PHE A 255 3532 3790 3639 148 -35 159 C
ATOM 2568 CD2 PHE A 255 -7.004 7.668 16.211 1.00 28.20 C
ANISOU 2568 CD2 PHE A 255 3472 3736 3507 124 -12 148 C
ATOM 2569 CE1 PHE A 255 -4.737 9.116 15.805 1.00 31.59 C
ANISOU 2569 CE1 PHE A 255 3883 4107 4013 144 -7 174 C
ATOM 2570 CE2 PHE A 255 -5.893 7.056 15.703 1.00 30.26 C
ANISOU 2570 CE2 PHE A 255 3737 3966 3793 120 15 162 C
ATOM 2571 CZ PHE A 255 -4.757 7.790 15.481 1.00 31.45 C
ANISOU 2571 CZ PHE A 255 3879 4088 3982 130 18 175 C
ATOM 2572 N THR A 256 -10.316 10.946 19.079 1.00 23.39 N
ANISOU 2572 N THR A 256 2820 3228 2840 158 -137 94 N
ATOM 2573 CA THR A 256 -11.173 12.003 19.577 1.00 24.00 C
ANISOU 2573 CA THR A 256 2886 3330 2902 169 -169 79 C
ATOM 2574 C THR A 256 -10.855 12.296 21.052 1.00 24.50 C
ANISOU 2574 C THR A 256 2931 3397 2982 182 -196 77 C
ATOM 2575 O THR A 256 -10.682 13.411 21.426 1.00 26.21 O
ANISOU 2575 O THR A 256 3135 3611 3212 198 -221 75 O
ATOM 2576 CB THR A 256 -12.661 11.615 19.437 1.00 24.86 C
ANISOU 2576 CB THR A 256 3004 3475 2966 159 -171 62 C
ATOM 2577 OG1 THR A 256 -13.018 11.458 18.067 1.00 27.05 O
ANISOU 2577 OG1 THR A 256 3300 3749 3229 149 -150 64 O
ATOM 2578 CG2 THR A 256 -13.540 12.630 20.048 1.00 24.35 C
ANISOU 2578 CG2 THR A 256 2927 3438 2887 171 -205 45 C
ATOM 2579 N PHE A 257 -10.763 11.252 21.843 1.00 23.49 N
ANISOU 2579 N PHE A 257 2803 3273 2851 174 -189 77 N
ATOM 2580 CA PHE A 257 -10.495 11.337 23.266 1.00 24.96 C
ANISOU 2580 CA PHE A 257 2973 3462 3049 183 -211 75 C
ATOM 2581 C PHE A 257 -9.054 11.664 23.660 1.00 27.51 C
ANISOU 2581 C PHE A 257 3287 3747 3418 194 -215 90 C
ATOM 2582 O PHE A 257 -8.837 12.584 24.366 1.00 28.91 O
ANISOU 2582 O PHE A 257 3451 3923 3611 211 -242 89 O
ATOM 2583 CB PHE A 257 -10.910 10.039 23.929 1.00 23.59 C
ANISOU 2583 CB PHE A 257 2804 3305 2854 168 -202 70 C
ATOM 2584 CG PHE A 257 -10.719 10.016 25.412 1.00 24.83 C
ANISOU 2584 CG PHE A 257 2948 3466 3020 176 -224 67 C
ATOM 2585 CD1 PHE A 257 -11.370 10.899 26.203 1.00 24.97 C
ANISOU 2585 CD1 PHE A 257 2953 3507 3025 189 -255 54 C
ATOM 2586 CD2 PHE A 257 -9.895 9.086 26.001 1.00 25.61 C
ANISOU 2586 CD2 PHE A 257 3048 3545 3138 169 -215 76 C
ATOM 2587 CE1 PHE A 257 -11.218 10.865 27.559 1.00 26.08 C
ANISOU 2587 CE1 PHE A 257 3084 3653 3173 197 -274 50 C
ATOM 2588 CE2 PHE A 257 -9.725 9.056 27.356 1.00 26.77 C
ANISOU 2588 CE2 PHE A 257 3185 3695 3292 175 -235 72 C
ATOM 2589 CZ PHE A 257 -10.386 9.953 28.132 1.00 26.98 C
ANISOU 2589 CZ PHE A 257 3200 3745 3306 189 -265 60 C
ATOM 2590 N PHE A 258 -8.105 10.874 23.197 1.00 28.02 N
ANISOU 2590 N PHE A 258 3359 3783 3504 185 -188 105 N
ATOM 2591 CA PHE A 258 -6.707 11.033 23.530 1.00 29.74 C
ANISOU 2591 CA PHE A 258 3569 3964 3768 194 -189 120 C
ATOM 2592 C PHE A 258 -5.982 12.169 22.850 1.00 33.22 C
ANISOU 2592 C PHE A 258 4005 4380 4239 207 -192 131 C
ATOM 2593 O PHE A 258 -5.021 12.615 23.343 1.00 34.20 O
ANISOU 2593 O PHE A 258 4117 4478 4398 219 -204 141 O
ATOM 2594 CB PHE A 258 -5.941 9.740 23.302 1.00 28.88 C
ANISOU 2594 CB PHE A 258 3468 3831 3672 180 -159 130 C
ATOM 2595 CG PHE A 258 -6.269 8.659 24.275 1.00 28.45 C
ANISOU 2595 CG PHE A 258 3416 3791 3603 169 -161 123 C
ATOM 2596 CD1 PHE A 258 -6.198 8.880 25.635 1.00 29.19 C
ANISOU 2596 CD1 PHE A 258 3498 3888 3704 178 -187 118 C
ATOM 2597 CD2 PHE A 258 -6.646 7.420 23.839 1.00 27.82 C
ANISOU 2597 CD2 PHE A 258 3350 3720 3500 150 -137 121 C
ATOM 2598 CE1 PHE A 258 -6.500 7.883 26.527 1.00 29.20 C
ANISOU 2598 CE1 PHE A 258 3502 3902 3691 167 -189 112 C
ATOM 2599 CE2 PHE A 258 -6.939 6.425 24.727 1.00 27.94 C
ANISOU 2599 CE2 PHE A 258 3367 3748 3501 139 -140 116 C
ATOM 2600 CZ PHE A 258 -6.879 6.657 26.067 1.00 27.88 C
ANISOU 2600 CZ PHE A 258 3348 3745 3501 147 -166 111 C
ATOM 2601 N CYS A 259 -6.461 12.616 21.712 1.00 35.10 N
ANISOU 2601 N CYS A 259 4250 4625 4460 204 -184 129 N
ATOM 2602 CA CYS A 259 -5.810 13.679 20.991 1.00 38.08 C
ANISOU 2602 CA CYS A 259 4624 4982 4863 215 -187 140 C
ATOM 2603 C CYS A 259 -6.684 14.866 20.736 1.00 38.91 C
ANISOU 2603 C CYS A 259 4726 5108 4949 224 -212 129 C
ATOM 2604 O CYS A 259 -7.103 15.078 19.652 1.00 38.36 O
ANISOU 2604 O CYS A 259 4668 5044 4864 217 -200 127 O
ATOM 2605 CB CYS A 259 -5.254 13.178 19.654 1.00 40.60 C
ANISOU 2605 CB CYS A 259 4957 5279 5189 203 -150 153 C
ATOM 2606 SG CYS A 259 -4.064 14.274 18.834 1.00 50.06 S
ANISOU 2606 SG CYS A 259 6150 6442 6429 213 -147 172 S
ATOM 2607 N PRO A 260 -6.858 15.731 21.724 1.00 40.22 N
ANISOU 2607 N PRO A 260 4878 5284 5121 240 -248 122 N
ATOM 2608 CA PRO A 260 -7.658 16.937 21.555 1.00 41.56 C
ANISOU 2608 CA PRO A 260 5043 5474 5274 250 -276 110 C
ATOM 2609 C PRO A 260 -7.061 17.990 20.610 1.00 44.69 C
ANISOU 2609 C PRO A 260 5439 5849 5693 257 -280 122 C
ATOM 2610 O PRO A 260 -7.794 18.850 20.206 1.00 45.70 O
ANISOU 2610 O PRO A 260 5568 5992 5802 261 -298 111 O
ATOM 2611 CB PRO A 260 -7.787 17.487 22.969 1.00 42.28 C
ANISOU 2611 CB PRO A 260 5118 5577 5370 268 -313 102 C
ATOM 2612 CG PRO A 260 -6.701 16.862 23.730 1.00 42.38 C
ANISOU 2612 CG PRO A 260 5126 5563 5415 269 -306 115 C
ATOM 2613 CD PRO A 260 -6.437 15.542 23.106 1.00 40.00 C
ANISOU 2613 CD PRO A 260 4838 5252 5110 249 -265 122 C
ATOM 2614 N ASP A 261 -5.774 17.909 20.291 1.00 45.41 N
ANISOU 2614 N ASP A 261 5529 5904 5822 258 -263 142 N
ATOM 2615 CA ASP A 261 -5.101 18.775 19.365 1.00 47.09 C
ANISOU 2615 CA ASP A 261 5741 6093 6057 262 -262 156 C
ATOM 2616 C ASP A 261 -5.233 18.308 17.932 1.00 46.36 C
ANISOU 2616 C ASP A 261 5667 5997 5950 245 -226 160 C
ATOM 2617 O ASP A 261 -4.860 19.012 17.026 1.00 47.36 O
ANISOU 2617 O ASP A 261 5797 6109 6088 246 -223 169 O
ATOM 2618 CB ASP A 261 -3.634 18.846 19.697 1.00 51.73 C
ANISOU 2618 CB ASP A 261 6318 6643 6694 270 -259 177 C
ATOM 2619 CG ASP A 261 -3.381 19.544 20.977 1.00 59.97 C
ANISOU 2619 CG ASP A 261 7344 7685 7758 290 -297 176 C
ATOM 2620 OD1 ASP A 261 -4.219 20.351 21.392 1.00 60.71 O
ANISOU 2620 OD1 ASP A 261 7432 7802 7832 300 -331 162 O
ATOM 2621 OD2 ASP A 261 -2.344 19.277 21.568 1.00 64.25 O
ANISOU 2621 OD2 ASP A 261 7878 8199 8334 295 -295 189 O
ATOM 2622 N CYS A 262 -5.719 17.098 17.749 1.00 44.38 N
ANISOU 2622 N CYS A 262 5430 5759 5674 230 -199 153 N
ATOM 2623 CA CYS A 262 -5.937 16.534 16.445 1.00 43.88 C
ANISOU 2623 CA CYS A 262 5387 5694 5594 214 -166 156 C
ATOM 2624 C CYS A 262 -7.328 16.947 15.971 1.00 42.44 C
ANISOU 2624 C CYS A 262 5214 5541 5370 210 -178 137 C
ATOM 2625 O CYS A 262 -8.258 17.016 16.737 1.00 41.23 O
ANISOU 2625 O CYS A 262 5056 5416 5195 213 -201 120 O
ATOM 2626 CB CYS A 262 -5.896 15.014 16.490 1.00 44.62 C
ANISOU 2626 CB CYS A 262 5489 5787 5677 199 -134 157 C
ATOM 2627 SG CYS A 262 -4.380 14.118 16.834 1.00 52.05 S
ANISOU 2627 SG CYS A 262 6424 6692 6659 198 -110 176 S
ATOM 2628 N SER A 263 -7.451 17.211 14.693 1.00 41.48 N
ANISOU 2628 N SER A 263 5107 5413 5240 202 -163 140 N
ATOM 2629 CA SER A 263 -8.727 17.540 14.162 1.00 40.49 C
ANISOU 2629 CA SER A 263 4993 5313 5078 197 -174 123 C
ATOM 2630 C SER A 263 -9.614 16.303 14.259 1.00 37.53 C
ANISOU 2630 C SER A 263 4630 4960 4670 184 -156 112 C
ATOM 2631 O SER A 263 -9.198 15.196 14.044 1.00 37.24 O
ANISOU 2631 O SER A 263 4602 4913 4636 174 -126 120 O
ATOM 2632 CB SER A 263 -8.633 17.973 12.708 1.00 44.05 C
ANISOU 2632 CB SER A 263 5460 5749 5526 190 -158 130 C
ATOM 2633 OG SER A 263 -8.430 19.350 12.598 1.00 50.07 O
ANISOU 2633 OG SER A 263 6214 6505 6304 201 -187 131 O
ATOM 2634 N HIS A 264 -10.880 16.528 14.512 1.00 34.73 N
ANISOU 2634 N HIS A 264 4276 4635 4283 184 -177 92 N
ATOM 2635 CA HIS A 264 -11.806 15.443 14.611 1.00 32.06 C
ANISOU 2635 CA HIS A 264 3948 4319 3912 172 -164 81 C
ATOM 2636 C HIS A 264 -11.906 14.774 13.277 1.00 31.82 C
ANISOU 2636 C HIS A 264 3942 4278 3869 157 -131 87 C
ATOM 2637 O HIS A 264 -11.943 15.421 12.265 1.00 32.87 O
ANISOU 2637 O HIS A 264 4087 4402 4002 156 -129 88 O
ATOM 2638 CB HIS A 264 -13.181 15.954 15.014 1.00 30.81 C
ANISOU 2638 CB HIS A 264 3787 4196 3724 175 -193 58 C
ATOM 2639 CG HIS A 264 -14.111 14.899 15.524 1.00 29.05 C
ANISOU 2639 CG HIS A 264 3567 4000 3470 165 -187 47 C
ATOM 2640 ND1 HIS A 264 -14.689 13.959 14.718 1.00 31.57 N
ANISOU 2640 ND1 HIS A 264 3906 4324 3766 150 -162 46 N
ATOM 2641 CD2 HIS A 264 -14.580 14.656 16.764 1.00 29.41 C
ANISOU 2641 CD2 HIS A 264 3599 4071 3507 169 -204 36 C
ATOM 2642 CE1 HIS A 264 -15.447 13.164 15.437 1.00 31.01 C
ANISOU 2642 CE1 HIS A 264 3833 4278 3672 144 -164 36 C
ATOM 2643 NE2 HIS A 264 -15.406 13.575 16.681 1.00 30.11 N
ANISOU 2643 NE2 HIS A 264 3698 4178 3566 155 -189 30 N
ATOM 2644 N ALA A 265 -12.003 13.460 13.294 1.00 30.77 N
ANISOU 2644 N ALA A 265 3818 4148 3724 146 -106 89 N
ATOM 2645 CA ALA A 265 -12.237 12.662 12.116 1.00 31.45 C
ANISOU 2645 CA ALA A 265 3929 4228 3793 132 -75 93 C
ATOM 2646 C ALA A 265 -13.425 13.228 11.314 1.00 31.44 C
ANISOU 2646 C ALA A 265 3942 4241 3761 128 -86 79 C
ATOM 2647 O ALA A 265 -14.454 13.536 11.849 1.00 30.47 O
ANISOU 2647 O ALA A 265 3813 4146 3618 130 -110 61 O
ATOM 2648 CB ALA A 265 -12.511 11.239 12.515 1.00 30.53 C
ANISOU 2648 CB ALA A 265 3818 4122 3660 121 -59 92 C
ATOM 2649 N PRO A 266 -13.273 13.348 10.002 1.00 32.21 N
ANISOU 2649 N PRO A 266 4060 4321 3858 122 -67 85 N
ATOM 2650 CA PRO A 266 -14.360 13.942 9.244 1.00 32.51 C
ANISOU 2650 CA PRO A 266 4112 4370 3870 119 -79 71 C
ATOM 2651 C PRO A 266 -15.662 13.148 9.263 1.00 31.96 C
ANISOU 2651 C PRO A 266 4055 4326 3765 109 -79 57 C
ATOM 2652 O PRO A 266 -15.686 11.981 9.421 1.00 30.86 O
ANISOU 2652 O PRO A 266 3920 4190 3617 102 -60 61 O
ATOM 2653 CB PRO A 266 -13.789 14.056 7.842 1.00 34.02 C
ANISOU 2653 CB PRO A 266 4324 4533 4069 113 -54 84 C
ATOM 2654 CG PRO A 266 -12.731 13.070 7.776 1.00 35.09 C
ANISOU 2654 CG PRO A 266 4461 4649 4222 110 -22 102 C
ATOM 2655 CD PRO A 266 -12.185 12.907 9.138 1.00 32.92 C
ANISOU 2655 CD PRO A 266 4161 4380 3967 118 -34 104 C
ATOM 2656 N LEU A 267 -16.747 13.852 9.059 1.00 32.28 N
ANISOU 2656 N LEU A 267 4098 4382 3783 109 -102 39 N
ATOM 2657 CA LEU A 267 -18.055 13.268 9.044 1.00 32.56 C
ANISOU 2657 CA LEU A 267 4144 4442 3786 101 -105 25 C
ATOM 2658 C LEU A 267 -18.207 12.067 8.132 1.00 31.59 C
ANISOU 2658 C LEU A 267 4046 4309 3647 88 -72 33 C
ATOM 2659 O LEU A 267 -18.751 11.102 8.527 1.00 30.69 O
ANISOU 2659 O LEU A 267 3934 4210 3516 82 -67 29 O
ATOM 2660 CB LEU A 267 -19.103 14.327 8.791 1.00 34.57 C
ANISOU 2660 CB LEU A 267 4400 4711 4024 104 -134 5 C
ATOM 2661 CG LEU A 267 -20.549 13.947 8.917 1.00 36.67 C
ANISOU 2661 CG LEU A 267 4671 5005 4257 97 -144 -14 C
ATOM 2662 CD1 LEU A 267 -20.760 13.137 10.158 1.00 36.13 C
ANISOU 2662 CD1 LEU A 267 4586 4961 4183 98 -146 -16 C
ATOM 2663 CD2 LEU A 267 -21.386 15.196 8.958 1.00 38.04 C
ANISOU 2663 CD2 LEU A 267 4839 5193 4422 104 -179 -34 C
ATOM 2664 N TRP A 268 -17.659 12.114 6.933 1.00 31.97 N
ANISOU 2664 N TRP A 268 4115 4329 3702 84 -51 44 N
ATOM 2665 CA TRP A 268 -17.721 11.006 6.008 1.00 32.52 C
ANISOU 2665 CA TRP A 268 4210 4386 3758 73 -20 53 C
ATOM 2666 C TRP A 268 -17.084 9.720 6.566 1.00 30.69 C
ANISOU 2666 C TRP A 268 3973 4153 3534 70 1 65 C
ATOM 2667 O TRP A 268 -17.583 8.670 6.353 1.00 30.34 O
ANISOU 2667 O TRP A 268 3943 4115 3471 62 14 65 O
ATOM 2668 CB TRP A 268 -17.169 11.405 4.638 1.00 34.43 C
ANISOU 2668 CB TRP A 268 4475 4599 4009 71 -2 63 C
ATOM 2669 CG TRP A 268 -15.715 11.617 4.571 1.00 36.78 C
ANISOU 2669 CG TRP A 268 4764 4873 4339 77 14 81 C
ATOM 2670 CD1 TRP A 268 -15.068 12.777 4.683 1.00 38.78 C
ANISOU 2670 CD1 TRP A 268 5004 5117 4616 85 0 84 C
ATOM 2671 CD2 TRP A 268 -14.724 10.626 4.399 1.00 37.73 C
ANISOU 2671 CD2 TRP A 268 4888 4974 4472 74 46 98 C
ATOM 2672 NE1 TRP A 268 -13.740 12.593 4.585 1.00 40.23 N
ANISOU 2672 NE1 TRP A 268 5182 5278 4827 88 22 103 N
ATOM 2673 CE2 TRP A 268 -13.495 11.270 4.411 1.00 39.76 C
ANISOU 2673 CE2 TRP A 268 5133 5212 4762 81 51 111 C
ATOM 2674 CE3 TRP A 268 -14.754 9.248 4.247 1.00 37.92 C
ANISOU 2674 CE3 TRP A 268 4924 4997 4485 67 70 104 C
ATOM 2675 CZ2 TRP A 268 -12.323 10.595 4.269 1.00 41.23 C
ANISOU 2675 CZ2 TRP A 268 5318 5377 4969 81 79 129 C
ATOM 2676 CZ3 TRP A 268 -13.611 8.594 4.118 1.00 39.89 C
ANISOU 2676 CZ3 TRP A 268 5174 5227 4755 67 96 120 C
ATOM 2677 CH2 TRP A 268 -12.400 9.255 4.122 1.00 41.34 C
ANISOU 2677 CH2 TRP A 268 5344 5391 4971 74 102 132 C
ATOM 2678 N LEU A 269 -15.991 9.868 7.294 1.00 32.25 N
ANISOU 2678 N LEU A 269 4151 4343 3761 78 2 75 N
ATOM 2679 CA LEU A 269 -15.273 8.790 7.934 1.00 32.00 C
ANISOU 2679 CA LEU A 269 4110 4307 3740 76 18 86 C
ATOM 2680 C LEU A 269 -16.080 8.244 9.106 1.00 30.91 C
ANISOU 2680 C LEU A 269 3960 4200 3585 73 1 74 C
ATOM 2681 O LEU A 269 -16.108 7.073 9.310 1.00 30.57 O
ANISOU 2681 O LEU A 269 3921 4160 3533 66 14 79 O
ATOM 2682 CB LEU A 269 -13.893 9.220 8.387 1.00 32.55 C
ANISOU 2682 CB LEU A 269 4162 4357 3847 85 21 98 C
ATOM 2683 CG LEU A 269 -13.000 8.102 8.857 1.00 32.54 C
ANISOU 2683 CG LEU A 269 4156 4346 3862 82 41 111 C
ATOM 2684 CD1 LEU A 269 -12.968 6.991 7.843 1.00 32.92 C
ANISOU 2684 CD1 LEU A 269 4230 4382 3897 72 72 119 C
ATOM 2685 CD2 LEU A 269 -11.610 8.580 9.168 1.00 33.33 C
ANISOU 2685 CD2 LEU A 269 4240 4423 4002 91 44 124 C
ATOM 2686 N MET A 270 -16.709 9.121 9.863 1.00 26.14 N
ANISOU 2686 N MET A 270 3338 3617 2975 80 -29 60 N
ATOM 2687 CA MET A 270 -17.565 8.712 10.942 1.00 25.09 C
ANISOU 2687 CA MET A 270 3193 3515 2824 78 -47 48 C
ATOM 2688 C MET A 270 -18.639 7.808 10.377 1.00 24.77 C
ANISOU 2688 C MET A 270 3173 3488 2751 65 -37 43 C
ATOM 2689 O MET A 270 -18.813 6.726 10.835 1.00 25.74 O
ANISOU 2689 O MET A 270 3296 3621 2864 58 -30 45 O
ATOM 2690 CB MET A 270 -18.221 9.883 11.647 1.00 24.59 C
ANISOU 2690 CB MET A 270 3112 3475 2758 87 -81 31 C
ATOM 2691 CG MET A 270 -17.290 10.807 12.384 1.00 27.95 C
ANISOU 2691 CG MET A 270 3515 3892 3213 101 -97 35 C
ATOM 2692 SD MET A 270 -16.111 9.996 13.431 1.00 28.66 S
ANISOU 2692 SD MET A 270 3589 3971 3328 103 -86 49 S
ATOM 2693 CE MET A 270 -17.170 9.195 14.600 1.00 25.23 C
ANISOU 2693 CE MET A 270 3146 3574 2866 97 -99 36 C
ATOM 2694 N TYR A 271 -19.318 8.267 9.337 1.00 24.03 N
ANISOU 2694 N TYR A 271 3097 3390 2643 63 -38 36 N
ATOM 2695 CA TYR A 271 -20.389 7.518 8.706 1.00 25.09 C
ANISOU 2695 CA TYR A 271 3253 3534 2747 52 -31 31 C
ATOM 2696 C TYR A 271 -19.900 6.140 8.229 1.00 24.07 C
ANISOU 2696 C TYR A 271 3140 3389 2616 43 -1 47 C
ATOM 2697 O TYR A 271 -20.555 5.169 8.423 1.00 22.89 O
ANISOU 2697 O TYR A 271 2997 3254 2447 35 1 45 O
ATOM 2698 CB TYR A 271 -21.018 8.314 7.560 1.00 26.87 C
ANISOU 2698 CB TYR A 271 3497 3751 2961 52 -36 23 C
ATOM 2699 CG TYR A 271 -21.919 9.464 7.924 1.00 30.07 C
ANISOU 2699 CG TYR A 271 3890 4176 3358 58 -69 3 C
ATOM 2700 CD1 TYR A 271 -22.544 9.523 9.129 1.00 31.45 C
ANISOU 2700 CD1 TYR A 271 4042 4382 3524 61 -90 -10 C
ATOM 2701 CD2 TYR A 271 -22.162 10.487 7.023 1.00 33.06 C
ANISOU 2701 CD2 TYR A 271 4281 4544 3737 60 -78 -4 C
ATOM 2702 CE1 TYR A 271 -23.380 10.566 9.454 1.00 33.83 C
ANISOU 2702 CE1 TYR A 271 4333 4705 3818 67 -120 -29 C
ATOM 2703 CE2 TYR A 271 -23.000 11.535 7.327 1.00 34.63 C
ANISOU 2703 CE2 TYR A 271 4469 4761 3927 65 -109 -24 C
ATOM 2704 CZ TYR A 271 -23.611 11.574 8.546 1.00 36.08 C
ANISOU 2704 CZ TYR A 271 4629 4976 4103 69 -130 -37 C
ATOM 2705 OH TYR A 271 -24.432 12.604 8.883 1.00 39.23 O
ANISOU 2705 OH TYR A 271 5016 5395 4494 75 -162 -57 O
ATOM 2706 N LEU A 272 -18.727 6.117 7.625 1.00 23.57 N
ANISOU 2706 N LEU A 272 3084 3296 2576 46 20 62 N
ATOM 2707 CA LEU A 272 -18.114 4.923 7.126 1.00 25.22 C
ANISOU 2707 CA LEU A 272 3308 3487 2786 40 48 77 C
ATOM 2708 C LEU A 272 -17.798 3.943 8.250 1.00 23.46 C
ANISOU 2708 C LEU A 272 3070 3276 2568 36 49 81 C
ATOM 2709 O LEU A 272 -18.050 2.803 8.113 1.00 23.81 O
ANISOU 2709 O LEU A 272 3126 3322 2597 28 59 85 O
ATOM 2710 CB LEU A 272 -16.863 5.268 6.339 1.00 28.46 C
ANISOU 2710 CB LEU A 272 3726 3866 3223 45 69 91 C
ATOM 2711 CG LEU A 272 -16.089 4.164 5.646 1.00 34.31 C
ANISOU 2711 CG LEU A 272 4484 4584 3969 40 101 106 C
ATOM 2712 CD1 LEU A 272 -17.005 3.321 4.806 1.00 36.05 C
ANISOU 2712 CD1 LEU A 272 4732 4807 4159 31 110 105 C
ATOM 2713 CD2 LEU A 272 -14.933 4.682 4.830 1.00 36.24 C
ANISOU 2713 CD2 LEU A 272 4733 4797 4238 45 121 119 C
ATOM 2714 N ALA A 273 -17.235 4.444 9.336 1.00 21.58 N
ANISOU 2714 N ALA A 273 2806 3043 2350 43 35 80 N
ATOM 2715 CA ALA A 273 -16.900 3.651 10.493 1.00 21.30 C
ANISOU 2715 CA ALA A 273 2755 3018 2321 40 32 82 C
ATOM 2716 C ALA A 273 -18.170 3.045 11.131 1.00 20.96 C
ANISOU 2716 C ALA A 273 2709 3008 2246 32 17 71 C
ATOM 2717 O ALA A 273 -18.187 1.917 11.486 1.00 20.78 O
ANISOU 2717 O ALA A 273 2689 2990 2216 23 23 76 O
ATOM 2718 CB ALA A 273 -16.139 4.484 11.471 1.00 20.83 C
ANISOU 2718 CB ALA A 273 2669 2956 2288 51 17 82 C
ATOM 2719 N ILE A 274 -19.226 3.834 11.225 1.00 20.57 N
ANISOU 2719 N ILE A 274 2656 2980 2180 34 -4 56 N
ATOM 2720 CA ILE A 274 -20.501 3.408 11.777 1.00 20.43 C
ANISOU 2720 CA ILE A 274 2636 2994 2133 27 -18 45 C
ATOM 2721 C ILE A 274 -21.128 2.314 10.921 1.00 20.74 C
ANISOU 2721 C ILE A 274 2700 3032 2149 15 -3 49 C
ATOM 2722 O ILE A 274 -21.543 1.325 11.392 1.00 19.84 O
ANISOU 2722 O ILE A 274 2585 2933 2019 6 -4 51 O
ATOM 2723 CB ILE A 274 -21.470 4.587 11.983 1.00 20.64 C
ANISOU 2723 CB ILE A 274 2652 3042 2148 34 -44 27 C
ATOM 2724 CG1 ILE A 274 -20.963 5.533 13.062 1.00 20.68 C
ANISOU 2724 CG1 ILE A 274 2631 3055 2173 46 -63 21 C
ATOM 2725 CG2 ILE A 274 -22.847 4.094 12.318 1.00 20.94 C
ANISOU 2725 CG2 ILE A 274 2691 3112 2154 25 -55 15 C
ATOM 2726 CD1 ILE A 274 -21.609 6.865 13.081 1.00 22.02 C
ANISOU 2726 CD1 ILE A 274 2792 3237 2339 55 -87 5 C
ATOM 2727 N VAL A 275 -21.154 2.550 9.623 1.00 21.52 N
ANISOU 2727 N VAL A 275 2821 3110 2245 16 9 52 N
ATOM 2728 CA VAL A 275 -21.692 1.631 8.658 1.00 23.05 C
ANISOU 2728 CA VAL A 275 3041 3297 2418 7 23 57 C
ATOM 2729 C VAL A 275 -20.948 0.285 8.687 1.00 22.41 C
ANISOU 2729 C VAL A 275 2968 3205 2343 0 43 73 C
ATOM 2730 O VAL A 275 -21.545 -0.730 8.631 1.00 21.33 O
ANISOU 2730 O VAL A 275 2841 3077 2186 -9 45 75 O
ATOM 2731 CB VAL A 275 -21.738 2.297 7.256 1.00 26.51 C
ANISOU 2731 CB VAL A 275 3502 3713 2857 11 33 58 C
ATOM 2732 CG1 VAL A 275 -21.592 1.293 6.151 1.00 28.83 C
ANISOU 2732 CG1 VAL A 275 3826 3985 3142 5 56 70 C
ATOM 2733 CG2 VAL A 275 -22.987 3.135 7.109 1.00 27.60 C
ANISOU 2733 CG2 VAL A 275 3642 3868 2976 11 11 40 C
ATOM 2734 N LEU A 276 -19.637 0.332 8.833 1.00 22.45 N
ANISOU 2734 N LEU A 276 2965 3190 2376 6 55 83 N
ATOM 2735 CA LEU A 276 -18.815 -0.846 8.895 1.00 23.46 C
ANISOU 2735 CA LEU A 276 3097 3303 2512 0 72 96 C
ATOM 2736 C LEU A 276 -19.160 -1.668 10.145 1.00 21.81 C
ANISOU 2736 C LEU A 276 2874 3120 2294 -8 59 94 C
ATOM 2737 O LEU A 276 -19.250 -2.847 10.105 1.00 21.86 O
ANISOU 2737 O LEU A 276 2890 3128 2290 -17 65 100 O
ATOM 2738 CB LEU A 276 -17.338 -0.480 8.873 1.00 25.02 C
ANISOU 2738 CB LEU A 276 3287 3475 2745 8 86 106 C
ATOM 2739 CG LEU A 276 -16.353 -1.622 8.967 1.00 26.69 C
ANISOU 2739 CG LEU A 276 3501 3670 2970 4 103 118 C
ATOM 2740 CD1 LEU A 276 -16.488 -2.633 7.855 1.00 25.70 C
ANISOU 2740 CD1 LEU A 276 3404 3533 2830 -2 123 126 C
ATOM 2741 CD2 LEU A 276 -14.927 -1.182 9.173 1.00 28.17 C
ANISOU 2741 CD2 LEU A 276 3675 3834 3194 12 113 126 C
ATOM 2742 N ALA A 277 -19.343 -0.976 11.239 1.00 20.59 N
ANISOU 2742 N ALA A 277 2694 2984 2143 -4 39 84 N
ATOM 2743 CA ALA A 277 -19.725 -1.586 12.474 1.00 19.74 C
ANISOU 2743 CA ALA A 277 2572 2903 2027 -11 24 80 C
ATOM 2744 C ALA A 277 -21.069 -2.311 12.304 1.00 19.53 C
ANISOU 2744 C ALA A 277 2557 2899 1965 -23 17 76 C
ATOM 2745 O ALA A 277 -21.178 -3.416 12.683 1.00 19.93 O
ANISOU 2745 O ALA A 277 2609 2957 2005 -33 18 81 O
ATOM 2746 CB ALA A 277 -19.785 -0.558 13.567 1.00 19.18 C
ANISOU 2746 CB ALA A 277 2475 2849 1964 -3 3 69 C
ATOM 2747 N HIS A 278 -22.044 -1.661 11.686 1.00 18.70 N
ANISOU 2747 N HIS A 278 2460 2803 1844 -20 11 67 N
ATOM 2748 CA HIS A 278 -23.369 -2.204 11.410 1.00 18.87 C
ANISOU 2748 CA HIS A 278 2492 2844 1833 -29 4 62 C
ATOM 2749 C HIS A 278 -23.345 -3.406 10.457 1.00 20.62 C
ANISOU 2749 C HIS A 278 2741 3049 2045 -38 21 75 C
ATOM 2750 O HIS A 278 -24.077 -4.327 10.617 1.00 20.69 O
ANISOU 2750 O HIS A 278 2755 3073 2033 -48 16 77 O
ATOM 2751 CB HIS A 278 -24.291 -1.124 10.887 1.00 17.41 C
ANISOU 2751 CB HIS A 278 2311 2667 1638 -24 -7 48 C
ATOM 2752 CG HIS A 278 -24.638 -0.088 11.896 1.00 18.16 C
ANISOU 2752 CG HIS A 278 2379 2785 1734 -17 -28 33 C
ATOM 2753 ND1 HIS A 278 -25.183 1.115 11.564 1.00 19.65 N
ANISOU 2753 ND1 HIS A 278 2567 2979 1922 -9 -40 20 N
ATOM 2754 CD2 HIS A 278 -24.514 -0.078 13.241 1.00 18.29 C
ANISOU 2754 CD2 HIS A 278 2371 2823 1755 -17 -41 29 C
ATOM 2755 CE1 HIS A 278 -25.387 1.824 12.653 1.00 19.50 C
ANISOU 2755 CE1 HIS A 278 2522 2983 1905 -3 -60 8 C
ATOM 2756 NE2 HIS A 278 -24.996 1.114 13.686 1.00 18.71 N
ANISOU 2756 NE2 HIS A 278 2408 2893 1808 -8 -60 14 N
ATOM 2757 N THR A 279 -22.405 -3.398 9.518 1.00 21.37 N
ANISOU 2757 N THR A 279 2852 3112 2157 -32 41 85 N
ATOM 2758 CA THR A 279 -22.181 -4.453 8.533 1.00 23.21 C
ANISOU 2758 CA THR A 279 3111 3324 2383 -37 60 97 C
ATOM 2759 C THR A 279 -21.842 -5.793 9.174 1.00 23.24 C
ANISOU 2759 C THR A 279 3112 3333 2386 -47 61 107 C
ATOM 2760 O THR A 279 -22.073 -6.808 8.621 1.00 24.12 O
ANISOU 2760 O THR A 279 3243 3439 2484 -53 67 114 O
ATOM 2761 CB THR A 279 -21.103 -4.042 7.499 1.00 26.34 C
ANISOU 2761 CB THR A 279 3521 3685 2801 -28 82 105 C
ATOM 2762 OG1 THR A 279 -21.580 -2.947 6.749 1.00 28.58 O
ANISOU 2762 OG1 THR A 279 3813 3964 3082 -21 80 97 O
ATOM 2763 CG2 THR A 279 -20.816 -5.135 6.541 1.00 27.61 C
ANISOU 2763 CG2 THR A 279 3708 3826 2957 -31 101 118 C
ATOM 2764 N ASN A 280 -21.284 -5.749 10.361 1.00 22.63 N
ANISOU 2764 N ASN A 280 3011 3265 2323 -47 53 105 N
ATOM 2765 CA ASN A 280 -20.967 -6.947 11.094 1.00 23.19 C
ANISOU 2765 CA ASN A 280 3077 3341 2393 -58 51 112 C
ATOM 2766 C ASN A 280 -22.197 -7.811 11.335 1.00 23.72 C
ANISOU 2766 C ASN A 280 3150 3435 2429 -70 37 111 C
ATOM 2767 O ASN A 280 -22.121 -8.983 11.326 1.00 24.87 O
ANISOU 2767 O ASN A 280 3304 3578 2567 -79 39 120 O
ATOM 2768 CB ASN A 280 -20.259 -6.688 12.405 1.00 22.84 C
ANISOU 2768 CB ASN A 280 3006 3304 2368 -57 42 109 C
ATOM 2769 CG ASN A 280 -19.854 -7.972 13.062 1.00 25.62 C
ANISOU 2769 CG ASN A 280 3356 3657 2720 -68 40 117 C
ATOM 2770 OD1 ASN A 280 -19.029 -8.671 12.549 1.00 29.09 O
ANISOU 2770 OD1 ASN A 280 3809 4074 3172 -69 54 127 O
ATOM 2771 ND2 ASN A 280 -20.469 -8.301 14.125 1.00 21.61 N
ANISOU 2771 ND2 ASN A 280 2836 3177 2199 -77 22 112 N
ATOM 2772 N SER A 281 -23.343 -7.186 11.502 1.00 22.91 N
ANISOU 2772 N SER A 281 3041 3356 2309 -70 23 100 N
ATOM 2773 CA SER A 281 -24.627 -7.813 11.628 1.00 23.49 C
ANISOU 2773 CA SER A 281 3119 3454 2352 -81 10 98 C
ATOM 2774 C SER A 281 -25.156 -8.516 10.356 1.00 23.85 C
ANISOU 2774 C SER A 281 3194 3486 2380 -84 18 106 C
ATOM 2775 O SER A 281 -26.131 -9.152 10.424 1.00 24.00 O
ANISOU 2775 O SER A 281 3218 3523 2377 -93 8 107 O
ATOM 2776 CB SER A 281 -25.665 -6.810 12.126 1.00 23.88 C
ANISOU 2776 CB SER A 281 3152 3531 2389 -79 -7 82 C
ATOM 2777 OG SER A 281 -25.346 -6.281 13.368 1.00 27.81 O
ANISOU 2777 OG SER A 281 3623 4046 2898 -77 -17 75 O
ATOM 2778 N VAL A 282 -24.461 -8.353 9.253 1.00 24.08 N
ANISOU 2778 N VAL A 282 3243 3484 2422 -76 37 112 N
ATOM 2779 CA VAL A 282 -24.819 -8.978 8.004 1.00 24.94 C
ANISOU 2779 CA VAL A 282 3382 3576 2518 -76 46 120 C
ATOM 2780 C VAL A 282 -23.981 -10.228 7.745 1.00 27.31 C
ANISOU 2780 C VAL A 282 3696 3858 2824 -80 58 135 C
ATOM 2781 O VAL A 282 -24.476 -11.182 7.232 1.00 28.22 O
ANISOU 2781 O VAL A 282 3831 3971 2922 -86 56 142 O
ATOM 2782 CB VAL A 282 -24.624 -8.005 6.800 1.00 25.36 C
ANISOU 2782 CB VAL A 282 3453 3604 2580 -64 60 117 C
ATOM 2783 CG1 VAL A 282 -24.874 -8.708 5.483 1.00 26.79 C
ANISOU 2783 CG1 VAL A 282 3668 3764 2748 -64 71 127 C
ATOM 2784 CG2 VAL A 282 -25.481 -6.774 6.911 1.00 24.26 C
ANISOU 2784 CG2 VAL A 282 3303 3480 2435 -60 47 102 C
ATOM 2785 N VAL A 283 -22.720 -10.187 8.142 1.00 27.17 N
ANISOU 2785 N VAL A 283 3667 3827 2831 -77 67 138 N
ATOM 2786 CA VAL A 283 -21.777 -11.217 7.827 1.00 29.51 C
ANISOU 2786 CA VAL A 283 3975 4102 3136 -78 80 150 C
ATOM 2787 C VAL A 283 -21.909 -12.628 8.381 1.00 30.78 C
ANISOU 2787 C VAL A 283 4136 4274 3285 -91 69 157 C
ATOM 2788 O VAL A 283 -21.614 -13.538 7.681 1.00 32.01 O
ANISOU 2788 O VAL A 283 4311 4412 3437 -92 77 167 O
ATOM 2789 CB VAL A 283 -20.318 -10.744 7.928 1.00 30.75 C
ANISOU 2789 CB VAL A 283 4120 4236 3326 -70 96 152 C
ATOM 2790 CG1 VAL A 283 -20.100 -9.449 7.208 1.00 32.16 C
ANISOU 2790 CG1 VAL A 283 4302 4401 3516 -57 108 147 C
ATOM 2791 CG2 VAL A 283 -19.883 -10.591 9.344 1.00 30.75 C
ANISOU 2791 CG2 VAL A 283 4092 4252 3341 -74 84 147 C
ATOM 2792 N ASN A 284 -22.342 -12.815 9.609 1.00 30.31 N
ANISOU 2792 N ASN A 284 4056 4242 3218 -101 50 153 N
ATOM 2793 CA ASN A 284 -22.439 -14.183 10.158 1.00 31.54 C
ANISOU 2793 CA ASN A 284 4213 4409 3363 -115 38 161 C
ATOM 2794 C ASN A 284 -23.171 -15.260 9.316 1.00 31.94 C
ANISOU 2794 C ASN A 284 4289 4456 3389 -121 35 170 C
ATOM 2795 O ASN A 284 -22.602 -16.264 9.047 1.00 32.52 O
ANISOU 2795 O ASN A 284 4375 4515 3465 -124 38 180 O
ATOM 2796 CB ASN A 284 -22.842 -14.204 11.634 1.00 32.35 C
ANISOU 2796 CB ASN A 284 4289 4542 3459 -127 18 155 C
ATOM 2797 CG ASN A 284 -21.884 -13.414 12.508 1.00 36.10 C
ANISOU 2797 CG ASN A 284 4741 5013 3961 -121 21 148 C
ATOM 2798 OD1 ASN A 284 -20.838 -12.989 12.081 1.00 36.66 O
ANISOU 2798 OD1 ASN A 284 4814 5058 4057 -111 37 149 O
ATOM 2799 ND2 ASN A 284 -22.256 -13.228 13.730 1.00 37.68 N
ANISOU 2799 ND2 ASN A 284 4920 5240 4157 -128 5 141 N
ATOM 2800 N PRO A 285 -24.391 -14.997 8.850 1.00 32.03 N
ANISOU 2800 N PRO A 285 4311 4480 3379 -121 28 168 N
ATOM 2801 CA PRO A 285 -25.114 -15.949 8.006 1.00 33.28 C
ANISOU 2801 CA PRO A 285 4496 4635 3516 -125 24 177 C
ATOM 2802 C PRO A 285 -24.295 -16.413 6.792 1.00 34.87 C
ANISOU 2802 C PRO A 285 4723 4800 3726 -116 43 187 C
ATOM 2803 O PRO A 285 -24.348 -17.550 6.453 1.00 35.47 O
ANISOU 2803 O PRO A 285 4815 4870 3791 -120 38 197 O
ATOM 2804 CB PRO A 285 -26.354 -15.188 7.575 1.00 33.23 C
ANISOU 2804 CB PRO A 285 4494 4639 3493 -122 18 170 C
ATOM 2805 CG PRO A 285 -26.529 -14.147 8.591 1.00 33.03 C
ANISOU 2805 CG PRO A 285 4440 4637 3474 -123 12 157 C
ATOM 2806 CD PRO A 285 -25.175 -13.792 9.093 1.00 31.44 C
ANISOU 2806 CD PRO A 285 4223 4424 3300 -117 23 155 C
ATOM 2807 N PHE A 286 -23.499 -15.540 6.217 1.00 35.67 N
ANISOU 2807 N PHE A 286 4826 4879 3846 -103 63 183 N
ATOM 2808 CA PHE A 286 -22.653 -15.907 5.095 1.00 38.19 C
ANISOU 2808 CA PHE A 286 5170 5166 4175 -93 83 192 C
ATOM 2809 C PHE A 286 -21.561 -16.851 5.537 1.00 38.53 C
ANISOU 2809 C PHE A 286 5207 5200 4232 -97 85 198 C
ATOM 2810 O PHE A 286 -21.318 -17.827 4.890 1.00 39.43 O
ANISOU 2810 O PHE A 286 5342 5300 4341 -96 88 208 O
ATOM 2811 CB PHE A 286 -22.081 -14.688 4.383 1.00 39.10 C
ANISOU 2811 CB PHE A 286 5287 5260 4307 -79 104 187 C
ATOM 2812 CG PHE A 286 -23.096 -13.932 3.632 1.00 40.81 C
ANISOU 2812 CG PHE A 286 5519 5478 4510 -75 102 181 C
ATOM 2813 CD1 PHE A 286 -23.866 -12.991 4.266 1.00 41.15 C
ANISOU 2813 CD1 PHE A 286 5543 5544 4549 -77 90 170 C
ATOM 2814 CD2 PHE A 286 -23.324 -14.200 2.301 1.00 43.31 C
ANISOU 2814 CD2 PHE A 286 5868 5773 4816 -68 113 188 C
ATOM 2815 CE1 PHE A 286 -24.847 -12.320 3.606 1.00 42.28 C
ANISOU 2815 CE1 PHE A 286 5699 5688 4678 -74 86 164 C
ATOM 2816 CE2 PHE A 286 -24.305 -13.519 1.619 1.00 44.20 C
ANISOU 2816 CE2 PHE A 286 5995 5884 4914 -65 109 183 C
ATOM 2817 CZ PHE A 286 -25.064 -12.573 2.266 1.00 42.93 C
ANISOU 2817 CZ PHE A 286 5814 5746 4750 -68 96 170 C
ATOM 2818 N ILE A 287 -20.919 -16.562 6.656 1.00 37.90 N
ANISOU 2818 N ILE A 287 5100 5129 4170 -101 82 193 N
ATOM 2819 CA ILE A 287 -19.889 -17.427 7.170 1.00 39.17 C
ANISOU 2819 CA ILE A 287 5254 5281 4346 -106 82 198 C
ATOM 2820 C ILE A 287 -20.429 -18.830 7.487 1.00 39.66 C
ANISOU 2820 C ILE A 287 5324 5357 4387 -119 61 205 C
ATOM 2821 O ILE A 287 -19.762 -19.803 7.230 1.00 40.68 O
ANISOU 2821 O ILE A 287 5464 5471 4521 -120 63 212 O
ATOM 2822 CB ILE A 287 -19.190 -16.825 8.382 1.00 39.54 C
ANISOU 2822 CB ILE A 287 5272 5337 4416 -108 79 190 C
ATOM 2823 CG1 ILE A 287 -18.608 -15.480 8.028 1.00 39.76 C
ANISOU 2823 CG1 ILE A 287 5293 5350 4466 -94 97 184 C
ATOM 2824 CG2 ILE A 287 -18.090 -17.733 8.847 1.00 40.60 C
ANISOU 2824 CG2 ILE A 287 5401 5459 4568 -113 79 194 C
ATOM 2825 CD1 ILE A 287 -17.688 -15.532 6.856 1.00 42.03 C
ANISOU 2825 CD1 ILE A 287 5598 5604 4767 -82 122 190 C
ATOM 2826 N TYR A 288 -21.634 -18.920 8.036 1.00 39.18 N
ANISOU 2826 N TYR A 288 5258 5326 4305 -130 41 203 N
ATOM 2827 CA TYR A 288 -22.241 -20.206 8.333 1.00 40.24 C
ANISOU 2827 CA TYR A 288 5399 5473 4417 -144 20 211 C
ATOM 2828 C TYR A 288 -22.511 -20.947 7.034 1.00 42.36 C
ANISOU 2828 C TYR A 288 5700 5724 4672 -138 24 222 C
ATOM 2829 O TYR A 288 -22.197 -22.089 6.933 1.00 43.61 O
ANISOU 2829 O TYR A 288 5868 5874 4826 -143 16 230 O
ATOM 2830 CB TYR A 288 -23.526 -20.082 9.129 1.00 39.16 C
ANISOU 2830 CB TYR A 288 5249 5372 4259 -156 -1 208 C
ATOM 2831 CG TYR A 288 -23.371 -19.366 10.420 1.00 38.34 C
ANISOU 2831 CG TYR A 288 5115 5288 4166 -161 -7 198 C
ATOM 2832 CD1 TYR A 288 -22.250 -19.515 11.166 1.00 39.45 C
ANISOU 2832 CD1 TYR A 288 5241 5421 4328 -164 -5 196 C
ATOM 2833 CD2 TYR A 288 -24.332 -18.520 10.860 1.00 37.79 C
ANISOU 2833 CD2 TYR A 288 5032 5243 4086 -163 -14 189 C
ATOM 2834 CE1 TYR A 288 -22.095 -18.840 12.349 1.00 39.63 C
ANISOU 2834 CE1 TYR A 288 5237 5459 4361 -167 -11 187 C
ATOM 2835 CE2 TYR A 288 -24.198 -17.845 12.020 1.00 37.79 C
ANISOU 2835 CE2 TYR A 288 5005 5261 4094 -166 -19 179 C
ATOM 2836 CZ TYR A 288 -23.081 -18.011 12.770 1.00 39.17 C
ANISOU 2836 CZ TYR A 288 5166 5427 4290 -168 -18 179 C
ATOM 2837 OH TYR A 288 -22.948 -17.329 13.928 1.00 38.91 O
ANISOU 2837 OH TYR A 288 5107 5410 4266 -170 -24 169 O
ATOM 2838 N ALA A 289 -23.072 -20.255 6.061 1.00 42.91 N
ANISOU 2838 N ALA A 289 5784 5785 4733 -128 34 220 N
ATOM 2839 CA ALA A 289 -23.380 -20.819 4.773 1.00 45.40 C
ANISOU 2839 CA ALA A 289 6133 6081 5036 -120 39 230 C
ATOM 2840 C ALA A 289 -22.176 -21.385 4.063 1.00 48.20 C
ANISOU 2840 C ALA A 289 6503 6407 5405 -111 55 236 C
ATOM 2841 O ALA A 289 -22.248 -22.457 3.547 1.00 48.93 O
ANISOU 2841 O ALA A 289 6615 6490 5486 -112 48 245 O
ATOM 2842 CB ALA A 289 -24.087 -19.833 3.892 1.00 45.24 C
ANISOU 2842 CB ALA A 289 6125 6055 5008 -110 49 225 C
ATOM 2843 N TYR A 290 -21.075 -20.665 4.062 1.00 49.47 N
ANISOU 2843 N TYR A 290 6653 6551 5591 -103 76 230 N
ATOM 2844 CA TYR A 290 -19.860 -21.107 3.415 1.00 51.99 C
ANISOU 2844 CA TYR A 290 6984 6843 5927 -93 94 234 C
ATOM 2845 C TYR A 290 -19.042 -22.156 4.151 1.00 52.58 C
ANISOU 2845 C TYR A 290 7049 6917 6012 -102 85 237 C
ATOM 2846 O TYR A 290 -18.389 -22.968 3.525 1.00 53.50 O
ANISOU 2846 O TYR A 290 7182 7014 6132 -96 91 243 O
ATOM 2847 CB TYR A 290 -18.972 -19.913 3.099 1.00 53.30 C
ANISOU 2847 CB TYR A 290 7142 6992 6118 -81 121 228 C
ATOM 2848 CG TYR A 290 -19.372 -19.262 1.826 1.00 56.50 C
ANISOU 2848 CG TYR A 290 7571 7382 6515 -69 137 229 C
ATOM 2849 CD1 TYR A 290 -18.887 -19.711 0.617 1.00 59.42 C
ANISOU 2849 CD1 TYR A 290 7968 7725 6884 -58 154 236 C
ATOM 2850 CD2 TYR A 290 -20.277 -18.245 1.810 1.00 57.88 C
ANISOU 2850 CD2 TYR A 290 7743 7568 6681 -68 134 223 C
ATOM 2851 CE1 TYR A 290 -19.285 -19.147 -0.568 1.00 61.61 C
ANISOU 2851 CE1 TYR A 290 8270 7987 7152 -47 168 237 C
ATOM 2852 CE2 TYR A 290 -20.686 -17.675 0.632 1.00 59.98 C
ANISOU 2852 CE2 TYR A 290 8032 7818 6938 -58 146 223 C
ATOM 2853 CZ TYR A 290 -20.181 -18.132 -0.554 1.00 62.62 C
ANISOU 2853 CZ TYR A 290 8394 8125 7272 -48 163 231 C
ATOM 2854 OH TYR A 290 -20.580 -17.556 -1.717 1.00 66.31 O
ANISOU 2854 OH TYR A 290 8887 8577 7732 -38 175 231 O
ATOM 2855 N ARG A 291 -19.083 -22.148 5.475 1.00 51.35 N
ANISOU 2855 N ARG A 291 6866 6783 5861 -115 68 232 N
ATOM 2856 CA ARG A 291 -18.264 -23.065 6.242 1.00 51.24 C
ANISOU 2856 CA ARG A 291 6843 6768 5860 -124 58 233 C
ATOM 2857 C ARG A 291 -18.946 -24.187 6.964 1.00 50.45 C
ANISOU 2857 C ARG A 291 6741 6688 5738 -141 28 238 C
ATOM 2858 O ARG A 291 -18.297 -25.066 7.436 1.00 50.75 O
ANISOU 2858 O ARG A 291 6775 6722 5784 -149 18 240 O
ATOM 2859 CB ARG A 291 -17.400 -22.280 7.233 1.00 51.58 C
ANISOU 2859 CB ARG A 291 6856 6812 5930 -125 64 224 C
ATOM 2860 CG ARG A 291 -16.704 -21.099 6.608 1.00 54.35 C
ANISOU 2860 CG ARG A 291 7205 7143 6303 -109 93 220 C
ATOM 2861 CD ARG A 291 -15.560 -20.617 7.429 1.00 58.08 C
ANISOU 2861 CD ARG A 291 7654 7608 6808 -108 100 213 C
ATOM 2862 NE ARG A 291 -14.928 -21.733 8.075 1.00 62.24 N
ANISOU 2862 NE ARG A 291 8175 8131 7342 -119 86 215 N
ATOM 2863 CZ ARG A 291 -13.750 -22.223 7.738 1.00 65.00 C
ANISOU 2863 CZ ARG A 291 8529 8455 7712 -113 98 216 C
ATOM 2864 NH1 ARG A 291 -13.077 -21.660 6.778 1.00 65.65 N
ANISOU 2864 NH1 ARG A 291 8620 8515 7810 -97 126 217 N
ATOM 2865 NH2 ARG A 291 -13.255 -23.264 8.375 1.00 64.87 N
ANISOU 2865 NH2 ARG A 291 8509 8437 7702 -124 83 217 N
ATOM 2866 N ILE A 292 -20.234 -24.116 7.134 1.00 49.55 N
ANISOU 2866 N ILE A 292 6628 6599 5601 -149 12 240 N
ATOM 2867 CA ILE A 292 -20.883 -25.134 7.878 1.00 49.63 C
ANISOU 2867 CA ILE A 292 6636 6631 5592 -166 -17 245 C
ATOM 2868 C ILE A 292 -21.917 -25.750 7.013 1.00 50.62 C
ANISOU 2868 C ILE A 292 6786 6757 5690 -165 -27 255 C
ATOM 2869 O ILE A 292 -22.918 -25.174 6.775 1.00 49.80 O
ANISOU 2869 O ILE A 292 6684 6665 5572 -164 -28 255 O
ATOM 2870 CB ILE A 292 -21.500 -24.578 9.171 1.00 49.37 C
ANISOU 2870 CB ILE A 292 6575 6629 5555 -179 -30 238 C
ATOM 2871 CG1 ILE A 292 -20.440 -23.856 9.996 1.00 49.65 C
ANISOU 2871 CG1 ILE A 292 6587 6660 5620 -178 -20 228 C
ATOM 2872 CG2 ILE A 292 -22.124 -25.691 9.983 1.00 49.89 C
ANISOU 2872 CG2 ILE A 292 6638 6718 5601 -199 -61 245 C
ATOM 2873 CD1 ILE A 292 -20.966 -22.985 11.096 1.00 49.32 C
ANISOU 2873 CD1 ILE A 292 6519 6644 5576 -185 -27 219 C
ATOM 2874 N ARG A 293 -21.693 -26.996 6.589 1.00 52.49 N
ANISOU 2874 N ARG A 293 7041 6983 5920 -167 -38 265 N
ATOM 2875 CA ARG A 293 -22.616 -27.753 5.714 1.00 54.10 C
ANISOU 2875 CA ARG A 293 7272 7185 6099 -165 -51 277 C
ATOM 2876 C ARG A 293 -24.163 -28.015 6.042 1.00 53.16 C
ANISOU 2876 C ARG A 293 7153 7094 5951 -178 -76 283 C
ATOM 2877 O ARG A 293 -25.242 -27.868 5.346 1.00 53.91 O
ANISOU 2877 O ARG A 293 7264 7192 6027 -174 -79 288 O
ATOM 2878 CB ARG A 293 -21.931 -29.081 5.331 1.00 57.83 C
ANISOU 2878 CB ARG A 293 7761 7639 6571 -165 -60 285 C
ATOM 2879 CG ARG A 293 -22.728 -29.990 4.410 1.00 65.28 C
ANISOU 2879 CG ARG A 293 8735 8578 7491 -161 -76 299 C
ATOM 2880 CD ARG A 293 -22.067 -31.358 4.276 1.00 72.32 C
ANISOU 2880 CD ARG A 293 9639 9457 8382 -163 -91 306 C
ATOM 2881 NE ARG A 293 -20.819 -31.296 3.520 1.00 78.95 N
ANISOU 2881 NE ARG A 293 10489 10267 9242 -147 -67 302 N
ATOM 2882 CZ ARG A 293 -19.606 -31.421 4.048 1.00 83.62 C
ANISOU 2882 CZ ARG A 293 11065 10849 9857 -149 -60 295 C
ATOM 2883 NH1 ARG A 293 -19.454 -31.614 5.350 1.00 83.20 N
ANISOU 2883 NH1 ARG A 293 10987 10814 9809 -167 -77 290 N
ATOM 2884 NH2 ARG A 293 -18.539 -31.349 3.272 1.00 85.43 N
ANISOU 2884 NH2 ARG A 293 11305 11052 10104 -132 -37 292 N
ATOM 2885 N GLU A 294 -24.341 -28.197 7.338 1.00 51.43 N
ANISOU 2885 N GLU A 294 6909 6901 5729 -196 -94 280 N
ATOM 2886 CA GLU A 294 -25.648 -28.429 7.887 1.00 50.28 C
ANISOU 2886 CA GLU A 294 6758 6785 5560 -211 -117 285 C
ATOM 2887 C GLU A 294 -26.493 -27.163 7.884 1.00 47.53 C
ANISOU 2887 C GLU A 294 6400 6451 5208 -206 -106 277 C
ATOM 2888 O GLU A 294 -27.679 -27.234 7.777 1.00 47.48 O
ANISOU 2888 O GLU A 294 6398 6460 5181 -211 -119 282 O
ATOM 2889 CB GLU A 294 -25.538 -29.057 9.259 1.00 53.58 C
ANISOU 2889 CB GLU A 294 7155 7227 5977 -232 -139 285 C
ATOM 2890 CG GLU A 294 -26.854 -29.493 9.856 1.00 59.73 C
ANISOU 2890 CG GLU A 294 7927 8037 6730 -250 -165 292 C
ATOM 2891 CD GLU A 294 -27.347 -30.820 9.348 1.00 67.39 C
ANISOU 2891 CD GLU A 294 8919 9004 7680 -255 -189 309 C
ATOM 2892 OE1 GLU A 294 -26.532 -31.643 8.940 1.00 70.91 O
ANISOU 2892 OE1 GLU A 294 9380 9429 8134 -252 -192 314 O
ATOM 2893 OE2 GLU A 294 -28.553 -31.030 9.373 1.00 68.61 O
ANISOU 2893 OE2 GLU A 294 9077 9179 7814 -263 -205 316 O
ATOM 2894 N PHE A 295 -25.869 -26.002 8.002 1.00 45.29 N
ANISOU 2894 N PHE A 295 6103 6161 4944 -197 -84 264 N
ATOM 2895 CA PHE A 295 -26.576 -24.733 7.943 1.00 43.70 C
ANISOU 2895 CA PHE A 295 5893 5971 4742 -191 -73 255 C
ATOM 2896 C PHE A 295 -26.900 -24.463 6.492 1.00 44.50 C
ANISOU 2896 C PHE A 295 6023 6049 4838 -175 -60 258 C
ATOM 2897 O PHE A 295 -27.985 -24.118 6.148 1.00 44.32 O
ANISOU 2897 O PHE A 295 6006 6034 4800 -174 -65 258 O
ATOM 2898 CB PHE A 295 -25.713 -23.580 8.461 1.00 41.88 C
ANISOU 2898 CB PHE A 295 5641 5738 4536 -184 -55 241 C
ATOM 2899 CG PHE A 295 -25.990 -23.192 9.882 1.00 40.47 C
ANISOU 2899 CG PHE A 295 5431 5589 4356 -198 -66 233 C
ATOM 2900 CD1 PHE A 295 -27.149 -22.560 10.216 1.00 40.11 C
ANISOU 2900 CD1 PHE A 295 5375 5570 4296 -201 -74 228 C
ATOM 2901 CD2 PHE A 295 -25.091 -23.478 10.870 1.00 40.19 C
ANISOU 2901 CD2 PHE A 295 5378 5557 4336 -206 -70 231 C
ATOM 2902 CE1 PHE A 295 -27.412 -22.217 11.513 1.00 39.82 C
ANISOU 2902 CE1 PHE A 295 5310 5562 4257 -213 -84 220 C
ATOM 2903 CE2 PHE A 295 -25.346 -23.127 12.168 1.00 39.88 C
ANISOU 2903 CE2 PHE A 295 5312 5545 4295 -217 -81 223 C
ATOM 2904 CZ PHE A 295 -26.510 -22.507 12.484 1.00 39.22 C
ANISOU 2904 CZ PHE A 295 5219 5488 4195 -221 -88 218 C
ATOM 2905 N ARG A 296 -25.887 -24.594 5.671 1.00 45.02 N
ANISOU 2905 N ARG A 296 6105 6084 4918 -162 -43 261 N
ATOM 2906 CA ARG A 296 -25.983 -24.406 4.250 1.00 46.60 C
ANISOU 2906 CA ARG A 296 6335 6257 5115 -146 -28 264 C
ATOM 2907 C ARG A 296 -27.118 -25.225 3.629 1.00 48.09 C
ANISOU 2907 C ARG A 296 6547 6448 5278 -148 -47 276 C
ATOM 2908 O ARG A 296 -27.948 -24.674 2.951 1.00 48.60 O
ANISOU 2908 O ARG A 296 6625 6509 5333 -142 -44 275 O
ATOM 2909 CB ARG A 296 -24.640 -24.702 3.633 1.00 48.24 C
ANISOU 2909 CB ARG A 296 6554 6435 5340 -134 -10 266 C
ATOM 2910 CG ARG A 296 -24.631 -24.722 2.146 1.00 52.43 C
ANISOU 2910 CG ARG A 296 7119 6937 5867 -118 5 272 C
ATOM 2911 CD ARG A 296 -23.214 -24.681 1.628 1.00 54.86 C
ANISOU 2911 CD ARG A 296 7432 7217 6196 -105 29 271 C
ATOM 2912 NE ARG A 296 -22.480 -25.911 1.768 1.00 54.20 N
ANISOU 2912 NE ARG A 296 7352 7126 6115 -108 21 278 N
ATOM 2913 CZ ARG A 296 -21.403 -26.041 2.510 1.00 55.45 C
ANISOU 2913 CZ ARG A 296 7491 7284 6295 -113 25 273 C
ATOM 2914 NH1 ARG A 296 -20.787 -27.185 2.589 1.00 55.81 N
ANISOU 2914 NH1 ARG A 296 7542 7322 6342 -116 14 278 N
ATOM 2915 NH2 ARG A 296 -20.946 -25.026 3.191 1.00 54.35 N
ANISOU 2915 NH2 ARG A 296 7327 7151 6174 -114 37 262 N
ATOM 2916 N GLN A 297 -27.167 -26.521 3.920 1.00 48.59 N
ANISOU 2916 N GLN A 297 6616 6517 5331 -158 -69 287 N
ATOM 2917 CA GLN A 297 -28.213 -27.419 3.426 1.00 50.54 C
ANISOU 2917 CA GLN A 297 6883 6765 5553 -162 -91 301 C
ATOM 2918 C GLN A 297 -29.574 -27.004 3.905 1.00 49.97 C
ANISOU 2918 C GLN A 297 6799 6720 5466 -172 -105 299 C
ATOM 2919 O GLN A 297 -30.516 -27.087 3.188 1.00 50.56 O
ANISOU 2919 O GLN A 297 6894 6791 5526 -168 -112 305 O
ATOM 2920 CB GLN A 297 -27.935 -28.874 3.819 1.00 54.37 C
ANISOU 2920 CB GLN A 297 7372 7255 6033 -173 -114 312 C
ATOM 2921 CG GLN A 297 -26.755 -29.493 3.103 1.00 61.42 C
ANISOU 2921 CG GLN A 297 8284 8118 6937 -161 -103 316 C
ATOM 2922 CD GLN A 297 -26.332 -30.833 3.669 1.00 69.80 C
ANISOU 2922 CD GLN A 297 9343 9184 7995 -173 -127 325 C
ATOM 2923 OE1 GLN A 297 -26.618 -31.149 4.807 1.00 72.46 O
ANISOU 2923 OE1 GLN A 297 9658 9547 8327 -192 -147 325 O
ATOM 2924 NE2 GLN A 297 -25.631 -31.626 2.863 1.00 70.85 N
ANISOU 2924 NE2 GLN A 297 9498 9291 8130 -162 -126 331 N
ATOM 2925 N THR A 298 -29.663 -26.546 5.143 1.00 48.30 N
ANISOU 2925 N THR A 298 6556 6538 5258 -185 -109 290 N
ATOM 2926 CA THR A 298 -30.914 -26.089 5.711 1.00 48.28 C
ANISOU 2926 CA THR A 298 6539 6565 5242 -195 -122 286 C
ATOM 2927 C THR A 298 -31.341 -24.764 5.130 1.00 48.24 C
ANISOU 2927 C THR A 298 6536 6553 5241 -182 -104 275 C
ATOM 2928 O THR A 298 -32.492 -24.517 4.996 1.00 48.83 O
ANISOU 2928 O THR A 298 6612 6638 5301 -184 -114 274 O
ATOM 2929 CB THR A 298 -30.834 -25.962 7.238 1.00 48.46 C
ANISOU 2929 CB THR A 298 6526 6620 5267 -211 -131 279 C
ATOM 2930 OG1 THR A 298 -30.176 -27.095 7.772 1.00 49.03 O
ANISOU 2930 OG1 THR A 298 6596 6693 5340 -222 -144 288 O
ATOM 2931 CG2 THR A 298 -32.187 -25.831 7.829 1.00 48.94 C
ANISOU 2931 CG2 THR A 298 6572 6712 5309 -224 -148 279 C
ATOM 2932 N PHE A 299 -30.388 -23.903 4.810 1.00 47.43 N
ANISOU 2932 N PHE A 299 6432 6431 5158 -169 -80 265 N
ATOM 2933 CA PHE A 299 -30.693 -22.626 4.197 1.00 48.26 C
ANISOU 2933 CA PHE A 299 6541 6528 5269 -157 -64 254 C
ATOM 2934 C PHE A 299 -31.339 -22.921 2.825 1.00 51.64 C
ANISOU 2934 C PHE A 299 7005 6932 5684 -147 -65 262 C
ATOM 2935 O PHE A 299 -32.337 -22.347 2.481 1.00 51.80 O
ANISOU 2935 O PHE A 299 7030 6955 5695 -145 -68 258 O
ATOM 2936 CB PHE A 299 -29.434 -21.757 4.006 1.00 46.49 C
ANISOU 2936 CB PHE A 299 6312 6284 5068 -145 -37 244 C
ATOM 2937 CG PHE A 299 -28.862 -21.152 5.275 1.00 44.61 C
ANISOU 2937 CG PHE A 299 6039 6066 4845 -151 -35 233 C
ATOM 2938 CD1 PHE A 299 -29.549 -21.155 6.454 1.00 44.75 C
ANISOU 2938 CD1 PHE A 299 6032 6119 4854 -166 -52 229 C
ATOM 2939 CD2 PHE A 299 -27.619 -20.599 5.264 1.00 44.33 C
ANISOU 2939 CD2 PHE A 299 5996 6014 4833 -142 -14 227 C
ATOM 2940 CE1 PHE A 299 -29.009 -20.599 7.594 1.00 44.67 C
ANISOU 2940 CE1 PHE A 299 5991 6125 4857 -170 -50 219 C
ATOM 2941 CE2 PHE A 299 -27.070 -20.043 6.388 1.00 44.37 C
ANISOU 2941 CE2 PHE A 299 5971 6035 4853 -147 -13 218 C
ATOM 2942 CZ PHE A 299 -27.764 -20.050 7.557 1.00 44.14 C
ANISOU 2942 CZ PHE A 299 5918 6039 4814 -161 -31 214 C
ATOM 2943 N ARG A 300 -30.732 -23.818 2.060 1.00 53.78 N
ANISOU 2943 N ARG A 300 7301 7178 5955 -140 -62 274 N
ATOM 2944 CA ARG A 300 -31.254 -24.200 0.738 1.00 56.79 C
ANISOU 2944 CA ARG A 300 7720 7533 6324 -130 -64 284 C
ATOM 2945 C ARG A 300 -32.668 -24.732 0.818 1.00 58.14 C
ANISOU 2945 C ARG A 300 7896 7720 6474 -139 -90 292 C
ATOM 2946 O ARG A 300 -33.501 -24.366 0.047 1.00 58.68 O
ANISOU 2946 O ARG A 300 7983 7778 6535 -133 -91 291 O
ATOM 2947 CB ARG A 300 -30.359 -25.230 0.068 1.00 59.83 C
ANISOU 2947 CB ARG A 300 8128 7893 6712 -122 -60 296 C
ATOM 2948 CG ARG A 300 -29.009 -24.724 -0.366 1.00 65.39 C
ANISOU 2948 CG ARG A 300 8835 8574 7436 -109 -31 289 C
ATOM 2949 CD ARG A 300 -28.394 -25.707 -1.324 1.00 72.09 C
ANISOU 2949 CD ARG A 300 9714 9394 8283 -98 -28 301 C
ATOM 2950 NE ARG A 300 -26.985 -25.454 -1.542 1.00 77.43 N
ANISOU 2950 NE ARG A 300 10388 10052 8979 -89 -2 297 N
ATOM 2951 CZ ARG A 300 -26.031 -26.300 -1.191 1.00 81.13 C
ANISOU 2951 CZ ARG A 300 10852 10519 9457 -91 -4 301 C
ATOM 2952 NH1 ARG A 300 -24.765 -26.001 -1.440 1.00 81.82 N
ANISOU 2952 NH1 ARG A 300 10936 10587 9563 -82 21 296 N
ATOM 2953 NH2 ARG A 300 -26.349 -27.455 -0.609 1.00 80.98 N
ANISOU 2953 NH2 ARG A 300 10830 10514 9426 -103 -31 310 N
ATOM 2954 N LYS A 301 -32.928 -25.577 1.784 1.00 58.52 N
ANISOU 2954 N LYS A 301 7927 7794 6514 -155 -111 299 N
ATOM 2955 CA LYS A 301 -34.250 -26.113 1.965 1.00 60.35 C
ANISOU 2955 CA LYS A 301 8161 8043 6726 -166 -137 307 C
ATOM 2956 C LYS A 301 -35.253 -25.058 2.304 1.00 60.35 C
ANISOU 2956 C LYS A 301 8145 8064 6724 -169 -138 295 C
ATOM 2957 O LYS A 301 -36.322 -25.054 1.784 1.00 60.60 O
ANISOU 2957 O LYS A 301 8190 8092 6743 -168 -149 298 O
ATOM 2958 CB LYS A 301 -34.244 -27.136 3.069 1.00 63.67 C
ANISOU 2958 CB LYS A 301 8562 8491 7139 -184 -159 316 C
ATOM 2959 CG LYS A 301 -33.602 -28.447 2.727 1.00 69.94 C
ANISOU 2959 CG LYS A 301 9375 9268 7930 -183 -169 331 C
ATOM 2960 CD LYS A 301 -34.161 -29.473 3.674 1.00 76.25 C
ANISOU 2960 CD LYS A 301 10160 10096 8715 -204 -199 342 C
ATOM 2961 CE LYS A 301 -35.649 -29.223 3.865 1.00 81.31 C
ANISOU 2961 CE LYS A 301 10795 10759 9341 -212 -214 344 C
ATOM 2962 NZ LYS A 301 -35.962 -28.196 4.896 1.00 83.51 N
ANISOU 2962 NZ LYS A 301 11039 11068 9623 -221 -207 328 N
ATOM 2963 N ILE A 302 -34.912 -24.167 3.214 1.00 60.42 N
ANISOU 2963 N ILE A 302 8122 8092 6743 -174 -127 280 N
ATOM 2964 CA ILE A 302 -35.826 -23.116 3.586 1.00 61.49 C
ANISOU 2964 CA ILE A 302 8240 8248 6876 -176 -128 266 C
ATOM 2965 C ILE A 302 -36.098 -22.243 2.394 1.00 63.48 C
ANISOU 2965 C ILE A 302 8516 8473 7132 -161 -115 259 C
ATOM 2966 O ILE A 302 -37.211 -21.870 2.157 1.00 64.37 O
ANISOU 2966 O ILE A 302 8632 8590 7235 -161 -124 255 O
ATOM 2967 CB ILE A 302 -35.281 -22.200 4.703 1.00 60.40 C
ANISOU 2967 CB ILE A 302 8067 8133 6751 -180 -118 250 C
ATOM 2968 CG1 ILE A 302 -35.112 -22.947 6.017 1.00 61.11 C
ANISOU 2968 CG1 ILE A 302 8131 8253 6836 -198 -132 255 C
ATOM 2969 CG2 ILE A 302 -36.217 -21.040 4.924 1.00 60.57 C
ANISOU 2969 CG2 ILE A 302 8072 8171 6769 -180 -119 235 C
ATOM 2970 CD1 ILE A 302 -34.306 -22.187 7.026 1.00 60.80 C
ANISOU 2970 CD1 ILE A 302 8062 8228 6812 -200 -121 241 C
ATOM 2971 N ILE A 303 -35.050 -21.901 1.668 1.00 64.24 N
ANISOU 2971 N ILE A 303 8627 8540 7242 -147 -94 257 N
ATOM 2972 CA ILE A 303 -35.169 -21.040 0.519 1.00 66.29 C
ANISOU 2972 CA ILE A 303 8910 8771 7506 -132 -80 250 C
ATOM 2973 C ILE A 303 -35.955 -21.788 -0.570 1.00 70.24 C
ANISOU 2973 C ILE A 303 9447 9249 7992 -127 -92 263 C
ATOM 2974 O ILE A 303 -36.902 -21.260 -1.092 1.00 70.91 O
ANISOU 2974 O ILE A 303 9543 9328 8071 -124 -97 258 O
ATOM 2975 CB ILE A 303 -33.799 -20.524 0.023 1.00 65.33 C
ANISOU 2975 CB ILE A 303 8795 8624 7403 -119 -53 245 C
ATOM 2976 CG1 ILE A 303 -33.184 -19.546 1.008 1.00 64.74 C
ANISOU 2976 CG1 ILE A 303 8686 8569 7344 -122 -42 230 C
ATOM 2977 CG2 ILE A 303 -33.936 -19.755 -1.266 1.00 65.91 C
ANISOU 2977 CG2 ILE A 303 8898 8667 7480 -105 -39 240 C
ATOM 2978 CD1 ILE A 303 -31.705 -19.384 0.804 1.00 65.14 C
ANISOU 2978 CD1 ILE A 303 8737 8599 7413 -113 -19 230 C
ATOM 2979 N ARG A 304 -35.583 -23.024 -0.873 1.00 72.96 N
ANISOU 2979 N ARG A 304 9809 9582 8331 -127 -98 280 N
ATOM 2980 CA ARG A 304 -36.307 -23.784 -1.898 1.00 77.08 C
ANISOU 2980 CA ARG A 304 10367 10082 8839 -121 -112 294 C
ATOM 2981 C ARG A 304 -37.787 -23.919 -1.566 1.00 79.74 C
ANISOU 2981 C ARG A 304 10697 10438 9161 -132 -137 296 C
ATOM 2982 O ARG A 304 -38.613 -23.459 -2.305 1.00 80.90 O
ANISOU 2982 O ARG A 304 10862 10571 9304 -126 -139 293 O
ATOM 2983 CB ARG A 304 -35.639 -25.134 -2.226 1.00 80.06 C
ANISOU 2983 CB ARG A 304 10763 10444 9212 -119 -118 312 C
ATOM 2984 CG ARG A 304 -34.320 -25.013 -2.994 1.00 85.12 C
ANISOU 2984 CG ARG A 304 11422 11055 9866 -103 -92 311 C
ATOM 2985 CD ARG A 304 -33.537 -26.320 -3.047 1.00 90.81 C
ANISOU 2985 CD ARG A 304 12152 11767 10584 -103 -98 326 C
ATOM 2986 NE ARG A 304 -32.182 -26.173 -3.603 1.00 95.61 N
ANISOU 2986 NE ARG A 304 12770 12350 11206 -89 -72 323 N
ATOM 2987 CZ ARG A 304 -31.266 -27.152 -3.676 1.00 99.14 C
ANISOU 2987 CZ ARG A 304 13225 12788 11656 -86 -72 332 C
ATOM 2988 NH1 ARG A 304 -30.070 -26.921 -4.204 1.00 99.08 N
ANISOU 2988 NH1 ARG A 304 13225 12758 11662 -74 -47 328 N
ATOM 2989 NH2 ARG A 304 -31.534 -28.370 -3.229 1.00 99.49 N
ANISOU 2989 NH2 ARG A 304 13268 12845 11689 -96 -99 345 N
ATOM 2990 N SER A 305 -38.107 -24.533 -0.444 1.00 80.81 N
ANISOU 2990 N SER A 305 10806 10607 9289 -148 -154 302 N
ATOM 2991 CA SER A 305 -39.479 -24.707 0.014 1.00 83.01 C
ANISOU 2991 CA SER A 305 11075 10911 9555 -161 -178 304 C
ATOM 2992 C SER A 305 -40.273 -23.426 -0.016 1.00 83.86 C
ANISOU 2992 C SER A 305 11173 11025 9666 -159 -173 286 C
ATOM 2993 O SER A 305 -41.447 -23.443 0.291 1.00 85.03 O
ANISOU 2993 O SER A 305 11312 11191 9804 -167 -190 286 O
ATOM 2994 CB SER A 305 -39.516 -25.242 1.454 1.00 84.52 C
ANISOU 2994 CB SER A 305 11231 11143 9741 -180 -191 307 C
ATOM 2995 OG SER A 305 -39.219 -26.622 1.529 1.00 87.47 O
ANISOU 2995 OG SER A 305 11614 11515 10107 -186 -207 326 O
TER 2996 SER A 305
HETATM 2997 C1 QGE A1201 -22.278 8.662 16.182 0.90 34.42 C
ANISOU 2997 C1 QGE A1201 4298 4868 3911 80 -155 -27 C
HETATM 2998 C10 QGE A1201 -20.118 4.913 18.593 0.90 27.81 C
ANISOU 2998 C10 QGE A1201 3451 4019 3098 55 -115 13 C
HETATM 2999 C11 QGE A1201 -19.225 3.032 19.258 0.90 27.89 C
ANISOU 2999 C11 QGE A1201 3465 4017 3116 38 -95 31 C
HETATM 3000 C12 QGE A1201 -20.546 2.583 19.117 0.90 27.81 C
ANISOU 3000 C12 QGE A1201 3461 4035 3070 28 -98 22 C
HETATM 3001 C13 QGE A1201 -19.755 12.624 15.588 0.90 45.47 C
ANISOU 3001 C13 QGE A1201 5675 6204 5395 125 -193 -19 C
HETATM 3002 C14 QGE A1201 -18.699 11.899 14.808 0.90 46.13 C
ANISOU 3002 C14 QGE A1201 5775 6256 5497 118 -161 2 C
HETATM 3003 C15 QGE A1201 -23.380 10.487 14.877 0.90 36.81 C
ANISOU 3003 C15 QGE A1201 4610 5173 4202 89 -179 -49 C
HETATM 3004 C16 QGE A1201 -23.200 10.290 13.353 0.90 37.89 C
ANISOU 3004 C16 QGE A1201 4775 5282 4340 81 -157 -39 C
HETATM 3005 C17 QGE A1201 -21.848 10.747 12.752 0.90 38.04 C
ANISOU 3005 C17 QGE A1201 4799 5264 4390 87 -145 -23 C
HETATM 3006 C18 QGE A1201 -18.032 2.209 19.710 0.90 27.23 C
ANISOU 3006 C18 QGE A1201 3380 3910 3055 34 -84 45 C
HETATM 3007 C2 QGE A1201 -22.211 9.965 15.729 0.90 36.23 C
ANISOU 3007 C2 QGE A1201 4526 5089 4151 91 -170 -33 C
HETATM 3008 C3 QGE A1201 -21.047 10.689 15.998 0.90 38.02 C
ANISOU 3008 C3 QGE A1201 4741 5295 4409 104 -175 -25 C
HETATM 3009 C4 QGE A1201 -20.032 10.127 16.769 0.90 35.84 C
ANISOU 3009 C4 QGE A1201 4456 5009 4154 105 -166 -12 C
HETATM 3010 C5 QGE A1201 -21.255 8.122 16.957 0.90 32.27 C
ANISOU 3010 C5 QGE A1201 4016 4586 3658 80 -147 -14 C
HETATM 3011 C6 QGE A1201 -20.107 8.822 17.194 0.90 32.80 C
ANISOU 3011 C6 QGE A1201 4073 4631 3757 93 -151 -6 C
HETATM 3012 C7 QGE A1201 -19.104 7.081 18.286 0.90 29.69 C
ANISOU 3012 C7 QGE A1201 3676 4230 3376 81 -131 12 C
HETATM 3013 C8 QGE A1201 -20.184 6.290 18.121 0.90 29.00 C
ANISOU 3013 C8 QGE A1201 3597 4164 3256 68 -127 6 C
HETATM 3014 C9 QGE A1201 -21.376 6.746 17.394 0.90 29.99 C
ANISOU 3014 C9 QGE A1201 3732 4307 3358 67 -134 -7 C
HETATM 3015 N1 QGE A1201 -19.024 4.331 18.993 0.90 27.19 N
ANISOU 3015 N1 QGE A1201 3369 3920 3041 53 -105 26 N
HETATM 3016 O1 QGE A1201 -19.035 8.347 17.891 0.90 31.01 O
ANISOU 3016 O1 QGE A1201 3839 4390 3553 94 -144 7 O
HETATM 3017 O2 QGE A1201 -22.436 6.148 17.140 0.90 29.47 O
ANISOU 3017 O2 QGE A1201 3674 4260 3263 56 -131 -14 O
HETATM 3018 O3 QGE A1201 -20.955 11.998 15.587 0.90 42.15 O
ANISOU 3018 O3 QGE A1201 5261 5810 4943 115 -192 -31 O
HETATM 3019 O4 QGE A1201 -19.485 13.689 16.133 0.90 47.84 O
ANISOU 3019 O4 QGE A1201 5960 6507 5711 140 -218 -24 O
HETATM 3020 S1 QGE A1201 -21.515 3.888 18.543 0.90 28.62 S
ANISOU 3020 S1 QGE A1201 3562 4152 3160 38 -112 7 S
HETATM 3021 NA NA A1202 -23.520 -8.398 16.550 1.00 41.99 NA1+
HETATM 3022 C1 CLR A1203 -8.179 10.793 13.262 1.00 37.16 C
HETATM 3023 C2 CLR A1203 -8.222 12.315 13.213 1.00 36.91 C
HETATM 3024 C3 CLR A1203 -6.837 12.924 12.993 1.00 36.74 C
HETATM 3025 C4 CLR A1203 -6.261 12.448 11.661 1.00 36.51 C
HETATM 3026 C5 CLR A1203 -6.329 10.942 11.565 1.00 36.93 C
HETATM 3027 C6 CLR A1203 -5.243 10.305 11.080 1.00 36.88 C
HETATM 3028 C7 CLR A1203 -5.152 8.798 10.999 1.00 37.10 C
HETATM 3029 C8 CLR A1203 -6.528 8.124 11.016 1.00 37.16 C
HETATM 3030 C9 CLR A1203 -7.374 8.702 12.186 1.00 37.10 C
HETATM 3031 C10 CLR A1203 -7.621 10.207 11.956 1.00 37.29 C
HETATM 3032 C11 CLR A1203 -8.704 7.937 12.460 1.00 37.09 C
HETATM 3033 C12 CLR A1203 -8.471 6.404 12.478 1.00 37.15 C
HETATM 3034 C13 CLR A1203 -7.719 5.869 11.234 1.00 37.78 C
HETATM 3035 C14 CLR A1203 -6.363 6.600 11.149 1.00 37.53 C
HETATM 3036 C15 CLR A1203 -5.558 5.857 10.098 1.00 37.99 C
HETATM 3037 C16 CLR A1203 -5.968 4.411 10.370 1.00 38.21 C
HETATM 3038 C17 CLR A1203 -7.194 4.423 11.313 1.00 38.43 C
HETATM 3039 C18 CLR A1203 -8.577 6.087 9.963 1.00 37.54 C
HETATM 3040 C19 CLR A1203 -8.586 10.463 10.781 1.00 37.24 C
HETATM 3041 C20 CLR A1203 -8.150 3.238 11.054 1.00 39.21 C
HETATM 3042 C21 CLR A1203 -9.429 3.291 11.892 1.00 39.32 C
HETATM 3043 C22 CLR A1203 -7.423 1.930 11.371 1.00 39.94 C
HETATM 3044 C23 CLR A1203 -8.197 0.652 11.043 1.00 40.88 C
HETATM 3045 C24 CLR A1203 -7.291 -0.560 11.276 1.00 41.86 C
HETATM 3046 C25 CLR A1203 -7.993 -1.923 11.254 1.00 42.59 C
HETATM 3047 C26 CLR A1203 -8.795 -2.162 12.525 1.00 42.47 C
HETATM 3048 C27 CLR A1203 -8.879 -2.128 10.031 1.00 43.08 C
HETATM 3049 O1 CLR A1203 -7.012 14.341 12.923 1.00 36.67 O
HETATM 3050 C1 CLR A1204 -3.106 8.273 21.258 1.00 29.04 C
HETATM 3051 C2 CLR A1204 -2.908 9.792 21.186 1.00 28.90 C
HETATM 3052 C3 CLR A1204 -1.917 10.212 20.107 1.00 28.88 C
HETATM 3053 C4 CLR A1204 -2.350 9.681 18.740 1.00 28.91 C
HETATM 3054 C5 CLR A1204 -2.598 8.182 18.833 1.00 29.43 C
HETATM 3055 C6 CLR A1204 -1.994 7.385 17.923 1.00 29.95 C
HETATM 3056 C7 CLR A1204 -2.268 5.894 17.798 1.00 30.49 C
HETATM 3057 C8 CLR A1204 -3.426 5.409 18.685 1.00 30.57 C
HETATM 3058 C9 CLR A1204 -3.431 6.115 20.073 1.00 30.23 C
HETATM 3059 C10 CLR A1204 -3.538 7.653 19.925 1.00 29.57 C
HETATM 3060 C11 CLR A1204 -4.501 5.562 21.070 1.00 30.53 C
HETATM 3061 C12 CLR A1204 -4.528 4.013 21.083 1.00 30.88 C
HETATM 3062 C13 CLR A1204 -4.595 3.368 19.670 1.00 31.67 C
HETATM 3063 C14 CLR A1204 -3.393 3.876 18.840 1.00 31.14 C
HETATM 3064 C15 CLR A1204 -3.365 3.008 17.594 1.00 31.83 C
HETATM 3065 C16 CLR A1204 -3.844 1.646 18.116 1.00 32.63 C
HETATM 3066 C17 CLR A1204 -4.353 1.839 19.565 1.00 32.97 C
HETATM 3067 C18 CLR A1204 -5.959 3.731 19.054 1.00 31.30 C
HETATM 3068 C19 CLR A1204 -4.962 8.127 19.573 1.00 29.20 C
HETATM 3069 C20 CLR A1204 -5.481 0.853 19.962 1.00 34.71 C
HETATM 3070 C21 CLR A1204 -5.905 0.962 21.434 1.00 33.99 C
HETATM 3071 C22 CLR A1204 -5.101 -0.604 19.654 1.00 37.07 C
HETATM 3072 C23 CLR A1204 -6.264 -1.585 19.826 1.00 38.82 C
HETATM 3073 C24 CLR A1204 -5.778 -2.995 20.166 1.00 40.55 C
HETATM 3074 C25 CLR A1204 -5.073 -3.667 18.991 1.00 41.95 C
HETATM 3075 C26 CLR A1204 -4.460 -4.999 19.409 1.00 42.30 C
HETATM 3076 C27 CLR A1204 -6.024 -3.885 17.822 1.00 42.58 C
HETATM 3077 O1 CLR A1204 -1.922 11.641 20.059 1.00 28.77 O
HETATM 3078 C1 CLR A1205 1.196 10.754 21.914 1.00 32.06 C
HETATM 3079 C2 CLR A1205 1.536 12.207 22.250 1.00 32.25 C
HETATM 3080 C3 CLR A1205 1.263 12.533 23.720 1.00 32.16 C
HETATM 3081 C4 CLR A1205 2.053 11.623 24.650 1.00 31.74 C
HETATM 3082 C5 CLR A1205 1.852 10.182 24.265 1.00 31.84 C
HETATM 3083 C6 CLR A1205 1.631 9.340 25.290 1.00 32.05 C
HETATM 3084 C7 CLR A1205 1.363 7.866 25.107 1.00 32.45 C
HETATM 3085 C8 CLR A1205 1.733 7.349 23.705 1.00 32.38 C
HETATM 3086 C9 CLR A1205 1.335 8.357 22.591 1.00 32.03 C
HETATM 3087 C10 CLR A1205 1.964 9.750 22.798 1.00 32.07 C
HETATM 3088 C11 CLR A1205 1.570 7.804 21.148 1.00 31.90 C
HETATM 3089 C12 CLR A1205 0.856 6.431 21.020 1.00 32.16 C
HETATM 3090 C13 CLR A1205 1.293 5.407 22.109 1.00 32.87 C
HETATM 3091 C14 CLR A1205 0.985 6.020 23.490 1.00 32.87 C
HETATM 3092 C15 CLR A1205 1.179 4.902 24.520 1.00 33.46 C
HETATM 3093 C16 CLR A1205 0.677 3.690 23.737 1.00 33.70 C
HETATM 3094 C17 CLR A1205 0.484 4.096 22.247 1.00 33.54 C
HETATM 3095 C18 CLR A1205 2.793 5.082 21.969 1.00 32.92 C
HETATM 3096 C19 CLR A1205 3.454 9.795 22.402 1.00 32.12 C
HETATM 3097 C20 CLR A1205 0.743 2.910 21.296 1.00 34.15 C
HETATM 3098 C21 CLR A1205 0.599 3.230 19.801 1.00 33.81 C
HETATM 3099 C22 CLR A1205 -0.225 1.774 21.674 1.00 35.38 C
HETATM 3100 C23 CLR A1205 0.029 0.434 20.983 1.00 36.68 C
HETATM 3101 C24 CLR A1205 -1.072 -0.508 21.458 1.00 38.21 C
HETATM 3102 C25 CLR A1205 -1.055 -1.910 20.846 1.00 39.59 C
HETATM 3103 C26 CLR A1205 -0.932 -1.950 19.321 1.00 39.28 C
HETATM 3104 C27 CLR A1205 -0.091 -2.836 21.573 1.00 40.34 C
HETATM 3105 O1 CLR A1205 1.673 13.877 23.983 1.00 32.73 O
HETATM 3106 C1 OLA A1206 -8.219 14.834 8.392 1.00 64.81 C
HETATM 3107 O1 OLA A1206 -8.242 15.743 7.526 1.00 65.01 O
HETATM 3108 O2 OLA A1206 -8.591 15.002 9.584 1.00 64.90 O
HETATM 3109 C2 OLA A1206 -7.738 13.467 7.962 1.00 64.11 C
HETATM 3110 C3 OLA A1206 -8.925 12.676 7.427 1.00 63.47 C
HETATM 3111 C4 OLA A1206 -8.512 11.660 6.373 1.00 62.95 C
HETATM 3112 C5 OLA A1206 -8.015 10.370 7.007 1.00 62.58 C
HETATM 3113 C6 OLA A1206 -8.580 9.158 6.278 1.00 62.18 C
HETATM 3114 C7 OLA A1206 -7.626 7.977 6.383 1.00 62.08 C
HETATM 3115 C8 OLA A1206 -7.926 6.935 5.310 1.00 62.17 C
HETATM 3116 C9 OLA A1206 -8.572 5.727 5.948 1.00 62.25 C
HETATM 3117 C10 OLA A1206 -9.634 5.094 5.438 1.00 62.15 C
HETATM 3118 C11 OLA A1206 -10.322 5.473 4.146 1.00 61.98 C
HETATM 3119 C12 OLA A1206 -11.096 4.263 3.629 1.00 61.94 C
HETATM 3120 C13 OLA A1206 -11.604 4.494 2.211 1.00 61.99 C
HETATM 3121 C10 OLA A1207 -28.391 -11.372 3.333 1.00 45.42 C
HETATM 3122 C11 OLA A1207 -28.900 -12.789 3.251 1.00 45.91 C
HETATM 3123 C12 OLA A1207 -30.339 -12.792 2.734 1.00 46.22 C
HETATM 3124 C13 OLA A1207 -30.818 -14.205 2.421 1.00 46.35 C
HETATM 3125 C14 OLA A1207 -32.270 -14.211 1.952 1.00 46.43 C
HETATM 3126 C1 OLA A1208 -31.666 14.407 8.162 1.00 72.30 C
HETATM 3127 O1 OLA A1208 -30.873 13.475 7.890 1.00 72.43 O
HETATM 3128 O2 OLA A1208 -31.263 15.536 8.535 1.00 72.50 O
HETATM 3129 C2 OLA A1208 -33.161 14.182 8.029 1.00 71.79 C
HETATM 3130 C3 OLA A1208 -33.528 12.705 8.153 1.00 71.36 C
HETATM 3131 C4 OLA A1208 -35.038 12.495 8.239 1.00 70.98 C
HETATM 3132 C5 OLA A1208 -35.381 11.012 8.380 1.00 70.62 C
HETATM 3133 C6 OLA A1208 -35.073 10.259 7.090 1.00 70.26 C
HETATM 3134 C7 OLA A1208 -35.231 8.754 7.264 1.00 69.98 C
HETATM 3135 C8 OLA A1208 -36.628 8.287 6.871 1.00 69.73 C
HETATM 3136 C9 OLA A1208 -36.712 8.011 5.383 1.00 69.32 C
HETATM 3137 C10 OLA A1208 -36.928 6.791 4.877 1.00 69.08 C
HETATM 3138 C11 OLA A1208 -37.102 5.553 5.735 1.00 68.94 C
HETATM 3139 C12 OLA A1208 -37.782 4.442 4.940 1.00 68.84 C
HETATM 3140 C2 OLA A1209 -20.273 11.293 -3.654 1.00 49.93 C
HETATM 3141 C3 OLA A1209 -20.668 9.990 -2.967 1.00 49.82 C
HETATM 3142 C4 OLA A1209 -21.825 9.324 -3.698 1.00 49.51 C
HETATM 3143 C5 OLA A1209 -21.493 7.873 -4.032 1.00 49.04 C
HETATM 3144 C6 OLA A1209 -21.768 6.936 -2.860 1.00 48.40 C
HETATM 3145 C7 OLA A1209 -22.831 5.902 -3.223 1.00 47.51 C
HETATM 3146 C8 OLA A1209 -22.716 4.654 -2.359 1.00 46.79 C
HETATM 3147 C9 OLA A1209 -23.986 3.845 -2.461 1.00 46.38 C
HETATM 3148 C1 OLA A1210 -33.689 -10.546 -3.369 1.00 58.04 C
HETATM 3149 C2 OLA A1210 -34.280 -9.445 -2.492 1.00 58.06 C
HETATM 3150 C3 OLA A1210 -33.215 -8.735 -1.658 1.00 58.05 C
HETATM 3151 C4 OLA A1210 -33.829 -7.694 -0.724 1.00 58.24 C
HETATM 3152 C5 OLA A1210 -34.526 -6.572 -1.492 1.00 58.41 C
HETATM 3153 C6 OLA A1210 -34.937 -5.409 -0.596 1.00 58.66 C
HETATM 3154 C7 OLA A1210 -34.006 -4.217 -0.809 1.00 59.00 C
HETATM 3155 C8 OLA A1210 -34.493 -3.007 -0.044 1.00 58.99 C
HETATM 3156 C10 OLA A1210 -9.255 -14.962 16.944 1.00 50.39 C
HETATM 3157 C11 OLA A1210 -10.567 -14.393 17.473 1.00 50.33 C
HETATM 3158 C12 OLA A1210 -10.337 -13.298 18.510 1.00 50.12 C
HETATM 3159 C13 OLA A1210 -10.203 -11.917 17.872 1.00 50.22 C
HETATM 3160 C14 OLA A1210 -9.029 -11.186 18.505 1.00 50.39 C
HETATM 3161 C15 OLA A1210 -8.976 -9.699 18.173 1.00 50.51 C
HETATM 3162 C16 OLA A1210 -7.920 -9.016 19.044 1.00 50.44 C
HETATM 3163 C17 OLA A1210 -8.221 -7.548 19.279 1.00 50.38 C
HETATM 3164 C10 OLC A1211 -4.828 -2.506 25.395 1.00 56.52 C
HETATM 3165 C9 OLC A1211 -4.399 -1.416 24.735 1.00 56.12 C
HETATM 3166 C11 OLC A1211 -5.135 -2.515 26.885 1.00 56.71 C
HETATM 3167 C8 OLC A1211 -4.173 -0.084 25.425 1.00 55.52 C
HETATM 3168 C24 OLC A1211 -1.236 13.113 26.114 1.00 55.68 C
HETATM 3169 C12 OLC A1211 -6.610 -2.810 27.134 1.00 56.56 C
HETATM 3170 C7 OLC A1211 -3.414 0.892 24.537 1.00 54.85 C
HETATM 3171 C6 OLC A1211 -3.094 2.129 25.365 1.00 54.24 C
HETATM 3172 C5 OLC A1211 -3.283 3.437 24.609 1.00 53.55 C
HETATM 3173 C4 OLC A1211 -2.920 4.586 25.542 1.00 53.01 C
HETATM 3174 C3 OLC A1211 -3.030 5.961 24.903 1.00 52.77 C
HETATM 3175 C2 OLC A1211 -2.633 7.010 25.937 1.00 53.21 C
HETATM 3176 C21 OLC A1211 -1.753 10.754 25.472 1.00 55.09 C
HETATM 3177 C1 OLC A1211 -2.510 8.402 25.364 1.00 54.01 C
HETATM 3178 C22 OLC A1211 -2.071 11.876 26.443 1.00 55.71 C
HETATM 3179 O19 OLC A1211 -2.828 8.660 24.235 1.00 54.61 O
HETATM 3180 O25 OLC A1211 -1.995 14.056 25.349 1.00 55.98 O
HETATM 3181 O23 OLC A1211 -3.481 12.144 26.378 1.00 56.40 O
HETATM 3182 O20 OLC A1211 -2.011 9.516 26.130 1.00 54.65 O
HETATM 3183 C18 OLC A1212 -35.500 -1.439 7.800 1.00 43.15 C
HETATM 3184 C10 OLC A1212 -43.572 2.355 14.221 1.00 55.06 C
HETATM 3185 C9 OLC A1212 -43.111 3.582 13.948 1.00 55.00 C
HETATM 3186 C17 OLC A1212 -35.379 -0.768 9.157 1.00 43.02 C
HETATM 3187 C11 OLC A1212 -43.118 1.086 13.531 1.00 54.92 C
HETATM 3188 C8 OLC A1212 -42.060 3.847 12.900 1.00 55.34 C
HETATM 3189 C24 OLC A1212 -40.918 17.187 14.044 1.00 62.47 C
HETATM 3190 C7 OLC A1212 -41.978 5.338 12.597 1.00 55.78 C
HETATM 3191 C6 OLC A1212 -40.716 5.948 13.193 1.00 56.12 C
HETATM 3192 C5 OLC A1212 -40.443 7.356 12.672 1.00 56.68 C
HETATM 3193 C4 OLC A1212 -41.363 8.411 13.279 1.00 57.19 C
HETATM 3194 C3 OLC A1212 -40.658 9.756 13.411 1.00 57.75 C
HETATM 3195 C2 OLC A1212 -41.626 10.924 13.611 1.00 58.62 C
HETATM 3196 C21 OLC A1212 -40.889 14.714 13.954 1.00 61.57 C
HETATM 3197 C1 OLC A1212 -40.913 12.262 13.695 1.00 60.07 C
HETATM 3198 C22 OLC A1212 -41.779 15.929 14.161 1.00 62.33 C
HETATM 3199 O19 OLC A1212 -39.694 12.338 13.796 1.00 60.89 O
HETATM 3200 O25 OLC A1212 -41.322 18.178 15.001 1.00 62.54 O
HETATM 3201 O23 OLC A1212 -42.824 15.919 13.174 1.00 62.82 O
HETATM 3202 O20 OLC A1212 -41.641 13.526 13.671 1.00 60.72 O
HETATM 3203 C10 OLC A1213 -38.428 2.321 14.928 1.00 47.45 C
HETATM 3204 C9 OLC A1213 -37.822 3.174 15.749 1.00 47.52 C
HETATM 3205 C11 OLC A1213 -38.828 0.948 15.415 1.00 47.38 C
HETATM 3206 C8 OLC A1213 -37.425 4.558 15.284 1.00 47.54 C
HETATM 3207 C24 OLC A1213 -39.533 16.478 19.769 1.00 56.71 C
HETATM 3208 C7 OLC A1213 -37.302 5.459 16.509 1.00 47.92 C
HETATM 3209 C6 OLC A1213 -37.016 6.909 16.128 1.00 48.29 C
HETATM 3210 C5 OLC A1213 -37.346 7.910 17.233 1.00 48.71 C
HETATM 3211 C4 OLC A1213 -37.859 9.196 16.599 1.00 49.62 C
HETATM 3212 C3 OLC A1213 -37.787 10.410 17.512 1.00 50.76 C
HETATM 3213 C2 OLC A1213 -38.097 11.692 16.735 1.00 51.95 C
HETATM 3214 C21 OLC A1213 -39.760 15.019 17.754 1.00 55.23 C
HETATM 3215 C1 OLC A1213 -38.727 12.767 17.603 1.00 53.49 C
HETATM 3216 C22 OLC A1213 -39.112 16.284 18.314 1.00 56.23 C
HETATM 3217 O19 OLC A1213 -39.197 12.519 18.702 1.00 53.81 O
HETATM 3218 O25 OLC A1213 -39.454 17.874 20.093 1.00 56.97 O
HETATM 3219 O23 OLC A1213 -37.679 16.246 18.228 1.00 56.34 O
HETATM 3220 O20 OLC A1213 -38.802 14.151 17.153 1.00 54.44 O
HETATM 3221 C1 OLA A1214 -32.084 7.381 36.406 1.00 53.27 C
HETATM 3222 O1 OLA A1214 -33.316 7.436 36.195 1.00 53.82 O
HETATM 3223 O2 OLA A1214 -31.383 8.415 36.536 1.00 53.84 O
HETATM 3224 C2 OLA A1214 -31.402 6.033 36.485 1.00 52.20 C
HETATM 3225 C3 OLA A1214 -32.392 4.900 36.743 1.00 51.31 C
HETATM 3226 C4 OLA A1214 -31.633 3.634 37.090 1.00 50.79 C
HETATM 3227 C5 OLA A1214 -32.595 2.537 37.500 1.00 50.32 C
HETATM 3228 C6 OLA A1214 -31.866 1.510 38.347 1.00 49.78 C
HETATM 3229 C7 OLA A1214 -30.941 0.663 37.494 1.00 49.08 C
HETATM 3230 C8 OLA A1214 -30.044 -0.180 38.380 1.00 48.43 C
HETATM 3231 C9 OLA A1214 -30.775 -1.438 38.747 1.00 48.43 C
HETATM 3232 C10 OLA A1214 -30.071 -2.481 39.170 1.00 48.68 C
HETATM 3233 C1 OLA A1215 -34.554 6.367 32.929 1.00 60.01 C
HETATM 3234 O1 OLA A1215 -35.570 6.419 33.661 1.00 60.63 O
HETATM 3235 O2 OLA A1215 -33.873 7.378 32.650 1.00 59.97 O
HETATM 3236 C2 OLA A1215 -34.149 5.029 32.354 1.00 59.23 C
HETATM 3237 C3 OLA A1215 -32.891 4.497 33.028 1.00 58.48 C
HETATM 3238 C4 OLA A1215 -32.581 3.104 32.489 1.00 57.88 C
HETATM 3239 C5 OLA A1215 -31.497 2.405 33.299 1.00 57.34 C
HETATM 3240 C6 OLA A1215 -30.931 1.209 32.538 1.00 56.96 C
HETATM 3241 C7 OLA A1215 -30.502 0.090 33.479 1.00 56.77 C
HETATM 3242 C8 OLA A1215 -30.323 -1.207 32.713 1.00 56.91 C
HETATM 3243 C9 OLA A1215 -29.966 -2.345 33.644 1.00 57.16 C
HETATM 3244 C10 OLA A1215 -30.681 -3.477 33.723 1.00 57.48 C
HETATM 3245 C11 OLA A1215 -31.939 -3.733 32.909 1.00 57.75 C
HETATM 3246 C12 OLA A1215 -32.064 -5.219 32.586 1.00 57.86 C
HETATM 3247 C13 OLA A1215 -33.199 -5.481 31.601 1.00 57.99 C
HETATM 3248 C14 OLA A1215 -33.373 -6.983 31.386 1.00 58.11 C
HETATM 3249 C15 OLA A1215 -33.424 -7.373 29.908 1.00 58.07 C
HETATM 3250 C16 OLA A1215 -33.135 -8.867 29.731 1.00 57.90 C
HETATM 3251 C17 OLA A1215 -33.739 -9.424 28.447 1.00 57.77 C
HETATM 3252 C18 OLA A1215 -33.727 -10.939 28.449 1.00 57.70 C
HETATM 3253 C18 OLC A1216 -36.908 -0.972 24.879 1.00 62.61 C
HETATM 3254 C10 OLC A1216 -33.745 -8.301 24.350 1.00 61.39 C
HETATM 3255 C9 OLC A1216 -33.413 -9.590 24.445 1.00 61.18 C
HETATM 3256 C17 OLC A1216 -36.389 -1.231 23.477 1.00 62.45 C
HETATM 3257 C11 OLC A1216 -34.700 -7.766 23.313 1.00 61.79 C
HETATM 3258 C8 OLC A1216 -33.912 -10.688 23.530 1.00 60.98 C
HETATM 3259 C24 OLC A1216 -32.236 -23.653 25.072 1.00 67.86 C
HETATM 3260 C16 OLC A1216 -35.535 -2.494 23.412 1.00 62.40 C
HETATM 3261 C12 OLC A1216 -35.585 -6.692 23.942 1.00 62.04 C
HETATM 3262 C7 OLC A1216 -32.917 -11.844 23.582 1.00 60.86 C
HETATM 3263 C15 OLC A1216 -36.357 -3.756 23.660 1.00 62.39 C
HETATM 3264 C13 OLC A1216 -36.618 -6.157 22.952 1.00 62.13 C
HETATM 3265 C6 OLC A1216 -33.416 -13.097 22.876 1.00 60.94 C
HETATM 3266 C14 OLC A1216 -36.240 -4.750 22.506 1.00 62.33 C
HETATM 3267 C5 OLC A1216 -32.402 -14.232 22.998 1.00 61.03 C
HETATM 3268 C4 OLC A1216 -32.865 -15.465 22.233 1.00 61.54 C
HETATM 3269 C3 OLC A1216 -31.961 -16.676 22.451 1.00 62.22 C
HETATM 3270 C2 OLC A1216 -32.798 -17.827 23.003 1.00 63.48 C
HETATM 3271 C21 OLC A1216 -32.129 -21.394 24.005 1.00 66.72 C
HETATM 3272 C1 OLC A1216 -32.192 -19.199 22.798 1.00 64.70 C
HETATM 3273 C22 OLC A1216 -32.906 -22.706 24.083 1.00 67.53 C
HETATM 3274 O19 OLC A1216 -31.129 -19.341 22.223 1.00 64.87 O
HETATM 3275 O25 OLC A1216 -33.006 -24.858 25.177 1.00 68.05 O
HETATM 3276 O23 OLC A1216 -34.245 -22.462 24.522 1.00 68.04 O
HETATM 3277 O20 OLC A1216 -32.871 -20.387 23.310 1.00 65.87 O
HETATM 3278 C1 OLA A1217 -36.215 14.687 13.245 1.00 60.49 C
HETATM 3279 O1 OLA A1217 -35.573 15.736 12.969 1.00 60.76 O
HETATM 3280 O2 OLA A1217 -37.417 14.707 13.600 1.00 60.96 O
HETATM 3281 C2 OLA A1217 -35.492 13.355 13.162 1.00 59.34 C
HETATM 3282 C3 OLA A1217 -36.439 12.170 13.005 1.00 58.28 C
HETATM 3283 C4 OLA A1217 -35.698 10.981 12.396 1.00 57.36 C
HETATM 3284 C5 OLA A1217 -36.599 9.763 12.215 1.00 56.54 C
HETATM 3285 C6 OLA A1217 -35.827 8.621 11.558 1.00 55.84 C
HETATM 3286 C7 OLA A1217 -36.551 7.285 11.693 1.00 55.40 C
HETATM 3287 C8 OLA A1217 -35.625 6.121 11.357 1.00 55.16 C
HETATM 3288 C9 OLA A1217 -36.161 5.320 10.194 1.00 55.07 C
HETATM 3289 C1 OLA A1218 -20.740 13.492 4.038 1.00 64.95 C
HETATM 3290 O1 OLA A1218 -19.752 14.220 4.283 1.00 65.29 O
HETATM 3291 O2 OLA A1218 -21.857 13.693 4.564 1.00 65.19 O
HETATM 3292 C2 OLA A1218 -20.570 12.347 3.060 1.00 64.13 C
HETATM 3293 C3 OLA A1218 -21.481 11.178 3.427 1.00 63.35 C
HETATM 3294 C4 OLA A1218 -20.966 9.868 2.837 1.00 62.63 C
HETATM 3295 C5 OLA A1218 -21.733 8.689 3.421 1.00 61.96 C
HETATM 3296 C6 OLA A1218 -20.926 7.395 3.369 1.00 61.42 C
HETATM 3297 C7 OLA A1218 -21.786 6.220 3.825 1.00 60.80 C
HETATM 3298 C8 OLA A1218 -21.135 4.876 3.524 1.00 60.50 C
HETATM 3299 C9 OLA A1218 -20.956 4.721 2.027 1.00 60.34 C
HETATM 3300 C10 OLA A1218 -20.379 3.666 1.444 1.00 60.23 C
HETATM 3301 C11 OLA A1218 -19.855 2.482 2.216 1.00 60.37 C
HETATM 3302 C12 OLA A1218 -20.651 1.237 1.839 1.00 60.58 C
HETATM 3303 C13 OLA A1218 -20.338 0.084 2.792 1.00 60.68 C
HETATM 3304 C1 OLA A1219 -34.512 -20.945 18.153 1.00 57.10 C
HETATM 3305 O1 OLA A1219 -34.020 -20.887 17.004 1.00 57.70 O
HETATM 3306 O2 OLA A1219 -34.229 -21.873 18.952 1.00 57.18 O
HETATM 3307 C2 OLA A1219 -35.492 -19.875 18.593 1.00 56.24 C
HETATM 3308 C3 OLA A1219 -35.404 -18.607 17.742 1.00 55.65 C
HETATM 3309 C4 OLA A1219 -35.363 -17.356 18.623 1.00 54.97 C
HETATM 3310 C5 OLA A1219 -35.309 -16.088 17.777 1.00 54.28 C
HETATM 3311 C6 OLA A1219 -35.190 -14.841 18.646 1.00 53.73 C
HETATM 3312 C7 OLA A1219 -35.558 -13.595 17.839 1.00 53.32 C
HETATM 3313 C8 OLA A1219 -35.139 -12.327 18.572 1.00 53.03 C
HETATM 3314 C9 OLA A1219 -35.405 -11.096 17.738 1.00 52.86 C
HETATM 3315 C10 OLA A1220 -22.060 -23.453 28.417 1.00 52.55 C
HETATM 3316 C11 OLA A1220 -20.975 -23.084 27.423 1.00 52.44 C
HETATM 3317 C12 OLA A1220 -19.917 -22.203 28.081 1.00 52.03 C
HETATM 3318 C13 OLA A1220 -20.529 -20.879 28.503 1.00 51.84 C
HETATM 3319 C14 OLA A1220 -19.473 -19.903 29.007 1.00 51.87 C
HETATM 3320 C15 OLA A1220 -20.134 -18.616 29.481 1.00 51.89 C
HETATM 3321 C16 OLA A1220 -19.264 -17.403 29.188 1.00 51.99 C
HETATM 3322 C17 OLA A1220 -20.131 -16.154 29.123 1.00 52.17 C
HETATM 3323 C18 OLA A1220 -19.308 -14.951 28.728 1.00 52.26 C
HETATM 3324 O HOH A1301 -32.537 17.183 28.856 1.00 45.06 O
HETATM 3325 O HOH A1302 -1.169 -62.987 20.078 1.00 45.05 O
HETATM 3326 O HOH A1303 -16.214 15.242 20.726 1.00 37.00 O
HETATM 3327 O HOH A1304 -31.337 7.655 32.575 1.00 45.63 O
HETATM 3328 O HOH A1305 -14.560 -27.087 17.347 1.00 42.33 O
HETATM 3329 O HOH A1306 -9.982 14.701 25.259 1.00 45.39 O
HETATM 3330 O HOH A1307 -24.665 23.999 30.164 1.00 63.84 O
HETATM 3331 O HOH A1308 -22.759 -27.965 21.395 1.00 53.93 O
HETATM 3332 O HOH A1309 -23.648 15.493 5.197 1.00 66.57 O
HETATM 3333 O HOH A1310 -4.321 -63.674 27.250 1.00 66.18 O
HETATM 3334 O HOH A1311 -25.323 5.519 18.834 1.00 26.66 O
HETATM 3335 O HOH A1312 -24.846 13.647 11.339 1.00 38.89 O
HETATM 3336 O HOH A1313 -32.463 24.023 26.049 1.00 56.62 O
HETATM 3337 O HOH A1314 -10.328 19.393 20.694 1.00 46.70 O
HETATM 3338 O HOH A1315 -21.888 -6.654 15.619 1.00 26.95 O
HETATM 3339 O HOH A1316 -18.023 13.057 23.840 1.00 45.44 O
HETATM 3340 O HOH A1317 -18.770 -11.490 13.115 1.00 28.48 O
HETATM 3341 O HOH A1318 -25.988 -12.083 21.551 1.00 21.90 O
HETATM 3342 O HOH A1319 -24.395 5.658 15.429 1.00 37.45 O
HETATM 3343 O HOH A1320 -11.286 15.216 23.272 1.00 40.23 O
HETATM 3344 O HOH A1321 -26.275 18.567 22.347 1.00 27.66 O
HETATM 3345 O HOH A1322 -13.311 17.552 11.461 1.00 49.93 O
HETATM 3346 O HOH A1323 -24.258 16.852 2.096 1.00 45.65 O
HETATM 3347 O HOH A1324 -44.437 18.015 12.873 1.00 67.88 O
HETATM 3348 O HOH A1325 -23.621 15.161 33.445 1.00 45.68 O
HETATM 3349 O HOH A1326 -7.302 10.321 30.488 1.00 49.52 O
HETATM 3350 O HOH A1327 -18.271 16.084 16.390 1.00 63.62 O
HETATM 3351 O HOH A1328 17.709 -57.218 18.158 1.00 73.57 O
HETATM 3352 O HOH A1329 -15.332 9.892 17.903 1.00 26.41 O
HETATM 3353 O HOH A1330 -16.196 -16.921 19.166 1.00 29.48 O
HETATM 3354 O HOH A1331 -27.155 -11.463 6.842 1.00 40.49 O
HETATM 3355 O HOH A1332 0.590 -61.919 29.748 1.00 48.55 O
HETATM 3356 O HOH A1333 -25.099 -15.876 14.763 1.00 33.29 O
HETATM 3357 O HOH A1334 -22.294 -9.877 15.411 1.00 46.37 O
HETATM 3358 O HOH A1335 -4.428 14.706 26.501 1.00 58.40 O
HETATM 3359 O HOH A1336 -16.038 0.527 12.585 1.00 23.54 O
HETATM 3360 O HOH A1337 -19.292 -1.734 22.234 1.00 22.56 O
HETATM 3361 O HOH A1338 -28.884 9.147 35.296 1.00 46.44 O
HETATM 3362 O HOH A1339 -23.143 -4.698 14.142 1.00 22.26 O
HETATM 3363 O HOH A1340 -25.307 -13.317 13.685 1.00 29.56 O
HETATM 3364 O HOH A1341 -2.191 13.338 22.234 1.00 38.40 O
HETATM 3365 O HOH A1342 -26.015 -12.047 25.515 1.00 32.70 O
HETATM 3366 O HOH A1343 -21.803 13.343 17.861 1.00 33.62 O
HETATM 3367 O HOH A1344 -31.318 21.521 28.009 1.00 59.57 O
HETATM 3368 O HOH A1345 -23.789 -11.198 11.464 1.00 33.73 O
HETATM 3369 O HOH A1346 -27.496 3.086 16.963 1.00 20.51 O
HETATM 3370 O HOH A1347 -24.988 2.739 15.945 1.00 22.43 O
HETATM 3371 O HOH A1348 -22.559 18.347 26.773 1.00 56.35 O
HETATM 3372 O HOH A1349 -27.596 20.904 22.646 1.00 27.56 O
HETATM 3373 O HOH A1350 -25.387 7.631 13.471 1.00 24.34 O
HETATM 3374 O HOH A1351 -11.433 11.975 15.825 1.00 27.44 O
HETATM 3375 O HOH A1352 -20.778 -2.736 24.319 1.00 25.90 O
HETATM 3376 O HOH A1353 -25.675 -14.363 24.867 1.00 31.81 O
HETATM 3377 O HOH A1354 -28.574 2.609 19.585 1.00 20.24 O
HETATM 3378 O HOH A1355 -15.025 3.471 21.894 1.00 18.89 O
HETATM 3379 O HOH A1356 -37.083 17.552 28.239 1.00 50.33 O
HETATM 3380 O HOH A1357 -4.225 -26.140 25.106 1.00 54.53 O
HETATM 3381 O HOH A1358 -34.072 13.749 30.297 1.00 52.95 O
HETATM 3382 O HOH A1359 -20.608 -11.492 15.342 1.00 35.19 O
HETATM 3383 O HOH A1360 -25.868 18.871 25.098 1.00 27.79 O
HETATM 3384 O HOH A1361 -9.765 14.989 18.534 1.00 47.33 O
HETATM 3385 O HOH A1362 -25.046 12.114 16.697 1.00 33.87 O
HETATM 3386 O HOH A1363 -18.080 -2.921 20.258 1.00 20.45 O
HETATM 3387 O HOH A1364 -34.004 30.224 19.145 1.00 61.07 O
HETATM 3388 O HOH A1365 5.956 -76.114 26.675 1.00 45.48 O
HETATM 3389 O HOH A1366 -25.734 17.168 27.054 1.00 48.25 O
HETATM 3390 O HOH A1367 -18.030 -17.457 16.970 1.00 33.50 O
HETATM 3391 O HOH A1368 -2.867 16.792 24.645 1.00 66.33 O
HETATM 3392 O HOH A1369 -29.748 18.076 29.523 1.00 57.91 O
HETATM 3393 O HOH A1370 -16.512 16.756 8.492 1.00 42.91 O
HETATM 3394 O HOH A1371 -27.588 5.416 17.661 1.00 23.55 O
HETATM 3395 O HOH A1372 -27.812 11.778 34.812 1.00 54.37 O
HETATM 3396 O HOH A1373 -25.642 -29.585 23.042 1.00 48.21 O
HETATM 3397 O HOH A1374 -35.967 18.356 16.426 1.00 48.17 O
HETATM 3398 O HOH A1375 3.066 -73.385 24.225 1.00 61.83 O
HETATM 3399 O HOH A1376 -20.966 16.530 18.744 1.00 55.22 O
HETATM 3400 O HOH A1377 -24.816 -6.609 17.581 1.00 35.76 O
HETATM 3401 O HOH A1378 -21.019 -27.390 17.695 1.00 56.46 O
HETATM 3402 O HOH A1379 -17.201 15.065 5.889 1.00 38.29 O
HETATM 3403 O HOH A1380 -16.888 13.590 26.296 1.00 43.02 O
HETATM 3404 O HOH A1381 -3.539 16.271 21.762 1.00 39.43 O
HETATM 3405 O HOH A1382 -21.985 -29.332 9.128 1.00 53.41 O
HETATM 3406 O HOH A1383 -15.004 12.310 28.561 1.00 29.37 O
HETATM 3407 O HOH A1384 -17.948 16.419 19.237 1.00 63.50 O
HETATM 3408 O HOH A1385 -9.201 13.355 16.659 1.00 29.63 O
HETATM 3409 O HOH A1386 -11.289 10.664 32.512 1.00 44.78 O
HETATM 3410 O HOH A1387 -17.234 12.074 32.583 1.00 52.50 O
HETATM 3411 O HOH A1388 -20.415 -18.256 15.746 1.00 48.80 O
HETATM 3412 O HOH A1389 -18.812 -28.298 7.467 1.00 53.45 O
HETATM 3413 O HOH A1390 -17.466 14.807 12.261 1.00 42.89 O
HETATM 3414 O HOH A1391 -15.357 13.823 31.210 1.00 58.49 O
HETATM 3415 O HOH A1392 -5.986 -61.485 28.413 1.00 61.10 O
HETATM 3416 O HOH A1393 -11.388 17.472 17.820 1.00 60.56 O
HETATM 3417 O HOH A1394 -31.001 -29.884 6.110 1.00 55.27 O
HETATM 3418 O HOH A1395 8.113 -72.762 21.932 1.00 59.64 O
HETATM 3419 O HOH A1396 -7.242 14.528 26.751 1.00 64.74 O
HETATM 3420 O HOH A1397 -15.913 16.855 12.056 1.00 64.98 O
HETATM 3421 O HOH A1398 -29.144 15.050 34.325 1.00 61.31 O
HETATM 3422 O HOH A1399 -12.713 13.510 30.067 1.00 62.30 O
HETATM 3423 O HOH A1400 -7.723 12.227 27.917 1.00 66.11 O
HETATM 3424 O HOH A1401 -23.638 13.945 13.776 1.00 68.47 O
HETATM 3425 O HOH A1402 -13.482 13.724 24.046 1.00 37.11 O
HETATM 3426 O HOH A1403 -31.263 16.469 31.195 1.00 59.45 O
HETATM 3427 O HOH A1404 -15.736 14.255 22.865 1.00 49.27 O
CONECT 410 3021
CONECT 546 1201
CONECT 562 1110
CONECT 589 1245
CONECT 694 3021
CONECT 1110 562
CONECT 1201 546
CONECT 1245 589
CONECT 2606 2627
CONECT 2627 2606
CONECT 2997 3007 3010
CONECT 2998 3013 3015 3020
CONECT 2999 3000 3006 3015
CONECT 3000 2999 3020
CONECT 3001 3002 3018 3019
CONECT 3002 3001
CONECT 3003 3004 3007
CONECT 3004 3003 3005
CONECT 3005 3004
CONECT 3006 2999
CONECT 3007 2997 3003 3008
CONECT 3008 3007 3009 3018
CONECT 3009 3008 3011
CONECT 3010 2997 3011 3014
CONECT 3011 3009 3010 3016
CONECT 3012 3013 3016
CONECT 3013 2998 3012 3014
CONECT 3014 3010 3013 3017
CONECT 3015 2998 2999
CONECT 3016 3011 3012
CONECT 3017 3014
CONECT 3018 3001 3008
CONECT 3019 3001
CONECT 3020 2998 3000
CONECT 3021 410 694 3338 3357
CONECT 3021 3400
CONECT 3022 3023 3031
CONECT 3023 3022 3024
CONECT 3024 3023 3025 3049
CONECT 3025 3024 3026
CONECT 3026 3025 3027 3031
CONECT 3027 3026 3028
CONECT 3028 3027 3029
CONECT 3029 3028 3030 3035
CONECT 3030 3029 3031 3032
CONECT 3031 3022 3026 3030 3040
CONECT 3032 3030 3033
CONECT 3033 3032 3034
CONECT 3034 3033 3035 3038 3039
CONECT 3035 3029 3034 3036
CONECT 3036 3035 3037
CONECT 3037 3036 3038
CONECT 3038 3034 3037 3041
CONECT 3039 3034
CONECT 3040 3031
CONECT 3041 3038 3042 3043
CONECT 3042 3041
CONECT 3043 3041 3044
CONECT 3044 3043 3045
CONECT 3045 3044 3046
CONECT 3046 3045 3047 3048
CONECT 3047 3046
CONECT 3048 3046
CONECT 3049 3024
CONECT 3050 3051 3059
CONECT 3051 3050 3052
CONECT 3052 3051 3053 3077
CONECT 3053 3052 3054
CONECT 3054 3053 3055 3059
CONECT 3055 3054 3056
CONECT 3056 3055 3057
CONECT 3057 3056 3058 3063
CONECT 3058 3057 3059 3060
CONECT 3059 3050 3054 3058 3068
CONECT 3060 3058 3061
CONECT 3061 3060 3062
CONECT 3062 3061 3063 3066 3067
CONECT 3063 3057 3062 3064
CONECT 3064 3063 3065
CONECT 3065 3064 3066
CONECT 3066 3062 3065 3069
CONECT 3067 3062
CONECT 3068 3059
CONECT 3069 3066 3070 3071
CONECT 3070 3069
CONECT 3071 3069 3072
CONECT 3072 3071 3073
CONECT 3073 3072 3074
CONECT 3074 3073 3075 3076
CONECT 3075 3074
CONECT 3076 3074
CONECT 3077 3052
CONECT 3078 3079 3087
CONECT 3079 3078 3080
CONECT 3080 3079 3081 3105
CONECT 3081 3080 3082
CONECT 3082 3081 3083 3087
CONECT 3083 3082 3084
CONECT 3084 3083 3085
CONECT 3085 3084 3086 3091
CONECT 3086 3085 3087 3088
CONECT 3087 3078 3082 3086 3096
CONECT 3088 3086 3089
CONECT 3089 3088 3090
CONECT 3090 3089 3091 3094 3095
CONECT 3091 3085 3090 3092
CONECT 3092 3091 3093
CONECT 3093 3092 3094
CONECT 3094 3090 3093 3097
CONECT 3095 3090
CONECT 3096 3087
CONECT 3097 3094 3098 3099
CONECT 3098 3097
CONECT 3099 3097 3100
CONECT 3100 3099 3101
CONECT 3101 3100 3102
CONECT 3102 3101 3103 3104
CONECT 3103 3102
CONECT 3104 3102
CONECT 3105 3080
CONECT 3106 3107 3108 3109
CONECT 3107 3106
CONECT 3108 3106
CONECT 3109 3106 3110
CONECT 3110 3109 3111
CONECT 3111 3110 3112
CONECT 3112 3111 3113
CONECT 3113 3112 3114
CONECT 3114 3113 3115
CONECT 3115 3114 3116
CONECT 3116 3115 3117
CONECT 3117 3116 3118
CONECT 3118 3117 3119
CONECT 3119 3118 3120
CONECT 3120 3119
CONECT 3121 3122
CONECT 3122 3121 3123
CONECT 3123 3122 3124
CONECT 3124 3123 3125
CONECT 3125 3124
CONECT 3126 3127 3128 3129
CONECT 3127 3126
CONECT 3128 3126
CONECT 3129 3126 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 3138
CONECT 3138 3137 3139
CONECT 3139 3138
CONECT 3140 3141
CONECT 3141 3140 3142
CONECT 3142 3141 3143
CONECT 3143 3142 3144
CONECT 3144 3143 3145
CONECT 3145 3144 3146
CONECT 3146 3145 3147
CONECT 3147 3146
CONECT 3148 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
CONECT 3157 3156 3158
CONECT 3158 3157 3159
CONECT 3159 3158 3160
CONECT 3160 3159 3161
CONECT 3161 3160 3162
CONECT 3162 3161 3163
CONECT 3163 3162
CONECT 3164 3165 3166
CONECT 3165 3164 3167
CONECT 3166 3164 3169
CONECT 3167 3165 3170
CONECT 3168 3178 3180
CONECT 3169 3166
CONECT 3170 3167 3171
CONECT 3171 3170 3172
CONECT 3172 3171 3173
CONECT 3173 3172 3174
CONECT 3174 3173 3175
CONECT 3175 3174 3177
CONECT 3176 3178 3182
CONECT 3177 3175 3179 3182
CONECT 3178 3168 3176 3181
CONECT 3179 3177
CONECT 3180 3168
CONECT 3181 3178
CONECT 3182 3176 3177
CONECT 3183 3186
CONECT 3184 3185 3187
CONECT 3185 3184 3188
CONECT 3186 3183
CONECT 3187 3184
CONECT 3188 3185 3190
CONECT 3189 3198 3200
CONECT 3190 3188 3191
CONECT 3191 3190 3192
CONECT 3192 3191 3193
CONECT 3193 3192 3194
CONECT 3194 3193 3195
CONECT 3195 3194 3197
CONECT 3196 3198 3202
CONECT 3197 3195 3199 3202
CONECT 3198 3189 3196 3201
CONECT 3199 3197
CONECT 3200 3189
CONECT 3201 3198
CONECT 3202 3196 3197
CONECT 3203 3204 3205
CONECT 3204 3203 3206
CONECT 3205 3203
CONECT 3206 3204 3208
CONECT 3207 3216 3218
CONECT 3208 3206 3209
CONECT 3209 3208 3210
CONECT 3210 3209 3211
CONECT 3211 3210 3212
CONECT 3212 3211 3213
CONECT 3213 3212 3215
CONECT 3214 3216 3220
CONECT 3215 3213 3217 3220
CONECT 3216 3207 3214 3219
CONECT 3217 3215
CONECT 3218 3207
CONECT 3219 3216
CONECT 3220 3214 3215
CONECT 3221 3222 3223 3224
CONECT 3222 3221
CONECT 3223 3221
CONECT 3224 3221 3225
CONECT 3225 3224 3226
CONECT 3226 3225 3227
CONECT 3227 3226 3228
CONECT 3228 3227 3229
CONECT 3229 3228 3230
CONECT 3230 3229 3231
CONECT 3231 3230 3232
CONECT 3232 3231
CONECT 3233 3234 3235 3236
CONECT 3234 3233
CONECT 3235 3233
CONECT 3236 3233 3237
CONECT 3237 3236 3238
CONECT 3238 3237 3239
CONECT 3239 3238 3240
CONECT 3240 3239 3241
CONECT 3241 3240 3242
CONECT 3242 3241 3243
CONECT 3243 3242 3244
CONECT 3244 3243 3245
CONECT 3245 3244 3246
CONECT 3246 3245 3247
CONECT 3247 3246 3248
CONECT 3248 3247 3249
CONECT 3249 3248 3250
CONECT 3250 3249 3251
CONECT 3251 3250 3252
CONECT 3252 3251
CONECT 3253 3256
CONECT 3254 3255 3257
CONECT 3255 3254 3258
CONECT 3256 3253 3260
CONECT 3257 3254 3261
CONECT 3258 3255 3262
CONECT 3259 3273 3275
CONECT 3260 3256 3263
CONECT 3261 3257 3264
CONECT 3262 3258 3265
CONECT 3263 3260 3266
CONECT 3264 3261 3266
CONECT 3265 3262 3267
CONECT 3266 3263 3264
CONECT 3267 3265 3268
CONECT 3268 3267 3269
CONECT 3269 3268 3270
CONECT 3270 3269 3272
CONECT 3271 3273 3277
CONECT 3272 3270 3274 3277
CONECT 3273 3259 3271 3276
CONECT 3274 3272
CONECT 3275 3259
CONECT 3276 3273
CONECT 3277 3271 3272
CONECT 3278 3279 3280 3281
CONECT 3279 3278
CONECT 3280 3278
CONECT 3281 3278 3282
CONECT 3282 3281 3283
CONECT 3283 3282 3284
CONECT 3284 3283 3285
CONECT 3285 3284 3286
CONECT 3286 3285 3287
CONECT 3287 3286 3288
CONECT 3288 3287
CONECT 3289 3290 3291 3292
CONECT 3290 3289
CONECT 3291 3289
CONECT 3292 3289 3293
CONECT 3293 3292 3294
CONECT 3294 3293 3295
CONECT 3295 3294 3296
CONECT 3296 3295 3297
CONECT 3297 3296 3298
CONECT 3298 3297 3299
CONECT 3299 3298 3300
CONECT 3300 3299 3301
CONECT 3301 3300 3302
CONECT 3302 3301 3303
CONECT 3303 3302
CONECT 3304 3305 3306 3307
CONECT 3305 3304
CONECT 3306 3304
CONECT 3307 3304 3308
CONECT 3308 3307 3309
CONECT 3309 3308 3310
CONECT 3310 3309 3311
CONECT 3311 3310 3312
CONECT 3312 3311 3313
CONECT 3313 3312 3314
CONECT 3314 3313
CONECT 3315 3316
CONECT 3316 3315 3317
CONECT 3317 3316 3318
CONECT 3318 3317 3319
CONECT 3319 3318 3320
CONECT 3320 3319 3321
CONECT 3321 3320 3322
CONECT 3322 3321 3323
CONECT 3323 3322
CONECT 3338 3021
CONECT 3357 3021
CONECT 3400 3021
MASTER 493 0 20 18 2 0 30 6 3389 1 341 34
END