HEADER MEMBRANE PROTEIN 19-AUG-17 6AQF
TITLE CRYSTAL STRUCTURE OF A2AAR-BRIL IN COMPLEX WITH THE ANTAGONIST
TITLE 2 ZM241385 PRODUCED FROM PICHIA PASTORIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE
COMPND 3 RECEPTOR A2A;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP P29274 RESIDUES 2-208 AND 219-316 LINKED VIA UNP P0ABE7
COMPND 6 RESIDUES 23-128,UNP P29274 RESIDUES 2-208 AND 219-316 LINKED VIA UNP
COMPND 7 P0ABE7 RESIDUES 23-128,UNP P29274 RESIDUES 2-208 AND 219-316 LINKED
COMPND 8 VIA UNP P0ABE7 RESIDUES 23-128;
COMPND 9 SYNONYM: CYTOCHROME B-562;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: 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: PICHIA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4919
KEYWDS A2AAR, GPCR, ADENOSINE RECEPTOR, HUMAN A2AAR_BRIL CHIMERA, LCP,
KEYWDS 2 ANTAGONIST COMPLEX, PICHIA PASTORIS, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.T.EDDY,M.Y.LEE,Z.GAO,K.WHITE,T.DIDENKO,R.HORST,M.AUDET,P.STANCZAK,
AUTHOR 2 K.M.MCCLARY,G.W.HAN,K.A.JACOBSON,R.C.STEVENS,K.WUTHRICH
REVDAT 3 24-JAN-18 6AQF 1 JRNL
REVDAT 2 17-JAN-18 6AQF 1 JRNL
REVDAT 1 10-JAN-18 6AQF 0
JRNL AUTH M.T.EDDY,M.Y.LEE,Z.G.GAO,K.L.WHITE,T.DIDENKO,R.HORST,
JRNL AUTH 2 M.AUDET,P.STANCZAK,K.M.MCCLARY,G.W.HAN,K.A.JACOBSON,
JRNL AUTH 3 R.C.STEVENS,K.WUTHRICH
JRNL TITL ALLOSTERIC COUPLING OF DRUG BINDING AND INTRACELLULAR
JRNL TITL 2 SIGNALING IN THE A2A ADENOSINE RECEPTOR.
JRNL REF CELL V. 172 68 2018
JRNL REFN ISSN 1097-4172
JRNL PMID 29290469
JRNL DOI 10.1016/J.CELL.2017.12.004
REMARK 2
REMARK 2 RESOLUTION. 2.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 3 NUMBER OF REFLECTIONS : 16035
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 797
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.68
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.40
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2455
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2120
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2349
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.32
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 106
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2950
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 288
REMARK 3 SOLVENT ATOMS : 19
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.66500
REMARK 3 B22 (A**2) : 0.79790
REMARK 3 B33 (A**2) : 0.86710
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) : 0.380
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.585
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.295
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.597
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.300
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 : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3313 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4487 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1550 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 57 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 470 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3313 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 444 ; 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 : 3714 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.16
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.96
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|-2 - A|306 }
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2278 188.3940 17.7777
REMARK 3 T TENSOR
REMARK 3 T11: -0.1732 T22: -0.2452
REMARK 3 T33: -0.2656 T12: -0.0024
REMARK 3 T13: -0.0007 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.8681 L22: 1.1336
REMARK 3 L33: 0.9304 L12: -0.1586
REMARK 3 L13: -0.0706 L23: 0.0261
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: 0.0151 S13: 0.0597
REMARK 3 S21: -0.0518 S22: -0.0214 S23: 0.0480
REMARK 3 S31: -0.0825 S32: 0.0283 S33: 0.0163
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1001 - A|1106 }
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3143 236.4660 20.2439
REMARK 3 T TENSOR
REMARK 3 T11: -0.1617 T22: -0.2967
REMARK 3 T33: 0.0962 T12: 0.0591
REMARK 3 T13: -0.0156 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 2.7786 L22: 9.3011
REMARK 3 L33: 4.7623 L12: -2.6997
REMARK 3 L13: -0.3787 L23: 1.8571
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: -0.2175 S13: -0.2760
REMARK 3 S21: -0.0832 S22: 0.1664 S23: 0.2060
REMARK 3 S31: -0.0237 S32: 0.0679 S33: -0.1734
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6AQF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229566.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-15
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 : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16063
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.160
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.64800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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: 4EIY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-28 % (V/V) PEG400 40-60 MM SODIUM
REMARK 280 THIOCYANATE 2% (V/V) 2,5-HEXANEDIOL 100MM SODIUM CITRATE PH 5.0,
REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.28700
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 70.28700
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 19.91850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.48650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.91850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.48650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.28700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.91850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.48650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.28700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.91850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.48650
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 MET A -9
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 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 VAL A 307
REMARK 465 LEU A 308
REMARK 465 ARG A 309
REMARK 465 GLN A 310
REMARK 465 GLN A 311
REMARK 465 GLU A 312
REMARK 465 PRO A 313
REMARK 465 PHE A 314
REMARK 465 LYS A 315
REMARK 465 ALA A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 107 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 111 NE CZ NH1 NH2
REMARK 470 LYS A 122 CD CE NZ
REMARK 470 GLN A 148 CG CD OE1 NE2
REMARK 470 LYS A 153 CG CD CE NZ
REMARK 470 GLU A 161 CG CD OE1 OE2
REMARK 470 ARG A 199 NE CZ NH1 NH2
REMARK 470 ARG A 206 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1002 CG OD1 OD2
REMARK 470 LYS A1015 CG CD CE NZ
REMARK 470 LYS A1019 CG CD CE NZ
REMARK 470 LYS A1032 CG CD CE NZ
REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2
REMARK 470 HIS A1063 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 ARG A 220 CD NE CZ NH1 NH2
REMARK 470 ARG A 222 NE CZ NH1 NH2
REMARK 470 LYS A 227 CD CE NZ
REMARK 470 LYS A 233 CG CD CE NZ
REMARK 470 ASP A 261 CG OD1 OD2
REMARK 470 ARG A 293 CZ NH1 NH2
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 CYS A 166 90.91 -63.63
REMARK 500 TYR A1101 -53.17 -128.72
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 OLB A 1205
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 OLA A 1211
REMARK 610 OLA A 1212
REMARK 610 OLC A 1213
REMARK 610 OLC A 1214
REMARK 610 OLC A 1215
REMARK 610 OLC A 1216
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZMA A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR 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 OLB 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 OLA A 1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA 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 OLC A 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC 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
DBREF 6AQF A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 6AQF A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 6AQF A 219 316 UNP P29274 AA2AR_HUMAN 219 316
SEQADV 6AQF MET A -9 UNP P29274 INITIATING METHIONINE
SEQADV 6AQF ASP A -8 UNP P29274 EXPRESSION TAG
SEQADV 6AQF TYR A -7 UNP P29274 EXPRESSION TAG
SEQADV 6AQF LYS A -6 UNP P29274 EXPRESSION TAG
SEQADV 6AQF ASP A -5 UNP P29274 EXPRESSION TAG
SEQADV 6AQF ASP A -4 UNP P29274 EXPRESSION TAG
SEQADV 6AQF ASP A -3 UNP P29274 EXPRESSION TAG
SEQADV 6AQF ASP A -2 UNP P29274 EXPRESSION TAG
SEQADV 6AQF GLY A -1 UNP P29274 EXPRESSION TAG
SEQADV 6AQF ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 6AQF PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 6AQF TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 6AQF ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 6AQF LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 6AQF HIS A 317 UNP P29274 EXPRESSION TAG
SEQADV 6AQF HIS A 318 UNP P29274 EXPRESSION TAG
SEQADV 6AQF HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 6AQF HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 6AQF HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 6AQF HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 6AQF HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 6AQF HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 6AQF HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 6AQF HIS A 326 UNP P29274 EXPRESSION TAG
SEQRES 1 A 432 MET ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE
SEQRES 2 A 432 MET GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE
SEQRES 3 A 432 ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP
SEQRES 4 A 432 ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN
SEQRES 5 A 432 TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE ALA VAL
SEQRES 6 A 432 GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR
SEQRES 7 A 432 GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA
SEQRES 8 A 432 CYS PHE VAL LEU VAL LEU THR GLN SER SER ILE PHE SER
SEQRES 9 A 432 LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ARG
SEQRES 10 A 432 ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG
SEQRES 11 A 432 ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE
SEQRES 12 A 432 ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS
SEQRES 13 A 432 GLY GLN PRO LYS GLU GLY LYS ASN HIS SER GLN GLY CYS
SEQRES 14 A 432 GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL
SEQRES 15 A 432 PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS
SEQRES 16 A 432 VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU
SEQRES 17 A 432 ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU ALA ASP LEU
SEQRES 18 A 432 GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL
SEQRES 19 A 432 ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA
SEQRES 20 A 432 LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS
SEQRES 21 A 432 ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER
SEQRES 22 A 432 PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU
SEQRES 23 A 432 VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU
SEQRES 24 A 432 GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU
SEQRES 25 A 432 LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU
SEQRES 26 A 432 ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA
SEQRES 27 A 432 LYS SER LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS
SEQRES 28 A 432 TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE
SEQRES 29 A 432 CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR
SEQRES 30 A 432 LEU ALA ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN
SEQRES 31 A 432 PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN
SEQRES 32 A 432 THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN
SEQRES 33 A 432 GLN GLU PRO PHE LYS ALA HIS HIS HIS HIS HIS HIS HIS
SEQRES 34 A 432 HIS HIS HIS
HET ZMA A1201 25
HET CLR A1202 28
HET CLR A1203 28
HET CLR A1204 28
HET OLB A1205 15
HET OLA A1206 16
HET OLA A1207 16
HET OLA A1208 14
HET OLA A1209 18
HET OLA A1210 11
HET OLA A1211 9
HET OLA A1212 14
HET OLC A1213 19
HET OLC A1214 16
HET OLC A1215 17
HET OLC A1216 14
HETNAM ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3,
HETNAM 2 ZMA 5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL
HETNAM CLR CHOLESTEROL
HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM OLA OLEIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 ZMA C16 H15 N7 O2
FORMUL 3 CLR 3(C27 H46 O)
FORMUL 6 OLB C21 H40 O4
FORMUL 7 OLA 7(C18 H34 O2)
FORMUL 14 OLC 4(C21 H40 O4)
FORMUL 18 HOH *19(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 SER A 67 1 10
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 GLY A 158 1 9
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 ALA A 1020 1 43
HELIX 13 AB4 ASN A 1022 LYS A 1042 1 21
HELIX 14 AB5 LYS A 1059 GLU A 1081 1 23
HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11
HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9
HELIX 17 AB8 TYR A 1101 CYS A 259 1 47
HELIX 18 AB9 PRO A 266 THR A 279 1 14
HELIX 19 AC1 THR A 279 ILE A 292 1 14
HELIX 20 AC2 ILE A 292 HIS A 306 1 15
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 2.05
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.04
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.04
SITE 1 AC1 11 LEU A 85 PHE A 168 GLU A 169 MET A 177
SITE 2 AC1 11 TRP A 246 LEU A 249 HIS A 250 ASN A 253
SITE 3 AC1 11 MET A 270 ILE A 274 HOH A1312
SITE 1 AC2 3 PRO A 248 SER A 263 OLA A1207
SITE 1 AC3 4 CYS A 254 PHE A 255 CYS A 259 OLC A1213
SITE 1 AC4 5 ALA A 72 ALA A 73 GLY A 76 ILE A 80
SITE 2 AC4 5 OLC A1215
SITE 1 AC5 4 HIS A 75 MET A 140 TYR A 179 OLC A1214
SITE 1 AC6 4 THR A 65 PHE A 70 OLA A1207 OLC A1213
SITE 1 AC7 5 PHE A 255 CYS A 262 CLR A1202 OLA A1206
SITE 2 AC7 5 OLC A1213
SITE 1 AC8 2 TRP A 268 OLA A1212
SITE 1 AC9 4 GLY A 5 LEU A 267 TYR A 271 OLA A1212
SITE 1 AD1 2 ILE A 3 SER A 7
SITE 1 AD2 4 ALA A 97 ASP A 101 VAL A 116 ILE A 124
SITE 1 AD3 3 TYR A 290 OLA A1208 OLA A1209
SITE 1 AD4 7 THR A 65 PHE A 70 CYS A 71 CLR A1203
SITE 2 AD4 7 OLA A1206 OLA A1207 HOH A1304
SITE 1 AD5 4 TYR A 179 OLB A1205 OLC A1215 OLC A1216
SITE 1 AD6 3 PHE A 258 CLR A1204 OLC A1214
SITE 1 AD7 2 OLC A1214 HOH A1307
CRYST1 39.837 180.973 140.574 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 0.025102 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005526 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007114 0.00000
ATOM 1 N ASP A -2 22.775 152.793 1.254 1.00 90.47 N
ANISOU 1 N ASP A -2 13351 9728 11295 281 -52 -1594 N
ATOM 2 CA ASP A -2 22.269 153.019 2.606 1.00 89.28 C
ANISOU 2 CA ASP A -2 13110 9568 11244 221 -52 -1483 C
ATOM 3 C ASP A -2 22.357 154.515 2.960 1.00 90.40 C
ANISOU 3 C ASP A -2 13152 9868 11327 221 -52 -1389 C
ATOM 4 O ASP A -2 23.067 154.895 3.896 1.00 89.32 O
ANISOU 4 O ASP A -2 12960 9770 11209 266 6 -1285 O
ATOM 5 CB ASP A -2 23.036 152.158 3.638 1.00 91.52 C
ANISOU 5 CB ASP A -2 13405 9752 11617 278 26 -1415 C
ATOM 6 CG ASP A -2 23.223 150.703 3.255 1.00105.53 C
ANISOU 6 CG ASP A -2 15289 11366 13443 304 43 -1503 C
ATOM 7 OD1 ASP A -2 22.219 149.957 3.245 1.00107.64 O
ANISOU 7 OD1 ASP A -2 15589 11521 13788 214 -5 -1556 O
ATOM 8 OD2 ASP A -2 24.377 150.304 2.994 1.00112.14 O
ANISOU 8 OD2 ASP A -2 16175 12184 14247 416 107 -1518 O
ATOM 9 N GLY A -1 21.644 155.343 2.196 1.00 85.56 N
ANISOU 9 N GLY A -1 12521 9343 10644 173 -121 -1428 N
ATOM 10 CA GLY A -1 21.619 156.793 2.388 1.00 83.58 C
ANISOU 10 CA GLY A -1 12187 9234 10336 169 -130 -1351 C
ATOM 11 C GLY A -1 22.842 157.500 1.835 1.00 85.25 C
ANISOU 11 C GLY A -1 12409 9546 10435 264 -74 -1334 C
ATOM 12 O GLY A -1 23.957 156.974 1.916 1.00 85.42 O
ANISOU 12 O GLY A -1 12464 9537 10455 346 0 -1328 O
ATOM 13 N ALA A 0 22.633 158.711 1.269 1.00 79.02 N
ANISOU 13 N ALA A 0 11591 8877 9557 253 -108 -1323 N
ATOM 14 CA ALA A 0 23.663 159.559 0.650 1.00 77.39 C
ANISOU 14 CA ALA A 0 11391 8777 9238 328 -58 -1302 C
ATOM 15 C ALA A 0 24.869 159.814 1.580 1.00 77.74 C
ANISOU 15 C ALA A 0 11379 8849 9309 392 32 -1206 C
ATOM 16 O ALA A 0 24.662 159.925 2.792 1.00 76.92 O
ANISOU 16 O ALA A 0 11207 8730 9290 361 35 -1128 O
ATOM 17 CB ALA A 0 23.054 160.885 0.234 1.00 77.55 C
ANISOU 17 CB ALA A 0 11371 8906 9187 290 -114 -1278 C
ATOM 18 N PRO A 1 26.125 159.905 1.050 1.00 72.01 N
ANISOU 18 N PRO A 1 10678 8167 8514 481 105 -1210 N
ATOM 19 CA PRO A 1 27.282 160.146 1.938 1.00 70.03 C
ANISOU 19 CA PRO A 1 10363 7949 8297 540 183 -1121 C
ATOM 20 C PRO A 1 27.133 161.433 2.759 1.00 69.43 C
ANISOU 20 C PRO A 1 10190 7961 8230 499 170 -1020 C
ATOM 21 O PRO A 1 26.656 162.441 2.227 1.00 68.60 O
ANISOU 21 O PRO A 1 10074 7931 8059 463 133 -1017 O
ATOM 22 CB PRO A 1 28.471 160.231 0.973 1.00 72.41 C
ANISOU 22 CB PRO A 1 10702 8304 8508 628 255 -1153 C
ATOM 23 CG PRO A 1 28.029 159.527 -0.251 1.00 78.41 C
ANISOU 23 CG PRO A 1 11568 9015 9208 630 228 -1271 C
ATOM 24 CD PRO A 1 26.556 159.788 -0.359 1.00 74.15 C
ANISOU 24 CD PRO A 1 11034 8465 8674 531 124 -1296 C
ATOM 25 N PRO A 2 27.493 161.410 4.064 1.00 62.85 N
ANISOU 25 N PRO A 2 9290 7114 7475 505 195 -938 N
ATOM 26 CA PRO A 2 27.313 162.611 4.903 1.00 60.26 C
ANISOU 26 CA PRO A 2 8877 6864 7157 465 181 -850 C
ATOM 27 C PRO A 2 28.197 163.800 4.510 1.00 60.21 C
ANISOU 27 C PRO A 2 8832 6972 7074 498 219 -812 C
ATOM 28 O PRO A 2 27.795 164.928 4.778 1.00 59.40 O
ANISOU 28 O PRO A 2 8680 6933 6957 453 192 -765 O
ATOM 29 CB PRO A 2 27.660 162.118 6.315 1.00 61.73 C
ANISOU 29 CB PRO A 2 9019 7004 7433 479 205 -781 C
ATOM 30 CG PRO A 2 27.588 160.631 6.246 1.00 67.50 C
ANISOU 30 CG PRO A 2 9816 7615 8216 502 213 -834 C
ATOM 31 CD PRO A 2 28.028 160.287 4.859 1.00 64.35 C
ANISOU 31 CD PRO A 2 9487 7215 7746 550 233 -922 C
ATOM 32 N ILE A 3 29.359 163.566 3.852 1.00 54.14 N
ANISOU 32 N ILE A 3 8086 6226 6261 574 285 -835 N
ATOM 33 CA ILE A 3 30.291 164.620 3.430 1.00 52.61 C
ANISOU 33 CA ILE A 3 7853 6135 6000 604 334 -799 C
ATOM 34 C ILE A 3 29.700 165.521 2.303 1.00 54.52 C
ANISOU 34 C ILE A 3 8133 6436 6144 568 304 -827 C
ATOM 35 O ILE A 3 30.165 166.652 2.142 1.00 53.64 O
ANISOU 35 O ILE A 3 7983 6409 5988 566 330 -778 O
ATOM 36 CB ILE A 3 31.667 164.023 3.017 1.00 56.48 C
ANISOU 36 CB ILE A 3 8353 6630 6476 698 420 -819 C
ATOM 37 CG1 ILE A 3 32.821 165.000 3.315 1.00 56.44 C
ANISOU 37 CG1 ILE A 3 8263 6722 6462 724 478 -747 C
ATOM 38 CG2 ILE A 3 31.680 163.550 1.554 1.00 58.82 C
ANISOU 38 CG2 ILE A 3 8746 6917 6688 732 441 -912 C
ATOM 39 CD1 ILE A 3 34.205 164.374 3.378 1.00 66.74 C
ANISOU 39 CD1 ILE A 3 9538 8029 7792 817 558 -744 C
ATOM 40 N MET A 4 28.711 165.026 1.528 1.00 49.79 N
ANISOU 40 N MET A 4 7611 5793 5514 540 248 -903 N
ATOM 41 CA MET A 4 28.106 165.787 0.428 1.00 49.22 C
ANISOU 41 CA MET A 4 7583 5774 5344 513 208 -931 C
ATOM 42 C MET A 4 27.275 166.969 0.958 1.00 52.16 C
ANISOU 42 C MET A 4 7897 6191 5731 446 150 -868 C
ATOM 43 O MET A 4 27.511 168.107 0.548 1.00 51.76 O
ANISOU 43 O MET A 4 7833 6218 5616 445 162 -828 O
ATOM 44 CB MET A 4 27.257 164.878 -0.468 1.00 52.23 C
ANISOU 44 CB MET A 4 8057 6094 5693 501 152 -1035 C
ATOM 45 CG MET A 4 28.091 163.939 -1.312 1.00 56.60 C
ANISOU 45 CG MET A 4 8688 6620 6198 574 213 -1108 C
ATOM 46 SD MET A 4 27.117 163.039 -2.529 1.00 61.71 S
ANISOU 46 SD MET A 4 9456 7207 6784 557 140 -1241 S
ATOM 47 CE MET A 4 26.908 164.304 -3.793 1.00 58.18 C
ANISOU 47 CE MET A 4 9049 6874 6182 552 116 -1239 C
ATOM 48 N GLY A 5 26.355 166.688 1.883 1.00 47.45 N
ANISOU 48 N GLY A 5 7265 5542 5222 394 94 -856 N
ATOM 49 CA GLY A 5 25.515 167.692 2.526 1.00 45.80 C
ANISOU 49 CA GLY A 5 6995 5364 5042 335 44 -800 C
ATOM 50 C GLY A 5 26.313 168.546 3.490 1.00 47.85 C
ANISOU 50 C GLY A 5 7178 5673 5330 344 93 -711 C
ATOM 51 O GLY A 5 26.015 169.732 3.667 1.00 46.46 O
ANISOU 51 O GLY A 5 6964 5550 5140 315 73 -663 O
ATOM 52 N SER A 6 27.355 167.940 4.105 1.00 43.49 N
ANISOU 52 N SER A 6 6605 5101 4819 389 154 -692 N
ATOM 53 CA SER A 6 28.275 168.595 5.034 1.00 41.89 C
ANISOU 53 CA SER A 6 6329 4944 4646 403 199 -616 C
ATOM 54 C SER A 6 29.057 169.705 4.317 1.00 43.74 C
ANISOU 54 C SER A 6 6552 5262 4805 420 240 -590 C
ATOM 55 O SER A 6 29.121 170.821 4.835 1.00 42.72 O
ANISOU 55 O SER A 6 6369 5180 4682 392 237 -531 O
ATOM 56 CB SER A 6 29.230 167.574 5.648 1.00 45.90 C
ANISOU 56 CB SER A 6 6822 5411 5206 458 249 -611 C
ATOM 57 OG SER A 6 30.040 168.148 6.659 1.00 57.63 O
ANISOU 57 OG SER A 6 8231 6939 6725 468 278 -539 O
ATOM 58 N SER A 7 29.602 169.410 3.109 1.00 39.56 N
ANISOU 58 N SER A 7 6080 4748 4204 464 280 -636 N
ATOM 59 CA SER A 7 30.361 170.350 2.271 1.00 39.32 C
ANISOU 59 CA SER A 7 6052 4794 4094 482 331 -614 C
ATOM 60 C SER A 7 29.533 171.568 1.879 1.00 42.44 C
ANISOU 60 C SER A 7 6458 5228 4439 432 282 -589 C
ATOM 61 O SER A 7 30.083 172.665 1.810 1.00 41.25 O
ANISOU 61 O SER A 7 6276 5135 4263 424 317 -535 O
ATOM 62 CB SER A 7 30.869 169.661 1.012 1.00 43.43 C
ANISOU 62 CB SER A 7 6648 5315 4540 537 379 -679 C
ATOM 63 OG SER A 7 31.806 168.661 1.369 1.00 53.92 O
ANISOU 63 OG SER A 7 7958 6614 5916 595 437 -694 O
ATOM 64 N VAL A 8 28.218 171.379 1.642 1.00 39.59 N
ANISOU 64 N VAL A 8 6137 4833 4072 397 201 -627 N
ATOM 65 CA VAL A 8 27.281 172.459 1.294 1.00 39.41 C
ANISOU 65 CA VAL A 8 6124 4841 4010 355 142 -605 C
ATOM 66 C VAL A 8 27.152 173.407 2.497 1.00 42.82 C
ANISOU 66 C VAL A 8 6473 5285 4510 317 131 -532 C
ATOM 67 O VAL A 8 27.304 174.614 2.336 1.00 42.34 O
ANISOU 67 O VAL A 8 6399 5271 4417 304 140 -483 O
ATOM 68 CB VAL A 8 25.895 171.912 0.837 1.00 43.08 C
ANISOU 68 CB VAL A 8 6637 5265 4467 328 50 -668 C
ATOM 69 CG1 VAL A 8 24.887 173.040 0.618 1.00 42.28 C
ANISOU 69 CG1 VAL A 8 6531 5195 4339 291 -18 -640 C
ATOM 70 CG2 VAL A 8 26.024 171.056 -0.416 1.00 43.73 C
ANISOU 70 CG2 VAL A 8 6811 5336 4469 365 55 -748 C
ATOM 71 N TYR A 9 26.909 172.841 3.692 1.00 39.44 N
ANISOU 71 N TYR A 9 5998 4814 4174 301 117 -526 N
ATOM 72 CA TYR A 9 26.733 173.563 4.947 1.00 39.22 C
ANISOU 72 CA TYR A 9 5898 4792 4210 267 106 -467 C
ATOM 73 C TYR A 9 27.980 174.372 5.317 1.00 43.66 C
ANISOU 73 C TYR A 9 6415 5404 4771 281 168 -411 C
ATOM 74 O TYR A 9 27.847 175.545 5.654 1.00 42.96 O
ANISOU 74 O TYR A 9 6295 5343 4685 252 158 -366 O
ATOM 75 CB TYR A 9 26.357 172.583 6.084 1.00 40.70 C
ANISOU 75 CB TYR A 9 6057 4922 4485 257 90 -475 C
ATOM 76 CG TYR A 9 26.372 173.191 7.471 1.00 42.35 C
ANISOU 76 CG TYR A 9 6198 5140 4753 232 91 -416 C
ATOM 77 CD1 TYR A 9 25.404 174.115 7.862 1.00 44.04 C
ANISOU 77 CD1 TYR A 9 6389 5364 4981 190 48 -393 C
ATOM 78 CD2 TYR A 9 27.358 172.848 8.393 1.00 43.00 C
ANISOU 78 CD2 TYR A 9 6243 5222 4874 256 133 -386 C
ATOM 79 CE1 TYR A 9 25.423 174.687 9.132 1.00 44.80 C
ANISOU 79 CE1 TYR A 9 6430 5469 5124 171 52 -346 C
ATOM 80 CE2 TYR A 9 27.386 173.415 9.667 1.00 43.37 C
ANISOU 80 CE2 TYR A 9 6235 5281 4964 235 130 -337 C
ATOM 81 CZ TYR A 9 26.413 174.329 10.033 1.00 52.21 C
ANISOU 81 CZ TYR A 9 7338 6409 6092 191 91 -319 C
ATOM 82 OH TYR A 9 26.438 174.882 11.289 1.00 56.19 O
ANISOU 82 OH TYR A 9 7795 6924 6631 173 91 -277 O
ATOM 83 N ILE A 10 29.177 173.762 5.230 1.00 41.07 N
ANISOU 83 N ILE A 10 6079 5083 4442 324 230 -417 N
ATOM 84 CA ILE A 10 30.443 174.408 5.581 1.00 40.77 C
ANISOU 84 CA ILE A 10 5985 5093 4413 336 290 -368 C
ATOM 85 C ILE A 10 30.735 175.579 4.601 1.00 46.08 C
ANISOU 85 C ILE A 10 6676 5818 5015 326 317 -344 C
ATOM 86 O ILE A 10 31.052 176.670 5.073 1.00 46.29 O
ANISOU 86 O ILE A 10 6656 5874 5057 296 326 -293 O
ATOM 87 CB ILE A 10 31.605 173.371 5.690 1.00 43.85 C
ANISOU 87 CB ILE A 10 6356 5478 4825 393 348 -383 C
ATOM 88 CG1 ILE A 10 31.290 172.342 6.817 1.00 44.11 C
ANISOU 88 CG1 ILE A 10 6372 5454 4933 400 317 -390 C
ATOM 89 CG2 ILE A 10 32.953 174.057 5.954 1.00 43.78 C
ANISOU 89 CG2 ILE A 10 6278 5528 4829 404 408 -336 C
ATOM 90 CD1 ILE A 10 32.153 171.026 6.864 1.00 49.30 C
ANISOU 90 CD1 ILE A 10 7031 6081 5617 466 360 -416 C
ATOM 91 N THR A 11 30.560 175.383 3.276 1.00 42.83 N
ANISOU 91 N THR A 11 6337 5414 4522 346 327 -380 N
ATOM 92 CA THR A 11 30.793 176.440 2.274 1.00 43.00 C
ANISOU 92 CA THR A 11 6391 5482 4465 340 356 -352 C
ATOM 93 C THR A 11 29.859 177.654 2.502 1.00 47.48 C
ANISOU 93 C THR A 11 6956 6050 5034 290 297 -313 C
ATOM 94 O THR A 11 30.326 178.794 2.443 1.00 47.16 O
ANISOU 94 O THR A 11 6896 6040 4981 270 329 -259 O
ATOM 95 CB THR A 11 30.644 175.889 0.848 1.00 48.77 C
ANISOU 95 CB THR A 11 7213 6218 5099 375 367 -404 C
ATOM 96 OG1 THR A 11 31.433 174.707 0.717 1.00 48.32 O
ANISOU 96 OG1 THR A 11 7160 6150 5050 425 421 -448 O
ATOM 97 CG2 THR A 11 31.094 176.883 -0.205 1.00 48.28 C
ANISOU 97 CG2 THR A 11 7189 6208 4947 377 417 -368 C
ATOM 98 N VAL A 12 28.561 177.402 2.780 1.00 44.10 N
ANISOU 98 N VAL A 12 6543 5585 4627 272 216 -338 N
ATOM 99 CA VAL A 12 27.549 178.431 3.030 1.00 43.40 C
ANISOU 99 CA VAL A 12 6449 5492 4549 235 155 -308 C
ATOM 100 C VAL A 12 27.888 179.191 4.333 1.00 47.06 C
ANISOU 100 C VAL A 12 6837 5957 5088 205 167 -258 C
ATOM 101 O VAL A 12 27.830 180.424 4.335 1.00 46.36 O
ANISOU 101 O VAL A 12 6742 5882 4991 182 165 -213 O
ATOM 102 CB VAL A 12 26.115 177.827 3.043 1.00 46.88 C
ANISOU 102 CB VAL A 12 6911 5895 5006 224 69 -354 C
ATOM 103 CG1 VAL A 12 25.078 178.807 3.603 1.00 46.00 C
ANISOU 103 CG1 VAL A 12 6770 5777 4930 190 11 -323 C
ATOM 104 CG2 VAL A 12 25.710 177.364 1.646 1.00 47.30 C
ANISOU 104 CG2 VAL A 12 7046 5954 4971 247 43 -403 C
ATOM 105 N GLU A 13 28.264 178.468 5.416 1.00 43.42 N
ANISOU 105 N GLU A 13 6323 5478 4695 207 179 -265 N
ATOM 106 CA GLU A 13 28.622 179.073 6.707 1.00 42.46 C
ANISOU 106 CA GLU A 13 6135 5361 4638 182 185 -225 C
ATOM 107 C GLU A 13 29.854 179.964 6.569 1.00 45.89 C
ANISOU 107 C GLU A 13 6541 5836 5060 176 245 -184 C
ATOM 108 O GLU A 13 29.884 181.051 7.153 1.00 45.37 O
ANISOU 108 O GLU A 13 6445 5775 5020 142 239 -147 O
ATOM 109 CB GLU A 13 28.865 178.003 7.776 1.00 43.83 C
ANISOU 109 CB GLU A 13 6269 5512 4872 194 187 -240 C
ATOM 110 CG GLU A 13 27.599 177.351 8.301 1.00 55.92 C
ANISOU 110 CG GLU A 13 7810 6998 6439 182 131 -266 C
ATOM 111 CD GLU A 13 26.912 178.060 9.449 1.00 78.00 C
ANISOU 111 CD GLU A 13 10568 9786 9281 147 99 -239 C
ATOM 112 OE1 GLU A 13 26.981 177.546 10.590 1.00 69.29 O
ANISOU 112 OE1 GLU A 13 9434 8668 8227 146 99 -232 O
ATOM 113 OE2 GLU A 13 26.268 179.105 9.203 1.00 73.55 O
ANISOU 113 OE2 GLU A 13 10013 9230 8703 126 73 -225 O
ATOM 114 N LEU A 14 30.847 179.526 5.764 1.00 42.55 N
ANISOU 114 N LEU A 14 6129 5439 4600 207 305 -192 N
ATOM 115 CA LEU A 14 32.062 180.296 5.512 1.00 42.87 C
ANISOU 115 CA LEU A 14 6137 5520 4632 199 372 -153 C
ATOM 116 C LEU A 14 31.734 181.564 4.726 1.00 45.80 C
ANISOU 116 C LEU A 14 6550 5901 4952 171 374 -118 C
ATOM 117 O LEU A 14 32.282 182.622 5.039 1.00 45.49 O
ANISOU 117 O LEU A 14 6474 5874 4935 136 398 -74 O
ATOM 118 CB LEU A 14 33.140 179.466 4.792 1.00 43.94 C
ANISOU 118 CB LEU A 14 6272 5684 4740 245 444 -172 C
ATOM 119 CG LEU A 14 33.877 178.425 5.659 1.00 49.57 C
ANISOU 119 CG LEU A 14 6925 6394 5516 277 458 -190 C
ATOM 120 CD1 LEU A 14 34.722 177.502 4.804 1.00 50.57 C
ANISOU 120 CD1 LEU A 14 7064 6538 5610 334 525 -219 C
ATOM 121 CD2 LEU A 14 34.733 179.085 6.764 1.00 52.34 C
ANISOU 121 CD2 LEU A 14 7184 6771 5934 249 468 -149 C
ATOM 122 N ALA A 15 30.795 181.471 3.761 1.00 41.53 N
ANISOU 122 N ALA A 15 6086 5347 4344 185 341 -137 N
ATOM 123 CA ALA A 15 30.329 182.610 2.967 1.00 41.31 C
ANISOU 123 CA ALA A 15 6111 5323 4261 167 331 -100 C
ATOM 124 C ALA A 15 29.671 183.678 3.871 1.00 44.07 C
ANISOU 124 C ALA A 15 6433 5647 4666 127 281 -68 C
ATOM 125 O ALA A 15 29.898 184.870 3.659 1.00 44.05 O
ANISOU 125 O ALA A 15 6438 5646 4653 102 302 -19 O
ATOM 126 CB ALA A 15 29.355 182.141 1.894 1.00 42.43 C
ANISOU 126 CB ALA A 15 6336 5459 4325 196 285 -136 C
ATOM 127 N ILE A 16 28.905 183.239 4.901 1.00 39.46 N
ANISOU 127 N ILE A 16 5816 5036 4142 122 224 -95 N
ATOM 128 CA ILE A 16 28.233 184.096 5.890 1.00 38.73 C
ANISOU 128 CA ILE A 16 5694 4917 4105 91 181 -75 C
ATOM 129 C ILE A 16 29.290 184.748 6.815 1.00 41.63 C
ANISOU 129 C ILE A 16 6000 5294 4525 60 222 -45 C
ATOM 130 O ILE A 16 29.165 185.932 7.125 1.00 39.78 O
ANISOU 130 O ILE A 16 5761 5044 4310 29 214 -13 O
ATOM 131 CB ILE A 16 27.151 183.299 6.700 1.00 41.48 C
ANISOU 131 CB ILE A 16 6024 5239 4498 96 120 -114 C
ATOM 132 CG1 ILE A 16 25.965 182.885 5.798 1.00 42.13 C
ANISOU 132 CG1 ILE A 16 6160 5311 4538 115 65 -144 C
ATOM 133 CG2 ILE A 16 26.640 184.086 7.935 1.00 41.74 C
ANISOU 133 CG2 ILE A 16 6017 5250 4593 68 91 -98 C
ATOM 134 CD1 ILE A 16 25.211 181.645 6.281 1.00 50.36 C
ANISOU 134 CD1 ILE A 16 7187 6330 5618 121 27 -193 C
ATOM 135 N ALA A 17 30.312 183.975 7.254 1.00 38.59 N
ANISOU 135 N ALA A 17 5568 4931 4166 68 260 -57 N
ATOM 136 CA ALA A 17 31.381 184.466 8.135 1.00 38.11 C
ANISOU 136 CA ALA A 17 5439 4886 4156 40 290 -35 C
ATOM 137 C ALA A 17 32.148 185.638 7.499 1.00 43.56 C
ANISOU 137 C ALA A 17 6132 5590 4829 9 340 8 C
ATOM 138 O ALA A 17 32.356 186.647 8.168 1.00 43.51 O
ANISOU 138 O ALA A 17 6097 5572 4864 -33 335 31 O
ATOM 139 CB ALA A 17 32.338 183.339 8.487 1.00 38.57 C
ANISOU 139 CB ALA A 17 5449 4970 4236 67 320 -55 C
ATOM 140 N VAL A 18 32.499 185.535 6.196 1.00 40.71 N
ANISOU 140 N VAL A 18 5812 5249 4407 27 389 19 N
ATOM 141 CA VAL A 18 33.225 186.581 5.457 1.00 40.88 C
ANISOU 141 CA VAL A 18 5844 5283 4405 -2 450 68 C
ATOM 142 C VAL A 18 32.368 187.876 5.367 1.00 43.53 C
ANISOU 142 C VAL A 18 6228 5577 4733 -32 413 102 C
ATOM 143 O VAL A 18 32.898 188.969 5.589 1.00 42.62 O
ANISOU 143 O VAL A 18 6093 5450 4651 -78 440 140 O
ATOM 144 CB VAL A 18 33.695 186.086 4.056 1.00 44.97 C
ANISOU 144 CB VAL A 18 6407 5834 4844 33 514 71 C
ATOM 145 CG1 VAL A 18 34.316 187.218 3.234 1.00 45.44 C
ANISOU 145 CG1 VAL A 18 6489 5902 4872 0 581 130 C
ATOM 146 CG2 VAL A 18 34.687 184.937 4.193 1.00 44.75 C
ANISOU 146 CG2 VAL A 18 6324 5844 4836 64 560 40 C
ATOM 147 N LEU A 19 31.058 187.740 5.083 1.00 39.50 N
ANISOU 147 N LEU A 19 5776 5042 4189 -5 351 87 N
ATOM 148 CA LEU A 19 30.154 188.884 4.948 1.00 39.69 C
ANISOU 148 CA LEU A 19 5848 5027 4207 -19 311 118 C
ATOM 149 C LEU A 19 29.799 189.521 6.302 1.00 44.12 C
ANISOU 149 C LEU A 19 6364 5552 4846 -50 271 113 C
ATOM 150 O LEU A 19 29.534 190.721 6.341 1.00 44.21 O
ANISOU 150 O LEU A 19 6399 5528 4872 -73 263 147 O
ATOM 151 CB LEU A 19 28.881 188.498 4.177 1.00 39.78 C
ANISOU 151 CB LEU A 19 5925 5030 4158 23 253 100 C
ATOM 152 CG LEU A 19 29.108 188.034 2.719 1.00 44.71 C
ANISOU 152 CG LEU A 19 6615 5688 4686 56 285 104 C
ATOM 153 CD1 LEU A 19 27.908 187.265 2.185 1.00 44.40 C
ANISOU 153 CD1 LEU A 19 6623 5648 4600 97 214 63 C
ATOM 154 CD2 LEU A 19 29.514 189.196 1.806 1.00 46.08 C
ANISOU 154 CD2 LEU A 19 6843 5857 4808 41 333 172 C
ATOM 155 N ALA A 20 29.824 188.739 7.398 1.00 40.55 N
ANISOU 155 N ALA A 20 5856 5109 4443 -48 249 72 N
ATOM 156 CA ALA A 20 29.542 189.229 8.745 1.00 40.30 C
ANISOU 156 CA ALA A 20 5785 5052 4476 -73 215 62 C
ATOM 157 C ALA A 20 30.727 190.024 9.285 1.00 45.65 C
ANISOU 157 C ALA A 20 6417 5731 5196 -122 254 82 C
ATOM 158 O ALA A 20 30.523 190.978 10.041 1.00 45.30 O
ANISOU 158 O ALA A 20 6367 5652 5191 -153 233 87 O
ATOM 159 CB ALA A 20 29.218 188.072 9.682 1.00 40.37 C
ANISOU 159 CB ALA A 20 5756 5072 4512 -52 184 17 C
ATOM 160 N ILE A 21 31.959 189.637 8.893 1.00 42.78 N
ANISOU 160 N ILE A 21 6020 5408 4827 -130 310 92 N
ATOM 161 CA ILE A 21 33.182 190.311 9.330 1.00 43.40 C
ANISOU 161 CA ILE A 21 6043 5497 4952 -181 348 109 C
ATOM 162 C ILE A 21 33.333 191.655 8.572 1.00 48.87 C
ANISOU 162 C ILE A 21 6777 6156 5636 -221 383 160 C
ATOM 163 O ILE A 21 33.327 192.698 9.221 1.00 48.94 O
ANISOU 163 O ILE A 21 6779 6126 5690 -265 367 167 O
ATOM 164 CB ILE A 21 34.436 189.383 9.219 1.00 46.57 C
ANISOU 164 CB ILE A 21 6379 5955 5360 -170 396 101 C
ATOM 165 CG1 ILE A 21 34.377 188.278 10.311 1.00 46.57 C
ANISOU 165 CG1 ILE A 21 6333 5975 5387 -140 354 58 C
ATOM 166 CG2 ILE A 21 35.757 190.175 9.332 1.00 47.01 C
ANISOU 166 CG2 ILE A 21 6373 6028 5462 -228 446 128 C
ATOM 167 CD1 ILE A 21 35.089 186.944 9.962 1.00 55.15 C
ANISOU 167 CD1 ILE A 21 7386 7107 6461 -94 388 43 C
ATOM 168 N LEU A 22 33.422 191.629 7.225 1.00 46.60 N
ANISOU 168 N LEU A 22 6539 5880 5287 -203 430 193 N
ATOM 169 CA LEU A 22 33.614 192.805 6.362 1.00 47.41 C
ANISOU 169 CA LEU A 22 6692 5954 5370 -236 474 251 C
ATOM 170 C LEU A 22 32.600 193.945 6.608 1.00 50.25 C
ANISOU 170 C LEU A 22 7106 6242 5743 -248 424 269 C
ATOM 171 O LEU A 22 33.009 195.097 6.767 1.00 50.31 O
ANISOU 171 O LEU A 22 7116 6209 5791 -301 447 302 O
ATOM 172 CB LEU A 22 33.569 192.404 4.877 1.00 48.16 C
ANISOU 172 CB LEU A 22 6850 6075 5373 -196 517 278 C
ATOM 173 CG LEU A 22 34.815 191.728 4.298 1.00 53.72 C
ANISOU 173 CG LEU A 22 7513 6839 6059 -194 601 282 C
ATOM 174 CD1 LEU A 22 34.506 191.117 2.950 1.00 54.13 C
ANISOU 174 CD1 LEU A 22 7641 6918 6008 -140 627 288 C
ATOM 175 CD2 LEU A 22 35.973 192.714 4.145 1.00 57.18 C
ANISOU 175 CD2 LEU A 22 7916 7274 6536 -261 679 333 C
ATOM 176 N GLY A 23 31.311 193.610 6.632 1.00 45.01 N
ANISOU 176 N GLY A 23 6484 5564 5052 -199 359 246 N
ATOM 177 CA GLY A 23 30.232 194.570 6.830 1.00 44.23 C
ANISOU 177 CA GLY A 23 6434 5403 4966 -194 310 259 C
ATOM 178 C GLY A 23 30.231 195.242 8.189 1.00 46.64 C
ANISOU 178 C GLY A 23 6700 5669 5351 -231 283 235 C
ATOM 179 O GLY A 23 30.038 196.459 8.269 1.00 47.12 O
ANISOU 179 O GLY A 23 6795 5670 5440 -257 281 263 O
ATOM 180 N ASN A 24 30.431 194.460 9.268 1.00 40.24 N
ANISOU 180 N ASN A 24 5823 4890 4575 -233 262 184 N
ATOM 181 CA ASN A 24 30.437 195.018 10.616 1.00 39.07 C
ANISOU 181 CA ASN A 24 5641 4712 4490 -265 234 154 C
ATOM 182 C ASN A 24 31.782 195.705 10.946 1.00 43.33 C
ANISOU 182 C ASN A 24 6139 5248 5077 -336 275 165 C
ATOM 183 O ASN A 24 31.785 196.622 11.771 1.00 42.88 O
ANISOU 183 O ASN A 24 6079 5145 5067 -374 256 152 O
ATOM 184 CB ASN A 24 30.047 193.982 11.650 1.00 36.84 C
ANISOU 184 CB ASN A 24 5317 4463 4219 -238 194 100 C
ATOM 185 CG ASN A 24 28.568 193.675 11.609 1.00 52.75 C
ANISOU 185 CG ASN A 24 7367 6461 6213 -185 148 85 C
ATOM 186 OD1 ASN A 24 27.746 194.373 12.210 1.00 50.19 O
ANISOU 186 OD1 ASN A 24 7061 6093 5914 -181 118 74 O
ATOM 187 ND2 ASN A 24 28.187 192.647 10.869 1.00 39.54 N
ANISOU 187 ND2 ASN A 24 5705 4821 4497 -144 143 82 N
ATOM 188 N VAL A 25 32.898 195.334 10.259 1.00 39.90 N
ANISOU 188 N VAL A 25 5671 4858 4629 -355 332 189 N
ATOM 189 CA VAL A 25 34.192 196.015 10.425 1.00 40.25 C
ANISOU 189 CA VAL A 25 5667 4902 4725 -427 376 206 C
ATOM 190 C VAL A 25 34.022 197.462 9.898 1.00 45.55 C
ANISOU 190 C VAL A 25 6403 5497 5409 -467 398 254 C
ATOM 191 O VAL A 25 34.472 198.415 10.535 1.00 45.29 O
ANISOU 191 O VAL A 25 6352 5419 5437 -530 397 250 O
ATOM 192 CB VAL A 25 35.355 195.240 9.735 1.00 44.31 C
ANISOU 192 CB VAL A 25 6126 5485 5224 -430 440 223 C
ATOM 193 CG1 VAL A 25 36.479 196.164 9.263 1.00 44.83 C
ANISOU 193 CG1 VAL A 25 6168 5539 5326 -502 509 267 C
ATOM 194 CG2 VAL A 25 35.908 194.154 10.655 1.00 43.80 C
ANISOU 194 CG2 VAL A 25 5976 5481 5183 -414 416 174 C
ATOM 195 N LEU A 26 33.299 197.601 8.768 1.00 42.94 N
ANISOU 195 N LEU A 26 6152 5146 5019 -427 411 298 N
ATOM 196 CA LEU A 26 32.974 198.857 8.095 1.00 43.35 C
ANISOU 196 CA LEU A 26 6281 5122 5066 -445 430 355 C
ATOM 197 C LEU A 26 32.136 199.773 9.006 1.00 45.57 C
ANISOU 197 C LEU A 26 6593 5326 5396 -450 372 331 C
ATOM 198 O LEU A 26 32.393 200.975 9.047 1.00 44.92 O
ANISOU 198 O LEU A 26 6540 5173 5357 -501 391 359 O
ATOM 199 CB LEU A 26 32.228 198.542 6.782 1.00 43.68 C
ANISOU 199 CB LEU A 26 6402 5176 5020 -381 436 396 C
ATOM 200 CG LEU A 26 31.961 199.683 5.800 1.00 49.68 C
ANISOU 200 CG LEU A 26 7253 5870 5752 -387 463 472 C
ATOM 201 CD1 LEU A 26 33.251 200.182 5.154 1.00 51.16 C
ANISOU 201 CD1 LEU A 26 7433 6059 5947 -453 557 529 C
ATOM 202 CD2 LEU A 26 30.989 199.235 4.721 1.00 51.96 C
ANISOU 202 CD2 LEU A 26 7617 6178 5947 -309 438 496 C
ATOM 203 N VAL A 27 31.173 199.203 9.758 1.00 41.50 N
ANISOU 203 N VAL A 27 6070 4823 4877 -399 308 278 N
ATOM 204 CA VAL A 27 30.326 199.959 10.693 1.00 41.53 C
ANISOU 204 CA VAL A 27 6096 4761 4922 -393 259 247 C
ATOM 205 C VAL A 27 31.210 200.578 11.807 1.00 46.70 C
ANISOU 205 C VAL A 27 6705 5391 5648 -467 262 212 C
ATOM 206 O VAL A 27 31.144 201.792 12.026 1.00 45.45 O
ANISOU 206 O VAL A 27 6586 5151 5532 -502 262 221 O
ATOM 207 CB VAL A 27 29.180 199.079 11.269 1.00 44.25 C
ANISOU 207 CB VAL A 27 6430 5137 5247 -325 201 198 C
ATOM 208 CG1 VAL A 27 28.514 199.733 12.482 1.00 43.61 C
ANISOU 208 CG1 VAL A 27 6355 5003 5214 -324 161 154 C
ATOM 209 CG2 VAL A 27 28.149 198.754 10.193 1.00 44.12 C
ANISOU 209 CG2 VAL A 27 6466 5125 5172 -258 184 229 C
ATOM 210 N CYS A 28 32.045 199.738 12.473 1.00 44.60 N
ANISOU 210 N CYS A 28 6358 5194 5393 -490 261 173 N
ATOM 211 CA CYS A 28 32.972 200.115 13.541 1.00 45.85 C
ANISOU 211 CA CYS A 28 6460 5350 5611 -558 253 134 C
ATOM 212 C CYS A 28 33.932 201.196 13.070 1.00 53.01 C
ANISOU 212 C CYS A 28 7369 6208 6563 -639 301 173 C
ATOM 213 O CYS A 28 34.195 202.143 13.814 1.00 53.64 O
ANISOU 213 O CYS A 28 7450 6230 6699 -696 285 147 O
ATOM 214 CB CYS A 28 33.736 198.897 14.044 1.00 46.33 C
ANISOU 214 CB CYS A 28 6435 5505 5666 -555 246 101 C
ATOM 215 SG CYS A 28 32.705 197.665 14.875 1.00 49.70 S
ANISOU 215 SG CYS A 28 6854 5977 6052 -475 190 51 S
ATOM 216 N TRP A 29 34.444 201.057 11.833 1.00 51.00 N
ANISOU 216 N TRP A 29 7120 5976 6283 -646 363 236 N
ATOM 217 CA TRP A 29 35.385 201.990 11.222 1.00 52.37 C
ANISOU 217 CA TRP A 29 7293 6108 6495 -724 426 287 C
ATOM 218 C TRP A 29 34.716 203.353 10.918 1.00 54.21 C
ANISOU 218 C TRP A 29 7625 6226 6746 -737 428 324 C
ATOM 219 O TRP A 29 35.348 204.388 11.120 1.00 53.52 O
ANISOU 219 O TRP A 29 7538 6074 6725 -818 450 334 O
ATOM 220 CB TRP A 29 35.999 201.363 9.959 1.00 52.47 C
ANISOU 220 CB TRP A 29 7292 6183 6462 -714 498 344 C
ATOM 221 CG TRP A 29 37.199 202.087 9.426 1.00 55.78 C
ANISOU 221 CG TRP A 29 7684 6585 6927 -801 576 393 C
ATOM 222 CD1 TRP A 29 37.341 202.618 8.179 1.00 59.75 C
ANISOU 222 CD1 TRP A 29 8245 7057 7400 -814 649 474 C
ATOM 223 CD2 TRP A 29 38.417 202.384 10.133 1.00 56.75 C
ANISOU 223 CD2 TRP A 29 7710 6719 7134 -891 588 367 C
ATOM 224 NE1 TRP A 29 38.572 203.222 8.058 1.00 60.72 N
ANISOU 224 NE1 TRP A 29 8314 7170 7589 -910 716 503 N
ATOM 225 CE2 TRP A 29 39.250 203.102 9.247 1.00 62.28 C
ANISOU 225 CE2 TRP A 29 8411 7393 7861 -961 676 436 C
ATOM 226 CE3 TRP A 29 38.882 202.124 11.437 1.00 57.98 C
ANISOU 226 CE3 TRP A 29 7780 6908 7343 -921 530 293 C
ATOM 227 CZ2 TRP A 29 40.522 203.564 9.620 1.00 62.75 C
ANISOU 227 CZ2 TRP A 29 8378 7456 8010 -1064 708 429 C
ATOM 228 CZ3 TRP A 29 40.140 202.583 11.806 1.00 60.48 C
ANISOU 228 CZ3 TRP A 29 8009 7231 7742 -1018 552 284 C
ATOM 229 CH2 TRP A 29 40.944 203.294 10.905 1.00 62.31 C
ANISOU 229 CH2 TRP A 29 8232 7434 8010 -1091 640 350 C
ATOM 230 N ALA A 30 33.433 203.345 10.485 1.00 49.59 N
ANISOU 230 N ALA A 30 7119 5613 6109 -657 401 342 N
ATOM 231 CA ALA A 30 32.651 204.548 10.170 1.00 49.56 C
ANISOU 231 CA ALA A 30 7213 5501 6117 -648 395 380 C
ATOM 232 C ALA A 30 32.372 205.376 11.418 1.00 54.05 C
ANISOU 232 C ALA A 30 7788 5994 6755 -675 349 320 C
ATOM 233 O ALA A 30 32.448 206.603 11.363 1.00 55.67 O
ANISOU 233 O ALA A 30 8047 6097 7008 -719 365 345 O
ATOM 234 CB ALA A 30 31.341 204.169 9.495 1.00 49.71 C
ANISOU 234 CB ALA A 30 7296 5527 6065 -547 364 403 C
ATOM 235 N VAL A 31 32.060 204.711 12.541 1.00 48.95 N
ANISOU 235 N VAL A 31 7094 5395 6111 -649 296 242 N
ATOM 236 CA VAL A 31 31.800 205.364 13.822 1.00 48.38 C
ANISOU 236 CA VAL A 31 7026 5265 6090 -669 252 173 C
ATOM 237 C VAL A 31 33.130 205.945 14.334 1.00 53.30 C
ANISOU 237 C VAL A 31 7603 5869 6781 -778 269 152 C
ATOM 238 O VAL A 31 33.145 207.071 14.832 1.00 53.13 O
ANISOU 238 O VAL A 31 7620 5751 6815 -824 260 130 O
ATOM 239 CB VAL A 31 31.123 204.392 14.835 1.00 50.61 C
ANISOU 239 CB VAL A 31 7272 5615 6344 -608 197 102 C
ATOM 240 CG1 VAL A 31 30.987 205.015 16.228 1.00 50.38 C
ANISOU 240 CG1 VAL A 31 7247 5538 6357 -632 157 26 C
ATOM 241 CG2 VAL A 31 29.758 203.941 14.324 1.00 49.61 C
ANISOU 241 CG2 VAL A 31 7188 5497 6166 -510 179 122 C
ATOM 242 N TRP A 32 34.240 205.204 14.137 1.00 51.02 N
ANISOU 242 N TRP A 32 7229 5666 6489 -819 296 160 N
ATOM 243 CA TRP A 32 35.590 205.591 14.546 1.00 52.69 C
ANISOU 243 CA TRP A 32 7372 5879 6767 -924 311 142 C
ATOM 244 C TRP A 32 36.068 206.901 13.888 1.00 57.52 C
ANISOU 244 C TRP A 32 8029 6388 7436 -1004 364 197 C
ATOM 245 O TRP A 32 36.638 207.735 14.588 1.00 57.89 O
ANISOU 245 O TRP A 32 8062 6376 7556 -1088 350 159 O
ATOM 246 CB TRP A 32 36.601 204.461 14.245 1.00 51.97 C
ANISOU 246 CB TRP A 32 7180 5907 6659 -934 339 153 C
ATOM 247 CG TRP A 32 38.035 204.836 14.504 1.00 54.50 C
ANISOU 247 CG TRP A 32 7415 6238 7053 -1042 360 144 C
ATOM 248 CD1 TRP A 32 38.923 205.355 13.608 1.00 58.43 C
ANISOU 248 CD1 TRP A 32 7894 6717 7591 -1113 435 206 C
ATOM 249 CD2 TRP A 32 38.726 204.765 15.758 1.00 54.93 C
ANISOU 249 CD2 TRP A 32 7391 6325 7154 -1092 304 67 C
ATOM 250 NE1 TRP A 32 40.118 205.630 14.228 1.00 58.79 N
ANISOU 250 NE1 TRP A 32 7845 6778 7714 -1210 429 172 N
ATOM 251 CE2 TRP A 32 40.030 205.268 15.547 1.00 59.92 C
ANISOU 251 CE2 TRP A 32 7950 6955 7861 -1197 343 85 C
ATOM 252 CE3 TRP A 32 38.369 204.322 17.045 1.00 56.00 C
ANISOU 252 CE3 TRP A 32 7510 6493 7272 -1058 224 -13 C
ATOM 253 CZ2 TRP A 32 40.980 205.338 16.572 1.00 60.05 C
ANISOU 253 CZ2 TRP A 32 7874 7004 7938 -1269 295 20 C
ATOM 254 CZ3 TRP A 32 39.309 204.400 18.062 1.00 58.31 C
ANISOU 254 CZ3 TRP A 32 7723 6818 7615 -1126 177 -74 C
ATOM 255 CH2 TRP A 32 40.600 204.893 17.820 1.00 60.06 C
ANISOU 255 CH2 TRP A 32 7868 7040 7913 -1229 207 -60 C
ATOM 256 N LEU A 33 35.883 207.070 12.567 1.00 54.71 N
ANISOU 256 N LEU A 33 7729 6011 7049 -983 425 286 N
ATOM 257 CA LEU A 33 36.410 208.254 11.887 1.00 56.28 C
ANISOU 257 CA LEU A 33 7971 6113 7298 -1062 486 351 C
ATOM 258 C LEU A 33 35.421 209.442 11.801 1.00 58.72 C
ANISOU 258 C LEU A 33 8402 6284 7624 -1039 472 373 C
ATOM 259 O LEU A 33 35.891 210.580 11.719 1.00 59.59 O
ANISOU 259 O LEU A 33 8546 6291 7803 -1121 504 398 O
ATOM 260 CB LEU A 33 36.965 207.919 10.489 1.00 57.40 C
ANISOU 260 CB LEU A 33 8108 6301 7400 -1067 572 444 C
ATOM 261 CG LEU A 33 36.040 207.314 9.437 1.00 62.97 C
ANISOU 261 CG LEU A 33 8882 7042 8004 -960 583 500 C
ATOM 262 CD1 LEU A 33 35.659 208.358 8.389 1.00 64.63 C
ANISOU 262 CD1 LEU A 33 9206 7150 8201 -959 630 594 C
ATOM 263 CD2 LEU A 33 36.745 206.182 8.719 1.00 66.99 C
ANISOU 263 CD2 LEU A 33 9324 7671 8460 -947 634 525 C
ATOM 264 N ASN A 34 34.093 209.202 11.837 1.00 52.58 N
ANISOU 264 N ASN A 34 7685 5500 6791 -932 426 362 N
ATOM 265 CA ASN A 34 33.108 210.286 11.753 1.00 51.99 C
ANISOU 265 CA ASN A 34 7721 5299 6733 -895 411 383 C
ATOM 266 C ASN A 34 32.625 210.717 13.149 1.00 54.59 C
ANISOU 266 C ASN A 34 8056 5576 7109 -892 347 284 C
ATOM 267 O ASN A 34 32.061 209.904 13.889 1.00 53.36 O
ANISOU 267 O ASN A 34 7863 5492 6918 -831 296 219 O
ATOM 268 CB ASN A 34 31.922 209.885 10.864 1.00 50.92 C
ANISOU 268 CB ASN A 34 7649 5183 6516 -778 400 436 C
ATOM 269 CG ASN A 34 30.993 211.015 10.467 1.00 65.78 C
ANISOU 269 CG ASN A 34 9646 6937 8411 -734 394 484 C
ATOM 270 OD1 ASN A 34 30.942 212.083 11.085 1.00 60.61 O
ANISOU 270 OD1 ASN A 34 9033 6169 7829 -769 385 457 O
ATOM 271 ND2 ASN A 34 30.209 210.791 9.428 1.00 53.52 N
ANISOU 271 ND2 ASN A 34 8148 5399 6788 -649 394 552 N
ATOM 272 N ASER A 35 32.837 212.005 13.490 0.60 51.71 N
ANISOU 272 N ASER A 35 7743 5081 6822 -956 353 274 N
ATOM 273 N BSER A 35 32.835 212.003 13.488 0.40 51.78 N
ANISOU 273 N BSER A 35 7753 5091 6831 -956 353 274 N
ATOM 274 CA ASER A 35 32.447 212.604 14.772 0.60 51.52 C
ANISOU 274 CA ASER A 35 7742 4989 6845 -960 300 179 C
ATOM 275 CA BSER A 35 32.449 212.599 14.770 0.40 51.59 C
ANISOU 275 CA BSER A 35 7750 4998 6854 -960 300 179 C
ATOM 276 C ASER A 35 30.918 212.761 14.899 0.60 54.55 C
ANISOU 276 C ASER A 35 8200 5330 7198 -839 265 168 C
ATOM 277 C BSER A 35 30.921 212.762 14.898 0.40 54.57 C
ANISOU 277 C BSER A 35 8203 5332 7200 -839 265 168 C
ATOM 278 O ASER A 35 30.405 212.818 16.021 0.60 53.80 O
ANISOU 278 O ASER A 35 8105 5223 7111 -811 219 79 O
ATOM 279 O BSER A 35 30.412 212.822 16.020 0.40 53.83 O
ANISOU 279 O BSER A 35 8109 5227 7116 -811 219 79 O
ATOM 280 CB ASER A 35 33.130 213.956 14.963 0.60 56.37 C
ANISOU 280 CB ASER A 35 8398 5467 7554 -1067 322 175 C
ATOM 281 CB BSER A 35 33.138 213.947 14.957 0.40 56.54 C
ANISOU 281 CB BSER A 35 8418 5489 7574 -1067 322 175 C
ATOM 282 OG ASER A 35 32.728 214.900 13.983 0.60 66.41 O
ANISOU 282 OG ASER A 35 9771 6619 8843 -1052 364 266 O
ATOM 283 OG BSER A 35 33.051 214.384 16.303 0.40 65.98 O
ANISOU 283 OG BSER A 35 9618 6639 8813 -1090 269 65 O
ATOM 284 N ASN A 36 30.197 212.819 13.756 1.00 50.76 N
ANISOU 284 N ASN A 36 7780 4830 6678 -766 286 258 N
ATOM 285 CA ASN A 36 28.727 212.947 13.711 1.00 50.10 C
ANISOU 285 CA ASN A 36 7756 4711 6567 -645 252 260 C
ATOM 286 C ASN A 36 28.037 211.636 14.147 1.00 53.26 C
ANISOU 286 C ASN A 36 8090 5242 6903 -565 211 210 C
ATOM 287 O ASN A 36 26.874 211.661 14.556 1.00 52.52 O
ANISOU 287 O ASN A 36 8020 5134 6803 -477 176 177 O
ATOM 288 CB ASN A 36 28.253 213.352 12.312 1.00 49.73 C
ANISOU 288 CB ASN A 36 7787 4614 6492 -594 279 374 C
ATOM 289 CG ASN A 36 28.705 214.728 11.881 1.00 70.78 C
ANISOU 289 CG ASN A 36 10538 7132 9223 -656 321 433 C
ATOM 290 OD1 ASN A 36 28.058 215.736 12.167 1.00 64.87 O
ANISOU 290 OD1 ASN A 36 9867 6258 8523 -623 306 424 O
ATOM 291 ND2 ASN A 36 29.818 214.801 11.166 1.00 61.94 N
ANISOU 291 ND2 ASN A 36 9408 6020 8109 -746 379 498 N
ATOM 292 N LEU A 37 28.759 210.501 14.049 1.00 49.30 N
ANISOU 292 N LEU A 37 7505 4865 6361 -597 219 206 N
ATOM 293 CA LEU A 37 28.286 209.175 14.435 1.00 47.81 C
ANISOU 293 CA LEU A 37 7251 4800 6116 -536 186 164 C
ATOM 294 C LEU A 37 28.791 208.809 15.837 1.00 51.21 C
ANISOU 294 C LEU A 37 7617 5275 6566 -581 160 67 C
ATOM 295 O LEU A 37 28.596 207.678 16.283 1.00 49.92 O
ANISOU 295 O LEU A 37 7395 5213 6360 -545 137 30 O
ATOM 296 CB LEU A 37 28.749 208.114 13.409 1.00 47.34 C
ANISOU 296 CB LEU A 37 7148 4845 5996 -534 211 222 C
ATOM 297 CG LEU A 37 28.152 208.168 11.993 1.00 52.25 C
ANISOU 297 CG LEU A 37 7829 5455 6570 -474 227 313 C
ATOM 298 CD1 LEU A 37 29.008 207.368 11.014 1.00 52.07 C
ANISOU 298 CD1 LEU A 37 7771 5517 6497 -502 269 366 C
ATOM 299 CD2 LEU A 37 26.709 207.658 11.966 1.00 52.98 C
ANISOU 299 CD2 LEU A 37 7932 5575 6622 -363 178 300 C
ATOM 300 N GLN A 38 29.448 209.750 16.525 1.00 48.66 N
ANISOU 300 N GLN A 38 7309 4875 6305 -659 161 25 N
ATOM 301 CA GLN A 38 29.989 209.495 17.858 1.00 48.57 C
ANISOU 301 CA GLN A 38 7244 4903 6306 -705 129 -68 C
ATOM 302 C GLN A 38 29.035 210.010 18.938 1.00 53.74 C
ANISOU 302 C GLN A 38 7947 5500 6971 -655 95 -145 C
ATOM 303 O GLN A 38 29.330 210.963 19.657 1.00 54.98 O
ANISOU 303 O GLN A 38 8139 5572 7177 -707 85 -200 O
ATOM 304 CB GLN A 38 31.402 210.074 18.006 1.00 50.51 C
ANISOU 304 CB GLN A 38 7462 5119 6611 -829 143 -78 C
ATOM 305 CG GLN A 38 32.461 209.181 17.376 1.00 54.65 C
ANISOU 305 CG GLN A 38 7901 5747 7116 -873 170 -33 C
ATOM 306 CD GLN A 38 33.747 209.902 17.082 1.00 66.78 C
ANISOU 306 CD GLN A 38 9415 7239 8720 -992 204 -10 C
ATOM 307 OE1 GLN A 38 34.220 210.743 17.855 1.00 62.61 O
ANISOU 307 OE1 GLN A 38 8893 6641 8253 -1067 183 -66 O
ATOM 308 NE2 GLN A 38 34.368 209.548 15.971 1.00 56.73 N
ANISOU 308 NE2 GLN A 38 8109 6008 7436 -1015 257 70 N
ATOM 309 N ASN A 39 27.875 209.354 19.030 1.00 49.72 N
ANISOU 309 N ASN A 39 7439 5038 6416 -554 81 -151 N
ATOM 310 CA ASN A 39 26.818 209.602 20.011 1.00 48.89 C
ANISOU 310 CA ASN A 39 7365 4901 6308 -488 58 -219 C
ATOM 311 C ASN A 39 26.627 208.333 20.853 1.00 51.83 C
ANISOU 311 C ASN A 39 7671 5396 6624 -456 36 -269 C
ATOM 312 O ASN A 39 27.183 207.285 20.507 1.00 51.06 O
ANISOU 312 O ASN A 39 7511 5396 6493 -473 37 -240 O
ATOM 313 CB ASN A 39 25.511 210.035 19.322 1.00 46.07 C
ANISOU 313 CB ASN A 39 7065 4483 5956 -392 66 -174 C
ATOM 314 CG ASN A 39 25.079 209.152 18.174 1.00 66.43 C
ANISOU 314 CG ASN A 39 9616 7135 8491 -339 71 -96 C
ATOM 315 OD1 ASN A 39 24.813 207.954 18.335 1.00 63.47 O
ANISOU 315 OD1 ASN A 39 9180 6866 8068 -306 59 -108 O
ATOM 316 ND2 ASN A 39 24.995 209.726 16.983 1.00 55.17 N
ANISOU 316 ND2 ASN A 39 8238 5648 7076 -329 88 -14 N
ATOM 317 N VAL A 40 25.849 208.422 21.943 1.00 48.23 N
ANISOU 317 N VAL A 40 7235 4933 6159 -408 21 -341 N
ATOM 318 CA VAL A 40 25.584 207.303 22.853 1.00 47.35 C
ANISOU 318 CA VAL A 40 7072 4926 5992 -376 6 -387 C
ATOM 319 C VAL A 40 24.828 206.184 22.116 1.00 50.15 C
ANISOU 319 C VAL A 40 7385 5358 6310 -307 14 -331 C
ATOM 320 O VAL A 40 25.174 205.010 22.287 1.00 50.01 O
ANISOU 320 O VAL A 40 7309 5440 6251 -313 6 -329 O
ATOM 321 CB VAL A 40 24.839 207.763 24.134 1.00 51.60 C
ANISOU 321 CB VAL A 40 7651 5430 6525 -335 0 -472 C
ATOM 322 CG1 VAL A 40 24.531 206.583 25.047 1.00 50.60 C
ANISOU 322 CG1 VAL A 40 7478 5412 6337 -301 -8 -509 C
ATOM 323 CG2 VAL A 40 25.643 208.823 24.884 1.00 52.29 C
ANISOU 323 CG2 VAL A 40 7782 5441 6644 -409 -15 -539 C
ATOM 324 N THR A 41 23.846 206.546 21.265 1.00 46.01 N
ANISOU 324 N THR A 41 6892 4786 5803 -243 25 -284 N
ATOM 325 CA THR A 41 23.053 205.594 20.475 1.00 44.92 C
ANISOU 325 CA THR A 41 6719 4713 5636 -180 24 -234 C
ATOM 326 C THR A 41 23.966 204.664 19.659 1.00 48.61 C
ANISOU 326 C THR A 41 7141 5256 6073 -223 26 -183 C
ATOM 327 O THR A 41 23.758 203.452 19.688 1.00 48.11 O
ANISOU 327 O THR A 41 7027 5280 5972 -199 20 -182 O
ATOM 328 CB THR A 41 22.057 206.315 19.554 1.00 50.76 C
ANISOU 328 CB THR A 41 7503 5380 6402 -115 26 -185 C
ATOM 329 OG1 THR A 41 21.494 207.444 20.223 1.00 53.22 O
ANISOU 329 OG1 THR A 41 7868 5598 6756 -86 31 -229 O
ATOM 330 CG2 THR A 41 20.953 205.395 19.055 1.00 47.50 C
ANISOU 330 CG2 THR A 41 7052 5032 5965 -38 15 -158 C
ATOM 331 N ASN A 42 24.998 205.221 18.987 1.00 44.63 N
ANISOU 331 N ASN A 42 6654 4714 5588 -288 39 -145 N
ATOM 332 CA ASN A 42 25.921 204.445 18.161 1.00 43.44 C
ANISOU 332 CA ASN A 42 6463 4631 5412 -327 51 -98 C
ATOM 333 C ASN A 42 26.980 203.672 18.970 1.00 47.14 C
ANISOU 333 C ASN A 42 6868 5176 5866 -382 44 -139 C
ATOM 334 O ASN A 42 27.637 202.801 18.388 1.00 46.23 O
ANISOU 334 O ASN A 42 6708 5131 5727 -398 54 -106 O
ATOM 335 CB ASN A 42 26.585 205.318 17.108 1.00 42.26 C
ANISOU 335 CB ASN A 42 6352 4418 5288 -374 77 -35 C
ATOM 336 CG ASN A 42 25.666 205.696 15.969 1.00 55.09 C
ANISOU 336 CG ASN A 42 8030 5997 6904 -311 81 30 C
ATOM 337 OD1 ASN A 42 24.668 205.026 15.680 1.00 51.78 O
ANISOU 337 OD1 ASN A 42 7601 5621 6453 -237 63 38 O
ATOM 338 ND2 ASN A 42 25.998 206.768 15.275 1.00 40.57 N
ANISOU 338 ND2 ASN A 42 6249 4071 5093 -341 103 80 N
ATOM 339 N TYR A 43 27.114 203.913 20.299 1.00 43.82 N
ANISOU 339 N TYR A 43 6445 4750 5456 -402 25 -210 N
ATOM 340 CA TYR A 43 28.061 203.105 21.082 1.00 43.53 C
ANISOU 340 CA TYR A 43 6348 4794 5398 -443 8 -246 C
ATOM 341 C TYR A 43 27.460 201.708 21.288 1.00 45.45 C
ANISOU 341 C TYR A 43 6552 5125 5591 -381 2 -246 C
ATOM 342 O TYR A 43 28.193 200.717 21.281 1.00 43.75 O
ANISOU 342 O TYR A 43 6282 4987 5353 -397 -2 -237 O
ATOM 343 CB TYR A 43 28.463 203.764 22.411 1.00 45.91 C
ANISOU 343 CB TYR A 43 6662 5067 5714 -485 -17 -322 C
ATOM 344 CG TYR A 43 29.123 205.124 22.267 1.00 50.39 C
ANISOU 344 CG TYR A 43 7266 5540 6339 -557 -13 -329 C
ATOM 345 CD1 TYR A 43 29.902 205.433 21.150 1.00 53.12 C
ANISOU 345 CD1 TYR A 43 7601 5864 6718 -610 13 -266 C
ATOM 346 CD2 TYR A 43 29.010 206.085 23.266 1.00 52.14 C
ANISOU 346 CD2 TYR A 43 7535 5693 6583 -578 -33 -400 C
ATOM 347 CE1 TYR A 43 30.501 206.685 21.009 1.00 55.30 C
ANISOU 347 CE1 TYR A 43 7912 6046 7054 -683 23 -268 C
ATOM 348 CE2 TYR A 43 29.616 207.335 23.142 1.00 54.29 C
ANISOU 348 CE2 TYR A 43 7845 5868 6916 -650 -30 -409 C
ATOM 349 CZ TYR A 43 30.358 207.633 22.010 1.00 63.51 C
ANISOU 349 CZ TYR A 43 8999 7011 8123 -705 -1 -340 C
ATOM 350 OH TYR A 43 30.950 208.870 21.889 1.00 67.70 O
ANISOU 350 OH TYR A 43 9566 7438 8718 -783 6 -345 O
ATOM 351 N PHE A 44 26.114 201.626 21.370 1.00 41.80 N
ANISOU 351 N PHE A 44 6115 4648 5118 -310 3 -251 N
ATOM 352 CA PHE A 44 25.416 200.346 21.485 1.00 40.95 C
ANISOU 352 CA PHE A 44 5974 4614 4973 -256 1 -247 C
ATOM 353 C PHE A 44 25.380 199.623 20.129 1.00 44.64 C
ANISOU 353 C PHE A 44 6421 5112 5427 -238 11 -185 C
ATOM 354 O PHE A 44 25.389 198.388 20.115 1.00 44.16 O
ANISOU 354 O PHE A 44 6321 5122 5338 -221 9 -180 O
ATOM 355 CB PHE A 44 24.000 200.518 22.050 1.00 42.57 C
ANISOU 355 CB PHE A 44 6202 4794 5178 -192 4 -276 C
ATOM 356 CG PHE A 44 23.944 201.085 23.449 1.00 44.43 C
ANISOU 356 CG PHE A 44 6461 5007 5412 -198 0 -344 C
ATOM 357 CD1 PHE A 44 24.286 200.305 24.549 1.00 47.04 C
ANISOU 357 CD1 PHE A 44 6767 5403 5703 -207 -9 -381 C
ATOM 358 CD2 PHE A 44 23.520 202.390 23.671 1.00 46.50 C
ANISOU 358 CD2 PHE A 44 6779 5182 5708 -191 4 -371 C
ATOM 359 CE1 PHE A 44 24.220 200.827 25.845 1.00 48.02 C
ANISOU 359 CE1 PHE A 44 6922 5511 5812 -210 -14 -446 C
ATOM 360 CE2 PHE A 44 23.449 202.907 24.965 1.00 49.48 C
ANISOU 360 CE2 PHE A 44 7186 5538 6077 -193 2 -442 C
ATOM 361 CZ PHE A 44 23.796 202.121 26.044 1.00 47.29 C
ANISOU 361 CZ PHE A 44 6885 5332 5751 -204 -7 -480 C
ATOM 362 N VAL A 45 25.384 200.379 18.995 1.00 40.51 N
ANISOU 362 N VAL A 45 5932 4537 4923 -243 22 -139 N
ATOM 363 CA VAL A 45 25.399 199.763 17.662 1.00 39.52 C
ANISOU 363 CA VAL A 45 5798 4443 4774 -227 31 -82 C
ATOM 364 C VAL A 45 26.813 199.163 17.395 1.00 41.83 C
ANISOU 364 C VAL A 45 6050 4790 5054 -280 47 -67 C
ATOM 365 O VAL A 45 26.907 198.164 16.690 1.00 40.44 O
ANISOU 365 O VAL A 45 5850 4668 4847 -262 54 -43 O
ATOM 366 CB VAL A 45 24.889 200.656 16.483 1.00 43.88 C
ANISOU 366 CB VAL A 45 6407 4931 5336 -205 37 -30 C
ATOM 367 CG1 VAL A 45 23.726 201.549 16.895 1.00 43.71 C
ANISOU 367 CG1 VAL A 45 6423 4840 5343 -159 23 -49 C
ATOM 368 CG2 VAL A 45 25.999 201.464 15.820 1.00 44.49 C
ANISOU 368 CG2 VAL A 45 6507 4968 5428 -266 64 10 C
ATOM 369 N VAL A 46 27.887 199.764 17.982 1.00 38.49 N
ANISOU 369 N VAL A 46 5615 4351 4658 -345 52 -87 N
ATOM 370 CA VAL A 46 29.288 199.317 17.888 1.00 37.86 C
ANISOU 370 CA VAL A 46 5482 4322 4579 -399 65 -79 C
ATOM 371 C VAL A 46 29.424 197.993 18.655 1.00 41.69 C
ANISOU 371 C VAL A 46 5914 4889 5036 -376 46 -110 C
ATOM 372 O VAL A 46 30.087 197.068 18.166 1.00 41.25 O
ANISOU 372 O VAL A 46 5816 4892 4964 -375 60 -89 O
ATOM 373 CB VAL A 46 30.272 200.416 18.391 1.00 41.65 C
ANISOU 373 CB VAL A 46 5960 4758 5107 -477 66 -99 C
ATOM 374 CG1 VAL A 46 31.594 199.834 18.897 1.00 41.19 C
ANISOU 374 CG1 VAL A 46 5827 4768 5055 -525 59 -118 C
ATOM 375 CG2 VAL A 46 30.525 201.449 17.301 1.00 41.88 C
ANISOU 375 CG2 VAL A 46 6030 4718 5163 -512 101 -46 C
ATOM 376 N SER A 47 28.757 197.900 19.834 1.00 38.03 N
ANISOU 376 N SER A 47 5458 4425 4565 -351 20 -158 N
ATOM 377 CA SER A 47 28.704 196.692 20.674 1.00 37.48 C
ANISOU 377 CA SER A 47 5352 4423 4465 -323 3 -183 C
ATOM 378 C SER A 47 27.982 195.549 19.908 1.00 39.76 C
ANISOU 378 C SER A 47 5635 4746 4727 -269 14 -153 C
ATOM 379 O SER A 47 28.442 194.403 19.921 1.00 39.09 O
ANISOU 379 O SER A 47 5511 4718 4623 -258 14 -147 O
ATOM 380 CB SER A 47 28.005 196.994 21.999 1.00 40.69 C
ANISOU 380 CB SER A 47 5784 4814 4864 -307 -18 -234 C
ATOM 381 OG SER A 47 28.101 195.902 22.898 1.00 47.02 O
ANISOU 381 OG SER A 47 6556 5679 5633 -287 -32 -253 O
ATOM 382 N LEU A 48 26.880 195.894 19.210 1.00 35.19 N
ANISOU 382 N LEU A 48 5094 4127 4151 -234 20 -135 N
ATOM 383 CA LEU A 48 26.084 195.001 18.369 1.00 34.46 C
ANISOU 383 CA LEU A 48 5001 4056 4038 -187 22 -111 C
ATOM 384 C LEU A 48 26.904 194.548 17.142 1.00 39.66 C
ANISOU 384 C LEU A 48 5648 4741 4680 -199 41 -72 C
ATOM 385 O LEU A 48 26.845 193.371 16.768 1.00 38.55 O
ANISOU 385 O LEU A 48 5488 4644 4516 -174 43 -66 O
ATOM 386 CB LEU A 48 24.811 195.740 17.939 1.00 34.39 C
ANISOU 386 CB LEU A 48 5032 3994 4040 -152 15 -103 C
ATOM 387 CG LEU A 48 23.750 194.987 17.147 1.00 38.33 C
ANISOU 387 CG LEU A 48 5530 4509 4524 -103 4 -86 C
ATOM 388 CD1 LEU A 48 23.278 193.743 17.885 1.00 37.19 C
ANISOU 388 CD1 LEU A 48 5350 4410 4372 -82 -1 -112 C
ATOM 389 CD2 LEU A 48 22.548 195.897 16.884 1.00 41.63 C
ANISOU 389 CD2 LEU A 48 5980 4875 4963 -66 -9 -81 C
ATOM 390 N ALA A 49 27.707 195.470 16.558 1.00 37.64 N
ANISOU 390 N ALA A 49 5406 4459 4438 -240 60 -47 N
ATOM 391 CA ALA A 49 28.584 195.168 15.423 1.00 38.30 C
ANISOU 391 CA ALA A 49 5480 4569 4504 -255 91 -8 C
ATOM 392 C ALA A 49 29.748 194.262 15.857 1.00 42.32 C
ANISOU 392 C ALA A 49 5927 5139 5013 -274 100 -22 C
ATOM 393 O ALA A 49 30.182 193.433 15.063 1.00 42.24 O
ANISOU 393 O ALA A 49 5901 5170 4980 -260 123 -2 O
ATOM 394 CB ALA A 49 29.117 196.451 14.794 1.00 39.78 C
ANISOU 394 CB ALA A 49 5697 4706 4711 -298 116 26 C
ATOM 395 N ALA A 50 30.220 194.391 17.116 1.00 38.97 N
ANISOU 395 N ALA A 50 5471 4724 4611 -301 80 -56 N
ATOM 396 CA ALA A 50 31.310 193.568 17.655 1.00 39.09 C
ANISOU 396 CA ALA A 50 5423 4800 4629 -313 78 -69 C
ATOM 397 C ALA A 50 30.842 192.112 17.879 1.00 42.73 C
ANISOU 397 C ALA A 50 5872 5303 5061 -257 67 -78 C
ATOM 398 O ALA A 50 31.589 191.165 17.598 1.00 41.15 O
ANISOU 398 O ALA A 50 5633 5149 4853 -245 81 -69 O
ATOM 399 CB ALA A 50 31.834 194.167 18.953 1.00 39.93 C
ANISOU 399 CB ALA A 50 5507 4903 4760 -353 48 -106 C
ATOM 400 N ALA A 51 29.592 191.944 18.352 1.00 39.75 N
ANISOU 400 N ALA A 51 5527 4905 4671 -224 47 -95 N
ATOM 401 CA ALA A 51 28.987 190.627 18.581 1.00 39.36 C
ANISOU 401 CA ALA A 51 5472 4883 4602 -178 40 -102 C
ATOM 402 C ALA A 51 28.792 189.890 17.254 1.00 43.90 C
ANISOU 402 C ALA A 51 6056 5465 5158 -151 59 -79 C
ATOM 403 O ALA A 51 28.923 188.671 17.216 1.00 43.86 O
ANISOU 403 O ALA A 51 6034 5489 5141 -124 62 -80 O
ATOM 404 CB ALA A 51 27.656 190.773 19.307 1.00 39.70 C
ANISOU 404 CB ALA A 51 5543 4897 4643 -156 23 -122 C
ATOM 405 N ASP A 52 28.533 190.638 16.164 1.00 40.97 N
ANISOU 405 N ASP A 52 5719 5067 4783 -157 72 -57 N
ATOM 406 CA ASP A 52 28.347 190.090 14.822 1.00 40.97 C
ANISOU 406 CA ASP A 52 5739 5075 4754 -132 87 -37 C
ATOM 407 C ASP A 52 29.700 189.711 14.193 1.00 44.71 C
ANISOU 407 C ASP A 52 6185 5585 5218 -144 124 -20 C
ATOM 408 O ASP A 52 29.758 188.703 13.483 1.00 43.83 O
ANISOU 408 O ASP A 52 6076 5497 5080 -114 137 -20 O
ATOM 409 CB ASP A 52 27.554 191.065 13.938 1.00 43.29 C
ANISOU 409 CB ASP A 52 6083 5328 5038 -129 83 -15 C
ATOM 410 CG ASP A 52 26.102 191.269 14.372 1.00 61.28 C
ANISOU 410 CG ASP A 52 8381 7575 7327 -103 47 -32 C
ATOM 411 OD1 ASP A 52 25.650 190.572 15.318 1.00 62.34 O
ANISOU 411 OD1 ASP A 52 8492 7722 7474 -90 33 -60 O
ATOM 412 OD2 ASP A 52 25.414 192.122 13.764 1.00 71.84 O
ANISOU 412 OD2 ASP A 52 9756 8877 8663 -93 37 -14 O
ATOM 413 N ILE A 53 30.789 190.479 14.486 1.00 41.27 N
ANISOU 413 N ILE A 53 5719 5155 4807 -188 142 -11 N
ATOM 414 CA ILE A 53 32.159 190.170 14.032 1.00 41.11 C
ANISOU 414 CA ILE A 53 5654 5175 4790 -203 182 4 C
ATOM 415 C ILE A 53 32.577 188.830 14.681 1.00 45.17 C
ANISOU 415 C ILE A 53 6123 5734 5307 -171 172 -18 C
ATOM 416 O ILE A 53 33.105 187.947 14.000 1.00 45.41 O
ANISOU 416 O ILE A 53 6138 5796 5322 -144 202 -12 O
ATOM 417 CB ILE A 53 33.163 191.324 14.358 1.00 44.52 C
ANISOU 417 CB ILE A 53 6053 5600 5261 -266 196 14 C
ATOM 418 CG1 ILE A 53 32.893 192.570 13.490 1.00 45.68 C
ANISOU 418 CG1 ILE A 53 6253 5698 5406 -295 220 47 C
ATOM 419 CG2 ILE A 53 34.631 190.871 14.205 1.00 45.11 C
ANISOU 419 CG2 ILE A 53 6056 5729 5355 -281 232 22 C
ATOM 420 CD1 ILE A 53 33.413 193.934 14.068 1.00 52.66 C
ANISOU 420 CD1 ILE A 53 7125 6544 6338 -363 217 49 C
ATOM 421 N ALA A 54 32.293 188.679 15.991 1.00 41.16 N
ANISOU 421 N ALA A 54 5600 5225 4814 -170 132 -42 N
ATOM 422 CA ALA A 54 32.591 187.477 16.772 1.00 40.77 C
ANISOU 422 CA ALA A 54 5516 5209 4766 -137 116 -57 C
ATOM 423 C ALA A 54 31.827 186.236 16.251 1.00 43.37 C
ANISOU 423 C ALA A 54 5875 5533 5070 -86 120 -60 C
ATOM 424 O ALA A 54 32.311 185.124 16.434 1.00 43.06 O
ANISOU 424 O ALA A 54 5810 5518 5031 -54 124 -64 O
ATOM 425 CB ALA A 54 32.273 187.714 18.241 1.00 41.15 C
ANISOU 425 CB ALA A 54 5561 5252 4823 -147 73 -78 C
ATOM 426 N VAL A 55 30.661 186.426 15.597 1.00 39.38 N
ANISOU 426 N VAL A 55 5423 4994 4547 -78 116 -61 N
ATOM 427 CA VAL A 55 29.865 185.331 15.020 1.00 38.91 C
ANISOU 427 CA VAL A 55 5392 4925 4467 -39 114 -70 C
ATOM 428 C VAL A 55 30.661 184.706 13.847 1.00 43.27 C
ANISOU 428 C VAL A 55 5943 5500 4998 -19 152 -64 C
ATOM 429 O VAL A 55 30.766 183.482 13.763 1.00 43.93 O
ANISOU 429 O VAL A 55 6022 5591 5077 16 157 -77 O
ATOM 430 CB VAL A 55 28.420 185.778 14.615 1.00 42.12 C
ANISOU 430 CB VAL A 55 5845 5295 4863 -38 92 -74 C
ATOM 431 CG1 VAL A 55 27.781 184.828 13.595 1.00 41.91 C
ANISOU 431 CG1 VAL A 55 5849 5262 4812 -7 90 -85 C
ATOM 432 CG2 VAL A 55 27.522 185.919 15.842 1.00 41.12 C
ANISOU 432 CG2 VAL A 55 5715 5149 4758 -42 63 -88 C
ATOM 433 N GLY A 56 31.249 185.550 13.006 1.00 39.40 N
ANISOU 433 N GLY A 56 5456 5018 4495 -40 182 -44 N
ATOM 434 CA GLY A 56 32.044 185.115 11.863 1.00 39.63 C
ANISOU 434 CA GLY A 56 5486 5074 4499 -22 230 -36 C
ATOM 435 C GLY A 56 33.402 184.540 12.214 1.00 43.77 C
ANISOU 435 C GLY A 56 5945 5639 5048 -12 260 -35 C
ATOM 436 O GLY A 56 33.854 183.585 11.579 1.00 43.91 O
ANISOU 436 O GLY A 56 5960 5675 5049 26 291 -44 O
ATOM 437 N VAL A 57 34.070 185.126 13.211 1.00 40.54 N
ANISOU 437 N VAL A 57 5481 5244 4678 -45 247 -29 N
ATOM 438 CA VAL A 57 35.409 184.725 13.662 1.00 40.62 C
ANISOU 438 CA VAL A 57 5415 5298 4720 -39 264 -26 C
ATOM 439 C VAL A 57 35.338 183.459 14.559 1.00 45.40 C
ANISOU 439 C VAL A 57 6004 5909 5335 8 233 -44 C
ATOM 440 O VAL A 57 36.194 182.585 14.409 1.00 45.55 O
ANISOU 440 O VAL A 57 5985 5958 5365 47 257 -45 O
ATOM 441 CB VAL A 57 36.121 185.917 14.387 1.00 44.17 C
ANISOU 441 CB VAL A 57 5813 5760 5209 -98 253 -16 C
ATOM 442 CG1 VAL A 57 37.439 185.506 15.041 1.00 44.23 C
ANISOU 442 CG1 VAL A 57 5731 5819 5257 -93 252 -18 C
ATOM 443 CG2 VAL A 57 36.347 187.090 13.435 1.00 44.23 C
ANISOU 443 CG2 VAL A 57 5836 5757 5214 -145 295 8 C
ATOM 444 N LEU A 58 34.355 183.368 15.496 1.00 42.00 N
ANISOU 444 N LEU A 58 5604 5451 4905 7 184 -54 N
ATOM 445 CA LEU A 58 34.282 182.263 16.462 1.00 41.72 C
ANISOU 445 CA LEU A 58 5558 5416 4877 46 157 -62 C
ATOM 446 C LEU A 58 33.021 181.380 16.382 1.00 44.58 C
ANISOU 446 C LEU A 58 5980 5736 5221 74 145 -74 C
ATOM 447 O LEU A 58 33.186 180.161 16.326 1.00 44.88 O
ANISOU 447 O LEU A 58 6021 5770 5263 119 153 -78 O
ATOM 448 CB LEU A 58 34.423 182.791 17.911 1.00 42.13 C
ANISOU 448 CB LEU A 58 5583 5480 4944 22 112 -61 C
ATOM 449 CG LEU A 58 35.816 183.273 18.363 1.00 47.96 C
ANISOU 449 CG LEU A 58 6245 6266 5709 2 105 -55 C
ATOM 450 CD1 LEU A 58 35.713 184.106 19.609 1.00 48.24 C
ANISOU 450 CD1 LEU A 58 6276 6306 5749 -36 57 -64 C
ATOM 451 CD2 LEU A 58 36.766 182.105 18.632 1.00 50.84 C
ANISOU 451 CD2 LEU A 58 6560 6667 6089 56 105 -48 C
ATOM 452 N ALA A 59 31.789 181.952 16.419 1.00 39.75 N
ANISOU 452 N ALA A 59 5413 5092 4599 49 126 -80 N
ATOM 453 CA ALA A 59 30.538 181.165 16.423 1.00 38.94 C
ANISOU 453 CA ALA A 59 5355 4950 4490 67 112 -93 C
ATOM 454 C ALA A 59 30.355 180.234 15.202 1.00 42.44 C
ANISOU 454 C ALA A 59 5829 5378 4919 96 133 -107 C
ATOM 455 O ALA A 59 29.871 179.113 15.383 1.00 42.59 O
ANISOU 455 O ALA A 59 5866 5371 4946 121 126 -118 O
ATOM 456 CB ALA A 59 29.331 182.073 16.547 1.00 39.34 C
ANISOU 456 CB ALA A 59 5434 4976 4538 36 91 -97 C
ATOM 457 N ILE A 60 30.732 180.680 13.984 1.00 37.89 N
ANISOU 457 N ILE A 60 5262 4815 4319 93 159 -108 N
ATOM 458 CA ILE A 60 30.602 179.870 12.770 1.00 37.37 C
ANISOU 458 CA ILE A 60 5233 4739 4226 123 178 -127 C
ATOM 459 C ILE A 60 31.689 178.747 12.783 1.00 40.31 C
ANISOU 459 C ILE A 60 5580 5125 4609 167 209 -132 C
ATOM 460 O ILE A 60 31.286 177.582 12.653 1.00 39.25 O
ANISOU 460 O ILE A 60 5475 4959 4478 198 205 -154 O
ATOM 461 CB ILE A 60 30.566 180.745 11.485 1.00 40.84 C
ANISOU 461 CB ILE A 60 5703 5190 4625 108 197 -123 C
ATOM 462 CG1 ILE A 60 29.143 181.336 11.305 1.00 41.20 C
ANISOU 462 CG1 ILE A 60 5789 5206 4660 87 155 -127 C
ATOM 463 CG2 ILE A 60 30.988 179.961 10.235 1.00 41.39 C
ANISOU 463 CG2 ILE A 60 5803 5267 4657 145 233 -142 C
ATOM 464 CD1 ILE A 60 29.080 182.707 10.642 1.00 50.95 C
ANISOU 464 CD1 ILE A 60 7042 6448 5869 61 160 -104 C
ATOM 465 N PRO A 61 33.014 178.999 13.027 1.00 36.55 N
ANISOU 465 N PRO A 61 5048 4690 4148 174 236 -114 N
ATOM 466 CA PRO A 61 33.963 177.864 13.117 1.00 36.43 C
ANISOU 466 CA PRO A 61 5004 4686 4151 227 260 -119 C
ATOM 467 C PRO A 61 33.547 176.842 14.194 1.00 39.35 C
ANISOU 467 C PRO A 61 5381 5023 4548 252 227 -120 C
ATOM 468 O PRO A 61 33.730 175.645 13.997 1.00 38.37 O
ANISOU 468 O PRO A 61 5272 4876 4431 300 241 -133 O
ATOM 469 CB PRO A 61 35.290 178.544 13.463 1.00 38.28 C
ANISOU 469 CB PRO A 61 5161 4975 4408 217 280 -95 C
ATOM 470 CG PRO A 61 35.153 179.910 12.897 1.00 42.43 C
ANISOU 470 CG PRO A 61 5694 5514 4915 163 291 -84 C
ATOM 471 CD PRO A 61 33.731 180.284 13.183 1.00 37.53 C
ANISOU 471 CD PRO A 61 5128 4851 4281 134 246 -91 C
ATOM 472 N PHE A 62 32.925 177.314 15.298 1.00 35.70 N
ANISOU 472 N PHE A 62 4915 4552 4096 219 187 -106 N
ATOM 473 CA PHE A 62 32.386 176.470 16.368 1.00 34.77 C
ANISOU 473 CA PHE A 62 4813 4403 3997 235 159 -99 C
ATOM 474 C PHE A 62 31.191 175.657 15.851 1.00 37.37 C
ANISOU 474 C PHE A 62 5203 4675 4323 238 157 -122 C
ATOM 475 O PHE A 62 31.097 174.471 16.159 1.00 37.20 O
ANISOU 475 O PHE A 62 5199 4617 4319 270 158 -123 O
ATOM 476 CB PHE A 62 31.969 177.320 17.585 1.00 36.15 C
ANISOU 476 CB PHE A 62 4974 4588 4172 197 125 -81 C
ATOM 477 CG PHE A 62 33.055 177.914 18.464 1.00 38.03 C
ANISOU 477 CG PHE A 62 5156 4876 4418 193 110 -62 C
ATOM 478 CD1 PHE A 62 34.403 177.730 18.163 1.00 41.56 C
ANISOU 478 CD1 PHE A 62 5550 5362 4878 221 128 -57 C
ATOM 479 CD2 PHE A 62 32.728 178.657 19.593 1.00 39.66 C
ANISOU 479 CD2 PHE A 62 5358 5092 4618 161 78 -54 C
ATOM 480 CE1 PHE A 62 35.400 178.269 18.985 1.00 42.46 C
ANISOU 480 CE1 PHE A 62 5603 5525 5005 214 105 -42 C
ATOM 481 CE2 PHE A 62 33.725 179.193 20.412 1.00 42.58 C
ANISOU 481 CE2 PHE A 62 5678 5509 4993 155 55 -44 C
ATOM 482 CZ PHE A 62 35.053 179.002 20.099 1.00 41.19 C
ANISOU 482 CZ PHE A 62 5444 5372 4835 178 65 -38 C
ATOM 483 N ALA A 63 30.292 176.286 15.055 1.00 34.02 N
ANISOU 483 N ALA A 63 4808 4240 3878 204 151 -141 N
ATOM 484 CA ALA A 63 29.121 175.630 14.447 1.00 34.32 C
ANISOU 484 CA ALA A 63 4896 4230 3914 199 140 -169 C
ATOM 485 C ALA A 63 29.528 174.523 13.464 1.00 40.04 C
ANISOU 485 C ALA A 63 5649 4932 4630 240 164 -198 C
ATOM 486 O ALA A 63 28.871 173.486 13.421 1.00 39.82 O
ANISOU 486 O ALA A 63 5656 4853 4620 248 155 -219 O
ATOM 487 CB ALA A 63 28.246 176.647 13.736 1.00 34.80 C
ANISOU 487 CB ALA A 63 4974 4296 3952 162 122 -180 C
ATOM 488 N ILE A 64 30.602 174.739 12.681 1.00 38.32 N
ANISOU 488 N ILE A 64 5419 4752 4390 265 198 -201 N
ATOM 489 CA ILE A 64 31.126 173.755 11.718 1.00 38.90 C
ANISOU 489 CA ILE A 64 5521 4811 4449 312 231 -233 C
ATOM 490 C ILE A 64 31.701 172.560 12.501 1.00 44.01 C
ANISOU 490 C ILE A 64 6154 5429 5137 359 240 -225 C
ATOM 491 O ILE A 64 31.523 171.410 12.084 1.00 45.20 O
ANISOU 491 O ILE A 64 6348 5530 5295 391 249 -257 O
ATOM 492 CB ILE A 64 32.183 174.415 10.768 1.00 41.85 C
ANISOU 492 CB ILE A 64 5875 5239 4786 326 277 -231 C
ATOM 493 CG1 ILE A 64 31.523 175.474 9.850 1.00 41.70 C
ANISOU 493 CG1 ILE A 64 5888 5236 4718 286 268 -236 C
ATOM 494 CG2 ILE A 64 32.981 173.371 9.950 1.00 42.00 C
ANISOU 494 CG2 ILE A 64 5912 5252 4794 387 324 -261 C
ATOM 495 CD1 ILE A 64 32.471 176.525 9.272 1.00 48.42 C
ANISOU 495 CD1 ILE A 64 6712 6145 5542 278 311 -211 C
ATOM 496 N THR A 65 32.359 172.843 13.644 1.00 39.60 N
ANISOU 496 N THR A 65 5541 4900 4604 364 234 -185 N
ATOM 497 CA THR A 65 32.987 171.843 14.515 1.00 39.72 C
ANISOU 497 CA THR A 65 5539 4897 4656 414 236 -165 C
ATOM 498 C THR A 65 31.933 170.906 15.118 1.00 43.72 C
ANISOU 498 C THR A 65 6095 5331 5186 408 212 -165 C
ATOM 499 O THR A 65 32.073 169.692 14.993 1.00 43.51 O
ANISOU 499 O THR A 65 6098 5252 5180 452 226 -177 O
ATOM 500 CB THR A 65 33.824 172.543 15.608 1.00 45.42 C
ANISOU 500 CB THR A 65 6192 5675 5389 412 221 -122 C
ATOM 501 OG1 THR A 65 34.802 173.370 14.990 1.00 46.63 O
ANISOU 501 OG1 THR A 65 6296 5891 5531 410 248 -123 O
ATOM 502 CG2 THR A 65 34.533 171.575 16.511 1.00 44.02 C
ANISOU 502 CG2 THR A 65 5994 5487 5243 470 215 -96 C
ATOM 503 N ILE A 66 30.880 171.475 15.743 1.00 40.80 N
ANISOU 503 N ILE A 66 5732 4955 4815 353 182 -153 N
ATOM 504 CA ILE A 66 29.804 170.763 16.437 1.00 40.97 C
ANISOU 504 CA ILE A 66 5790 4915 4863 334 165 -145 C
ATOM 505 C ILE A 66 28.972 169.882 15.476 1.00 45.77 C
ANISOU 505 C ILE A 66 6452 5456 5481 327 168 -192 C
ATOM 506 O ILE A 66 28.413 168.877 15.929 1.00 46.48 O
ANISOU 506 O ILE A 66 6574 5481 5606 327 167 -188 O
ATOM 507 CB ILE A 66 28.920 171.750 17.263 1.00 43.77 C
ANISOU 507 CB ILE A 66 6129 5289 5211 278 141 -124 C
ATOM 508 CG1 ILE A 66 28.205 171.040 18.413 1.00 44.51 C
ANISOU 508 CG1 ILE A 66 6243 5337 5331 270 136 -95 C
ATOM 509 CG2 ILE A 66 27.946 172.574 16.422 1.00 43.85 C
ANISOU 509 CG2 ILE A 66 6149 5306 5206 231 128 -155 C
ATOM 510 CD1 ILE A 66 28.481 171.608 19.691 1.00 50.32 C
ANISOU 510 CD1 ILE A 66 6953 6112 6055 268 126 -54 C
ATOM 511 N SER A 67 28.935 170.213 14.164 1.00 41.21 N
ANISOU 511 N SER A 67 5890 4894 4873 322 173 -235 N
ATOM 512 CA SER A 67 28.191 169.411 13.192 1.00 41.23 C
ANISOU 512 CA SER A 67 5947 4839 4878 315 167 -288 C
ATOM 513 C SER A 67 28.912 168.076 12.841 1.00 46.73 C
ANISOU 513 C SER A 67 6678 5485 5591 376 196 -311 C
ATOM 514 O SER A 67 28.253 167.157 12.351 1.00 47.86 O
ANISOU 514 O SER A 67 6873 5559 5752 369 188 -353 O
ATOM 515 CB SER A 67 27.906 170.211 11.925 1.00 43.39 C
ANISOU 515 CB SER A 67 6235 5149 5102 295 158 -325 C
ATOM 516 OG SER A 67 29.093 170.519 11.214 1.00 51.61 O
ANISOU 516 OG SER A 67 7267 6238 6105 336 194 -329 O
ATOM 517 N THR A 68 30.233 167.962 13.096 1.00 42.96 N
ANISOU 517 N THR A 68 6170 5038 5114 434 227 -286 N
ATOM 518 CA THR A 68 30.998 166.744 12.779 1.00 43.67 C
ANISOU 518 CA THR A 68 6288 5082 5223 504 258 -307 C
ATOM 519 C THR A 68 30.686 165.602 13.752 1.00 50.14 C
ANISOU 519 C THR A 68 7134 5820 6098 517 251 -282 C
ATOM 520 O THR A 68 30.773 164.436 13.361 1.00 51.69 O
ANISOU 520 O THR A 68 7380 5942 6318 556 267 -314 O
ATOM 521 CB THR A 68 32.524 166.998 12.737 1.00 48.38 C
ANISOU 521 CB THR A 68 6831 5741 5809 566 295 -287 C
ATOM 522 OG1 THR A 68 33.019 167.311 14.045 1.00 46.65 O
ANISOU 522 OG1 THR A 68 6555 5555 5613 574 280 -224 O
ATOM 523 CG2 THR A 68 32.932 168.067 11.713 1.00 44.12 C
ANISOU 523 CG2 THR A 68 6268 5277 5217 553 316 -306 C
ATOM 524 N GLY A 69 30.347 165.942 14.996 1.00 46.97 N
ANISOU 524 N GLY A 69 6705 5428 5712 488 230 -226 N
ATOM 525 CA GLY A 69 30.043 164.966 16.040 1.00 47.14 C
ANISOU 525 CA GLY A 69 6754 5379 5780 498 226 -188 C
ATOM 526 C GLY A 69 31.278 164.297 16.609 1.00 52.65 C
ANISOU 526 C GLY A 69 7438 6072 6495 582 243 -150 C
ATOM 527 O GLY A 69 31.189 163.193 17.148 1.00 53.80 O
ANISOU 527 O GLY A 69 7624 6138 6679 611 249 -127 O
ATOM 528 N PHE A 70 32.438 164.976 16.506 1.00 49.21 N
ANISOU 528 N PHE A 70 6943 5721 6035 622 251 -140 N
ATOM 529 CA PHE A 70 33.759 164.546 16.973 1.00 49.61 C
ANISOU 529 CA PHE A 70 6957 5792 6102 707 261 -106 C
ATOM 530 C PHE A 70 33.776 164.266 18.491 1.00 54.60 C
ANISOU 530 C PHE A 70 7585 6411 6749 720 234 -33 C
ATOM 531 O PHE A 70 33.032 164.901 19.243 1.00 51.94 O
ANISOU 531 O PHE A 70 7246 6095 6395 659 210 -7 O
ATOM 532 CB PHE A 70 34.805 165.625 16.613 1.00 50.89 C
ANISOU 532 CB PHE A 70 7039 6060 6236 718 269 -108 C
ATOM 533 CG PHE A 70 34.867 166.830 17.529 1.00 51.63 C
ANISOU 533 CG PHE A 70 7075 6233 6308 673 235 -67 C
ATOM 534 CD1 PHE A 70 33.795 167.713 17.624 1.00 53.56 C
ANISOU 534 CD1 PHE A 70 7333 6488 6528 590 215 -73 C
ATOM 535 CD2 PHE A 70 35.993 167.077 18.304 1.00 53.36 C
ANISOU 535 CD2 PHE A 70 7227 6514 6534 716 219 -26 C
ATOM 536 CE1 PHE A 70 33.842 168.806 18.494 1.00 53.18 C
ANISOU 536 CE1 PHE A 70 7241 6505 6460 551 186 -41 C
ATOM 537 CE2 PHE A 70 36.052 168.192 19.144 1.00 55.08 C
ANISOU 537 CE2 PHE A 70 7397 6801 6729 671 183 3 C
ATOM 538 CZ PHE A 70 34.974 169.045 19.237 1.00 52.07 C
ANISOU 538 CZ PHE A 70 7040 6423 6323 589 169 -6 C
ATOM 539 N CYS A 71 34.618 163.312 18.932 1.00 54.91 N
ANISOU 539 N CYS A 71 7627 6419 6817 805 240 -2 N
ATOM 540 CA CYS A 71 34.737 162.968 20.354 1.00 56.64 C
ANISOU 540 CA CYS A 71 7850 6629 7043 831 212 73 C
ATOM 541 C CYS A 71 35.476 164.087 21.080 1.00 59.47 C
ANISOU 541 C CYS A 71 8127 7101 7367 829 178 106 C
ATOM 542 O CYS A 71 36.533 164.527 20.617 1.00 59.82 O
ANISOU 542 O CYS A 71 8103 7214 7411 864 181 89 O
ATOM 543 CB CYS A 71 35.426 161.620 20.549 1.00 59.30 C
ANISOU 543 CB CYS A 71 8216 6893 7420 930 224 99 C
ATOM 544 SG CYS A 71 34.473 160.199 19.949 1.00 64.75 S
ANISOU 544 SG CYS A 71 9017 7427 8159 925 259 66 S
ATOM 545 N ALA A 72 34.890 164.582 22.187 1.00 54.07 N
ANISOU 545 N ALA A 72 7451 6438 6656 782 148 148 N
ATOM 546 CA ALA A 72 35.445 165.676 22.987 1.00 53.09 C
ANISOU 546 CA ALA A 72 7262 6416 6495 769 108 174 C
ATOM 547 C ALA A 72 34.964 165.620 24.411 1.00 56.86 C
ANISOU 547 C ALA A 72 7774 6888 6944 757 79 234 C
ATOM 548 O ALA A 72 33.885 165.082 24.664 1.00 56.68 O
ANISOU 548 O ALA A 72 7819 6790 6925 726 98 248 O
ATOM 549 CB ALA A 72 35.044 167.021 22.384 1.00 52.87 C
ANISOU 549 CB ALA A 72 7200 6445 6442 689 110 128 C
ATOM 550 N ALA A 73 35.738 166.227 25.340 1.00 53.57 N
ANISOU 550 N ALA A 73 7307 6552 6494 777 33 266 N
ATOM 551 CA ALA A 73 35.360 166.368 26.747 1.00 53.32 C
ANISOU 551 CA ALA A 73 7308 6535 6416 765 1 320 C
ATOM 552 C ALA A 73 34.068 167.176 26.794 1.00 56.32 C
ANISOU 552 C ALA A 73 7716 6911 6771 670 18 296 C
ATOM 553 O ALA A 73 33.973 168.207 26.123 1.00 54.60 O
ANISOU 553 O ALA A 73 7457 6736 6551 618 21 246 O
ATOM 554 CB ALA A 73 36.471 167.059 27.527 1.00 54.27 C
ANISOU 554 CB ALA A 73 7360 6755 6503 794 -59 339 C
ATOM 555 N CYS A 74 33.054 166.663 27.507 1.00 54.52 N
ANISOU 555 N CYS A 74 7558 6625 6530 649 37 333 N
ATOM 556 CA CYS A 74 31.705 167.227 27.573 1.00 54.65 C
ANISOU 556 CA CYS A 74 7604 6627 6534 566 63 314 C
ATOM 557 C CYS A 74 31.652 168.719 27.927 1.00 57.98 C
ANISOU 557 C CYS A 74 7984 7135 6910 517 37 290 C
ATOM 558 O CYS A 74 30.808 169.413 27.358 1.00 57.50 O
ANISOU 558 O CYS A 74 7918 7072 6857 454 57 247 O
ATOM 559 CB CYS A 74 30.812 166.424 28.508 1.00 55.93 C
ANISOU 559 CB CYS A 74 7840 6725 6687 560 89 371 C
ATOM 560 SG CYS A 74 29.049 166.604 28.144 1.00 59.46 S
ANISOU 560 SG CYS A 74 8316 7118 7159 465 140 341 S
ATOM 561 N HIS A 75 32.517 169.217 28.836 1.00 54.33 N
ANISOU 561 N HIS A 75 7495 6745 6401 545 -10 312 N
ATOM 562 CA HIS A 75 32.506 170.645 29.184 1.00 53.71 C
ANISOU 562 CA HIS A 75 7384 6742 6283 496 -37 282 C
ATOM 563 C HIS A 75 33.078 171.512 28.044 1.00 56.57 C
ANISOU 563 C HIS A 75 7677 7143 6675 472 -43 225 C
ATOM 564 O HIS A 75 32.611 172.636 27.846 1.00 55.36 O
ANISOU 564 O HIS A 75 7508 7014 6510 413 -41 188 O
ATOM 565 CB HIS A 75 33.222 170.911 30.505 1.00 55.24 C
ANISOU 565 CB HIS A 75 7574 6999 6414 527 -91 317 C
ATOM 566 CG HIS A 75 32.385 170.529 31.681 1.00 59.29 C
ANISOU 566 CG HIS A 75 8162 7488 6875 526 -77 365 C
ATOM 567 ND1 HIS A 75 32.318 169.217 32.123 1.00 61.94 N
ANISOU 567 ND1 HIS A 75 8554 7768 7213 578 -61 428 N
ATOM 568 CD2 HIS A 75 31.557 171.288 32.435 1.00 61.06 C
ANISOU 568 CD2 HIS A 75 8418 7734 7049 480 -67 359 C
ATOM 569 CE1 HIS A 75 31.472 169.225 33.141 1.00 61.71 C
ANISOU 569 CE1 HIS A 75 8586 7730 7130 558 -40 462 C
ATOM 570 NE2 HIS A 75 30.991 170.449 33.369 1.00 61.54 N
ANISOU 570 NE2 HIS A 75 8551 7757 7074 501 -41 420 N
ATOM 571 N GLY A 76 34.030 170.963 27.286 1.00 53.09 N
ANISOU 571 N GLY A 76 7197 6701 6273 520 -44 221 N
ATOM 572 CA GLY A 76 34.619 171.622 26.125 1.00 52.37 C
ANISOU 572 CA GLY A 76 7046 6642 6212 503 -37 174 C
ATOM 573 C GLY A 76 33.606 171.712 25.001 1.00 55.77 C
ANISOU 573 C GLY A 76 7504 7022 6665 457 9 136 C
ATOM 574 O GLY A 76 33.518 172.734 24.312 1.00 54.07 O
ANISOU 574 O GLY A 76 7260 6834 6449 411 14 98 O
ATOM 575 N CYS A 77 32.806 170.637 24.846 1.00 53.02 N
ANISOU 575 N CYS A 77 7214 6596 6335 468 39 147 N
ATOM 576 CA CYS A 77 31.713 170.517 23.880 1.00 52.70 C
ANISOU 576 CA CYS A 77 7206 6500 6317 426 74 112 C
ATOM 577 C CYS A 77 30.629 171.562 24.201 1.00 53.20 C
ANISOU 577 C CYS A 77 7278 6578 6358 357 72 99 C
ATOM 578 O CYS A 77 30.082 172.177 23.281 1.00 52.05 O
ANISOU 578 O CYS A 77 7125 6430 6220 316 83 60 O
ATOM 579 CB CYS A 77 31.150 169.098 23.899 1.00 54.47 C
ANISOU 579 CB CYS A 77 7490 6637 6571 451 98 131 C
ATOM 580 SG CYS A 77 29.836 168.798 22.689 1.00 58.69 S
ANISOU 580 SG CYS A 77 8061 7100 7139 399 130 82 S
ATOM 581 N LEU A 78 30.347 171.772 25.512 1.00 48.03 N
ANISOU 581 N LEU A 78 6640 5940 5671 350 58 133 N
ATOM 582 CA LEU A 78 29.383 172.758 26.005 1.00 47.03 C
ANISOU 582 CA LEU A 78 6521 5830 5519 295 60 122 C
ATOM 583 C LEU A 78 29.795 174.182 25.630 1.00 49.50 C
ANISOU 583 C LEU A 78 6788 6201 5818 264 39 86 C
ATOM 584 O LEU A 78 28.935 174.963 25.219 1.00 48.76 O
ANISOU 584 O LEU A 78 6696 6101 5728 219 50 58 O
ATOM 585 CB LEU A 78 29.215 172.668 27.531 1.00 47.45 C
ANISOU 585 CB LEU A 78 6604 5897 5527 304 52 166 C
ATOM 586 CG LEU A 78 28.219 171.659 28.064 1.00 52.18 C
ANISOU 586 CG LEU A 78 7259 6434 6135 302 89 203 C
ATOM 587 CD1 LEU A 78 28.411 171.474 29.539 1.00 52.90 C
ANISOU 587 CD1 LEU A 78 7383 6547 6170 328 79 255 C
ATOM 588 CD2 LEU A 78 26.781 172.077 27.761 1.00 53.66 C
ANISOU 588 CD2 LEU A 78 7453 6593 6343 243 123 177 C
ATOM 589 N PHE A 79 31.100 174.525 25.775 1.00 44.69 N
ANISOU 589 N PHE A 79 6137 5646 5198 289 8 88 N
ATOM 590 CA PHE A 79 31.603 175.855 25.429 1.00 43.62 C
ANISOU 590 CA PHE A 79 5956 5560 5056 255 -10 57 C
ATOM 591 C PHE A 79 31.418 176.132 23.919 1.00 45.93 C
ANISOU 591 C PHE A 79 6237 5835 5380 234 17 24 C
ATOM 592 O PHE A 79 31.009 177.240 23.561 1.00 45.08 O
ANISOU 592 O PHE A 79 6123 5736 5268 190 18 0 O
ATOM 593 CB PHE A 79 33.072 176.045 25.853 1.00 45.77 C
ANISOU 593 CB PHE A 79 6177 5893 5322 283 -49 66 C
ATOM 594 CG PHE A 79 33.571 177.456 25.632 1.00 47.48 C
ANISOU 594 CG PHE A 79 6347 6156 5538 238 -67 35 C
ATOM 595 CD1 PHE A 79 33.301 178.461 26.555 1.00 50.78 C
ANISOU 595 CD1 PHE A 79 6775 6596 5922 201 -94 23 C
ATOM 596 CD2 PHE A 79 34.287 177.787 24.488 1.00 49.77 C
ANISOU 596 CD2 PHE A 79 6589 6461 5860 230 -52 17 C
ATOM 597 CE1 PHE A 79 33.740 179.768 26.337 1.00 51.83 C
ANISOU 597 CE1 PHE A 79 6871 6759 6061 154 -110 -7 C
ATOM 598 CE2 PHE A 79 34.730 179.095 24.273 1.00 52.73 C
ANISOU 598 CE2 PHE A 79 6925 6869 6240 181 -63 -6 C
ATOM 599 CZ PHE A 79 34.453 180.076 25.199 1.00 50.86 C
ANISOU 599 CZ PHE A 79 6700 6648 5977 142 -94 -19 C
ATOM 600 N ILE A 80 31.688 175.114 23.057 1.00 41.57 N
ANISOU 600 N ILE A 80 5688 5253 4854 270 39 24 N
ATOM 601 CA ILE A 80 31.553 175.148 21.592 1.00 40.53 C
ANISOU 601 CA ILE A 80 5557 5104 4741 261 65 -6 C
ATOM 602 C ILE A 80 30.078 175.415 21.202 1.00 43.23 C
ANISOU 602 C ILE A 80 5937 5405 5082 218 75 -26 C
ATOM 603 O ILE A 80 29.821 176.238 20.328 1.00 43.09 O
ANISOU 603 O ILE A 80 5915 5396 5061 188 80 -50 O
ATOM 604 CB ILE A 80 32.099 173.810 20.966 1.00 44.07 C
ANISOU 604 CB ILE A 80 6012 5522 5211 317 86 -5 C
ATOM 605 CG1 ILE A 80 33.641 173.683 21.088 1.00 45.09 C
ANISOU 605 CG1 ILE A 80 6085 5699 5348 364 80 9 C
ATOM 606 CG2 ILE A 80 31.638 173.564 19.522 1.00 44.89 C
ANISOU 606 CG2 ILE A 80 6140 5591 5323 310 114 -41 C
ATOM 607 CD1 ILE A 80 34.531 174.580 20.188 1.00 53.75 C
ANISOU 607 CD1 ILE A 80 7127 6848 6447 350 93 -12 C
ATOM 608 N ALA A 81 29.128 174.729 21.857 1.00 39.38 N
ANISOU 608 N ALA A 81 5486 4876 4601 215 79 -12 N
ATOM 609 CA ALA A 81 27.687 174.829 21.587 1.00 38.39 C
ANISOU 609 CA ALA A 81 5387 4713 4487 177 88 -29 C
ATOM 610 C ALA A 81 27.023 176.087 22.155 1.00 41.68 C
ANISOU 610 C ALA A 81 5796 5154 4888 138 79 -33 C
ATOM 611 O ALA A 81 26.081 176.584 21.538 1.00 41.46 O
ANISOU 611 O ALA A 81 5771 5112 4870 108 81 -55 O
ATOM 612 CB ALA A 81 26.972 173.605 22.147 1.00 39.23 C
ANISOU 612 CB ALA A 81 5528 4764 4614 184 103 -9 C
ATOM 613 N CYS A 82 27.461 176.566 23.335 1.00 38.48 N
ANISOU 613 N CYS A 82 5381 4783 4456 140 67 -13 N
ATOM 614 CA CYS A 82 26.824 177.675 24.058 1.00 38.28 C
ANISOU 614 CA CYS A 82 5358 4776 4412 109 62 -20 C
ATOM 615 C CYS A 82 27.423 179.060 23.781 1.00 40.57 C
ANISOU 615 C CYS A 82 5621 5103 4689 89 43 -41 C
ATOM 616 O CYS A 82 26.768 180.044 24.131 1.00 39.52 O
ANISOU 616 O CYS A 82 5494 4973 4549 63 42 -55 O
ATOM 617 CB CYS A 82 26.824 177.391 25.559 1.00 39.25 C
ANISOU 617 CB CYS A 82 5499 4911 4505 122 62 9 C
ATOM 618 SG CYS A 82 25.850 175.942 26.040 1.00 43.57 S
ANISOU 618 SG CYS A 82 6083 5403 5068 133 96 42 S
ATOM 619 N PHE A 83 28.646 179.166 23.205 1.00 36.69 N
ANISOU 619 N PHE A 83 5101 4639 4201 100 33 -43 N
ATOM 620 CA PHE A 83 29.267 180.482 22.980 1.00 36.14 C
ANISOU 620 CA PHE A 83 5005 4600 4126 73 19 -59 C
ATOM 621 C PHE A 83 28.395 181.427 22.115 1.00 39.57 C
ANISOU 621 C PHE A 83 5453 5012 4571 41 29 -79 C
ATOM 622 O PHE A 83 28.349 182.623 22.401 1.00 39.04 O
ANISOU 622 O PHE A 83 5383 4952 4498 14 18 -91 O
ATOM 623 CB PHE A 83 30.684 180.377 22.396 1.00 37.89 C
ANISOU 623 CB PHE A 83 5186 4853 4357 86 16 -55 C
ATOM 624 CG PHE A 83 31.367 181.723 22.267 1.00 39.35 C
ANISOU 624 CG PHE A 83 5340 5068 4545 49 4 -68 C
ATOM 625 CD1 PHE A 83 31.738 182.448 23.398 1.00 42.85 C
ANISOU 625 CD1 PHE A 83 5772 5537 4974 30 -27 -73 C
ATOM 626 CD2 PHE A 83 31.608 182.283 21.017 1.00 40.73 C
ANISOU 626 CD2 PHE A 83 5504 5239 4733 31 26 -74 C
ATOM 627 CE1 PHE A 83 32.344 183.704 23.279 1.00 43.80 C
ANISOU 627 CE1 PHE A 83 5865 5674 5104 -13 -38 -89 C
ATOM 628 CE2 PHE A 83 32.226 183.535 20.900 1.00 43.77 C
ANISOU 628 CE2 PHE A 83 5863 5642 5125 -10 20 -81 C
ATOM 629 CZ PHE A 83 32.584 184.238 22.030 1.00 42.21 C
ANISOU 629 CZ PHE A 83 5651 5464 4924 -34 -12 -90 C
ATOM 630 N VAL A 84 27.683 180.890 21.103 1.00 36.21 N
ANISOU 630 N VAL A 84 5044 4556 4159 48 44 -84 N
ATOM 631 CA VAL A 84 26.801 181.674 20.222 1.00 35.44 C
ANISOU 631 CA VAL A 84 4959 4438 4067 27 45 -99 C
ATOM 632 C VAL A 84 25.647 182.327 21.044 1.00 39.09 C
ANISOU 632 C VAL A 84 5434 4886 4533 11 41 -106 C
ATOM 633 O VAL A 84 25.241 183.449 20.722 1.00 39.08 O
ANISOU 633 O VAL A 84 5436 4877 4535 -6 36 -117 O
ATOM 634 CB VAL A 84 26.274 180.834 19.021 1.00 38.52 C
ANISOU 634 CB VAL A 84 5366 4804 4467 39 52 -108 C
ATOM 635 CG1 VAL A 84 25.400 179.658 19.470 1.00 38.00 C
ANISOU 635 CG1 VAL A 84 5313 4708 4417 49 56 -107 C
ATOM 636 CG2 VAL A 84 25.563 181.702 17.987 1.00 37.89 C
ANISOU 636 CG2 VAL A 84 5300 4713 4385 24 45 -120 C
ATOM 637 N LEU A 85 25.172 181.648 22.120 1.00 34.77 N
ANISOU 637 N LEU A 85 4892 4333 3984 20 48 -98 N
ATOM 638 CA LEU A 85 24.104 182.144 22.999 1.00 34.21 C
ANISOU 638 CA LEU A 85 4831 4253 3914 10 56 -104 C
ATOM 639 C LEU A 85 24.540 183.404 23.757 1.00 38.99 C
ANISOU 639 C LEU A 85 5439 4879 4499 -3 45 -115 C
ATOM 640 O LEU A 85 23.693 184.248 24.051 1.00 38.95 O
ANISOU 640 O LEU A 85 5441 4860 4497 -11 51 -131 O
ATOM 641 CB LEU A 85 23.629 181.074 23.993 1.00 33.96 C
ANISOU 641 CB LEU A 85 4810 4214 3880 22 75 -86 C
ATOM 642 CG LEU A 85 23.213 179.730 23.415 1.00 38.61 C
ANISOU 642 CG LEU A 85 5401 4772 4495 29 86 -76 C
ATOM 643 CD1 LEU A 85 23.110 178.688 24.505 1.00 39.06 C
ANISOU 643 CD1 LEU A 85 5475 4820 4545 41 107 -48 C
ATOM 644 CD2 LEU A 85 21.909 179.834 22.648 1.00 40.63 C
ANISOU 644 CD2 LEU A 85 5649 5001 4788 13 90 -94 C
ATOM 645 N VAL A 86 25.856 183.528 24.057 1.00 35.71 N
ANISOU 645 N VAL A 86 5013 4493 4064 -4 28 -111 N
ATOM 646 CA VAL A 86 26.460 184.693 24.719 1.00 35.93 C
ANISOU 646 CA VAL A 86 5039 4538 4073 -23 10 -128 C
ATOM 647 C VAL A 86 26.361 185.896 23.761 1.00 40.68 C
ANISOU 647 C VAL A 86 5639 5119 4696 -47 8 -143 C
ATOM 648 O VAL A 86 25.945 186.981 24.167 1.00 40.78 O
ANISOU 648 O VAL A 86 5668 5116 4709 -61 6 -163 O
ATOM 649 CB VAL A 86 27.931 184.409 25.145 1.00 39.79 C
ANISOU 649 CB VAL A 86 5506 5068 4547 -20 -15 -119 C
ATOM 650 CG1 VAL A 86 28.616 185.664 25.690 1.00 39.69 C
ANISOU 650 CG1 VAL A 86 5486 5071 4523 -50 -41 -144 C
ATOM 651 CG2 VAL A 86 28.010 183.264 26.155 1.00 39.69 C
ANISOU 651 CG2 VAL A 86 5502 5072 4506 11 -17 -98 C
ATOM 652 N LEU A 87 26.705 185.673 22.481 1.00 36.94 N
ANISOU 652 N LEU A 87 5154 4642 4240 -47 13 -131 N
ATOM 653 CA LEU A 87 26.685 186.694 21.439 1.00 36.44 C
ANISOU 653 CA LEU A 87 5096 4559 4191 -66 14 -134 C
ATOM 654 C LEU A 87 25.259 187.139 21.135 1.00 41.00 C
ANISOU 654 C LEU A 87 5697 5102 4781 -59 18 -141 C
ATOM 655 O LEU A 87 25.035 188.331 20.902 1.00 41.14 O
ANISOU 655 O LEU A 87 5728 5095 4807 -72 15 -148 O
ATOM 656 CB LEU A 87 27.396 186.196 20.164 1.00 36.03 C
ANISOU 656 CB LEU A 87 5030 4517 4141 -61 25 -118 C
ATOM 657 CG LEU A 87 28.877 185.777 20.332 1.00 40.17 C
ANISOU 657 CG LEU A 87 5519 5080 4662 -63 25 -109 C
ATOM 658 CD1 LEU A 87 29.455 185.216 19.029 1.00 39.73 C
ANISOU 658 CD1 LEU A 87 5454 5035 4608 -51 47 -96 C
ATOM 659 CD2 LEU A 87 29.746 186.924 20.900 1.00 41.22 C
ANISOU 659 CD2 LEU A 87 5634 5226 4802 -100 11 -118 C
ATOM 660 N THR A 88 24.295 186.195 21.185 1.00 37.04 N
ANISOU 660 N THR A 88 5195 4594 4284 -38 25 -140 N
ATOM 661 CA THR A 88 22.871 186.459 20.965 1.00 36.36 C
ANISOU 661 CA THR A 88 5116 4481 4218 -28 26 -148 C
ATOM 662 C THR A 88 22.322 187.297 22.138 1.00 38.62 C
ANISOU 662 C THR A 88 5409 4758 4505 -29 34 -165 C
ATOM 663 O THR A 88 21.585 188.254 21.899 1.00 38.43 O
ANISOU 663 O THR A 88 5393 4709 4498 -25 32 -174 O
ATOM 664 CB THR A 88 22.100 185.138 20.777 1.00 47.48 C
ANISOU 664 CB THR A 88 6514 5886 5639 -14 32 -144 C
ATOM 665 OG1 THR A 88 22.786 184.320 19.833 1.00 51.36 O
ANISOU 665 OG1 THR A 88 7007 6385 6123 -11 27 -136 O
ATOM 666 CG2 THR A 88 20.674 185.349 20.295 1.00 46.08 C
ANISOU 666 CG2 THR A 88 6331 5688 5491 -7 26 -153 C
ATOM 667 N GLN A 89 22.711 186.962 23.393 1.00 33.28 N
ANISOU 667 N GLN A 89 4736 4103 3807 -30 43 -168 N
ATOM 668 CA GLN A 89 22.251 187.683 24.580 1.00 32.61 C
ANISOU 668 CA GLN A 89 4666 4014 3710 -29 54 -189 C
ATOM 669 C GLN A 89 22.829 189.102 24.633 1.00 37.85 C
ANISOU 669 C GLN A 89 5346 4664 4371 -47 38 -210 C
ATOM 670 O GLN A 89 22.146 190.024 25.086 1.00 37.03 O
ANISOU 670 O GLN A 89 5260 4537 4274 -41 48 -233 O
ATOM 671 CB GLN A 89 22.582 186.912 25.864 1.00 33.57 C
ANISOU 671 CB GLN A 89 4795 4165 3795 -23 64 -185 C
ATOM 672 CG GLN A 89 21.638 187.252 27.021 1.00 39.30 C
ANISOU 672 CG GLN A 89 5538 4888 4506 -11 92 -202 C
ATOM 673 CD GLN A 89 20.190 186.910 26.739 1.00 52.96 C
ANISOU 673 CD GLN A 89 7250 6598 6272 3 123 -197 C
ATOM 674 OE1 GLN A 89 19.863 185.871 26.157 1.00 49.22 O
ANISOU 674 OE1 GLN A 89 6756 6122 5822 4 128 -175 O
ATOM 675 NE2 GLN A 89 19.285 187.768 27.171 1.00 43.79 N
ANISOU 675 NE2 GLN A 89 6095 5423 5121 15 145 -221 N
ATOM 676 N SER A 90 24.074 189.277 24.155 1.00 35.82 N
ANISOU 676 N SER A 90 5082 4417 4110 -69 19 -203 N
ATOM 677 CA SER A 90 24.729 190.576 24.068 1.00 36.63 C
ANISOU 677 CA SER A 90 5198 4502 4220 -98 5 -218 C
ATOM 678 C SER A 90 24.024 191.444 23.028 1.00 42.96 C
ANISOU 678 C SER A 90 6013 5257 5052 -94 10 -213 C
ATOM 679 O SER A 90 23.983 192.663 23.184 1.00 44.66 O
ANISOU 679 O SER A 90 6252 5437 5280 -106 7 -230 O
ATOM 680 CB SER A 90 26.200 190.410 23.708 1.00 40.02 C
ANISOU 680 CB SER A 90 5603 4957 4646 -125 -11 -206 C
ATOM 681 OG SER A 90 26.822 191.678 23.589 1.00 50.11 O
ANISOU 681 OG SER A 90 6889 6211 5939 -161 -21 -219 O
ATOM 682 N SER A 91 23.451 190.811 21.986 1.00 38.63 N
ANISOU 682 N SER A 91 5454 4708 4514 -74 14 -189 N
ATOM 683 CA SER A 91 22.733 191.504 20.925 1.00 38.83 C
ANISOU 683 CA SER A 91 5494 4697 4562 -63 10 -178 C
ATOM 684 C SER A 91 21.371 192.015 21.409 1.00 45.57 C
ANISOU 684 C SER A 91 6355 5524 5436 -34 16 -196 C
ATOM 685 O SER A 91 21.020 193.150 21.077 1.00 45.95 O
ANISOU 685 O SER A 91 6425 5531 5504 -27 11 -198 O
ATOM 686 CB SER A 91 22.561 190.601 19.707 1.00 40.88 C
ANISOU 686 CB SER A 91 5742 4971 4818 -49 5 -153 C
ATOM 687 OG SER A 91 23.816 190.368 19.088 1.00 46.30 O
ANISOU 687 OG SER A 91 6426 5677 5489 -71 8 -136 O
ATOM 688 N ILE A 92 20.621 191.209 22.210 1.00 42.97 N
ANISOU 688 N ILE A 92 6007 5214 5105 -16 30 -207 N
ATOM 689 CA ILE A 92 19.302 191.619 22.710 1.00 43.85 C
ANISOU 689 CA ILE A 92 6114 5307 5240 14 46 -225 C
ATOM 690 C ILE A 92 19.450 192.763 23.733 1.00 48.77 C
ANISOU 690 C ILE A 92 6768 5907 5857 12 57 -257 C
ATOM 691 O ILE A 92 18.574 193.624 23.780 1.00 49.41 O
ANISOU 691 O ILE A 92 6856 5953 5964 38 65 -272 O
ATOM 692 CB ILE A 92 18.389 190.465 23.254 1.00 47.16 C
ANISOU 692 CB ILE A 92 6501 5752 5665 29 68 -226 C
ATOM 693 CG1 ILE A 92 18.854 189.915 24.598 1.00 48.16 C
ANISOU 693 CG1 ILE A 92 6637 5907 5755 19 92 -235 C
ATOM 694 CG2 ILE A 92 18.192 189.332 22.241 1.00 46.93 C
ANISOU 694 CG2 ILE A 92 6446 5737 5648 27 53 -203 C
ATOM 695 CD1 ILE A 92 18.192 190.569 25.816 1.00 60.37 C
ANISOU 695 CD1 ILE A 92 8196 7446 7295 36 124 -264 C
ATOM 696 N PHE A 93 20.530 192.769 24.546 1.00 44.89 N
ANISOU 696 N PHE A 93 6293 5433 5330 -16 55 -271 N
ATOM 697 CA PHE A 93 20.758 193.845 25.513 1.00 45.35 C
ANISOU 697 CA PHE A 93 6385 5468 5377 -24 59 -310 C
ATOM 698 C PHE A 93 21.086 195.145 24.768 1.00 47.25 C
ANISOU 698 C PHE A 93 6652 5654 5647 -38 42 -311 C
ATOM 699 O PHE A 93 20.589 196.210 25.146 1.00 46.69 O
ANISOU 699 O PHE A 93 6611 5538 5592 -24 51 -340 O
ATOM 700 CB PHE A 93 21.879 193.498 26.519 1.00 47.70 C
ANISOU 700 CB PHE A 93 6691 5803 5628 -52 48 -326 C
ATOM 701 CG PHE A 93 21.531 192.503 27.603 1.00 49.95 C
ANISOU 701 CG PHE A 93 6973 6132 5875 -34 69 -328 C
ATOM 702 CD1 PHE A 93 20.321 192.584 28.288 1.00 53.83 C
ANISOU 702 CD1 PHE A 93 7473 6617 6364 -1 107 -346 C
ATOM 703 CD2 PHE A 93 22.443 191.526 27.991 1.00 52.35 C
ANISOU 703 CD2 PHE A 93 7266 6482 6142 -48 54 -312 C
ATOM 704 CE1 PHE A 93 20.007 191.668 29.300 1.00 55.04 C
ANISOU 704 CE1 PHE A 93 7627 6809 6478 13 135 -342 C
ATOM 705 CE2 PHE A 93 22.130 190.614 29.005 1.00 55.29 C
ANISOU 705 CE2 PHE A 93 7644 6890 6475 -29 75 -307 C
ATOM 706 CZ PHE A 93 20.914 190.691 29.653 1.00 53.74 C
ANISOU 706 CZ PHE A 93 7459 6685 6273 -2 118 -320 C
ATOM 707 N SER A 94 21.894 195.040 23.690 1.00 41.80 N
ANISOU 707 N SER A 94 5952 4966 4964 -65 24 -278 N
ATOM 708 CA SER A 94 22.273 196.175 22.858 1.00 41.29 C
ANISOU 708 CA SER A 94 5913 4849 4925 -83 14 -266 C
ATOM 709 C SER A 94 21.037 196.788 22.198 1.00 44.41 C
ANISOU 709 C SER A 94 6323 5198 5353 -39 18 -255 C
ATOM 710 O SER A 94 20.870 198.003 22.260 1.00 45.12 O
ANISOU 710 O SER A 94 6449 5228 5467 -35 19 -268 O
ATOM 711 CB SER A 94 23.306 195.767 21.813 1.00 43.29 C
ANISOU 711 CB SER A 94 6152 5124 5174 -115 5 -228 C
ATOM 712 OG SER A 94 24.619 195.976 22.309 1.00 49.30 O
ANISOU 712 OG SER A 94 6908 5897 5926 -165 -2 -242 O
ATOM 713 N LEU A 95 20.142 195.943 21.645 1.00 39.44 N
ANISOU 713 N LEU A 95 5664 4595 4727 -4 17 -234 N
ATOM 714 CA LEU A 95 18.900 196.370 20.990 1.00 38.93 C
ANISOU 714 CA LEU A 95 5598 4499 4693 44 11 -222 C
ATOM 715 C LEU A 95 17.949 197.030 21.981 1.00 43.21 C
ANISOU 715 C LEU A 95 6146 5013 5259 80 31 -260 C
ATOM 716 O LEU A 95 17.336 198.037 21.632 1.00 42.82 O
ANISOU 716 O LEU A 95 6117 4910 5242 113 26 -257 O
ATOM 717 CB LEU A 95 18.197 195.195 20.282 1.00 38.17 C
ANISOU 717 CB LEU A 95 5460 4445 4597 65 -1 -200 C
ATOM 718 CG LEU A 95 18.882 194.660 19.029 1.00 41.53 C
ANISOU 718 CG LEU A 95 5889 4890 5001 46 -21 -163 C
ATOM 719 CD1 LEU A 95 18.535 193.213 18.790 1.00 41.17 C
ANISOU 719 CD1 LEU A 95 5805 4893 4945 51 -27 -160 C
ATOM 720 CD2 LEU A 95 18.538 195.478 17.836 1.00 43.19 C
ANISOU 720 CD2 LEU A 95 6127 5063 5221 68 -44 -132 C
ATOM 721 N LEU A 96 17.860 196.491 23.219 1.00 40.50 N
ANISOU 721 N LEU A 96 5789 4703 4896 77 56 -293 N
ATOM 722 CA LEU A 96 17.016 197.020 24.296 1.00 41.28 C
ANISOU 722 CA LEU A 96 5894 4784 5006 112 87 -334 C
ATOM 723 C LEU A 96 17.542 198.382 24.802 1.00 46.48 C
ANISOU 723 C LEU A 96 6611 5383 5665 101 88 -368 C
ATOM 724 O LEU A 96 16.741 199.257 25.147 1.00 47.45 O
ANISOU 724 O LEU A 96 6751 5461 5815 142 106 -395 O
ATOM 725 CB LEU A 96 16.923 195.998 25.451 1.00 41.30 C
ANISOU 725 CB LEU A 96 5876 4843 4973 107 116 -353 C
ATOM 726 CG LEU A 96 16.073 196.332 26.713 1.00 46.67 C
ANISOU 726 CG LEU A 96 6564 5521 5649 142 162 -396 C
ATOM 727 CD1 LEU A 96 14.629 196.758 26.361 1.00 47.29 C
ANISOU 727 CD1 LEU A 96 6610 5573 5784 200 181 -396 C
ATOM 728 CD2 LEU A 96 16.042 195.145 27.663 1.00 47.59 C
ANISOU 728 CD2 LEU A 96 6662 5697 5723 133 193 -396 C
ATOM 729 N ALA A 97 18.871 198.567 24.833 1.00 42.23 N
ANISOU 729 N ALA A 97 6099 4843 5104 45 69 -370 N
ATOM 730 CA ALA A 97 19.473 199.827 25.279 1.00 41.85 C
ANISOU 730 CA ALA A 97 6104 4734 5062 21 64 -406 C
ATOM 731 C ALA A 97 19.227 200.948 24.259 1.00 44.93 C
ANISOU 731 C ALA A 97 6525 5046 5502 35 55 -382 C
ATOM 732 O ALA A 97 18.939 202.072 24.663 1.00 44.72 O
ANISOU 732 O ALA A 97 6541 4950 5498 52 64 -416 O
ATOM 733 CB ALA A 97 20.952 199.645 25.520 1.00 42.30 C
ANISOU 733 CB ALA A 97 6166 4816 5089 -47 43 -411 C
ATOM 734 N ILE A 98 19.293 200.629 22.943 1.00 40.32 N
ANISOU 734 N ILE A 98 5922 4469 4929 34 37 -323 N
ATOM 735 CA ILE A 98 19.022 201.569 21.849 1.00 39.49 C
ANISOU 735 CA ILE A 98 5848 4296 4860 54 26 -286 C
ATOM 736 C ILE A 98 17.559 202.051 21.940 1.00 43.07 C
ANISOU 736 C ILE A 98 6301 4715 5350 132 34 -296 C
ATOM 737 O ILE A 98 17.315 203.258 21.847 1.00 44.45 O
ANISOU 737 O ILE A 98 6522 4807 5559 155 35 -302 O
ATOM 738 CB ILE A 98 19.354 200.932 20.477 1.00 41.91 C
ANISOU 738 CB ILE A 98 6136 4635 5154 41 7 -222 C
ATOM 739 CG1 ILE A 98 20.877 200.829 20.298 1.00 41.93 C
ANISOU 739 CG1 ILE A 98 6145 4651 5134 -34 6 -209 C
ATOM 740 CG2 ILE A 98 18.725 201.721 19.312 1.00 43.90 C
ANISOU 740 CG2 ILE A 98 6417 4828 5433 82 -8 -176 C
ATOM 741 CD1 ILE A 98 21.364 199.727 19.340 1.00 46.60 C
ANISOU 741 CD1 ILE A 98 6704 5307 5696 -49 -1 -166 C
ATOM 742 N ALA A 99 16.607 201.119 22.163 1.00 37.48 N
ANISOU 742 N ALA A 99 5538 4065 4638 172 42 -301 N
ATOM 743 CA ALA A 99 15.180 201.426 22.285 1.00 37.18 C
ANISOU 743 CA ALA A 99 5478 4009 4640 248 52 -313 C
ATOM 744 C ALA A 99 14.895 202.369 23.477 1.00 41.93 C
ANISOU 744 C ALA A 99 6115 4560 5256 272 87 -373 C
ATOM 745 O ALA A 99 14.157 203.335 23.294 1.00 42.24 O
ANISOU 745 O ALA A 99 6174 4535 5340 328 90 -376 O
ATOM 746 CB ALA A 99 14.375 200.142 22.419 1.00 37.33 C
ANISOU 746 CB ALA A 99 5424 4107 4654 267 60 -310 C
ATOM 747 N ILE A 100 15.499 202.114 24.675 1.00 38.31 N
ANISOU 747 N ILE A 100 5670 4128 4757 234 111 -421 N
ATOM 748 CA ILE A 100 15.321 202.945 25.887 1.00 38.50 C
ANISOU 748 CA ILE A 100 5738 4111 4780 253 144 -488 C
ATOM 749 C ILE A 100 15.928 204.351 25.637 1.00 43.43 C
ANISOU 749 C ILE A 100 6436 4634 5431 236 128 -500 C
ATOM 750 O ILE A 100 15.297 205.358 25.969 1.00 43.75 O
ANISOU 750 O ILE A 100 6513 4605 5506 285 148 -535 O
ATOM 751 CB ILE A 100 15.901 202.250 27.167 1.00 41.07 C
ANISOU 751 CB ILE A 100 6066 4498 5041 214 164 -532 C
ATOM 752 CG1 ILE A 100 15.130 200.944 27.489 1.00 40.85 C
ANISOU 752 CG1 ILE A 100 5971 4554 4994 238 192 -518 C
ATOM 753 CG2 ILE A 100 15.895 203.189 28.387 1.00 41.97 C
ANISOU 753 CG2 ILE A 100 6241 4566 5140 226 192 -608 C
ATOM 754 CD1 ILE A 100 15.826 199.960 28.494 1.00 44.49 C
ANISOU 754 CD1 ILE A 100 6432 5087 5384 195 203 -535 C
ATOM 755 N ASP A 101 17.129 204.399 25.018 1.00 39.56 N
ANISOU 755 N ASP A 101 5966 4135 4931 166 97 -469 N
ATOM 756 CA ASP A 101 17.856 205.615 24.640 1.00 39.60 C
ANISOU 756 CA ASP A 101 6035 4045 4965 131 82 -468 C
ATOM 757 C ASP A 101 16.981 206.527 23.758 1.00 44.22 C
ANISOU 757 C ASP A 101 6646 4549 5608 196 80 -432 C
ATOM 758 O ASP A 101 16.910 207.732 24.018 1.00 44.87 O
ANISOU 758 O ASP A 101 6790 4533 5726 210 88 -462 O
ATOM 759 CB ASP A 101 19.151 205.232 23.900 1.00 40.65 C
ANISOU 759 CB ASP A 101 6160 4204 5080 50 56 -422 C
ATOM 760 CG ASP A 101 19.958 206.399 23.383 1.00 48.85 C
ANISOU 760 CG ASP A 101 7258 5150 6155 2 46 -408 C
ATOM 761 OD1 ASP A 101 20.825 206.892 24.130 1.00 49.97 O
ANISOU 761 OD1 ASP A 101 7430 5263 6293 -57 43 -457 O
ATOM 762 OD2 ASP A 101 19.746 206.795 22.218 1.00 52.40 O
ANISOU 762 OD2 ASP A 101 7723 5555 6632 21 40 -345 O
ATOM 763 N ARG A 102 16.310 205.948 22.731 1.00 39.98 N
ANISOU 763 N ARG A 102 6063 4049 5080 237 64 -370 N
ATOM 764 CA ARG A 102 15.429 206.704 21.834 1.00 40.29 C
ANISOU 764 CA ARG A 102 6119 4023 5167 308 52 -328 C
ATOM 765 C ARG A 102 14.157 207.167 22.562 1.00 45.23 C
ANISOU 765 C ARG A 102 6735 4620 5830 396 77 -374 C
ATOM 766 O ARG A 102 13.674 208.263 22.285 1.00 45.61 O
ANISOU 766 O ARG A 102 6826 4576 5926 450 76 -368 O
ATOM 767 CB ARG A 102 15.088 205.915 20.554 1.00 38.31 C
ANISOU 767 CB ARG A 102 5821 3828 4906 326 19 -256 C
ATOM 768 CG ARG A 102 16.282 205.683 19.609 1.00 46.04 C
ANISOU 768 CG ARG A 102 6822 4819 5853 253 0 -201 C
ATOM 769 CD ARG A 102 16.954 206.964 19.105 1.00 50.68 C
ANISOU 769 CD ARG A 102 7490 5301 6465 227 -1 -172 C
ATOM 770 NE ARG A 102 17.872 207.540 20.093 1.00 53.37 N
ANISOU 770 NE ARG A 102 7869 5597 6811 162 22 -228 N
ATOM 771 CZ ARG A 102 18.197 208.828 20.164 1.00 64.95 C
ANISOU 771 CZ ARG A 102 9408 6951 8317 147 30 -235 C
ATOM 772 NH1 ARG A 102 17.683 209.700 19.304 1.00 50.43 N
ANISOU 772 NH1 ARG A 102 7617 5030 6516 197 22 -182 N
ATOM 773 NH2 ARG A 102 19.039 209.256 21.096 1.00 49.15 N
ANISOU 773 NH2 ARG A 102 7436 4918 6321 82 43 -294 N
ATOM 774 N TYR A 103 13.662 206.374 23.528 1.00 42.05 N
ANISOU 774 N TYR A 103 6280 4291 5406 410 106 -421 N
ATOM 775 CA TYR A 103 12.500 206.748 24.329 1.00 43.12 C
ANISOU 775 CA TYR A 103 6401 4410 5573 491 145 -470 C
ATOM 776 C TYR A 103 12.829 207.931 25.266 1.00 48.90 C
ANISOU 776 C TYR A 103 7215 5052 6314 491 173 -538 C
ATOM 777 O TYR A 103 11.972 208.797 25.454 1.00 49.71 O
ANISOU 777 O TYR A 103 7337 5088 6465 569 194 -563 O
ATOM 778 CB TYR A 103 11.962 205.549 25.117 1.00 44.11 C
ANISOU 778 CB TYR A 103 6452 4639 5668 498 177 -495 C
ATOM 779 CG TYR A 103 10.759 205.880 25.970 1.00 46.73 C
ANISOU 779 CG TYR A 103 6760 4962 6031 580 229 -545 C
ATOM 780 CD1 TYR A 103 9.538 206.213 25.389 1.00 49.43 C
ANISOU 780 CD1 TYR A 103 7056 5284 6439 668 226 -522 C
ATOM 781 CD2 TYR A 103 10.845 205.880 27.359 1.00 47.61 C
ANISOU 781 CD2 TYR A 103 6897 5089 6104 573 282 -616 C
ATOM 782 CE1 TYR A 103 8.432 206.541 26.171 1.00 51.70 C
ANISOU 782 CE1 TYR A 103 7315 5566 6763 748 281 -568 C
ATOM 783 CE2 TYR A 103 9.745 206.198 28.150 1.00 49.44 C
ANISOU 783 CE2 TYR A 103 7110 5316 6362 652 341 -663 C
ATOM 784 CZ TYR A 103 8.538 206.524 27.553 1.00 59.38 C
ANISOU 784 CZ TYR A 103 8314 6554 7695 739 343 -639 C
ATOM 785 OH TYR A 103 7.449 206.840 28.330 1.00 62.51 O
ANISOU 785 OH TYR A 103 8681 6947 8121 821 408 -686 O
ATOM 786 N ILE A 104 14.069 207.993 25.807 1.00 45.58 N
ANISOU 786 N ILE A 104 6844 4626 5851 405 169 -570 N
ATOM 787 CA ILE A 104 14.521 209.089 26.682 1.00 46.12 C
ANISOU 787 CA ILE A 104 6996 4607 5922 389 185 -643 C
ATOM 788 C ILE A 104 14.678 210.369 25.841 1.00 51.61 C
ANISOU 788 C ILE A 104 7757 5175 6679 398 165 -613 C
ATOM 789 O ILE A 104 14.332 211.457 26.313 1.00 52.25 O
ANISOU 789 O ILE A 104 7899 5158 6796 440 186 -663 O
ATOM 790 CB ILE A 104 15.827 208.716 27.459 1.00 48.53 C
ANISOU 790 CB ILE A 104 7323 4952 6165 290 174 -684 C
ATOM 791 CG1 ILE A 104 15.548 207.622 28.522 1.00 47.83 C
ANISOU 791 CG1 ILE A 104 7189 4973 6012 297 203 -722 C
ATOM 792 CG2 ILE A 104 16.474 209.949 28.120 1.00 50.36 C
ANISOU 792 CG2 ILE A 104 7647 5082 6407 255 174 -755 C
ATOM 793 CD1 ILE A 104 16.799 206.862 29.066 1.00 50.22 C
ANISOU 793 CD1 ILE A 104 7488 5347 6245 207 179 -737 C
ATOM 794 N ALA A 105 15.167 210.224 24.591 1.00 48.63 N
ANISOU 794 N ALA A 105 7371 4795 6310 362 128 -530 N
ATOM 795 CA ALA A 105 15.376 211.329 23.645 1.00 48.76 C
ANISOU 795 CA ALA A 105 7451 4696 6378 364 110 -482 C
ATOM 796 C ALA A 105 14.058 211.969 23.184 1.00 53.22 C
ANISOU 796 C ALA A 105 8020 5200 7001 482 114 -457 C
ATOM 797 O ALA A 105 14.046 213.164 22.894 1.00 54.56 O
ANISOU 797 O ALA A 105 8263 5246 7220 504 113 -448 O
ATOM 798 CB ALA A 105 16.163 210.847 22.441 1.00 48.71 C
ANISOU 798 CB ALA A 105 7430 4725 6354 303 78 -396 C
ATOM 799 N ILE A 106 12.955 211.203 23.131 1.00 48.88 N
ANISOU 799 N ILE A 106 7389 4733 6450 555 117 -447 N
ATOM 800 CA ILE A 106 11.664 211.757 22.712 1.00 49.36 C
ANISOU 800 CA ILE A 106 7436 4747 6570 672 116 -424 C
ATOM 801 C ILE A 106 10.828 212.265 23.933 1.00 54.31 C
ANISOU 801 C ILE A 106 8067 5341 7226 747 167 -512 C
ATOM 802 O ILE A 106 10.134 213.269 23.794 1.00 54.71 O
ANISOU 802 O ILE A 106 8152 5297 7338 832 174 -514 O
ATOM 803 CB ILE A 106 10.870 210.766 21.804 1.00 51.48 C
ANISOU 803 CB ILE A 106 7611 5114 6836 716 82 -359 C
ATOM 804 CG1 ILE A 106 9.754 211.489 21.026 1.00 52.80 C
ANISOU 804 CG1 ILE A 106 7773 5221 7067 829 58 -314 C
ATOM 805 CG2 ILE A 106 10.348 209.521 22.545 1.00 50.46 C
ANISOU 805 CG2 ILE A 106 7386 5110 6677 717 107 -398 C
ATOM 806 CD1 ILE A 106 9.831 211.316 19.573 1.00 60.93 C
ANISOU 806 CD1 ILE A 106 8801 6261 8087 830 -1 -218 C
ATOM 807 N ARG A 107 10.910 211.594 25.108 1.00 50.91 N
ANISOU 807 N ARG A 107 7608 4987 6750 718 206 -583 N
ATOM 808 CA ARG A 107 10.139 211.952 26.308 1.00 51.24 C
ANISOU 808 CA ARG A 107 7652 5013 6802 785 265 -668 C
ATOM 809 C ARG A 107 10.713 213.165 27.052 1.00 55.70 C
ANISOU 809 C ARG A 107 8330 5459 7375 769 285 -742 C
ATOM 810 O ARG A 107 9.943 214.038 27.468 1.00 56.84 O
ANISOU 810 O ARG A 107 8505 5525 7565 857 321 -787 O
ATOM 811 CB ARG A 107 10.029 210.759 27.275 1.00 49.95 C
ANISOU 811 CB ARG A 107 7425 4976 6577 759 302 -709 C
ATOM 812 N ILE A 108 12.045 213.206 27.255 1.00 50.94 N
ANISOU 812 N ILE A 108 7784 4842 6729 658 264 -759 N
ATOM 813 CA ILE A 108 12.706 214.296 27.988 1.00 51.04 C
ANISOU 813 CA ILE A 108 7903 4744 6746 623 275 -837 C
ATOM 814 C ILE A 108 13.985 214.744 27.239 1.00 54.11 C
ANISOU 814 C ILE A 108 8348 5066 7146 520 227 -793 C
ATOM 815 O ILE A 108 15.095 214.536 27.746 1.00 53.12 O
ANISOU 815 O ILE A 108 8243 4964 6975 418 213 -830 O
ATOM 816 CB ILE A 108 12.986 213.898 29.469 1.00 54.04 C
ANISOU 816 CB ILE A 108 8294 5186 7053 591 308 -937 C
ATOM 817 CG1 ILE A 108 13.333 212.397 29.615 1.00 53.16 C
ANISOU 817 CG1 ILE A 108 8100 5230 6867 534 298 -909 C
ATOM 818 CG2 ILE A 108 11.806 214.275 30.355 1.00 55.75 C
ANISOU 818 CG2 ILE A 108 8516 5384 7281 701 372 -1009 C
ATOM 819 CD1 ILE A 108 14.427 212.100 30.595 1.00 63.04 C
ANISOU 819 CD1 ILE A 108 9387 6523 8042 442 288 -972 C
ATOM 820 N PRO A 109 13.850 215.383 26.040 1.00 50.95 N
ANISOU 820 N PRO A 109 7971 4581 6807 546 204 -713 N
ATOM 821 CA PRO A 109 15.050 215.791 25.279 1.00 51.46 C
ANISOU 821 CA PRO A 109 8086 4584 6883 445 170 -662 C
ATOM 822 C PRO A 109 15.941 216.832 25.978 1.00 59.20 C
ANISOU 822 C PRO A 109 9164 5448 7882 373 175 -738 C
ATOM 823 O PRO A 109 17.152 216.852 25.742 1.00 58.94 O
ANISOU 823 O PRO A 109 9149 5406 7840 260 151 -721 O
ATOM 824 CB PRO A 109 14.469 216.365 23.983 1.00 53.18 C
ANISOU 824 CB PRO A 109 8321 4726 7160 513 154 -565 C
ATOM 825 CG PRO A 109 13.071 216.718 24.300 1.00 57.28 C
ANISOU 825 CG PRO A 109 8828 5218 7719 649 179 -594 C
ATOM 826 CD PRO A 109 12.616 215.705 25.291 1.00 52.07 C
ANISOU 826 CD PRO A 109 8090 4688 7007 666 206 -658 C
ATOM 827 N LEU A 110 15.356 217.681 26.843 1.00 58.37 N
ANISOU 827 N LEU A 110 9119 5255 7805 437 205 -824 N
ATOM 828 CA LEU A 110 16.087 218.718 27.574 1.00 59.84 C
ANISOU 828 CA LEU A 110 9405 5321 8012 375 208 -911 C
ATOM 829 C LEU A 110 16.902 218.134 28.749 1.00 64.00 C
ANISOU 829 C LEU A 110 9921 5935 8461 287 201 -1003 C
ATOM 830 O LEU A 110 17.746 218.833 29.311 1.00 63.85 O
ANISOU 830 O LEU A 110 9974 5837 8450 208 187 -1075 O
ATOM 831 CB LEU A 110 15.095 219.783 28.077 1.00 61.42 C
ANISOU 831 CB LEU A 110 9675 5398 8264 486 245 -976 C
ATOM 832 CG LEU A 110 15.052 221.122 27.321 1.00 67.55 C
ANISOU 832 CG LEU A 110 10544 5989 9135 511 242 -936 C
ATOM 833 CD1 LEU A 110 14.504 220.966 25.908 1.00 67.58 C
ANISOU 833 CD1 LEU A 110 10505 5998 9173 572 225 -800 C
ATOM 834 CD2 LEU A 110 14.189 222.106 28.050 1.00 71.80 C
ANISOU 834 CD2 LEU A 110 11154 6410 9718 616 281 -1023 C
ATOM 835 N ARG A 111 16.667 216.854 29.096 1.00 60.59 N
ANISOU 835 N ARG A 111 9400 5663 7957 299 205 -999 N
ATOM 836 CA ARG A 111 17.346 216.154 30.190 1.00 60.40 C
ANISOU 836 CA ARG A 111 9361 5739 7850 231 197 -1072 C
ATOM 837 C ARG A 111 18.221 214.987 29.683 1.00 64.09 C
ANISOU 837 C ARG A 111 9748 6331 8274 146 160 -1002 C
ATOM 838 O ARG A 111 18.962 214.404 30.478 1.00 63.18 O
ANISOU 838 O ARG A 111 9617 6295 8092 80 142 -1051 O
ATOM 839 CB ARG A 111 16.310 215.626 31.205 1.00 60.44 C
ANISOU 839 CB ARG A 111 9339 5824 7801 324 243 -1133 C
ATOM 840 CG ARG A 111 15.618 216.716 32.019 1.00 73.73 C
ANISOU 840 CG ARG A 111 11107 7398 9508 400 285 -1231 C
ATOM 841 CD ARG A 111 14.617 216.137 33.000 1.00 83.62 C
ANISOU 841 CD ARG A 111 12328 8742 10703 489 342 -1285 C
ATOM 842 N TYR A 112 18.137 214.660 28.369 1.00 60.94 N
ANISOU 842 N TYR A 112 9300 5946 7907 152 149 -890 N
ATOM 843 CA TYR A 112 18.838 213.550 27.702 1.00 59.85 C
ANISOU 843 CA TYR A 112 9086 5920 7735 88 121 -815 C
ATOM 844 C TYR A 112 20.371 213.611 27.834 1.00 64.90 C
ANISOU 844 C TYR A 112 9737 6559 8362 -43 86 -832 C
ATOM 845 O TYR A 112 20.983 212.578 28.119 1.00 63.93 O
ANISOU 845 O TYR A 112 9555 6553 8182 -91 68 -831 O
ATOM 846 CB TYR A 112 18.454 213.478 26.206 1.00 60.32 C
ANISOU 846 CB TYR A 112 9118 5966 7837 122 116 -700 C
ATOM 847 CG TYR A 112 19.190 212.405 25.429 1.00 60.73 C
ANISOU 847 CG TYR A 112 9101 6121 7854 60 93 -625 C
ATOM 848 CD1 TYR A 112 18.709 211.100 25.378 1.00 61.83 C
ANISOU 848 CD1 TYR A 112 9158 6390 7946 95 94 -599 C
ATOM 849 CD2 TYR A 112 20.369 212.693 24.746 1.00 61.25 C
ANISOU 849 CD2 TYR A 112 9183 6152 7938 -35 74 -582 C
ATOM 850 CE1 TYR A 112 19.391 210.104 24.676 1.00 61.45 C
ANISOU 850 CE1 TYR A 112 9052 6430 7865 42 75 -537 C
ATOM 851 CE2 TYR A 112 21.065 211.703 24.054 1.00 60.88 C
ANISOU 851 CE2 TYR A 112 9072 6201 7858 -87 59 -518 C
ATOM 852 CZ TYR A 112 20.569 210.411 24.016 1.00 65.56 C
ANISOU 852 CZ TYR A 112 9590 6919 8401 -46 58 -498 C
ATOM 853 OH TYR A 112 21.238 209.440 23.313 1.00 64.11 O
ANISOU 853 OH TYR A 112 9349 6823 8187 -91 46 -439 O
ATOM 854 N ASN A 113 20.985 214.778 27.570 1.00 63.01 N
ANISOU 854 N ASN A 113 9568 6191 8183 -99 77 -841 N
ATOM 855 CA ASN A 113 22.442 214.945 27.598 1.00 63.74 C
ANISOU 855 CA ASN A 113 9663 6273 8282 -229 44 -852 C
ATOM 856 C ASN A 113 23.044 214.751 28.996 1.00 68.43 C
ANISOU 856 C ASN A 113 10262 6917 8821 -281 20 -963 C
ATOM 857 O ASN A 113 24.146 214.209 29.107 1.00 68.14 O
ANISOU 857 O ASN A 113 10178 6952 8759 -371 -14 -962 O
ATOM 858 CB ASN A 113 22.850 216.309 27.036 1.00 67.58 C
ANISOU 858 CB ASN A 113 10228 6595 8854 -276 46 -838 C
ATOM 859 CG ASN A 113 22.610 216.459 25.549 1.00 93.43 C
ANISOU 859 CG ASN A 113 13498 9828 12173 -252 62 -714 C
ATOM 860 OD1 ASN A 113 22.755 215.514 24.758 1.00 83.24 O
ANISOU 860 OD1 ASN A 113 12138 8639 10852 -255 59 -633 O
ATOM 861 ND2 ASN A 113 22.268 217.670 25.129 1.00 88.98 N
ANISOU 861 ND2 ASN A 113 13019 9111 11680 -227 77 -698 N
ATOM 862 N GLY A 114 22.322 215.178 30.031 1.00 65.11 N
ANISOU 862 N GLY A 114 9898 6462 8381 -219 36 -1055 N
ATOM 863 CA GLY A 114 22.759 215.045 31.416 1.00 65.01 C
ANISOU 863 CA GLY A 114 9905 6495 8302 -254 13 -1166 C
ATOM 864 C GLY A 114 22.532 213.666 32.004 1.00 67.56 C
ANISOU 864 C GLY A 114 10159 6980 8530 -220 15 -1164 C
ATOM 865 O GLY A 114 23.227 213.276 32.945 1.00 67.60 O
ANISOU 865 O GLY A 114 10159 7055 8471 -271 -19 -1226 O
ATOM 866 N LEU A 115 21.554 212.921 31.462 1.00 62.66 N
ANISOU 866 N LEU A 115 9484 6420 7902 -134 52 -1091 N
ATOM 867 CA LEU A 115 21.174 211.590 31.935 1.00 61.49 C
ANISOU 867 CA LEU A 115 9272 6416 7675 -94 64 -1079 C
ATOM 868 C LEU A 115 21.933 210.488 31.173 1.00 63.26 C
ANISOU 868 C LEU A 115 9410 6739 7886 -150 35 -992 C
ATOM 869 O LEU A 115 22.531 209.618 31.808 1.00 61.32 O
ANISOU 869 O LEU A 115 9130 6595 7575 -185 11 -1008 O
ATOM 870 CB LEU A 115 19.640 211.425 31.792 1.00 61.57 C
ANISOU 870 CB LEU A 115 9267 6430 7695 26 121 -1055 C
ATOM 871 CG LEU A 115 18.986 210.066 32.101 1.00 65.84 C
ANISOU 871 CG LEU A 115 9736 7105 8174 77 147 -1027 C
ATOM 872 CD1 LEU A 115 18.980 209.780 33.572 1.00 66.71 C
ANISOU 872 CD1 LEU A 115 9876 7275 8197 85 161 -1113 C
ATOM 873 CD2 LEU A 115 17.542 210.058 31.658 1.00 68.31 C
ANISOU 873 CD2 LEU A 115 10023 7406 8527 183 197 -991 C
ATOM 874 N VAL A 116 21.921 210.541 29.824 1.00 59.66 N
ANISOU 874 N VAL A 116 8926 6253 7491 -153 37 -901 N
ATOM 875 CA VAL A 116 22.560 209.547 28.951 1.00 58.37 C
ANISOU 875 CA VAL A 116 8686 6174 7319 -195 18 -816 C
ATOM 876 C VAL A 116 23.933 210.075 28.479 1.00 62.51 C
ANISOU 876 C VAL A 116 9216 6653 7883 -303 -15 -803 C
ATOM 877 O VAL A 116 24.027 210.802 27.486 1.00 62.73 O
ANISOU 877 O VAL A 116 9266 6594 7973 -320 -7 -752 O
ATOM 878 CB VAL A 116 21.646 209.139 27.765 1.00 61.41 C
ANISOU 878 CB VAL A 116 9033 6568 7730 -127 43 -725 C
ATOM 879 CG1 VAL A 116 22.036 207.772 27.234 1.00 60.19 C
ANISOU 879 CG1 VAL A 116 8798 6531 7540 -146 31 -661 C
ATOM 880 CG2 VAL A 116 20.179 209.132 28.175 1.00 61.33 C
ANISOU 880 CG2 VAL A 116 9031 6557 7717 -20 80 -748 C
ATOM 881 N THR A 117 24.986 209.713 29.225 1.00 58.77 N
ANISOU 881 N THR A 117 8719 6239 7370 -375 -52 -848 N
ATOM 882 CA THR A 117 26.378 210.118 29.001 1.00 58.87 C
ANISOU 882 CA THR A 117 8721 6228 7418 -486 -88 -850 C
ATOM 883 C THR A 117 27.172 208.924 28.444 1.00 60.85 C
ANISOU 883 C THR A 117 8880 6594 7647 -521 -102 -782 C
ATOM 884 O THR A 117 26.774 207.776 28.641 1.00 59.87 O
ANISOU 884 O THR A 117 8712 6570 7465 -469 -97 -763 O
ATOM 885 CB THR A 117 26.956 210.664 30.333 1.00 69.81 C
ANISOU 885 CB THR A 117 10149 7595 8781 -538 -127 -963 C
ATOM 886 OG1 THR A 117 26.105 211.712 30.806 1.00 70.21 O
ANISOU 886 OG1 THR A 117 10290 7538 8849 -490 -105 -1027 O
ATOM 887 CG2 THR A 117 28.381 211.207 30.204 1.00 70.63 C
ANISOU 887 CG2 THR A 117 10238 7665 8934 -661 -169 -978 C
ATOM 888 N GLY A 118 28.269 209.217 27.742 1.00 56.81 N
ANISOU 888 N GLY A 118 8340 6061 7185 -608 -114 -746 N
ATOM 889 CA GLY A 118 29.166 208.227 27.155 1.00 55.51 C
ANISOU 889 CA GLY A 118 8088 5993 7011 -648 -123 -686 C
ATOM 890 C GLY A 118 29.794 207.287 28.168 1.00 59.20 C
ANISOU 890 C GLY A 118 8502 6574 7416 -663 -166 -730 C
ATOM 891 O GLY A 118 29.849 206.078 27.923 1.00 58.20 O
ANISOU 891 O GLY A 118 8315 6547 7251 -633 -163 -684 O
ATOM 892 N THR A 119 30.256 207.829 29.326 1.00 56.30 N
ANISOU 892 N THR A 119 8164 6191 7037 -708 -210 -823 N
ATOM 893 CA THR A 119 30.885 207.047 30.405 1.00 55.93 C
ANISOU 893 CA THR A 119 8077 6248 6924 -722 -263 -871 C
ATOM 894 C THR A 119 29.862 206.096 31.032 1.00 58.00 C
ANISOU 894 C THR A 119 8353 6584 7103 -623 -246 -874 C
ATOM 895 O THR A 119 30.200 204.949 31.339 1.00 57.62 O
ANISOU 895 O THR A 119 8249 6642 7001 -608 -266 -854 O
ATOM 896 CB THR A 119 31.544 207.944 31.464 1.00 69.67 C
ANISOU 896 CB THR A 119 9856 7948 8667 -791 -319 -974 C
ATOM 897 OG1 THR A 119 30.582 208.859 31.981 1.00 74.13 O
ANISOU 897 OG1 THR A 119 10520 8420 9227 -751 -299 -1037 O
ATOM 898 CG2 THR A 119 32.752 208.703 30.925 1.00 70.07 C
ANISOU 898 CG2 THR A 119 9872 7947 8805 -905 -342 -971 C
ATOM 899 N ARG A 120 28.607 206.558 31.181 1.00 53.14 N
ANISOU 899 N ARG A 120 7805 5907 6480 -555 -205 -892 N
ATOM 900 CA ARG A 120 27.505 205.746 31.701 1.00 51.54 C
ANISOU 900 CA ARG A 120 7611 5761 6209 -462 -175 -890 C
ATOM 901 C ARG A 120 27.118 204.674 30.685 1.00 53.93 C
ANISOU 901 C ARG A 120 7853 6120 6519 -420 -142 -794 C
ATOM 902 O ARG A 120 26.738 203.574 31.086 1.00 54.03 O
ANISOU 902 O ARG A 120 7839 6216 6473 -373 -134 -778 O
ATOM 903 CB ARG A 120 26.294 206.615 32.045 1.00 50.16 C
ANISOU 903 CB ARG A 120 7516 5501 6041 -401 -135 -936 C
ATOM 904 CG ARG A 120 26.497 207.440 33.294 1.00 56.45 C
ANISOU 904 CG ARG A 120 8384 6260 6806 -424 -162 -1045 C
ATOM 905 CD ARG A 120 25.384 208.441 33.481 1.00 58.62 C
ANISOU 905 CD ARG A 120 8738 6433 7103 -365 -118 -1090 C
ATOM 906 NE ARG A 120 25.647 209.302 34.631 1.00 58.89 N
ANISOU 906 NE ARG A 120 8848 6421 7107 -391 -145 -1203 N
ATOM 907 CZ ARG A 120 24.835 210.264 35.045 1.00 68.01 C
ANISOU 907 CZ ARG A 120 10084 7483 8273 -345 -112 -1268 C
ATOM 908 NH1 ARG A 120 25.153 210.998 36.102 1.00 56.34 N
ANISOU 908 NH1 ARG A 120 8680 5966 6761 -373 -141 -1378 N
ATOM 909 NH2 ARG A 120 23.699 210.507 34.402 1.00 50.09 N
ANISOU 909 NH2 ARG A 120 7823 5160 6049 -267 -52 -1226 N
ATOM 910 N ALA A 121 27.232 204.989 29.374 1.00 48.64 N
ANISOU 910 N ALA A 121 7164 5401 5915 -439 -124 -730 N
ATOM 911 CA ALA A 121 26.948 204.055 28.285 1.00 47.05 C
ANISOU 911 CA ALA A 121 6910 5247 5720 -405 -99 -643 C
ATOM 912 C ALA A 121 27.962 202.905 28.274 1.00 50.31 C
ANISOU 912 C ALA A 121 7252 5762 6104 -437 -125 -615 C
ATOM 913 O ALA A 121 27.548 201.753 28.169 1.00 48.46 O
ANISOU 913 O ALA A 121 6982 5596 5833 -389 -112 -579 O
ATOM 914 CB ALA A 121 26.962 204.776 26.951 1.00 47.61 C
ANISOU 914 CB ALA A 121 6991 5241 5858 -423 -78 -588 C
ATOM 915 N LYS A 122 29.278 203.220 28.418 1.00 48.03 N
ANISOU 915 N LYS A 122 6936 5479 5834 -517 -163 -635 N
ATOM 916 CA LYS A 122 30.382 202.243 28.457 1.00 47.86 C
ANISOU 916 CA LYS A 122 6839 5551 5794 -549 -192 -613 C
ATOM 917 C LYS A 122 30.239 201.273 29.647 1.00 50.15 C
ANISOU 917 C LYS A 122 7124 5927 6006 -507 -218 -644 C
ATOM 918 O LYS A 122 30.531 200.082 29.502 1.00 48.54 O
ANISOU 918 O LYS A 122 6866 5802 5775 -486 -221 -602 O
ATOM 919 CB LYS A 122 31.752 202.946 28.511 1.00 51.56 C
ANISOU 919 CB LYS A 122 7279 6004 6308 -645 -231 -639 C
ATOM 920 CG LYS A 122 32.266 203.385 27.147 1.00 65.52 C
ANISOU 920 CG LYS A 122 9020 7728 8148 -692 -199 -579 C
ATOM 921 N GLY A 123 29.777 201.794 30.785 1.00 46.49 N
ANISOU 921 N GLY A 123 6721 5442 5503 -493 -232 -714 N
ATOM 922 CA GLY A 123 29.520 201.016 31.992 1.00 46.28 C
ANISOU 922 CA GLY A 123 6707 5487 5391 -451 -249 -745 C
ATOM 923 C GLY A 123 28.401 200.007 31.797 1.00 50.19 C
ANISOU 923 C GLY A 123 7200 6015 5856 -371 -199 -695 C
ATOM 924 O GLY A 123 28.541 198.854 32.214 1.00 49.81 O
ANISOU 924 O GLY A 123 7123 6046 5756 -345 -208 -671 O
ATOM 925 N ILE A 124 27.292 200.428 31.130 1.00 46.08 N
ANISOU 925 N ILE A 124 6705 5432 5372 -334 -148 -676 N
ATOM 926 CA ILE A 124 26.130 199.580 30.815 1.00 44.89 C
ANISOU 926 CA ILE A 124 6544 5303 5208 -265 -100 -631 C
ATOM 927 C ILE A 124 26.561 198.428 29.887 1.00 47.36 C
ANISOU 927 C ILE A 124 6791 5671 5534 -266 -101 -558 C
ATOM 928 O ILE A 124 26.208 197.285 30.168 1.00 46.88 O
ANISOU 928 O ILE A 124 6710 5667 5434 -228 -88 -533 O
ATOM 929 CB ILE A 124 24.950 200.413 30.218 1.00 47.74 C
ANISOU 929 CB ILE A 124 6939 5583 5618 -227 -57 -629 C
ATOM 930 CG1 ILE A 124 24.236 201.217 31.330 1.00 48.85 C
ANISOU 930 CG1 ILE A 124 7145 5685 5732 -198 -41 -702 C
ATOM 931 CG2 ILE A 124 23.947 199.530 29.446 1.00 46.68 C
ANISOU 931 CG2 ILE A 124 6769 5471 5495 -172 -19 -568 C
ATOM 932 CD1 ILE A 124 23.496 202.450 30.867 1.00 56.86 C
ANISOU 932 CD1 ILE A 124 8202 6599 6805 -178 -15 -719 C
ATOM 933 N ILE A 125 27.351 198.727 28.826 1.00 43.64 N
ANISOU 933 N ILE A 125 6288 5178 5114 -311 -111 -526 N
ATOM 934 CA ILE A 125 27.862 197.762 27.834 1.00 43.03 C
ANISOU 934 CA ILE A 125 6152 5145 5051 -314 -108 -463 C
ATOM 935 C ILE A 125 28.761 196.693 28.513 1.00 46.77 C
ANISOU 935 C ILE A 125 6585 5704 5482 -320 -140 -461 C
ATOM 936 O ILE A 125 28.612 195.509 28.212 1.00 45.61 O
ANISOU 936 O ILE A 125 6408 5604 5320 -286 -127 -419 O
ATOM 937 CB ILE A 125 28.591 198.486 26.654 1.00 46.46 C
ANISOU 937 CB ILE A 125 6570 5537 5545 -365 -106 -435 C
ATOM 938 CG1 ILE A 125 27.588 199.347 25.844 1.00 46.85 C
ANISOU 938 CG1 ILE A 125 6663 5506 5631 -343 -74 -419 C
ATOM 939 CG2 ILE A 125 29.317 197.483 25.718 1.00 46.85 C
ANISOU 939 CG2 ILE A 125 6558 5641 5601 -371 -100 -377 C
ATOM 940 CD1 ILE A 125 28.193 200.458 24.951 1.00 53.79 C
ANISOU 940 CD1 ILE A 125 7555 6317 6566 -397 -69 -401 C
ATOM 941 N ALA A 126 29.666 197.112 29.425 1.00 44.44 N
ANISOU 941 N ALA A 126 6290 5426 5169 -361 -186 -508 N
ATOM 942 CA ALA A 126 30.570 196.220 30.163 1.00 44.35 C
ANISOU 942 CA ALA A 126 6240 5495 5116 -363 -228 -509 C
ATOM 943 C ALA A 126 29.782 195.243 31.047 1.00 48.31 C
ANISOU 943 C ALA A 126 6768 6039 5547 -301 -216 -504 C
ATOM 944 O ALA A 126 30.036 194.037 30.979 1.00 48.31 O
ANISOU 944 O ALA A 126 6732 6093 5528 -274 -218 -462 O
ATOM 945 CB ALA A 126 31.547 197.029 31.006 1.00 45.88 C
ANISOU 945 CB ALA A 126 6436 5693 5304 -420 -287 -569 C
ATOM 946 N ILE A 127 28.796 195.754 31.826 1.00 44.25 N
ANISOU 946 N ILE A 127 6318 5496 5000 -276 -197 -545 N
ATOM 947 CA ILE A 127 27.919 194.958 32.698 1.00 43.82 C
ANISOU 947 CA ILE A 127 6295 5475 4880 -220 -171 -541 C
ATOM 948 C ILE A 127 27.096 193.960 31.834 1.00 47.61 C
ANISOU 948 C ILE A 127 6748 5957 5385 -179 -121 -477 C
ATOM 949 O ILE A 127 27.008 192.783 32.190 1.00 46.89 O
ANISOU 949 O ILE A 127 6647 5914 5257 -148 -114 -443 O
ATOM 950 CB ILE A 127 27.019 195.885 33.580 1.00 47.15 C
ANISOU 950 CB ILE A 127 6788 5857 5270 -204 -149 -602 C
ATOM 951 CG1 ILE A 127 27.857 196.575 34.687 1.00 48.36 C
ANISOU 951 CG1 ILE A 127 6976 6025 5375 -238 -208 -671 C
ATOM 952 CG2 ILE A 127 25.824 195.138 34.196 1.00 47.31 C
ANISOU 952 CG2 ILE A 127 6835 5899 5241 -143 -96 -587 C
ATOM 953 CD1 ILE A 127 27.262 197.887 35.261 1.00 53.12 C
ANISOU 953 CD1 ILE A 127 7650 6564 5971 -241 -194 -747 C
ATOM 954 N CYS A 128 26.547 194.424 30.690 1.00 44.44 N
ANISOU 954 N CYS A 128 6337 5503 5046 -181 -92 -460 N
ATOM 955 CA CYS A 128 25.743 193.604 29.774 1.00 43.62 C
ANISOU 955 CA CYS A 128 6208 5396 4969 -148 -53 -408 C
ATOM 956 C CYS A 128 26.554 192.460 29.139 1.00 45.33 C
ANISOU 956 C CYS A 128 6375 5656 5192 -152 -67 -360 C
ATOM 957 O CYS A 128 26.001 191.366 28.993 1.00 43.93 O
ANISOU 957 O CYS A 128 6186 5498 5007 -120 -44 -326 O
ATOM 958 CB CYS A 128 25.073 194.467 28.712 1.00 44.05 C
ANISOU 958 CB CYS A 128 6268 5387 5081 -148 -31 -404 C
ATOM 959 SG CYS A 128 23.704 195.470 29.348 1.00 48.63 S
ANISOU 959 SG CYS A 128 6899 5914 5663 -115 3 -449 S
ATOM 960 N TRP A 129 27.853 192.691 28.799 1.00 41.02 N
ANISOU 960 N TRP A 129 5798 5125 4662 -192 -103 -359 N
ATOM 961 CA TRP A 129 28.746 191.657 28.250 1.00 40.20 C
ANISOU 961 CA TRP A 129 5643 5064 4566 -191 -115 -318 C
ATOM 962 C TRP A 129 29.052 190.587 29.314 1.00 44.40 C
ANISOU 962 C TRP A 129 6173 5653 5045 -164 -134 -311 C
ATOM 963 O TRP A 129 29.096 189.404 28.977 1.00 43.36 O
ANISOU 963 O TRP A 129 6018 5545 4912 -135 -123 -271 O
ATOM 964 CB TRP A 129 30.044 192.255 27.697 1.00 39.07 C
ANISOU 964 CB TRP A 129 5461 4925 4459 -241 -141 -321 C
ATOM 965 CG TRP A 129 29.972 192.606 26.239 1.00 39.76 C
ANISOU 965 CG TRP A 129 5536 4975 4595 -255 -111 -293 C
ATOM 966 CD1 TRP A 129 29.861 193.854 25.701 1.00 42.92 C
ANISOU 966 CD1 TRP A 129 5956 5319 5031 -290 -102 -304 C
ATOM 967 CD2 TRP A 129 29.980 191.690 25.133 1.00 39.01 C
ANISOU 967 CD2 TRP A 129 5414 4894 4514 -233 -86 -248 C
ATOM 968 NE1 TRP A 129 29.807 193.776 24.328 1.00 41.97 N
ANISOU 968 NE1 TRP A 129 5825 5181 4939 -288 -73 -264 N
ATOM 969 CE2 TRP A 129 29.884 192.459 23.951 1.00 42.98 C
ANISOU 969 CE2 TRP A 129 5924 5355 5053 -254 -63 -233 C
ATOM 970 CE3 TRP A 129 30.074 190.289 25.023 1.00 39.71 C
ANISOU 970 CE3 TRP A 129 5478 5022 4586 -195 -80 -220 C
ATOM 971 CZ2 TRP A 129 29.889 191.876 22.675 1.00 41.97 C
ANISOU 971 CZ2 TRP A 129 5780 5230 4935 -239 -36 -194 C
ATOM 972 CZ3 TRP A 129 30.067 189.714 23.762 1.00 40.77 C
ANISOU 972 CZ3 TRP A 129 5597 5155 4739 -181 -53 -187 C
ATOM 973 CH2 TRP A 129 29.980 190.502 22.606 1.00 41.48 C
ANISOU 973 CH2 TRP A 129 5695 5209 4855 -202 -32 -176 C
ATOM 974 N VAL A 130 29.200 191.005 30.600 1.00 42.01 N
ANISOU 974 N VAL A 130 5901 5368 4693 -169 -163 -350 N
ATOM 975 CA VAL A 130 29.420 190.130 31.765 1.00 42.06 C
ANISOU 975 CA VAL A 130 5920 5427 4633 -139 -185 -343 C
ATOM 976 C VAL A 130 28.176 189.230 31.955 1.00 46.82 C
ANISOU 976 C VAL A 130 6553 6023 5214 -92 -132 -312 C
ATOM 977 O VAL A 130 28.330 188.013 32.112 1.00 47.07 O
ANISOU 977 O VAL A 130 6574 6085 5226 -62 -130 -270 O
ATOM 978 CB VAL A 130 29.756 190.946 33.059 1.00 46.24 C
ANISOU 978 CB VAL A 130 6489 5974 5108 -156 -229 -400 C
ATOM 979 CG1 VAL A 130 29.681 190.082 34.319 1.00 45.94 C
ANISOU 979 CG1 VAL A 130 6484 5986 4984 -116 -241 -389 C
ATOM 980 CG2 VAL A 130 31.125 191.614 32.960 1.00 46.60 C
ANISOU 980 CG2 VAL A 130 6491 6035 5178 -208 -291 -427 C
ATOM 981 N LEU A 131 26.959 189.830 31.929 1.00 42.76 N
ANISOU 981 N LEU A 131 6072 5466 4709 -86 -88 -331 N
ATOM 982 CA LEU A 131 25.683 189.123 32.091 1.00 42.61 C
ANISOU 982 CA LEU A 131 6071 5437 4680 -50 -32 -307 C
ATOM 983 C LEU A 131 25.407 188.155 30.930 1.00 46.42 C
ANISOU 983 C LEU A 131 6515 5908 5214 -39 -10 -259 C
ATOM 984 O LEU A 131 24.852 187.081 31.165 1.00 46.24 O
ANISOU 984 O LEU A 131 6496 5893 5179 -14 19 -225 O
ATOM 985 CB LEU A 131 24.513 190.110 32.230 1.00 42.96 C
ANISOU 985 CB LEU A 131 6147 5441 4737 -45 7 -343 C
ATOM 986 CG LEU A 131 24.435 190.902 33.531 1.00 48.68 C
ANISOU 986 CG LEU A 131 6925 6173 5399 -42 3 -395 C
ATOM 987 CD1 LEU A 131 23.609 192.159 33.344 1.00 48.83 C
ANISOU 987 CD1 LEU A 131 6965 6137 5451 -43 30 -439 C
ATOM 988 CD2 LEU A 131 23.872 190.051 34.677 1.00 51.80 C
ANISOU 988 CD2 LEU A 131 7354 6604 5725 -7 38 -379 C
ATOM 989 N SER A 132 25.798 188.530 29.689 1.00 42.65 N
ANISOU 989 N SER A 132 6006 5410 4791 -61 -22 -256 N
ATOM 990 CA SER A 132 25.630 187.708 28.483 1.00 41.69 C
ANISOU 990 CA SER A 132 5853 5277 4712 -52 -7 -219 C
ATOM 991 C SER A 132 26.410 186.401 28.615 1.00 46.19 C
ANISOU 991 C SER A 132 6404 5881 5265 -36 -20 -184 C
ATOM 992 O SER A 132 25.895 185.344 28.229 1.00 45.33 O
ANISOU 992 O SER A 132 6290 5763 5170 -15 4 -155 O
ATOM 993 CB SER A 132 26.076 188.471 27.242 1.00 43.69 C
ANISOU 993 CB SER A 132 6085 5507 5010 -78 -19 -223 C
ATOM 994 OG SER A 132 25.257 189.613 27.061 1.00 51.05 O
ANISOU 994 OG SER A 132 7038 6398 5961 -85 -6 -248 O
ATOM 995 N PHE A 133 27.630 186.473 29.203 1.00 43.55 N
ANISOU 995 N PHE A 133 6060 5585 4903 -43 -61 -190 N
ATOM 996 CA PHE A 133 28.475 185.307 29.472 1.00 43.76 C
ANISOU 996 CA PHE A 133 6068 5648 4912 -18 -80 -157 C
ATOM 997 C PHE A 133 27.785 184.386 30.491 1.00 48.05 C
ANISOU 997 C PHE A 133 6649 6196 5410 15 -60 -133 C
ATOM 998 O PHE A 133 27.669 183.189 30.234 1.00 47.74 O
ANISOU 998 O PHE A 133 6606 6150 5382 41 -42 -95 O
ATOM 999 CB PHE A 133 29.880 185.726 29.950 1.00 45.92 C
ANISOU 999 CB PHE A 133 6314 5964 5168 -33 -136 -172 C
ATOM 1000 CG PHE A 133 30.860 185.886 28.810 1.00 47.64 C
ANISOU 1000 CG PHE A 133 6476 6186 5438 -53 -147 -168 C
ATOM 1001 CD1 PHE A 133 31.435 184.773 28.200 1.00 50.62 C
ANISOU 1001 CD1 PHE A 133 6820 6579 5836 -24 -142 -133 C
ATOM 1002 CD2 PHE A 133 31.178 187.146 28.315 1.00 49.61 C
ANISOU 1002 CD2 PHE A 133 6710 6421 5717 -100 -155 -198 C
ATOM 1003 CE1 PHE A 133 32.310 184.921 27.116 1.00 51.30 C
ANISOU 1003 CE1 PHE A 133 6853 6671 5966 -39 -140 -130 C
ATOM 1004 CE2 PHE A 133 32.056 187.293 27.233 1.00 52.30 C
ANISOU 1004 CE2 PHE A 133 7001 6767 6105 -120 -153 -189 C
ATOM 1005 CZ PHE A 133 32.616 186.180 26.641 1.00 50.18 C
ANISOU 1005 CZ PHE A 133 6696 6521 5851 -89 -143 -155 C
ATOM 1006 N ALA A 134 27.245 184.966 31.588 1.00 44.48 N
ANISOU 1006 N ALA A 134 6239 5750 4910 14 -54 -156 N
ATOM 1007 CA ALA A 134 26.542 184.263 32.666 1.00 44.35 C
ANISOU 1007 CA ALA A 134 6267 5742 4842 42 -25 -133 C
ATOM 1008 C ALA A 134 25.294 183.520 32.164 1.00 47.44 C
ANISOU 1008 C ALA A 134 6660 6095 5272 51 37 -105 C
ATOM 1009 O ALA A 134 25.125 182.349 32.496 1.00 47.99 O
ANISOU 1009 O ALA A 134 6743 6163 5328 73 57 -62 O
ATOM 1010 CB ALA A 134 26.155 185.243 33.769 1.00 45.41 C
ANISOU 1010 CB ALA A 134 6446 5888 4919 36 -22 -174 C
ATOM 1011 N ILE A 135 24.442 184.187 31.365 1.00 42.27 N
ANISOU 1011 N ILE A 135 5990 5405 4666 33 62 -129 N
ATOM 1012 CA ILE A 135 23.202 183.626 30.818 1.00 41.38 C
ANISOU 1012 CA ILE A 135 5867 5257 4598 35 112 -112 C
ATOM 1013 C ILE A 135 23.521 182.537 29.748 1.00 43.49 C
ANISOU 1013 C ILE A 135 6107 5509 4910 38 104 -82 C
ATOM 1014 O ILE A 135 23.029 181.409 29.864 1.00 42.71 O
ANISOU 1014 O ILE A 135 6014 5394 4821 49 133 -49 O
ATOM 1015 CB ILE A 135 22.295 184.776 30.268 1.00 44.46 C
ANISOU 1015 CB ILE A 135 6246 5621 5027 21 127 -150 C
ATOM 1016 CG1 ILE A 135 21.740 185.649 31.427 1.00 45.57 C
ANISOU 1016 CG1 ILE A 135 6421 5770 5126 27 151 -180 C
ATOM 1017 CG2 ILE A 135 21.152 184.252 29.378 1.00 44.82 C
ANISOU 1017 CG2 ILE A 135 6263 5633 5133 20 159 -136 C
ATOM 1018 CD1 ILE A 135 21.409 187.131 31.046 1.00 50.95 C
ANISOU 1018 CD1 ILE A 135 7100 6426 5832 18 146 -227 C
ATOM 1019 N GLY A 136 24.334 182.892 28.750 1.00 38.41 N
ANISOU 1019 N GLY A 136 5437 4866 4293 28 70 -94 N
ATOM 1020 CA GLY A 136 24.721 182.013 27.650 1.00 37.37 C
ANISOU 1020 CA GLY A 136 5281 4720 4197 34 64 -75 C
ATOM 1021 C GLY A 136 25.505 180.767 28.023 1.00 40.97 C
ANISOU 1021 C GLY A 136 5742 5189 4637 60 56 -40 C
ATOM 1022 O GLY A 136 25.401 179.754 27.325 1.00 39.96 O
ANISOU 1022 O GLY A 136 5608 5034 4539 71 68 -22 O
ATOM 1023 N LEU A 137 26.300 180.824 29.122 1.00 37.36 N
ANISOU 1023 N LEU A 137 5297 4768 4130 74 32 -31 N
ATOM 1024 CA LEU A 137 27.093 179.675 29.578 1.00 36.75 C
ANISOU 1024 CA LEU A 137 5226 4704 4033 109 18 8 C
ATOM 1025 C LEU A 137 26.495 179.028 30.836 1.00 39.77 C
ANISOU 1025 C LEU A 137 5656 5085 4371 127 42 42 C
ATOM 1026 O LEU A 137 27.199 178.266 31.499 1.00 39.84 O
ANISOU 1026 O LEU A 137 5680 5111 4347 160 23 77 O
ATOM 1027 CB LEU A 137 28.581 180.035 29.835 1.00 36.98 C
ANISOU 1027 CB LEU A 137 5228 4782 4040 119 -37 2 C
ATOM 1028 CG LEU A 137 29.395 180.745 28.730 1.00 41.42 C
ANISOU 1028 CG LEU A 137 5740 5355 4641 98 -57 -25 C
ATOM 1029 CD1 LEU A 137 30.798 181.083 29.238 1.00 41.59 C
ANISOU 1029 CD1 LEU A 137 5729 5430 4643 103 -111 -30 C
ATOM 1030 CD2 LEU A 137 29.452 179.929 27.408 1.00 42.98 C
ANISOU 1030 CD2 LEU A 137 5918 5524 4889 111 -34 -14 C
ATOM 1031 N THR A 138 25.192 179.277 31.144 1.00 35.71 N
ANISOU 1031 N THR A 138 5163 4549 3856 109 88 35 N
ATOM 1032 CA THR A 138 24.513 178.667 32.309 1.00 35.75 C
ANISOU 1032 CA THR A 138 5214 4551 3819 122 127 71 C
ATOM 1033 C THR A 138 24.613 177.104 32.225 1.00 39.54 C
ANISOU 1033 C THR A 138 5708 4997 4318 146 143 126 C
ATOM 1034 O THR A 138 24.950 176.521 33.256 1.00 39.08 O
ANISOU 1034 O THR A 138 5689 4953 4205 174 142 168 O
ATOM 1035 CB THR A 138 23.079 179.206 32.482 1.00 39.32 C
ANISOU 1035 CB THR A 138 5672 4985 4284 98 182 52 C
ATOM 1036 OG1 THR A 138 23.171 180.530 33.008 1.00 38.47 O
ANISOU 1036 OG1 THR A 138 5573 4911 4135 91 166 9 O
ATOM 1037 CG2 THR A 138 22.233 178.370 33.439 1.00 35.38 C
ANISOU 1037 CG2 THR A 138 5211 4473 3760 106 241 96 C
ATOM 1038 N PRO A 139 24.476 176.423 31.041 1.00 36.28 N
ANISOU 1038 N PRO A 139 5270 4541 3976 139 151 126 N
ATOM 1039 CA PRO A 139 24.653 174.957 31.011 1.00 36.73 C
ANISOU 1039 CA PRO A 139 5348 4557 4051 164 164 174 C
ATOM 1040 C PRO A 139 25.991 174.461 31.578 1.00 42.75 C
ANISOU 1040 C PRO A 139 6125 5348 4772 213 122 208 C
ATOM 1041 O PRO A 139 26.032 173.374 32.147 1.00 42.12 O
ANISOU 1041 O PRO A 139 6083 5241 4679 242 137 262 O
ATOM 1042 CB PRO A 139 24.546 174.627 29.520 1.00 37.77 C
ANISOU 1042 CB PRO A 139 5446 4649 4255 151 162 148 C
ATOM 1043 CG PRO A 139 23.618 175.653 28.999 1.00 41.91 C
ANISOU 1043 CG PRO A 139 5945 5177 4803 110 174 103 C
ATOM 1044 CD PRO A 139 24.047 176.911 29.710 1.00 37.46 C
ANISOU 1044 CD PRO A 139 5379 4668 4185 111 150 84 C
ATOM 1045 N MET A 140 27.063 175.272 31.475 1.00 41.16 N
ANISOU 1045 N MET A 140 5891 5199 4549 223 68 180 N
ATOM 1046 CA MET A 140 28.394 174.936 32.003 1.00 42.40 C
ANISOU 1046 CA MET A 140 6045 5394 4670 269 17 206 C
ATOM 1047 C MET A 140 28.423 174.928 33.544 1.00 47.50 C
ANISOU 1047 C MET A 140 6741 6075 5231 291 5 241 C
ATOM 1048 O MET A 140 29.343 174.358 34.133 1.00 47.41 O
ANISOU 1048 O MET A 140 6741 6088 5186 338 -34 278 O
ATOM 1049 CB MET A 140 29.448 175.924 31.488 1.00 44.89 C
ANISOU 1049 CB MET A 140 6303 5760 4993 261 -35 162 C
ATOM 1050 CG MET A 140 29.410 176.132 29.999 1.00 48.79 C
ANISOU 1050 CG MET A 140 6755 6229 5554 238 -21 127 C
ATOM 1051 SD MET A 140 31.033 175.876 29.285 1.00 54.46 S
ANISOU 1051 SD MET A 140 7414 6978 6301 274 -62 125 S
ATOM 1052 CE MET A 140 31.742 177.449 29.554 1.00 51.36 C
ANISOU 1052 CE MET A 140 6978 6651 5885 237 -107 84 C
ATOM 1053 N LEU A 141 27.430 175.571 34.189 1.00 44.50 N
ANISOU 1053 N LEU A 141 6393 5701 4816 260 40 228 N
ATOM 1054 CA LEU A 141 27.344 175.653 35.648 1.00 45.05 C
ANISOU 1054 CA LEU A 141 6519 5805 4792 278 38 254 C
ATOM 1055 C LEU A 141 26.635 174.424 36.242 1.00 49.21 C
ANISOU 1055 C LEU A 141 7105 6288 5305 298 96 325 C
ATOM 1056 O LEU A 141 26.555 174.310 37.472 1.00 49.58 O
ANISOU 1056 O LEU A 141 7210 6361 5267 319 103 361 O
ATOM 1057 CB LEU A 141 26.656 176.958 36.102 1.00 44.94 C
ANISOU 1057 CB LEU A 141 6515 5818 4741 242 55 203 C
ATOM 1058 CG LEU A 141 27.292 178.282 35.633 1.00 49.20 C
ANISOU 1058 CG LEU A 141 7008 6393 5293 216 2 134 C
ATOM 1059 CD1 LEU A 141 26.324 179.433 35.807 1.00 49.54 C
ANISOU 1059 CD1 LEU A 141 7063 6435 5327 180 37 84 C
ATOM 1060 CD2 LEU A 141 28.595 178.584 36.370 1.00 51.10 C
ANISOU 1060 CD2 LEU A 141 7248 6696 5470 240 -79 128 C
ATOM 1061 N GLY A 142 26.166 173.512 35.377 1.00 44.56 N
ANISOU 1061 N GLY A 142 6504 5631 4795 289 136 344 N
ATOM 1062 CA GLY A 142 25.519 172.279 35.817 1.00 44.64 C
ANISOU 1062 CA GLY A 142 6566 5585 4809 300 193 412 C
ATOM 1063 C GLY A 142 24.247 171.853 35.112 1.00 47.59 C
ANISOU 1063 C GLY A 142 6929 5890 5264 253 263 408 C
ATOM 1064 O GLY A 142 23.880 170.679 35.182 1.00 48.35 O
ANISOU 1064 O GLY A 142 7057 5924 5388 258 304 461 O
ATOM 1065 N TRP A 143 23.550 172.786 34.453 1.00 42.48 N
ANISOU 1065 N TRP A 143 6236 5250 4654 208 276 346 N
ATOM 1066 CA TRP A 143 22.316 172.496 33.720 1.00 41.67 C
ANISOU 1066 CA TRP A 143 6110 5091 4632 161 331 333 C
ATOM 1067 C TRP A 143 22.666 171.935 32.324 1.00 46.32 C
ANISOU 1067 C TRP A 143 6663 5634 5300 159 303 310 C
ATOM 1068 O TRP A 143 22.481 172.614 31.309 1.00 45.62 O
ANISOU 1068 O TRP A 143 6528 5552 5253 134 285 254 O
ATOM 1069 CB TRP A 143 21.459 173.773 33.614 1.00 39.70 C
ANISOU 1069 CB TRP A 143 5826 4873 4387 125 349 278 C
ATOM 1070 CG TRP A 143 20.015 173.558 33.254 1.00 40.47 C
ANISOU 1070 CG TRP A 143 5898 4927 4552 79 411 272 C
ATOM 1071 CD1 TRP A 143 19.413 172.382 32.903 1.00 43.53 C
ANISOU 1071 CD1 TRP A 143 6287 5248 5005 58 449 303 C
ATOM 1072 CD2 TRP A 143 18.989 174.558 33.227 1.00 40.02 C
ANISOU 1072 CD2 TRP A 143 5806 4889 4511 50 441 231 C
ATOM 1073 NE1 TRP A 143 18.081 172.594 32.640 1.00 43.01 N
ANISOU 1073 NE1 TRP A 143 6182 5165 4997 12 497 282 N
ATOM 1074 CE2 TRP A 143 17.790 173.919 32.840 1.00 44.20 C
ANISOU 1074 CE2 TRP A 143 6308 5369 5118 11 494 240 C
ATOM 1075 CE3 TRP A 143 18.968 175.941 33.484 1.00 40.85 C
ANISOU 1075 CE3 TRP A 143 5900 5045 4577 54 428 185 C
ATOM 1076 CZ2 TRP A 143 16.578 174.610 32.723 1.00 43.59 C
ANISOU 1076 CZ2 TRP A 143 6184 5299 5080 -19 533 207 C
ATOM 1077 CZ3 TRP A 143 17.769 176.627 33.357 1.00 42.28 C
ANISOU 1077 CZ3 TRP A 143 6042 5226 4795 29 469 153 C
ATOM 1078 CH2 TRP A 143 16.592 175.964 32.982 1.00 43.22 C
ANISOU 1078 CH2 TRP A 143 6127 5303 4991 -4 520 166 C
ATOM 1079 N ASN A 144 23.168 170.689 32.284 1.00 43.07 N
ANISOU 1079 N ASN A 144 6282 5176 4906 188 301 355 N
ATOM 1080 CA ASN A 144 23.592 170.005 31.061 1.00 42.54 C
ANISOU 1080 CA ASN A 144 6196 5062 4906 196 279 335 C
ATOM 1081 C ASN A 144 23.303 168.483 31.150 1.00 47.20 C
ANISOU 1081 C ASN A 144 6831 5566 5538 203 317 387 C
ATOM 1082 O ASN A 144 23.013 167.980 32.240 1.00 46.54 O
ANISOU 1082 O ASN A 144 6795 5466 5421 210 354 450 O
ATOM 1083 CB ASN A 144 25.092 170.271 30.812 1.00 41.05 C
ANISOU 1083 CB ASN A 144 5989 4920 4689 247 216 323 C
ATOM 1084 CG ASN A 144 25.997 169.795 31.931 1.00 50.23 C
ANISOU 1084 CG ASN A 144 7191 6105 5790 305 195 383 C
ATOM 1085 OD1 ASN A 144 26.128 168.603 32.200 1.00 45.74 O
ANISOU 1085 OD1 ASN A 144 6665 5482 5234 336 210 437 O
ATOM 1086 ND2 ASN A 144 26.631 170.710 32.624 1.00 38.82 N
ANISOU 1086 ND2 ASN A 144 5736 4736 4277 320 154 376 N
ATOM 1087 N ASN A 145 23.418 167.755 30.015 1.00 44.44 N
ANISOU 1087 N ASN A 145 6472 5157 5257 202 309 362 N
ATOM 1088 CA ASN A 145 23.169 166.310 29.964 1.00 45.61 C
ANISOU 1088 CA ASN A 145 6664 5209 5456 205 341 402 C
ATOM 1089 C ASN A 145 24.473 165.500 30.046 1.00 53.55 C
ANISOU 1089 C ASN A 145 7702 6195 6449 281 311 437 C
ATOM 1090 O ASN A 145 24.448 164.294 29.793 1.00 53.26 O
ANISOU 1090 O ASN A 145 7704 6071 6463 294 330 460 O
ATOM 1091 CB ASN A 145 22.385 165.908 28.700 1.00 43.81 C
ANISOU 1091 CB ASN A 145 6415 4917 5315 155 352 348 C
ATOM 1092 CG ASN A 145 21.127 166.694 28.408 1.00 62.39 C
ANISOU 1092 CG ASN A 145 8723 7290 7694 86 370 306 C
ATOM 1093 OD1 ASN A 145 20.252 166.881 29.266 1.00 52.89 O
ANISOU 1093 OD1 ASN A 145 7522 6093 6482 53 415 336 O
ATOM 1094 ND2 ASN A 145 20.982 167.108 27.152 1.00 53.70 N
ANISOU 1094 ND2 ASN A 145 7582 6195 6628 65 339 236 N
ATOM 1095 N CYS A 146 25.597 166.141 30.445 1.00 53.55 N
ANISOU 1095 N CYS A 146 7687 6276 6386 333 263 442 N
ATOM 1096 CA CYS A 146 26.905 165.479 30.585 1.00 55.55 C
ANISOU 1096 CA CYS A 146 7955 6525 6626 414 227 476 C
ATOM 1097 C CYS A 146 26.849 164.328 31.606 1.00 62.63 C
ANISOU 1097 C CYS A 146 8926 7361 7509 449 254 565 C
ATOM 1098 O CYS A 146 27.556 163.335 31.433 1.00 63.17 O
ANISOU 1098 O CYS A 146 9020 7377 7605 508 244 594 O
ATOM 1099 CB CYS A 146 27.993 166.484 30.951 1.00 56.08 C
ANISOU 1099 CB CYS A 146 7981 6698 6630 451 169 465 C
ATOM 1100 SG CYS A 146 28.320 167.726 29.670 1.00 59.19 S
ANISOU 1100 SG CYS A 146 8293 7153 7045 420 139 371 S
ATOM 1101 N GLY A 147 26.005 164.475 32.632 1.00 60.68 N
ANISOU 1101 N GLY A 147 8714 7119 7221 415 293 608 N
ATOM 1102 CA GLY A 147 25.798 163.478 33.679 1.00 61.95 C
ANISOU 1102 CA GLY A 147 8953 7223 7360 438 330 701 C
ATOM 1103 C GLY A 147 25.092 162.216 33.212 1.00 67.25 C
ANISOU 1103 C GLY A 147 9665 7768 8119 411 384 722 C
ATOM 1104 O GLY A 147 25.268 161.156 33.821 1.00 67.77 O
ANISOU 1104 O GLY A 147 9799 7765 8184 450 405 801 O
ATOM 1105 N GLN A 148 24.282 162.322 32.132 1.00 63.82 N
ANISOU 1105 N GLN A 148 9190 7297 7761 343 405 652 N
ATOM 1106 CA GLN A 148 23.544 161.205 31.535 1.00 64.37 C
ANISOU 1106 CA GLN A 148 9288 7245 7925 303 448 652 C
ATOM 1107 C GLN A 148 23.908 161.087 30.024 1.00 67.65 C
ANISOU 1107 C GLN A 148 9665 7635 8405 306 412 566 C
ATOM 1108 O GLN A 148 23.129 161.514 29.166 1.00 66.52 O
ANISOU 1108 O GLN A 148 9477 7492 8304 241 416 497 O
ATOM 1109 CB GLN A 148 22.028 161.386 31.757 1.00 65.86 C
ANISOU 1109 CB GLN A 148 9465 7414 8144 208 511 651 C
ATOM 1110 N PRO A 149 25.097 160.529 29.672 1.00 64.45 N
ANISOU 1110 N PRO A 149 9275 7209 8003 386 377 569 N
ATOM 1111 CA PRO A 149 25.486 160.480 28.248 1.00 63.79 C
ANISOU 1111 CA PRO A 149 9159 7111 7968 395 349 484 C
ATOM 1112 C PRO A 149 24.858 159.345 27.435 1.00 67.53 C
ANISOU 1112 C PRO A 149 9671 7456 8532 361 379 456 C
ATOM 1113 O PRO A 149 24.460 158.315 27.981 1.00 67.70 O
ANISOU 1113 O PRO A 149 9754 7380 8589 354 417 514 O
ATOM 1114 CB PRO A 149 27.003 160.297 28.311 1.00 65.83 C
ANISOU 1114 CB PRO A 149 9416 7400 8195 499 308 504 C
ATOM 1115 CG PRO A 149 27.231 159.536 29.576 1.00 70.99 C
ANISOU 1115 CG PRO A 149 10134 8016 8824 547 322 605 C
ATOM 1116 CD PRO A 149 26.167 159.990 30.543 1.00 66.51 C
ANISOU 1116 CD PRO A 149 9581 7471 8220 479 358 646 C
ATOM 1117 N LYS A 150 24.817 159.537 26.105 1.00 63.52 N
ANISOU 1117 N LYS A 150 9130 6948 8058 342 358 365 N
ATOM 1118 CA LYS A 150 24.315 158.558 25.142 1.00 63.78 C
ANISOU 1118 CA LYS A 150 9196 6868 8171 311 372 316 C
ATOM 1119 C LYS A 150 25.449 157.561 24.876 1.00 67.91 C
ANISOU 1119 C LYS A 150 9766 7326 8712 404 366 325 C
ATOM 1120 O LYS A 150 26.224 157.712 23.928 1.00 66.82 O
ANISOU 1120 O LYS A 150 9606 7215 8568 450 340 264 O
ATOM 1121 CB LYS A 150 23.808 159.249 23.858 1.00 65.73 C
ANISOU 1121 CB LYS A 150 9392 7151 8431 257 347 214 C
ATOM 1122 CG LYS A 150 22.617 160.180 24.094 1.00 77.47 C
ANISOU 1122 CG LYS A 150 10830 8692 9911 170 353 205 C
ATOM 1123 CD LYS A 150 21.532 159.997 23.041 1.00 87.53 C
ANISOU 1123 CD LYS A 150 12091 9918 11249 91 347 129 C
ATOM 1124 CE LYS A 150 20.298 160.826 23.324 1.00 99.80 C
ANISOU 1124 CE LYS A 150 13591 11520 12809 11 355 125 C
ATOM 1125 NZ LYS A 150 20.507 162.271 23.031 1.00108.38 N
ANISOU 1125 NZ LYS A 150 14618 12727 13834 21 321 93 N
ATOM 1126 N GLU A 151 25.567 156.572 25.780 1.00 65.61 N
ANISOU 1126 N GLU A 151 9538 6951 8439 437 393 408 N
ATOM 1127 CA GLU A 151 26.592 155.523 25.823 1.00 66.31 C
ANISOU 1127 CA GLU A 151 9680 6966 8547 536 392 441 C
ATOM 1128 C GLU A 151 26.728 154.733 24.499 1.00 70.24 C
ANISOU 1128 C GLU A 151 10205 7372 9112 549 393 356 C
ATOM 1129 O GLU A 151 27.844 154.346 24.148 1.00 69.83 O
ANISOU 1129 O GLU A 151 10162 7311 9060 645 380 346 O
ATOM 1130 CB GLU A 151 26.339 154.566 27.004 1.00 68.78 C
ANISOU 1130 CB GLU A 151 10070 7186 8877 547 429 548 C
ATOM 1131 CG GLU A 151 24.931 153.994 27.074 1.00 81.38 C
ANISOU 1131 CG GLU A 151 11704 8677 10538 441 478 554 C
ATOM 1132 CD GLU A 151 24.436 153.595 28.451 1.00 99.38 C
ANISOU 1132 CD GLU A 151 14036 10918 12805 422 524 669 C
ATOM 1133 OE1 GLU A 151 24.678 152.435 28.860 1.00 82.63 O
ANISOU 1133 OE1 GLU A 151 11995 8679 10720 464 549 736 O
ATOM 1134 OE2 GLU A 151 23.760 154.429 29.098 1.00 88.83 O
ANISOU 1134 OE2 GLU A 151 12664 9663 11424 363 539 692 O
ATOM 1135 N GLY A 152 25.617 154.531 23.787 1.00 66.77 N
ANISOU 1135 N GLY A 152 9774 6870 8726 455 407 293 N
ATOM 1136 CA GLY A 152 25.582 153.828 22.509 1.00 66.95 C
ANISOU 1136 CA GLY A 152 9827 6805 8805 453 403 201 C
ATOM 1137 C GLY A 152 26.303 154.570 21.402 1.00 70.53 C
ANISOU 1137 C GLY A 152 10231 7353 9216 493 371 116 C
ATOM 1138 O GLY A 152 27.202 154.012 20.763 1.00 71.07 O
ANISOU 1138 O GLY A 152 10325 7385 9294 573 370 81 O
ATOM 1139 N LYS A 153 25.927 155.848 21.185 1.00 65.38 N
ANISOU 1139 N LYS A 153 9507 6820 8514 440 348 86 N
ATOM 1140 CA LYS A 153 26.531 156.720 20.175 1.00 64.09 C
ANISOU 1140 CA LYS A 153 9292 6755 8302 466 321 14 C
ATOM 1141 C LYS A 153 28.012 157.015 20.492 1.00 67.90 C
ANISOU 1141 C LYS A 153 9746 7313 8738 573 314 52 C
ATOM 1142 O LYS A 153 28.814 157.136 19.562 1.00 67.47 O
ANISOU 1142 O LYS A 153 9675 7292 8668 625 310 -4 O
ATOM 1143 CB LYS A 153 25.742 158.032 20.049 1.00 65.26 C
ANISOU 1143 CB LYS A 153 9377 7006 8413 386 300 -9 C
ATOM 1144 N ASN A 154 28.369 157.120 21.797 1.00 64.04 N
ANISOU 1144 N ASN A 154 9250 6856 8228 605 315 146 N
ATOM 1145 CA ASN A 154 29.736 157.403 22.251 1.00 63.66 C
ANISOU 1145 CA ASN A 154 9165 6884 8140 702 299 188 C
ATOM 1146 C ASN A 154 30.689 156.229 21.974 1.00 69.67 C
ANISOU 1146 C ASN A 154 9968 7562 8940 806 312 190 C
ATOM 1147 O ASN A 154 31.825 156.472 21.560 1.00 69.48 O
ANISOU 1147 O ASN A 154 9900 7601 8898 882 303 171 O
ATOM 1148 CB ASN A 154 29.762 157.778 23.737 1.00 61.45 C
ANISOU 1148 CB ASN A 154 8874 6653 7820 705 288 283 C
ATOM 1149 CG ASN A 154 29.176 159.140 24.072 1.00 69.01 C
ANISOU 1149 CG ASN A 154 9777 7719 8726 630 272 279 C
ATOM 1150 OD1 ASN A 154 28.708 159.898 23.209 1.00 57.80 O
ANISOU 1150 OD1 ASN A 154 8322 6341 7300 572 267 210 O
ATOM 1151 ND2 ASN A 154 29.188 159.485 25.350 1.00 56.22 N
ANISOU 1151 ND2 ASN A 154 8155 6144 7063 633 264 354 N
ATOM 1152 N HIS A 155 30.235 154.971 22.173 1.00 67.75 N
ANISOU 1152 N HIS A 155 9807 7178 8756 808 337 214 N
ATOM 1153 CA HIS A 155 31.066 153.790 21.910 1.00 69.23 C
ANISOU 1153 CA HIS A 155 10046 7270 8989 910 352 215 C
ATOM 1154 C HIS A 155 31.200 153.541 20.401 1.00 73.16 C
ANISOU 1154 C HIS A 155 10553 7735 9511 918 364 102 C
ATOM 1155 O HIS A 155 32.271 153.125 19.954 1.00 73.30 O
ANISOU 1155 O HIS A 155 10568 7744 9537 1020 373 82 O
ATOM 1156 CB HIS A 155 30.533 152.533 22.624 1.00 71.50 C
ANISOU 1156 CB HIS A 155 10427 7405 9335 908 378 279 C
ATOM 1157 CG HIS A 155 30.528 152.613 24.124 1.00 75.46 C
ANISOU 1157 CG HIS A 155 10935 7931 9805 918 372 398 C
ATOM 1158 ND1 HIS A 155 31.387 153.459 24.815 1.00 77.05 N
ANISOU 1158 ND1 HIS A 155 11071 8266 9938 974 337 447 N
ATOM 1159 CD2 HIS A 155 29.772 151.937 25.020 1.00 78.15 C
ANISOU 1159 CD2 HIS A 155 11345 8177 10172 880 397 475 C
ATOM 1160 CE1 HIS A 155 31.112 153.282 26.097 1.00 76.93 C
ANISOU 1160 CE1 HIS A 155 11091 8237 9900 970 339 548 C
ATOM 1161 NE2 HIS A 155 30.147 152.378 26.270 1.00 77.94 N
ANISOU 1161 NE2 HIS A 155 11302 8230 10082 915 379 572 N
ATOM 1162 N SER A 156 30.135 153.824 19.619 1.00 69.24 N
ANISOU 1162 N SER A 156 10064 7226 9020 816 364 28 N
ATOM 1163 CA SER A 156 30.141 153.672 18.161 1.00 69.43 C
ANISOU 1163 CA SER A 156 10104 7227 9050 814 370 -85 C
ATOM 1164 C SER A 156 31.120 154.665 17.506 1.00 73.32 C
ANISOU 1164 C SER A 156 10521 7857 9480 864 363 -122 C
ATOM 1165 O SER A 156 31.798 154.304 16.542 1.00 73.91 O
ANISOU 1165 O SER A 156 10609 7916 9556 928 381 -186 O
ATOM 1166 CB SER A 156 28.738 153.849 17.589 1.00 72.92 C
ANISOU 1166 CB SER A 156 10562 7638 9505 690 359 -147 C
ATOM 1167 OG SER A 156 28.248 155.167 17.760 1.00 81.76 O
ANISOU 1167 OG SER A 156 11610 8881 10572 621 335 -138 O
ATOM 1168 N GLN A 157 31.203 155.900 18.044 1.00 68.65 N
ANISOU 1168 N GLN A 157 9852 7395 8835 835 341 -81 N
ATOM 1169 CA GLN A 157 32.110 156.949 17.566 1.00 67.61 C
ANISOU 1169 CA GLN A 157 9642 7397 8650 870 335 -102 C
ATOM 1170 C GLN A 157 33.557 156.658 17.982 1.00 70.98 C
ANISOU 1170 C GLN A 157 10035 7853 9081 990 343 -57 C
ATOM 1171 O GLN A 157 34.488 157.165 17.351 1.00 70.60 O
ANISOU 1171 O GLN A 157 9930 7887 9008 1038 353 -89 O
ATOM 1172 CB GLN A 157 31.678 158.326 18.097 1.00 67.90 C
ANISOU 1172 CB GLN A 157 9614 7548 8637 795 307 -72 C
ATOM 1173 CG GLN A 157 30.535 158.969 17.313 1.00 89.10 C
ANISOU 1173 CG GLN A 157 12302 10248 11304 694 296 -135 C
ATOM 1174 CD GLN A 157 30.987 159.639 16.032 1.00114.13 C
ANISOU 1174 CD GLN A 157 15443 13489 14432 704 301 -207 C
ATOM 1175 OE1 GLN A 157 31.883 160.493 16.022 1.00109.99 O
ANISOU 1175 OE1 GLN A 157 14854 13067 13870 737 302 -192 O
ATOM 1176 NE2 GLN A 157 30.345 159.293 14.924 1.00107.76 N
ANISOU 1176 NE2 GLN A 157 14684 12630 13628 670 303 -286 N
ATOM 1177 N GLY A 158 33.722 155.862 19.043 1.00 66.85 N
ANISOU 1177 N GLY A 158 9544 7265 8592 1036 340 19 N
ATOM 1178 CA GLY A 158 35.018 155.475 19.589 1.00 66.94 C
ANISOU 1178 CA GLY A 158 9525 7294 8614 1156 337 73 C
ATOM 1179 C GLY A 158 35.562 156.437 20.627 1.00 69.46 C
ANISOU 1179 C GLY A 158 9765 7739 8889 1163 299 145 C
ATOM 1180 O GLY A 158 36.780 156.580 20.761 1.00 69.34 O
ANISOU 1180 O GLY A 158 9685 7791 8870 1250 289 164 O
ATOM 1181 N CYS A 159 34.664 157.094 21.382 1.00 64.70 N
ANISOU 1181 N CYS A 159 9163 7167 8254 1072 277 181 N
ATOM 1182 CA CYS A 159 35.046 158.060 22.412 1.00 63.66 C
ANISOU 1182 CA CYS A 159 8966 7150 8073 1067 238 240 C
ATOM 1183 C CYS A 159 35.606 157.345 23.642 1.00 69.67 C
ANISOU 1183 C CYS A 159 9749 7883 8841 1149 216 335 C
ATOM 1184 O CYS A 159 35.156 156.250 23.995 1.00 70.00 O
ANISOU 1184 O CYS A 159 9874 7805 8916 1166 234 372 O
ATOM 1185 CB CYS A 159 33.877 158.969 22.787 1.00 62.38 C
ANISOU 1185 CB CYS A 159 8804 7023 7873 951 227 242 C
ATOM 1186 SG CYS A 159 33.075 159.802 21.388 1.00 65.03 S
ANISOU 1186 SG CYS A 159 9122 7386 8200 855 244 141 S
ATOM 1187 N GLY A 160 36.589 157.983 24.269 1.00 66.74 N
ANISOU 1187 N GLY A 160 9302 7622 8435 1197 175 372 N
ATOM 1188 CA GLY A 160 37.242 157.486 25.470 1.00 67.44 C
ANISOU 1188 CA GLY A 160 9398 7711 8514 1281 139 463 C
ATOM 1189 C GLY A 160 36.560 157.971 26.730 1.00 71.48 C
ANISOU 1189 C GLY A 160 9936 8254 8968 1222 111 527 C
ATOM 1190 O GLY A 160 35.468 158.549 26.666 1.00 70.36 O
ANISOU 1190 O GLY A 160 9813 8115 8806 1116 128 502 O
ATOM 1191 N GLU A 161 37.214 157.739 27.886 1.00 68.98 N
ANISOU 1191 N GLU A 161 9620 7967 8623 1295 66 610 N
ATOM 1192 CA GLU A 161 36.729 158.111 29.217 1.00 68.56 C
ANISOU 1192 CA GLU A 161 9600 7950 8502 1259 37 681 C
ATOM 1193 C GLU A 161 36.533 159.626 29.338 1.00 71.02 C
ANISOU 1193 C GLU A 161 9843 8386 8755 1174 11 640 C
ATOM 1194 O GLU A 161 37.446 160.398 29.028 1.00 70.68 O
ANISOU 1194 O GLU A 161 9706 8443 8705 1193 -24 603 O
ATOM 1195 CB GLU A 161 37.698 157.610 30.298 1.00 71.02 C
ANISOU 1195 CB GLU A 161 9914 8283 8787 1371 -18 770 C
ATOM 1196 N GLY A 162 35.326 160.023 29.747 1.00 66.12 N
ANISOU 1196 N GLY A 162 9270 7753 8101 1080 34 646 N
ATOM 1197 CA GLY A 162 34.942 161.419 29.939 1.00 64.48 C
ANISOU 1197 CA GLY A 162 9016 7645 7840 996 17 610 C
ATOM 1198 C GLY A 162 34.551 162.159 28.673 1.00 66.04 C
ANISOU 1198 C GLY A 162 9166 7860 8068 924 44 518 C
ATOM 1199 O GLY A 162 34.085 163.303 28.741 1.00 64.91 O
ANISOU 1199 O GLY A 162 8993 7782 7888 850 38 486 O
ATOM 1200 N GLN A 163 34.737 161.512 27.508 1.00 61.20 N
ANISOU 1200 N GLN A 163 8550 7184 7517 949 75 474 N
ATOM 1201 CA GLN A 163 34.424 162.088 26.202 1.00 59.32 C
ANISOU 1201 CA GLN A 163 8277 6957 7303 891 101 388 C
ATOM 1202 C GLN A 163 32.994 161.760 25.784 1.00 61.48 C
ANISOU 1202 C GLN A 163 8617 7142 7603 813 145 363 C
ATOM 1203 O GLN A 163 32.419 160.770 26.244 1.00 60.98 O
ANISOU 1203 O GLN A 163 8626 6983 7561 818 167 407 O
ATOM 1204 CB GLN A 163 35.411 161.604 25.121 1.00 60.73 C
ANISOU 1204 CB GLN A 163 8422 7123 7528 962 114 346 C
ATOM 1205 CG GLN A 163 36.864 162.037 25.325 1.00 65.41 C
ANISOU 1205 CG GLN A 163 8926 7815 8110 1033 74 358 C
ATOM 1206 CD GLN A 163 37.694 161.923 24.065 1.00 79.10 C
ANISOU 1206 CD GLN A 163 10609 9561 9885 1078 101 299 C
ATOM 1207 OE1 GLN A 163 37.617 160.927 23.341 1.00 74.38 O
ANISOU 1207 OE1 GLN A 163 9924 9059 9277 1073 89 271 O
ATOM 1208 NE2 GLN A 163 38.515 162.929 23.769 1.00 67.13 N
ANISOU 1208 NE2 GLN A 163 9147 7944 8415 1122 142 279 N
ATOM 1209 N VAL A 164 32.422 162.617 24.925 1.00 57.05 N
ANISOU 1209 N VAL A 164 8026 6611 7038 738 156 296 N
ATOM 1210 CA VAL A 164 31.074 162.480 24.366 1.00 56.47 C
ANISOU 1210 CA VAL A 164 7993 6472 6990 658 187 258 C
ATOM 1211 C VAL A 164 31.106 162.830 22.870 1.00 59.28 C
ANISOU 1211 C VAL A 164 8322 6840 7364 638 196 173 C
ATOM 1212 O VAL A 164 31.934 163.645 22.454 1.00 58.17 O
ANISOU 1212 O VAL A 164 8120 6783 7199 657 181 148 O
ATOM 1213 CB VAL A 164 29.979 163.323 25.102 1.00 59.67 C
ANISOU 1213 CB VAL A 164 8398 6911 7362 575 187 275 C
ATOM 1214 CG1 VAL A 164 29.765 162.872 26.546 1.00 59.88 C
ANISOU 1214 CG1 VAL A 164 8469 6917 7366 590 190 359 C
ATOM 1215 CG2 VAL A 164 30.255 164.824 25.026 1.00 58.82 C
ANISOU 1215 CG2 VAL A 164 8223 6918 7208 546 159 246 C
ATOM 1216 N ALA A 165 30.198 162.229 22.073 1.00 56.03 N
ANISOU 1216 N ALA A 165 7955 6345 6990 598 220 129 N
ATOM 1217 CA ALA A 165 30.041 162.558 20.655 1.00 55.80 C
ANISOU 1217 CA ALA A 165 7914 6323 6966 572 225 48 C
ATOM 1218 C ALA A 165 29.418 163.957 20.684 1.00 59.82 C
ANISOU 1218 C ALA A 165 8378 6914 7436 499 208 31 C
ATOM 1219 O ALA A 165 28.269 164.118 21.100 1.00 59.68 O
ANISOU 1219 O ALA A 165 8377 6872 7428 431 209 33 O
ATOM 1220 CB ALA A 165 29.185 161.509 19.949 1.00 56.95 C
ANISOU 1220 CB ALA A 165 8124 6355 7160 544 244 8 C
ATOM 1221 N CYS A 166 30.234 164.978 20.396 1.00 56.21 N
ANISOU 1221 N CYS A 166 7863 6553 6942 515 194 21 N
ATOM 1222 CA CYS A 166 29.843 166.383 20.468 1.00 55.22 C
ANISOU 1222 CA CYS A 166 7695 6505 6780 456 177 13 C
ATOM 1223 C CYS A 166 28.734 166.770 19.481 1.00 58.14 C
ANISOU 1223 C CYS A 166 8078 6859 7154 391 178 -42 C
ATOM 1224 O CYS A 166 29.003 167.171 18.345 1.00 58.09 O
ANISOU 1224 O CYS A 166 8060 6880 7133 392 179 -89 O
ATOM 1225 CB CYS A 166 31.056 167.295 20.326 1.00 55.51 C
ANISOU 1225 CB CYS A 166 7670 6635 6786 485 165 11 C
ATOM 1226 SG CYS A 166 30.774 168.991 20.891 1.00 58.76 S
ANISOU 1226 SG CYS A 166 8036 7134 7157 423 140 20 S
ATOM 1227 N LEU A 167 27.475 166.655 19.958 1.00 53.27 N
ANISOU 1227 N LEU A 167 7483 6200 6555 335 178 -33 N
ATOM 1228 CA LEU A 167 26.239 167.003 19.246 1.00 51.81 C
ANISOU 1228 CA LEU A 167 7303 6001 6382 269 171 -77 C
ATOM 1229 C LEU A 167 25.379 167.861 20.167 1.00 53.23 C
ANISOU 1229 C LEU A 167 7458 6216 6553 219 166 -48 C
ATOM 1230 O LEU A 167 25.140 167.468 21.315 1.00 53.24 O
ANISOU 1230 O LEU A 167 7472 6194 6562 217 180 1 O
ATOM 1231 CB LEU A 167 25.472 165.746 18.775 1.00 52.28 C
ANISOU 1231 CB LEU A 167 7410 5961 6492 250 180 -105 C
ATOM 1232 CG LEU A 167 26.179 164.826 17.764 1.00 57.30 C
ANISOU 1232 CG LEU A 167 8083 6551 7139 299 187 -147 C
ATOM 1233 CD1 LEU A 167 25.503 163.475 17.698 1.00 57.85 C
ANISOU 1233 CD1 LEU A 167 8207 6508 7266 284 198 -161 C
ATOM 1234 CD2 LEU A 167 26.250 165.458 16.371 1.00 59.34 C
ANISOU 1234 CD2 LEU A 167 8333 6852 7364 293 173 -213 C
ATOM 1235 N PHE A 168 24.936 169.039 19.669 1.00 47.13 N
ANISOU 1235 N PHE A 168 6654 5496 5759 183 148 -77 N
ATOM 1236 CA PHE A 168 24.163 170.052 20.397 1.00 45.28 C
ANISOU 1236 CA PHE A 168 6392 5299 5512 141 144 -60 C
ATOM 1237 C PHE A 168 23.012 169.472 21.239 1.00 49.13 C
ANISOU 1237 C PHE A 168 6893 5738 6037 105 165 -35 C
ATOM 1238 O PHE A 168 22.958 169.754 22.440 1.00 49.25 O
ANISOU 1238 O PHE A 168 6903 5774 6034 104 180 9 O
ATOM 1239 CB PHE A 168 23.608 171.129 19.437 1.00 45.92 C
ANISOU 1239 CB PHE A 168 6449 5417 5583 109 122 -104 C
ATOM 1240 CG PHE A 168 23.025 172.356 20.111 1.00 46.44 C
ANISOU 1240 CG PHE A 168 6485 5528 5634 80 118 -90 C
ATOM 1241 CD1 PHE A 168 21.723 172.351 20.604 1.00 49.43 C
ANISOU 1241 CD1 PHE A 168 6854 5885 6043 40 127 -86 C
ATOM 1242 CD2 PHE A 168 23.772 173.520 20.238 1.00 47.79 C
ANISOU 1242 CD2 PHE A 168 6634 5760 5765 92 108 -84 C
ATOM 1243 CE1 PHE A 168 21.195 173.476 21.251 1.00 49.85 C
ANISOU 1243 CE1 PHE A 168 6881 5978 6083 22 129 -76 C
ATOM 1244 CE2 PHE A 168 23.233 174.655 20.862 1.00 50.37 C
ANISOU 1244 CE2 PHE A 168 6940 6120 6079 69 105 -78 C
ATOM 1245 CZ PHE A 168 21.950 174.624 21.364 1.00 48.56 C
ANISOU 1245 CZ PHE A 168 6705 5869 5876 38 116 -75 C
ATOM 1246 N GLU A 169 22.094 168.693 20.625 1.00 45.04 N
ANISOU 1246 N GLU A 169 6389 5157 5568 71 167 -64 N
ATOM 1247 CA GLU A 169 20.916 168.163 21.324 1.00 45.18 C
ANISOU 1247 CA GLU A 169 6410 5126 5632 25 192 -42 C
ATOM 1248 C GLU A 169 21.255 167.073 22.363 1.00 50.10 C
ANISOU 1248 C GLU A 169 7072 5696 6266 47 227 16 C
ATOM 1249 O GLU A 169 20.413 166.763 23.216 1.00 50.55 O
ANISOU 1249 O GLU A 169 7133 5724 6350 12 260 52 O
ATOM 1250 CB GLU A 169 19.857 167.657 20.333 1.00 46.76 C
ANISOU 1250 CB GLU A 169 6606 5273 5887 -24 177 -94 C
ATOM 1251 CG GLU A 169 19.072 168.792 19.684 1.00 54.70 C
ANISOU 1251 CG GLU A 169 7565 6331 6888 -56 146 -134 C
ATOM 1252 CD GLU A 169 17.707 168.467 19.103 1.00 69.80 C
ANISOU 1252 CD GLU A 169 9455 8205 8861 -116 129 -174 C
ATOM 1253 OE1 GLU A 169 17.206 167.338 19.314 1.00 61.48 O
ANISOU 1253 OE1 GLU A 169 8417 7078 7865 -147 148 -170 O
ATOM 1254 OE2 GLU A 169 17.110 169.373 18.479 1.00 56.08 O
ANISOU 1254 OE2 GLU A 169 7679 6510 7117 -132 95 -207 O
ATOM 1255 N ASP A 170 22.487 166.546 22.335 1.00 46.02 N
ANISOU 1255 N ASP A 170 6585 5171 5730 107 223 31 N
ATOM 1256 CA ASP A 170 22.923 165.535 23.292 1.00 46.47 C
ANISOU 1256 CA ASP A 170 6685 5178 5793 141 250 92 C
ATOM 1257 C ASP A 170 23.556 166.170 24.544 1.00 48.03 C
ANISOU 1257 C ASP A 170 6876 5444 5931 175 251 150 C
ATOM 1258 O ASP A 170 23.576 165.528 25.594 1.00 48.71 O
ANISOU 1258 O ASP A 170 6997 5499 6012 190 276 212 O
ATOM 1259 CB ASP A 170 23.913 164.552 22.632 1.00 49.56 C
ANISOU 1259 CB ASP A 170 7111 5520 6200 198 243 79 C
ATOM 1260 CG ASP A 170 23.320 163.686 21.527 1.00 66.55 C
ANISOU 1260 CG ASP A 170 9288 7588 8410 169 243 22 C
ATOM 1261 OD1 ASP A 170 22.842 164.249 20.515 1.00 68.15 O
ANISOU 1261 OD1 ASP A 170 9465 7815 8612 134 220 -40 O
ATOM 1262 OD2 ASP A 170 23.392 162.447 21.645 1.00 76.09 O
ANISOU 1262 OD2 ASP A 170 10546 8705 9660 184 263 39 O
ATOM 1263 N VAL A 171 24.067 167.409 24.449 1.00 41.72 N
ANISOU 1263 N VAL A 171 6035 4732 5083 185 224 130 N
ATOM 1264 CA VAL A 171 24.741 168.036 25.595 1.00 40.91 C
ANISOU 1264 CA VAL A 171 5926 4695 4921 215 216 174 C
ATOM 1265 C VAL A 171 23.925 169.193 26.232 1.00 43.15 C
ANISOU 1265 C VAL A 171 6187 5031 5177 171 223 172 C
ATOM 1266 O VAL A 171 24.012 169.393 27.448 1.00 43.36 O
ANISOU 1266 O VAL A 171 6229 5086 5159 182 232 216 O
ATOM 1267 CB VAL A 171 26.191 168.497 25.261 1.00 44.10 C
ANISOU 1267 CB VAL A 171 6304 5159 5293 268 179 161 C
ATOM 1268 CG1 VAL A 171 27.115 167.302 25.059 1.00 44.41 C
ANISOU 1268 CG1 VAL A 171 6368 5152 5353 330 179 181 C
ATOM 1269 CG2 VAL A 171 26.241 169.432 24.053 1.00 43.07 C
ANISOU 1269 CG2 VAL A 171 6133 5066 5165 245 161 99 C
ATOM 1270 N VAL A 172 23.171 169.954 25.422 1.00 37.52 N
ANISOU 1270 N VAL A 172 5441 4332 4484 127 217 122 N
ATOM 1271 CA VAL A 172 22.386 171.095 25.891 1.00 36.71 C
ANISOU 1271 CA VAL A 172 5312 4273 4361 92 224 113 C
ATOM 1272 C VAL A 172 20.934 170.625 26.127 1.00 42.27 C
ANISOU 1272 C VAL A 172 6018 4930 5113 44 265 121 C
ATOM 1273 O VAL A 172 20.330 170.081 25.201 1.00 43.56 O
ANISOU 1273 O VAL A 172 6174 5045 5332 16 264 91 O
ATOM 1274 CB VAL A 172 22.466 172.308 24.912 1.00 39.74 C
ANISOU 1274 CB VAL A 172 5657 4703 4740 80 192 59 C
ATOM 1275 CG1 VAL A 172 21.936 173.588 25.559 1.00 38.93 C
ANISOU 1275 CG1 VAL A 172 5534 4648 4609 59 196 53 C
ATOM 1276 CG2 VAL A 172 23.888 172.520 24.388 1.00 39.28 C
ANISOU 1276 CG2 VAL A 172 5592 4677 4655 120 160 48 C
ATOM 1277 N PRO A 173 20.363 170.780 27.349 1.00 38.73 N
ANISOU 1277 N PRO A 173 5580 4493 4642 32 304 159 N
ATOM 1278 CA PRO A 173 18.980 170.325 27.579 1.00 38.68 C
ANISOU 1278 CA PRO A 173 5565 4444 4688 -17 352 170 C
ATOM 1279 C PRO A 173 17.951 171.237 26.903 1.00 41.82 C
ANISOU 1279 C PRO A 173 5905 4862 5120 -57 345 118 C
ATOM 1280 O PRO A 173 18.119 172.457 26.890 1.00 40.77 O
ANISOU 1280 O PRO A 173 5751 4788 4951 -45 323 93 O
ATOM 1281 CB PRO A 173 18.839 170.363 29.110 1.00 40.67 C
ANISOU 1281 CB PRO A 173 5846 4716 4889 -8 399 227 C
ATOM 1282 CG PRO A 173 20.204 170.634 29.646 1.00 44.87 C
ANISOU 1282 CG PRO A 173 6409 5293 5345 48 365 248 C
ATOM 1283 CD PRO A 173 20.926 171.375 28.575 1.00 39.89 C
ANISOU 1283 CD PRO A 173 5746 4696 4715 61 307 192 C
ATOM 1284 N MET A 174 16.881 170.642 26.351 1.00 38.36 N
ANISOU 1284 N MET A 174 5443 4376 4758 -103 359 101 N
ATOM 1285 CA MET A 174 15.825 171.364 25.648 1.00 37.85 C
ANISOU 1285 CA MET A 174 5318 4327 4736 -138 345 54 C
ATOM 1286 C MET A 174 15.012 172.245 26.580 1.00 41.49 C
ANISOU 1286 C MET A 174 5748 4830 5185 -148 387 66 C
ATOM 1287 O MET A 174 14.581 173.312 26.146 1.00 41.23 O
ANISOU 1287 O MET A 174 5672 4835 5157 -149 364 28 O
ATOM 1288 CB MET A 174 14.913 170.403 24.892 1.00 41.16 C
ANISOU 1288 CB MET A 174 5715 4682 5241 -187 344 32 C
ATOM 1289 CG MET A 174 14.358 170.987 23.612 1.00 45.67 C
ANISOU 1289 CG MET A 174 6238 5269 5845 -205 289 -32 C
ATOM 1290 SD MET A 174 15.569 171.779 22.514 1.00 50.08 S
ANISOU 1290 SD MET A 174 6817 5869 6340 -156 221 -70 S
ATOM 1291 CE MET A 174 16.245 170.374 21.708 1.00 47.07 C
ANISOU 1291 CE MET A 174 6485 5423 5978 -151 201 -85 C
ATOM 1292 N ASN A 175 14.852 171.847 27.868 1.00 38.45 N
ANISOU 1292 N ASN A 175 5390 4440 4779 -149 450 120 N
ATOM 1293 CA ASN A 175 14.131 172.639 28.876 1.00 38.27 C
ANISOU 1293 CA ASN A 175 5347 4459 4734 -152 502 133 C
ATOM 1294 C ASN A 175 14.887 173.951 29.170 1.00 41.27 C
ANISOU 1294 C ASN A 175 5740 4904 5035 -108 472 114 C
ATOM 1295 O ASN A 175 14.252 174.940 29.537 1.00 41.92 O
ANISOU 1295 O ASN A 175 5794 5024 5110 -108 494 95 O
ATOM 1296 CB ASN A 175 13.852 171.843 30.172 1.00 39.52 C
ANISOU 1296 CB ASN A 175 5543 4597 4877 -161 582 200 C
ATOM 1297 CG ASN A 175 15.035 171.189 30.861 1.00 56.32 C
ANISOU 1297 CG ASN A 175 7750 6715 6935 -123 579 251 C
ATOM 1298 OD1 ASN A 175 16.206 171.503 30.628 1.00 55.76 O
ANISOU 1298 OD1 ASN A 175 7705 6670 6813 -81 521 239 O
ATOM 1299 ND2 ASN A 175 14.744 170.284 31.772 1.00 41.13 N
ANISOU 1299 ND2 ASN A 175 5863 4756 5008 -134 644 315 N
ATOM 1300 N TYR A 176 16.225 173.968 28.970 1.00 35.88 N
ANISOU 1300 N TYR A 176 5097 4233 4301 -73 423 114 N
ATOM 1301 CA TYR A 176 17.030 175.183 29.112 1.00 34.82 C
ANISOU 1301 CA TYR A 176 4972 4155 4105 -41 386 91 C
ATOM 1302 C TYR A 176 16.790 176.084 27.887 1.00 37.90 C
ANISOU 1302 C TYR A 176 5316 4554 4529 -49 341 36 C
ATOM 1303 O TYR A 176 16.570 177.281 28.038 1.00 36.74 O
ANISOU 1303 O TYR A 176 5154 4442 4365 -42 337 11 O
ATOM 1304 CB TYR A 176 18.539 174.863 29.280 1.00 35.66 C
ANISOU 1304 CB TYR A 176 5122 4272 4154 -4 348 111 C
ATOM 1305 CG TYR A 176 19.434 176.055 29.002 1.00 36.82 C
ANISOU 1305 CG TYR A 176 5262 4467 4261 16 297 76 C
ATOM 1306 CD1 TYR A 176 19.729 176.979 30.001 1.00 38.97 C
ANISOU 1306 CD1 TYR A 176 5553 4786 4469 31 299 74 C
ATOM 1307 CD2 TYR A 176 19.932 176.296 27.724 1.00 36.95 C
ANISOU 1307 CD2 TYR A 176 5255 4480 4303 16 250 43 C
ATOM 1308 CE1 TYR A 176 20.508 178.106 29.739 1.00 39.02 C
ANISOU 1308 CE1 TYR A 176 5551 4828 4448 40 253 39 C
ATOM 1309 CE2 TYR A 176 20.689 177.433 27.443 1.00 37.48 C
ANISOU 1309 CE2 TYR A 176 5315 4586 4341 27 212 14 C
ATOM 1310 CZ TYR A 176 20.970 178.339 28.454 1.00 44.13 C
ANISOU 1310 CZ TYR A 176 6171 5468 5129 36 212 12 C
ATOM 1311 OH TYR A 176 21.733 179.451 28.188 1.00 43.60 O
ANISOU 1311 OH TYR A 176 6095 5431 5040 39 174 -17 O
ATOM 1312 N MET A 177 16.869 175.502 26.680 1.00 35.01 N
ANISOU 1312 N MET A 177 4936 4156 4209 -61 306 18 N
ATOM 1313 CA MET A 177 16.708 176.203 25.408 1.00 34.97 C
ANISOU 1313 CA MET A 177 4899 4159 4229 -65 259 -28 C
ATOM 1314 C MET A 177 15.320 176.836 25.263 1.00 39.32 C
ANISOU 1314 C MET A 177 5398 4714 4827 -86 272 -51 C
ATOM 1315 O MET A 177 15.223 177.989 24.837 1.00 38.79 O
ANISOU 1315 O MET A 177 5313 4673 4752 -75 245 -78 O
ATOM 1316 CB MET A 177 16.972 175.250 24.216 1.00 37.44 C
ANISOU 1316 CB MET A 177 5217 4434 4575 -73 226 -43 C
ATOM 1317 CG MET A 177 18.435 174.861 24.027 1.00 41.09 C
ANISOU 1317 CG MET A 177 5719 4898 4995 -41 204 -32 C
ATOM 1318 SD MET A 177 19.633 176.232 24.101 1.00 45.42 S
ANISOU 1318 SD MET A 177 6272 5506 5478 -10 175 -41 S
ATOM 1319 CE MET A 177 19.118 177.211 22.706 1.00 41.93 C
ANISOU 1319 CE MET A 177 5801 5073 5058 -23 138 -86 C
ATOM 1320 N VAL A 178 14.259 176.094 25.628 1.00 36.38 N
ANISOU 1320 N VAL A 178 5001 4316 4507 -117 314 -37 N
ATOM 1321 CA VAL A 178 12.878 176.561 25.498 1.00 36.46 C
ANISOU 1321 CA VAL A 178 4947 4331 4575 -137 329 -57 C
ATOM 1322 C VAL A 178 12.500 177.544 26.638 1.00 41.18 C
ANISOU 1322 C VAL A 178 5537 4965 5143 -118 379 -49 C
ATOM 1323 O VAL A 178 12.148 178.685 26.340 1.00 40.89 O
ANISOU 1323 O VAL A 178 5472 4953 5110 -101 359 -78 O
ATOM 1324 CB VAL A 178 11.883 175.371 25.395 1.00 40.66 C
ANISOU 1324 CB VAL A 178 5444 4820 5186 -184 357 -48 C
ATOM 1325 CG1 VAL A 178 10.426 175.842 25.393 1.00 41.07 C
ANISOU 1325 CG1 VAL A 178 5415 4884 5305 -205 377 -66 C
ATOM 1326 CG2 VAL A 178 12.173 174.525 24.160 1.00 40.18 C
ANISOU 1326 CG2 VAL A 178 5392 4720 5155 -201 300 -72 C
ATOM 1327 N TYR A 179 12.554 177.118 27.914 1.00 38.39 N
ANISOU 1327 N TYR A 179 5215 4615 4758 -118 443 -10 N
ATOM 1328 CA TYR A 179 12.113 177.964 29.028 1.00 38.59 C
ANISOU 1328 CA TYR A 179 5238 4674 4749 -100 498 -6 C
ATOM 1329 C TYR A 179 13.066 179.101 29.386 1.00 43.17 C
ANISOU 1329 C TYR A 179 5863 5290 5250 -61 471 -24 C
ATOM 1330 O TYR A 179 12.609 180.236 29.515 1.00 43.42 O
ANISOU 1330 O TYR A 179 5875 5343 5281 -43 477 -53 O
ATOM 1331 CB TYR A 179 11.835 177.132 30.289 1.00 39.91 C
ANISOU 1331 CB TYR A 179 5431 4835 4897 -112 580 44 C
ATOM 1332 CG TYR A 179 10.662 176.183 30.171 1.00 42.56 C
ANISOU 1332 CG TYR A 179 5714 5137 5321 -159 628 61 C
ATOM 1333 CD1 TYR A 179 9.422 176.625 29.711 1.00 44.55 C
ANISOU 1333 CD1 TYR A 179 5880 5395 5652 -177 638 31 C
ATOM 1334 CD2 TYR A 179 10.767 174.859 30.587 1.00 43.94 C
ANISOU 1334 CD2 TYR A 179 5921 5271 5503 -186 666 111 C
ATOM 1335 CE1 TYR A 179 8.328 175.764 29.631 1.00 44.91 C
ANISOU 1335 CE1 TYR A 179 5866 5411 5787 -226 681 44 C
ATOM 1336 CE2 TYR A 179 9.675 173.994 30.527 1.00 45.50 C
ANISOU 1336 CE2 TYR A 179 6068 5431 5788 -238 715 128 C
ATOM 1337 CZ TYR A 179 8.461 174.448 30.040 1.00 51.20 C
ANISOU 1337 CZ TYR A 179 6697 6164 6593 -261 722 93 C
ATOM 1338 OH TYR A 179 7.387 173.596 29.975 1.00 51.86 O
ANISOU 1338 OH TYR A 179 6720 6213 6772 -319 767 106 O
ATOM 1339 N PHE A 180 14.356 178.806 29.598 1.00 39.67 N
ANISOU 1339 N PHE A 180 5477 4851 4744 -47 442 -6 N
ATOM 1340 CA PHE A 180 15.326 179.805 30.033 1.00 39.47 C
ANISOU 1340 CA PHE A 180 5492 4859 4646 -18 414 -23 C
ATOM 1341 C PHE A 180 15.810 180.685 28.880 1.00 44.27 C
ANISOU 1341 C PHE A 180 6084 5469 5269 -12 348 -61 C
ATOM 1342 O PHE A 180 15.652 181.905 28.961 1.00 45.34 O
ANISOU 1342 O PHE A 180 6214 5618 5393 1 342 -92 O
ATOM 1343 CB PHE A 180 16.513 179.120 30.724 1.00 41.38 C
ANISOU 1343 CB PHE A 180 5791 5110 4821 -5 405 13 C
ATOM 1344 CG PHE A 180 17.389 180.006 31.571 1.00 43.02 C
ANISOU 1344 CG PHE A 180 6041 5358 4946 20 386 0 C
ATOM 1345 CD1 PHE A 180 17.104 180.210 32.917 1.00 46.61 C
ANISOU 1345 CD1 PHE A 180 6532 5837 5340 33 435 11 C
ATOM 1346 CD2 PHE A 180 18.533 180.594 31.040 1.00 45.00 C
ANISOU 1346 CD2 PHE A 180 6298 5622 5178 28 321 -23 C
ATOM 1347 CE1 PHE A 180 17.927 181.016 33.709 1.00 47.67 C
ANISOU 1347 CE1 PHE A 180 6709 6008 5394 54 410 -8 C
ATOM 1348 CE2 PHE A 180 19.360 181.395 31.833 1.00 48.22 C
ANISOU 1348 CE2 PHE A 180 6740 6065 5515 44 298 -39 C
ATOM 1349 CZ PHE A 180 19.050 181.603 33.162 1.00 46.81 C
ANISOU 1349 CZ PHE A 180 6600 5911 5275 56 338 -34 C
ATOM 1350 N ASN A 181 16.389 180.095 27.819 1.00 39.71 N
ANISOU 1350 N ASN A 181 5501 4873 4713 -20 302 -59 N
ATOM 1351 CA ASN A 181 16.938 180.881 26.715 1.00 39.73 C
ANISOU 1351 CA ASN A 181 5496 4878 4720 -15 246 -88 C
ATOM 1352 C ASN A 181 15.861 181.550 25.834 1.00 44.73 C
ANISOU 1352 C ASN A 181 6085 5501 5408 -20 234 -115 C
ATOM 1353 O ASN A 181 15.965 182.758 25.599 1.00 45.27 O
ANISOU 1353 O ASN A 181 6155 5579 5468 -7 213 -138 O
ATOM 1354 CB ASN A 181 17.889 180.060 25.844 1.00 40.12 C
ANISOU 1354 CB ASN A 181 5558 4916 4770 -17 209 -79 C
ATOM 1355 CG ASN A 181 18.749 180.924 24.954 1.00 62.29 C
ANISOU 1355 CG ASN A 181 8369 7737 7563 -9 163 -100 C
ATOM 1356 OD1 ASN A 181 18.474 181.099 23.764 1.00 59.41 O
ANISOU 1356 OD1 ASN A 181 7987 7360 7227 -14 136 -116 O
ATOM 1357 ND2 ASN A 181 19.787 181.518 25.521 1.00 53.41 N
ANISOU 1357 ND2 ASN A 181 7267 6638 6391 1 152 -98 N
ATOM 1358 N PHE A 182 14.853 180.796 25.341 1.00 39.76 N
ANISOU 1358 N PHE A 182 5417 4851 4839 -38 242 -114 N
ATOM 1359 CA PHE A 182 13.833 181.394 24.482 1.00 38.78 C
ANISOU 1359 CA PHE A 182 5245 4722 4767 -38 220 -140 C
ATOM 1360 C PHE A 182 12.847 182.280 25.256 1.00 43.37 C
ANISOU 1360 C PHE A 182 5796 5316 5365 -24 260 -150 C
ATOM 1361 O PHE A 182 12.857 183.488 25.039 1.00 43.41 O
ANISOU 1361 O PHE A 182 5804 5329 5363 -1 240 -170 O
ATOM 1362 CB PHE A 182 13.065 180.332 23.667 1.00 40.16 C
ANISOU 1362 CB PHE A 182 5382 4874 5004 -66 205 -143 C
ATOM 1363 CG PHE A 182 11.999 180.841 22.714 1.00 41.19 C
ANISOU 1363 CG PHE A 182 5457 5004 5189 -65 168 -170 C
ATOM 1364 CD1 PHE A 182 12.192 182.012 21.979 1.00 43.38 C
ANISOU 1364 CD1 PHE A 182 5741 5293 5449 -38 123 -187 C
ATOM 1365 CD2 PHE A 182 10.830 180.119 22.506 1.00 42.94 C
ANISOU 1365 CD2 PHE A 182 5620 5213 5482 -93 173 -177 C
ATOM 1366 CE1 PHE A 182 11.216 182.467 21.085 1.00 44.05 C
ANISOU 1366 CE1 PHE A 182 5778 5378 5580 -29 81 -206 C
ATOM 1367 CE2 PHE A 182 9.862 180.567 21.598 1.00 45.53 C
ANISOU 1367 CE2 PHE A 182 5892 5547 5861 -89 127 -202 C
ATOM 1368 CZ PHE A 182 10.063 181.735 20.893 1.00 43.27 C
ANISOU 1368 CZ PHE A 182 5616 5274 5550 -53 79 -216 C
ATOM 1369 N PHE A 183 11.987 181.693 26.115 1.00 40.04 N
ANISOU 1369 N PHE A 183 5348 4895 4971 -37 321 -136 N
ATOM 1370 CA PHE A 183 10.915 182.403 26.815 1.00 40.24 C
ANISOU 1370 CA PHE A 183 5334 4933 5021 -22 371 -146 C
ATOM 1371 C PHE A 183 11.381 183.586 27.682 1.00 43.90 C
ANISOU 1371 C PHE A 183 5842 5415 5423 12 391 -160 C
ATOM 1372 O PHE A 183 10.943 184.707 27.426 1.00 42.82 O
ANISOU 1372 O PHE A 183 5686 5278 5305 38 379 -186 O
ATOM 1373 CB PHE A 183 10.054 181.445 27.658 1.00 42.50 C
ANISOU 1373 CB PHE A 183 5590 5218 5340 -47 445 -121 C
ATOM 1374 CG PHE A 183 9.200 180.461 26.883 1.00 44.42 C
ANISOU 1374 CG PHE A 183 5770 5439 5668 -86 434 -118 C
ATOM 1375 CD1 PHE A 183 8.840 180.708 25.562 1.00 47.19 C
ANISOU 1375 CD1 PHE A 183 6078 5784 6069 -87 362 -147 C
ATOM 1376 CD2 PHE A 183 8.732 179.301 27.484 1.00 47.50 C
ANISOU 1376 CD2 PHE A 183 6146 5814 6088 -123 493 -88 C
ATOM 1377 CE1 PHE A 183 8.055 179.799 24.850 1.00 48.27 C
ANISOU 1377 CE1 PHE A 183 6157 5901 6281 -126 343 -152 C
ATOM 1378 CE2 PHE A 183 7.945 178.391 26.769 1.00 50.66 C
ANISOU 1378 CE2 PHE A 183 6487 6188 6574 -167 479 -91 C
ATOM 1379 CZ PHE A 183 7.608 178.651 25.460 1.00 48.22 C
ANISOU 1379 CZ PHE A 183 6133 5876 6312 -168 401 -127 C
ATOM 1380 N ALA A 184 12.262 183.352 28.669 1.00 41.05 N
ANISOU 1380 N ALA A 184 5541 5065 4989 12 415 -143 N
ATOM 1381 CA ALA A 184 12.708 184.392 29.595 1.00 41.00 C
ANISOU 1381 CA ALA A 184 5582 5077 4920 39 432 -162 C
ATOM 1382 C ALA A 184 13.801 185.344 29.052 1.00 44.92 C
ANISOU 1382 C ALA A 184 6115 5570 5384 49 366 -185 C
ATOM 1383 O ALA A 184 13.738 186.534 29.352 1.00 44.02 O
ANISOU 1383 O ALA A 184 6015 5454 5256 71 369 -216 O
ATOM 1384 CB ALA A 184 13.197 183.754 30.885 1.00 41.89 C
ANISOU 1384 CB ALA A 184 5746 5209 4963 37 477 -135 C
ATOM 1385 N CYS A 185 14.800 184.845 28.305 1.00 42.44 N
ANISOU 1385 N CYS A 185 5816 5251 5060 33 314 -171 N
ATOM 1386 CA CYS A 185 15.938 185.675 27.883 1.00 42.73 C
ANISOU 1386 CA CYS A 185 5884 5286 5064 35 262 -187 C
ATOM 1387 C CYS A 185 15.846 186.257 26.450 1.00 45.31 C
ANISOU 1387 C CYS A 185 6188 5592 5435 36 215 -198 C
ATOM 1388 O CYS A 185 16.591 187.201 26.154 1.00 44.46 O
ANISOU 1388 O CYS A 185 6106 5479 5309 38 184 -212 O
ATOM 1389 CB CYS A 185 17.235 184.897 28.062 1.00 43.43 C
ANISOU 1389 CB CYS A 185 6004 5390 5107 23 240 -165 C
ATOM 1390 SG CYS A 185 17.565 184.425 29.778 1.00 48.29 S
ANISOU 1390 SG CYS A 185 6663 6034 5650 31 280 -149 S
ATOM 1391 N VAL A 186 14.970 185.724 25.575 1.00 40.47 N
ANISOU 1391 N VAL A 186 5531 4968 4877 32 207 -192 N
ATOM 1392 CA VAL A 186 14.843 186.258 24.219 1.00 39.87 C
ANISOU 1392 CA VAL A 186 5440 4877 4831 38 158 -199 C
ATOM 1393 C VAL A 186 13.435 186.858 24.002 1.00 44.89 C
ANISOU 1393 C VAL A 186 6030 5503 5522 60 164 -214 C
ATOM 1394 O VAL A 186 13.333 188.020 23.617 1.00 44.25 O
ANISOU 1394 O VAL A 186 5957 5408 5449 83 143 -226 O
ATOM 1395 CB VAL A 186 15.216 185.207 23.129 1.00 43.20 C
ANISOU 1395 CB VAL A 186 5856 5296 5260 19 123 -185 C
ATOM 1396 CG1 VAL A 186 14.798 185.661 21.726 1.00 42.61 C
ANISOU 1396 CG1 VAL A 186 5766 5210 5213 28 74 -193 C
ATOM 1397 CG2 VAL A 186 16.711 184.894 23.167 1.00 42.54 C
ANISOU 1397 CG2 VAL A 186 5814 5221 5126 9 112 -173 C
ATOM 1398 N LEU A 187 12.373 186.085 24.260 1.00 43.32 N
ANISOU 1398 N LEU A 187 5782 5310 5367 54 194 -210 N
ATOM 1399 CA LEU A 187 10.989 186.490 24.027 1.00 44.53 C
ANISOU 1399 CA LEU A 187 5873 5461 5585 74 199 -223 C
ATOM 1400 C LEU A 187 10.537 187.653 24.927 1.00 49.15 C
ANISOU 1400 C LEU A 187 6460 6045 6170 110 241 -241 C
ATOM 1401 O LEU A 187 10.004 188.627 24.387 1.00 49.92 O
ANISOU 1401 O LEU A 187 6538 6129 6300 143 216 -255 O
ATOM 1402 CB LEU A 187 10.048 185.285 24.174 1.00 45.31 C
ANISOU 1402 CB LEU A 187 5912 5566 5735 48 227 -214 C
ATOM 1403 CG LEU A 187 8.748 185.333 23.366 1.00 51.09 C
ANISOU 1403 CG LEU A 187 6565 6300 6548 56 198 -226 C
ATOM 1404 CD1 LEU A 187 9.013 185.409 21.871 1.00 51.01 C
ANISOU 1404 CD1 LEU A 187 6562 6281 6538 57 112 -231 C
ATOM 1405 CD2 LEU A 187 7.889 184.120 23.665 1.00 54.69 C
ANISOU 1405 CD2 LEU A 187 6960 6760 7060 19 234 -219 C
ATOM 1406 N VAL A 188 10.762 187.580 26.263 1.00 44.98 N
ANISOU 1406 N VAL A 188 5960 5528 5601 108 303 -243 N
ATOM 1407 CA VAL A 188 10.397 188.662 27.197 1.00 45.39 C
ANISOU 1407 CA VAL A 188 6026 5579 5642 144 348 -268 C
ATOM 1408 C VAL A 188 11.099 189.990 26.756 1.00 48.77 C
ANISOU 1408 C VAL A 188 6502 5979 6049 165 302 -288 C
ATOM 1409 O VAL A 188 10.364 190.947 26.498 1.00 48.46 O
ANISOU 1409 O VAL A 188 6442 5920 6050 204 300 -305 O
ATOM 1410 CB VAL A 188 10.650 188.309 28.695 1.00 49.54 C
ANISOU 1410 CB VAL A 188 6589 6126 6109 138 417 -267 C
ATOM 1411 CG1 VAL A 188 10.691 189.560 29.578 1.00 49.65 C
ANISOU 1411 CG1 VAL A 188 6645 6133 6086 174 448 -304 C
ATOM 1412 CG2 VAL A 188 9.604 187.323 29.208 1.00 49.83 C
ANISOU 1412 CG2 VAL A 188 6570 6181 6183 127 483 -248 C
ATOM 1413 N PRO A 189 12.455 190.059 26.560 1.00 44.64 N
ANISOU 1413 N PRO A 189 6037 5451 5472 142 264 -282 N
ATOM 1414 CA PRO A 189 13.072 191.324 26.105 1.00 43.98 C
ANISOU 1414 CA PRO A 189 5995 5336 5379 153 226 -297 C
ATOM 1415 C PRO A 189 12.562 191.819 24.747 1.00 47.02 C
ANISOU 1415 C PRO A 189 6353 5695 5815 173 179 -288 C
ATOM 1416 O PRO A 189 12.456 193.035 24.567 1.00 46.59 O
ANISOU 1416 O PRO A 189 6321 5606 5774 201 168 -301 O
ATOM 1417 CB PRO A 189 14.558 190.980 26.027 1.00 45.03 C
ANISOU 1417 CB PRO A 189 6174 5478 5458 115 196 -285 C
ATOM 1418 CG PRO A 189 14.732 189.877 26.984 1.00 49.40 C
ANISOU 1418 CG PRO A 189 6728 6066 5977 98 231 -276 C
ATOM 1419 CD PRO A 189 13.503 189.046 26.811 1.00 45.31 C
ANISOU 1419 CD PRO A 189 6151 5557 5508 105 258 -262 C
ATOM 1420 N LEU A 190 12.217 190.902 23.807 1.00 43.01 N
ANISOU 1420 N LEU A 190 5805 5204 5335 161 149 -265 N
ATOM 1421 CA LEU A 190 11.679 191.306 22.498 1.00 42.49 C
ANISOU 1421 CA LEU A 190 5715 5122 5309 183 97 -255 C
ATOM 1422 C LEU A 190 10.317 191.976 22.667 1.00 45.86 C
ANISOU 1422 C LEU A 190 6093 5538 5795 232 112 -270 C
ATOM 1423 O LEU A 190 10.109 193.049 22.105 1.00 45.04 O
ANISOU 1423 O LEU A 190 6002 5404 5709 268 82 -270 O
ATOM 1424 CB LEU A 190 11.577 190.140 21.506 1.00 42.32 C
ANISOU 1424 CB LEU A 190 5663 5120 5297 159 58 -237 C
ATOM 1425 CG LEU A 190 12.863 189.683 20.810 1.00 47.37 C
ANISOU 1425 CG LEU A 190 6350 5763 5887 126 27 -220 C
ATOM 1426 CD1 LEU A 190 12.586 188.470 19.926 1.00 47.94 C
ANISOU 1426 CD1 LEU A 190 6392 5852 5971 107 -4 -213 C
ATOM 1427 CD2 LEU A 190 13.495 190.797 19.971 1.00 50.14 C
ANISOU 1427 CD2 LEU A 190 6747 6088 6216 139 -9 -210 C
ATOM 1428 N LEU A 191 9.415 191.374 23.486 1.00 42.12 N
ANISOU 1428 N LEU A 191 5564 5089 5352 234 163 -280 N
ATOM 1429 CA LEU A 191 8.092 191.929 23.781 1.00 42.13 C
ANISOU 1429 CA LEU A 191 5504 5087 5415 282 191 -296 C
ATOM 1430 C LEU A 191 8.216 193.300 24.487 1.00 47.92 C
ANISOU 1430 C LEU A 191 6285 5788 6135 325 222 -321 C
ATOM 1431 O LEU A 191 7.397 194.191 24.223 1.00 48.63 O
ANISOU 1431 O LEU A 191 6347 5855 6275 379 214 -331 O
ATOM 1432 CB LEU A 191 7.241 190.953 24.611 1.00 41.97 C
ANISOU 1432 CB LEU A 191 5418 5102 5427 267 254 -299 C
ATOM 1433 CG LEU A 191 6.723 189.689 23.886 1.00 45.92 C
ANISOU 1433 CG LEU A 191 5852 5626 5970 231 224 -282 C
ATOM 1434 CD1 LEU A 191 6.163 188.687 24.874 1.00 46.16 C
ANISOU 1434 CD1 LEU A 191 5837 5682 6021 202 299 -278 C
ATOM 1435 CD2 LEU A 191 5.664 190.017 22.830 1.00 47.25 C
ANISOU 1435 CD2 LEU A 191 5946 5795 6212 264 166 -284 C
ATOM 1436 N LEU A 192 9.273 193.487 25.321 1.00 44.48 N
ANISOU 1436 N LEU A 192 5923 5345 5632 301 249 -334 N
ATOM 1437 CA LEU A 192 9.561 194.759 26.000 1.00 44.93 C
ANISOU 1437 CA LEU A 192 6038 5364 5668 331 272 -365 C
ATOM 1438 C LEU A 192 9.959 195.821 24.974 1.00 49.07 C
ANISOU 1438 C LEU A 192 6602 5837 6205 348 212 -357 C
ATOM 1439 O LEU A 192 9.425 196.923 25.027 1.00 49.02 O
ANISOU 1439 O LEU A 192 6604 5790 6233 399 219 -375 O
ATOM 1440 CB LEU A 192 10.664 194.607 27.066 1.00 44.83 C
ANISOU 1440 CB LEU A 192 6093 5361 5577 294 300 -382 C
ATOM 1441 CG LEU A 192 10.292 193.880 28.363 1.00 49.92 C
ANISOU 1441 CG LEU A 192 6726 6048 6195 289 373 -394 C
ATOM 1442 CD1 LEU A 192 11.522 193.641 29.216 1.00 49.63 C
ANISOU 1442 CD1 LEU A 192 6758 6025 6073 251 377 -402 C
ATOM 1443 CD2 LEU A 192 9.249 194.660 29.177 1.00 53.60 C
ANISOU 1443 CD2 LEU A 192 7177 6503 6685 346 438 -431 C
ATOM 1444 N MET A 193 10.853 195.469 24.014 1.00 46.09 N
ANISOU 1444 N MET A 193 6248 5461 5803 308 157 -326 N
ATOM 1445 CA MET A 193 11.299 196.344 22.916 1.00 46.06 C
ANISOU 1445 CA MET A 193 6284 5413 5805 316 103 -306 C
ATOM 1446 C MET A 193 10.126 196.760 22.051 1.00 50.00 C
ANISOU 1446 C MET A 193 6737 5896 6363 374 72 -291 C
ATOM 1447 O MET A 193 10.094 197.903 21.595 1.00 50.22 O
ANISOU 1447 O MET A 193 6802 5872 6410 409 50 -285 O
ATOM 1448 CB MET A 193 12.353 195.667 22.036 1.00 47.98 C
ANISOU 1448 CB MET A 193 6547 5673 6008 265 61 -274 C
ATOM 1449 CG MET A 193 13.707 195.579 22.652 1.00 51.98 C
ANISOU 1449 CG MET A 193 7105 6184 6460 215 76 -282 C
ATOM 1450 SD MET A 193 14.752 194.594 21.560 1.00 56.59 S
ANISOU 1450 SD MET A 193 7693 6799 7009 167 36 -244 S
ATOM 1451 CE MET A 193 15.241 193.264 22.667 1.00 52.85 C
ANISOU 1451 CE MET A 193 7204 6378 6500 130 70 -257 C
ATOM 1452 N LEU A 194 9.159 195.836 21.825 1.00 46.42 N
ANISOU 1452 N LEU A 194 6204 5487 5946 382 67 -285 N
ATOM 1453 CA LEU A 194 7.943 196.123 21.058 1.00 46.96 C
ANISOU 1453 CA LEU A 194 6211 5553 6077 438 30 -274 C
ATOM 1454 C LEU A 194 7.133 197.198 21.793 1.00 49.62 C
ANISOU 1454 C LEU A 194 6535 5856 6460 504 72 -301 C
ATOM 1455 O LEU A 194 6.707 198.166 21.170 1.00 49.34 O
ANISOU 1455 O LEU A 194 6507 5781 6459 560 37 -290 O
ATOM 1456 CB LEU A 194 7.102 194.850 20.818 1.00 47.42 C
ANISOU 1456 CB LEU A 194 6178 5667 6170 421 20 -271 C
ATOM 1457 CG LEU A 194 5.759 195.034 20.072 1.00 53.46 C
ANISOU 1457 CG LEU A 194 6861 6442 7009 476 -25 -264 C
ATOM 1458 CD1 LEU A 194 5.967 195.286 18.576 1.00 53.87 C
ANISOU 1458 CD1 LEU A 194 6941 6482 7044 488 -117 -232 C
ATOM 1459 CD2 LEU A 194 4.850 193.829 20.271 1.00 56.03 C
ANISOU 1459 CD2 LEU A 194 7086 6820 7382 453 -12 -274 C
ATOM 1460 N GLY A 195 7.005 197.039 23.111 1.00 45.54 N
ANISOU 1460 N GLY A 195 6011 5354 5938 499 147 -335 N
ATOM 1461 CA GLY A 195 6.312 197.975 23.988 1.00 45.88 C
ANISOU 1461 CA GLY A 195 6049 5369 6014 560 203 -371 C
ATOM 1462 C GLY A 195 6.928 199.360 24.019 1.00 49.10 C
ANISOU 1462 C GLY A 195 6548 5701 6406 586 195 -384 C
ATOM 1463 O GLY A 195 6.199 200.349 23.926 1.00 49.59 O
ANISOU 1463 O GLY A 195 6603 5720 6519 657 197 -394 O
ATOM 1464 N VAL A 196 8.282 199.437 24.114 1.00 44.01 N
ANISOU 1464 N VAL A 196 5987 5039 5696 527 184 -383 N
ATOM 1465 CA VAL A 196 9.066 200.684 24.146 1.00 43.15 C
ANISOU 1465 CA VAL A 196 5971 4855 5570 530 175 -396 C
ATOM 1466 C VAL A 196 8.900 201.442 22.814 1.00 47.12 C
ANISOU 1466 C VAL A 196 6487 5306 6110 566 112 -353 C
ATOM 1467 O VAL A 196 8.657 202.649 22.841 1.00 47.15 O
ANISOU 1467 O VAL A 196 6531 5238 6146 618 116 -365 O
ATOM 1468 CB VAL A 196 10.567 200.435 24.491 1.00 45.54 C
ANISOU 1468 CB VAL A 196 6341 5162 5802 450 172 -401 C
ATOM 1469 CG1 VAL A 196 11.396 201.718 24.396 1.00 45.16 C
ANISOU 1469 CG1 VAL A 196 6380 5031 5746 441 157 -412 C
ATOM 1470 CG2 VAL A 196 10.718 199.817 25.878 1.00 45.16 C
ANISOU 1470 CG2 VAL A 196 6290 5158 5709 425 230 -441 C
ATOM 1471 N TYR A 197 8.999 200.738 21.666 1.00 43.58 N
ANISOU 1471 N TYR A 197 6011 4892 5654 544 56 -305 N
ATOM 1472 CA TYR A 197 8.852 201.363 20.346 1.00 43.86 C
ANISOU 1472 CA TYR A 197 6066 4889 5710 578 -7 -259 C
ATOM 1473 C TYR A 197 7.436 201.904 20.129 1.00 50.21 C
ANISOU 1473 C TYR A 197 6814 5677 6586 671 -19 -257 C
ATOM 1474 O TYR A 197 7.301 202.973 19.542 1.00 50.77 O
ANISOU 1474 O TYR A 197 6927 5681 6681 722 -48 -234 O
ATOM 1475 CB TYR A 197 9.285 200.431 19.198 1.00 43.89 C
ANISOU 1475 CB TYR A 197 6059 4939 5678 534 -61 -214 C
ATOM 1476 CG TYR A 197 10.779 200.502 18.962 1.00 44.85 C
ANISOU 1476 CG TYR A 197 6259 5043 5740 465 -64 -197 C
ATOM 1477 CD1 TYR A 197 11.390 201.696 18.576 1.00 47.09 C
ANISOU 1477 CD1 TYR A 197 6622 5251 6020 469 -73 -176 C
ATOM 1478 CD2 TYR A 197 11.593 199.396 19.189 1.00 44.70 C
ANISOU 1478 CD2 TYR A 197 6231 5078 5673 397 -51 -203 C
ATOM 1479 CE1 TYR A 197 12.772 201.787 18.428 1.00 47.42 C
ANISOU 1479 CE1 TYR A 197 6724 5276 6016 400 -67 -163 C
ATOM 1480 CE2 TYR A 197 12.978 199.475 19.042 1.00 45.28 C
ANISOU 1480 CE2 TYR A 197 6364 5140 5700 336 -49 -190 C
ATOM 1481 CZ TYR A 197 13.563 200.673 18.665 1.00 54.94 C
ANISOU 1481 CZ TYR A 197 7658 6293 6924 335 -56 -172 C
ATOM 1482 OH TYR A 197 14.925 200.755 18.513 1.00 57.62 O
ANISOU 1482 OH TYR A 197 8044 6622 7225 271 -51 -159 O
ATOM 1483 N LEU A 198 6.406 201.230 20.673 1.00 48.03 N
ANISOU 1483 N LEU A 198 6444 5457 6350 695 9 -282 N
ATOM 1484 CA LEU A 198 5.013 201.687 20.600 1.00 49.21 C
ANISOU 1484 CA LEU A 198 6520 5601 6577 786 5 -287 C
ATOM 1485 C LEU A 198 4.840 202.992 21.374 1.00 52.58 C
ANISOU 1485 C LEU A 198 6994 5951 7032 847 54 -321 C
ATOM 1486 O LEU A 198 4.121 203.885 20.919 1.00 52.97 O
ANISOU 1486 O LEU A 198 7035 5954 7137 931 28 -308 O
ATOM 1487 CB LEU A 198 4.050 200.616 21.137 1.00 49.70 C
ANISOU 1487 CB LEU A 198 6466 5741 6676 784 39 -310 C
ATOM 1488 CG LEU A 198 3.751 199.463 20.183 1.00 54.83 C
ANISOU 1488 CG LEU A 198 7046 6456 7330 750 -24 -279 C
ATOM 1489 CD1 LEU A 198 3.280 198.241 20.945 1.00 55.21 C
ANISOU 1489 CD1 LEU A 198 7010 6573 7394 708 27 -303 C
ATOM 1490 CD2 LEU A 198 2.729 199.870 19.117 1.00 58.75 C
ANISOU 1490 CD2 LEU A 198 7483 6951 7887 824 -101 -252 C
ATOM 1491 N ARG A 199 5.543 203.111 22.517 1.00 47.99 N
ANISOU 1491 N ARG A 199 6470 5355 6410 807 120 -365 N
ATOM 1492 CA ARG A 199 5.549 204.296 23.375 1.00 48.09 C
ANISOU 1492 CA ARG A 199 6543 5292 6436 852 171 -411 C
ATOM 1493 C ARG A 199 6.267 205.480 22.687 1.00 52.03 C
ANISOU 1493 C ARG A 199 7145 5692 6932 859 128 -386 C
ATOM 1494 O ARG A 199 5.867 206.624 22.906 1.00 53.59 O
ANISOU 1494 O ARG A 199 7378 5811 7173 929 145 -406 O
ATOM 1495 CB ARG A 199 6.194 203.981 24.734 1.00 47.65 C
ANISOU 1495 CB ARG A 199 6525 5257 6322 797 241 -466 C
ATOM 1496 CG ARG A 199 5.353 203.067 25.628 1.00 58.59 C
ANISOU 1496 CG ARG A 199 7823 6722 7716 807 306 -494 C
ATOM 1497 CD ARG A 199 4.690 203.831 26.759 1.00 75.67 C
ANISOU 1497 CD ARG A 199 9994 8856 9903 875 386 -555 C
ATOM 1498 N ILE A 200 7.303 205.207 21.849 1.00 46.74 N
ANISOU 1498 N ILE A 200 6522 5024 6215 789 77 -341 N
ATOM 1499 CA ILE A 200 8.054 206.225 21.091 1.00 46.11 C
ANISOU 1499 CA ILE A 200 6537 4854 6129 782 40 -305 C
ATOM 1500 C ILE A 200 7.131 206.836 20.024 1.00 49.95 C
ANISOU 1500 C ILE A 200 7005 5303 6670 872 -12 -255 C
ATOM 1501 O ILE A 200 7.038 208.065 19.930 1.00 49.76 O
ANISOU 1501 O ILE A 200 7044 5181 6682 925 -13 -250 O
ATOM 1502 CB ILE A 200 9.370 205.660 20.458 1.00 47.65 C
ANISOU 1502 CB ILE A 200 6774 5074 6259 684 9 -268 C
ATOM 1503 CG1 ILE A 200 10.430 205.356 21.539 1.00 47.12 C
ANISOU 1503 CG1 ILE A 200 6740 5022 6141 602 53 -317 C
ATOM 1504 CG2 ILE A 200 9.941 206.606 19.380 1.00 47.37 C
ANISOU 1504 CG2 ILE A 200 6819 4955 6223 683 -33 -211 C
ATOM 1505 CD1 ILE A 200 11.610 204.451 21.079 1.00 50.31 C
ANISOU 1505 CD1 ILE A 200 7151 5479 6484 509 31 -287 C
ATOM 1506 N PHE A 201 6.449 205.970 19.239 1.00 46.07 N
ANISOU 1506 N PHE A 201 6429 4888 6186 890 -60 -219 N
ATOM 1507 CA PHE A 201 5.536 206.379 18.171 1.00 46.66 C
ANISOU 1507 CA PHE A 201 6476 4948 6306 975 -125 -169 C
ATOM 1508 C PHE A 201 4.315 207.127 18.733 1.00 52.75 C
ANISOU 1508 C PHE A 201 7199 5683 7160 1084 -98 -200 C
ATOM 1509 O PHE A 201 3.862 208.078 18.097 1.00 54.06 O
ANISOU 1509 O PHE A 201 7391 5783 7367 1165 -137 -165 O
ATOM 1510 CB PHE A 201 5.113 205.179 17.296 1.00 47.64 C
ANISOU 1510 CB PHE A 201 6516 5171 6415 959 -185 -137 C
ATOM 1511 CG PHE A 201 6.247 204.543 16.516 1.00 48.10 C
ANISOU 1511 CG PHE A 201 6627 5256 6393 871 -218 -100 C
ATOM 1512 CD1 PHE A 201 7.078 205.313 15.704 1.00 51.49 C
ANISOU 1512 CD1 PHE A 201 7159 5618 6786 859 -244 -49 C
ATOM 1513 CD2 PHE A 201 6.463 203.171 16.563 1.00 49.46 C
ANISOU 1513 CD2 PHE A 201 6746 5518 6530 802 -217 -113 C
ATOM 1514 CE1 PHE A 201 8.130 204.725 14.989 1.00 51.61 C
ANISOU 1514 CE1 PHE A 201 7217 5662 6728 781 -264 -15 C
ATOM 1515 CE2 PHE A 201 7.514 202.585 15.848 1.00 51.63 C
ANISOU 1515 CE2 PHE A 201 7067 5816 6733 729 -242 -82 C
ATOM 1516 CZ PHE A 201 8.334 203.365 15.057 1.00 49.84 C
ANISOU 1516 CZ PHE A 201 6938 5530 6470 720 -264 -34 C
ATOM 1517 N LEU A 202 3.830 206.746 19.935 1.00 49.38 N
ANISOU 1517 N LEU A 202 6710 5297 6756 1088 -27 -265 N
ATOM 1518 CA LEU A 202 2.714 207.417 20.609 1.00 50.54 C
ANISOU 1518 CA LEU A 202 6808 5415 6979 1190 16 -304 C
ATOM 1519 C LEU A 202 3.117 208.815 21.094 1.00 53.67 C
ANISOU 1519 C LEU A 202 7316 5689 7387 1227 53 -330 C
ATOM 1520 O LEU A 202 2.336 209.751 20.934 1.00 54.03 O
ANISOU 1520 O LEU A 202 7359 5671 7501 1332 47 -325 O
ATOM 1521 CB LEU A 202 2.182 206.584 21.791 1.00 50.90 C
ANISOU 1521 CB LEU A 202 6766 5540 7034 1175 95 -363 C
ATOM 1522 CG LEU A 202 1.102 205.556 21.441 1.00 56.45 C
ANISOU 1522 CG LEU A 202 7323 6343 7782 1193 71 -348 C
ATOM 1523 CD1 LEU A 202 1.087 204.405 22.436 1.00 56.12 C
ANISOU 1523 CD1 LEU A 202 7223 6384 7715 1126 142 -387 C
ATOM 1524 CD2 LEU A 202 -0.266 206.206 21.351 1.00 60.64 C
ANISOU 1524 CD2 LEU A 202 7769 6859 8411 1318 68 -351 C
ATOM 1525 N ALA A 203 4.335 208.954 21.669 1.00 48.99 N
ANISOU 1525 N ALA A 203 6820 5060 6733 1142 87 -358 N
ATOM 1526 CA ALA A 203 4.872 210.227 22.169 1.00 49.15 C
ANISOU 1526 CA ALA A 203 6955 4960 6760 1155 120 -391 C
ATOM 1527 C ALA A 203 5.061 211.235 21.035 1.00 53.91 C
ANISOU 1527 C ALA A 203 7633 5462 7388 1192 59 -325 C
ATOM 1528 O ALA A 203 4.646 212.385 21.177 1.00 54.84 O
ANISOU 1528 O ALA A 203 7798 5479 7562 1274 73 -338 O
ATOM 1529 CB ALA A 203 6.190 209.999 22.889 1.00 48.98 C
ANISOU 1529 CB ALA A 203 7007 4938 6664 1041 151 -430 C
ATOM 1530 N ALA A 204 5.659 210.795 19.904 1.00 49.75 N
ANISOU 1530 N ALA A 204 7120 4963 6820 1136 -6 -253 N
ATOM 1531 CA ALA A 204 5.888 211.623 18.718 1.00 49.81 C
ANISOU 1531 CA ALA A 204 7201 4886 6837 1163 -64 -175 C
ATOM 1532 C ALA A 204 4.569 212.131 18.138 1.00 53.83 C
ANISOU 1532 C ALA A 204 7662 5373 7417 1297 -104 -141 C
ATOM 1533 O ALA A 204 4.468 213.317 17.842 1.00 54.54 O
ANISOU 1533 O ALA A 204 7828 5348 7548 1363 -114 -115 O
ATOM 1534 CB ALA A 204 6.644 210.833 17.669 1.00 49.65 C
ANISOU 1534 CB ALA A 204 7188 4928 6750 1082 -116 -110 C
ATOM 1535 N ARG A 205 3.553 211.246 18.022 1.00 49.41 N
ANISOU 1535 N ARG A 205 6974 4921 6879 1339 -127 -143 N
ATOM 1536 CA ARG A 205 2.223 211.575 17.508 1.00 49.96 C
ANISOU 1536 CA ARG A 205 6969 4992 7021 1467 -172 -115 C
ATOM 1537 C ARG A 205 1.537 212.621 18.409 1.00 54.03 C
ANISOU 1537 C ARG A 205 7491 5422 7616 1568 -112 -169 C
ATOM 1538 O ARG A 205 1.086 213.649 17.899 1.00 55.22 O
ANISOU 1538 O ARG A 205 7680 5483 7818 1668 -144 -131 O
ATOM 1539 CB ARG A 205 1.361 210.302 17.380 1.00 50.17 C
ANISOU 1539 CB ARG A 205 6846 5159 7059 1469 -199 -122 C
ATOM 1540 CG ARG A 205 0.013 210.529 16.688 1.00 61.93 C
ANISOU 1540 CG ARG A 205 8242 6666 8622 1593 -266 -87 C
ATOM 1541 CD ARG A 205 -0.894 209.315 16.754 1.00 72.80 C
ANISOU 1541 CD ARG A 205 9460 8176 10026 1588 -281 -109 C
ATOM 1542 NE ARG A 205 -1.422 209.082 18.101 1.00 82.39 N
ANISOU 1542 NE ARG A 205 10597 9420 11288 1598 -182 -187 N
ATOM 1543 CZ ARG A 205 -2.340 208.168 18.400 1.00 97.66 C
ANISOU 1543 CZ ARG A 205 12384 11456 13266 1603 -170 -214 C
ATOM 1544 NH1 ARG A 205 -2.851 207.393 17.451 1.00 86.89 N
ANISOU 1544 NH1 ARG A 205 10931 10172 11911 1598 -259 -176 N
ATOM 1545 NH2 ARG A 205 -2.758 208.025 19.650 1.00 84.18 N
ANISOU 1545 NH2 ARG A 205 10620 9771 11594 1611 -68 -281 N
ATOM 1546 N ARG A 206 1.493 212.368 19.736 1.00 49.07 N
ANISOU 1546 N ARG A 206 6834 4819 6991 1545 -23 -255 N
ATOM 1547 CA ARG A 206 0.894 213.250 20.740 1.00 49.62 C
ANISOU 1547 CA ARG A 206 6911 4818 7123 1633 50 -322 C
ATOM 1548 C ARG A 206 1.553 214.635 20.737 1.00 54.30 C
ANISOU 1548 C ARG A 206 7656 5252 7726 1651 58 -320 C
ATOM 1549 O ARG A 206 0.846 215.645 20.809 1.00 55.39 O
ANISOU 1549 O ARG A 206 7809 5299 7937 1769 69 -328 O
ATOM 1550 CB ARG A 206 1.000 212.621 22.137 1.00 49.09 C
ANISOU 1550 CB ARG A 206 6811 4813 7027 1579 145 -411 C
ATOM 1551 N GLN A 207 2.899 214.670 20.628 1.00 49.34 N
ANISOU 1551 N GLN A 207 7134 4586 7028 1535 53 -309 N
ATOM 1552 CA GLN A 207 3.697 215.893 20.601 1.00 49.61 C
ANISOU 1552 CA GLN A 207 7314 4467 7067 1522 61 -306 C
ATOM 1553 C GLN A 207 3.452 216.697 19.326 1.00 55.50 C
ANISOU 1553 C GLN A 207 8109 5128 7852 1595 -10 -210 C
ATOM 1554 O GLN A 207 3.374 217.925 19.405 1.00 56.43 O
ANISOU 1554 O GLN A 207 8314 5105 8022 1661 5 -214 O
ATOM 1555 CB GLN A 207 5.189 215.572 20.749 1.00 49.47 C
ANISOU 1555 CB GLN A 207 7373 4453 6969 1369 69 -313 C
ATOM 1556 CG GLN A 207 5.626 215.502 22.202 1.00 49.67 C
ANISOU 1556 CG GLN A 207 7421 4483 6969 1314 145 -420 C
ATOM 1557 CD GLN A 207 6.983 214.883 22.394 1.00 62.08 C
ANISOU 1557 CD GLN A 207 9030 6097 8459 1167 145 -429 C
ATOM 1558 OE1 GLN A 207 7.130 213.915 23.141 1.00 58.55 O
ANISOU 1558 OE1 GLN A 207 8528 5756 7964 1113 175 -476 O
ATOM 1559 NE2 GLN A 207 8.013 215.442 21.762 1.00 51.25 N
ANISOU 1559 NE2 GLN A 207 7754 4644 7074 1099 116 -384 N
ATOM 1560 N LEU A 208 3.326 216.014 18.163 1.00 52.37 N
ANISOU 1560 N LEU A 208 7661 4812 7426 1587 -86 -126 N
ATOM 1561 CA LEU A 208 3.059 216.645 16.866 1.00 53.30 C
ANISOU 1561 CA LEU A 208 7821 4867 7564 1659 -162 -25 C
ATOM 1562 C LEU A 208 1.649 217.235 16.836 1.00 59.64 C
ANISOU 1562 C LEU A 208 8561 5640 8459 1824 -179 -23 C
ATOM 1563 O LEU A 208 1.475 218.365 16.374 1.00 60.35 O
ANISOU 1563 O LEU A 208 8732 5605 8594 1909 -201 24 O
ATOM 1564 CB LEU A 208 3.257 215.653 15.709 1.00 52.60 C
ANISOU 1564 CB LEU A 208 7690 4889 7407 1607 -238 52 C
ATOM 1565 CG LEU A 208 4.707 215.452 15.241 1.00 56.65 C
ANISOU 1565 CG LEU A 208 8298 5390 7836 1472 -240 90 C
ATOM 1566 CD1 LEU A 208 4.882 214.118 14.525 1.00 55.57 C
ANISOU 1566 CD1 LEU A 208 8091 5396 7626 1406 -289 124 C
ATOM 1567 CD2 LEU A 208 5.174 216.603 14.352 1.00 59.70 C
ANISOU 1567 CD2 LEU A 208 8817 5641 8225 1493 -267 176 C
ATOM 1568 N ALA A1001 0.657 216.491 17.379 1.00 69.61 N
ANISOU 1568 N ALA A1001 10470 3860 12120 1551 -950 72 N
ATOM 1569 CA ALA A1001 -0.741 216.913 17.485 1.00 69.49 C
ANISOU 1569 CA ALA A1001 10275 3774 12355 1162 -902 141 C
ATOM 1570 C ALA A1001 -0.869 218.144 18.391 1.00 72.40 C
ANISOU 1570 C ALA A1001 10392 4505 12613 1109 -745 298 C
ATOM 1571 O ALA A1001 -1.675 219.029 18.099 1.00 70.57 O
ANISOU 1571 O ALA A1001 9909 4418 12488 884 -754 250 O
ATOM 1572 CB ALA A1001 -1.593 215.774 18.022 1.00 73.78 C
ANISOU 1572 CB ALA A1001 11007 3828 13198 966 -801 298 C
ATOM 1573 N ASP A1002 -0.041 218.212 19.463 1.00 69.64 N
ANISOU 1573 N ASP A1002 10134 4294 12032 1357 -643 457 N
ATOM 1574 CA ASP A1002 -0.002 219.314 20.427 1.00 67.70 C
ANISOU 1574 CA ASP A1002 9728 4369 11626 1371 -527 585 C
ATOM 1575 C ASP A1002 0.527 220.602 19.782 1.00 69.62 C
ANISOU 1575 C ASP A1002 9682 5024 11747 1394 -619 391 C
ATOM 1576 O ASP A1002 0.007 221.681 20.079 1.00 67.60 O
ANISOU 1576 O ASP A1002 9231 4975 11480 1245 -545 431 O
ATOM 1577 CB ASP A1002 0.850 218.937 21.648 1.00 70.90 C
ANISOU 1577 CB ASP A1002 10378 4777 11785 1699 -495 749 C
ATOM 1578 N LEU A1003 1.547 220.489 18.901 1.00 66.82 N
ANISOU 1578 N LEU A1003 9319 4760 11310 1583 -736 185 N
ATOM 1579 CA LEU A1003 2.143 221.630 18.190 1.00 64.78 C
ANISOU 1579 CA LEU A1003 8831 4829 10953 1598 -744 5 C
ATOM 1580 C LEU A1003 1.143 222.245 17.217 1.00 68.11 C
ANISOU 1580 C LEU A1003 9187 5240 11453 1341 -765 -76 C
ATOM 1581 O LEU A1003 1.079 223.468 17.109 1.00 65.53 O
ANISOU 1581 O LEU A1003 8689 5156 11056 1257 -717 -107 O
ATOM 1582 CB LEU A1003 3.424 221.223 17.437 1.00 65.81 C
ANISOU 1582 CB LEU A1003 8986 5002 11018 1863 -776 -188 C
ATOM 1583 CG LEU A1003 4.695 221.071 18.273 1.00 71.41 C
ANISOU 1583 CG LEU A1003 9614 5859 11661 2174 -805 -199 C
ATOM 1584 CD1 LEU A1003 5.719 220.219 17.549 1.00 73.64 C
ANISOU 1584 CD1 LEU A1003 9960 6060 11959 2455 -829 -372 C
ATOM 1585 CD2 LEU A1003 5.295 222.427 18.637 1.00 71.73 C
ANISOU 1585 CD2 LEU A1003 9330 6264 11659 2157 -762 -267 C
ATOM 1586 N GLU A1004 0.353 221.394 16.531 1.00 67.33 N
ANISOU 1586 N GLU A1004 9240 4833 11507 1231 -871 -127 N
ATOM 1587 CA GLU A1004 -0.684 221.813 15.588 1.00 67.38 C
ANISOU 1587 CA GLU A1004 9210 4779 11612 1032 -995 -244 C
ATOM 1588 C GLU A1004 -1.865 222.434 16.345 1.00 70.78 C
ANISOU 1588 C GLU A1004 9421 5249 12223 791 -941 -101 C
ATOM 1589 O GLU A1004 -2.437 223.415 15.867 1.00 68.50 O
ANISOU 1589 O GLU A1004 9002 5095 11929 696 -1006 -174 O
ATOM 1590 CB GLU A1004 -1.140 220.622 14.724 1.00 71.74 C
ANISOU 1590 CB GLU A1004 9982 4959 12317 1003 -1188 -384 C
ATOM 1591 CG GLU A1004 -2.053 220.976 13.553 1.00 85.04 C
ANISOU 1591 CG GLU A1004 11684 6566 14061 885 -1430 -584 C
ATOM 1592 CD GLU A1004 -1.566 222.031 12.576 1.00108.00 C
ANISOU 1592 CD GLU A1004 14672 9711 16651 1026 -1444 -722 C
ATOM 1593 OE1 GLU A1004 -0.420 221.914 12.084 1.00109.49 O
ANISOU 1593 OE1 GLU A1004 15041 9965 16595 1252 -1331 -796 O
ATOM 1594 OE2 GLU A1004 -2.345 222.967 12.283 1.00100.28 O
ANISOU 1594 OE2 GLU A1004 13591 8831 15681 922 -1546 -758 O
ATOM 1595 N ASP A1005 -2.208 221.879 17.533 1.00 69.57 N
ANISOU 1595 N ASP A1005 9261 4965 12209 724 -792 110 N
ATOM 1596 CA ASP A1005 -3.294 222.369 18.387 1.00 69.99 C
ANISOU 1596 CA ASP A1005 9120 5032 12442 519 -641 270 C
ATOM 1597 C ASP A1005 -3.039 223.809 18.827 1.00 71.50 C
ANISOU 1597 C ASP A1005 9157 5595 12415 573 -556 305 C
ATOM 1598 O ASP A1005 -3.945 224.632 18.717 1.00 70.44 O
ANISOU 1598 O ASP A1005 8822 5543 12397 428 -556 285 O
ATOM 1599 CB ASP A1005 -3.499 221.460 19.612 1.00 74.51 C
ANISOU 1599 CB ASP A1005 9831 5366 13115 495 -408 518 C
ATOM 1600 CG ASP A1005 -4.385 220.253 19.354 1.00 91.55 C
ANISOU 1600 CG ASP A1005 12039 7082 15664 280 -407 519 C
ATOM 1601 OD1 ASP A1005 -5.425 220.410 18.669 1.00 93.51 O
ANISOU 1601 OD1 ASP A1005 12049 7241 16239 45 -531 375 O
ATOM 1602 OD2 ASP A1005 -4.067 219.162 19.878 1.00100.60 O
ANISOU 1602 OD2 ASP A1005 13463 7947 16812 351 -294 655 O
ATOM 1603 N ASN A1006 -1.800 224.116 19.279 1.00 67.13 N
ANISOU 1603 N ASN A1006 8680 5250 11576 792 -516 325 N
ATOM 1604 CA ASN A1006 -1.375 225.454 19.711 1.00 64.78 C
ANISOU 1604 CA ASN A1006 8254 5276 11083 846 -461 322 C
ATOM 1605 C ASN A1006 -1.402 226.446 18.538 1.00 66.74 C
ANISOU 1605 C ASN A1006 8402 5665 11292 787 -552 142 C
ATOM 1606 O ASN A1006 -1.872 227.572 18.703 1.00 64.53 O
ANISOU 1606 O ASN A1006 8000 5534 10983 709 -510 154 O
ATOM 1607 CB ASN A1006 0.035 225.403 20.328 1.00 65.86 C
ANISOU 1607 CB ASN A1006 8457 5558 11006 1094 -471 314 C
ATOM 1608 CG ASN A1006 0.113 224.891 21.751 1.00 89.76 C
ANISOU 1608 CG ASN A1006 11647 8516 13940 1227 -396 509 C
ATOM 1609 OD1 ASN A1006 -0.828 224.997 22.548 1.00 88.47 O
ANISOU 1609 OD1 ASN A1006 11529 8279 13807 1125 -237 685 O
ATOM 1610 ND2 ASN A1006 1.275 224.385 22.125 1.00 80.29 N
ANISOU 1610 ND2 ASN A1006 10555 7344 12607 1494 -498 474 N
ATOM 1611 N TRP A1007 -0.910 226.007 17.359 1.00 64.15 N
ANISOU 1611 N TRP A1007 8183 5259 10931 853 -659 -18 N
ATOM 1612 CA TRP A1007 -0.850 226.773 16.113 1.00 63.20 C
ANISOU 1612 CA TRP A1007 8106 5205 10703 851 -719 -179 C
ATOM 1613 C TRP A1007 -2.255 227.170 15.649 1.00 67.91 C
ANISOU 1613 C TRP A1007 8660 5716 11428 704 -860 -207 C
ATOM 1614 O TRP A1007 -2.445 228.306 15.213 1.00 66.08 O
ANISOU 1614 O TRP A1007 8421 5606 11081 697 -869 -255 O
ATOM 1615 CB TRP A1007 -0.118 225.966 15.025 1.00 63.24 C
ANISOU 1615 CB TRP A1007 8319 5083 10626 992 -772 -330 C
ATOM 1616 CG TRP A1007 -0.136 226.603 13.665 1.00 64.48 C
ANISOU 1616 CG TRP A1007 8648 5240 10612 1028 -809 -482 C
ATOM 1617 CD1 TRP A1007 -0.819 226.167 12.567 1.00 69.08 C
ANISOU 1617 CD1 TRP A1007 9457 5614 11178 1046 -1024 -614 C
ATOM 1618 CD2 TRP A1007 0.525 227.816 13.273 1.00 63.33 C
ANISOU 1618 CD2 TRP A1007 8515 5276 10271 1062 -626 -517 C
ATOM 1619 NE1 TRP A1007 -0.602 227.018 11.507 1.00 68.79 N
ANISOU 1619 NE1 TRP A1007 9638 5621 10879 1135 -987 -714 N
ATOM 1620 CE2 TRP A1007 0.212 228.043 11.915 1.00 68.53 C
ANISOU 1620 CE2 TRP A1007 9479 5815 10746 1128 -704 -640 C
ATOM 1621 CE3 TRP A1007 1.357 228.734 13.939 1.00 63.21 C
ANISOU 1621 CE3 TRP A1007 8307 5483 10227 1044 -410 -470 C
ATOM 1622 CZ2 TRP A1007 0.702 229.149 11.208 1.00 67.83 C
ANISOU 1622 CZ2 TRP A1007 9549 5801 10421 1175 -503 -674 C
ATOM 1623 CZ3 TRP A1007 1.850 229.822 13.235 1.00 64.64 C
ANISOU 1623 CZ3 TRP A1007 8573 5737 10250 1044 -219 -529 C
ATOM 1624 CH2 TRP A1007 1.527 230.018 11.886 1.00 66.55 C
ANISOU 1624 CH2 TRP A1007 9162 5838 10287 1109 -230 -609 C
ATOM 1625 N GLU A1008 -3.230 226.238 15.756 1.00 67.25 N
ANISOU 1625 N GLU A1008 8535 5401 11615 591 -973 -188 N
ATOM 1626 CA GLU A1008 -4.634 226.471 15.404 1.00 68.54 C
ANISOU 1626 CA GLU A1008 8557 5464 12021 449 -1148 -251 C
ATOM 1627 C GLU A1008 -5.260 227.454 16.391 1.00 72.14 C
ANISOU 1627 C GLU A1008 8766 6089 12553 364 -985 -112 C
ATOM 1628 O GLU A1008 -5.920 228.394 15.957 1.00 71.79 O
ANISOU 1628 O GLU A1008 8635 6122 12518 359 -1100 -190 O
ATOM 1629 CB GLU A1008 -5.429 225.158 15.374 1.00 72.84 C
ANISOU 1629 CB GLU A1008 9056 5688 12933 309 -1268 -283 C
ATOM 1630 CG GLU A1008 -5.233 224.347 14.107 1.00 85.90 C
ANISOU 1630 CG GLU A1008 10962 7127 14551 388 -1551 -505 C
ATOM 1631 CD GLU A1008 -5.924 222.997 14.104 1.00113.55 C
ANISOU 1631 CD GLU A1008 14435 10262 18445 230 -1678 -559 C
ATOM 1632 OE1 GLU A1008 -7.135 222.939 14.416 1.00114.74 O
ANISOU 1632 OE1 GLU A1008 14289 10289 19016 10 -1725 -562 O
ATOM 1633 OE2 GLU A1008 -5.257 221.997 13.755 1.00107.62 O
ANISOU 1633 OE2 GLU A1008 13950 9326 17615 323 -1720 -616 O
ATOM 1634 N THR A1009 -5.003 227.264 17.710 1.00 68.90 N
ANISOU 1634 N THR A1009 8303 5729 12147 346 -724 87 N
ATOM 1635 CA THR A1009 -5.471 228.110 18.820 1.00 68.55 C
ANISOU 1635 CA THR A1009 8101 5833 12112 309 -512 235 C
ATOM 1636 C THR A1009 -4.976 229.567 18.626 1.00 71.12 C
ANISOU 1636 C THR A1009 8446 6417 12159 405 -525 174 C
ATOM 1637 O THR A1009 -5.706 230.507 18.941 1.00 70.53 O
ANISOU 1637 O THR A1009 8235 6434 12128 376 -474 198 O
ATOM 1638 CB THR A1009 -5.010 227.500 20.165 1.00 76.79 C
ANISOU 1638 CB THR A1009 9247 6848 13082 356 -263 443 C
ATOM 1639 OG1 THR A1009 -5.553 226.185 20.278 1.00 79.48 O
ANISOU 1639 OG1 THR A1009 9609 6887 13701 244 -210 514 O
ATOM 1640 CG2 THR A1009 -5.441 228.318 21.384 1.00 75.22 C
ANISOU 1640 CG2 THR A1009 8977 6781 12821 364 -19 597 C
ATOM 1641 N LEU A1010 -3.762 229.745 18.084 1.00 66.84 N
ANISOU 1641 N LEU A1010 8065 5964 11367 515 -567 89 N
ATOM 1642 CA LEU A1010 -3.199 231.065 17.827 1.00 65.48 C
ANISOU 1642 CA LEU A1010 7929 5975 10974 567 -533 27 C
ATOM 1643 C LEU A1010 -3.892 231.726 16.632 1.00 69.82 C
ANISOU 1643 C LEU A1010 8544 6475 11510 565 -692 -91 C
ATOM 1644 O LEU A1010 -4.072 232.940 16.643 1.00 69.20 O
ANISOU 1644 O LEU A1010 8468 6494 11330 578 -657 -96 O
ATOM 1645 CB LEU A1010 -1.683 230.966 17.585 1.00 65.35 C
ANISOU 1645 CB LEU A1010 8014 6034 10783 662 -473 -41 C
ATOM 1646 CG LEU A1010 -0.888 232.269 17.684 1.00 69.87 C
ANISOU 1646 CG LEU A1010 8570 6777 11200 672 -358 -91 C
ATOM 1647 CD1 LEU A1010 -0.495 232.565 19.130 1.00 70.05 C
ANISOU 1647 CD1 LEU A1010 8479 6935 11202 695 -294 -21 C
ATOM 1648 CD2 LEU A1010 0.358 232.207 16.814 1.00 73.88 C
ANISOU 1648 CD2 LEU A1010 9154 7293 11624 728 -279 -214 C
ATOM 1649 N ASN A1011 -4.304 230.929 15.626 1.00 67.45 N
ANISOU 1649 N ASN A1011 8335 5999 11295 575 -899 -198 N
ATOM 1650 CA ASN A1011 -4.958 231.428 14.415 1.00 68.18 C
ANISOU 1650 CA ASN A1011 8568 6011 11328 639 -1137 -339 C
ATOM 1651 C ASN A1011 -6.460 231.696 14.593 1.00 72.92 C
ANISOU 1651 C ASN A1011 8925 6567 12212 585 -1318 -363 C
ATOM 1652 O ASN A1011 -6.911 232.777 14.211 1.00 71.96 O
ANISOU 1652 O ASN A1011 8855 6495 11991 671 -1414 -410 O
ATOM 1653 CB ASN A1011 -4.741 230.469 13.242 1.00 70.60 C
ANISOU 1653 CB ASN A1011 9120 6132 11573 717 -1335 -487 C
ATOM 1654 CG ASN A1011 -3.340 230.466 12.675 1.00 96.09 C
ANISOU 1654 CG ASN A1011 12626 9394 14492 829 -1150 -514 C
ATOM 1655 OD1 ASN A1011 -2.511 231.346 12.957 1.00 86.78 O
ANISOU 1655 OD1 ASN A1011 11455 8369 13150 837 -894 -450 O
ATOM 1656 ND2 ASN A1011 -3.053 229.476 11.836 1.00 91.18 N
ANISOU 1656 ND2 ASN A1011 12224 8607 13812 917 -1263 -630 N
ATOM 1657 N ASP A1012 -7.235 230.724 15.130 1.00 71.75 N
ANISOU 1657 N ASP A1012 8515 6303 12443 451 -1349 -338 N
ATOM 1658 CA ASP A1012 -8.688 230.873 15.290 1.00 74.30 C
ANISOU 1658 CA ASP A1012 8508 6568 13153 377 -1488 -390 C
ATOM 1659 C ASP A1012 -9.048 231.953 16.317 1.00 77.43 C
ANISOU 1659 C ASP A1012 8713 7146 13559 379 -1237 -254 C
ATOM 1660 O ASP A1012 -10.058 232.632 16.132 1.00 78.41 O
ANISOU 1660 O ASP A1012 8645 7285 13862 425 -1385 -339 O
ATOM 1661 CB ASP A1012 -9.394 229.542 15.619 1.00 79.16 C
ANISOU 1661 CB ASP A1012 8869 6969 14241 187 -1501 -396 C
ATOM 1662 CG ASP A1012 -8.840 228.748 16.789 1.00 93.82 C
ANISOU 1662 CG ASP A1012 10729 8796 16122 78 -1122 -173 C
ATOM 1663 OD1 ASP A1012 -8.546 229.361 17.840 1.00 94.03 O
ANISOU 1663 OD1 ASP A1012 10740 8994 15994 104 -813 9 O
ATOM 1664 OD2 ASP A1012 -8.737 227.507 16.667 1.00101.78 O
ANISOU 1664 OD2 ASP A1012 11792 9585 17296 -12 -1156 -187 O
ATOM 1665 N ASN A1013 -8.217 232.140 17.366 1.00 72.23 N
ANISOU 1665 N ASN A1013 8126 6620 12699 366 -899 -72 N
ATOM 1666 CA ASN A1013 -8.443 233.188 18.370 1.00 71.40 C
ANISOU 1666 CA ASN A1013 7923 6674 12531 399 -666 39 C
ATOM 1667 C ASN A1013 -8.191 234.589 17.773 1.00 73.78 C
ANISOU 1667 C ASN A1013 8401 7084 12546 536 -773 -42 C
ATOM 1668 O ASN A1013 -8.825 235.547 18.218 1.00 73.60 O
ANISOU 1668 O ASN A1013 8271 7136 12556 592 -707 -24 O
ATOM 1669 CB ASN A1013 -7.595 232.970 19.619 1.00 71.02 C
ANISOU 1669 CB ASN A1013 7968 6709 12308 389 -358 215 C
ATOM 1670 CG ASN A1013 -8.194 232.005 20.608 1.00 97.21 C
ANISOU 1670 CG ASN A1013 11138 9912 15886 289 -123 365 C
ATOM 1671 OD1 ASN A1013 -8.277 230.799 20.371 1.00 93.85 O
ANISOU 1671 OD1 ASN A1013 10695 9304 15660 193 -161 371 O
ATOM 1672 ND2 ASN A1013 -8.597 232.512 21.760 1.00 90.44 N
ANISOU 1672 ND2 ASN A1013 10224 9128 15012 318 160 497 N
ATOM 1673 N LEU A1014 -7.291 234.701 16.760 1.00 69.14 N
ANISOU 1673 N LEU A1014 8111 6475 11684 599 -898 -127 N
ATOM 1674 CA LEU A1014 -7.013 235.958 16.049 1.00 68.44 C
ANISOU 1674 CA LEU A1014 8276 6415 11313 719 -953 -188 C
ATOM 1675 C LEU A1014 -8.239 236.378 15.236 1.00 74.38 C
ANISOU 1675 C LEU A1014 9007 7078 12175 843 -1266 -310 C
ATOM 1676 O LEU A1014 -8.541 237.571 15.162 1.00 74.13 O
ANISOU 1676 O LEU A1014 9072 7075 12020 960 -1283 -318 O
ATOM 1677 CB LEU A1014 -5.791 235.834 15.118 1.00 68.02 C
ANISOU 1677 CB LEU A1014 8556 6317 10971 752 -929 -238 C
ATOM 1678 CG LEU A1014 -4.396 236.083 15.709 1.00 70.97 C
ANISOU 1678 CG LEU A1014 8978 6800 11187 687 -639 -175 C
ATOM 1679 CD1 LEU A1014 -3.311 235.603 14.754 1.00 71.13 C
ANISOU 1679 CD1 LEU A1014 9226 6755 11045 714 -584 -241 C
ATOM 1680 CD2 LEU A1014 -4.178 237.554 16.041 1.00 73.15 C
ANISOU 1680 CD2 LEU A1014 9336 7139 11318 694 -495 -153 C
ATOM 1681 N LYS A1015 -8.952 235.387 14.648 1.00 72.78 N
ANISOU 1681 N LYS A1015 8679 6749 12227 832 -1548 -425 N
ATOM 1682 CA LYS A1015 -10.180 235.580 13.869 1.00 75.59 C
ANISOU 1682 CA LYS A1015 8944 7005 12772 967 -1954 -601 C
ATOM 1683 C LYS A1015 -11.320 236.091 14.758 1.00 80.34 C
ANISOU 1683 C LYS A1015 9105 7684 13736 956 -1893 -579 C
ATOM 1684 O LYS A1015 -12.130 236.899 14.303 1.00 81.64 O
ANISOU 1684 O LYS A1015 9244 7835 13942 1146 -2154 -695 O
ATOM 1685 CB LYS A1015 -10.593 234.271 13.181 1.00 80.48 C
ANISOU 1685 CB LYS A1015 9477 7452 13651 914 -2275 -763 C
ATOM 1686 N VAL A1016 -11.364 235.624 16.027 1.00 76.27 N
ANISOU 1686 N VAL A1016 8284 7237 13456 769 -1532 -427 N
ATOM 1687 CA VAL A1016 -12.349 235.993 17.052 1.00 77.57 C
ANISOU 1687 CA VAL A1016 8044 7472 13959 744 -1324 -368 C
ATOM 1688 C VAL A1016 -12.208 237.495 17.383 1.00 81.38 C
ANISOU 1688 C VAL A1016 8702 8083 14135 919 -1204 -316 C
ATOM 1689 O VAL A1016 -13.225 238.188 17.453 1.00 83.37 O
ANISOU 1689 O VAL A1016 8725 8354 14597 1053 -1287 -391 O
ATOM 1690 CB VAL A1016 -12.214 235.084 18.312 1.00 80.90 C
ANISOU 1690 CB VAL A1016 8275 7894 14569 532 -897 -180 C
ATOM 1691 CG1 VAL A1016 -12.956 235.652 19.522 1.00 81.87 C
ANISOU 1691 CG1 VAL A1016 8128 8105 14876 546 -535 -68 C
ATOM 1692 CG2 VAL A1016 -12.686 233.664 18.013 1.00 83.12 C
ANISOU 1692 CG2 VAL A1016 8318 7984 15279 348 -1008 -247 C
ATOM 1693 N ILE A1017 -10.956 237.990 17.547 1.00 75.40 N
ANISOU 1693 N ILE A1017 8330 7393 12926 921 -1029 -216 N
ATOM 1694 CA ILE A1017 -10.637 239.394 17.854 1.00 74.22 C
ANISOU 1694 CA ILE A1017 8405 7317 12476 1045 -905 -177 C
ATOM 1695 C ILE A1017 -11.082 240.303 16.684 1.00 80.42 C
ANISOU 1695 C ILE A1017 9408 8013 13136 1267 -1236 -311 C
ATOM 1696 O ILE A1017 -11.666 241.361 16.930 1.00 80.80 O
ANISOU 1696 O ILE A1017 9447 8079 13176 1428 -1233 -327 O
ATOM 1697 CB ILE A1017 -9.125 239.573 18.210 1.00 74.32 C
ANISOU 1697 CB ILE A1017 8724 7386 12129 953 -680 -87 C
ATOM 1698 CG1 ILE A1017 -8.776 238.828 19.517 1.00 73.75 C
ANISOU 1698 CG1 ILE A1017 8491 7399 12131 824 -401 39 C
ATOM 1699 CG2 ILE A1017 -8.727 241.060 18.313 1.00 74.49 C
ANISOU 1699 CG2 ILE A1017 9016 7419 11867 1048 -595 -89 C
ATOM 1700 CD1 ILE A1017 -7.290 238.499 19.720 1.00 78.04 C
ANISOU 1700 CD1 ILE A1017 9235 7984 12435 738 -301 76 C
ATOM 1701 N GLU A1018 -10.837 239.872 15.429 1.00 78.47 N
ANISOU 1701 N GLU A1018 9400 7650 12765 1315 -1524 -408 N
ATOM 1702 CA GLU A1018 -11.215 240.611 14.219 1.00 81.00 C
ANISOU 1702 CA GLU A1018 10049 7843 12883 1577 -1875 -531 C
ATOM 1703 C GLU A1018 -12.740 240.749 14.084 1.00 89.82 C
ANISOU 1703 C GLU A1018 10812 8941 14376 1765 -2228 -686 C
ATOM 1704 O GLU A1018 -13.213 241.774 13.594 1.00 91.55 O
ANISOU 1704 O GLU A1018 11242 9096 14448 2042 -2446 -755 O
ATOM 1705 CB GLU A1018 -10.649 239.930 12.962 1.00 83.02 C
ANISOU 1705 CB GLU A1018 10671 7966 12908 1609 -2092 -610 C
ATOM 1706 CG GLU A1018 -9.137 239.994 12.833 1.00 92.47 C
ANISOU 1706 CG GLU A1018 12249 9155 13729 1489 -1750 -493 C
ATOM 1707 CD GLU A1018 -8.573 239.283 11.618 1.00118.06 C
ANISOU 1707 CD GLU A1018 15863 12260 16735 1545 -1889 -567 C
ATOM 1708 OE1 GLU A1018 -8.777 238.054 11.492 1.00108.04 O
ANISOU 1708 OE1 GLU A1018 14390 10975 15684 1471 -2058 -647 O
ATOM 1709 OE2 GLU A1018 -7.903 239.955 10.801 1.00118.93 O
ANISOU 1709 OE2 GLU A1018 16501 12252 16433 1663 -1787 -541 O
ATOM 1710 N LYS A1019 -13.498 239.722 14.525 1.00 88.76 N
ANISOU 1710 N LYS A1019 10133 8839 14753 1620 -2275 -746 N
ATOM 1711 CA LYS A1019 -14.961 239.675 14.457 1.00 93.07 C
ANISOU 1711 CA LYS A1019 10184 9365 15812 1744 -2585 -929 C
ATOM 1712 C LYS A1019 -15.635 240.176 15.749 1.00 98.51 C
ANISOU 1712 C LYS A1019 10428 10184 16818 1718 -2217 -842 C
ATOM 1713 O LYS A1019 -16.859 240.331 15.766 1.00102.06 O
ANISOU 1713 O LYS A1019 10418 10632 17728 1848 -2410 -997 O
ATOM 1714 CB LYS A1019 -15.428 238.242 14.150 1.00 97.74 C
ANISOU 1714 CB LYS A1019 10409 9867 16863 1563 -2814 -1071 C
ATOM 1715 N ALA A1020 -14.845 240.441 16.813 1.00 92.51 N
ANISOU 1715 N ALA A1020 9806 9527 15818 1578 -1705 -618 N
ATOM 1716 CA ALA A1020 -15.334 240.909 18.116 1.00 93.39 C
ANISOU 1716 CA ALA A1020 9625 9747 16111 1577 -1293 -515 C
ATOM 1717 C ALA A1020 -16.050 242.270 18.031 1.00101.06 C
ANISOU 1717 C ALA A1020 10610 10732 17054 1901 -1419 -605 C
ATOM 1718 O ALA A1020 -15.756 243.082 17.147 1.00100.45 O
ANISOU 1718 O ALA A1020 10967 10580 16620 2110 -1717 -668 O
ATOM 1719 CB ALA A1020 -14.185 240.994 19.111 1.00 90.45 C
ANISOU 1719 CB ALA A1020 9547 9455 15364 1427 -846 -301 C
ATOM 1720 N ASP A1021 -16.996 242.498 18.962 1.00100.93 N
ANISOU 1720 N ASP A1021 10147 10789 17413 1958 -1154 -603 N
ATOM 1721 CA ASP A1021 -17.794 243.722 19.076 1.00103.58 C
ANISOU 1721 CA ASP A1021 10411 11145 17802 2289 -1211 -693 C
ATOM 1722 C ASP A1021 -17.966 244.133 20.559 1.00107.76 C
ANISOU 1722 C ASP A1021 10808 11775 18360 2284 -622 -551 C
ATOM 1723 O ASP A1021 -18.697 245.082 20.859 1.00109.90 O
ANISOU 1723 O ASP A1021 10965 12068 18725 2561 -572 -620 O
ATOM 1724 CB ASP A1021 -19.164 243.539 18.383 1.00110.74 C
ANISOU 1724 CB ASP A1021 10766 12012 19299 2474 -1641 -950 C
ATOM 1725 CG ASP A1021 -19.928 242.289 18.789 1.00125.17 C
ANISOU 1725 CG ASP A1021 11886 13850 21825 2214 -1478 -999 C
ATOM 1726 OD1 ASP A1021 -19.517 241.179 18.372 1.00124.61 O
ANISOU 1726 OD1 ASP A1021 11825 13709 21813 1951 -1597 -996 O
ATOM 1727 OD2 ASP A1021 -20.962 242.422 19.482 1.00135.16 O
ANISOU 1727 OD2 ASP A1021 12585 15165 23604 2277 -1219 -1051 O
ATOM 1728 N ASN A1022 -17.262 243.429 21.471 1.00101.93 N
ANISOU 1728 N ASN A1022 10153 11083 17494 2013 -194 -361 N
ATOM 1729 CA ASN A1022 -17.289 243.650 22.919 1.00101.96 C
ANISOU 1729 CA ASN A1022 10155 11160 17425 2013 376 -210 C
ATOM 1730 C ASN A1022 -15.868 243.602 23.513 1.00101.90 C
ANISOU 1730 C ASN A1022 10685 11175 16856 1867 564 -47 C
ATOM 1731 O ASN A1022 -14.986 242.942 22.956 1.00 98.39 O
ANISOU 1731 O ASN A1022 10427 10703 16255 1679 375 -20 O
ATOM 1732 CB ASN A1022 -18.181 242.596 23.585 1.00105.32 C
ANISOU 1732 CB ASN A1022 10017 11587 18415 1856 753 -157 C
ATOM 1733 CG ASN A1022 -18.599 242.926 24.995 1.00129.53 C
ANISOU 1733 CG ASN A1022 13030 14703 21482 1953 1374 -29 C
ATOM 1734 OD1 ASN A1022 -17.794 242.916 25.933 1.00120.42 O
ANISOU 1734 OD1 ASN A1022 12302 13572 19880 1911 1703 144 O
ATOM 1735 ND2 ASN A1022 -19.883 243.194 25.182 1.00127.32 N
ANISOU 1735 ND2 ASN A1022 12224 14434 21719 2108 1546 -130 N
ATOM 1736 N ALA A1023 -15.663 244.296 24.653 1.00 98.96 N
ANISOU 1736 N ALA A1023 10551 10849 16199 1980 918 35 N
ATOM 1737 CA ALA A1023 -14.389 244.357 25.378 1.00 96.00 C
ANISOU 1737 CA ALA A1023 10655 10497 15325 1892 1057 140 C
ATOM 1738 C ALA A1023 -14.062 243.023 26.078 1.00 99.78 C
ANISOU 1738 C ALA A1023 11082 10989 15841 1690 1330 300 C
ATOM 1739 O ALA A1023 -12.888 242.726 26.305 1.00 96.98 O
ANISOU 1739 O ALA A1023 11056 10645 15146 1586 1279 355 O
ATOM 1740 CB ALA A1023 -14.423 245.485 26.398 1.00 97.84 C
ANISOU 1740 CB ALA A1023 11160 10746 15267 2116 1304 135 C
ATOM 1741 N ALA A1024 -15.093 242.230 26.425 1.00 99.26 N
ANISOU 1741 N ALA A1024 10602 10900 16212 1643 1628 370 N
ATOM 1742 CA ALA A1024 -14.917 240.932 27.077 1.00 99.58 C
ANISOU 1742 CA ALA A1024 10625 10891 16318 1459 1940 547 C
ATOM 1743 C ALA A1024 -14.440 239.878 26.077 1.00100.73 C
ANISOU 1743 C ALA A1024 10679 10976 16618 1220 1604 524 C
ATOM 1744 O ALA A1024 -13.563 239.082 26.412 1.00 98.82 O
ANISOU 1744 O ALA A1024 10692 10705 16150 1107 1659 641 O
ATOM 1745 CB ALA A1024 -16.219 240.487 27.727 1.00105.16 C
ANISOU 1745 CB ALA A1024 10912 11543 17500 1458 2441 628 C
ATOM 1746 N GLN A1025 -15.009 239.889 24.848 1.00 96.86 N
ANISOU 1746 N GLN A1025 9861 10456 16486 1187 1227 354 N
ATOM 1747 CA GLN A1025 -14.702 238.961 23.753 1.00 94.91 C
ANISOU 1747 CA GLN A1025 9535 10130 16397 1004 861 284 C
ATOM 1748 C GLN A1025 -13.223 239.028 23.356 1.00 94.44 C
ANISOU 1748 C GLN A1025 9954 10102 15828 976 624 294 C
ATOM 1749 O GLN A1025 -12.598 237.982 23.175 1.00 93.24 O
ANISOU 1749 O GLN A1025 9878 9892 15657 818 579 347 O
ATOM 1750 CB GLN A1025 -15.592 239.244 22.530 1.00 97.78 C
ANISOU 1750 CB GLN A1025 9560 10457 17135 1076 429 57 C
ATOM 1751 CG GLN A1025 -17.081 238.988 22.763 1.00113.28 C
ANISOU 1751 CG GLN A1025 10899 12374 19768 1067 598 -13 C
ATOM 1752 CD GLN A1025 -17.915 239.272 21.538 1.00131.25 C
ANISOU 1752 CD GLN A1025 12843 14615 22410 1189 56 -286 C
ATOM 1753 OE1 GLN A1025 -17.913 240.380 20.988 1.00125.15 O
ANISOU 1753 OE1 GLN A1025 12265 13895 21393 1451 -256 -400 O
ATOM 1754 NE2 GLN A1025 -18.677 238.282 21.101 1.00126.27 N
ANISOU 1754 NE2 GLN A1025 11721 13867 22388 1017 -85 -412 N
ATOM 1755 N VAL A1026 -12.664 240.251 23.248 1.00 88.66 N
ANISOU 1755 N VAL A1026 9527 9441 14719 1126 503 237 N
ATOM 1756 CA VAL A1026 -11.259 240.474 22.896 1.00 84.99 C
ANISOU 1756 CA VAL A1026 9458 8995 13839 1086 336 224 C
ATOM 1757 C VAL A1026 -10.358 240.051 24.090 1.00 87.79 C
ANISOU 1757 C VAL A1026 10023 9400 13935 1038 593 355 C
ATOM 1758 O VAL A1026 -9.282 239.497 23.861 1.00 85.84 O
ANISOU 1758 O VAL A1026 9934 9151 13529 943 483 360 O
ATOM 1759 CB VAL A1026 -10.984 241.929 22.386 1.00 87.79 C
ANISOU 1759 CB VAL A1026 10070 9351 13936 1228 163 117 C
ATOM 1760 CG1 VAL A1026 -11.368 242.994 23.407 1.00 88.74 C
ANISOU 1760 CG1 VAL A1026 10260 9514 13943 1393 388 130 C
ATOM 1761 CG2 VAL A1026 -9.543 242.114 21.915 1.00 85.05 C
ANISOU 1761 CG2 VAL A1026 10062 8989 13263 1137 47 89 C
ATOM 1762 N LYS A1027 -10.825 240.249 25.342 1.00 85.69 N
ANISOU 1762 N LYS A1027 9766 9164 13628 1136 928 451 N
ATOM 1763 CA LYS A1027 -10.083 239.875 26.551 1.00 85.44 C
ANISOU 1763 CA LYS A1027 10011 9158 13296 1168 1140 569 C
ATOM 1764 C LYS A1027 -10.019 238.346 26.705 1.00 89.46 C
ANISOU 1764 C LYS A1027 10452 9586 13954 1038 1256 708 C
ATOM 1765 O LYS A1027 -8.944 237.814 26.986 1.00 88.01 O
ANISOU 1765 O LYS A1027 10509 9408 13523 1030 1175 743 O
ATOM 1766 CB LYS A1027 -10.706 240.522 27.803 1.00 90.61 C
ANISOU 1766 CB LYS A1027 10775 9835 13817 1358 1493 635 C
ATOM 1767 CG LYS A1027 -9.897 240.315 29.084 1.00106.39 C
ANISOU 1767 CG LYS A1027 13183 11848 15393 1470 1644 725 C
ATOM 1768 CD LYS A1027 -10.705 240.661 30.333 1.00120.72 C
ANISOU 1768 CD LYS A1027 15140 13645 17083 1677 2088 828 C
ATOM 1769 CE LYS A1027 -10.157 240.020 31.589 1.00133.29 C
ANISOU 1769 CE LYS A1027 17165 15195 18285 1810 2296 975 C
ATOM 1770 NZ LYS A1027 -8.866 240.621 32.022 1.00140.53 N
ANISOU 1770 NZ LYS A1027 18486 16176 18732 1939 1953 831 N
ATOM 1771 N ASP A1028 -11.162 237.649 26.515 1.00 87.81 N
ANISOU 1771 N ASP A1028 9900 9280 14182 941 1431 768 N
ATOM 1772 CA ASP A1028 -11.267 236.189 26.631 1.00 88.63 C
ANISOU 1772 CA ASP A1028 9930 9241 14505 787 1583 902 C
ATOM 1773 C ASP A1028 -10.436 235.468 25.560 1.00 87.96 C
ANISOU 1773 C ASP A1028 9872 9118 14430 661 1199 817 C
ATOM 1774 O ASP A1028 -9.864 234.417 25.851 1.00 87.66 O
ANISOU 1774 O ASP A1028 9997 8988 14320 611 1257 924 O
ATOM 1775 CB ASP A1028 -12.736 235.733 26.568 1.00 94.41 C
ANISOU 1775 CB ASP A1028 10208 9851 15813 669 1846 932 C
ATOM 1776 CG ASP A1028 -13.488 235.893 27.879 1.00110.43 C
ANISOU 1776 CG ASP A1028 12253 11848 17857 765 2427 1101 C
ATOM 1777 OD1 ASP A1028 -13.179 235.152 28.838 1.00113.34 O
ANISOU 1777 OD1 ASP A1028 12929 12112 18024 776 2774 1311 O
ATOM 1778 OD2 ASP A1028 -14.414 236.731 27.933 1.00118.06 O
ANISOU 1778 OD2 ASP A1028 12948 12874 19037 856 2553 1025 O
ATOM 1779 N ALA A1029 -10.351 236.039 24.343 1.00 81.26 N
ANISOU 1779 N ALA A1029 8922 8321 13633 648 828 630 N
ATOM 1780 CA ALA A1029 -9.578 235.476 23.234 1.00 78.60 C
ANISOU 1780 CA ALA A1029 8654 7945 13267 566 496 533 C
ATOM 1781 C ALA A1029 -8.070 235.644 23.453 1.00 79.03 C
ANISOU 1781 C ALA A1029 9037 8089 12900 629 422 532 C
ATOM 1782 O ALA A1029 -7.313 234.725 23.136 1.00 78.27 O
ANISOU 1782 O ALA A1029 9027 7940 12771 580 324 536 O
ATOM 1783 CB ALA A1029 -9.988 236.123 21.920 1.00 78.79 C
ANISOU 1783 CB ALA A1029 8562 7971 13403 586 166 347 C
ATOM 1784 N LEU A1030 -7.639 236.803 23.994 1.00 73.45 N
ANISOU 1784 N LEU A1030 8490 7504 11915 741 458 503 N
ATOM 1785 CA LEU A1030 -6.232 237.113 24.258 1.00 71.30 C
ANISOU 1785 CA LEU A1030 8451 7315 11325 789 362 449 C
ATOM 1786 C LEU A1030 -5.676 236.331 25.453 1.00 75.92 C
ANISOU 1786 C LEU A1030 9205 7900 11742 870 483 565 C
ATOM 1787 O LEU A1030 -4.487 236.003 25.448 1.00 74.47 O
ANISOU 1787 O LEU A1030 9127 7750 11416 897 331 507 O
ATOM 1788 CB LEU A1030 -6.035 238.617 24.493 1.00 70.73 C
ANISOU 1788 CB LEU A1030 8491 7324 11061 864 343 351 C
ATOM 1789 CG LEU A1030 -5.915 239.504 23.252 1.00 74.23 C
ANISOU 1789 CG LEU A1030 8937 7746 11523 815 176 218 C
ATOM 1790 CD1 LEU A1030 -6.219 240.942 23.598 1.00 75.05 C
ANISOU 1790 CD1 LEU A1030 9144 7864 11508 902 220 161 C
ATOM 1791 CD2 LEU A1030 -4.522 239.418 22.632 1.00 75.37 C
ANISOU 1791 CD2 LEU A1030 9173 7896 11568 735 55 121 C
ATOM 1792 N THR A1031 -6.517 236.053 26.478 1.00 74.82 N
ANISOU 1792 N THR A1031 9109 7710 11612 936 767 724 N
ATOM 1793 CA THR A1031 -6.119 235.300 27.678 1.00 76.54 C
ANISOU 1793 CA THR A1031 9601 7880 11602 1068 918 871 C
ATOM 1794 C THR A1031 -5.815 233.844 27.313 1.00 80.33 C
ANISOU 1794 C THR A1031 10077 8227 12219 993 877 952 C
ATOM 1795 O THR A1031 -4.856 233.275 27.837 1.00 80.00 O
ANISOU 1795 O THR A1031 10278 8174 11943 1126 783 979 O
ATOM 1796 CB THR A1031 -7.174 235.396 28.791 1.00 88.51 C
ANISOU 1796 CB THR A1031 11216 9333 13080 1163 1329 1044 C
ATOM 1797 OG1 THR A1031 -8.479 235.235 28.235 1.00 91.11 O
ANISOU 1797 OG1 THR A1031 11191 9581 13847 1001 1524 1086 O
ATOM 1798 CG2 THR A1031 -7.086 236.704 29.570 1.00 86.07 C
ANISOU 1798 CG2 THR A1031 11102 9141 12459 1345 1354 967 C
ATOM 1799 N LYS A1032 -6.606 233.267 26.385 1.00 77.55 N
ANISOU 1799 N LYS A1032 9455 7761 12251 802 899 958 N
ATOM 1800 CA LYS A1032 -6.427 231.909 25.868 1.00 78.51 C
ANISOU 1800 CA LYS A1032 9562 7716 12553 706 839 1001 C
ATOM 1801 C LYS A1032 -5.224 231.859 24.910 1.00 81.71 C
ANISOU 1801 C LYS A1032 9984 8201 12862 720 486 826 C
ATOM 1802 O LYS A1032 -4.583 230.815 24.778 1.00 82.01 O
ANISOU 1802 O LYS A1032 10131 8140 12888 748 407 849 O
ATOM 1803 CB LYS A1032 -7.704 231.425 25.163 1.00 82.29 C
ANISOU 1803 CB LYS A1032 9723 8034 13510 494 921 1004 C
ATOM 1804 N MET A1033 -4.924 232.996 24.253 1.00 77.14 N
ANISOU 1804 N MET A1033 9316 7777 12219 712 317 658 N
ATOM 1805 CA MET A1033 -3.809 233.165 23.322 1.00 75.54 C
ANISOU 1805 CA MET A1033 9120 7646 11937 714 83 492 C
ATOM 1806 C MET A1033 -2.476 233.232 24.088 1.00 79.37 C
ANISOU 1806 C MET A1033 9746 8236 12174 862 13 451 C
ATOM 1807 O MET A1033 -1.484 232.668 23.626 1.00 78.90 O
ANISOU 1807 O MET A1033 9686 8178 12113 897 -117 367 O
ATOM 1808 CB MET A1033 -4.025 234.437 22.489 1.00 76.74 C
ANISOU 1808 CB MET A1033 9191 7876 12091 660 6 360 C
ATOM 1809 CG MET A1033 -3.201 234.503 21.230 1.00 79.67 C
ANISOU 1809 CG MET A1033 9585 8247 12440 626 -141 215 C
ATOM 1810 SD MET A1033 -3.554 236.012 20.295 1.00 83.41 S
ANISOU 1810 SD MET A1033 10091 8740 12860 595 -181 108 S
ATOM 1811 CE MET A1033 -4.999 235.515 19.412 1.00 80.94 C
ANISOU 1811 CE MET A1033 9693 8292 12770 571 -309 110 C
ATOM 1812 N ARG A1034 -2.464 233.921 25.251 1.00 76.61 N
ANISOU 1812 N ARG A1034 9513 7969 11628 972 77 484 N
ATOM 1813 CA ARG A1034 -1.298 234.089 26.126 1.00 77.38 C
ANISOU 1813 CA ARG A1034 9748 8161 11491 1148 -66 403 C
ATOM 1814 C ARG A1034 -0.872 232.753 26.745 1.00 83.66 C
ANISOU 1814 C ARG A1034 10727 8864 12196 1317 -100 514 C
ATOM 1815 O ARG A1034 0.326 232.492 26.845 1.00 83.97 O
ANISOU 1815 O ARG A1034 10775 8963 12169 1451 -325 387 O
ATOM 1816 CB ARG A1034 -1.604 235.112 27.234 1.00 78.21 C
ANISOU 1816 CB ARG A1034 10007 8334 11376 1254 -3 407 C
ATOM 1817 CG ARG A1034 -0.369 235.654 27.941 1.00 88.40 C
ANISOU 1817 CG ARG A1034 11389 9733 12466 1409 -258 220 C
ATOM 1818 CD ARG A1034 -0.746 236.505 29.134 1.00100.04 C
ANISOU 1818 CD ARG A1034 13110 11233 13667 1559 -211 225 C
ATOM 1819 NE ARG A1034 0.427 236.878 29.926 1.00112.49 N
ANISOU 1819 NE ARG A1034 14807 12886 15048 1744 -534 16 N
ATOM 1820 CZ ARG A1034 0.838 236.233 31.014 1.00131.36 C
ANISOU 1820 CZ ARG A1034 17505 15253 17151 2040 -677 50 C
ATOM 1821 NH1 ARG A1034 0.171 235.175 31.459 1.00119.96 N
ANISOU 1821 NH1 ARG A1034 16322 13688 15569 2164 -446 326 N
ATOM 1822 NH2 ARG A1034 1.916 236.644 31.667 1.00121.94 N
ANISOU 1822 NH2 ARG A1034 16382 14133 15817 2222 -1061 -202 N
ATOM 1823 N ALA A1035 -1.853 231.922 27.169 1.00 82.02 N
ANISOU 1823 N ALA A1035 10661 8489 12015 1315 137 744 N
ATOM 1824 CA ALA A1035 -1.635 230.604 27.774 1.00 84.17 C
ANISOU 1824 CA ALA A1035 11195 8595 12192 1471 175 902 C
ATOM 1825 C ALA A1035 -0.983 229.651 26.776 1.00 88.19 C
ANISOU 1825 C ALA A1035 11590 9035 12885 1431 5 824 C
ATOM 1826 O ALA A1035 -0.104 228.880 27.161 1.00 89.58 O
ANISOU 1826 O ALA A1035 11946 9164 12927 1648 -144 824 O
ATOM 1827 CB ALA A1035 -2.952 230.027 28.268 1.00 86.84 C
ANISOU 1827 CB ALA A1035 11662 8722 12613 1394 561 1165 C
ATOM 1828 N ALA A1036 -1.399 229.727 25.492 1.00 83.28 N
ANISOU 1828 N ALA A1036 10703 8399 12541 1197 5 740 N
ATOM 1829 CA ALA A1036 -0.864 228.918 24.395 1.00 82.89 C
ANISOU 1829 CA ALA A1036 10571 8275 12649 1161 -133 641 C
ATOM 1830 C ALA A1036 0.569 229.349 24.040 1.00 86.80 C
ANISOU 1830 C ALA A1036 10960 8955 13065 1278 -348 421 C
ATOM 1831 O ALA A1036 1.396 228.498 23.705 1.00 87.04 O
ANISOU 1831 O ALA A1036 11010 8936 13126 1398 -460 357 O
ATOM 1832 CB ALA A1036 -1.765 229.030 23.174 1.00 82.34 C
ANISOU 1832 CB ALA A1036 10315 8136 12835 923 -103 589 C
ATOM 1833 N ALA A1037 0.856 230.666 24.141 1.00 82.85 N
ANISOU 1833 N ALA A1037 10335 8647 12499 1243 -382 298 N
ATOM 1834 CA ALA A1037 2.160 231.274 23.854 1.00 82.86 C
ANISOU 1834 CA ALA A1037 10165 8809 12511 1292 -529 69 C
ATOM 1835 C ALA A1037 3.227 230.856 24.878 1.00 89.81 C
ANISOU 1835 C ALA A1037 11105 9747 13273 1566 -739 2 C
ATOM 1836 O ALA A1037 4.364 230.591 24.486 1.00 90.15 O
ANISOU 1836 O ALA A1037 10974 9849 13429 1658 -872 -174 O
ATOM 1837 CB ALA A1037 2.033 232.789 23.825 1.00 82.46 C
ANISOU 1837 CB ALA A1037 10009 8879 12443 1157 -488 -27 C
ATOM 1838 N LEU A1038 2.860 230.795 26.175 1.00 88.80 N
ANISOU 1838 N LEU A1038 11235 9591 12913 1729 -769 132 N
ATOM 1839 CA LEU A1038 3.763 230.400 27.263 1.00 92.12 C
ANISOU 1839 CA LEU A1038 11819 10041 13140 2064 -1031 75 C
ATOM 1840 C LEU A1038 3.966 228.875 27.310 1.00 98.92 C
ANISOU 1840 C LEU A1038 12884 10727 13975 2267 -1070 201 C
ATOM 1841 O LEU A1038 5.030 228.423 27.735 1.00100.87 O
ANISOU 1841 O LEU A1038 13157 11009 14162 2564 -1357 75 O
ATOM 1842 CB LEU A1038 3.247 230.909 28.622 1.00 93.69 C
ANISOU 1842 CB LEU A1038 12345 10239 13014 2210 -1026 180 C
ATOM 1843 CG LEU A1038 3.331 232.423 28.860 1.00 97.83 C
ANISOU 1843 CG LEU A1038 12735 10925 13512 2113 -1094 -2 C
ATOM 1844 CD1 LEU A1038 2.290 232.876 29.864 1.00 98.75 C
ANISOU 1844 CD1 LEU A1038 13196 10988 13338 2174 -906 178 C
ATOM 1845 CD2 LEU A1038 4.723 232.844 29.316 1.00102.96 C
ANISOU 1845 CD2 LEU A1038 13246 11712 14161 2304 -1510 -316 C
ATOM 1846 N ASP A1039 2.952 228.092 26.875 1.00 95.70 N
ANISOU 1846 N ASP A1039 12608 10112 13640 2116 -807 425 N
ATOM 1847 CA ASP A1039 2.996 226.625 26.825 1.00 97.84 C
ANISOU 1847 CA ASP A1039 13107 10147 13920 2256 -794 561 C
ATOM 1848 C ASP A1039 3.916 226.143 25.699 1.00101.33 C
ANISOU 1848 C ASP A1039 13296 10619 14584 2275 -936 361 C
ATOM 1849 O ASP A1039 4.634 225.158 25.875 1.00102.93 O
ANISOU 1849 O ASP A1039 13638 10722 14748 2549 -1091 347 O
ATOM 1850 CB ASP A1039 1.581 226.040 26.636 1.00 99.78 C
ANISOU 1850 CB ASP A1039 13503 10137 14272 2020 -460 817 C
ATOM 1851 CG ASP A1039 0.995 225.308 27.835 1.00114.24 C
ANISOU 1851 CG ASP A1039 15798 11723 15886 2170 -267 1108 C
ATOM 1852 OD1 ASP A1039 1.594 225.381 28.934 1.00117.40 O
ANISOU 1852 OD1 ASP A1039 16492 12165 15950 2501 -410 1131 O
ATOM 1853 OD2 ASP A1039 -0.071 224.673 27.677 1.00120.77 O
ANISOU 1853 OD2 ASP A1039 16708 12294 16885 1962 32 1303 O
ATOM 1854 N ALA A1040 3.886 226.837 24.543 1.00 95.81 N
ANISOU 1854 N ALA A1040 12272 10039 14093 2016 -861 211 N
ATOM 1855 CA ALA A1040 4.716 226.529 23.376 1.00 95.66 C
ANISOU 1855 CA ALA A1040 12034 10050 14263 2022 -904 18 C
ATOM 1856 C ALA A1040 6.172 226.947 23.611 1.00101.46 C
ANISOU 1856 C ALA A1040 12505 10997 15049 2226 -1110 -234 C
ATOM 1857 O ALA A1040 7.074 226.400 22.971 1.00102.52 O
ANISOU 1857 O ALA A1040 12485 11137 15331 2356 -1156 -387 O
ATOM 1858 CB ALA A1040 4.161 227.224 22.143 1.00 93.86 C
ANISOU 1858 CB ALA A1040 11644 9851 14167 1715 -729 -39 C
ATOM 1859 N GLN A1041 6.395 227.906 24.539 1.00 98.32 N
ANISOU 1859 N GLN A1041 12041 10760 14556 2263 -1240 -300 N
ATOM 1860 CA GLN A1041 7.711 228.423 24.923 1.00100.29 C
ANISOU 1860 CA GLN A1041 11991 11203 14911 2434 -1497 -583 C
ATOM 1861 C GLN A1041 8.527 227.345 25.660 1.00107.42 C
ANISOU 1861 C GLN A1041 13017 12060 15739 2870 -1812 -627 C
ATOM 1862 O GLN A1041 9.753 227.325 25.535 1.00109.38 O
ANISOU 1862 O GLN A1041 12920 12432 16208 3044 -2018 -902 O
ATOM 1863 CB GLN A1041 7.553 229.685 25.795 1.00101.53 C
ANISOU 1863 CB GLN A1041 12132 11490 14956 2362 -1595 -643 C
ATOM 1864 CG GLN A1041 8.830 230.527 25.935 1.00119.45 C
ANISOU 1864 CG GLN A1041 13976 13949 17461 2397 -1829 -1000 C
ATOM 1865 CD GLN A1041 8.635 231.889 26.576 1.00138.46 C
ANISOU 1865 CD GLN A1041 16362 16446 19800 2258 -1899 -1092 C
ATOM 1866 OE1 GLN A1041 9.400 232.825 26.319 1.00134.92 O
ANISOU 1866 OE1 GLN A1041 15528 16104 19633 2107 -1946 -1367 O
ATOM 1867 NE2 GLN A1041 7.634 232.037 27.439 1.00129.41 N
ANISOU 1867 NE2 GLN A1041 15630 15237 18303 2308 -1884 -879 N
ATOM 1868 N LYS A1042 7.841 226.448 26.408 1.00104.59 N
ANISOU 1868 N LYS A1042 13148 11500 15092 3053 -1828 -359 N
ATOM 1869 CA LYS A1042 8.449 225.349 27.168 1.00134.99 C
ANISOU 1869 CA LYS A1042 17274 15235 18782 3511 -2114 -338 C
ATOM 1870 C LYS A1042 9.092 224.308 26.240 1.00157.25 C
ANISOU 1870 C LYS A1042 19953 17965 21827 3634 -2110 -424 C
ATOM 1871 O LYS A1042 8.477 223.863 25.271 1.00113.60 O
ANISOU 1871 O LYS A1042 14465 12294 16403 3396 -1818 -307 O
ATOM 1872 CB LYS A1042 7.406 224.669 28.072 1.00138.38 C
ANISOU 1872 CB LYS A1042 18334 15399 18845 3613 -1990 26 C
ATOM 1873 CG LYS A1042 7.093 225.435 29.350 1.00153.35 C
ANISOU 1873 CG LYS A1042 20504 17356 20405 3724 -2088 88 C
ATOM 1874 CD LYS A1042 6.163 224.639 30.255 1.00165.15 C
ANISOU 1874 CD LYS A1042 22670 18548 21530 3870 -1883 466 C
ATOM 1875 CE LYS A1042 5.966 225.302 31.595 1.00178.16 C
ANISOU 1875 CE LYS A1042 24696 20236 22762 4084 -1980 522 C
ATOM 1876 NZ LYS A1042 5.132 224.471 32.504 1.00189.75 N
ANISOU 1876 NZ LYS A1042 26880 21370 23844 4262 -1702 911 N
ATOM 1877 N MET A1058 17.696 229.370 18.103 1.00113.88 N
ANISOU 1877 N MET A1058 9567 13579 20125 2370 178 -2872 N
ATOM 1878 CA MET A1058 18.053 229.103 19.495 1.00115.62 C
ANISOU 1878 CA MET A1058 9569 13928 20434 2660 -516 -3034 C
ATOM 1879 C MET A1058 17.560 230.259 20.398 1.00118.15 C
ANISOU 1879 C MET A1058 9939 14293 20659 2394 -789 -3020 C
ATOM 1880 O MET A1058 16.410 230.211 20.836 1.00113.46 O
ANISOU 1880 O MET A1058 9929 13631 19551 2373 -961 -2728 O
ATOM 1881 CB MET A1058 19.565 228.818 19.661 1.00124.56 C
ANISOU 1881 CB MET A1058 9923 15199 22205 2927 -650 -3457 C
ATOM 1882 CG MET A1058 20.486 229.710 18.826 1.00132.04 C
ANISOU 1882 CG MET A1058 10210 16177 23781 2593 -69 -3717 C
ATOM 1883 SD MET A1058 22.234 229.247 18.950 1.00144.87 S
ANISOU 1883 SD MET A1058 10827 17962 26253 2933 -190 -4240 S
ATOM 1884 CE MET A1058 22.626 229.864 20.584 1.00144.11 C
ANISOU 1884 CE MET A1058 10315 18024 26416 3019 -1093 -4566 C
ATOM 1885 N LYS A1059 18.387 231.301 20.651 1.00118.42 N
ANISOU 1885 N LYS A1059 9370 14417 21205 2179 -798 -3340 N
ATOM 1886 CA LYS A1059 17.974 232.457 21.451 1.00116.89 C
ANISOU 1886 CA LYS A1059 9237 14237 20941 1924 -1041 -3364 C
ATOM 1887 C LYS A1059 17.039 233.356 20.635 1.00116.56 C
ANISOU 1887 C LYS A1059 9582 14052 20653 1478 -494 -3089 C
ATOM 1888 O LYS A1059 16.335 234.187 21.207 1.00113.80 O
ANISOU 1888 O LYS A1059 9492 13674 20072 1296 -650 -2998 O
ATOM 1889 CB LYS A1059 19.182 233.253 21.983 1.00125.16 C
ANISOU 1889 CB LYS A1059 9502 15387 22665 1834 -1276 -3840 C
ATOM 1890 CG LYS A1059 19.690 232.782 23.349 1.00141.66 C
ANISOU 1890 CG LYS A1059 11419 17611 24792 2285 -2129 -4103 C
ATOM 1891 CD LYS A1059 18.696 233.039 24.491 1.00147.08 C
ANISOU 1891 CD LYS A1059 12741 18279 24866 2378 -2611 -3913 C
ATOM 1892 CE LYS A1059 18.425 231.775 25.269 1.00156.18 C
ANISOU 1892 CE LYS A1059 14345 19450 25548 2938 -3110 -3767 C
ATOM 1893 NZ LYS A1059 17.146 231.850 26.019 1.00160.09 N
ANISOU 1893 NZ LYS A1059 15630 19863 25333 2973 -3258 -3411 N
ATOM 1894 N ASP A1060 17.021 233.160 19.300 1.00112.74 N
ANISOU 1894 N ASP A1060 9186 13466 20183 1351 129 -2962 N
ATOM 1895 CA ASP A1060 16.165 233.868 18.352 1.00109.43 C
ANISOU 1895 CA ASP A1060 9212 12885 19482 1015 648 -2696 C
ATOM 1896 C ASP A1060 14.703 233.453 18.572 1.00108.17 C
ANISOU 1896 C ASP A1060 9761 12671 18670 1110 419 -2340 C
ATOM 1897 O ASP A1060 13.828 234.323 18.597 1.00104.94 O
ANISOU 1897 O ASP A1060 9668 12187 18016 875 480 -2178 O
ATOM 1898 CB ASP A1060 16.616 233.571 16.908 1.00113.23 C
ANISOU 1898 CB ASP A1060 9669 13263 20092 971 1318 -2677 C
ATOM 1899 CG ASP A1060 16.017 234.447 15.817 1.00121.73 C
ANISOU 1899 CG ASP A1060 11166 14142 20943 644 1909 -2467 C
ATOM 1900 OD1 ASP A1060 15.254 235.381 16.151 1.00119.62 O
ANISOU 1900 OD1 ASP A1060 11163 13818 20468 420 1812 -2343 O
ATOM 1901 OD2 ASP A1060 16.330 234.212 14.632 1.00129.60 O
ANISOU 1901 OD2 ASP A1060 12260 15028 21953 646 2471 -2432 O
ATOM 1902 N PHE A1061 14.449 232.134 18.771 1.00104.11 N
ANISOU 1902 N PHE A1061 9468 12172 17916 1457 156 -2234 N
ATOM 1903 CA PHE A1061 13.107 231.597 19.028 1.00 99.70 C
ANISOU 1903 CA PHE A1061 9507 11536 16837 1540 -45 -1919 C
ATOM 1904 C PHE A1061 12.636 232.014 20.434 1.00101.96 C
ANISOU 1904 C PHE A1061 9879 11894 16966 1571 -501 -1890 C
ATOM 1905 O PHE A1061 11.456 232.330 20.599 1.00 98.10 O
ANISOU 1905 O PHE A1061 9793 11339 16143 1450 -503 -1656 O
ATOM 1906 CB PHE A1061 13.051 230.056 18.824 1.00101.94 C
ANISOU 1906 CB PHE A1061 10002 11760 16970 1875 -153 -1831 C
ATOM 1907 CG PHE A1061 12.799 229.169 20.029 1.00103.56 C
ANISOU 1907 CG PHE A1061 10383 11979 16985 2189 -658 -1757 C
ATOM 1908 CD1 PHE A1061 11.514 228.998 20.535 1.00103.50 C
ANISOU 1908 CD1 PHE A1061 10860 11878 16589 2155 -797 -1476 C
ATOM 1909 CD2 PHE A1061 13.838 228.457 20.617 1.00109.80 C
ANISOU 1909 CD2 PHE A1061 10882 12851 17987 2545 -964 -1963 C
ATOM 1910 CE1 PHE A1061 11.283 228.177 21.644 1.00105.03 C
ANISOU 1910 CE1 PHE A1061 11289 12037 16582 2445 -1174 -1375 C
ATOM 1911 CE2 PHE A1061 13.605 227.630 21.721 1.00113.19 C
ANISOU 1911 CE2 PHE A1061 11584 13249 18174 2877 -1415 -1869 C
ATOM 1912 CZ PHE A1061 12.328 227.492 22.224 1.00108.01 C
ANISOU 1912 CZ PHE A1061 11462 12475 17103 2815 -1482 -1559 C
ATOM 1913 N ARG A1062 13.555 232.005 21.432 1.00101.16 N
ANISOU 1913 N ARG A1062 9410 11921 17104 1763 -893 -2145 N
ATOM 1914 CA ARG A1062 13.270 232.395 22.818 1.00100.49 C
ANISOU 1914 CA ARG A1062 9448 11895 16837 1861 -1356 -2163 C
ATOM 1915 C ARG A1062 12.874 233.872 22.883 1.00101.85 C
ANISOU 1915 C ARG A1062 9618 12053 17026 1496 -1217 -2183 C
ATOM 1916 O ARG A1062 11.933 234.215 23.601 1.00 99.01 O
ANISOU 1916 O ARG A1062 9637 11668 16313 1489 -1368 -2014 O
ATOM 1917 CB ARG A1062 14.473 232.113 23.730 1.00105.65 C
ANISOU 1917 CB ARG A1062 9698 12677 17768 2182 -1852 -2499 C
ATOM 1918 N HIS A1063 13.565 234.732 22.099 1.00 99.68 N
ANISOU 1918 N HIS A1063 8948 11763 17163 1197 -875 -2373 N
ATOM 1919 CA HIS A1063 13.292 236.166 22.006 1.00 98.83 C
ANISOU 1919 CA HIS A1063 8847 11584 17118 830 -678 -2400 C
ATOM 1920 C HIS A1063 11.992 236.418 21.237 1.00 97.49 C
ANISOU 1920 C HIS A1063 9208 11284 16551 660 -322 -2048 C
ATOM 1921 O HIS A1063 11.189 237.238 21.675 1.00 95.16 O
ANISOU 1921 O HIS A1063 9176 10944 16036 539 -381 -1950 O
ATOM 1922 CB HIS A1063 14.459 236.912 21.342 1.00103.76 C
ANISOU 1922 CB HIS A1063 8911 12176 18339 552 -343 -2692 C
ATOM 1923 N GLY A1064 11.788 235.689 20.133 1.00 92.10 N
ANISOU 1923 N GLY A1064 8682 10536 15778 690 1 -1889 N
ATOM 1924 CA GLY A1064 10.602 235.779 19.283 1.00 87.93 C
ANISOU 1924 CA GLY A1064 8640 9876 14894 586 270 -1599 C
ATOM 1925 C GLY A1064 9.294 235.557 20.019 1.00 87.51 C
ANISOU 1925 C GLY A1064 8977 9824 14450 686 -11 -1371 C
ATOM 1926 O GLY A1064 8.294 236.218 19.724 1.00 84.69 O
ANISOU 1926 O GLY A1064 8915 9380 13883 544 112 -1211 O
ATOM 1927 N PHE A1065 9.302 234.631 20.994 1.00 83.74 N
ANISOU 1927 N PHE A1065 8507 9427 13882 950 -371 -1357 N
ATOM 1928 CA PHE A1065 8.147 234.315 21.832 1.00 81.07 C
ANISOU 1928 CA PHE A1065 8521 9073 13210 1063 -580 -1138 C
ATOM 1929 C PHE A1065 7.917 235.410 22.875 1.00 83.98 C
ANISOU 1929 C PHE A1065 8918 9490 13500 1005 -747 -1193 C
ATOM 1930 O PHE A1065 6.764 235.670 23.229 1.00 81.83 O
ANISOU 1930 O PHE A1065 8945 9174 12972 983 -732 -1000 O
ATOM 1931 CB PHE A1065 8.323 232.949 22.513 1.00 83.97 C
ANISOU 1931 CB PHE A1065 8959 9455 13489 1383 -847 -1093 C
ATOM 1932 CG PHE A1065 7.732 231.805 21.725 1.00 84.33 C
ANISOU 1932 CG PHE A1065 9230 9375 13437 1436 -709 -905 C
ATOM 1933 CD1 PHE A1065 8.489 231.129 20.776 1.00 88.93 C
ANISOU 1933 CD1 PHE A1065 9668 9929 14191 1499 -580 -1006 C
ATOM 1934 CD2 PHE A1065 6.417 231.406 21.926 1.00 84.71 C
ANISOU 1934 CD2 PHE A1065 9620 9313 13253 1420 -695 -651 C
ATOM 1935 CE1 PHE A1065 7.942 230.070 20.047 1.00 89.22 C
ANISOU 1935 CE1 PHE A1065 9953 9819 14126 1557 -491 -865 C
ATOM 1936 CE2 PHE A1065 5.870 230.351 21.192 1.00 87.08 C
ANISOU 1936 CE2 PHE A1065 10104 9462 13520 1441 -608 -520 C
ATOM 1937 CZ PHE A1065 6.637 229.686 20.260 1.00 86.36 C
ANISOU 1937 CZ PHE A1065 9919 9334 13558 1516 -532 -633 C
ATOM 1938 N ASP A1066 9.009 236.056 23.354 1.00 81.97 N
ANISOU 1938 N ASP A1066 8335 9313 13497 984 -906 -1480 N
ATOM 1939 CA ASP A1066 8.949 237.146 24.332 1.00 81.95 C
ANISOU 1939 CA ASP A1066 8356 9335 13446 935 -1109 -1601 C
ATOM 1940 C ASP A1066 8.302 238.395 23.729 1.00 81.56 C
ANISOU 1940 C ASP A1066 8427 9180 13381 626 -801 -1533 C
ATOM 1941 O ASP A1066 7.640 239.134 24.462 1.00 80.85 O
ANISOU 1941 O ASP A1066 8557 9070 13091 621 -901 -1498 O
ATOM 1942 CB ASP A1066 10.342 237.488 24.887 1.00 88.32 C
ANISOU 1942 CB ASP A1066 8726 10223 14608 973 -1404 -1986 C
ATOM 1943 CG ASP A1066 10.894 236.506 25.908 1.00103.74 C
ANISOU 1943 CG ASP A1066 10651 12278 16487 1373 -1880 -2094 C
ATOM 1944 OD1 ASP A1066 10.088 235.922 26.673 1.00103.26 O
ANISOU 1944 OD1 ASP A1066 11031 12206 15998 1619 -2034 -1873 O
ATOM 1945 OD2 ASP A1066 12.137 236.369 25.988 1.00114.20 O
ANISOU 1945 OD2 ASP A1066 11520 13678 18194 1452 -2101 -2414 O
ATOM 1946 N ILE A1067 8.481 238.630 22.405 1.00 75.24 N
ANISOU 1946 N ILE A1067 7540 8292 12757 408 -417 -1512 N
ATOM 1947 CA ILE A1067 7.862 239.779 21.738 1.00 72.70 C
ANISOU 1947 CA ILE A1067 7416 7828 12377 162 -119 -1425 C
ATOM 1948 C ILE A1067 6.361 239.461 21.563 1.00 71.96 C
ANISOU 1948 C ILE A1067 7730 7698 11912 255 -89 -1124 C
ATOM 1949 O ILE A1067 5.540 240.355 21.769 1.00 70.66 O
ANISOU 1949 O ILE A1067 7782 7472 11594 194 -65 -1049 O
ATOM 1950 CB ILE A1067 8.561 240.280 20.421 1.00 77.13 C
ANISOU 1950 CB ILE A1067 7845 8257 13201 -85 319 -1496 C
ATOM 1951 CG1 ILE A1067 7.801 239.877 19.136 1.00 75.18 C
ANISOU 1951 CG1 ILE A1067 7940 7906 12719 -72 616 -1253 C
ATOM 1952 CG2 ILE A1067 10.037 239.881 20.340 1.00 81.26 C
ANISOU 1952 CG2 ILE A1067 7873 8847 14157 -103 352 -1757 C
ATOM 1953 CD1 ILE A1067 8.092 240.719 17.885 1.00 82.75 C
ANISOU 1953 CD1 ILE A1067 9023 8663 13755 -292 1095 -1245 C
ATOM 1954 N LEU A1068 6.014 238.182 21.251 1.00 66.14 N
ANISOU 1954 N LEU A1068 7069 6990 11073 411 -112 -979 N
ATOM 1955 CA LEU A1068 4.639 237.701 21.069 1.00 63.12 C
ANISOU 1955 CA LEU A1068 6977 6560 10446 483 -107 -735 C
ATOM 1956 C LEU A1068 3.844 237.855 22.372 1.00 66.57 C
ANISOU 1956 C LEU A1068 7542 7047 10705 592 -292 -649 C
ATOM 1957 O LEU A1068 2.748 238.416 22.339 1.00 64.97 O
ANISOU 1957 O LEU A1068 7517 6792 10377 554 -220 -528 O
ATOM 1958 CB LEU A1068 4.620 236.241 20.586 1.00 62.62 C
ANISOU 1958 CB LEU A1068 6931 6484 10378 612 -127 -652 C
ATOM 1959 CG LEU A1068 3.259 235.680 20.164 1.00 65.12 C
ANISOU 1959 CG LEU A1068 7485 6707 10549 637 -115 -448 C
ATOM 1960 CD1 LEU A1068 2.981 235.953 18.702 1.00 64.59 C
ANISOU 1960 CD1 LEU A1068 7560 6524 10458 544 59 -440 C
ATOM 1961 CD2 LEU A1068 3.192 234.188 20.416 1.00 67.94 C
ANISOU 1961 CD2 LEU A1068 7865 7044 10907 789 -231 -369 C
ATOM 1962 N VAL A1069 4.422 237.407 23.514 1.00 64.36 N
ANISOU 1962 N VAL A1069 7193 6858 10402 760 -524 -725 N
ATOM 1963 CA VAL A1069 3.830 237.526 24.853 1.00 64.52 C
ANISOU 1963 CA VAL A1069 7410 6911 10194 916 -673 -654 C
ATOM 1964 C VAL A1069 3.681 239.028 25.178 1.00 68.48 C
ANISOU 1964 C VAL A1069 7956 7400 10664 804 -659 -763 C
ATOM 1965 O VAL A1069 2.616 239.452 25.635 1.00 67.85 O
ANISOU 1965 O VAL A1069 8093 7291 10398 843 -588 -631 O
ATOM 1966 CB VAL A1069 4.655 236.745 25.921 1.00 70.98 C
ANISOU 1966 CB VAL A1069 8220 7802 10946 1176 -966 -742 C
ATOM 1967 CG1 VAL A1069 4.262 237.128 27.349 1.00 72.14 C
ANISOU 1967 CG1 VAL A1069 8643 7967 10801 1365 -1121 -722 C
ATOM 1968 CG2 VAL A1069 4.524 235.236 25.719 1.00 70.57 C
ANISOU 1968 CG2 VAL A1069 8240 7708 10866 1318 -950 -577 C
ATOM 1969 N GLY A1070 4.720 239.806 24.865 1.00 65.55 N
ANISOU 1969 N GLY A1070 7368 7023 10516 652 -685 -1002 N
ATOM 1970 CA GLY A1070 4.751 241.252 25.052 1.00 65.67 C
ANISOU 1970 CA GLY A1070 7417 6971 10565 504 -664 -1141 C
ATOM 1971 C GLY A1070 3.651 241.982 24.306 1.00 66.16 C
ANISOU 1971 C GLY A1070 7688 6917 10532 384 -399 -972 C
ATOM 1972 O GLY A1070 3.059 242.912 24.852 1.00 66.17 O
ANISOU 1972 O GLY A1070 7874 6869 10397 399 -411 -975 O
ATOM 1973 N GLN A1071 3.364 241.561 23.058 1.00 60.11 N
ANISOU 1973 N GLN A1071 6926 6097 9816 305 -189 -839 N
ATOM 1974 CA GLN A1071 2.316 242.153 22.213 1.00 58.08 C
ANISOU 1974 CA GLN A1071 6888 5720 9459 248 -3 -693 C
ATOM 1975 C GLN A1071 0.921 241.774 22.721 1.00 60.35 C
ANISOU 1975 C GLN A1071 7317 6049 9564 415 -59 -507 C
ATOM 1976 O GLN A1071 -0.007 242.576 22.603 1.00 58.75 O
ANISOU 1976 O GLN A1071 7271 5775 9277 430 4 -445 O
ATOM 1977 CB GLN A1071 2.475 241.724 20.748 1.00 58.82 C
ANISOU 1977 CB GLN A1071 6997 5733 9617 171 181 -636 C
ATOM 1978 CG GLN A1071 3.603 242.428 20.000 1.00 73.82 C
ANISOU 1978 CG GLN A1071 8833 7519 11695 -28 402 -780 C
ATOM 1979 CD GLN A1071 4.012 241.697 18.741 1.00 88.22 C
ANISOU 1979 CD GLN A1071 10666 9293 13559 -45 599 -742 C
ATOM 1980 OE1 GLN A1071 4.377 240.514 18.761 1.00 82.44 O
ANISOU 1980 OE1 GLN A1071 9769 8667 12886 51 517 -750 O
ATOM 1981 NE2 GLN A1071 4.015 242.406 17.622 1.00 77.88 N
ANISOU 1981 NE2 GLN A1071 9600 7794 12196 -143 880 -705 N
ATOM 1982 N ILE A1072 0.773 240.548 23.274 1.00 57.44 N
ANISOU 1982 N ILE A1072 6889 5773 9164 546 -150 -418 N
ATOM 1983 CA ILE A1072 -0.493 240.060 23.830 1.00 56.75 C
ANISOU 1983 CA ILE A1072 6891 5698 8973 674 -127 -237 C
ATOM 1984 C ILE A1072 -0.816 240.894 25.082 1.00 62.12 C
ANISOU 1984 C ILE A1072 7707 6406 9489 780 -143 -262 C
ATOM 1985 O ILE A1072 -1.959 241.328 25.237 1.00 61.37 O
ANISOU 1985 O ILE A1072 7696 6281 9343 833 -32 -164 O
ATOM 1986 CB ILE A1072 -0.467 238.526 24.108 1.00 59.52 C
ANISOU 1986 CB ILE A1072 7197 6078 9341 766 -167 -128 C
ATOM 1987 CG1 ILE A1072 -0.457 237.732 22.783 1.00 58.56 C
ANISOU 1987 CG1 ILE A1072 6995 5892 9363 681 -143 -100 C
ATOM 1988 CG2 ILE A1072 -1.660 238.097 24.982 1.00 60.91 C
ANISOU 1988 CG2 ILE A1072 7471 6237 9435 879 -67 57 C
ATOM 1989 CD1 ILE A1072 -0.010 236.255 22.881 1.00 61.11 C
ANISOU 1989 CD1 ILE A1072 7279 6210 9731 757 -205 -53 C
ATOM 1990 N ASP A1073 0.206 241.159 25.927 1.00 60.76 N
ANISOU 1990 N ASP A1073 7551 6285 9252 828 -301 -423 N
ATOM 1991 CA ASP A1073 0.087 241.959 27.151 1.00 62.86 C
ANISOU 1991 CA ASP A1073 8007 6560 9315 960 -373 -500 C
ATOM 1992 C ASP A1073 -0.257 243.425 26.842 1.00 68.29 C
ANISOU 1992 C ASP A1073 8775 7154 10019 858 -296 -585 C
ATOM 1993 O ASP A1073 -0.902 244.071 27.666 1.00 69.03 O
ANISOU 1993 O ASP A1073 9071 7229 9930 993 -263 -579 O
ATOM 1994 CB ASP A1073 1.371 241.873 27.997 1.00 66.83 C
ANISOU 1994 CB ASP A1073 8495 7121 9776 1046 -662 -716 C
ATOM 1995 CG ASP A1073 1.676 240.488 28.554 1.00 76.35 C
ANISOU 1995 CG ASP A1073 9732 8395 10884 1243 -778 -630 C
ATOM 1996 OD1 ASP A1073 0.720 239.707 28.774 1.00 75.91 O
ANISOU 1996 OD1 ASP A1073 9821 8320 10701 1348 -597 -379 O
ATOM 1997 OD2 ASP A1073 2.869 240.198 28.801 1.00 83.53 O
ANISOU 1997 OD2 ASP A1073 10518 9355 11864 1299 -1050 -822 O
ATOM 1998 N ASP A1074 0.154 243.931 25.655 1.00 65.46 N
ANISOU 1998 N ASP A1074 8309 6711 9854 646 -233 -653 N
ATOM 1999 CA ASP A1074 -0.127 245.287 25.164 1.00 66.24 C
ANISOU 1999 CA ASP A1074 8538 6660 9969 544 -133 -709 C
ATOM 2000 C ASP A1074 -1.606 245.438 24.809 1.00 70.71 C
ANISOU 2000 C ASP A1074 9224 7193 10452 659 1 -522 C
ATOM 2001 O ASP A1074 -2.253 246.395 25.242 1.00 71.12 O
ANISOU 2001 O ASP A1074 9447 7177 10397 753 37 -539 O
ATOM 2002 CB ASP A1074 0.730 245.602 23.921 1.00 68.29 C
ANISOU 2002 CB ASP A1074 8710 6804 10434 305 -32 -787 C
ATOM 2003 CG ASP A1074 2.193 245.907 24.161 1.00 83.35 C
ANISOU 2003 CG ASP A1074 10441 8687 12543 136 -113 -1035 C
ATOM 2004 OD1 ASP A1074 2.628 245.855 25.332 1.00 85.84 O
ANISOU 2004 OD1 ASP A1074 10704 9088 12823 228 -347 -1183 O
ATOM 2005 OD2 ASP A1074 2.906 246.196 23.177 1.00 91.96 O
ANISOU 2005 OD2 ASP A1074 11448 9659 13834 -76 59 -1094 O
ATOM 2006 N ALA A1075 -2.127 244.491 24.004 1.00 67.30 N
ANISOU 2006 N ALA A1075 8681 6794 10095 664 49 -374 N
ATOM 2007 CA ALA A1075 -3.510 244.449 23.542 1.00 67.43 C
ANISOU 2007 CA ALA A1075 8711 6783 10125 769 111 -237 C
ATOM 2008 C ALA A1075 -4.482 244.140 24.690 1.00 73.54 C
ANISOU 2008 C ALA A1075 9455 7642 10846 943 180 -142 C
ATOM 2009 O ALA A1075 -5.573 244.707 24.716 1.00 74.68 O
ANISOU 2009 O ALA A1075 9622 7751 11002 1061 253 -102 O
ATOM 2010 CB ALA A1075 -3.653 243.418 22.437 1.00 67.22 C
ANISOU 2010 CB ALA A1075 8566 6754 10221 716 83 -159 C
ATOM 2011 N LEU A1076 -4.084 243.264 25.638 1.00 70.76 N
ANISOU 2011 N LEU A1076 9075 7383 10429 986 180 -105 N
ATOM 2012 CA LEU A1076 -4.880 242.880 26.811 1.00 72.14 C
ANISOU 2012 CA LEU A1076 9299 7605 10504 1158 330 12 C
ATOM 2013 C LEU A1076 -5.088 244.080 27.756 1.00 77.74 C
ANISOU 2013 C LEU A1076 10236 8295 11005 1308 381 -71 C
ATOM 2014 O LEU A1076 -6.173 244.220 28.320 1.00 78.94 O
ANISOU 2014 O LEU A1076 10419 8447 11126 1462 590 24 O
ATOM 2015 CB LEU A1076 -4.194 241.715 27.554 1.00 72.81 C
ANISOU 2015 CB LEU A1076 9424 7747 10493 1201 294 68 C
ATOM 2016 CG LEU A1076 -4.993 240.944 28.614 1.00 79.52 C
ANISOU 2016 CG LEU A1076 10374 8596 11244 1363 529 256 C
ATOM 2017 CD1 LEU A1076 -6.097 240.100 27.986 1.00 79.40 C
ANISOU 2017 CD1 LEU A1076 10111 8530 11526 1274 718 421 C
ATOM 2018 CD2 LEU A1076 -4.075 240.028 29.398 1.00 83.11 C
ANISOU 2018 CD2 LEU A1076 11003 9070 11503 1463 428 280 C
ATOM 2019 N LYS A1077 -4.059 244.944 27.904 1.00 74.40 N
ANISOU 2019 N LYS A1077 9955 7838 10476 1258 205 -266 N
ATOM 2020 CA LYS A1077 -4.089 246.159 28.727 1.00 76.00 C
ANISOU 2020 CA LYS A1077 10413 7981 10483 1381 190 -400 C
ATOM 2021 C LYS A1077 -5.101 247.161 28.140 1.00 80.46 C
ANISOU 2021 C LYS A1077 11003 8448 11121 1419 316 -380 C
ATOM 2022 O LYS A1077 -5.848 247.783 28.897 1.00 81.68 O
ANISOU 2022 O LYS A1077 11323 8578 11133 1622 442 -381 O
ATOM 2023 CB LYS A1077 -2.675 246.778 28.828 1.00 79.09 C
ANISOU 2023 CB LYS A1077 10871 8319 10861 1250 -67 -653 C
ATOM 2024 CG LYS A1077 -2.569 248.080 29.633 1.00 96.28 C
ANISOU 2024 CG LYS A1077 13332 10388 12863 1344 -146 -850 C
ATOM 2025 CD LYS A1077 -2.456 247.854 31.141 1.00109.42 C
ANISOU 2025 CD LYS A1077 15257 12115 14202 1608 -245 -911 C
ATOM 2026 CE LYS A1077 -2.291 249.145 31.912 1.00120.56 C
ANISOU 2026 CE LYS A1077 16986 13395 15427 1711 -375 -1152 C
ATOM 2027 NZ LYS A1077 -3.568 249.897 32.034 1.00127.85 N
ANISOU 2027 NZ LYS A1077 18096 14245 16234 1886 -99 -1053 N
ATOM 2028 N LEU A1078 -5.140 247.283 26.795 1.00 75.84 N
ANISOU 2028 N LEU A1078 10288 7795 10731 1267 283 -361 N
ATOM 2029 CA LEU A1078 -6.072 248.153 26.072 1.00 75.94 C
ANISOU 2029 CA LEU A1078 10350 7696 10807 1345 336 -342 C
ATOM 2030 C LEU A1078 -7.501 247.605 26.156 1.00 80.61 C
ANISOU 2030 C LEU A1078 10742 8368 11517 1522 475 -198 C
ATOM 2031 O LEU A1078 -8.449 248.388 26.214 1.00 81.66 O
ANISOU 2031 O LEU A1078 10917 8447 11663 1707 547 -207 O
ATOM 2032 CB LEU A1078 -5.653 248.314 24.596 1.00 74.75 C
ANISOU 2032 CB LEU A1078 10201 7430 10771 1174 251 -353 C
ATOM 2033 CG LEU A1078 -4.319 249.016 24.314 1.00 79.36 C
ANISOU 2033 CG LEU A1078 10946 7876 11332 960 207 -497 C
ATOM 2034 CD1 LEU A1078 -3.840 248.722 22.906 1.00 78.34 C
ANISOU 2034 CD1 LEU A1078 10799 7665 11302 795 217 -457 C
ATOM 2035 CD2 LEU A1078 -4.414 250.524 24.541 1.00 83.20 C
ANISOU 2035 CD2 LEU A1078 11731 8160 11721 1012 230 -606 C
ATOM 2036 N ALA A1079 -7.646 246.261 26.168 1.00 76.64 N
ANISOU 2036 N ALA A1079 10003 7975 11142 1463 521 -79 N
ATOM 2037 CA ALA A1079 -8.930 245.558 26.270 1.00 77.73 C
ANISOU 2037 CA ALA A1079 9873 8167 11494 1561 685 47 C
ATOM 2038 C ALA A1079 -9.564 245.758 27.653 1.00 84.66 C
ANISOU 2038 C ALA A1079 10828 9082 12255 1763 972 97 C
ATOM 2039 O ALA A1079 -10.788 245.878 27.753 1.00 86.36 O
ANISOU 2039 O ALA A1079 10851 9301 12663 1903 1160 142 O
ATOM 2040 CB ALA A1079 -8.737 244.076 25.993 1.00 77.40 C
ANISOU 2040 CB ALA A1079 9624 8175 11610 1409 674 149 C
ATOM 2041 N ASN A1080 -8.724 245.808 28.713 1.00 81.65 N
ANISOU 2041 N ASN A1080 10738 8724 11562 1803 999 71 N
ATOM 2042 CA ASN A1080 -9.147 246.017 30.101 1.00 84.01 C
ANISOU 2042 CA ASN A1080 11257 9035 11626 2037 1270 109 C
ATOM 2043 C ASN A1080 -9.551 247.478 30.341 1.00 88.99 C
ANISOU 2043 C ASN A1080 12082 9595 12134 2224 1294 -23 C
ATOM 2044 O ASN A1080 -10.359 247.747 31.231 1.00 91.23 O
ANISOU 2044 O ASN A1080 12466 9879 12317 2463 1596 19 O
ATOM 2045 CB ASN A1080 -8.037 245.600 31.072 1.00 84.34 C
ANISOU 2045 CB ASN A1080 11615 9103 11326 2066 1180 85 C
ATOM 2046 CG ASN A1080 -7.783 244.110 31.129 1.00103.86 C
ANISOU 2046 CG ASN A1080 13982 11618 13862 1974 1229 246 C
ATOM 2047 OD1 ASN A1080 -8.705 243.290 31.172 1.00 98.49 O
ANISOU 2047 OD1 ASN A1080 13114 10931 13376 1974 1531 432 O
ATOM 2048 ND2 ASN A1080 -6.516 243.725 31.180 1.00 94.83 N
ANISOU 2048 ND2 ASN A1080 12951 10498 12581 1901 942 165 N
ATOM 2049 N GLU A1081 -8.995 248.411 29.538 1.00 83.91 N
ANISOU 2049 N GLU A1081 11520 8864 11499 2125 1017 -175 N
ATOM 2050 CA GLU A1081 -9.273 249.848 29.603 1.00 85.11 C
ANISOU 2050 CA GLU A1081 11901 8890 11546 2280 996 -312 C
ATOM 2051 C GLU A1081 -10.525 250.226 28.776 1.00 89.91 C
ANISOU 2051 C GLU A1081 12274 9464 12425 2406 1063 -269 C
ATOM 2052 O GLU A1081 -10.939 251.391 28.788 1.00 91.10 O
ANISOU 2052 O GLU A1081 12606 9496 12511 2592 1065 -365 O
ATOM 2053 CB GLU A1081 -8.052 250.654 29.125 1.00 85.36 C
ANISOU 2053 CB GLU A1081 12157 8786 11492 2090 706 -486 C
ATOM 2054 CG GLU A1081 -6.943 250.759 30.157 1.00 96.87 C
ANISOU 2054 CG GLU A1081 13881 10237 12690 2061 579 -634 C
ATOM 2055 CD GLU A1081 -5.714 251.518 29.696 1.00121.98 C
ANISOU 2055 CD GLU A1081 17182 13262 15902 1820 320 -837 C
ATOM 2056 OE1 GLU A1081 -5.827 252.736 29.430 1.00125.08 O
ANISOU 2056 OE1 GLU A1081 17779 13457 16288 1836 302 -946 O
ATOM 2057 OE2 GLU A1081 -4.628 250.900 29.632 1.00117.54 O
ANISOU 2057 OE2 GLU A1081 16506 12757 15396 1620 154 -895 O
ATOM 2058 N GLY A1082 -11.105 249.244 28.078 1.00 85.66 N
ANISOU 2058 N GLY A1082 11343 9009 12194 2323 1081 -151 N
ATOM 2059 CA GLY A1082 -12.309 249.416 27.268 1.00 86.51 C
ANISOU 2059 CA GLY A1082 11152 9099 12618 2456 1062 -145 C
ATOM 2060 C GLY A1082 -12.097 249.767 25.807 1.00 88.05 C
ANISOU 2060 C GLY A1082 11375 9187 12891 2378 722 -203 C
ATOM 2061 O GLY A1082 -13.061 249.770 25.035 1.00 89.24 O
ANISOU 2061 O GLY A1082 11281 9324 13302 2510 609 -218 O
ATOM 2062 N LYS A1083 -10.842 250.070 25.413 1.00 81.32 N
ANISOU 2062 N LYS A1083 10832 8244 11823 2181 562 -248 N
ATOM 2063 CA LYS A1083 -10.468 250.438 24.043 1.00 79.69 C
ANISOU 2063 CA LYS A1083 10775 7891 11612 2100 324 -279 C
ATOM 2064 C LYS A1083 -10.524 249.202 23.134 1.00 81.33 C
ANISOU 2064 C LYS A1083 10705 8181 12017 1964 195 -211 C
ATOM 2065 O LYS A1083 -9.558 248.440 23.068 1.00 79.05 O
ANISOU 2065 O LYS A1083 10405 7942 11687 1727 194 -180 O
ATOM 2066 CB LYS A1083 -9.067 251.084 24.017 1.00 81.03 C
ANISOU 2066 CB LYS A1083 11312 7922 11556 1893 298 -350 C
ATOM 2067 CG LYS A1083 -8.963 252.385 24.801 1.00 93.85 C
ANISOU 2067 CG LYS A1083 13260 9403 12997 2008 368 -459 C
ATOM 2068 CD LYS A1083 -7.514 252.723 25.113 1.00102.53 C
ANISOU 2068 CD LYS A1083 14576 10406 13974 1742 348 -568 C
ATOM 2069 CE LYS A1083 -7.370 253.949 25.981 1.00115.58 C
ANISOU 2069 CE LYS A1083 16556 11896 15463 1838 377 -717 C
ATOM 2070 NZ LYS A1083 -7.807 253.699 27.382 1.00127.04 N
ANISOU 2070 NZ LYS A1083 17965 13511 16795 2037 470 -741 N
ATOM 2071 N VAL A1084 -11.670 248.997 22.457 1.00 78.65 N
ANISOU 2071 N VAL A1084 10127 7845 11910 2135 58 -215 N
ATOM 2072 CA VAL A1084 -11.908 247.839 21.586 1.00 77.82 C
ANISOU 2072 CA VAL A1084 9753 7790 12025 2041 -118 -193 C
ATOM 2073 C VAL A1084 -11.096 247.909 20.277 1.00 79.44 C
ANISOU 2073 C VAL A1084 10284 7858 12043 1949 -335 -210 C
ATOM 2074 O VAL A1084 -10.403 246.941 19.958 1.00 77.39 O
ANISOU 2074 O VAL A1084 9973 7643 11791 1739 -348 -174 O
ATOM 2075 CB VAL A1084 -13.412 247.574 21.288 1.00 84.88 C
ANISOU 2075 CB VAL A1084 10235 8720 13297 2253 -252 -247 C
ATOM 2076 CG1 VAL A1084 -14.052 246.759 22.403 1.00 85.91 C
ANISOU 2076 CG1 VAL A1084 9920 8996 13725 2200 49 -187 C
ATOM 2077 CG2 VAL A1084 -14.194 248.865 21.032 1.00 87.40 C
ANISOU 2077 CG2 VAL A1084 10688 8932 13588 2593 -382 -339 C
ATOM 2078 N LYS A1085 -11.184 249.026 19.528 1.00 76.42 N
ANISOU 2078 N LYS A1085 10270 7287 11479 2126 -470 -254 N
ATOM 2079 CA LYS A1085 -10.503 249.205 18.242 1.00 76.04 C
ANISOU 2079 CA LYS A1085 10629 7057 11207 2087 -604 -249 C
ATOM 2080 C LYS A1085 -8.970 249.257 18.383 1.00 77.78 C
ANISOU 2080 C LYS A1085 11079 7230 11243 1777 -365 -210 C
ATOM 2081 O LYS A1085 -8.272 248.736 17.510 1.00 76.62 O
ANISOU 2081 O LYS A1085 11068 7029 11015 1647 -380 -187 O
ATOM 2082 CB LYS A1085 -11.007 250.470 17.526 1.00 81.48 C
ANISOU 2082 CB LYS A1085 11738 7509 11711 2390 -758 -283 C
ATOM 2083 CG LYS A1085 -12.470 250.407 17.080 1.00 99.50 C
ANISOU 2083 CG LYS A1085 13799 9814 14194 2749 -1103 -367 C
ATOM 2084 CD LYS A1085 -12.650 249.812 15.686 1.00109.85 C
ANISOU 2084 CD LYS A1085 15250 11041 15449 2858 -1459 -407 C
ATOM 2085 CE LYS A1085 -14.101 249.802 15.270 1.00123.40 C
ANISOU 2085 CE LYS A1085 16701 12770 17415 3235 -1886 -549 C
ATOM 2086 NZ LYS A1085 -14.281 249.227 13.911 1.00134.30 N
ANISOU 2086 NZ LYS A1085 18272 14050 18707 3380 -2314 -629 N
ATOM 2087 N GLU A1086 -8.456 249.876 19.469 1.00 73.84 N
ANISOU 2087 N GLU A1086 10612 6745 10700 1675 -159 -228 N
ATOM 2088 CA GLU A1086 -7.019 249.991 19.742 1.00 72.49 C
ANISOU 2088 CA GLU A1086 10566 6532 10446 1383 23 -249 C
ATOM 2089 C GLU A1086 -6.431 248.625 20.096 1.00 74.21 C
ANISOU 2089 C GLU A1086 10445 6964 10787 1192 47 -229 C
ATOM 2090 O GLU A1086 -5.278 248.362 19.754 1.00 73.30 O
ANISOU 2090 O GLU A1086 10379 6817 10654 977 128 -247 O
ATOM 2091 CB GLU A1086 -6.743 251.014 20.861 1.00 74.79 C
ANISOU 2091 CB GLU A1086 10974 6766 10675 1367 143 -326 C
ATOM 2092 CG GLU A1086 -5.359 251.644 20.788 1.00 86.78 C
ANISOU 2092 CG GLU A1086 12722 8108 12143 1093 280 -401 C
ATOM 2093 CD GLU A1086 -5.250 253.049 21.353 1.00110.61 C
ANISOU 2093 CD GLU A1086 16037 10909 15080 1115 346 -500 C
ATOM 2094 OE1 GLU A1086 -4.878 253.184 22.541 1.00103.92 O
ANISOU 2094 OE1 GLU A1086 15092 10142 14251 1057 346 -612 O
ATOM 2095 OE2 GLU A1086 -5.512 254.017 20.602 1.00106.26 O
ANISOU 2095 OE2 GLU A1086 15868 10080 14424 1206 382 -473 O
ATOM 2096 N ALA A1087 -7.230 247.754 20.759 1.00 70.00 N
ANISOU 2096 N ALA A1087 9572 6624 10400 1278 3 -190 N
ATOM 2097 CA ALA A1087 -6.836 246.391 21.132 1.00 68.10 C
ANISOU 2097 CA ALA A1087 9053 6551 10269 1142 23 -148 C
ATOM 2098 C ALA A1087 -6.794 245.479 19.905 1.00 70.54 C
ANISOU 2098 C ALA A1087 9321 6835 10646 1092 -102 -123 C
ATOM 2099 O ALA A1087 -5.885 244.656 19.800 1.00 69.15 O
ANISOU 2099 O ALA A1087 9085 6707 10480 936 -69 -118 O
ATOM 2100 CB ALA A1087 -7.792 245.825 22.171 1.00 69.28 C
ANISOU 2100 CB ALA A1087 8926 6843 10554 1250 90 -90 C
ATOM 2101 N GLN A1088 -7.771 245.634 18.980 1.00 67.46 N
ANISOU 2101 N GLN A1088 8980 6359 10293 1261 -278 -131 N
ATOM 2102 CA GLN A1088 -7.877 244.861 17.733 1.00 67.08 C
ANISOU 2102 CA GLN A1088 8971 6252 10265 1277 -468 -144 C
ATOM 2103 C GLN A1088 -6.690 245.151 16.805 1.00 70.98 C
ANISOU 2103 C GLN A1088 9845 6605 10520 1179 -379 -148 C
ATOM 2104 O GLN A1088 -6.135 244.216 16.221 1.00 70.48 O
ANISOU 2104 O GLN A1088 9774 6551 10454 1089 -390 -149 O
ATOM 2105 CB GLN A1088 -9.202 245.159 17.012 1.00 70.20 C
ANISOU 2105 CB GLN A1088 9373 6567 10733 1539 -750 -198 C
ATOM 2106 CG GLN A1088 -10.416 244.506 17.667 1.00 73.31 C
ANISOU 2106 CG GLN A1088 9273 7090 11493 1600 -829 -218 C
ATOM 2107 CD GLN A1088 -11.718 244.960 17.060 1.00 79.89 C
ANISOU 2107 CD GLN A1088 10033 7854 12470 1884 -1135 -320 C
ATOM 2108 OE1 GLN A1088 -11.988 246.156 16.924 1.00 77.31 O
ANISOU 2108 OE1 GLN A1088 9954 7435 11986 2094 -1179 -344 O
ATOM 2109 NE2 GLN A1088 -12.575 244.013 16.716 1.00 65.33 N
ANISOU 2109 NE2 GLN A1088 7826 6036 10961 1908 -1374 -403 N
ATOM 2110 N ALA A1089 -6.291 246.438 16.693 1.00 67.71 N
ANISOU 2110 N ALA A1089 9767 6037 9923 1190 -246 -150 N
ATOM 2111 CA ALA A1089 -5.150 246.885 15.886 1.00 67.91 C
ANISOU 2111 CA ALA A1089 10161 5881 9762 1065 -45 -142 C
ATOM 2112 C ALA A1089 -3.833 246.379 16.486 1.00 70.24 C
ANISOU 2112 C ALA A1089 10228 6286 10173 786 171 -171 C
ATOM 2113 O ALA A1089 -2.915 246.030 15.742 1.00 69.78 O
ANISOU 2113 O ALA A1089 10280 6160 10073 671 324 -174 O
ATOM 2114 CB ALA A1089 -5.136 248.405 15.794 1.00 70.28 C
ANISOU 2114 CB ALA A1089 10850 5951 9903 1122 74 -136 C
ATOM 2115 N ALA A1090 -3.760 246.322 17.833 1.00 66.11 N
ANISOU 2115 N ALA A1090 9401 5928 9788 715 174 -204 N
ATOM 2116 CA ALA A1090 -2.597 245.843 18.581 1.00 65.38 C
ANISOU 2116 CA ALA A1090 9070 5957 9813 517 276 -265 C
ATOM 2117 C ALA A1090 -2.450 244.324 18.451 1.00 69.27 C
ANISOU 2117 C ALA A1090 9323 6599 10397 508 199 -235 C
ATOM 2118 O ALA A1090 -1.336 243.809 18.553 1.00 68.41 O
ANISOU 2118 O ALA A1090 9079 6545 10369 377 280 -290 O
ATOM 2119 CB ALA A1090 -2.717 246.237 20.044 1.00 65.81 C
ANISOU 2119 CB ALA A1090 8983 6118 9904 532 240 -314 C
ATOM 2120 N ALA A1091 -3.573 243.613 18.234 1.00 66.78 N
ANISOU 2120 N ALA A1091 8934 6330 10109 650 33 -168 N
ATOM 2121 CA ALA A1091 -3.606 242.161 18.053 1.00 66.57 C
ANISOU 2121 CA ALA A1091 8721 6387 10187 645 -56 -140 C
ATOM 2122 C ALA A1091 -3.292 241.788 16.603 1.00 72.99 C
ANISOU 2122 C ALA A1091 9747 7077 10910 658 -72 -160 C
ATOM 2123 O ALA A1091 -2.931 240.642 16.337 1.00 72.46 O
ANISOU 2123 O ALA A1091 9584 7046 10903 631 -103 -167 O
ATOM 2124 CB ALA A1091 -4.964 241.611 18.457 1.00 67.36 C
ANISOU 2124 CB ALA A1091 8624 6543 10425 753 -202 -86 C
ATOM 2125 N GLU A1092 -3.420 242.754 15.671 1.00 72.38 N
ANISOU 2125 N GLU A1092 10021 6828 10652 729 -39 -167 N
ATOM 2126 CA GLU A1092 -3.124 242.560 14.249 1.00 74.38 C
ANISOU 2126 CA GLU A1092 10616 6922 10723 792 -14 -177 C
ATOM 2127 C GLU A1092 -1.606 242.481 14.007 1.00 79.59 C
ANISOU 2127 C GLU A1092 11314 7553 11372 620 319 -201 C
ATOM 2128 O GLU A1092 -1.182 241.777 13.091 1.00 80.59 O
ANISOU 2128 O GLU A1092 11591 7619 11412 656 379 -216 O
ATOM 2129 CB GLU A1092 -3.736 243.688 13.399 1.00 77.95 C
ANISOU 2129 CB GLU A1092 11520 7164 10934 967 -63 -157 C
ATOM 2130 CG GLU A1092 -3.997 243.292 11.954 1.00 93.38 C
ANISOU 2130 CG GLU A1092 13880 8955 12647 1163 -205 -174 C
ATOM 2131 CD GLU A1092 -3.568 244.309 10.913 1.00125.84 C
ANISOU 2131 CD GLU A1092 18616 12791 16409 1254 22 -124 C
ATOM 2132 OE1 GLU A1092 -2.717 243.959 10.064 1.00125.78 O
ANISOU 2132 OE1 GLU A1092 18888 12672 16231 1229 266 -113 O
ATOM 2133 OE2 GLU A1092 -4.087 245.449 10.935 1.00124.86 O
ANISOU 2133 OE2 GLU A1092 18736 12537 16169 1367 -11 -88 O
ATOM 2134 N GLN A1093 -0.793 243.182 14.833 1.00 75.97 N
ANISOU 2134 N GLN A1093 10701 7132 11032 443 525 -232 N
ATOM 2135 CA GLN A1093 0.669 243.197 14.703 1.00 76.84 C
ANISOU 2135 CA GLN A1093 10731 7217 11248 256 841 -298 C
ATOM 2136 C GLN A1093 1.294 241.862 15.170 1.00 78.67 C
ANISOU 2136 C GLN A1093 10582 7644 11664 229 771 -353 C
ATOM 2137 O GLN A1093 2.495 241.658 14.977 1.00 79.72 O
ANISOU 2137 O GLN A1093 10584 7778 11929 117 1003 -432 O
ATOM 2138 CB GLN A1093 1.302 244.413 15.417 1.00 79.49 C
ANISOU 2138 CB GLN A1093 10994 7496 11711 68 1018 -364 C
ATOM 2139 CG GLN A1093 1.276 244.389 16.942 1.00 97.99 C
ANISOU 2139 CG GLN A1093 12975 10037 14222 31 810 -436 C
ATOM 2140 CD GLN A1093 1.827 245.663 17.535 1.00121.96 C
ANISOU 2140 CD GLN A1093 16009 12968 17363 -137 931 -539 C
ATOM 2141 OE1 GLN A1093 3.040 245.821 17.707 1.00119.10 O
ANISOU 2141 OE1 GLN A1093 15839 12522 16893 -79 863 -512 O
ATOM 2142 NE2 GLN A1093 0.948 246.606 17.854 1.00114.61 N
ANISOU 2142 NE2 GLN A1093 14837 12026 16682 -344 1100 -686 N
ATOM 2143 N LEU A1094 0.471 240.946 15.739 1.00 72.41 N
ANISOU 2143 N LEU A1094 9622 6989 10902 339 479 -313 N
ATOM 2144 CA LEU A1094 0.882 239.597 16.145 1.00 70.83 C
ANISOU 2144 CA LEU A1094 9156 6923 10832 361 386 -335 C
ATOM 2145 C LEU A1094 1.100 238.737 14.909 1.00 74.89 C
ANISOU 2145 C LEU A1094 9842 7345 11267 434 439 -345 C
ATOM 2146 O LEU A1094 1.874 237.782 14.966 1.00 75.57 O
ANISOU 2146 O LEU A1094 9762 7493 11459 444 473 -394 O
ATOM 2147 CB LEU A1094 -0.163 238.928 17.056 1.00 69.30 C
ANISOU 2147 CB LEU A1094 8810 6830 10690 442 134 -260 C
ATOM 2148 CG LEU A1094 -0.263 239.414 18.496 1.00 73.43 C
ANISOU 2148 CG LEU A1094 9168 7468 11263 422 92 -252 C
ATOM 2149 CD1 LEU A1094 -1.611 239.069 19.083 1.00 73.16 C
ANISOU 2149 CD1 LEU A1094 9092 7462 11245 509 -40 -145 C
ATOM 2150 CD2 LEU A1094 0.804 238.802 19.352 1.00 76.13 C
ANISOU 2150 CD2 LEU A1094 9298 7927 11700 414 74 -316 C
ATOM 2151 N LYS A1095 0.408 239.073 13.794 1.00 71.04 N
ANISOU 2151 N LYS A1095 9728 6696 10569 529 418 -311 N
ATOM 2152 CA LYS A1095 0.502 238.373 12.504 1.00 71.91 C
ANISOU 2152 CA LYS A1095 10133 6677 10513 650 440 -336 C
ATOM 2153 C LYS A1095 1.913 238.471 11.914 1.00 75.43 C
ANISOU 2153 C LYS A1095 10652 7065 10944 586 856 -384 C
ATOM 2154 O LYS A1095 2.355 237.541 11.243 1.00 76.06 O
ANISOU 2154 O LYS A1095 10816 7108 10975 675 922 -429 O
ATOM 2155 CB LYS A1095 -0.522 238.926 11.501 1.00 75.88 C
ANISOU 2155 CB LYS A1095 11087 7002 10744 812 286 -310 C
ATOM 2156 CG LYS A1095 -1.950 238.481 11.772 1.00 92.29 C
ANISOU 2156 CG LYS A1095 13046 9115 12906 912 -156 -314 C
ATOM 2157 CD LYS A1095 -2.903 239.024 10.724 1.00106.17 C
ANISOU 2157 CD LYS A1095 15233 10695 14412 1126 -386 -337 C
ATOM 2158 CE LYS A1095 -4.334 238.648 11.012 1.00118.81 C
ANISOU 2158 CE LYS A1095 16605 12332 16205 1211 -831 -385 C
ATOM 2159 NZ LYS A1095 -5.272 239.293 10.056 1.00131.59 N
ANISOU 2159 NZ LYS A1095 18608 13788 17604 1465 -1132 -443 N
ATOM 2160 N THR A1096 2.611 239.593 12.183 1.00 70.96 N
ANISOU 2160 N THR A1096 10034 6472 10454 425 1154 -391 N
ATOM 2161 CA THR A1096 3.977 239.876 11.739 1.00 72.40 C
ANISOU 2161 CA THR A1096 10187 6583 10738 303 1626 -452 C
ATOM 2162 C THR A1096 4.959 238.950 12.474 1.00 74.40 C
ANISOU 2162 C THR A1096 9916 7033 11318 253 1617 -568 C
ATOM 2163 O THR A1096 5.880 238.424 11.852 1.00 76.26 O
ANISOU 2163 O THR A1096 10116 7239 11620 277 1901 -635 O
ATOM 2164 CB THR A1096 4.304 241.367 11.964 1.00 80.39 C
ANISOU 2164 CB THR A1096 11243 7481 11822 105 1894 -445 C
ATOM 2165 OG1 THR A1096 3.207 242.170 11.514 1.00 79.29 O
ANISOU 2165 OG1 THR A1096 11577 7178 11373 213 1781 -332 O
ATOM 2166 CG2 THR A1096 5.589 241.804 11.268 1.00 82.06 C
ANISOU 2166 CG2 THR A1096 11495 7532 12153 -50 2480 -493 C
ATOM 2167 N THR A1097 4.748 238.751 13.789 1.00 67.70 N
ANISOU 2167 N THR A1097 8702 6372 10648 223 1297 -594 N
ATOM 2168 CA THR A1097 5.566 237.891 14.650 1.00 67.08 C
ANISOU 2168 CA THR A1097 8178 6475 10836 240 1182 -702 C
ATOM 2169 C THR A1097 5.347 236.426 14.267 1.00 70.75 C
ANISOU 2169 C THR A1097 8710 6955 11219 433 1032 -674 C
ATOM 2170 O THR A1097 6.294 235.637 14.255 1.00 71.35 O
ANISOU 2170 O THR A1097 8565 7088 11457 500 1107 -773 O
ATOM 2171 CB THR A1097 5.210 238.150 16.123 1.00 69.39 C
ANISOU 2171 CB THR A1097 8237 6913 11216 214 868 -706 C
ATOM 2172 OG1 THR A1097 5.225 239.557 16.367 1.00 67.99 O
ANISOU 2172 OG1 THR A1097 8091 6673 11068 49 981 -735 O
ATOM 2173 CG2 THR A1097 6.141 237.427 17.095 1.00 67.21 C
ANISOU 2173 CG2 THR A1097 7558 6802 11177 274 710 -836 C
ATOM 2174 N ARG A1098 4.087 236.083 13.950 1.00 66.42 N
ANISOU 2174 N ARG A1098 8450 6336 10453 525 806 -563 N
ATOM 2175 CA ARG A1098 3.629 234.758 13.555 1.00 66.19 C
ANISOU 2175 CA ARG A1098 8537 6259 10352 678 614 -544 C
ATOM 2176 C ARG A1098 4.344 234.294 12.284 1.00 73.03 C
ANISOU 2176 C ARG A1098 9627 7007 11114 779 869 -617 C
ATOM 2177 O ARG A1098 4.828 233.166 12.249 1.00 73.30 O
ANISOU 2177 O ARG A1098 9568 7055 11226 893 837 -675 O
ATOM 2178 CB ARG A1098 2.105 234.787 13.357 1.00 65.56 C
ANISOU 2178 CB ARG A1098 8688 6095 10127 713 336 -456 C
ATOM 2179 CG ARG A1098 1.462 233.430 13.112 1.00 75.32 C
ANISOU 2179 CG ARG A1098 9991 7254 11374 820 77 -458 C
ATOM 2180 CD ARG A1098 0.018 233.556 12.662 1.00 83.23 C
ANISOU 2180 CD ARG A1098 11186 8143 12294 851 -196 -434 C
ATOM 2181 NE ARG A1098 -0.104 234.229 11.367 1.00 89.85 N
ANISOU 2181 NE ARG A1098 12441 8843 12857 948 -144 -479 N
ATOM 2182 CZ ARG A1098 -1.257 234.489 10.761 1.00104.39 C
ANISOU 2182 CZ ARG A1098 14511 10569 14584 1038 -422 -501 C
ATOM 2183 NH1 ARG A1098 -2.405 234.123 11.317 1.00 88.27 N
ANISOU 2183 NH1 ARG A1098 12237 8543 12758 1004 -740 -496 N
ATOM 2184 NH2 ARG A1098 -1.271 235.114 9.592 1.00 96.33 N
ANISOU 2184 NH2 ARG A1098 13961 9401 13241 1181 -376 -535 N
ATOM 2185 N ASN A1099 4.448 235.176 11.270 1.00 71.94 N
ANISOU 2185 N ASN A1099 9821 6731 10781 761 1156 -608 N
ATOM 2186 CA ASN A1099 5.083 234.876 9.983 1.00 74.90 C
ANISOU 2186 CA ASN A1099 10521 6957 10980 882 1485 -659 C
ATOM 2187 C ASN A1099 6.621 234.859 10.054 1.00 81.64 C
ANISOU 2187 C ASN A1099 11040 7878 12102 818 1924 -761 C
ATOM 2188 O ASN A1099 7.248 234.066 9.346 1.00 83.58 O
ANISOU 2188 O ASN A1099 11379 8068 12312 967 2130 -832 O
ATOM 2189 CB ASN A1099 4.639 235.888 8.915 1.00 76.06 C
ANISOU 2189 CB ASN A1099 11227 6896 10777 915 1675 -589 C
ATOM 2190 CG ASN A1099 3.145 235.968 8.667 1.00 95.82 C
ANISOU 2190 CG ASN A1099 14061 9315 13030 1030 1219 -534 C
ATOM 2191 OD1 ASN A1099 2.384 235.013 8.881 1.00 87.17 O
ANISOU 2191 OD1 ASN A1099 12887 8256 11979 1113 798 -565 O
ATOM 2192 ND2 ASN A1099 2.691 237.126 8.206 1.00 89.11 N
ANISOU 2192 ND2 ASN A1099 13581 8330 11947 1040 1296 -461 N
ATOM 2193 N ALA A1100 7.220 235.737 10.884 1.00 78.28 N
ANISOU 2193 N ALA A1100 10216 7558 11968 609 2056 -795 N
ATOM 2194 CA ALA A1100 8.671 235.891 11.004 1.00 80.99 C
ANISOU 2194 CA ALA A1100 10138 7959 12674 509 2450 -937 C
ATOM 2195 C ALA A1100 9.329 234.979 12.048 1.00 84.77 C
ANISOU 2195 C ALA A1100 10057 8654 13496 583 2179 -1071 C
ATOM 2196 O ALA A1100 10.519 234.685 11.895 1.00 87.87 O
ANISOU 2196 O ALA A1100 10115 9089 14182 608 2462 -1222 O
ATOM 2197 CB ALA A1100 9.009 237.338 11.323 1.00 82.79 C
ANISOU 2197 CB ALA A1100 10223 8146 13087 235 2699 -951 C
ATOM 2198 N TYR A1101 8.599 234.544 13.102 1.00 77.92 N
ANISOU 2198 N TYR A1101 9096 7908 12602 637 1666 -1019 N
ATOM 2199 CA TYR A1101 9.210 233.719 14.153 1.00 77.77 C
ANISOU 2199 CA TYR A1101 8646 8061 12842 755 1386 -1128 C
ATOM 2200 C TYR A1101 8.450 232.418 14.483 1.00 78.73 C
ANISOU 2200 C TYR A1101 8941 8180 12793 962 1003 -1031 C
ATOM 2201 O TYR A1101 9.076 231.357 14.502 1.00 79.56 O
ANISOU 2201 O TYR A1101 8917 8307 13005 1156 955 -1112 O
ATOM 2202 CB TYR A1101 9.382 234.532 15.451 1.00 78.58 C
ANISOU 2202 CB TYR A1101 8409 8300 13147 622 1168 -1193 C
ATOM 2203 CG TYR A1101 10.263 235.755 15.315 1.00 83.21 C
ANISOU 2203 CG TYR A1101 8729 8867 14019 385 1504 -1337 C
ATOM 2204 CD1 TYR A1101 11.646 235.660 15.441 1.00 88.93 C
ANISOU 2204 CD1 TYR A1101 8937 9670 15181 379 1654 -1576 C
ATOM 2205 CD2 TYR A1101 9.712 237.015 15.105 1.00 83.27 C
ANISOU 2205 CD2 TYR A1101 8972 8759 13906 167 1663 -1252 C
ATOM 2206 CE1 TYR A1101 12.462 236.785 15.330 1.00 92.88 C
ANISOU 2206 CE1 TYR A1101 9135 10118 16037 111 1989 -1732 C
ATOM 2207 CE2 TYR A1101 10.518 238.148 14.991 1.00 87.11 C
ANISOU 2207 CE2 TYR A1101 9238 9172 14689 -85 2002 -1382 C
ATOM 2208 CZ TYR A1101 11.893 238.028 15.107 1.00 98.00 C
ANISOU 2208 CZ TYR A1101 10071 10616 16548 -137 2177 -1625 C
ATOM 2209 OH TYR A1101 12.692 239.140 15.006 1.00102.26 O
ANISOU 2209 OH TYR A1101 10337 11050 17468 -433 2536 -1776 O
ATOM 2210 N ILE A1102 7.137 232.505 14.787 1.00 72.03 N
ANISOU 2210 N ILE A1102 8351 7288 11728 919 750 -870 N
ATOM 2211 CA ILE A1102 6.292 231.378 15.216 1.00 70.21 C
ANISOU 2211 CA ILE A1102 8260 7015 11402 1045 426 -765 C
ATOM 2212 C ILE A1102 6.189 230.272 14.143 1.00 74.39 C
ANISOU 2212 C ILE A1102 9059 7383 11822 1193 458 -781 C
ATOM 2213 O ILE A1102 6.266 229.094 14.498 1.00 74.65 O
ANISOU 2213 O ILE A1102 9078 7379 11906 1345 283 -779 O
ATOM 2214 CB ILE A1102 4.891 231.868 15.670 1.00 71.01 C
ANISOU 2214 CB ILE A1102 8518 7090 11371 931 237 -612 C
ATOM 2215 CG1 ILE A1102 4.976 233.044 16.698 1.00 70.81 C
ANISOU 2215 CG1 ILE A1102 8294 7202 11409 808 219 -611 C
ATOM 2216 CG2 ILE A1102 4.003 230.720 16.185 1.00 71.19 C
ANISOU 2216 CG2 ILE A1102 8636 7035 11376 1010 -24 -499 C
ATOM 2217 CD1 ILE A1102 5.852 232.826 18.023 1.00 81.00 C
ANISOU 2217 CD1 ILE A1102 9276 8644 12856 898 62 -691 C
ATOM 2218 N GLN A1103 6.039 230.642 12.859 1.00 71.09 N
ANISOU 2218 N GLN A1103 8941 6843 11228 1176 675 -802 N
ATOM 2219 CA GLN A1103 5.953 229.685 11.748 1.00 72.12 C
ANISOU 2219 CA GLN A1103 9406 6797 11198 1344 698 -851 C
ATOM 2220 C GLN A1103 7.286 228.929 11.569 1.00 77.26 C
ANISOU 2220 C GLN A1103 9882 7478 11994 1522 913 -984 C
ATOM 2221 O GLN A1103 7.267 227.735 11.272 1.00 77.27 O
ANISOU 2221 O GLN A1103 10041 7363 11954 1704 792 -1024 O
ATOM 2222 CB GLN A1103 5.554 230.401 10.449 1.00 74.58 C
ANISOU 2222 CB GLN A1103 10153 6965 11218 1335 883 -849 C
ATOM 2223 CG GLN A1103 4.977 229.477 9.377 1.00 97.44 C
ANISOU 2223 CG GLN A1103 13510 9644 13868 1516 727 -900 C
ATOM 2224 CD GLN A1103 4.286 230.222 8.254 1.00124.69 C
ANISOU 2224 CD GLN A1103 17466 12940 16971 1551 750 -890 C
ATOM 2225 OE1 GLN A1103 4.745 231.269 7.772 1.00122.35 O
ANISOU 2225 OE1 GLN A1103 17313 12635 16538 1516 1119 -863 O
ATOM 2226 NE2 GLN A1103 3.175 229.672 7.786 1.00119.18 N
ANISOU 2226 NE2 GLN A1103 17070 12084 16127 1635 345 -925 N
ATOM 2227 N LYS A1104 8.428 229.621 11.777 1.00 75.06 N
ANISOU 2227 N LYS A1104 9250 7339 11930 1467 1219 -1072 N
ATOM 2228 CA LYS A1104 9.775 229.053 11.666 1.00 77.95 C
ANISOU 2228 CA LYS A1104 9324 7763 12531 1636 1449 -1234 C
ATOM 2229 C LYS A1104 10.081 228.092 12.819 1.00 81.34 C
ANISOU 2229 C LYS A1104 9451 8292 13163 1799 1083 -1270 C
ATOM 2230 O LYS A1104 10.822 227.132 12.608 1.00 83.14 O
ANISOU 2230 O LYS A1104 9601 8496 13493 2044 1129 -1382 O
ATOM 2231 CB LYS A1104 10.840 230.155 11.605 1.00 82.94 C
ANISOU 2231 CB LYS A1104 9586 8499 13430 1484 1873 -1343 C
ATOM 2232 CG LYS A1104 10.988 230.785 10.229 1.00102.04 C
ANISOU 2232 CG LYS A1104 12354 10759 15659 1427 2414 -1332 C
ATOM 2233 CD LYS A1104 12.043 231.880 10.231 1.00116.93 C
ANISOU 2233 CD LYS A1104 13840 12700 17887 1221 2895 -1433 C
ATOM 2234 CE LYS A1104 12.162 232.556 8.888 1.00132.03 C
ANISOU 2234 CE LYS A1104 16190 14404 19571 1162 3512 -1378 C
ATOM 2235 NZ LYS A1104 13.157 233.660 8.914 1.00145.78 N
ANISOU 2235 NZ LYS A1104 17533 16148 21708 902 4040 -1465 N
ATOM 2236 N TYR A1105 9.527 228.346 14.026 1.00 75.85 N
ANISOU 2236 N TYR A1105 8632 7688 12498 1703 740 -1174 N
ATOM 2237 CA TYR A1105 9.722 227.471 15.188 1.00 76.01 C
ANISOU 2237 CA TYR A1105 8491 7764 12625 1891 385 -1171 C
ATOM 2238 C TYR A1105 8.909 226.186 15.015 1.00 77.30 C
ANISOU 2238 C TYR A1105 9044 7720 12606 2026 185 -1055 C
ATOM 2239 O TYR A1105 9.440 225.105 15.269 1.00 78.32 O
ANISOU 2239 O TYR A1105 9153 7797 12807 2284 63 -1107 O
ATOM 2240 CB TYR A1105 9.370 228.172 16.525 1.00 76.34 C
ANISOU 2240 CB TYR A1105 8376 7938 12690 1776 127 -1098 C
ATOM 2241 CG TYR A1105 9.261 227.214 17.699 1.00 79.62 C
ANISOU 2241 CG TYR A1105 8835 8341 13077 1995 -237 -1026 C
ATOM 2242 CD1 TYR A1105 10.384 226.555 18.196 1.00 84.51 C
ANISOU 2242 CD1 TYR A1105 9211 9029 13871 2289 -386 -1177 C
ATOM 2243 CD2 TYR A1105 8.026 226.927 18.279 1.00 78.72 C
ANISOU 2243 CD2 TYR A1105 9028 8116 12765 1933 -409 -805 C
ATOM 2244 CE1 TYR A1105 10.284 225.645 19.246 1.00 86.04 C
ANISOU 2244 CE1 TYR A1105 9555 9165 13973 2542 -719 -1089 C
ATOM 2245 CE2 TYR A1105 7.914 226.016 19.330 1.00 80.59 C
ANISOU 2245 CE2 TYR A1105 9397 8285 12939 2141 -663 -703 C
ATOM 2246 CZ TYR A1105 9.048 225.380 19.813 1.00 91.67 C
ANISOU 2246 CZ TYR A1105 10644 9739 14446 2459 -827 -835 C
ATOM 2247 OH TYR A1105 8.950 224.487 20.853 1.00 95.68 O
ANISOU 2247 OH TYR A1105 11378 10143 14834 2712 -1081 -717 O
ATOM 2248 N LEU A1106 7.625 226.313 14.599 1.00 70.80 N
ANISOU 2248 N LEU A1106 8558 6759 11583 1856 131 -918 N
ATOM 2249 CA LEU A1106 6.706 225.196 14.358 1.00 70.15 C
ANISOU 2249 CA LEU A1106 8821 6437 11394 1907 -62 -835 C
ATOM 2250 C LEU A1106 7.289 224.239 13.302 1.00 75.13 C
ANISOU 2250 C LEU A1106 9646 6914 11986 2128 47 -972 C
ATOM 2251 O LEU A1106 7.302 223.030 13.528 1.00 76.25 O
ANISOU 2251 O LEU A1106 9915 6896 12160 2300 -117 -967 O
ATOM 2252 CB LEU A1106 5.315 225.721 13.929 1.00 68.53 C
ANISOU 2252 CB LEU A1106 8845 6136 11058 1678 -135 -738 C
ATOM 2253 CG LEU A1106 4.291 224.698 13.384 1.00 74.49 C
ANISOU 2253 CG LEU A1106 9928 6610 11766 1678 -338 -720 C
ATOM 2254 CD1 LEU A1106 3.691 223.840 14.500 1.00 74.80 C
ANISOU 2254 CD1 LEU A1106 9943 6534 11942 1648 -537 -576 C
ATOM 2255 CD2 LEU A1106 3.188 225.395 12.603 1.00 76.08 C
ANISOU 2255 CD2 LEU A1106 10312 6744 11851 1515 -408 -722 C
ATOM 2256 N GLU A 219 7.803 224.786 12.184 1.00 72.36 N
ANISOU 2256 N GLU A 219 11306 6137 10052 1583 -192 526 N
ATOM 2257 CA GLU A 219 8.409 224.026 11.092 1.00 70.84 C
ANISOU 2257 CA GLU A 219 11107 6047 9760 1506 -227 619 C
ATOM 2258 C GLU A 219 9.663 223.270 11.554 1.00 72.69 C
ANISOU 2258 C GLU A 219 11321 6360 9940 1327 -179 563 C
ATOM 2259 O GLU A 219 9.861 222.121 11.148 1.00 71.51 O
ANISOU 2259 O GLU A 219 11093 6367 9709 1276 -204 576 O
ATOM 2260 CB GLU A 219 8.754 224.957 9.924 1.00 73.42 C
ANISOU 2260 CB GLU A 219 11574 6242 10080 1522 -244 760 C
ATOM 2261 N ARG A 220 10.487 223.902 12.418 1.00 68.48 N
ANISOU 2261 N ARG A 220 10853 5716 9451 1236 -115 494 N
ATOM 2262 CA ARG A 220 11.725 223.321 12.949 1.00 66.83 C
ANISOU 2262 CA ARG A 220 10626 5565 9200 1068 -71 435 C
ATOM 2263 C ARG A 220 11.441 222.174 13.932 1.00 68.44 C
ANISOU 2263 C ARG A 220 10697 5929 9377 1054 -67 321 C
ATOM 2264 O ARG A 220 12.150 221.167 13.906 1.00 66.79 O
ANISOU 2264 O ARG A 220 10431 5845 9101 951 -63 311 O
ATOM 2265 CB ARG A 220 12.583 224.403 13.626 1.00 68.32 C
ANISOU 2265 CB ARG A 220 10922 5584 9454 984 -14 388 C
ATOM 2266 CG ARG A 220 14.047 224.013 13.802 1.00 79.80 C
ANISOU 2266 CG ARG A 220 12378 7073 10868 803 22 368 C
ATOM 2267 N ALA A 221 10.418 222.338 14.800 1.00 64.39 N
ANISOU 2267 N ALA A 221 10140 5408 8918 1157 -61 239 N
ATOM 2268 CA ALA A 221 10.013 221.352 15.803 1.00 62.21 C
ANISOU 2268 CA ALA A 221 9745 5270 8623 1157 -48 133 C
ATOM 2269 C ALA A 221 9.375 220.131 15.147 1.00 64.16 C
ANISOU 2269 C ALA A 221 9875 5688 8814 1197 -99 176 C
ATOM 2270 O ALA A 221 9.550 219.014 15.643 1.00 62.62 O
ANISOU 2270 O ALA A 221 9590 5630 8572 1136 -90 121 O
ATOM 2271 CB ALA A 221 9.046 221.979 16.793 1.00 63.61 C
ANISOU 2271 CB ALA A 221 9915 5379 8876 1268 -21 45 C
ATOM 2272 N ARG A 222 8.652 220.347 14.027 1.00 60.40 N
ANISOU 2272 N ARG A 222 9405 5203 8343 1298 -156 275 N
ATOM 2273 CA ARG A 222 7.973 219.301 13.256 1.00 59.32 C
ANISOU 2273 CA ARG A 222 9167 5215 8156 1344 -219 322 C
ATOM 2274 C ARG A 222 8.998 218.398 12.551 1.00 62.36 C
ANISOU 2274 C ARG A 222 9551 5696 8446 1220 -230 370 C
ATOM 2275 O ARG A 222 8.854 217.172 12.606 1.00 61.13 O
ANISOU 2275 O ARG A 222 9294 5690 8244 1192 -247 341 O
ATOM 2276 CB ARG A 222 6.998 219.930 12.244 1.00 60.34 C
ANISOU 2276 CB ARG A 222 9320 5293 8315 1486 -283 417 C
ATOM 2277 CG ARG A 222 6.074 218.948 11.537 1.00 68.28 C
ANISOU 2277 CG ARG A 222 10212 6447 9285 1553 -359 451 C
ATOM 2278 CD ARG A 222 5.131 219.666 10.593 1.00 78.38 C
ANISOU 2278 CD ARG A 222 11518 7668 10595 1699 -430 542 C
ATOM 2279 N SER A 223 10.039 218.998 11.919 1.00 59.01 N
ANISOU 2279 N SER A 223 9239 5183 7998 1146 -214 440 N
ATOM 2280 CA SER A 223 11.091 218.271 11.199 1.00 57.78 C
ANISOU 2280 CA SER A 223 9093 5105 7756 1032 -213 490 C
ATOM 2281 C SER A 223 11.903 217.378 12.140 1.00 59.62 C
ANISOU 2281 C SER A 223 9263 5428 7963 911 -169 398 C
ATOM 2282 O SER A 223 12.174 216.230 11.787 1.00 58.63 O
ANISOU 2282 O SER A 223 9073 5436 7769 862 -185 404 O
ATOM 2283 CB SER A 223 12.013 219.232 10.453 1.00 63.10 C
ANISOU 2283 CB SER A 223 9901 5651 8424 978 -190 581 C
ATOM 2284 OG SER A 223 12.855 219.964 11.329 1.00 74.57 O
ANISOU 2284 OG SER A 223 11412 6991 9929 892 -127 525 O
ATOM 2285 N THR A 224 12.257 217.889 13.342 1.00 55.22 N
ANISOU 2285 N THR A 224 8725 4798 7459 869 -117 309 N
ATOM 2286 CA THR A 224 13.023 217.154 14.362 1.00 53.44 C
ANISOU 2286 CA THR A 224 8447 4647 7210 762 -79 216 C
ATOM 2287 C THR A 224 12.244 215.903 14.811 1.00 55.59 C
ANISOU 2287 C THR A 224 8592 5073 7455 800 -98 161 C
ATOM 2288 O THR A 224 12.833 214.822 14.898 1.00 54.08 O
ANISOU 2288 O THR A 224 8344 4996 7207 721 -94 143 O
ATOM 2289 CB THR A 224 13.369 218.078 15.545 1.00 59.59 C
ANISOU 2289 CB THR A 224 9282 5309 8051 731 -31 130 C
ATOM 2290 OG1 THR A 224 14.011 219.247 15.043 1.00 58.82 O
ANISOU 2290 OG1 THR A 224 9302 5060 7989 697 -16 188 O
ATOM 2291 CG2 THR A 224 14.273 217.409 16.581 1.00 57.30 C
ANISOU 2291 CG2 THR A 224 8950 5090 7732 616 1 39 C
ATOM 2292 N LEU A 225 10.922 216.050 15.056 1.00 51.99 N
ANISOU 2292 N LEU A 225 8092 4618 7045 923 -116 139 N
ATOM 2293 CA LEU A 225 10.049 214.952 15.467 1.00 50.70 C
ANISOU 2293 CA LEU A 225 7805 4589 6869 966 -130 91 C
ATOM 2294 C LEU A 225 9.878 213.927 14.339 1.00 53.40 C
ANISOU 2294 C LEU A 225 8090 5048 7151 965 -186 160 C
ATOM 2295 O LEU A 225 9.921 212.730 14.615 1.00 51.79 O
ANISOU 2295 O LEU A 225 7802 4966 6908 921 -186 124 O
ATOM 2296 CB LEU A 225 8.687 215.468 15.954 1.00 51.63 C
ANISOU 2296 CB LEU A 225 7885 4670 7060 1099 -130 55 C
ATOM 2297 CG LEU A 225 8.676 216.061 17.373 1.00 56.92 C
ANISOU 2297 CG LEU A 225 8578 5272 7777 1102 -65 -49 C
ATOM 2298 CD1 LEU A 225 7.370 216.757 17.666 1.00 58.34 C
ANISOU 2298 CD1 LEU A 225 8736 5396 8035 1246 -62 -71 C
ATOM 2299 CD2 LEU A 225 8.935 214.997 18.432 1.00 58.34 C
ANISOU 2299 CD2 LEU A 225 8683 5568 7917 1031 -28 -133 C
ATOM 2300 N GLN A 226 9.745 214.385 13.075 1.00 50.62 N
ANISOU 2300 N GLN A 226 7792 4655 6786 1010 -234 258 N
ATOM 2301 CA GLN A 226 9.634 213.500 11.907 1.00 50.01 C
ANISOU 2301 CA GLN A 226 7680 4680 6641 1011 -292 324 C
ATOM 2302 C GLN A 226 10.939 212.711 11.712 1.00 53.25 C
ANISOU 2302 C GLN A 226 8102 5154 6976 880 -267 329 C
ATOM 2303 O GLN A 226 10.888 211.533 11.359 1.00 51.46 O
ANISOU 2303 O GLN A 226 7808 5048 6697 856 -293 327 O
ATOM 2304 CB GLN A 226 9.285 214.297 10.643 1.00 52.27 C
ANISOU 2304 CB GLN A 226 8042 4898 6922 1090 -346 431 C
ATOM 2305 CG GLN A 226 7.802 214.662 10.550 1.00 67.80 C
ANISOU 2305 CG GLN A 226 9959 6853 8948 1236 -399 437 C
ATOM 2306 CD GLN A 226 7.484 215.729 9.521 1.00 87.67 C
ANISOU 2306 CD GLN A 226 12569 9269 11473 1325 -445 539 C
ATOM 2307 OE1 GLN A 226 8.351 216.216 8.780 1.00 83.72 O
ANISOU 2307 OE1 GLN A 226 12179 8704 10929 1278 -436 616 O
ATOM 2308 NE2 GLN A 226 6.220 216.127 9.461 1.00 78.84 N
ANISOU 2308 NE2 GLN A 226 11407 8134 10414 1460 -494 546 N
ATOM 2309 N LYS A 227 12.099 213.358 11.992 1.00 50.81 N
ANISOU 2309 N LYS A 227 7875 4761 6671 794 -214 330 N
ATOM 2310 CA LYS A 227 13.437 212.763 11.929 1.00 49.98 C
ANISOU 2310 CA LYS A 227 7779 4703 6509 668 -181 330 C
ATOM 2311 C LYS A 227 13.588 211.663 12.983 1.00 52.82 C
ANISOU 2311 C LYS A 227 8045 5166 6858 616 -159 237 C
ATOM 2312 O LYS A 227 14.229 210.650 12.710 1.00 52.46 O
ANISOU 2312 O LYS A 227 7964 5215 6754 549 -158 241 O
ATOM 2313 CB LYS A 227 14.529 213.830 12.123 1.00 53.32 C
ANISOU 2313 CB LYS A 227 8299 5002 6958 593 -131 343 C
ATOM 2314 CG LYS A 227 14.848 214.636 10.873 1.00 67.29 C
ANISOU 2314 CG LYS A 227 10168 6687 8710 600 -138 455 C
ATOM 2315 N GLU A 228 12.986 211.861 14.175 1.00 48.57 N
ANISOU 2315 N GLU A 228 7471 4609 6373 652 -139 156 N
ATOM 2316 CA GLU A 228 13.004 210.897 15.282 1.00 47.00 C
ANISOU 2316 CA GLU A 228 7192 4502 6165 615 -115 70 C
ATOM 2317 C GLU A 228 12.129 209.683 14.963 1.00 50.28 C
ANISOU 2317 C GLU A 228 7508 5040 6555 658 -152 72 C
ATOM 2318 O GLU A 228 12.483 208.575 15.368 1.00 49.27 O
ANISOU 2318 O GLU A 228 7323 5007 6391 601 -140 37 O
ATOM 2319 CB GLU A 228 12.551 211.546 16.606 1.00 48.62 C
ANISOU 2319 CB GLU A 228 7399 4647 6428 649 -78 -13 C
ATOM 2320 CG GLU A 228 13.608 212.428 17.252 1.00 59.73 C
ANISOU 2320 CG GLU A 228 8887 5956 7851 575 -38 -47 C
ATOM 2321 CD GLU A 228 13.243 212.990 18.613 1.00 77.50 C
ANISOU 2321 CD GLU A 228 11148 8155 10145 602 -1 -142 C
ATOM 2322 OE1 GLU A 228 13.047 214.222 18.713 1.00 67.74 O
ANISOU 2322 OE1 GLU A 228 9985 6790 8963 643 10 -147 O
ATOM 2323 OE2 GLU A 228 13.170 212.202 19.585 1.00 71.89 O
ANISOU 2323 OE2 GLU A 228 10377 7527 9410 583 21 -211 O
ATOM 2324 N VAL A 229 10.993 209.887 14.248 1.00 47.16 N
ANISOU 2324 N VAL A 229 7094 4641 6183 758 -200 113 N
ATOM 2325 CA VAL A 229 10.073 208.814 13.847 1.00 46.66 C
ANISOU 2325 CA VAL A 229 6935 4688 6106 801 -246 116 C
ATOM 2326 C VAL A 229 10.772 207.933 12.810 1.00 51.18 C
ANISOU 2326 C VAL A 229 7513 5332 6599 739 -275 165 C
ATOM 2327 O VAL A 229 10.831 206.718 12.998 1.00 49.57 O
ANISOU 2327 O VAL A 229 7241 5226 6366 698 -276 133 O
ATOM 2328 CB VAL A 229 8.701 209.333 13.337 1.00 51.02 C
ANISOU 2328 CB VAL A 229 7460 5217 6708 925 -298 146 C
ATOM 2329 CG1 VAL A 229 7.849 208.201 12.763 1.00 50.43 C
ANISOU 2329 CG1 VAL A 229 7286 5258 6617 955 -357 153 C
ATOM 2330 CG2 VAL A 229 7.941 210.047 14.444 1.00 51.23 C
ANISOU 2330 CG2 VAL A 229 7464 5186 6814 992 -259 86 C
ATOM 2331 N HIS A 230 11.332 208.547 11.750 1.00 50.25 N
ANISOU 2331 N HIS A 230 7483 5162 6448 733 -293 242 N
ATOM 2332 CA HIS A 230 12.048 207.832 10.692 1.00 51.16 C
ANISOU 2332 CA HIS A 230 7618 5338 6481 680 -313 292 C
ATOM 2333 C HIS A 230 13.230 207.037 11.269 1.00 52.92 C
ANISOU 2333 C HIS A 230 7825 5612 6672 571 -261 251 C
ATOM 2334 O HIS A 230 13.464 205.911 10.829 1.00 52.68 O
ANISOU 2334 O HIS A 230 7756 5672 6587 538 -276 251 O
ATOM 2335 CB HIS A 230 12.526 208.784 9.582 1.00 53.83 C
ANISOU 2335 CB HIS A 230 8065 5598 6790 689 -323 384 C
ATOM 2336 CG HIS A 230 12.968 208.064 8.342 1.00 58.24 C
ANISOU 2336 CG HIS A 230 8643 6227 7257 662 -351 441 C
ATOM 2337 ND1 HIS A 230 14.193 207.405 8.282 1.00 59.81 N
ANISOU 2337 ND1 HIS A 230 8851 6471 7405 563 -307 435 N
ATOM 2338 CD2 HIS A 230 12.330 207.905 7.158 1.00 61.40 C
ANISOU 2338 CD2 HIS A 230 9058 6661 7609 726 -420 499 C
ATOM 2339 CE1 HIS A 230 14.258 206.875 7.069 1.00 59.73 C
ANISOU 2339 CE1 HIS A 230 8862 6518 7316 572 -342 487 C
ATOM 2340 NE2 HIS A 230 13.161 207.146 6.356 1.00 60.96 N
ANISOU 2340 NE2 HIS A 230 9025 6670 7465 666 -413 526 N
ATOM 2341 N ALA A 231 13.946 207.608 12.263 1.00 47.73 N
ANISOU 2341 N ALA A 231 7194 4894 6048 518 -205 211 N
ATOM 2342 CA ALA A 231 15.067 206.954 12.941 1.00 46.01 C
ANISOU 2342 CA ALA A 231 6956 4720 5805 420 -161 168 C
ATOM 2343 C ALA A 231 14.576 205.759 13.782 1.00 48.81 C
ANISOU 2343 C ALA A 231 7216 5169 6160 421 -161 100 C
ATOM 2344 O ALA A 231 15.187 204.690 13.716 1.00 48.45 O
ANISOU 2344 O ALA A 231 7137 5202 6070 366 -155 91 O
ATOM 2345 CB ALA A 231 15.814 207.950 13.813 1.00 46.67 C
ANISOU 2345 CB ALA A 231 7091 4712 5929 372 -114 138 C
ATOM 2346 N ALA A 232 13.449 205.917 14.518 1.00 44.33 N
ANISOU 2346 N ALA A 232 6606 4595 5644 487 -165 57 N
ATOM 2347 CA ALA A 232 12.878 204.833 15.332 1.00 43.15 C
ANISOU 2347 CA ALA A 232 6366 4529 5499 490 -157 -1 C
ATOM 2348 C ALA A 232 12.314 203.708 14.445 1.00 47.14 C
ANISOU 2348 C ALA A 232 6814 5123 5975 508 -205 24 C
ATOM 2349 O ALA A 232 12.314 202.556 14.872 1.00 46.07 O
ANISOU 2349 O ALA A 232 6617 5062 5824 476 -196 -10 O
ATOM 2350 CB ALA A 232 11.802 205.363 16.268 1.00 44.07 C
ANISOU 2350 CB ALA A 232 6453 4614 5679 559 -141 -48 C
ATOM 2351 N LYS A 233 11.870 204.032 13.209 1.00 44.38 N
ANISOU 2351 N LYS A 233 6488 4759 5615 558 -258 84 N
ATOM 2352 CA LYS A 233 11.363 203.042 12.253 1.00 44.07 C
ANISOU 2352 CA LYS A 233 6404 4798 5541 574 -314 105 C
ATOM 2353 C LYS A 233 12.529 202.172 11.758 1.00 47.40 C
ANISOU 2353 C LYS A 233 6848 5270 5890 494 -303 118 C
ATOM 2354 O LYS A 233 12.397 200.949 11.739 1.00 46.65 O
ANISOU 2354 O LYS A 233 6697 5252 5776 472 -315 93 O
ATOM 2355 CB LYS A 233 10.626 203.712 11.083 1.00 47.18 C
ANISOU 2355 CB LYS A 233 6828 5164 5933 652 -380 165 C
ATOM 2356 N SER A 234 13.690 202.797 11.448 1.00 43.82 N
ANISOU 2356 N SER A 234 6475 4770 5406 449 -273 154 N
ATOM 2357 CA SER A 234 14.917 202.117 10.993 1.00 42.70 C
ANISOU 2357 CA SER A 234 6356 4668 5200 376 -250 169 C
ATOM 2358 C SER A 234 15.439 201.104 12.035 1.00 47.70 C
ANISOU 2358 C SER A 234 6931 5355 5836 317 -212 108 C
ATOM 2359 O SER A 234 15.714 199.952 11.683 1.00 48.07 O
ANISOU 2359 O SER A 234 6951 5472 5842 291 -219 102 O
ATOM 2360 CB SER A 234 16.009 203.136 10.683 1.00 43.19 C
ANISOU 2360 CB SER A 234 6501 4659 5249 336 -214 215 C
ATOM 2361 OG SER A 234 15.556 204.115 9.767 1.00 45.02 O
ANISOU 2361 OG SER A 234 6797 4831 5478 391 -244 278 O
ATOM 2362 N LEU A 235 15.533 201.524 13.315 1.00 43.15 N
ANISOU 2362 N LEU A 235 6343 4747 5305 302 -175 64 N
ATOM 2363 CA LEU A 235 16.012 200.683 14.414 1.00 42.04 C
ANISOU 2363 CA LEU A 235 6157 4653 5164 253 -141 10 C
ATOM 2364 C LEU A 235 14.990 199.584 14.783 1.00 44.44 C
ANISOU 2364 C LEU A 235 6384 5022 5480 282 -157 -25 C
ATOM 2365 O LEU A 235 15.390 198.535 15.287 1.00 42.74 O
ANISOU 2365 O LEU A 235 6133 4860 5247 243 -139 -52 O
ATOM 2366 CB LEU A 235 16.361 201.538 15.647 1.00 42.42 C
ANISOU 2366 CB LEU A 235 6224 4645 5247 233 -102 -29 C
ATOM 2367 CG LEU A 235 17.388 202.671 15.427 1.00 47.63 C
ANISOU 2367 CG LEU A 235 6957 5231 5909 193 -83 -3 C
ATOM 2368 CD1 LEU A 235 17.167 203.795 16.407 1.00 48.46 C
ANISOU 2368 CD1 LEU A 235 7091 5258 6062 206 -63 -41 C
ATOM 2369 CD2 LEU A 235 18.835 202.159 15.471 1.00 48.45 C
ANISOU 2369 CD2 LEU A 235 7061 5370 5978 110 -58 -2 C
ATOM 2370 N ALA A 236 13.686 199.812 14.510 1.00 41.21 N
ANISOU 2370 N ALA A 236 5947 4606 5106 350 -192 -21 N
ATOM 2371 CA ALA A 236 12.624 198.828 14.756 1.00 40.01 C
ANISOU 2371 CA ALA A 236 5713 4511 4977 375 -209 -50 C
ATOM 2372 C ALA A 236 12.690 197.713 13.710 1.00 42.24 C
ANISOU 2372 C ALA A 236 5980 4854 5216 358 -249 -32 C
ATOM 2373 O ALA A 236 12.346 196.573 14.020 1.00 40.55 O
ANISOU 2373 O ALA A 236 5707 4692 5008 341 -249 -61 O
ATOM 2374 CB ALA A 236 11.260 199.496 14.738 1.00 41.31 C
ANISOU 2374 CB ALA A 236 5845 4651 5199 453 -235 -51 C
ATOM 2375 N ILE A 237 13.165 198.033 12.480 1.00 39.42 N
ANISOU 2375 N ILE A 237 5680 4484 4812 360 -280 16 N
ATOM 2376 CA ILE A 237 13.347 197.045 11.400 1.00 39.05 C
ANISOU 2376 CA ILE A 237 5635 4490 4711 345 -316 30 C
ATOM 2377 C ILE A 237 14.461 196.069 11.819 1.00 42.21 C
ANISOU 2377 C ILE A 237 6033 4926 5080 278 -272 8 C
ATOM 2378 O ILE A 237 14.311 194.869 11.619 1.00 41.94 O
ANISOU 2378 O ILE A 237 5962 4941 5030 263 -287 -12 O
ATOM 2379 CB ILE A 237 13.608 197.727 10.032 1.00 42.45 C
ANISOU 2379 CB ILE A 237 6140 4898 5089 368 -351 89 C
ATOM 2380 CG1 ILE A 237 12.296 198.337 9.490 1.00 43.62 C
ANISOU 2380 CG1 ILE A 237 6276 5031 5266 446 -416 109 C
ATOM 2381 CG2 ILE A 237 14.232 196.761 9.003 1.00 42.11 C
ANISOU 2381 CG2 ILE A 237 6121 4907 4971 339 -366 101 C
ATOM 2382 CD1 ILE A 237 12.468 199.586 8.639 1.00 50.26 C
ANISOU 2382 CD1 ILE A 237 7201 5815 6082 483 -433 174 C
ATOM 2383 N ILE A 238 15.521 196.582 12.475 1.00 39.05 N
ANISOU 2383 N ILE A 238 5664 4497 4677 238 -219 9 N
ATOM 2384 CA ILE A 238 16.644 195.797 13.004 1.00 38.98 C
ANISOU 2384 CA ILE A 238 5648 4519 4645 180 -178 -10 C
ATOM 2385 C ILE A 238 16.131 194.729 14.020 1.00 44.40 C
ANISOU 2385 C ILE A 238 6267 5243 5358 173 -168 -56 C
ATOM 2386 O ILE A 238 16.561 193.572 13.950 1.00 44.16 O
ANISOU 2386 O ILE A 238 6220 5255 5304 146 -162 -67 O
ATOM 2387 CB ILE A 238 17.719 196.731 13.642 1.00 41.81 C
ANISOU 2387 CB ILE A 238 6042 4834 5009 143 -134 -5 C
ATOM 2388 CG1 ILE A 238 18.267 197.777 12.621 1.00 42.55 C
ANISOU 2388 CG1 ILE A 238 6204 4882 5080 141 -135 48 C
ATOM 2389 CG2 ILE A 238 18.849 195.935 14.327 1.00 41.52 C
ANISOU 2389 CG2 ILE A 238 5986 4834 4955 88 -98 -28 C
ATOM 2390 CD1 ILE A 238 19.497 197.367 11.760 1.00 49.45 C
ANISOU 2390 CD1 ILE A 238 7105 5785 5900 99 -115 79 C
ATOM 2391 N VAL A 239 15.205 195.121 14.930 1.00 41.62 N
ANISOU 2391 N VAL A 239 5883 4873 5056 201 -161 -81 N
ATOM 2392 CA VAL A 239 14.612 194.244 15.959 1.00 41.57 C
ANISOU 2392 CA VAL A 239 5817 4899 5079 197 -141 -119 C
ATOM 2393 C VAL A 239 13.719 193.174 15.284 1.00 46.88 C
ANISOU 2393 C VAL A 239 6442 5611 5761 209 -180 -123 C
ATOM 2394 O VAL A 239 13.687 192.026 15.737 1.00 46.46 O
ANISOU 2394 O VAL A 239 6353 5589 5710 184 -164 -143 O
ATOM 2395 CB VAL A 239 13.839 195.051 17.042 1.00 45.30 C
ANISOU 2395 CB VAL A 239 6270 5341 5599 228 -115 -143 C
ATOM 2396 CG1 VAL A 239 13.219 194.132 18.098 1.00 44.88 C
ANISOU 2396 CG1 VAL A 239 6159 5324 5570 222 -85 -176 C
ATOM 2397 CG2 VAL A 239 14.745 196.082 17.709 1.00 44.98 C
ANISOU 2397 CG2 VAL A 239 6284 5258 5549 210 -83 -149 C
ATOM 2398 N GLY A 240 13.031 193.569 14.211 1.00 43.99 N
ANISOU 2398 N GLY A 240 6079 5238 5398 247 -232 -103 N
ATOM 2399 CA GLY A 240 12.157 192.697 13.438 1.00 44.03 C
ANISOU 2399 CA GLY A 240 6041 5277 5410 260 -284 -110 C
ATOM 2400 C GLY A 240 12.950 191.671 12.661 1.00 48.12 C
ANISOU 2400 C GLY A 240 6586 5824 5872 224 -296 -107 C
ATOM 2401 O GLY A 240 12.556 190.505 12.597 1.00 47.05 O
ANISOU 2401 O GLY A 240 6411 5719 5747 206 -310 -132 O
ATOM 2402 N LEU A 241 14.102 192.100 12.098 1.00 45.41 N
ANISOU 2402 N LEU A 241 6311 5469 5473 210 -283 -79 N
ATOM 2403 CA LEU A 241 15.008 191.235 11.342 1.00 44.91 C
ANISOU 2403 CA LEU A 241 6281 5433 5351 182 -283 -76 C
ATOM 2404 C LEU A 241 15.698 190.208 12.245 1.00 46.37 C
ANISOU 2404 C LEU A 241 6442 5635 5541 140 -236 -102 C
ATOM 2405 O LEU A 241 15.964 189.103 11.780 1.00 46.05 O
ANISOU 2405 O LEU A 241 6403 5620 5476 125 -243 -115 O
ATOM 2406 CB LEU A 241 16.052 192.054 10.578 1.00 45.31 C
ANISOU 2406 CB LEU A 241 6402 5466 5346 179 -269 -35 C
ATOM 2407 CG LEU A 241 15.591 192.700 9.264 1.00 50.97 C
ANISOU 2407 CG LEU A 241 7162 6176 6026 218 -322 -1 C
ATOM 2408 CD1 LEU A 241 16.694 193.546 8.689 1.00 51.62 C
ANISOU 2408 CD1 LEU A 241 7316 6235 6060 207 -290 46 C
ATOM 2409 CD2 LEU A 241 15.168 191.653 8.223 1.00 52.67 C
ANISOU 2409 CD2 LEU A 241 7378 6433 6201 227 -374 -17 C
ATOM 2410 N PHE A 242 15.964 190.563 13.528 1.00 40.97 N
ANISOU 2410 N PHE A 242 5743 4937 4888 127 -191 -109 N
ATOM 2411 CA PHE A 242 16.552 189.671 14.533 1.00 39.74 C
ANISOU 2411 CA PHE A 242 5567 4797 4736 95 -149 -128 C
ATOM 2412 C PHE A 242 15.544 188.574 14.903 1.00 42.57 C
ANISOU 2412 C PHE A 242 5871 5171 5131 94 -158 -154 C
ATOM 2413 O PHE A 242 15.916 187.405 15.023 1.00 41.11 O
ANISOU 2413 O PHE A 242 5680 5003 4938 72 -145 -165 O
ATOM 2414 CB PHE A 242 16.975 190.465 15.782 1.00 41.55 C
ANISOU 2414 CB PHE A 242 5799 5009 4980 85 -109 -132 C
ATOM 2415 CG PHE A 242 17.677 189.654 16.850 1.00 42.32 C
ANISOU 2415 CG PHE A 242 5883 5125 5071 57 -72 -146 C
ATOM 2416 CD1 PHE A 242 16.950 188.956 17.808 1.00 44.84 C
ANISOU 2416 CD1 PHE A 242 6164 5454 5418 58 -55 -165 C
ATOM 2417 CD2 PHE A 242 19.064 189.605 16.908 1.00 43.99 C
ANISOU 2417 CD2 PHE A 242 6119 5346 5250 32 -54 -136 C
ATOM 2418 CE1 PHE A 242 17.598 188.191 18.780 1.00 45.48 C
ANISOU 2418 CE1 PHE A 242 6242 5553 5487 37 -23 -170 C
ATOM 2419 CE2 PHE A 242 19.713 188.863 17.899 1.00 46.60 C
ANISOU 2419 CE2 PHE A 242 6436 5696 5573 13 -28 -146 C
ATOM 2420 CZ PHE A 242 18.975 188.163 18.829 1.00 44.46 C
ANISOU 2420 CZ PHE A 242 6138 5433 5322 18 -15 -161 C
ATOM 2421 N ALA A 243 14.272 188.966 15.086 1.00 39.50 N
ANISOU 2421 N ALA A 243 5444 4776 4789 119 -176 -163 N
ATOM 2422 CA ALA A 243 13.179 188.056 15.402 1.00 39.83 C
ANISOU 2422 CA ALA A 243 5425 4831 4879 115 -182 -185 C
ATOM 2423 C ALA A 243 12.944 187.065 14.249 1.00 45.87 C
ANISOU 2423 C ALA A 243 6185 5611 5631 106 -231 -195 C
ATOM 2424 O ALA A 243 12.876 185.862 14.492 1.00 45.46 O
ANISOU 2424 O ALA A 243 6112 5566 5594 77 -220 -212 O
ATOM 2425 CB ALA A 243 11.916 188.846 15.688 1.00 40.98 C
ANISOU 2425 CB ALA A 243 5523 4968 5078 149 -192 -190 C
ATOM 2426 N LEU A 244 12.900 187.562 12.998 1.00 43.25 N
ANISOU 2426 N LEU A 244 5885 5281 5267 129 -284 -184 N
ATOM 2427 CA LEU A 244 12.682 186.756 11.795 1.00 43.96 C
ANISOU 2427 CA LEU A 244 5984 5388 5332 125 -340 -198 C
ATOM 2428 C LEU A 244 13.796 185.716 11.557 1.00 47.24 C
ANISOU 2428 C LEU A 244 6439 5808 5700 95 -315 -207 C
ATOM 2429 O LEU A 244 13.509 184.625 11.062 1.00 46.19 O
ANISOU 2429 O LEU A 244 6298 5682 5569 79 -343 -235 O
ATOM 2430 CB LEU A 244 12.579 187.687 10.576 1.00 45.00 C
ANISOU 2430 CB LEU A 244 6157 5521 5420 162 -394 -176 C
ATOM 2431 CG LEU A 244 11.656 187.238 9.455 1.00 51.25 C
ANISOU 2431 CG LEU A 244 6934 6333 6206 177 -477 -195 C
ATOM 2432 CD1 LEU A 244 10.201 187.598 9.766 1.00 52.21 C
ANISOU 2432 CD1 LEU A 244 6977 6457 6404 201 -516 -204 C
ATOM 2433 CD2 LEU A 244 12.073 187.865 8.142 1.00 55.08 C
ANISOU 2433 CD2 LEU A 244 7493 6824 6611 206 -518 -167 C
ATOM 2434 N CYS A 245 15.056 186.060 11.891 1.00 44.02 N
ANISOU 2434 N CYS A 245 6073 5396 5257 88 -266 -186 N
ATOM 2435 CA CYS A 245 16.210 185.176 11.706 1.00 43.82 C
ANISOU 2435 CA CYS A 245 6081 5378 5191 69 -237 -191 C
ATOM 2436 C CYS A 245 16.361 184.148 12.847 1.00 46.44 C
ANISOU 2436 C CYS A 245 6381 5705 5559 44 -197 -205 C
ATOM 2437 O CYS A 245 16.850 183.052 12.583 1.00 46.37 O
ANISOU 2437 O CYS A 245 6387 5697 5535 32 -190 -220 O
ATOM 2438 CB CYS A 245 17.488 185.990 11.534 1.00 44.34 C
ANISOU 2438 CB CYS A 245 6192 5445 5209 71 -204 -160 C
ATOM 2439 SG CYS A 245 17.585 186.895 9.965 1.00 49.08 S
ANISOU 2439 SG CYS A 245 6851 6051 5747 97 -241 -134 S
ATOM 2440 N TRP A 246 15.952 184.486 14.092 1.00 41.46 N
ANISOU 2440 N TRP A 246 5714 5066 4972 39 -168 -200 N
ATOM 2441 CA TRP A 246 16.108 183.597 15.256 1.00 40.82 C
ANISOU 2441 CA TRP A 246 5611 4981 4916 18 -125 -205 C
ATOM 2442 C TRP A 246 14.855 182.801 15.649 1.00 41.54 C
ANISOU 2442 C TRP A 246 5653 5065 5067 4 -130 -223 C
ATOM 2443 O TRP A 246 15.012 181.736 16.248 1.00 39.82 O
ANISOU 2443 O TRP A 246 5430 4837 4864 -16 -101 -225 O
ATOM 2444 CB TRP A 246 16.609 184.379 16.478 1.00 39.85 C
ANISOU 2444 CB TRP A 246 5490 4860 4792 19 -83 -188 C
ATOM 2445 CG TRP A 246 18.075 184.663 16.393 1.00 41.11 C
ANISOU 2445 CG TRP A 246 5688 5028 4904 17 -66 -173 C
ATOM 2446 CD1 TRP A 246 18.664 185.813 15.957 1.00 44.04 C
ANISOU 2446 CD1 TRP A 246 6085 5399 5249 24 -71 -159 C
ATOM 2447 CD2 TRP A 246 19.139 183.730 16.629 1.00 41.03 C
ANISOU 2447 CD2 TRP A 246 5691 5026 4874 8 -44 -170 C
ATOM 2448 NE1 TRP A 246 20.032 185.667 15.936 1.00 43.56 N
ANISOU 2448 NE1 TRP A 246 6044 5350 5156 14 -51 -149 N
ATOM 2449 CE2 TRP A 246 20.353 184.398 16.347 1.00 45.01 C
ANISOU 2449 CE2 TRP A 246 6218 5541 5342 8 -36 -156 C
ATOM 2450 CE3 TRP A 246 19.188 182.401 17.090 1.00 42.20 C
ANISOU 2450 CE3 TRP A 246 5830 5169 5034 1 -28 -175 C
ATOM 2451 CZ2 TRP A 246 21.602 183.783 16.510 1.00 44.17 C
ANISOU 2451 CZ2 TRP A 246 6118 5449 5214 5 -14 -149 C
ATOM 2452 CZ3 TRP A 246 20.426 181.791 17.238 1.00 43.46 C
ANISOU 2452 CZ3 TRP A 246 6006 5338 5169 3 -9 -166 C
ATOM 2453 CH2 TRP A 246 21.614 182.479 16.956 1.00 43.94 C
ANISOU 2453 CH2 TRP A 246 6081 5417 5197 7 -4 -154 C
ATOM 2454 N LEU A 247 13.636 183.281 15.318 1.00 37.48 N
ANISOU 2454 N LEU A 247 5100 4552 4590 14 -165 -233 N
ATOM 2455 CA LEU A 247 12.407 182.569 15.684 1.00 37.65 C
ANISOU 2455 CA LEU A 247 5059 4568 4677 -5 -166 -250 C
ATOM 2456 C LEU A 247 12.292 181.156 15.072 1.00 41.17 C
ANISOU 2456 C LEU A 247 5506 5001 5135 -35 -190 -274 C
ATOM 2457 O LEU A 247 11.904 180.276 15.832 1.00 41.02 O
ANISOU 2457 O LEU A 247 5457 4968 5162 -63 -156 -276 O
ATOM 2458 CB LEU A 247 11.128 183.361 15.376 1.00 38.53 C
ANISOU 2458 CB LEU A 247 5118 4688 4833 16 -205 -257 C
ATOM 2459 CG LEU A 247 10.775 184.490 16.350 1.00 43.48 C
ANISOU 2459 CG LEU A 247 5722 5317 5482 42 -167 -243 C
ATOM 2460 CD1 LEU A 247 9.675 185.366 15.775 1.00 44.37 C
ANISOU 2460 CD1 LEU A 247 5790 5436 5630 76 -215 -248 C
ATOM 2461 CD2 LEU A 247 10.432 183.968 17.751 1.00 44.37 C
ANISOU 2461 CD2 LEU A 247 5798 5428 5634 20 -98 -241 C
ATOM 2462 N PRO A 248 12.629 180.859 13.782 1.00 37.21 N
ANISOU 2462 N PRO A 248 5042 4502 4594 -30 -241 -292 N
ATOM 2463 CA PRO A 248 12.471 179.472 13.295 1.00 37.17 C
ANISOU 2463 CA PRO A 248 5041 4478 4605 -60 -261 -324 C
ATOM 2464 C PRO A 248 13.213 178.427 14.143 1.00 42.84 C
ANISOU 2464 C PRO A 248 5779 5168 5328 -81 -201 -315 C
ATOM 2465 O PRO A 248 12.610 177.412 14.499 1.00 43.57 O
ANISOU 2465 O PRO A 248 5844 5235 5477 -115 -191 -328 O
ATOM 2466 CB PRO A 248 13.014 179.534 11.865 1.00 38.57 C
ANISOU 2466 CB PRO A 248 5275 4665 4714 -41 -312 -341 C
ATOM 2467 CG PRO A 248 12.791 180.946 11.448 1.00 42.67 C
ANISOU 2467 CG PRO A 248 5795 5211 5208 -7 -342 -321 C
ATOM 2468 CD PRO A 248 13.094 181.743 12.691 1.00 38.07 C
ANISOU 2468 CD PRO A 248 5196 4628 4641 1 -281 -286 C
ATOM 2469 N LEU A 249 14.480 178.700 14.516 1.00 38.76 N
ANISOU 2469 N LEU A 249 5307 4659 4761 -62 -161 -289 N
ATOM 2470 CA LEU A 249 15.316 177.821 15.341 1.00 38.32 C
ANISOU 2470 CA LEU A 249 5273 4583 4703 -69 -109 -273 C
ATOM 2471 C LEU A 249 14.715 177.675 16.745 1.00 42.84 C
ANISOU 2471 C LEU A 249 5807 5147 5324 -87 -63 -251 C
ATOM 2472 O LEU A 249 14.717 176.578 17.301 1.00 43.15 O
ANISOU 2472 O LEU A 249 5849 5156 5391 -107 -33 -245 O
ATOM 2473 CB LEU A 249 16.745 178.400 15.402 1.00 37.86 C
ANISOU 2473 CB LEU A 249 5256 4546 4583 -41 -87 -250 C
ATOM 2474 CG LEU A 249 17.906 177.534 15.894 1.00 42.15 C
ANISOU 2474 CG LEU A 249 5829 5078 5109 -34 -49 -236 C
ATOM 2475 CD1 LEU A 249 18.101 176.294 15.036 1.00 42.62 C
ANISOU 2475 CD1 LEU A 249 5918 5108 5169 -36 -63 -265 C
ATOM 2476 CD2 LEU A 249 19.189 178.322 15.844 1.00 44.14 C
ANISOU 2476 CD2 LEU A 249 6103 5360 5308 -10 -36 -217 C
ATOM 2477 N HIS A 250 14.152 178.764 17.293 1.00 39.30 N
ANISOU 2477 N HIS A 250 5324 4720 4886 -79 -54 -239 N
ATOM 2478 CA HIS A 250 13.507 178.743 18.607 1.00 38.94 C
ANISOU 2478 CA HIS A 250 5243 4672 4880 -91 -4 -220 C
ATOM 2479 C HIS A 250 12.190 177.954 18.571 1.00 41.81 C
ANISOU 2479 C HIS A 250 5552 5015 5319 -127 -7 -236 C
ATOM 2480 O HIS A 250 11.888 177.234 19.525 1.00 42.58 O
ANISOU 2480 O HIS A 250 5635 5094 5449 -150 44 -218 O
ATOM 2481 CB HIS A 250 13.254 180.170 19.108 1.00 39.66 C
ANISOU 2481 CB HIS A 250 5317 4791 4962 -67 7 -212 C
ATOM 2482 CG HIS A 250 14.474 180.867 19.633 1.00 42.33 C
ANISOU 2482 CG HIS A 250 5701 5144 5240 -45 27 -193 C
ATOM 2483 ND1 HIS A 250 14.903 182.081 19.105 1.00 43.88 N
ANISOU 2483 ND1 HIS A 250 5922 5339 5412 -49 71 -171 N
ATOM 2484 CD2 HIS A 250 15.361 180.464 20.568 1.00 43.38 C
ANISOU 2484 CD2 HIS A 250 5854 5291 5337 -23 8 -193 C
ATOM 2485 CE1 HIS A 250 16.010 182.388 19.760 1.00 42.70 C
ANISOU 2485 CE1 HIS A 250 5803 5208 5215 -31 70 -164 C
ATOM 2486 NE2 HIS A 250 16.318 181.451 20.659 1.00 42.98 N
ANISOU 2486 NE2 HIS A 250 5837 5249 5244 -18 36 -177 N
ATOM 2487 N ILE A 251 11.426 178.072 17.465 1.00 36.36 N
ANISOU 2487 N ILE A 251 4831 4328 4655 -132 -68 -268 N
ATOM 2488 CA ILE A 251 10.133 177.401 17.278 1.00 36.10 C
ANISOU 2488 CA ILE A 251 4734 4280 4702 -170 -85 -291 C
ATOM 2489 C ILE A 251 10.338 175.879 17.050 1.00 37.86 C
ANISOU 2489 C ILE A 251 4982 4457 4946 -210 -84 -305 C
ATOM 2490 O ILE A 251 9.526 175.101 17.540 1.00 37.45 O
ANISOU 2490 O ILE A 251 4887 4379 4964 -253 -58 -305 O
ATOM 2491 CB ILE A 251 9.290 178.095 16.163 1.00 39.41 C
ANISOU 2491 CB ILE A 251 5112 4723 5138 -157 -164 -321 C
ATOM 2492 CG1 ILE A 251 8.782 179.468 16.675 1.00 40.01 C
ANISOU 2492 CG1 ILE A 251 5148 4832 5223 -121 -149 -303 C
ATOM 2493 CG2 ILE A 251 8.102 177.235 15.696 1.00 40.10 C
ANISOU 2493 CG2 ILE A 251 5136 4796 5306 -203 -203 -355 C
ATOM 2494 CD1 ILE A 251 8.589 180.554 15.604 1.00 48.57 C
ANISOU 2494 CD1 ILE A 251 6232 5940 6280 -81 -221 -314 C
ATOM 2495 N ILE A 252 11.423 175.459 16.360 1.00 33.20 N
ANISOU 2495 N ILE A 252 4462 3854 4299 -195 -105 -315 N
ATOM 2496 CA ILE A 252 11.711 174.031 16.142 1.00 32.79 C
ANISOU 2496 CA ILE A 252 4444 3750 4264 -224 -101 -331 C
ATOM 2497 C ILE A 252 12.066 173.372 17.508 1.00 35.38 C
ANISOU 2497 C ILE A 252 4786 4050 4609 -235 -22 -286 C
ATOM 2498 O ILE A 252 11.626 172.256 17.772 1.00 35.53 O
ANISOU 2498 O ILE A 252 4797 4018 4684 -276 -1 -288 O
ATOM 2499 CB ILE A 252 12.798 173.791 15.048 1.00 35.49 C
ANISOU 2499 CB ILE A 252 4857 4089 4539 -196 -137 -356 C
ATOM 2500 CG1 ILE A 252 12.278 174.223 13.648 1.00 35.73 C
ANISOU 2500 CG1 ILE A 252 4881 4142 4552 -192 -219 -402 C
ATOM 2501 CG2 ILE A 252 13.230 172.315 15.018 1.00 36.59 C
ANISOU 2501 CG2 ILE A 252 5040 4167 4696 -216 -120 -369 C
ATOM 2502 CD1 ILE A 252 13.342 174.538 12.577 1.00 35.76 C
ANISOU 2502 CD1 ILE A 252 4953 4167 4468 -151 -247 -416 C
ATOM 2503 N ASN A 253 12.788 174.086 18.383 1.00 31.22 N
ANISOU 2503 N ASN A 253 4277 3552 4033 -201 20 -246 N
ATOM 2504 CA ASN A 253 13.129 173.597 19.719 1.00 31.91 C
ANISOU 2504 CA ASN A 253 4382 3623 4121 -203 89 -200 C
ATOM 2505 C ASN A 253 11.857 173.392 20.559 1.00 38.44 C
ANISOU 2505 C ASN A 253 5151 4438 5016 -243 133 -184 C
ATOM 2506 O ASN A 253 11.754 172.380 21.258 1.00 38.66 O
ANISOU 2506 O ASN A 253 5191 4423 5074 -270 180 -157 O
ATOM 2507 CB ASN A 253 14.118 174.537 20.422 1.00 30.38 C
ANISOU 2507 CB ASN A 253 4216 3470 3855 -160 112 -169 C
ATOM 2508 CG ASN A 253 15.512 174.515 19.827 1.00 43.13 C
ANISOU 2508 CG ASN A 253 5884 5092 5410 -125 87 -173 C
ATOM 2509 OD1 ASN A 253 15.867 173.670 18.994 1.00 35.82 O
ANISOU 2509 OD1 ASN A 253 4985 4135 4488 -126 64 -195 O
ATOM 2510 ND2 ASN A 253 16.351 175.426 20.271 1.00 34.71 N
ANISOU 2510 ND2 ASN A 253 4833 4065 4290 -94 95 -155 N
ATOM 2511 N CYS A 254 10.868 174.309 20.429 1.00 35.97 N
ANISOU 2511 N CYS A 254 4774 4161 4733 -247 118 -200 N
ATOM 2512 CA CYS A 254 9.562 174.210 21.091 1.00 36.78 C
ANISOU 2512 CA CYS A 254 4804 4260 4909 -283 160 -192 C
ATOM 2513 C CYS A 254 8.851 172.919 20.657 1.00 40.55 C
ANISOU 2513 C CYS A 254 5256 4684 5468 -344 149 -211 C
ATOM 2514 O CYS A 254 8.284 172.239 21.508 1.00 40.72 O
ANISOU 2514 O CYS A 254 5253 4677 5541 -383 213 -182 O
ATOM 2515 CB CYS A 254 8.699 175.439 20.805 1.00 37.61 C
ANISOU 2515 CB CYS A 254 4843 4413 5035 -266 132 -213 C
ATOM 2516 SG CYS A 254 9.164 176.925 21.737 1.00 41.21 S
ANISOU 2516 SG CYS A 254 5316 4917 5422 -209 172 -188 S
ATOM 2517 N PHE A 255 8.904 172.576 19.349 1.00 36.85 N
ANISOU 2517 N PHE A 255 4796 4199 5006 -353 72 -259 N
ATOM 2518 CA PHE A 255 8.284 171.361 18.797 1.00 37.95 C
ANISOU 2518 CA PHE A 255 4917 4282 5220 -413 48 -291 C
ATOM 2519 C PHE A 255 8.964 170.087 19.322 1.00 42.97 C
ANISOU 2519 C PHE A 255 5620 4850 5858 -432 98 -263 C
ATOM 2520 O PHE A 255 8.270 169.143 19.702 1.00 43.76 O
ANISOU 2520 O PHE A 255 5695 4898 6036 -490 133 -255 O
ATOM 2521 CB PHE A 255 8.305 171.368 17.254 1.00 39.60 C
ANISOU 2521 CB PHE A 255 5136 4495 5415 -410 -52 -354 C
ATOM 2522 CG PHE A 255 7.127 172.068 16.618 1.00 41.12 C
ANISOU 2522 CG PHE A 255 5241 4728 5653 -421 -113 -390 C
ATOM 2523 CD1 PHE A 255 5.934 171.388 16.385 1.00 44.97 C
ANISOU 2523 CD1 PHE A 255 5654 5190 6240 -486 -138 -421 C
ATOM 2524 CD2 PHE A 255 7.209 173.406 16.249 1.00 41.52 C
ANISOU 2524 CD2 PHE A 255 5283 4841 5652 -366 -150 -390 C
ATOM 2525 CE1 PHE A 255 4.838 172.043 15.815 1.00 46.18 C
ANISOU 2525 CE1 PHE A 255 5718 5388 6440 -491 -201 -453 C
ATOM 2526 CE2 PHE A 255 6.116 174.060 15.678 1.00 44.74 C
ANISOU 2526 CE2 PHE A 255 5611 5287 6103 -367 -210 -418 C
ATOM 2527 CZ PHE A 255 4.939 173.374 15.459 1.00 44.41 C
ANISOU 2527 CZ PHE A 255 5488 5226 6159 -427 -239 -450 C
ATOM 2528 N THR A 256 10.312 170.078 19.368 1.00 38.32 N
ANISOU 2528 N THR A 256 5112 4259 5187 -381 104 -245 N
ATOM 2529 CA THR A 256 11.119 168.952 19.837 1.00 38.34 C
ANISOU 2529 CA THR A 256 5185 4200 5181 -380 145 -215 C
ATOM 2530 C THR A 256 10.810 168.642 21.297 1.00 43.18 C
ANISOU 2530 C THR A 256 5791 4797 5819 -399 233 -149 C
ATOM 2531 O THR A 256 10.702 167.466 21.660 1.00 43.64 O
ANISOU 2531 O THR A 256 5874 4784 5924 -435 270 -127 O
ATOM 2532 CB THR A 256 12.609 169.267 19.632 1.00 45.77 C
ANISOU 2532 CB THR A 256 6196 5165 6029 -313 132 -207 C
ATOM 2533 OG1 THR A 256 12.833 169.547 18.248 1.00 48.09 O
ANISOU 2533 OG1 THR A 256 6500 5476 6298 -298 60 -265 O
ATOM 2534 CG2 THR A 256 13.533 168.138 20.101 1.00 40.98 C
ANISOU 2534 CG2 THR A 256 5660 4498 5412 -297 169 -174 C
ATOM 2535 N PHE A 257 10.650 169.702 22.114 1.00 39.41 N
ANISOU 2535 N PHE A 257 5283 4383 5309 -375 267 -119 N
ATOM 2536 CA PHE A 257 10.406 169.628 23.548 1.00 39.58 C
ANISOU 2536 CA PHE A 257 5304 4406 5330 -382 353 -56 C
ATOM 2537 C PHE A 257 8.934 169.364 23.894 1.00 45.59 C
ANISOU 2537 C PHE A 257 5986 5152 6185 -447 397 -52 C
ATOM 2538 O PHE A 257 8.660 168.449 24.667 1.00 46.77 O
ANISOU 2538 O PHE A 257 6148 5251 6371 -484 464 -8 O
ATOM 2539 CB PHE A 257 10.878 170.929 24.220 1.00 40.54 C
ANISOU 2539 CB PHE A 257 5431 4602 5370 -327 367 -37 C
ATOM 2540 CG PHE A 257 10.726 170.988 25.724 1.00 42.28 C
ANISOU 2540 CG PHE A 257 5662 4835 5566 -323 454 22 C
ATOM 2541 CD1 PHE A 257 11.506 170.186 26.551 1.00 44.65 C
ANISOU 2541 CD1 PHE A 257 6035 5104 5825 -309 495 77 C
ATOM 2542 CD2 PHE A 257 9.827 171.869 26.313 1.00 44.62 C
ANISOU 2542 CD2 PHE A 257 5901 5179 5874 -327 494 24 C
ATOM 2543 CE1 PHE A 257 11.370 170.246 27.941 1.00 45.79 C
ANISOU 2543 CE1 PHE A 257 6199 5265 5935 -302 573 135 C
ATOM 2544 CE2 PHE A 257 9.696 171.930 27.704 1.00 47.70 C
ANISOU 2544 CE2 PHE A 257 6310 5585 6230 -320 579 77 C
ATOM 2545 CZ PHE A 257 10.468 171.118 28.509 1.00 45.43 C
ANISOU 2545 CZ PHE A 257 6100 5268 5895 -309 617 132 C
ATOM 2546 N PHE A 258 8.004 170.175 23.374 1.00 42.12 N
ANISOU 2546 N PHE A 258 5462 4755 5785 -458 364 -93 N
ATOM 2547 CA PHE A 258 6.592 170.046 23.710 1.00 43.06 C
ANISOU 2547 CA PHE A 258 5489 4872 5999 -515 406 -91 C
ATOM 2548 C PHE A 258 5.879 168.914 22.977 1.00 51.54 C
ANISOU 2548 C PHE A 258 6527 5880 7175 -591 377 -124 C
ATOM 2549 O PHE A 258 4.884 168.434 23.520 1.00 51.78 O
ANISOU 2549 O PHE A 258 6495 5888 7290 -650 436 -103 O
ATOM 2550 CB PHE A 258 5.831 171.364 23.483 1.00 44.02 C
ANISOU 2550 CB PHE A 258 5527 5066 6132 -492 381 -121 C
ATOM 2551 CG PHE A 258 6.209 172.509 24.396 1.00 44.22 C
ANISOU 2551 CG PHE A 258 5573 5151 6079 -431 427 -92 C
ATOM 2552 CD1 PHE A 258 6.205 172.351 25.780 1.00 46.76 C
ANISOU 2552 CD1 PHE A 258 5916 5474 6378 -431 528 -35 C
ATOM 2553 CD2 PHE A 258 6.513 173.761 23.876 1.00 45.18 C
ANISOU 2553 CD2 PHE A 258 5692 5324 6150 -375 370 -122 C
ATOM 2554 CE1 PHE A 258 6.532 173.416 26.624 1.00 47.11 C
ANISOU 2554 CE1 PHE A 258 5983 5572 6346 -376 565 -17 C
ATOM 2555 CE2 PHE A 258 6.840 174.825 24.722 1.00 47.59 C
ANISOU 2555 CE2 PHE A 258 6018 5675 6389 -324 410 -102 C
ATOM 2556 CZ PHE A 258 6.844 174.645 26.090 1.00 45.74 C
ANISOU 2556 CZ PHE A 258 5807 5443 6130 -324 505 -54 C
ATOM 2557 N CYS A 259 6.341 168.497 21.763 1.00 51.58 N
ANISOU 2557 N CYS A 259 6567 5855 7175 -591 290 -176 N
ATOM 2558 CA CYS A 259 5.682 167.414 21.011 1.00 54.17 C
ANISOU 2558 CA CYS A 259 6869 6117 7598 -665 252 -219 C
ATOM 2559 C CYS A 259 6.578 166.156 20.918 1.00 58.36 C
ANISOU 2559 C CYS A 259 7500 6558 8115 -673 260 -210 C
ATOM 2560 O CYS A 259 7.258 165.964 19.903 1.00 57.10 O
ANISOU 2560 O CYS A 259 7394 6384 7918 -649 188 -258 O
ATOM 2561 CB CYS A 259 5.211 167.868 19.628 1.00 55.74 C
ANISOU 2561 CB CYS A 259 7017 6348 7815 -668 141 -297 C
ATOM 2562 SG CYS A 259 3.798 166.918 18.996 1.00 62.06 S
ANISOU 2562 SG CYS A 259 7723 7096 8760 -775 100 -352 S
ATOM 2563 N PRO A 260 6.572 165.268 21.948 1.00 56.07 N
ANISOU 2563 N PRO A 260 7240 6207 7857 -705 348 -148 N
ATOM 2564 CA PRO A 260 7.397 164.047 21.860 1.00 56.38 C
ANISOU 2564 CA PRO A 260 7377 6152 7892 -707 355 -137 C
ATOM 2565 C PRO A 260 6.805 162.990 20.919 1.00 61.42 C
ANISOU 2565 C PRO A 260 8003 6706 8627 -783 306 -200 C
ATOM 2566 O PRO A 260 7.548 162.133 20.440 1.00 61.85 O
ANISOU 2566 O PRO A 260 8141 6689 8670 -772 282 -219 O
ATOM 2567 CB PRO A 260 7.455 163.547 23.305 1.00 58.57 C
ANISOU 2567 CB PRO A 260 7687 6395 8172 -716 465 -44 C
ATOM 2568 CG PRO A 260 6.216 164.066 23.939 1.00 63.35 C
ANISOU 2568 CG PRO A 260 8191 7045 8835 -762 519 -23 C
ATOM 2569 CD PRO A 260 5.824 165.327 23.223 1.00 58.05 C
ANISOU 2569 CD PRO A 260 7442 6467 8147 -737 450 -83 C
ATOM 2570 N ASP A 261 5.483 163.055 20.648 1.00 58.28 N
ANISOU 2570 N ASP A 261 7500 6317 8326 -857 289 -235 N
ATOM 2571 CA ASP A 261 4.778 162.140 19.739 1.00 59.21 C
ANISOU 2571 CA ASP A 261 7590 6362 8544 -940 231 -304 C
ATOM 2572 C ASP A 261 4.960 162.574 18.266 1.00 62.37 C
ANISOU 2572 C ASP A 261 7992 6801 8903 -911 106 -399 C
ATOM 2573 O ASP A 261 4.602 161.832 17.347 1.00 62.52 O
ANISOU 2573 O ASP A 261 8012 6763 8979 -965 40 -470 O
ATOM 2574 CB ASP A 261 3.287 162.061 20.103 1.00 62.11 C
ANISOU 2574 CB ASP A 261 7831 6731 9037 -1033 264 -301 C
ATOM 2575 N CYS A 262 5.518 163.776 18.057 1.00 58.14 N
ANISOU 2575 N CYS A 262 7464 6362 8266 -827 76 -398 N
ATOM 2576 CA CYS A 262 5.819 164.360 16.751 1.00 57.52 C
ANISOU 2576 CA CYS A 262 7399 6333 8125 -785 -31 -470 C
ATOM 2577 C CYS A 262 7.204 163.917 16.314 1.00 58.80 C
ANISOU 2577 C CYS A 262 7684 6457 8200 -727 -42 -480 C
ATOM 2578 O CYS A 262 8.126 163.896 17.137 1.00 57.81 O
ANISOU 2578 O CYS A 262 7618 6324 8021 -678 27 -416 O
ATOM 2579 CB CYS A 262 5.734 165.885 16.812 1.00 57.46 C
ANISOU 2579 CB CYS A 262 7339 6437 8056 -726 -46 -454 C
ATOM 2580 SG CYS A 262 4.058 166.540 17.006 1.00 62.36 S
ANISOU 2580 SG CYS A 262 7803 7113 8777 -778 -56 -462 S
ATOM 2581 N SER A 263 7.369 163.608 15.015 1.00 53.77 N
ANISOU 2581 N SER A 263 7085 5803 7543 -726 -129 -562 N
ATOM 2582 CA SER A 263 8.674 163.255 14.453 1.00 51.97 C
ANISOU 2582 CA SER A 263 6968 5549 7230 -663 -140 -581 C
ATOM 2583 C SER A 263 9.597 164.464 14.548 1.00 51.97 C
ANISOU 2583 C SER A 263 6988 5641 7118 -574 -132 -544 C
ATOM 2584 O SER A 263 9.126 165.595 14.425 1.00 50.84 O
ANISOU 2584 O SER A 263 6782 5582 6955 -561 -162 -542 O
ATOM 2585 CB SER A 263 8.537 162.820 12.998 1.00 55.93 C
ANISOU 2585 CB SER A 263 7500 6027 7725 -680 -237 -682 C
ATOM 2586 OG SER A 263 7.696 161.689 12.865 1.00 68.83 O
ANISOU 2586 OG SER A 263 9117 7569 9466 -771 -252 -726 O
ATOM 2587 N HIS A 264 10.893 164.237 14.793 1.00 46.47 N
ANISOU 2587 N HIS A 264 6373 4928 6356 -512 -91 -513 N
ATOM 2588 CA HIS A 264 11.880 165.313 14.871 1.00 44.37 C
ANISOU 2588 CA HIS A 264 6127 4743 5989 -432 -82 -480 C
ATOM 2589 C HIS A 264 11.991 165.995 13.517 1.00 47.25 C
ANISOU 2589 C HIS A 264 6500 5164 6290 -404 -161 -543 C
ATOM 2590 O HIS A 264 11.942 165.306 12.494 1.00 47.60 O
ANISOU 2590 O HIS A 264 6582 5167 6336 -419 -211 -611 O
ATOM 2591 CB HIS A 264 13.244 164.758 15.300 1.00 44.79 C
ANISOU 2591 CB HIS A 264 6261 4761 5997 -376 -30 -443 C
ATOM 2592 CG HIS A 264 14.146 165.784 15.910 1.00 47.56 C
ANISOU 2592 CG HIS A 264 6613 5187 6271 -311 1 -386 C
ATOM 2593 ND1 HIS A 264 14.822 166.715 15.132 1.00 48.80 N
ANISOU 2593 ND1 HIS A 264 6781 5414 6347 -260 -34 -408 N
ATOM 2594 CD2 HIS A 264 14.461 165.990 17.210 1.00 49.16 C
ANISOU 2594 CD2 HIS A 264 6810 5403 6467 -294 63 -312 C
ATOM 2595 CE1 HIS A 264 15.524 167.448 15.981 1.00 47.61 C
ANISOU 2595 CE1 HIS A 264 6626 5313 6152 -219 5 -349 C
ATOM 2596 NE2 HIS A 264 15.334 167.055 17.241 1.00 48.19 N
ANISOU 2596 NE2 HIS A 264 6690 5357 6263 -235 60 -293 N
ATOM 2597 N ALA A 265 12.136 167.334 13.496 1.00 42.42 N
ANISOU 2597 N ALA A 265 5859 4640 5618 -364 -173 -520 N
ATOM 2598 CA ALA A 265 12.286 168.089 12.249 1.00 42.07 C
ANISOU 2598 CA ALA A 265 5829 4653 5504 -332 -242 -565 C
ATOM 2599 C ALA A 265 13.450 167.522 11.418 1.00 46.59 C
ANISOU 2599 C ALA A 265 6492 5201 6009 -289 -247 -600 C
ATOM 2600 O ALA A 265 14.408 166.998 12.002 1.00 45.62 O
ANISOU 2600 O ALA A 265 6412 5045 5876 -260 -188 -567 O
ATOM 2601 CB ALA A 265 12.505 169.565 12.541 1.00 41.79 C
ANISOU 2601 CB ALA A 265 5763 4700 5414 -289 -234 -521 C
ATOM 2602 N PRO A 266 13.373 167.526 10.070 1.00 44.33 N
ANISOU 2602 N PRO A 266 6238 4928 5677 -282 -315 -667 N
ATOM 2603 CA PRO A 266 14.469 166.925 9.290 1.00 44.54 C
ANISOU 2603 CA PRO A 266 6354 4931 5640 -238 -309 -703 C
ATOM 2604 C PRO A 266 15.798 167.670 9.478 1.00 48.62 C
ANISOU 2604 C PRO A 266 6898 5500 6076 -167 -258 -653 C
ATOM 2605 O PRO A 266 15.808 168.864 9.789 1.00 46.97 O
ANISOU 2605 O PRO A 266 6650 5358 5840 -152 -254 -608 O
ATOM 2606 CB PRO A 266 13.963 166.987 7.848 1.00 46.72 C
ANISOU 2606 CB PRO A 266 6654 5226 5873 -246 -396 -782 C
ATOM 2607 CG PRO A 266 12.958 168.086 7.839 1.00 51.22 C
ANISOU 2607 CG PRO A 266 7148 5861 6453 -266 -445 -766 C
ATOM 2608 CD PRO A 266 12.314 168.067 9.193 1.00 46.62 C
ANISOU 2608 CD PRO A 266 6488 5258 5966 -307 -401 -713 C
ATOM 2609 N LEU A 267 16.916 166.932 9.337 1.00 46.04 N
ANISOU 2609 N LEU A 267 6634 5137 5720 -126 -217 -661 N
ATOM 2610 CA LEU A 267 18.287 167.423 9.462 1.00 45.25 C
ANISOU 2610 CA LEU A 267 6558 5080 5556 -61 -167 -620 C
ATOM 2611 C LEU A 267 18.538 168.643 8.556 1.00 47.72 C
ANISOU 2611 C LEU A 267 6874 5476 5781 -32 -194 -624 C
ATOM 2612 O LEU A 267 19.196 169.583 9.002 1.00 46.43 O
ANISOU 2612 O LEU A 267 6689 5367 5587 -4 -162 -570 O
ATOM 2613 CB LEU A 267 19.273 166.294 9.108 1.00 46.11 C
ANISOU 2613 CB LEU A 267 6735 5133 5652 -20 -133 -651 C
ATOM 2614 CG LEU A 267 20.554 166.247 9.932 1.00 50.83 C
ANISOU 2614 CG LEU A 267 7335 5737 6241 34 -65 -591 C
ATOM 2615 CD1 LEU A 267 20.505 165.119 10.945 1.00 51.39 C
ANISOU 2615 CD1 LEU A 267 7412 5723 6390 23 -32 -566 C
ATOM 2616 CD2 LEU A 267 21.762 166.069 9.044 1.00 53.49 C
ANISOU 2616 CD2 LEU A 267 7723 6088 6511 99 -40 -620 C
ATOM 2617 N TRP A 268 17.996 168.640 7.307 1.00 43.69 N
ANISOU 2617 N TRP A 268 6394 4975 5232 -42 -256 -688 N
ATOM 2618 CA TRP A 268 18.166 169.743 6.353 1.00 43.21 C
ANISOU 2618 CA TRP A 268 6348 4988 5082 -14 -285 -690 C
ATOM 2619 C TRP A 268 17.504 171.036 6.868 1.00 46.26 C
ANISOU 2619 C TRP A 268 6668 5427 5483 -31 -305 -638 C
ATOM 2620 O TRP A 268 18.060 172.118 6.658 1.00 45.11 O
ANISOU 2620 O TRP A 268 6525 5338 5277 0 -291 -601 O
ATOM 2621 CB TRP A 268 17.658 169.380 4.935 1.00 42.66 C
ANISOU 2621 CB TRP A 268 6332 4916 4961 -19 -354 -770 C
ATOM 2622 CG TRP A 268 16.173 169.169 4.808 1.00 44.19 C
ANISOU 2622 CG TRP A 268 6488 5090 5212 -78 -435 -810 C
ATOM 2623 CD1 TRP A 268 15.513 167.975 4.825 1.00 47.67 C
ANISOU 2623 CD1 TRP A 268 6932 5458 5721 -124 -463 -867 C
ATOM 2624 CD2 TRP A 268 15.172 170.178 4.583 1.00 44.10 C
ANISOU 2624 CD2 TRP A 268 6427 5131 5197 -95 -501 -799 C
ATOM 2625 NE1 TRP A 268 14.165 168.176 4.643 1.00 47.37 N
ANISOU 2625 NE1 TRP A 268 6841 5430 5727 -174 -543 -892 N
ATOM 2626 CE2 TRP A 268 13.924 169.520 4.509 1.00 48.46 C
ANISOU 2626 CE2 TRP A 268 6944 5646 5823 -154 -568 -850 C
ATOM 2627 CE3 TRP A 268 15.208 171.581 4.454 1.00 44.97 C
ANISOU 2627 CE3 TRP A 268 6518 5313 5257 -67 -510 -748 C
ATOM 2628 CZ2 TRP A 268 12.719 170.214 4.324 1.00 48.04 C
ANISOU 2628 CZ2 TRP A 268 6828 5632 5795 -180 -645 -853 C
ATOM 2629 CZ3 TRP A 268 14.013 172.269 4.275 1.00 46.81 C
ANISOU 2629 CZ3 TRP A 268 6697 5576 5512 -89 -584 -748 C
ATOM 2630 CH2 TRP A 268 12.787 171.588 4.207 1.00 48.14 C
ANISOU 2630 CH2 TRP A 268 6823 5714 5753 -141 -652 -801 C
ATOM 2631 N LEU A 269 16.328 170.918 7.534 1.00 43.01 N
ANISOU 2631 N LEU A 269 6196 4993 5153 -80 -333 -635 N
ATOM 2632 CA LEU A 269 15.584 172.048 8.108 1.00 42.63 C
ANISOU 2632 CA LEU A 269 6080 4986 5131 -94 -348 -591 C
ATOM 2633 C LEU A 269 16.340 172.632 9.299 1.00 45.99 C
ANISOU 2633 C LEU A 269 6481 5427 5564 -75 -276 -522 C
ATOM 2634 O LEU A 269 16.347 173.848 9.478 1.00 45.50 O
ANISOU 2634 O LEU A 269 6396 5413 5479 -60 -275 -484 O
ATOM 2635 CB LEU A 269 14.154 171.626 8.523 1.00 43.12 C
ANISOU 2635 CB LEU A 269 6078 5018 5287 -151 -386 -611 C
ATOM 2636 CG LEU A 269 13.227 172.721 9.090 1.00 47.21 C
ANISOU 2636 CG LEU A 269 6519 5577 5843 -163 -401 -574 C
ATOM 2637 CD1 LEU A 269 12.931 173.800 8.055 1.00 47.78 C
ANISOU 2637 CD1 LEU A 269 6595 5705 5853 -135 -467 -583 C
ATOM 2638 CD2 LEU A 269 11.942 172.133 9.598 1.00 49.26 C
ANISOU 2638 CD2 LEU A 269 6708 5804 6205 -221 -421 -591 C
ATOM 2639 N MET A 270 16.994 171.769 10.088 1.00 43.23 N
ANISOU 2639 N MET A 270 6145 5038 5245 -73 -220 -506 N
ATOM 2640 CA MET A 270 17.785 172.167 11.247 1.00 43.05 C
ANISOU 2640 CA MET A 270 6104 5029 5223 -53 -158 -445 C
ATOM 2641 C MET A 270 18.937 173.059 10.847 1.00 47.31 C
ANISOU 2641 C MET A 270 6668 5620 5689 -9 -140 -423 C
ATOM 2642 O MET A 270 19.096 174.138 11.426 1.00 46.59 O
ANISOU 2642 O MET A 270 6547 5568 5588 -4 -125 -381 O
ATOM 2643 CB MET A 270 18.323 170.943 11.992 1.00 45.65 C
ANISOU 2643 CB MET A 270 6452 5302 5590 -51 -112 -434 C
ATOM 2644 CG MET A 270 18.111 171.030 13.482 1.00 49.49 C
ANISOU 2644 CG MET A 270 6898 5781 6123 -67 -72 -380 C
ATOM 2645 SD MET A 270 16.378 170.836 13.934 1.00 54.04 S
ANISOU 2645 SD MET A 270 7420 6330 6783 -131 -93 -388 S
ATOM 2646 CE MET A 270 16.059 169.323 13.157 1.00 51.77 C
ANISOU 2646 CE MET A 270 7170 5965 6534 -159 -117 -447 C
ATOM 2647 N TYR A 271 19.714 172.631 9.833 1.00 44.29 N
ANISOU 2647 N TYR A 271 6338 5236 5253 20 -137 -454 N
ATOM 2648 CA TYR A 271 20.868 173.384 9.362 1.00 44.37 C
ANISOU 2648 CA TYR A 271 6370 5295 5195 59 -110 -434 C
ATOM 2649 C TYR A 271 20.440 174.604 8.527 1.00 47.44 C
ANISOU 2649 C TYR A 271 6761 5730 5533 58 -149 -432 C
ATOM 2650 O TYR A 271 21.200 175.570 8.466 1.00 46.45 O
ANISOU 2650 O TYR A 271 6636 5646 5368 77 -123 -396 O
ATOM 2651 CB TYR A 271 21.871 172.473 8.632 1.00 46.64 C
ANISOU 2651 CB TYR A 271 6710 5567 5446 96 -82 -466 C
ATOM 2652 CG TYR A 271 22.629 171.597 9.613 1.00 49.15 C
ANISOU 2652 CG TYR A 271 7019 5849 5807 113 -33 -445 C
ATOM 2653 CD1 TYR A 271 23.623 172.129 10.428 1.00 50.98 C
ANISOU 2653 CD1 TYR A 271 7220 6114 6036 134 9 -393 C
ATOM 2654 CD2 TYR A 271 22.283 170.262 9.799 1.00 50.53 C
ANISOU 2654 CD2 TYR A 271 7214 5955 6030 104 -35 -476 C
ATOM 2655 CE1 TYR A 271 24.300 171.341 11.358 1.00 52.78 C
ANISOU 2655 CE1 TYR A 271 7438 6314 6300 156 45 -370 C
ATOM 2656 CE2 TYR A 271 22.951 169.461 10.727 1.00 51.71 C
ANISOU 2656 CE2 TYR A 271 7361 6068 6218 126 7 -449 C
ATOM 2657 CZ TYR A 271 23.961 170.007 11.507 1.00 60.42 C
ANISOU 2657 CZ TYR A 271 8433 7212 7311 155 45 -394 C
ATOM 2658 OH TYR A 271 24.633 169.245 12.436 1.00 61.42 O
ANISOU 2658 OH TYR A 271 8557 7309 7472 182 78 -363 O
ATOM 2659 N LEU A 272 19.201 174.609 7.975 1.00 43.58 N
ANISOU 2659 N LEU A 272 6269 5234 5054 35 -212 -465 N
ATOM 2660 CA LEU A 272 18.671 175.773 7.261 1.00 43.19 C
ANISOU 2660 CA LEU A 272 6221 5227 4963 39 -257 -456 C
ATOM 2661 C LEU A 272 18.314 176.862 8.284 1.00 44.24 C
ANISOU 2661 C LEU A 272 6297 5375 5136 29 -248 -405 C
ATOM 2662 O LEU A 272 18.554 178.045 8.036 1.00 42.83 O
ANISOU 2662 O LEU A 272 6124 5231 4920 45 -247 -373 O
ATOM 2663 CB LEU A 272 17.454 175.407 6.388 1.00 44.41 C
ANISOU 2663 CB LEU A 272 6383 5372 5118 21 -337 -509 C
ATOM 2664 CG LEU A 272 16.882 176.539 5.504 1.00 49.94 C
ANISOU 2664 CG LEU A 272 7092 6116 5766 36 -396 -500 C
ATOM 2665 CD1 LEU A 272 17.730 176.751 4.255 1.00 50.76 C
ANISOU 2665 CD1 LEU A 272 7274 6248 5762 72 -390 -507 C
ATOM 2666 CD2 LEU A 272 15.435 176.266 5.125 1.00 52.77 C
ANISOU 2666 CD2 LEU A 272 7421 6466 6161 10 -483 -543 C
ATOM 2667 N ALA A 273 17.774 176.448 9.445 1.00 40.17 N
ANISOU 2667 N ALA A 273 5732 4833 4696 2 -234 -398 N
ATOM 2668 CA ALA A 273 17.415 177.340 10.551 1.00 39.16 C
ANISOU 2668 CA ALA A 273 5553 4716 4608 -6 -217 -356 C
ATOM 2669 C ALA A 273 18.677 177.917 11.222 1.00 40.82 C
ANISOU 2669 C ALA A 273 5772 4945 4794 12 -160 -314 C
ATOM 2670 O ALA A 273 18.670 179.088 11.597 1.00 39.68 O
ANISOU 2670 O ALA A 273 5610 4822 4645 16 -155 -284 O
ATOM 2671 CB ALA A 273 16.560 176.597 11.568 1.00 39.90 C
ANISOU 2671 CB ALA A 273 5601 4777 4781 -39 -208 -361 C
ATOM 2672 N ILE A 274 19.764 177.113 11.326 1.00 37.11 N
ANISOU 2672 N ILE A 274 5326 4465 4308 24 -121 -315 N
ATOM 2673 CA ILE A 274 21.054 177.528 11.910 1.00 36.48 C
ANISOU 2673 CA ILE A 274 5246 4406 4208 41 -73 -279 C
ATOM 2674 C ILE A 274 21.711 178.579 10.982 1.00 40.66 C
ANISOU 2674 C ILE A 274 5799 4972 4678 58 -72 -267 C
ATOM 2675 O ILE A 274 22.208 179.591 11.468 1.00 39.88 O
ANISOU 2675 O ILE A 274 5685 4895 4574 56 -53 -234 O
ATOM 2676 CB ILE A 274 21.986 176.296 12.205 1.00 39.07 C
ANISOU 2676 CB ILE A 274 5587 4714 4542 58 -37 -284 C
ATOM 2677 CG1 ILE A 274 21.450 175.467 13.398 1.00 38.11 C
ANISOU 2677 CG1 ILE A 274 5445 4556 4480 40 -27 -277 C
ATOM 2678 CG2 ILE A 274 23.452 176.720 12.470 1.00 39.86 C
ANISOU 2678 CG2 ILE A 274 5684 4846 4614 81 4 -254 C
ATOM 2679 CD1 ILE A 274 21.911 173.991 13.454 1.00 40.40 C
ANISOU 2679 CD1 ILE A 274 5759 4803 4788 55 -7 -291 C
ATOM 2680 N VAL A 275 21.672 178.345 9.658 1.00 38.55 N
ANISOU 2680 N VAL A 275 5573 4709 4364 70 -93 -294 N
ATOM 2681 CA VAL A 275 22.216 179.235 8.627 1.00 38.58 C
ANISOU 2681 CA VAL A 275 5611 4745 4303 86 -88 -280 C
ATOM 2682 C VAL A 275 21.447 180.572 8.639 1.00 41.97 C
ANISOU 2682 C VAL A 275 6028 5184 4734 77 -120 -254 C
ATOM 2683 O VAL A 275 22.087 181.624 8.646 1.00 40.27 O
ANISOU 2683 O VAL A 275 5817 4986 4498 78 -95 -217 O
ATOM 2684 CB VAL A 275 22.194 178.527 7.241 1.00 43.19 C
ANISOU 2684 CB VAL A 275 6250 5330 4830 105 -106 -321 C
ATOM 2685 CG1 VAL A 275 22.031 179.505 6.081 1.00 43.61 C
ANISOU 2685 CG1 VAL A 275 6344 5412 4814 116 -130 -309 C
ATOM 2686 CG2 VAL A 275 23.442 177.674 7.056 1.00 43.08 C
ANISOU 2686 CG2 VAL A 275 6256 5317 4795 128 -51 -333 C
ATOM 2687 N LEU A 276 20.089 180.525 8.698 1.00 39.58 N
ANISOU 2687 N LEU A 276 5708 4867 4465 66 -173 -272 N
ATOM 2688 CA LEU A 276 19.229 181.718 8.723 1.00 39.42 C
ANISOU 2688 CA LEU A 276 5671 4852 4456 66 -208 -250 C
ATOM 2689 C LEU A 276 19.537 182.602 9.951 1.00 41.83 C
ANISOU 2689 C LEU A 276 5942 5154 4798 57 -171 -215 C
ATOM 2690 O LEU A 276 19.604 183.823 9.798 1.00 41.45 O
ANISOU 2690 O LEU A 276 5904 5111 4734 64 -173 -185 O
ATOM 2691 CB LEU A 276 17.732 181.332 8.670 1.00 39.80 C
ANISOU 2691 CB LEU A 276 5688 4887 4546 58 -269 -281 C
ATOM 2692 CG LEU A 276 16.662 182.444 8.847 1.00 44.50 C
ANISOU 2692 CG LEU A 276 6251 5486 5172 64 -307 -263 C
ATOM 2693 CD1 LEU A 276 16.789 183.553 7.795 1.00 44.79 C
ANISOU 2693 CD1 LEU A 276 6333 5539 5145 92 -334 -236 C
ATOM 2694 CD2 LEU A 276 15.273 181.865 8.796 1.00 46.64 C
ANISOU 2694 CD2 LEU A 276 6478 5749 5493 53 -363 -298 C
ATOM 2695 N SER A 277 19.774 181.994 11.135 1.00 36.93 N
ANISOU 2695 N SER A 277 5289 4523 4220 43 -139 -217 N
ATOM 2696 CA SER A 277 20.096 182.740 12.354 1.00 36.41 C
ANISOU 2696 CA SER A 277 5197 4457 4180 34 -107 -191 C
ATOM 2697 C SER A 277 21.460 183.456 12.229 1.00 42.65 C
ANISOU 2697 C SER A 277 6007 5264 4934 36 -73 -165 C
ATOM 2698 O SER A 277 21.624 184.568 12.750 1.00 41.89 O
ANISOU 2698 O SER A 277 5903 5166 4846 29 -63 -144 O
ATOM 2699 CB SER A 277 20.067 181.829 13.578 1.00 38.74 C
ANISOU 2699 CB SER A 277 5462 4741 4516 22 -83 -198 C
ATOM 2700 OG SER A 277 21.241 181.050 13.733 1.00 45.55 O
ANISOU 2700 OG SER A 277 6336 5609 5362 27 -51 -195 O
ATOM 2701 N HIS A 278 22.410 182.835 11.498 1.00 40.51 N
ANISOU 2701 N HIS A 278 5760 5007 4626 45 -53 -169 N
ATOM 2702 CA HIS A 278 23.739 183.391 11.267 1.00 40.47 C
ANISOU 2702 CA HIS A 278 5763 5021 4591 43 -14 -145 C
ATOM 2703 C HIS A 278 23.723 184.533 10.229 1.00 45.29 C
ANISOU 2703 C HIS A 278 6409 5636 5162 45 -21 -122 C
ATOM 2704 O HIS A 278 24.580 185.416 10.326 1.00 46.07 O
ANISOU 2704 O HIS A 278 6507 5743 5256 32 9 -93 O
ATOM 2705 CB HIS A 278 24.731 182.291 10.863 1.00 41.28 C
ANISOU 2705 CB HIS A 278 5874 5139 4673 58 16 -157 C
ATOM 2706 CG HIS A 278 25.033 181.301 11.956 1.00 44.39 C
ANISOU 2706 CG HIS A 278 6236 5525 5104 60 30 -167 C
ATOM 2707 ND1 HIS A 278 25.713 180.125 11.693 1.00 46.27 N
ANISOU 2707 ND1 HIS A 278 6480 5764 5335 82 52 -182 N
ATOM 2708 CD2 HIS A 278 24.763 181.355 13.283 1.00 45.62 C
ANISOU 2708 CD2 HIS A 278 6361 5673 5301 48 26 -159 C
ATOM 2709 CE1 HIS A 278 25.820 179.498 12.852 1.00 45.30 C
ANISOU 2709 CE1 HIS A 278 6330 5631 5250 83 57 -179 C
ATOM 2710 NE2 HIS A 278 25.270 180.202 13.839 1.00 45.42 N
ANISOU 2710 NE2 HIS A 278 6324 5643 5290 61 42 -165 N
ATOM 2711 N THR A 279 22.740 184.562 9.285 1.00 41.70 N
ANISOU 2711 N THR A 279 5986 5177 4683 60 -63 -131 N
ATOM 2712 CA THR A 279 22.631 185.639 8.271 1.00 42.14 C
ANISOU 2712 CA THR A 279 6084 5234 4694 69 -75 -102 C
ATOM 2713 C THR A 279 22.229 186.985 8.922 1.00 47.01 C
ANISOU 2713 C THR A 279 6688 5828 5346 59 -83 -74 C
ATOM 2714 O THR A 279 22.333 188.033 8.280 1.00 46.96 O
ANISOU 2714 O THR A 279 6718 5814 5312 63 -83 -39 O
ATOM 2715 CB THR A 279 21.653 185.304 7.114 1.00 47.33 C
ANISOU 2715 CB THR A 279 6778 5895 5310 92 -130 -121 C
ATOM 2716 OG1 THR A 279 20.314 185.251 7.603 1.00 48.49 O
ANISOU 2716 OG1 THR A 279 6893 6026 5506 94 -183 -140 O
ATOM 2717 CG2 THR A 279 22.021 184.034 6.340 1.00 42.74 C
ANISOU 2717 CG2 THR A 279 6224 5330 4685 104 -124 -156 C
ATOM 2718 N ASN A 280 21.780 186.955 10.189 1.00 44.35 N
ANISOU 2718 N ASN A 280 6306 5477 5067 49 -88 -88 N
ATOM 2719 CA ASN A 280 21.421 188.159 10.936 1.00 44.76 C
ANISOU 2719 CA ASN A 280 6347 5504 5156 43 -90 -71 C
ATOM 2720 C ASN A 280 22.654 189.029 11.190 1.00 49.02 C
ANISOU 2720 C ASN A 280 6896 6040 5691 18 -47 -44 C
ATOM 2721 O ASN A 280 22.529 190.251 11.277 1.00 49.20 O
ANISOU 2721 O ASN A 280 6934 6034 5726 14 -49 -22 O
ATOM 2722 CB ASN A 280 20.738 187.811 12.261 1.00 46.29 C
ANISOU 2722 CB ASN A 280 6494 5690 5404 38 -95 -96 C
ATOM 2723 CG ASN A 280 20.027 188.996 12.863 1.00 61.62 C
ANISOU 2723 CG ASN A 280 8429 7604 7379 45 -105 -88 C
ATOM 2724 OD1 ASN A 280 18.977 189.425 12.382 1.00 59.05 O
ANISOU 2724 OD1 ASN A 280 8107 7266 7063 69 -141 -86 O
ATOM 2725 ND2 ASN A 280 20.635 189.607 13.864 1.00 47.67 N
ANISOU 2725 ND2 ASN A 280 6655 5827 5631 26 -75 -86 N
ATOM 2726 N SER A 281 23.846 188.402 11.274 1.00 45.38 N
ANISOU 2726 N SER A 281 6423 5604 5217 3 -10 -46 N
ATOM 2727 CA SER A 281 25.125 189.084 11.487 1.00 45.13 C
ANISOU 2727 CA SER A 281 6385 5575 5187 -27 31 -24 C
ATOM 2728 C SER A 281 25.641 189.756 10.191 1.00 48.68 C
ANISOU 2728 C SER A 281 6879 6024 5594 -30 53 14 C
ATOM 2729 O SER A 281 26.718 190.354 10.211 1.00 49.00 O
ANISOU 2729 O SER A 281 6912 6066 5638 -60 93 36 O
ATOM 2730 CB SER A 281 26.162 188.103 12.030 1.00 48.38 C
ANISOU 2730 CB SER A 281 6758 6019 5606 -35 59 -39 C
ATOM 2731 OG SER A 281 25.767 187.612 13.301 1.00 56.09 O
ANISOU 2731 OG SER A 281 7702 6994 6616 -35 42 -63 O
ATOM 2732 N VAL A 282 24.852 189.698 9.091 1.00 44.41 N
ANISOU 2732 N VAL A 282 6382 5481 5011 0 27 22 N
ATOM 2733 CA VAL A 282 25.178 190.277 7.778 1.00 44.47 C
ANISOU 2733 CA VAL A 282 6444 5489 4962 5 45 61 C
ATOM 2734 C VAL A 282 24.210 191.438 7.417 1.00 48.57 C
ANISOU 2734 C VAL A 282 7005 5969 5479 21 7 91 C
ATOM 2735 O VAL A 282 24.612 192.367 6.715 1.00 48.46 O
ANISOU 2735 O VAL A 282 7037 5939 5438 13 31 139 O
ATOM 2736 CB VAL A 282 25.158 189.162 6.677 1.00 48.38 C
ANISOU 2736 CB VAL A 282 6969 6021 5394 34 42 45 C
ATOM 2737 CG1 VAL A 282 25.390 189.722 5.272 1.00 48.85 C
ANISOU 2737 CG1 VAL A 282 7096 6086 5378 46 60 87 C
ATOM 2738 CG2 VAL A 282 26.169 188.058 6.975 1.00 47.95 C
ANISOU 2738 CG2 VAL A 282 6877 5998 5344 27 85 18 C
ATOM 2739 N VAL A 283 22.954 191.383 7.896 1.00 45.52 N
ANISOU 2739 N VAL A 283 6603 5567 5125 44 -47 67 N
ATOM 2740 CA VAL A 283 21.891 192.324 7.523 1.00 45.68 C
ANISOU 2740 CA VAL A 283 6656 5554 5147 73 -92 91 C
ATOM 2741 C VAL A 283 22.048 193.759 8.087 1.00 49.80 C
ANISOU 2741 C VAL A 283 7189 6023 5711 57 -75 121 C
ATOM 2742 O VAL A 283 21.799 194.693 7.327 1.00 51.19 O
ANISOU 2742 O VAL A 283 7417 6169 5864 75 -86 166 O
ATOM 2743 CB VAL A 283 20.464 191.793 7.843 1.00 49.26 C
ANISOU 2743 CB VAL A 283 7075 6011 5631 104 -155 53 C
ATOM 2744 CG1 VAL A 283 20.130 190.566 6.999 1.00 49.28 C
ANISOU 2744 CG1 VAL A 283 7084 6053 5588 122 -186 27 C
ATOM 2745 CG2 VAL A 283 20.259 191.505 9.331 1.00 48.06 C
ANISOU 2745 CG2 VAL A 283 6861 5853 5548 87 -144 16 C
ATOM 2746 N ASN A 284 22.387 193.949 9.381 1.00 45.05 N
ANISOU 2746 N ASN A 284 6545 5406 5166 27 -52 98 N
ATOM 2747 CA ASN A 284 22.464 195.285 10.016 1.00 44.57 C
ANISOU 2747 CA ASN A 284 6497 5288 5150 11 -40 113 C
ATOM 2748 C ASN A 284 23.256 196.337 9.193 1.00 47.68 C
ANISOU 2748 C ASN A 284 6947 5648 5522 -12 -7 171 C
ATOM 2749 O ASN A 284 22.680 197.404 8.961 1.00 47.58 O
ANISOU 2749 O ASN A 284 6976 5581 5522 9 -24 200 O
ATOM 2750 CB ASN A 284 23.020 195.220 11.439 1.00 45.03 C
ANISOU 2750 CB ASN A 284 6509 5347 5256 -27 -17 76 C
ATOM 2751 CG ASN A 284 22.175 194.466 12.437 1.00 69.70 C
ANISOU 2751 CG ASN A 284 9586 8489 8407 -7 -41 28 C
ATOM 2752 OD1 ASN A 284 21.293 193.662 12.094 1.00 60.49 O
ANISOU 2752 OD1 ASN A 284 8406 7347 7230 26 -71 15 O
ATOM 2753 ND2 ASN A 284 22.471 194.680 13.712 1.00 62.38 N
ANISOU 2753 ND2 ASN A 284 8634 7553 7515 -30 -26 -1 N
ATOM 2754 N PRO A 285 24.507 196.088 8.692 1.00 43.04 N
ANISOU 2754 N PRO A 285 6363 5088 4903 -49 42 191 N
ATOM 2755 CA PRO A 285 25.199 197.134 7.903 1.00 42.73 C
ANISOU 2755 CA PRO A 285 6378 5012 4847 -74 82 252 C
ATOM 2756 C PRO A 285 24.424 197.599 6.663 1.00 45.43 C
ANISOU 2756 C PRO A 285 6792 5333 5135 -27 56 303 C
ATOM 2757 O PRO A 285 24.608 198.734 6.230 1.00 44.98 O
ANISOU 2757 O PRO A 285 6789 5221 5078 -38 75 357 O
ATOM 2758 CB PRO A 285 26.511 196.456 7.500 1.00 44.32 C
ANISOU 2758 CB PRO A 285 6557 5265 5018 -110 139 259 C
ATOM 2759 CG PRO A 285 26.740 195.437 8.559 1.00 48.14 C
ANISOU 2759 CG PRO A 285 6967 5790 5533 -119 131 198 C
ATOM 2760 CD PRO A 285 25.375 194.901 8.853 1.00 43.39 C
ANISOU 2760 CD PRO A 285 6361 5193 4933 -69 70 164 C
ATOM 2761 N PHE A 286 23.542 196.744 6.115 1.00 41.76 N
ANISOU 2761 N PHE A 286 6332 4910 4626 24 7 285 N
ATOM 2762 CA PHE A 286 22.737 197.075 4.935 1.00 42.23 C
ANISOU 2762 CA PHE A 286 6457 4961 4627 76 -33 328 C
ATOM 2763 C PHE A 286 21.628 198.041 5.288 1.00 46.85 C
ANISOU 2763 C PHE A 286 7055 5487 5259 113 -84 339 C
ATOM 2764 O PHE A 286 21.396 198.983 4.532 1.00 48.10 O
ANISOU 2764 O PHE A 286 7281 5603 5392 138 -92 399 O
ATOM 2765 CB PHE A 286 22.170 195.812 4.260 1.00 43.56 C
ANISOU 2765 CB PHE A 286 6621 5194 4737 114 -77 296 C
ATOM 2766 CG PHE A 286 23.195 195.154 3.372 1.00 44.74 C
ANISOU 2766 CG PHE A 286 6796 5390 4811 97 -26 308 C
ATOM 2767 CD1 PHE A 286 24.103 194.237 3.893 1.00 46.90 C
ANISOU 2767 CD1 PHE A 286 7017 5702 5102 62 20 268 C
ATOM 2768 CD2 PHE A 286 23.300 195.501 2.032 1.00 47.42 C
ANISOU 2768 CD2 PHE A 286 7218 5736 5062 119 -19 363 C
ATOM 2769 CE1 PHE A 286 25.085 193.664 3.082 1.00 48.13 C
ANISOU 2769 CE1 PHE A 286 7193 5900 5193 52 76 278 C
ATOM 2770 CE2 PHE A 286 24.287 194.934 1.223 1.00 50.76 C
ANISOU 2770 CE2 PHE A 286 7667 6204 5414 106 41 374 C
ATOM 2771 CZ PHE A 286 25.175 194.024 1.757 1.00 48.32 C
ANISOU 2771 CZ PHE A 286 7298 5932 5130 73 90 329 C
ATOM 2772 N ILE A 287 20.974 197.833 6.442 1.00 42.65 N
ANISOU 2772 N ILE A 287 6462 4949 4795 120 -110 284 N
ATOM 2773 CA ILE A 287 19.894 198.684 6.951 1.00 42.71 C
ANISOU 2773 CA ILE A 287 6467 4902 4858 160 -151 282 C
ATOM 2774 C ILE A 287 20.460 200.087 7.262 1.00 47.56 C
ANISOU 2774 C ILE A 287 7124 5435 5510 132 -110 320 C
ATOM 2775 O ILE A 287 19.826 201.076 6.895 1.00 48.64 O
ANISOU 2775 O ILE A 287 7309 5514 5657 174 -136 360 O
ATOM 2776 CB ILE A 287 19.184 198.022 8.175 1.00 44.99 C
ANISOU 2776 CB ILE A 287 6676 5212 5205 167 -172 212 C
ATOM 2777 CG1 ILE A 287 18.715 196.577 7.861 1.00 45.00 C
ANISOU 2777 CG1 ILE A 287 6635 5285 5175 182 -206 176 C
ATOM 2778 CG2 ILE A 287 18.027 198.873 8.738 1.00 45.80 C
ANISOU 2778 CG2 ILE A 287 6769 5264 5369 215 -206 205 C
ATOM 2779 CD1 ILE A 287 17.754 196.393 6.602 1.00 50.35 C
ANISOU 2779 CD1 ILE A 287 7342 5985 5803 238 -275 197 C
ATOM 2780 N TYR A 288 21.671 200.175 7.852 1.00 42.94 N
ANISOU 2780 N TYR A 288 6524 4844 4946 64 -51 309 N
ATOM 2781 CA TYR A 288 22.312 201.466 8.137 1.00 42.82 C
ANISOU 2781 CA TYR A 288 6549 4750 4973 24 -12 339 C
ATOM 2782 C TYR A 288 22.604 202.226 6.840 1.00 48.20 C
ANISOU 2782 C TYR A 288 7312 5393 5606 28 7 424 C
ATOM 2783 O TYR A 288 22.292 203.411 6.748 1.00 49.18 O
ANISOU 2783 O TYR A 288 7492 5435 5760 44 3 464 O
ATOM 2784 CB TYR A 288 23.616 201.297 8.950 1.00 42.69 C
ANISOU 2784 CB TYR A 288 6490 4746 4986 -56 41 309 C
ATOM 2785 CG TYR A 288 23.483 200.535 10.250 1.00 42.40 C
ANISOU 2785 CG TYR A 288 6379 4748 4984 -64 28 232 C
ATOM 2786 CD1 TYR A 288 22.364 200.691 11.063 1.00 43.89 C
ANISOU 2786 CD1 TYR A 288 6552 4914 5211 -21 -10 192 C
ATOM 2787 CD2 TYR A 288 24.502 199.701 10.698 1.00 42.53 C
ANISOU 2787 CD2 TYR A 288 6343 4821 4996 -112 56 203 C
ATOM 2788 CE1 TYR A 288 22.234 199.982 12.256 1.00 44.72 C
ANISOU 2788 CE1 TYR A 288 6597 5057 5340 -27 -16 128 C
ATOM 2789 CE2 TYR A 288 24.383 198.985 11.887 1.00 42.47 C
ANISOU 2789 CE2 TYR A 288 6275 4848 5012 -115 43 140 C
ATOM 2790 CZ TYR A 288 23.249 199.133 12.668 1.00 49.01 C
ANISOU 2790 CZ TYR A 288 7096 5655 5871 -75 9 104 C
ATOM 2791 OH TYR A 288 23.142 198.455 13.860 1.00 49.40 O
ANISOU 2791 OH TYR A 288 7094 5738 5937 -79 3 48 O
ATOM 2792 N ALA A 289 23.169 201.530 5.838 1.00 44.98 N
ANISOU 2792 N ALA A 289 6920 5046 5125 20 29 453 N
ATOM 2793 CA ALA A 289 23.526 202.075 4.528 1.00 45.92 C
ANISOU 2793 CA ALA A 289 7121 5146 5180 23 56 537 C
ATOM 2794 C ALA A 289 22.293 202.546 3.743 1.00 51.40 C
ANISOU 2794 C ALA A 289 7878 5812 5838 106 -9 580 C
ATOM 2795 O ALA A 289 22.363 203.568 3.059 1.00 51.33 O
ANISOU 2795 O ALA A 289 7950 5742 5812 114 6 656 O
ATOM 2796 CB ALA A 289 24.282 201.033 3.724 1.00 46.43 C
ANISOU 2796 CB ALA A 289 7181 5295 5167 7 91 542 C
ATOM 2797 N TYR A 290 21.165 201.823 3.864 1.00 48.40 N
ANISOU 2797 N TYR A 290 7460 5476 5453 165 -82 534 N
ATOM 2798 CA TYR A 290 19.939 202.176 3.156 1.00 49.13 C
ANISOU 2798 CA TYR A 290 7595 5554 5517 247 -157 567 C
ATOM 2799 C TYR A 290 19.086 203.212 3.894 1.00 51.20 C
ANISOU 2799 C TYR A 290 7854 5734 5863 285 -188 566 C
ATOM 2800 O TYR A 290 18.514 204.082 3.241 1.00 51.46 O
ANISOU 2800 O TYR A 290 7953 5716 5883 340 -221 627 O
ATOM 2801 CB TYR A 290 19.090 200.922 2.868 1.00 50.81 C
ANISOU 2801 CB TYR A 290 7762 5853 5690 291 -225 517 C
ATOM 2802 CG TYR A 290 19.454 200.241 1.567 1.00 54.85 C
ANISOU 2802 CG TYR A 290 8324 6427 6089 298 -225 545 C
ATOM 2803 CD1 TYR A 290 19.012 200.745 0.344 1.00 58.45 C
ANISOU 2803 CD1 TYR A 290 8866 6875 6466 352 -266 614 C
ATOM 2804 CD2 TYR A 290 20.240 199.094 1.553 1.00 55.56 C
ANISOU 2804 CD2 TYR A 290 8381 6585 6146 254 -186 503 C
ATOM 2805 CE1 TYR A 290 19.349 200.128 -0.860 1.00 59.94 C
ANISOU 2805 CE1 TYR A 290 9110 7125 6539 361 -264 636 C
ATOM 2806 CE2 TYR A 290 20.583 198.465 0.354 1.00 57.45 C
ANISOU 2806 CE2 TYR A 290 8671 6880 6277 264 -181 522 C
ATOM 2807 CZ TYR A 290 20.135 198.987 -0.851 1.00 67.13 C
ANISOU 2807 CZ TYR A 290 9986 8100 7419 316 -219 586 C
ATOM 2808 OH TYR A 290 20.478 198.384 -2.038 1.00 68.77 O
ANISOU 2808 OH TYR A 290 10254 8367 7509 328 -212 602 O
ATOM 2809 N ARG A 291 19.003 203.137 5.234 1.00 45.95 N
ANISOU 2809 N ARG A 291 7120 5057 5282 262 -177 498 N
ATOM 2810 CA ARG A 291 18.109 204.005 6.012 1.00 45.05 C
ANISOU 2810 CA ARG A 291 6997 4873 5248 305 -204 482 C
ATOM 2811 C ARG A 291 18.770 205.190 6.766 1.00 48.22 C
ANISOU 2811 C ARG A 291 7431 5175 5716 260 -149 489 C
ATOM 2812 O ARG A 291 18.040 206.108 7.146 1.00 47.61 O
ANISOU 2812 O ARG A 291 7372 5023 5695 307 -169 491 O
ATOM 2813 CB ARG A 291 17.311 203.159 7.012 1.00 42.11 C
ANISOU 2813 CB ARG A 291 6528 4550 4920 324 -235 398 C
ATOM 2814 CG ARG A 291 16.398 202.140 6.328 1.00 50.28 C
ANISOU 2814 CG ARG A 291 7527 5665 5911 375 -302 386 C
ATOM 2815 CD ARG A 291 15.277 201.657 7.220 1.00 58.14 C
ANISOU 2815 CD ARG A 291 8436 6687 6969 411 -339 321 C
ATOM 2816 NE ARG A 291 14.378 202.749 7.598 1.00 67.83 N
ANISOU 2816 NE ARG A 291 9667 7843 8260 473 -361 330 N
ATOM 2817 CZ ARG A 291 13.230 203.027 6.993 1.00 79.52 C
ANISOU 2817 CZ ARG A 291 11145 9321 9746 555 -430 355 C
ATOM 2818 NH1 ARG A 291 12.808 202.281 5.979 1.00 61.87 N
ANISOU 2818 NH1 ARG A 291 8905 7154 7451 580 -491 369 N
ATOM 2819 NH2 ARG A 291 12.485 204.043 7.407 1.00 67.84 N
ANISOU 2819 NH2 ARG A 291 9669 7774 8333 614 -442 361 N
ATOM 2820 N ILE A 292 20.099 205.181 7.009 1.00 44.41 N
ANISOU 2820 N ILE A 292 6951 4689 5233 172 -83 487 N
ATOM 2821 CA ILE A 292 20.748 206.278 7.749 1.00 44.32 C
ANISOU 2821 CA ILE A 292 6967 4584 5290 119 -37 485 C
ATOM 2822 C ILE A 292 21.766 206.963 6.823 1.00 49.39 C
ANISOU 2822 C ILE A 292 7683 5179 5902 68 15 568 C
ATOM 2823 O ILE A 292 22.803 206.378 6.508 1.00 48.97 O
ANISOU 2823 O ILE A 292 7612 5182 5811 6 60 576 O
ATOM 2824 CB ILE A 292 21.378 205.817 9.110 1.00 46.53 C
ANISOU 2824 CB ILE A 292 7173 4892 5615 54 -9 400 C
ATOM 2825 CG1 ILE A 292 20.364 205.016 9.975 1.00 46.09 C
ANISOU 2825 CG1 ILE A 292 7045 4891 5578 103 -52 326 C
ATOM 2826 CG2 ILE A 292 21.943 207.021 9.902 1.00 47.17 C
ANISOU 2826 CG2 ILE A 292 7286 4870 5768 1 26 388 C
ATOM 2827 CD1 ILE A 292 20.962 204.139 11.064 1.00 47.48 C
ANISOU 2827 CD1 ILE A 292 7148 5128 5765 49 -32 253 C
ATOM 2828 N ARG A 293 21.448 208.207 6.393 1.00 47.32 N
ANISOU 2828 N ARG A 293 7505 4813 5660 98 14 632 N
ATOM 2829 CA ARG A 293 22.238 209.042 5.480 1.00 48.16 C
ANISOU 2829 CA ARG A 293 7699 4855 5745 58 65 725 C
ATOM 2830 C ARG A 293 23.673 209.272 5.982 1.00 51.66 C
ANISOU 2830 C ARG A 293 8123 5276 6229 -60 141 711 C
ATOM 2831 O ARG A 293 24.602 209.222 5.175 1.00 51.75 O
ANISOU 2831 O ARG A 293 8160 5305 6198 -112 196 770 O
ATOM 2832 CB ARG A 293 21.537 210.392 5.244 1.00 49.38 C
ANISOU 2832 CB ARG A 293 7942 4884 5937 114 45 783 C
ATOM 2833 CG ARG A 293 22.091 211.191 4.056 1.00 60.20 C
ANISOU 2833 CG ARG A 293 9418 6190 7265 96 89 900 C
ATOM 2834 CD ARG A 293 21.358 212.504 3.839 1.00 71.11 C
ANISOU 2834 CD ARG A 293 10892 7439 8687 161 66 961 C
ATOM 2835 NE ARG A 293 20.050 212.314 3.213 1.00 80.07 N
ANISOU 2835 NE ARG A 293 12044 8605 9773 284 -17 988 N
ATOM 2836 N GLU A 294 23.848 209.525 7.295 1.00 47.60 N
ANISOU 2836 N GLU A 294 7563 4727 5797 -101 143 632 N
ATOM 2837 CA GLU A 294 25.159 209.752 7.911 1.00 47.35 C
ANISOU 2837 CA GLU A 294 7502 4676 5814 -213 200 606 C
ATOM 2838 C GLU A 294 26.070 208.519 7.757 1.00 49.68 C
ANISOU 2838 C GLU A 294 7721 5095 6061 -262 228 587 C
ATOM 2839 O GLU A 294 27.249 208.694 7.451 1.00 49.15 O
ANISOU 2839 O GLU A 294 7651 5025 6000 -345 289 620 O
ATOM 2840 CB GLU A 294 25.017 210.136 9.391 1.00 48.52 C
ANISOU 2840 CB GLU A 294 7616 4776 6044 -233 181 514 C
ATOM 2841 CG GLU A 294 26.216 210.890 9.949 1.00 61.63 C
ANISOU 2841 CG GLU A 294 9277 6368 7771 -345 229 498 C
ATOM 2842 CD GLU A 294 26.564 212.205 9.273 1.00 87.61 C
ANISOU 2842 CD GLU A 294 12662 9530 11097 -382 270 580 C
ATOM 2843 OE1 GLU A 294 27.743 212.375 8.888 1.00 81.46 O
ANISOU 2843 OE1 GLU A 294 11879 8746 10328 -475 328 619 O
ATOM 2844 OE2 GLU A 294 25.664 213.065 9.125 1.00 84.10 O
ANISOU 2844 OE2 GLU A 294 12293 8987 10674 -316 247 608 O
ATOM 2845 N PHE A 295 25.518 207.286 7.937 1.00 44.73 N
ANISOU 2845 N PHE A 295 7032 4571 5391 -211 187 538 N
ATOM 2846 CA PHE A 295 26.259 206.024 7.779 1.00 43.65 C
ANISOU 2846 CA PHE A 295 6827 4550 5207 -241 208 517 C
ATOM 2847 C PHE A 295 26.611 205.783 6.301 1.00 47.97 C
ANISOU 2847 C PHE A 295 7420 5133 5673 -233 244 599 C
ATOM 2848 O PHE A 295 27.745 205.405 5.996 1.00 48.36 O
ANISOU 2848 O PHE A 295 7441 5228 5706 -294 302 613 O
ATOM 2849 CB PHE A 295 25.464 204.816 8.334 1.00 44.00 C
ANISOU 2849 CB PHE A 295 6808 4681 5232 -184 154 446 C
ATOM 2850 CG PHE A 295 25.720 204.460 9.781 1.00 44.33 C
ANISOU 2850 CG PHE A 295 6775 4743 5326 -219 145 360 C
ATOM 2851 CD1 PHE A 295 26.908 203.845 10.164 1.00 46.88 C
ANISOU 2851 CD1 PHE A 295 7036 5124 5654 -287 179 333 C
ATOM 2852 CD2 PHE A 295 24.759 204.708 10.756 1.00 46.09 C
ANISOU 2852 CD2 PHE A 295 6990 4933 5590 -178 103 306 C
ATOM 2853 CE1 PHE A 295 27.148 203.524 11.503 1.00 47.26 C
ANISOU 2853 CE1 PHE A 295 7021 5193 5742 -314 163 256 C
ATOM 2854 CE2 PHE A 295 24.992 204.373 12.093 1.00 48.53 C
ANISOU 2854 CE2 PHE A 295 7240 5264 5934 -208 96 228 C
ATOM 2855 CZ PHE A 295 26.186 203.782 12.459 1.00 46.45 C
ANISOU 2855 CZ PHE A 295 6921 5057 5670 -275 123 205 C
ATOM 2856 N ARG A 296 25.636 206.012 5.396 1.00 43.59 N
ANISOU 2856 N ARG A 296 6936 4560 5066 -155 209 652 N
ATOM 2857 CA ARG A 296 25.753 205.816 3.954 1.00 43.46 C
ANISOU 2857 CA ARG A 296 6981 4578 4956 -130 230 730 C
ATOM 2858 C ARG A 296 26.893 206.646 3.367 1.00 49.06 C
ANISOU 2858 C ARG A 296 7739 5234 5667 -204 317 807 C
ATOM 2859 O ARG A 296 27.696 206.114 2.598 1.00 49.39 O
ANISOU 2859 O ARG A 296 7780 5339 5648 -232 373 840 O
ATOM 2860 CB ARG A 296 24.430 206.175 3.274 1.00 43.10 C
ANISOU 2860 CB ARG A 296 7006 4502 4869 -33 163 772 C
ATOM 2861 CG ARG A 296 24.371 205.832 1.780 1.00 52.08 C
ANISOU 2861 CG ARG A 296 8210 5689 5889 8 166 843 C
ATOM 2862 CD ARG A 296 23.202 206.496 1.077 1.00 58.36 C
ANISOU 2862 CD ARG A 296 9088 6435 6649 99 101 902 C
ATOM 2863 NE ARG A 296 21.916 206.187 1.703 1.00 63.87 N
ANISOU 2863 NE ARG A 296 9738 7147 7384 170 10 838 N
ATOM 2864 CZ ARG A 296 21.096 207.098 2.212 1.00 75.17 C
ANISOU 2864 CZ ARG A 296 11185 8493 8884 213 -31 840 C
ATOM 2865 NH1 ARG A 296 19.953 206.730 2.774 1.00 64.61 N
ANISOU 2865 NH1 ARG A 296 9791 7179 7581 277 -105 780 N
ATOM 2866 NH2 ARG A 296 21.408 208.385 2.157 1.00 61.64 N
ANISOU 2866 NH2 ARG A 296 9543 6666 7210 194 7 904 N
ATOM 2867 N GLN A 297 26.967 207.937 3.738 1.00 45.90 N
ANISOU 2867 N GLN A 297 7383 4716 5340 -237 332 836 N
ATOM 2868 CA GLN A 297 27.998 208.856 3.265 1.00 46.61 C
ANISOU 2868 CA GLN A 297 7522 4737 5451 -317 416 912 C
ATOM 2869 C GLN A 297 29.388 208.461 3.799 1.00 50.28 C
ANISOU 2869 C GLN A 297 7896 5247 5959 -422 481 871 C
ATOM 2870 O GLN A 297 30.361 208.521 3.046 1.00 50.44 O
ANISOU 2870 O GLN A 297 7927 5284 5954 -477 561 932 O
ATOM 2871 CB GLN A 297 27.651 210.304 3.638 1.00 48.72 C
ANISOU 2871 CB GLN A 297 7857 4856 5798 -325 408 940 C
ATOM 2872 CG GLN A 297 26.481 210.862 2.820 1.00 66.75 C
ANISOU 2872 CG GLN A 297 10244 7086 8033 -223 361 1011 C
ATOM 2873 CD GLN A 297 26.261 212.340 3.028 1.00 89.84 C
ANISOU 2873 CD GLN A 297 13249 9853 11033 -230 367 1055 C
ATOM 2874 OE1 GLN A 297 26.723 213.177 2.244 1.00 88.84 O
ANISOU 2874 OE1 GLN A 297 13209 9650 10898 -262 424 1154 O
ATOM 2875 NE2 GLN A 297 25.521 212.696 4.068 1.00 79.62 N
ANISOU 2875 NE2 GLN A 297 11934 8503 9814 -195 311 984 N
ATOM 2876 N THR A 298 29.474 208.015 5.068 1.00 46.35 N
ANISOU 2876 N THR A 298 7308 4779 5525 -445 447 772 N
ATOM 2877 CA THR A 298 30.743 207.593 5.664 1.00 46.30 C
ANISOU 2877 CA THR A 298 7207 4823 5563 -536 492 727 C
ATOM 2878 C THR A 298 31.215 206.297 4.997 1.00 52.34 C
ANISOU 2878 C THR A 298 7924 5715 6248 -519 522 730 C
ATOM 2879 O THR A 298 32.409 206.169 4.728 1.00 53.47 O
ANISOU 2879 O THR A 298 8024 5892 6400 -589 595 751 O
ATOM 2880 CB THR A 298 30.649 207.466 7.187 1.00 48.11 C
ANISOU 2880 CB THR A 298 7363 5050 5867 -555 440 624 C
ATOM 2881 OG1 THR A 298 29.938 208.584 7.710 1.00 46.29 O
ANISOU 2881 OG1 THR A 298 7193 4704 5693 -542 405 616 O
ATOM 2882 CG2 THR A 298 32.012 207.432 7.838 1.00 46.97 C
ANISOU 2882 CG2 THR A 298 7134 4928 5786 -660 481 588 C
ATOM 2883 N PHE A 299 30.282 205.369 4.682 1.00 48.32 N
ANISOU 2883 N PHE A 299 7422 5272 5665 -428 468 709 N
ATOM 2884 CA PHE A 299 30.606 204.126 3.982 1.00 48.11 C
ANISOU 2884 CA PHE A 299 7365 5357 5557 -402 491 707 C
ATOM 2885 C PHE A 299 31.211 204.453 2.610 1.00 54.80 C
ANISOU 2885 C PHE A 299 8279 6205 6339 -418 571 803 C
ATOM 2886 O PHE A 299 32.301 203.968 2.308 1.00 55.43 O
ANISOU 2886 O PHE A 299 8311 6345 6406 -464 644 810 O
ATOM 2887 CB PHE A 299 29.369 203.207 3.845 1.00 49.03 C
ANISOU 2887 CB PHE A 299 7491 5526 5611 -305 411 669 C
ATOM 2888 CG PHE A 299 28.839 202.555 5.109 1.00 49.48 C
ANISOU 2888 CG PHE A 299 7473 5609 5718 -286 346 575 C
ATOM 2889 CD1 PHE A 299 29.603 202.520 6.275 1.00 51.99 C
ANISOU 2889 CD1 PHE A 299 7712 5930 6112 -350 359 520 C
ATOM 2890 CD2 PHE A 299 27.587 201.951 5.126 1.00 51.02 C
ANISOU 2890 CD2 PHE A 299 7675 5830 5879 -206 272 542 C
ATOM 2891 CE1 PHE A 299 29.110 201.920 7.436 1.00 52.02 C
ANISOU 2891 CE1 PHE A 299 7657 5959 6151 -330 303 440 C
ATOM 2892 CE2 PHE A 299 27.093 201.350 6.289 1.00 52.57 C
ANISOU 2892 CE2 PHE A 299 7805 6049 6120 -192 222 462 C
ATOM 2893 CZ PHE A 299 27.858 201.338 7.435 1.00 50.42 C
ANISOU 2893 CZ PHE A 299 7465 5777 5914 -252 240 414 C
ATOM 2894 N ARG A 300 30.550 205.345 1.828 1.00 52.64 N
ANISOU 2894 N ARG A 300 8114 5860 6027 -383 564 879 N
ATOM 2895 CA ARG A 300 31.003 205.796 0.506 1.00 54.18 C
ANISOU 2895 CA ARG A 300 8393 6042 6149 -392 640 983 C
ATOM 2896 C ARG A 300 32.410 206.393 0.556 1.00 59.32 C
ANISOU 2896 C ARG A 300 9012 6664 6863 -503 746 1021 C
ATOM 2897 O ARG A 300 33.238 206.036 -0.283 1.00 59.57 O
ANISOU 2897 O ARG A 300 9042 6753 6838 -526 830 1065 O
ATOM 2898 CB ARG A 300 30.032 206.818 -0.100 1.00 55.87 C
ANISOU 2898 CB ARG A 300 8728 6165 6333 -338 603 1059 C
ATOM 2899 CG ARG A 300 28.766 206.188 -0.669 1.00 68.41 C
ANISOU 2899 CG ARG A 300 10362 7802 7827 -225 516 1051 C
ATOM 2900 CD ARG A 300 28.210 206.981 -1.838 1.00 81.57 C
ANISOU 2900 CD ARG A 300 12162 9417 9414 -171 511 1158 C
ATOM 2901 NE ARG A 300 27.727 208.301 -1.426 1.00 92.63 N
ANISOU 2901 NE ARG A 300 13614 10687 10893 -171 487 1196 N
ATOM 2902 CZ ARG A 300 26.468 208.572 -1.103 1.00106.30 C
ANISOU 2902 CZ ARG A 300 15366 12378 12645 -92 389 1175 C
ATOM 2903 NH1 ARG A 300 25.542 207.621 -1.152 1.00 88.73 N
ANISOU 2903 NH1 ARG A 300 13110 10234 10369 -13 304 1119 N
ATOM 2904 NH2 ARG A 300 26.121 209.799 -0.736 1.00 95.84 N
ANISOU 2904 NH2 ARG A 300 14091 10929 11396 -91 377 1209 N
ATOM 2905 N LYS A 301 32.686 207.260 1.557 1.00 55.87 N
ANISOU 2905 N LYS A 301 8542 6142 6544 -572 741 998 N
ATOM 2906 CA LYS A 301 33.987 207.901 1.761 1.00 56.57 C
ANISOU 2906 CA LYS A 301 8587 6192 6713 -690 829 1023 C
ATOM 2907 C LYS A 301 35.096 206.869 2.034 1.00 60.08 C
ANISOU 2907 C LYS A 301 8907 6749 7171 -735 874 971 C
ATOM 2908 O LYS A 301 36.180 207.002 1.466 1.00 60.20 O
ANISOU 2908 O LYS A 301 8901 6783 7191 -801 974 1023 O
ATOM 2909 CB LYS A 301 33.919 208.923 2.907 1.00 59.39 C
ANISOU 2909 CB LYS A 301 8934 6438 7194 -747 792 985 C
ATOM 2910 CG LYS A 301 35.008 209.985 2.830 1.00 80.27 C
ANISOU 2910 CG LYS A 301 11580 9000 9919 -865 879 1041 C
ATOM 2911 CD LYS A 301 35.039 210.878 4.059 1.00 93.85 C
ANISOU 2911 CD LYS A 301 13279 10616 11763 -929 838 983 C
ATOM 2912 CE LYS A 301 36.108 211.938 3.931 1.00109.22 C
ANISOU 2912 CE LYS A 301 15229 12475 13796 -1055 923 1038 C
ATOM 2913 NZ LYS A 301 36.136 212.846 5.106 1.00119.12 N
ANISOU 2913 NZ LYS A 301 16472 13620 15170 -1120 879 975 N
ATOM 2914 N ILE A 302 34.827 205.850 2.888 1.00 55.94 N
ANISOU 2914 N ILE A 302 8301 6297 6654 -698 805 873 N
ATOM 2915 CA ILE A 302 35.798 204.801 3.226 1.00 55.94 C
ANISOU 2915 CA ILE A 302 8183 6403 6669 -726 835 819 C
ATOM 2916 C ILE A 302 36.145 203.987 1.963 1.00 62.94 C
ANISOU 2916 C ILE A 302 9087 7377 7450 -687 905 865 C
ATOM 2917 O ILE A 302 37.324 203.880 1.628 1.00 63.78 O
ANISOU 2917 O ILE A 302 9137 7524 7572 -745 997 890 O
ATOM 2918 CB ILE A 302 35.315 203.880 4.397 1.00 57.30 C
ANISOU 2918 CB ILE A 302 8281 6625 6863 -684 742 713 C
ATOM 2919 CG1 ILE A 302 35.153 204.673 5.712 1.00 56.78 C
ANISOU 2919 CG1 ILE A 302 8192 6482 6900 -731 685 661 C
ATOM 2920 CG2 ILE A 302 36.263 202.674 4.606 1.00 57.69 C
ANISOU 2920 CG2 ILE A 302 8218 6787 6914 -694 771 666 C
ATOM 2921 CD1 ILE A 302 34.207 204.047 6.736 1.00 54.80 C
ANISOU 2921 CD1 ILE A 302 7917 6253 6651 -669 586 575 C
ATOM 2922 N ILE A 303 35.124 203.445 1.265 1.00 60.46 N
ANISOU 2922 N ILE A 303 8851 7090 7030 -589 862 872 N
ATOM 2923 CA ILE A 303 35.268 202.610 0.065 1.00 61.21 C
ANISOU 2923 CA ILE A 303 8980 7268 7009 -538 913 903 C
ATOM 2924 C ILE A 303 35.997 203.367 -1.069 1.00 67.74 C
ANISOU 2924 C ILE A 303 9870 8072 7796 -582 1028 1009 C
ATOM 2925 O ILE A 303 36.941 202.811 -1.627 1.00 68.35 O
ANISOU 2925 O ILE A 303 9907 8221 7840 -599 1118 1023 O
ATOM 2926 CB ILE A 303 33.892 202.043 -0.399 1.00 63.70 C
ANISOU 2926 CB ILE A 303 9374 7602 7225 -430 825 886 C
ATOM 2927 CG1 ILE A 303 33.287 201.118 0.683 1.00 62.59 C
ANISOU 2927 CG1 ILE A 303 9160 7499 7124 -393 729 782 C
ATOM 2928 CG2 ILE A 303 34.007 201.305 -1.747 1.00 64.52 C
ANISOU 2928 CG2 ILE A 303 9535 7783 7196 -378 875 920 C
ATOM 2929 CD1 ILE A 303 31.776 201.185 0.825 1.00 70.46 C
ANISOU 2929 CD1 ILE A 303 10214 8461 8097 -320 622 762 C
ATOM 2930 N ARG A 304 35.579 204.610 -1.391 1.00 65.89 N
ANISOU 2930 N ARG A 304 9734 7736 7567 -597 1030 1086 N
ATOM 2931 CA ARG A 304 36.183 205.429 -2.454 1.00 67.94 C
ANISOU 2931 CA ARG A 304 10068 7958 7788 -640 1140 1200 C
ATOM 2932 C ARG A 304 37.685 205.662 -2.230 1.00 75.43 C
ANISOU 2932 C ARG A 304 10918 8918 8826 -753 1252 1213 C
ATOM 2933 O ARG A 304 38.477 205.387 -3.134 1.00 76.34 O
ANISOU 2933 O ARG A 304 11034 9090 8881 -767 1361 1264 O
ATOM 2934 CB ARG A 304 35.467 206.781 -2.592 1.00 67.47 C
ANISOU 2934 CB ARG A 304 10121 7768 7745 -642 1111 1273 C
ATOM 2935 CG ARG A 304 34.248 206.732 -3.495 1.00 75.23 C
ANISOU 2935 CG ARG A 304 11234 8750 8601 -532 1050 1316 C
ATOM 2936 CD ARG A 304 33.750 208.117 -3.882 1.00 89.46 C
ANISOU 2936 CD ARG A 304 13158 10424 10408 -532 1048 1415 C
ATOM 2937 NE ARG A 304 34.774 208.934 -4.547 1.00103.20 N
ANISOU 2937 NE ARG A 304 14939 12118 12156 -616 1180 1520 N
ATOM 2938 CZ ARG A 304 35.039 208.913 -5.851 1.00119.27 C
ANISOU 2938 CZ ARG A 304 17062 14187 14069 -595 1262 1614 C
ATOM 2939 NH1 ARG A 304 35.986 209.694 -6.354 1.00108.40 N
ANISOU 2939 NH1 ARG A 304 15714 12762 12712 -681 1390 1710 N
ATOM 2940 NH2 ARG A 304 34.362 208.108 -6.662 1.00106.05 N
ANISOU 2940 NH2 ARG A 304 15449 12596 12249 -492 1219 1611 N
ATOM 2941 N SER A 305 38.071 206.137 -1.029 1.00 73.46 N
ANISOU 2941 N SER A 305 10580 8617 8714 -830 1225 1163 N
ATOM 2942 CA SER A 305 39.460 206.406 -0.656 1.00 74.97 C
ANISOU 2942 CA SER A 305 10661 8815 9010 -945 1311 1165 C
ATOM 2943 C SER A 305 40.259 205.100 -0.513 1.00 80.20 C
ANISOU 2943 C SER A 305 11197 9609 9665 -934 1341 1101 C
ATOM 2944 O SER A 305 41.217 204.897 -1.262 1.00 81.33 O
ANISOU 2944 O SER A 305 11308 9807 9785 -965 1457 1147 O
ATOM 2945 CB SER A 305 39.515 207.216 0.636 1.00 79.28 C
ANISOU 2945 CB SER A 305 11156 9272 9696 -1021 1251 1115 C
ATOM 2946 OG SER A 305 40.842 207.610 0.939 1.00 92.20 O
ANISOU 2946 OG SER A 305 12690 10905 11439 -1141 1329 1122 O
ATOM 2947 N HIS A 306 39.845 204.208 0.418 1.00 75.91 N
ANISOU 2947 N HIS A 306 10588 9116 9139 -885 1241 998 N
ATOM 2948 CA HIS A 306 40.498 202.919 0.682 1.00109.61 C
ANISOU 2948 CA HIS A 306 14741 13502 13407 -862 1252 931 C
ATOM 2949 C HIS A 306 39.922 201.834 -0.227 1.00125.78 C
ANISOU 2949 C HIS A 306 16850 15624 15316 -752 1251 928 C
ATOM 2950 O HIS A 306 40.574 200.823 -0.481 1.00 83.84 O
ANISOU 2950 O HIS A 306 11472 10407 9978 -728 1300 901 O
ATOM 2951 CB HIS A 306 40.346 202.511 2.163 1.00109.33 C
ANISOU 2951 CB HIS A 306 14610 13474 13454 -865 1146 828 C
ATOM 2952 CG HIS A 306 40.584 203.627 3.136 1.00113.14 C
ANISOU 2952 CG HIS A 306 15061 13868 14057 -958 1115 817 C
ATOM 2953 ND1 HIS A 306 41.862 203.984 3.529 1.00115.79 N
ANISOU 2953 ND1 HIS A 306 15286 14212 14496 -1062 1171 816 N
ATOM 2954 CD2 HIS A 306 39.694 204.434 3.759 1.00114.58 C
ANISOU 2954 CD2 HIS A 306 15309 13955 14272 -960 1035 803 C
ATOM 2955 CE1 HIS A 306 41.710 204.992 4.372 1.00115.36 C
ANISOU 2955 CE1 HIS A 306 15239 14063 14529 -1127 1119 797 C
ATOM 2956 NE2 HIS A 306 40.424 205.298 4.542 1.00115.00 N
ANISOU 2956 NE2 HIS A 306 15300 13950 14443 -1066 1040 789 N
TER 2957 HIS A 306
HETATM 2958 C1 ZMA A1201 19.743 167.920 15.739 1.00 51.47 C
HETATM 2959 C2 ZMA A1201 19.419 166.567 15.864 1.00 52.86 C
HETATM 2960 C3 ZMA A1201 20.252 165.599 15.283 1.00 55.44 C
HETATM 2961 O4 ZMA A1201 19.937 164.276 15.398 1.00 57.85 O
HETATM 2962 C5 ZMA A1201 21.410 165.974 14.586 1.00 54.23 C
HETATM 2963 C6 ZMA A1201 21.733 167.327 14.454 1.00 52.34 C
HETATM 2964 C7 ZMA A1201 20.899 168.294 15.036 1.00 50.32 C
HETATM 2965 C8 ZMA A1201 21.257 169.754 14.901 1.00 45.50 C
HETATM 2966 C9 ZMA A1201 22.139 170.178 16.070 1.00 40.92 C
HETATM 2967 N10 ZMA A1201 22.336 171.610 16.095 1.00 37.51 N
HETATM 2968 C11 ZMA A1201 21.506 172.438 16.774 1.00 34.44 C
HETATM 2969 N12 ZMA A1201 21.882 173.736 16.950 1.00 33.42 N
HETATM 2970 N13 ZMA A1201 20.316 171.992 17.278 1.00 31.88 N
HETATM 2971 C14 ZMA A1201 19.487 172.822 17.957 1.00 31.42 C
HETATM 2972 N15 ZMA A1201 18.316 172.343 18.440 1.00 29.37 N
HETATM 2973 N16 ZMA A1201 19.864 174.105 18.127 1.00 33.93 N
HETATM 2974 N17 ZMA A1201 19.145 175.096 18.795 1.00 34.64 N
HETATM 2975 C18 ZMA A1201 21.030 174.537 17.633 1.00 33.77 C
HETATM 2976 N19 ZMA A1201 21.164 175.849 17.941 1.00 33.96 N
HETATM 2977 C20 ZMA A1201 20.020 176.115 18.624 1.00 34.66 C
HETATM 2978 C21 ZMA A1201 19.731 177.459 19.166 1.00 35.57 C
HETATM 2979 C22 ZMA A1201 20.685 178.436 19.312 1.00 37.05 C
HETATM 2980 C23 ZMA A1201 19.949 179.509 19.788 1.00 38.36 C
HETATM 2981 C24 ZMA A1201 18.605 179.154 19.872 1.00 37.79 C
HETATM 2982 O25 ZMA A1201 18.460 177.843 19.453 1.00 37.29 O
HETATM 2983 C1 CLR A1202 8.254 170.158 13.364 1.00 58.93 C
HETATM 2984 C2 CLR A1202 8.167 168.641 13.573 1.00 58.79 C
HETATM 2985 C3 CLR A1202 6.779 168.071 13.267 1.00 58.68 C
HETATM 2986 C4 CLR A1202 6.288 168.481 11.873 1.00 58.14 C
HETATM 2987 C5 CLR A1202 6.461 169.973 11.626 1.00 58.67 C
HETATM 2988 C6 CLR A1202 5.419 170.624 11.056 1.00 59.13 C
HETATM 2989 C7 CLR A1202 5.337 172.132 10.873 1.00 59.74 C
HETATM 2990 C8 CLR A1202 6.710 172.821 10.961 1.00 60.51 C
HETATM 2991 C9 CLR A1202 7.555 172.206 12.107 1.00 59.48 C
HETATM 2992 C10 CLR A1202 7.778 170.678 11.987 1.00 59.38 C
HETATM 2993 C11 CLR A1202 8.884 172.978 12.325 1.00 59.50 C
HETATM 2994 C12 CLR A1202 8.759 174.509 12.375 1.00 60.03 C
HETATM 2995 C13 CLR A1202 7.970 175.089 11.193 1.00 61.53 C
HETATM 2996 C14 CLR A1202 6.628 174.341 11.205 1.00 61.34 C
HETATM 2997 C15 CLR A1202 5.707 175.185 10.325 1.00 61.72 C
HETATM 2998 C16 CLR A1202 6.118 176.610 10.701 1.00 62.88 C
HETATM 2999 C17 CLR A1202 7.485 176.542 11.412 1.00 62.82 C
HETATM 3000 C18 CLR A1202 8.785 174.924 9.883 1.00 61.96 C
HETATM 3001 C19 CLR A1202 8.802 170.334 10.888 1.00 59.72 C
HETATM 3002 C20 CLR A1202 8.471 177.695 11.086 1.00 64.69 C
HETATM 3003 C21 CLR A1202 9.544 177.801 12.167 1.00 65.37 C
HETATM 3004 C22 CLR A1202 7.797 179.048 10.786 1.00 66.72 C
HETATM 3005 C23 CLR A1202 7.724 180.077 11.918 1.00 69.05 C
HETATM 3006 C24 CLR A1202 7.573 181.496 11.372 1.00 71.38 C
HETATM 3007 C25 CLR A1202 8.804 182.356 11.648 1.00 72.67 C
HETATM 3008 C26 CLR A1202 9.536 182.675 10.352 1.00 74.24 C
HETATM 3009 C27 CLR A1202 8.434 183.649 12.362 1.00 71.66 C
HETATM 3010 O1 CLR A1202 6.836 166.643 13.345 1.00 58.66 O
HETATM 3011 C1 CLR A1203 3.080 172.854 21.272 1.00 52.54 C
HETATM 3012 C2 CLR A1203 2.788 171.350 21.260 1.00 51.53 C
HETATM 3013 C3 CLR A1203 1.829 170.953 20.140 1.00 52.40 C
HETATM 3014 C4 CLR A1203 2.297 171.462 18.767 1.00 53.01 C
HETATM 3015 C5 CLR A1203 2.712 172.927 18.803 1.00 52.61 C
HETATM 3016 C6 CLR A1203 2.279 173.718 17.792 1.00 52.56 C
HETATM 3017 C7 CLR A1203 2.332 175.239 17.824 1.00 52.01 C
HETATM 3018 C8 CLR A1203 3.497 175.730 18.692 1.00 52.87 C
HETATM 3019 C9 CLR A1203 3.471 174.999 20.059 1.00 53.58 C
HETATM 3020 C10 CLR A1203 3.595 173.457 19.943 1.00 53.03 C
HETATM 3021 C11 CLR A1203 4.492 175.585 21.072 1.00 54.36 C
HETATM 3022 C12 CLR A1203 4.599 177.121 21.104 1.00 54.89 C
HETATM 3023 C13 CLR A1203 4.731 177.773 19.717 1.00 55.04 C
HETATM 3024 C14 CLR A1203 3.523 177.252 18.920 1.00 54.43 C
HETATM 3025 C15 CLR A1203 3.422 178.186 17.711 1.00 54.53 C
HETATM 3026 C16 CLR A1203 3.889 179.532 18.270 1.00 54.51 C
HETATM 3027 C17 CLR A1203 4.415 179.292 19.700 1.00 55.63 C
HETATM 3028 C18 CLR A1203 6.105 177.426 19.081 1.00 54.62 C
HETATM 3029 C19 CLR A1203 5.043 173.012 19.658 1.00 52.38 C
HETATM 3030 C20 CLR A1203 5.479 180.332 20.143 1.00 57.81 C
HETATM 3031 C21 CLR A1203 6.175 180.081 21.482 1.00 57.44 C
HETATM 3032 C22 CLR A1203 4.849 181.714 20.273 1.00 60.99 C
HETATM 3033 C23 CLR A1203 5.560 182.720 19.381 1.00 63.64 C
HETATM 3034 C24 CLR A1203 4.868 184.074 19.460 1.00 65.44 C
HETATM 3035 C25 CLR A1203 5.879 185.190 19.679 1.00 66.75 C
HETATM 3036 C26 CLR A1203 6.330 185.801 18.353 1.00 66.67 C
HETATM 3037 C27 CLR A1203 5.296 186.243 20.617 1.00 67.61 C
HETATM 3038 O1 CLR A1203 1.729 169.525 20.128 1.00 52.64 O
HETATM 3039 C1 CLR A1204 38.546 170.559 22.146 1.00 56.94 C
HETATM 3040 C2 CLR A1204 38.296 169.078 22.476 1.00 56.65 C
HETATM 3041 C3 CLR A1204 38.631 168.753 23.935 1.00 57.14 C
HETATM 3042 C4 CLR A1204 37.829 169.644 24.881 1.00 57.11 C
HETATM 3043 C5 CLR A1204 37.965 171.115 24.510 1.00 57.37 C
HETATM 3044 C6 CLR A1204 38.174 171.969 25.541 1.00 57.90 C
HETATM 3045 C7 CLR A1204 38.588 173.419 25.379 1.00 58.71 C
HETATM 3046 C8 CLR A1204 38.168 173.995 24.017 1.00 58.63 C
HETATM 3047 C9 CLR A1204 38.509 172.987 22.887 1.00 57.62 C
HETATM 3048 C10 CLR A1204 37.836 171.590 23.050 1.00 57.18 C
HETATM 3049 C11 CLR A1204 38.279 173.629 21.493 1.00 57.49 C
HETATM 3050 C12 CLR A1204 38.878 175.040 21.305 1.00 57.97 C
HETATM 3051 C13 CLR A1204 38.468 176.042 22.404 1.00 58.98 C
HETATM 3052 C14 CLR A1204 38.851 175.347 23.724 1.00 59.25 C
HETATM 3053 C15 CLR A1204 38.770 176.448 24.781 1.00 59.08 C
HETATM 3054 C16 CLR A1204 39.273 177.673 24.014 1.00 59.73 C
HETATM 3055 C17 CLR A1204 39.374 177.302 22.521 1.00 59.52 C
HETATM 3056 C18 CLR A1204 36.961 176.386 22.282 1.00 57.95 C
HETATM 3057 C19 CLR A1204 36.341 171.620 22.679 1.00 56.29 C
HETATM 3058 C20 CLR A1204 39.176 178.530 21.591 1.00 61.13 C
HETATM 3059 C21 CLR A1204 39.215 178.248 20.086 1.00 61.91 C
HETATM 3060 C22 CLR A1204 40.254 179.588 21.849 1.00 62.99 C
HETATM 3061 C23 CLR A1204 39.672 180.970 22.118 1.00 64.57 C
HETATM 3062 C24 CLR A1204 39.945 181.928 20.954 1.00 65.89 C
HETATM 3063 C25 CLR A1204 40.232 183.385 21.350 1.00 68.09 C
HETATM 3064 C26 CLR A1204 39.152 184.073 22.186 1.00 68.29 C
HETATM 3065 C27 CLR A1204 41.628 183.616 21.923 1.00 69.32 C
HETATM 3066 O1 CLR A1204 38.321 167.387 24.223 1.00 57.70 O
HETATM 3067 C1 OLB A1205 7.014 176.952 33.321 1.00 86.80 C
HETATM 3068 C2 OLB A1205 7.484 178.379 33.473 1.00 84.96 C
HETATM 3069 C3 OLB A1205 7.849 178.945 32.106 1.00 83.34 C
HETATM 3070 C4 OLB A1205 7.760 180.465 32.100 1.00 82.29 C
HETATM 3071 C5 OLB A1205 8.836 181.073 31.208 1.00 81.06 C
HETATM 3072 O19 OLB A1205 5.834 176.717 33.102 1.00 87.94 O
HETATM 3073 O20 OLB A1205 7.900 175.929 33.410 1.00 87.02 O
HETATM 3074 C21 OLB A1205 7.747 174.886 34.374 1.00 86.85 C
HETATM 3075 C22 OLB A1205 7.272 173.619 33.676 1.00 87.23 C
HETATM 3076 O23 OLB A1205 8.126 172.524 34.024 1.00 86.90 O
HETATM 3077 C24 OLB A1205 5.845 173.314 34.115 1.00 88.47 C
HETATM 3078 O25 OLB A1205 5.386 172.125 33.460 1.00 89.22 O
HETATM 3079 C6 OLB A1205 9.604 182.166 31.939 1.00 80.57 C
HETATM 3080 C7 OLB A1205 9.271 183.547 31.387 1.00 80.67 C
HETATM 3081 C8 OLB A1205 9.259 184.598 32.494 1.00 80.52 C
HETATM 3082 C1 OLA A1206 36.850 165.035 13.483 1.00 76.79 C
HETATM 3083 O1 OLA A1206 37.689 164.142 13.222 1.00 77.35 O
HETATM 3084 O2 OLA A1206 35.633 164.750 13.394 1.00 77.38 O
HETATM 3085 C2 OLA A1206 37.309 166.415 13.912 1.00 74.80 C
HETATM 3086 C3 OLA A1206 36.726 167.517 13.030 1.00 72.29 C
HETATM 3087 C4 OLA A1206 37.270 168.880 13.441 1.00 70.47 C
HETATM 3088 C5 OLA A1206 36.437 170.004 12.837 1.00 69.47 C
HETATM 3089 C6 OLA A1206 37.303 171.192 12.427 1.00 68.80 C
HETATM 3090 C7 OLA A1206 36.461 172.461 12.374 1.00 68.33 C
HETATM 3091 C8 OLA A1206 37.249 173.689 11.936 1.00 67.98 C
HETATM 3092 C9 OLA A1206 36.407 174.429 10.918 1.00 69.11 C
HETATM 3093 C10 OLA A1206 36.583 175.694 10.515 1.00 69.96 C
HETATM 3094 C11 OLA A1206 37.674 176.618 11.009 1.00 70.56 C
HETATM 3095 C12 OLA A1206 38.245 177.385 9.822 1.00 70.78 C
HETATM 3096 C13 OLA A1206 38.600 178.818 10.203 1.00 70.83 C
HETATM 3097 C14 OLA A1206 40.110 178.995 10.322 1.00 71.30 C
HETATM 3098 C1 OLA A1207 41.888 167.023 13.707 1.00 72.13 C
HETATM 3099 O1 OLA A1207 42.756 166.147 13.917 1.00 72.31 O
HETATM 3100 O2 OLA A1207 40.688 166.736 13.925 1.00 73.97 O
HETATM 3101 C2 OLA A1207 42.291 168.384 13.180 1.00 69.28 C
HETATM 3102 C3 OLA A1207 41.567 169.512 13.908 1.00 67.31 C
HETATM 3103 C4 OLA A1207 42.086 170.866 13.444 1.00 66.56 C
HETATM 3104 C5 OLA A1207 40.960 171.888 13.370 1.00 66.85 C
HETATM 3105 C6 OLA A1207 41.375 173.181 14.058 1.00 67.72 C
HETATM 3106 C7 OLA A1207 41.378 174.358 13.089 1.00 67.83 C
HETATM 3107 C8 OLA A1207 42.197 175.523 13.635 1.00 67.52 C
HETATM 3108 C9 OLA A1207 42.311 176.566 12.546 1.00 68.37 C
HETATM 3109 C10 OLA A1207 43.003 177.709 12.619 1.00 68.97 C
HETATM 3110 C11 OLA A1207 43.807 178.181 13.810 1.00 69.08 C
HETATM 3111 C12 OLA A1207 43.292 179.556 14.219 1.00 69.93 C
HETATM 3112 C13 OLA A1207 44.170 180.683 13.690 1.00 71.03 C
HETATM 3113 C14 OLA A1207 43.897 181.985 14.437 1.00 71.49 C
HETATM 3114 C1 OLA A1208 16.281 164.953 1.857 1.00 95.79 C
HETATM 3115 O1 OLA A1208 15.326 164.241 1.475 1.00 95.85 O
HETATM 3116 O2 OLA A1208 16.836 164.679 2.943 1.00 96.93 O
HETATM 3117 C2 OLA A1208 16.762 166.117 1.020 1.00 94.40 C
HETATM 3118 C3 OLA A1208 15.878 167.339 1.254 1.00 93.41 C
HETATM 3119 C4 OLA A1208 16.721 168.606 1.310 1.00 92.48 C
HETATM 3120 C5 OLA A1208 15.899 169.850 0.997 1.00 91.77 C
HETATM 3121 C6 OLA A1208 16.771 170.905 0.323 1.00 90.94 C
HETATM 3122 C7 OLA A1208 16.949 172.137 1.204 1.00 90.07 C
HETATM 3123 C8 OLA A1208 16.380 173.378 0.526 1.00 89.43 C
HETATM 3124 C9 OLA A1208 17.356 174.529 0.659 1.00 88.94 C
HETATM 3125 C10 OLA A1208 17.010 175.823 0.728 1.00 88.94 C
HETATM 3126 C11 OLA A1208 15.591 176.356 0.691 1.00 88.71 C
HETATM 3127 C12 OLA A1208 15.616 177.880 0.651 1.00 88.09 C
HETATM 3128 C1 OLA A1209 25.441 167.553 8.155 1.00 79.56 C
HETATM 3129 O1 OLA A1209 26.296 168.434 8.408 1.00 80.70 O
HETATM 3130 O2 OLA A1209 25.304 166.599 8.955 1.00 79.30 O
HETATM 3131 C2 OLA A1209 24.594 167.621 6.902 1.00 78.12 C
HETATM 3132 C3 OLA A1209 23.869 168.960 6.804 1.00 76.73 C
HETATM 3133 C4 OLA A1209 23.185 169.106 5.453 1.00 76.11 C
HETATM 3134 C5 OLA A1209 22.146 170.219 5.471 1.00 76.16 C
HETATM 3135 C6 OLA A1209 22.088 170.921 4.119 1.00 76.07 C
HETATM 3136 C7 OLA A1209 21.450 172.299 4.246 1.00 75.63 C
HETATM 3137 C8 OLA A1209 22.301 173.347 3.538 1.00 75.71 C
HETATM 3138 C9 OLA A1209 22.254 174.652 4.306 1.00 74.82 C
HETATM 3139 C10 OLA A1209 21.921 175.837 3.777 1.00 74.14 C
HETATM 3140 C11 OLA A1209 21.524 176.067 2.331 1.00 73.76 C
HETATM 3141 C12 OLA A1209 21.771 177.523 1.944 1.00 73.30 C
HETATM 3142 C13 OLA A1209 20.523 178.384 2.137 1.00 72.39 C
HETATM 3143 C14 OLA A1209 20.705 179.802 1.590 1.00 71.64 C
HETATM 3144 C15 OLA A1209 21.169 180.807 2.648 1.00 71.07 C
HETATM 3145 C16 OLA A1209 20.014 181.437 3.426 1.00 70.28 C
HETATM 3146 C1 OLA A1210 35.996 167.772 4.063 1.00 90.22 C
HETATM 3147 O1 OLA A1210 36.423 167.730 2.883 1.00 90.93 O
HETATM 3148 O2 OLA A1210 36.320 166.848 4.845 1.00 89.65 O
HETATM 3149 C2 OLA A1210 35.120 168.906 4.567 1.00 89.21 C
HETATM 3150 C3 OLA A1210 34.376 169.637 3.449 1.00 87.92 C
HETATM 3151 C4 OLA A1210 35.096 170.931 3.084 1.00 86.24 C
HETATM 3152 C5 OLA A1210 34.284 171.767 2.101 1.00 84.44 C
HETATM 3153 C6 OLA A1210 34.433 173.254 2.401 1.00 82.70 C
HETATM 3154 C7 OLA A1210 35.267 173.951 1.334 1.00 81.44 C
HETATM 3155 C8 OLA A1210 35.384 175.440 1.633 1.00 81.21 C
HETATM 3156 C9 OLA A1210 36.248 176.102 0.586 1.00 81.05 C
HETATM 3157 C1 OLA A1211 20.682 203.842 28.309 1.00 72.75 C
HETATM 3158 O1 OLA A1211 20.121 204.096 27.219 1.00 73.17 O
HETATM 3159 O2 OLA A1211 21.766 204.411 28.585 1.00 73.19 O
HETATM 3160 C2 OLA A1211 20.048 202.868 29.278 1.00 70.55 C
HETATM 3161 C3 OLA A1211 20.408 201.443 28.875 1.00 68.38 C
HETATM 3162 C4 OLA A1211 19.956 200.428 29.917 1.00 66.50 C
HETATM 3163 C5 OLA A1211 19.506 199.137 29.242 1.00 65.91 C
HETATM 3164 C6 OLA A1211 20.239 197.924 29.803 1.00 65.72 C
HETATM 3165 C7 OLA A1211 19.792 196.645 29.104 1.00 65.30 C
HETATM 3166 C1 OLA A1212 20.798 195.313 -3.063 1.00 79.90 C
HETATM 3167 O1 OLA A1212 21.783 195.403 -3.827 1.00 79.28 O
HETATM 3168 O2 OLA A1212 19.651 195.480 -3.541 1.00 80.64 O
HETATM 3169 C2 OLA A1212 20.998 195.026 -1.590 1.00 79.06 C
HETATM 3170 C3 OLA A1212 20.488 193.632 -1.237 1.00 77.83 C
HETATM 3171 C4 OLA A1212 21.603 192.754 -0.683 1.00 76.99 C
HETATM 3172 C5 OLA A1212 21.411 192.509 0.809 1.00 76.45 C
HETATM 3173 C6 OLA A1212 21.368 191.018 1.130 1.00 75.75 C
HETATM 3174 C7 OLA A1212 21.210 190.776 2.630 1.00 74.46 C
HETATM 3175 C8 OLA A1212 22.180 189.708 3.129 1.00 73.63 C
HETATM 3176 C9 OLA A1212 21.499 188.352 3.157 1.00 72.54 C
HETATM 3177 C10 OLA A1212 22.129 187.167 3.127 1.00 71.41 C
HETATM 3178 C11 OLA A1212 23.631 186.974 3.064 1.00 70.39 C
HETATM 3179 C12 OLA A1212 23.948 185.566 2.573 1.00 69.44 C
HETATM 3180 C10 OLC A1213 39.324 177.806 14.972 1.00 63.80 C
HETATM 3181 C9 OLC A1213 38.573 176.698 15.042 1.00 64.24 C
HETATM 3182 C11 OLC A1213 39.271 178.953 15.957 1.00 63.46 C
HETATM 3183 C8 OLC A1213 37.545 176.414 16.116 1.00 65.01 C
HETATM 3184 C24 OLC A1213 39.751 164.071 15.853 1.00 82.46 C
HETATM 3185 C12 OLC A1213 39.734 180.236 15.279 1.00 63.33 C
HETATM 3186 C7 OLC A1213 38.115 175.408 17.108 1.00 66.72 C
HETATM 3187 C6 OLC A1213 37.433 174.057 16.947 1.00 68.23 C
HETATM 3188 C5 OLC A1213 38.122 172.976 17.769 1.00 69.81 C
HETATM 3189 C4 OLC A1213 38.377 171.737 16.918 1.00 71.30 C
HETATM 3190 C3 OLC A1213 38.564 170.504 17.792 1.00 72.34 C
HETATM 3191 C2 OLC A1213 38.858 169.269 16.942 1.00 73.68 C
HETATM 3192 C21 OLC A1213 39.593 165.648 17.799 1.00 78.07 C
HETATM 3193 C1 OLC A1213 39.354 168.096 17.766 1.00 75.04 C
HETATM 3194 C22 OLC A1213 38.841 164.634 16.944 1.00 80.79 C
HETATM 3195 O19 OLC A1213 39.532 168.199 18.973 1.00 74.74 O
HETATM 3196 O25 OLC A1213 40.683 163.118 16.386 1.00 83.65 O
HETATM 3197 O23 OLC A1213 38.311 163.585 17.767 1.00 81.77 O
HETATM 3198 O20 OLC A1213 39.616 166.919 17.138 1.00 76.71 O
HETATM 3199 C9 OLC A1214 6.065 183.743 29.508 1.00124.36 C
HETATM 3200 C8 OLC A1214 5.932 182.315 29.039 1.00124.31 C
HETATM 3201 C24 OLC A1214 2.601 170.378 29.784 1.00127.24 C
HETATM 3202 C7 OLC A1214 4.507 181.824 29.270 1.00124.31 C
HETATM 3203 C6 OLC A1214 4.492 180.556 30.117 1.00124.37 C
HETATM 3204 C5 OLC A1214 4.070 179.348 29.289 1.00124.57 C
HETATM 3205 C4 OLC A1214 4.390 178.046 30.014 1.00125.00 C
HETATM 3206 C3 OLC A1214 3.583 176.891 29.432 1.00125.60 C
HETATM 3207 C2 OLC A1214 3.079 175.969 30.538 1.00126.13 C
HETATM 3208 C21 OLC A1214 2.567 172.573 30.987 1.00126.91 C
HETATM 3209 C1 OLC A1214 3.750 174.616 30.441 1.00126.53 C
HETATM 3210 C22 OLC A1214 3.287 171.232 30.843 1.00126.94 C
HETATM 3211 O19 OLC A1214 4.931 174.494 30.728 1.00126.84 O
HETATM 3212 O25 OLC A1214 3.245 169.100 29.709 1.00127.44 O
HETATM 3213 O23 OLC A1214 4.666 171.413 30.498 1.00126.70 O
HETATM 3214 O20 OLC A1214 3.049 173.530 30.038 1.00126.68 O
HETATM 3215 C10 OLC A1215 44.137 184.458 24.517 1.00 77.62 C
HETATM 3216 C9 OLC A1215 44.363 183.261 25.050 1.00 77.13 C
HETATM 3217 C8 OLC A1215 44.153 182.008 24.232 1.00 75.90 C
HETATM 3218 C24 OLC A1215 42.332 168.720 26.238 1.00 79.80 C
HETATM 3219 C7 OLC A1215 43.545 180.920 25.112 1.00 75.06 C
HETATM 3220 C6 OLC A1215 43.587 179.563 24.417 1.00 73.92 C
HETATM 3221 C5 OLC A1215 43.258 178.427 25.378 1.00 73.20 C
HETATM 3222 C4 OLC A1215 42.992 177.143 24.600 1.00 73.19 C
HETATM 3223 C3 OLC A1215 43.166 175.902 25.467 1.00 73.70 C
HETATM 3224 C2 OLC A1215 42.684 174.657 24.722 1.00 74.42 C
HETATM 3225 C21 OLC A1215 42.645 171.195 26.062 1.00 77.87 C
HETATM 3226 C1 OLC A1215 42.183 173.564 25.648 1.00 75.76 C
HETATM 3227 C22 OLC A1215 41.652 170.046 25.927 1.00 79.83 C
HETATM 3228 O19 OLC A1215 41.697 173.822 26.742 1.00 76.76 O
HETATM 3229 O25 OLC A1215 41.346 167.680 26.195 1.00 80.11 O
HETATM 3230 O23 OLC A1215 40.569 170.237 26.844 1.00 81.36 O
HETATM 3231 O20 OLC A1215 42.225 172.276 25.229 1.00 76.39 O
HETATM 3232 C24 OLC A1216 38.909 176.790 30.101 1.00 93.64 C
HETATM 3233 C7 OLC A1216 42.968 186.333 28.473 1.00 94.54 C
HETATM 3234 C6 OLC A1216 41.956 185.427 27.783 1.00 94.64 C
HETATM 3235 C5 OLC A1216 41.482 184.319 28.717 1.00 94.76 C
HETATM 3236 C4 OLC A1216 40.092 183.833 28.324 1.00 95.19 C
HETATM 3237 C3 OLC A1216 40.097 182.342 28.001 1.00 95.56 C
HETATM 3238 C2 OLC A1216 38.748 181.705 28.322 1.00 95.62 C
HETATM 3239 C21 OLC A1216 37.735 178.423 28.624 1.00 94.16 C
HETATM 3240 C1 OLC A1216 38.561 180.430 27.529 1.00 95.44 C
HETATM 3241 C22 OLC A1216 38.188 176.973 28.770 1.00 93.42 C
HETATM 3242 O19 OLC A1216 38.195 180.477 26.363 1.00 95.29 O
HETATM 3243 O25 OLC A1216 39.343 175.429 30.223 1.00 93.95 O
HETATM 3244 O23 OLC A1216 37.053 176.101 28.727 1.00 92.51 O
HETATM 3245 O20 OLC A1216 38.801 179.224 28.102 1.00 95.08 O
HETATM 3246 O HOH A1301 16.667 206.540 9.481 1.00 50.01 O
HETATM 3247 O HOH A1302 15.054 171.023 17.935 1.00 50.23 O
HETATM 3248 O HOH A1303 16.490 198.603 19.066 1.00 46.01 O
HETATM 3249 O HOH A1304 42.531 162.800 14.416 1.00 79.71 O
HETATM 3250 O HOH A1305 26.136 193.292 25.669 1.00 58.59 O
HETATM 3251 O HOH A1306 16.418 180.365 12.522 1.00 40.12 O
HETATM 3252 O HOH A1307 36.622 173.458 29.274 1.00 64.14 O
HETATM 3253 O HOH A1308 23.864 185.652 14.055 1.00 66.86 O
HETATM 3254 O HOH A1309 39.449 201.173 6.341 1.00 53.81 O
HETATM 3255 O HOH A1310 26.034 195.869 24.840 1.00 45.13 O
HETATM 3256 O HOH A1311 26.508 162.243 22.433 1.00 37.91 O
HETATM 3257 O HOH A1312 24.926 171.551 14.787 1.00 40.43 O
HETATM 3258 O HOH A1313 22.272 167.484 17.950 1.00 50.09 O
HETATM 3259 O HOH A1314 25.579 169.675 16.656 1.00 49.10 O
HETATM 3260 O HOH A1315 26.529 161.943 25.108 1.00 50.53 O
HETATM 3261 O HOH A1316 18.929 209.634 7.607 1.00 49.87 O
HETATM 3262 O HOH A1317 34.358 209.902 20.933 1.00 72.35 O
HETATM 3263 O HOH A1318 17.330 165.589 6.045 1.00 57.61 O
HETATM 3264 O HOH A1319 34.721 166.968 8.279 1.00 78.57 O
CONECT 544 1186
CONECT 560 1100
CONECT 580 1226
CONECT 1100 560
CONECT 1186 544
CONECT 1226 580
CONECT 2562 2580
CONECT 2580 2562
CONECT 2958 2959 2964
CONECT 2959 2958 2960
CONECT 2960 2959 2961 2962
CONECT 2961 2960
CONECT 2962 2960 2963
CONECT 2963 2962 2964
CONECT 2964 2958 2963 2965
CONECT 2965 2964 2966
CONECT 2966 2965 2967
CONECT 2967 2966 2968
CONECT 2968 2967 2969 2970
CONECT 2969 2968 2975
CONECT 2970 2968 2971
CONECT 2971 2970 2972 2973
CONECT 2972 2971
CONECT 2973 2971 2974 2975
CONECT 2974 2973 2977
CONECT 2975 2969 2973 2976
CONECT 2976 2975 2977
CONECT 2977 2974 2976 2978
CONECT 2978 2977 2979 2982
CONECT 2979 2978 2980
CONECT 2980 2979 2981
CONECT 2981 2980 2982
CONECT 2982 2978 2981
CONECT 2983 2984 2992
CONECT 2984 2983 2985
CONECT 2985 2984 2986 3010
CONECT 2986 2985 2987
CONECT 2987 2986 2988 2992
CONECT 2988 2987 2989
CONECT 2989 2988 2990
CONECT 2990 2989 2991 2996
CONECT 2991 2990 2992 2993
CONECT 2992 2983 2987 2991 3001
CONECT 2993 2991 2994
CONECT 2994 2993 2995
CONECT 2995 2994 2996 2999 3000
CONECT 2996 2990 2995 2997
CONECT 2997 2996 2998
CONECT 2998 2997 2999
CONECT 2999 2995 2998 3002
CONECT 3000 2995
CONECT 3001 2992
CONECT 3002 2999 3003 3004
CONECT 3003 3002
CONECT 3004 3002 3005
CONECT 3005 3004 3006
CONECT 3006 3005 3007
CONECT 3007 3006 3008 3009
CONECT 3008 3007
CONECT 3009 3007
CONECT 3010 2985
CONECT 3011 3012 3020
CONECT 3012 3011 3013
CONECT 3013 3012 3014 3038
CONECT 3014 3013 3015
CONECT 3015 3014 3016 3020
CONECT 3016 3015 3017
CONECT 3017 3016 3018
CONECT 3018 3017 3019 3024
CONECT 3019 3018 3020 3021
CONECT 3020 3011 3015 3019 3029
CONECT 3021 3019 3022
CONECT 3022 3021 3023
CONECT 3023 3022 3024 3027 3028
CONECT 3024 3018 3023 3025
CONECT 3025 3024 3026
CONECT 3026 3025 3027
CONECT 3027 3023 3026 3030
CONECT 3028 3023
CONECT 3029 3020
CONECT 3030 3027 3031 3032
CONECT 3031 3030
CONECT 3032 3030 3033
CONECT 3033 3032 3034
CONECT 3034 3033 3035
CONECT 3035 3034 3036 3037
CONECT 3036 3035
CONECT 3037 3035
CONECT 3038 3013
CONECT 3039 3040 3048
CONECT 3040 3039 3041
CONECT 3041 3040 3042 3066
CONECT 3042 3041 3043
CONECT 3043 3042 3044 3048
CONECT 3044 3043 3045
CONECT 3045 3044 3046
CONECT 3046 3045 3047 3052
CONECT 3047 3046 3048 3049
CONECT 3048 3039 3043 3047 3057
CONECT 3049 3047 3050
CONECT 3050 3049 3051
CONECT 3051 3050 3052 3055 3056
CONECT 3052 3046 3051 3053
CONECT 3053 3052 3054
CONECT 3054 3053 3055
CONECT 3055 3051 3054 3058
CONECT 3056 3051
CONECT 3057 3048
CONECT 3058 3055 3059 3060
CONECT 3059 3058
CONECT 3060 3058 3061
CONECT 3061 3060 3062
CONECT 3062 3061 3063
CONECT 3063 3062 3064 3065
CONECT 3064 3063
CONECT 3065 3063
CONECT 3066 3041
CONECT 3067 3068 3072 3073
CONECT 3068 3067 3069
CONECT 3069 3068 3070
CONECT 3070 3069 3071
CONECT 3071 3070 3079
CONECT 3072 3067
CONECT 3073 3067 3074
CONECT 3074 3073 3075
CONECT 3075 3074 3076 3077
CONECT 3076 3075
CONECT 3077 3075 3078
CONECT 3078 3077
CONECT 3079 3071 3080
CONECT 3080 3079 3081
CONECT 3081 3080
CONECT 3082 3083 3084 3085
CONECT 3083 3082
CONECT 3084 3082
CONECT 3085 3082 3086
CONECT 3086 3085 3087
CONECT 3087 3086 3088
CONECT 3088 3087 3089
CONECT 3089 3088 3090
CONECT 3090 3089 3091
CONECT 3091 3090 3092
CONECT 3092 3091 3093
CONECT 3093 3092 3094
CONECT 3094 3093 3095
CONECT 3095 3094 3096
CONECT 3096 3095 3097
CONECT 3097 3096
CONECT 3098 3099 3100 3101
CONECT 3099 3098
CONECT 3100 3098
CONECT 3101 3098 3102
CONECT 3102 3101 3103
CONECT 3103 3102 3104
CONECT 3104 3103 3105
CONECT 3105 3104 3106
CONECT 3106 3105 3107
CONECT 3107 3106 3108
CONECT 3108 3107 3109
CONECT 3109 3108 3110
CONECT 3110 3109 3111
CONECT 3111 3110 3112
CONECT 3112 3111 3113
CONECT 3113 3112
CONECT 3114 3115 3116 3117
CONECT 3115 3114
CONECT 3116 3114
CONECT 3117 3114 3118
CONECT 3118 3117 3119
CONECT 3119 3118 3120
CONECT 3120 3119 3121
CONECT 3121 3120 3122
CONECT 3122 3121 3123
CONECT 3123 3122 3124
CONECT 3124 3123 3125
CONECT 3125 3124 3126
CONECT 3126 3125 3127
CONECT 3127 3126
CONECT 3128 3129 3130 3131
CONECT 3129 3128
CONECT 3130 3128
CONECT 3131 3128 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 3140
CONECT 3140 3139 3141
CONECT 3141 3140 3142
CONECT 3142 3141 3143
CONECT 3143 3142 3144
CONECT 3144 3143 3145
CONECT 3145 3144
CONECT 3146 3147 3148 3149
CONECT 3147 3146
CONECT 3148 3146
CONECT 3149 3146 3150
CONECT 3150 3149 3151
CONECT 3151 3150 3152
CONECT 3152 3151 3153
CONECT 3153 3152 3154
CONECT 3154 3153 3155
CONECT 3155 3154 3156
CONECT 3156 3155
CONECT 3157 3158 3159 3160
CONECT 3158 3157
CONECT 3159 3157
CONECT 3160 3157 3161
CONECT 3161 3160 3162
CONECT 3162 3161 3163
CONECT 3163 3162 3164
CONECT 3164 3163 3165
CONECT 3165 3164
CONECT 3166 3167 3168 3169
CONECT 3167 3166
CONECT 3168 3166
CONECT 3169 3166 3170
CONECT 3170 3169 3171
CONECT 3171 3170 3172
CONECT 3172 3171 3173
CONECT 3173 3172 3174
CONECT 3174 3173 3175
CONECT 3175 3174 3176
CONECT 3176 3175 3177
CONECT 3177 3176 3178
CONECT 3178 3177 3179
CONECT 3179 3178
CONECT 3180 3181 3182
CONECT 3181 3180 3183
CONECT 3182 3180 3185
CONECT 3183 3181 3186
CONECT 3184 3194 3196
CONECT 3185 3182
CONECT 3186 3183 3187
CONECT 3187 3186 3188
CONECT 3188 3187 3189
CONECT 3189 3188 3190
CONECT 3190 3189 3191
CONECT 3191 3190 3193
CONECT 3192 3194 3198
CONECT 3193 3191 3195 3198
CONECT 3194 3184 3192 3197
CONECT 3195 3193
CONECT 3196 3184
CONECT 3197 3194
CONECT 3198 3192 3193
CONECT 3199 3200
CONECT 3200 3199 3202
CONECT 3201 3210 3212
CONECT 3202 3200 3203
CONECT 3203 3202 3204
CONECT 3204 3203 3205
CONECT 3205 3204 3206
CONECT 3206 3205 3207
CONECT 3207 3206 3209
CONECT 3208 3210 3214
CONECT 3209 3207 3211 3214
CONECT 3210 3201 3208 3213
CONECT 3211 3209
CONECT 3212 3201
CONECT 3213 3210
CONECT 3214 3208 3209
CONECT 3215 3216
CONECT 3216 3215 3217
CONECT 3217 3216 3219
CONECT 3218 3227 3229
CONECT 3219 3217 3220
CONECT 3220 3219 3221
CONECT 3221 3220 3222
CONECT 3222 3221 3223
CONECT 3223 3222 3224
CONECT 3224 3223 3226
CONECT 3225 3227 3231
CONECT 3226 3224 3228 3231
CONECT 3227 3218 3225 3230
CONECT 3228 3226
CONECT 3229 3218
CONECT 3230 3227
CONECT 3231 3225 3226
CONECT 3232 3241 3243
CONECT 3233 3234
CONECT 3234 3233 3235
CONECT 3235 3234 3236
CONECT 3236 3235 3237
CONECT 3237 3236 3238
CONECT 3238 3237 3240
CONECT 3239 3241 3245
CONECT 3240 3238 3242 3245
CONECT 3241 3232 3239 3244
CONECT 3242 3240
CONECT 3243 3232
CONECT 3244 3241
CONECT 3245 3239 3240
MASTER 438 0 16 20 2 0 21 6 3257 1 296 34
END