HEADER MEMBRANE PROTEIN 30-DEC-18 6J21
TITLE CRYSTAL STRUCTURE OF THE HUMAN NK1 SUBSTANCE P RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBSTANCE-P RECEPTOR,ENDOLYSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SPR,NK-1 RECEPTOR,NK-1R,TACHYKININ RECEPTOR 1,LYSIS PROTEIN,
COMPND 5 LYSOZYME,MURAMIDASE;
COMPND 6 EC: 3.2.1.17;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: THE FUSION PROTEIN OF SUBSTANCE-P RECEPTOR NK1R
COMPND 10 (RESIDUES 2-226), MINI-T4L (RESIDUES 1001-1010, 1017-1117), LINKER
COMPND 11 GGGSGG (RESIDUES 1011-1016), AND NK1R (RESIDUES 237-335)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;
SOURCE 3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;
SOURCE 4 ORGANISM_TAXID: 9606, 10665;
SOURCE 5 GENE: TACR1, NK1R, TAC1R, E, T4TP126;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS GPCR, COMPLEX, ANTAGONIST, SIGNALLING PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.CHEN,M.LU,H.ZHANG,B.WU,Q.ZHAO
REVDAT 1 06-MAR-19 6J21 0
JRNL AUTH S.CHEN,M.LU,D.LIU,L.YANG,C.YI,L.MA,H.ZHANG,Q.LIU,
JRNL AUTH 2 T.M.FRIMURER,M.W.WANG,T.W.SCHWARTZ,R.C.STEVENS,B.WU,
JRNL AUTH 3 K.WUTHRICH,Q.ZHAO
JRNL TITL HUMAN SUBSTANCE P RECEPTOR BINDING MODE OF THE ANTAGONIST
JRNL TITL 2 DRUG APREPITANT BY NMR AND CRYSTALLOGRAPHY.
JRNL REF NAT COMMUN V. 10 638 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 30733446
JRNL DOI 10.1038/S41467-019-08568-5
REMARK 2
REMARK 2 RESOLUTION. 3.20 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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 13746
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.710
REMARK 3 FREE R VALUE TEST SET COUNT : 647
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 : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.46
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.94
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2897
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2420
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2774
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.25
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 123
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 : 3082
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 132.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 122.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.28050
REMARK 3 B22 (A**2) : -7.28050
REMARK 3 B33 (A**2) : 14.56110
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) : 0.470
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.217
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.394
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 1.145
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.398
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 : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3229 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4424 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1010 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 46 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 481 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3229 ; 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 : 439 ; 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 : 3605 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.26
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.25
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1682 138.8760 188.1050
REMARK 3 T TENSOR
REMARK 3 T11: -0.1467 T22: -0.4257
REMARK 3 T33: -0.4339 T12: -0.0468
REMARK 3 T13: 0.1356 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 1.4540 L22: 0.1835
REMARK 3 L33: 5.2346 L12: -0.3404
REMARK 3 L13: 1.7043 L23: -0.5571
REMARK 3 S TENSOR
REMARK 3 S11: -0.2091 S12: 0.0858 S13: -0.1492
REMARK 3 S21: -0.0484 S22: 0.0684 S23: -0.0398
REMARK 3 S31: 0.7568 S32: 0.5351 S33: 0.1407
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6J21 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010328.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13746
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 12.10
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 9.80
REMARK 200 R MERGE FOR SHELL (I) : 0.77000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4U15
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, PH 6.0-6.6, 25-35% PEG 400,
REMARK 280 200-350MM AMMONIUM TARTRATE DIBASIC, LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.55500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 79.08000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.55500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.55500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.08000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.55500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.55500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 79.08000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.55500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.55500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 79.08000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 2
REMARK 465 ASN A 3
REMARK 465 VAL A 4
REMARK 465 LEU A 5
REMARK 465 PRO A 6
REMARK 465 VAL A 7
REMARK 465 ASP A 8
REMARK 465 SER A 9
REMARK 465 ASP A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 PRO A 13
REMARK 465 ASN A 14
REMARK 465 ILE A 15
REMARK 465 SER A 16
REMARK 465 THR A 17
REMARK 465 ASN A 18
REMARK 465 THR A 19
REMARK 465 SER A 20
REMARK 465 GLU A 21
REMARK 465 PRO A 22
REMARK 465 ASN A 23
REMARK 465 GLN A 24
REMARK 465 GLY A 1011
REMARK 465 GLY A 1012
REMARK 465 GLY A 1013
REMARK 465 SER A 1014
REMARK 465 GLY A 1015
REMARK 465 GLY A 1016
REMARK 465 CYS A 322
REMARK 465 CYS A 323
REMARK 465 PRO A 324
REMARK 465 PHE A 325
REMARK 465 ILE A 326
REMARK 465 SER A 327
REMARK 465 ALA A 328
REMARK 465 GLY A 329
REMARK 465 ASP A 330
REMARK 465 TYR A 331
REMARK 465 GLU A 332
REMARK 465 GLY A 333
REMARK 465 LEU A 334
REMARK 465 GLU A 335
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 PHE A 25 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 30 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 30 CZ3 CH2
REMARK 470 ILE A 32 CG1 CG2 CD1
REMARK 470 VAL A 33 CG1 CG2
REMARK 470 LEU A 58 CD1 CD2
REMARK 470 LYS A 61 CG CD CE NZ
REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 64 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 69 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 94 CG1 CG2
REMARK 470 LEU A 142 CG CD1 CD2
REMARK 470 THR A 145 OG1 CG2
REMARK 470 SER A 176 OG
REMARK 470 VAL A 178 CG1 CG2
REMARK 470 GLU A 186 CG CD OE1 OE2
REMARK 470 ASN A 189 CG OD1 ND2
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 ILE A 191 CG1 CG2 CD1
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 GLU A1004 CG CD OE1 OE2
REMARK 470 ASP A1017 CG OD1 OD2
REMARK 470 GLU A1018 CG CD OE1 OE2
REMARK 470 GLU A1020 CG CD OE1 OE2
REMARK 470 LYS A1021 CG CD CE NZ
REMARK 470 LEU A1022 CG CD1 CD2
REMARK 470 GLN A1025 CG CD OE1 NE2
REMARK 470 ARG A1075 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1103 CG CD CE NZ
REMARK 470 LYS A 243 CG CD CE NZ
REMARK 470 ILE A 273 CG1 CG2 CD1
REMARK 470 ASN A 274 CG OD1 ND2
REMARK 470 LEU A 277 CG CD1 CD2
REMARK 470 TYR A 278 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 279 CG CD1 CD2
REMARK 470 LYS A 280 CG CD CE NZ
REMARK 470 LYS A 281 CG CD CE NZ
REMARK 470 PHE A 282 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CYS A 307 SG
REMARK 470 LEU A 314 CG CD1 CD2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 HIS A 318 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 320 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 321 CG CD NE 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 PHE A 110 -62.32 -90.75
REMARK 500 GLU A 186 93.36 -69.91
REMARK 500 ASN A 189 -2.89 -140.12
REMARK 500 TYR A 205 -72.27 -137.61
REMARK 500 GLU A1018 148.08 -173.45
REMARK 500 PHE A1070 47.09 -72.52
REMARK 500 GLN A 239 -70.41 -61.02
REMARK 500 LYS A 281 -139.92 69.77
REMARK 500 ALA A 319 57.91 -97.73
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 OLC A 1202
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GBQ A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1202
DBREF 6J21 A 2 226 UNP P25103 NK1R_HUMAN 2 226
DBREF 6J21 A 1001 1010 UNP D9IEF7 D9IEF7_BPT4 2 11
DBREF 6J21 A 1017 1117 UNP D9IEF7 D9IEF7_BPT4 61 161
DBREF 6J21 A 237 335 UNP P25103 NK1R_HUMAN 237 335
SEQADV 6J21 ASP A 78 UNP P25103 GLU 78 ENGINEERED MUTATION
SEQADV 6J21 TRP A 121 UNP P25103 TYR 121 ENGINEERED MUTATION
SEQADV 6J21 ALA A 165 UNP P25103 GLN 165 ENGINEERED MUTATION
SEQADV 6J21 ARG A 222 UNP P25103 THR 222 ENGINEERED MUTATION
SEQADV 6J21 GLY A 1011 UNP D9IEF7 LINKER
SEQADV 6J21 GLY A 1012 UNP D9IEF7 LINKER
SEQADV 6J21 GLY A 1013 UNP D9IEF7 LINKER
SEQADV 6J21 SER A 1014 UNP D9IEF7 LINKER
SEQADV 6J21 GLY A 1015 UNP D9IEF7 LINKER
SEQADV 6J21 GLY A 1016 UNP D9IEF7 LINKER
SEQADV 6J21 ALA A 1053 UNP D9IEF7 CYS 97 ENGINEERED MUTATION
SEQRES 1 A 441 ASP ASN VAL LEU PRO VAL ASP SER ASP LEU SER PRO ASN
SEQRES 2 A 441 ILE SER THR ASN THR SER GLU PRO ASN GLN PHE VAL GLN
SEQRES 3 A 441 PRO ALA TRP GLN ILE VAL LEU TRP ALA ALA ALA TYR THR
SEQRES 4 A 441 VAL ILE VAL VAL THR SER VAL VAL GLY ASN VAL VAL VAL
SEQRES 5 A 441 MET TRP ILE ILE LEU ALA HIS LYS ARG MET ARG THR VAL
SEQRES 6 A 441 THR ASN TYR PHE LEU VAL ASN LEU ALA PHE ALA ASP ALA
SEQRES 7 A 441 SER MET ALA ALA PHE ASN THR VAL VAL ASN PHE THR TYR
SEQRES 8 A 441 ALA VAL HIS ASN GLU TRP TYR TYR GLY LEU PHE TYR CYS
SEQRES 9 A 441 LYS PHE HIS ASN PHE PHE PRO ILE ALA ALA VAL PHE ALA
SEQRES 10 A 441 SER ILE TRP SER MET THR ALA VAL ALA PHE ASP ARG TYR
SEQRES 11 A 441 MET ALA ILE ILE HIS PRO LEU GLN PRO ARG LEU SER ALA
SEQRES 12 A 441 THR ALA THR LYS VAL VAL ILE CYS VAL ILE TRP VAL LEU
SEQRES 13 A 441 ALA LEU LEU LEU ALA PHE PRO ALA GLY TYR TYR SER THR
SEQRES 14 A 441 THR GLU THR MET PRO SER ARG VAL VAL CYS MET ILE GLU
SEQRES 15 A 441 TRP PRO GLU HIS PRO ASN LYS ILE TYR GLU LYS VAL TYR
SEQRES 16 A 441 HIS ILE CYS VAL THR VAL LEU ILE TYR PHE LEU PRO LEU
SEQRES 17 A 441 LEU VAL ILE GLY TYR ALA TYR THR VAL VAL GLY ILE ARG
SEQRES 18 A 441 LEU TRP ALA SER ASN ILE PHE GLU MET LEU ARG ILE ASP
SEQRES 19 A 441 GLU GLY GLY GLY SER GLY GLY ASP GLU ALA GLU LYS LEU
SEQRES 20 A 441 PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU
SEQRES 21 A 441 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP
SEQRES 22 A 441 ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN
SEQRES 23 A 441 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU
SEQRES 24 A 441 ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL
SEQRES 25 A 441 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN
SEQRES 26 A 441 ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR
SEQRES 27 A 441 TRP ASP ALA TYR HIS GLU GLN VAL SER ALA LYS ARG LYS
SEQRES 28 A 441 VAL VAL LYS MET MET ILE VAL VAL VAL CYS THR PHE ALA
SEQRES 29 A 441 ILE CYS TRP LEU PRO PHE HIS ILE PHE PHE LEU LEU PRO
SEQRES 30 A 441 TYR ILE ASN PRO ASP LEU TYR LEU LYS LYS PHE ILE GLN
SEQRES 31 A 441 GLN VAL TYR LEU ALA ILE MET TRP LEU ALA MET SER SER
SEQRES 32 A 441 THR MET TYR ASN PRO ILE ILE TYR CYS CYS LEU ASN ASP
SEQRES 33 A 441 ARG PHE ARG LEU GLY PHE LYS HIS ALA PHE ARG CYS CYS
SEQRES 34 A 441 PRO PHE ILE SER ALA GLY ASP TYR GLU GLY LEU GLU
HET GBQ A1201 37
HET OLC A1202 19
HETNAM GBQ 5-[[(2~{R},3~{S})-2-[(1~{R})-1-[3,5-
HETNAM 2 GBQ BIS(TRIFLUOROMETHYL)PHENYL]ETHOXY]-3-(4-FLUOROPHENYL)
HETNAM 3 GBQ MORPHOLIN-4-YL]METHYL]-1,2-DIHYDRO-1,2,4-TRIAZOL-3-ONE
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 GBQ C23 H21 F7 N4 O3
FORMUL 3 OLC C21 H40 O4
HELIX 1 AA1 PRO A 28 ALA A 59 1 32
HELIX 2 AA2 THR A 65 ASN A 96 1 32
HELIX 3 AA3 TYR A 100 ILE A 135 1 36
HELIX 4 AA4 SER A 143 TYR A 168 1 26
HELIX 5 AA5 LYS A 190 TYR A 205 1 16
HELIX 6 AA6 TYR A 205 ALA A 225 1 21
HELIX 7 AA7 ASN A 1001 GLU A 1010 1 10
HELIX 8 AA8 LEU A 1022 LEU A 1035 1 14
HELIX 9 AA9 LEU A 1040 LEU A 1047 1 8
HELIX 10 AB1 ASP A 1048 GLY A 1063 1 16
HELIX 11 AB2 GLY A 1063 ALA A 1068 1 6
HELIX 12 AB3 PHE A 1070 GLN A 1079 1 10
HELIX 13 AB4 ARG A 1081 ALA A 1090 1 10
HELIX 14 AB5 SER A 1092 THR A 1098 1 7
HELIX 15 AB6 THR A 1098 GLY A 1112 1 15
HELIX 16 AB7 TRP A 1114 HIS A 237 5 5
HELIX 17 AB8 SER A 241 LEU A 270 1 30
HELIX 18 AB9 PRO A 271 ILE A 273 5 3
HELIX 19 AC1 ASN A 274 LEU A 279 1 6
HELIX 20 AC2 PHE A 282 ASN A 309 1 28
HELIX 21 AC3 ASN A 309 ALA A 319 1 11
SHEET 1 AA1 2 SER A 169 THR A 173 0
SHEET 2 AA1 2 VAL A 178 ILE A 182 -1 O VAL A 179 N GLU A 172
SSBOND 1 CYS A 105 CYS A 180 1555 1555 2.04
CISPEP 1 ALA A 59 HIS A 60 0 10.09
SITE 1 AC1 13 ASN A 109 PRO A 112 ILE A 113 VAL A 116
SITE 2 AC1 13 ILE A 182 TRP A 184 GLU A 193 HIS A 197
SITE 3 AC1 13 VAL A 200 THR A 201 TRP A 261 PHE A 264
SITE 4 AC1 13 PHE A 268
SITE 1 AC2 2 GLY A 213 GLY A 220
CRYST1 103.110 103.110 158.160 90.00 90.00 90.00 P 42 21 2 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 0.009698 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009698 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006323 0.00000
ATOM 1 N PHE A 25 -1.843 123.629 222.528 1.00177.60 N
ANISOU 1 N PHE A 25 25785 22843 18852 -762 1299 3527 N
ATOM 2 CA PHE A 25 -1.632 122.418 223.324 1.00180.62 C
ANISOU 2 CA PHE A 25 26520 23036 19072 -886 1220 3794 C
ATOM 3 C PHE A 25 -1.648 121.123 222.482 1.00186.83 C
ANISOU 3 C PHE A 25 27926 23229 19830 -1153 1092 3925 C
ATOM 4 O PHE A 25 -1.274 120.059 222.990 1.00188.76 O
ANISOU 4 O PHE A 25 28582 23166 19972 -1158 1003 4096 O
ATOM 5 CB PHE A 25 -2.640 122.346 224.485 1.00184.60 C
ANISOU 5 CB PHE A 25 26743 24063 19335 -1195 1213 4060 C
ATOM 6 N VAL A 26 -2.061 121.224 221.195 1.00182.59 N
ANISOU 6 N VAL A 26 27476 22521 19377 -1358 1070 3837 N
ATOM 7 CA VAL A 26 -2.131 120.099 220.246 1.00184.50 C
ANISOU 7 CA VAL A 26 28310 22196 19595 -1613 935 3925 C
ATOM 8 C VAL A 26 -0.693 119.697 219.840 1.00186.85 C
ANISOU 8 C VAL A 26 28993 21978 20025 -1137 920 3729 C
ATOM 9 O VAL A 26 -0.015 120.460 219.141 1.00183.87 O
ANISOU 9 O VAL A 26 28424 21605 19834 -793 1013 3446 O
ATOM 10 CB VAL A 26 -3.047 120.403 219.012 1.00187.76 C
ANISOU 10 CB VAL A 26 28650 22640 20049 -1963 923 3879 C
ATOM 11 CG1 VAL A 26 -3.327 119.140 218.199 1.00190.45 C
ANISOU 11 CG1 VAL A 26 29626 22417 20318 -2302 753 4014 C
ATOM 12 CG2 VAL A 26 -4.362 121.059 219.434 1.00187.99 C
ANISOU 12 CG2 VAL A 26 28188 23298 19940 -2333 963 4029 C
ATOM 13 N GLN A 27 -0.227 118.514 220.307 1.00184.64 N
ANISOU 13 N GLN A 27 29248 21282 19625 -1112 796 3888 N
ATOM 14 CA GLN A 27 1.129 118.009 220.036 1.00183.44 C
ANISOU 14 CA GLN A 27 29490 20672 19538 -627 767 3728 C
ATOM 15 C GLN A 27 1.177 116.501 219.604 1.00189.33 C
ANISOU 15 C GLN A 27 31023 20766 20148 -778 557 3875 C
ATOM 16 O GLN A 27 1.898 115.716 220.233 1.00191.24 O
ANISOU 16 O GLN A 27 31636 20737 20291 -534 478 3950 O
ATOM 17 CB GLN A 27 2.051 118.293 221.245 1.00183.84 C
ANISOU 17 CB GLN A 27 29333 20936 19581 -193 846 3700 C
ATOM 18 CG GLN A 27 1.452 117.916 222.606 1.00194.99 C
ANISOU 18 CG GLN A 27 30712 22574 20803 -448 802 4004 C
ATOM 19 CD GLN A 27 2.299 118.400 223.749 1.00208.31 C
ANISOU 19 CD GLN A 27 32098 24552 22497 -27 900 3949 C
ATOM 20 OE1 GLN A 27 2.461 119.605 223.969 1.00201.72 O
ANISOU 20 OE1 GLN A 27 30709 24165 21772 160 1039 3783 O
ATOM 21 NE2 GLN A 27 2.841 117.470 224.516 1.00198.65 N
ANISOU 21 NE2 GLN A 27 31255 23077 21146 122 814 4093 N
ATOM 22 N PRO A 28 0.484 116.077 218.505 1.00185.39 N
ANISOU 22 N PRO A 28 30822 19981 19635 -1143 452 3901 N
ATOM 23 CA PRO A 28 0.516 114.651 218.123 1.00188.31 C
ANISOU 23 CA PRO A 28 31987 19706 19856 -1292 221 4040 C
ATOM 24 C PRO A 28 1.669 114.244 217.203 1.00188.81 C
ANISOU 24 C PRO A 28 32491 19271 19977 -772 174 3790 C
ATOM 25 O PRO A 28 2.076 115.018 216.335 1.00185.43 O
ANISOU 25 O PRO A 28 31774 18961 19720 -462 305 3510 O
ATOM 26 CB PRO A 28 -0.845 114.434 217.437 1.00191.61 C
ANISOU 26 CB PRO A 28 32492 20097 20215 -1948 123 4188 C
ATOM 27 CG PRO A 28 -1.512 115.808 217.375 1.00192.93 C
ANISOU 27 CG PRO A 28 31873 20934 20498 -2091 320 4117 C
ATOM 28 CD PRO A 28 -0.436 116.818 217.623 1.00184.92 C
ANISOU 28 CD PRO A 28 30427 20168 19665 -1474 513 3833 C
ATOM 29 N ALA A 29 2.172 113.007 217.379 1.00186.39 N
ANISOU 29 N ALA A 29 32900 18415 19506 -680 -29 3900 N
ATOM 30 CA ALA A 29 3.262 112.444 216.577 1.00185.82 C
ANISOU 30 CA ALA A 29 33331 17850 19423 -155 -110 3685 C
ATOM 31 C ALA A 29 2.833 112.204 215.126 1.00186.77 C
ANISOU 31 C ALA A 29 33748 17639 19576 -327 -200 3561 C
ATOM 32 O ALA A 29 3.641 112.403 214.216 1.00185.02 O
ANISOU 32 O ALA A 29 33566 17300 19433 139 -150 3282 O
ATOM 33 CB ALA A 29 3.760 111.151 217.201 1.00191.10 C
ANISOU 33 CB ALA A 29 34712 18024 19874 -24 -328 3855 C
ATOM 34 N TRP A 30 1.552 111.810 214.913 1.00182.60 N
ANISOU 34 N TRP A 30 33401 17004 18973 -1006 -332 3776 N
ATOM 35 CA TRP A 30 0.951 111.558 213.597 1.00181.73 C
ANISOU 35 CA TRP A 30 33575 16598 18877 -1278 -436 3700 C
ATOM 36 C TRP A 30 1.009 112.804 212.723 1.00177.85 C
ANISOU 36 C TRP A 30 32468 16493 18612 -1102 -209 3418 C
ATOM 37 O TRP A 30 1.105 112.692 211.503 1.00177.06 O
ANISOU 37 O TRP A 30 32599 16121 18553 -973 -250 3225 O
ATOM 38 CB TRP A 30 -0.504 111.092 213.748 1.00183.11 C
ANISOU 38 CB TRP A 30 33901 16750 18923 -2100 -591 4021 C
ATOM 39 N GLN A 31 0.977 113.987 213.359 1.00169.13 N
ANISOU 39 N GLN A 31 30605 16016 17642 -1077 17 3393 N
ATOM 40 CA GLN A 31 1.047 115.289 212.700 1.00163.72 C
ANISOU 40 CA GLN A 31 29291 15747 17169 -922 229 3149 C
ATOM 41 C GLN A 31 2.491 115.724 212.392 1.00162.87 C
ANISOU 41 C GLN A 31 29054 15660 17171 -218 349 2857 C
ATOM 42 O GLN A 31 2.738 116.213 211.290 1.00160.14 O
ANISOU 42 O GLN A 31 28530 15366 16951 -62 428 2632 O
ATOM 43 CB GLN A 31 0.306 116.360 213.522 1.00162.69 C
ANISOU 43 CB GLN A 31 28457 16256 17102 -1190 385 3249 C
ATOM 44 CG GLN A 31 -1.221 116.270 213.419 1.00178.84 C
ANISOU 44 CG GLN A 31 30436 18442 19072 -1880 318 3458 C
ATOM 45 CD GLN A 31 -1.973 117.280 214.264 1.00194.47 C
ANISOU 45 CD GLN A 31 31779 21065 21044 -2122 443 3590 C
ATOM 46 OE1 GLN A 31 -1.449 118.317 214.693 1.00185.87 O
ANISOU 46 OE1 GLN A 31 30166 20383 20075 -1786 615 3446 O
ATOM 47 NE2 GLN A 31 -3.234 116.986 214.535 1.00188.99 N
ANISOU 47 NE2 GLN A 31 31123 20498 20187 -2719 345 3873 N
ATOM 48 N ILE A 32 3.434 115.546 213.357 1.00157.97 N
ANISOU 48 N ILE A 32 28506 15028 16487 192 359 2872 N
ATOM 49 CA ILE A 32 4.851 115.923 213.228 1.00154.91 C
ANISOU 49 CA ILE A 32 27978 14720 16161 858 464 2627 C
ATOM 50 C ILE A 32 5.552 115.237 212.043 1.00158.82 C
ANISOU 50 C ILE A 32 28976 14771 16597 1199 364 2444 C
ATOM 51 O ILE A 32 6.261 115.910 211.291 1.00155.94 O
ANISOU 51 O ILE A 32 28337 14580 16333 1556 480 2204 O
ATOM 52 CB ILE A 32 5.618 115.708 214.550 1.00158.59 C
ANISOU 52 CB ILE A 32 28430 15285 16542 1181 482 2713 C
ATOM 53 N VAL A 33 5.330 113.913 211.866 1.00158.32 N
ANISOU 53 N VAL A 33 29657 14143 16354 1080 134 2562 N
ATOM 54 CA VAL A 33 5.898 113.106 210.779 1.00159.71 C
ANISOU 54 CA VAL A 33 30421 13834 16427 1395 -8 2400 C
ATOM 55 C VAL A 33 5.320 113.522 209.428 1.00160.57 C
ANISOU 55 C VAL A 33 30422 13942 16646 1147 17 2268 C
ATOM 56 O VAL A 33 6.035 113.522 208.427 1.00160.11 O
ANISOU 56 O VAL A 33 30501 13754 16578 1534 16 2039 O
ATOM 57 CB VAL A 33 5.699 111.598 211.030 1.00168.73 C
ANISOU 57 CB VAL A 33 32428 14346 17334 1282 -295 2582 C
ATOM 58 N LEU A 34 4.028 113.885 209.415 1.00154.96 N
ANISOU 58 N LEU A 34 29440 13416 16023 516 43 2415 N
ATOM 59 CA LEU A 34 3.289 114.341 208.241 1.00152.77 C
ANISOU 59 CA LEU A 34 28991 13200 15854 195 76 2325 C
ATOM 60 C LEU A 34 3.784 115.728 207.772 1.00151.17 C
ANISOU 60 C LEU A 34 28106 13479 15851 500 314 2084 C
ATOM 61 O LEU A 34 3.845 115.969 206.565 1.00150.16 O
ANISOU 61 O LEU A 34 27993 13284 15776 597 329 1899 O
ATOM 62 CB LEU A 34 1.788 114.370 208.580 1.00153.07 C
ANISOU 62 CB LEU A 34 28871 13393 15895 -538 44 2578 C
ATOM 63 CG LEU A 34 0.805 114.544 207.428 1.00157.30 C
ANISOU 63 CG LEU A 34 29385 13900 16481 -984 13 2554 C
ATOM 64 CD1 LEU A 34 -0.375 113.602 207.586 1.00160.63 C
ANISOU 64 CD1 LEU A 34 30230 14060 16741 -1642 -197 2844 C
ATOM 65 CD2 LEU A 34 0.334 116.006 207.315 1.00156.07 C
ANISOU 65 CD2 LEU A 34 28425 14353 16523 -1102 240 2472 C
ATOM 66 N TRP A 35 4.117 116.635 208.722 1.00143.84 N
ANISOU 66 N TRP A 35 26600 13029 15022 634 484 2092 N
ATOM 67 CA TRP A 35 4.621 117.985 208.434 1.00138.90 C
ANISOU 67 CA TRP A 35 25337 12865 14574 894 686 1890 C
ATOM 68 C TRP A 35 6.035 117.939 207.848 1.00141.50 C
ANISOU 68 C TRP A 35 25766 13127 14871 1517 713 1667 C
ATOM 69 O TRP A 35 6.298 118.639 206.871 1.00138.71 O
ANISOU 69 O TRP A 35 25158 12931 14616 1639 796 1483 O
ATOM 70 CB TRP A 35 4.625 118.861 209.696 1.00135.23 C
ANISOU 70 CB TRP A 35 24320 12874 14186 890 819 1965 C
ATOM 71 CG TRP A 35 3.364 119.628 209.968 1.00134.30 C
ANISOU 71 CG TRP A 35 23799 13077 14153 385 875 2080 C
ATOM 72 CD1 TRP A 35 2.565 119.514 211.066 1.00138.15 C
ANISOU 72 CD1 TRP A 35 24209 13709 14572 64 852 2307 C
ATOM 73 CD2 TRP A 35 2.825 120.707 209.191 1.00131.15 C
ANISOU 73 CD2 TRP A 35 22969 12958 13904 200 969 1968 C
ATOM 74 NE1 TRP A 35 1.541 120.428 211.007 1.00135.59 N
ANISOU 74 NE1 TRP A 35 23438 13751 14329 -297 924 2337 N
ATOM 75 CE2 TRP A 35 1.673 121.173 209.864 1.00134.59 C
ANISOU 75 CE2 TRP A 35 23101 13695 14341 -217 993 2129 C
ATOM 76 CE3 TRP A 35 3.198 121.323 207.985 1.00130.32 C
ANISOU 76 CE3 TRP A 35 22709 12892 13916 349 1030 1752 C
ATOM 77 CZ2 TRP A 35 0.888 122.223 209.371 1.00131.43 C
ANISOU 77 CZ2 TRP A 35 22270 13615 14051 -458 1069 2069 C
ATOM 78 CZ3 TRP A 35 2.421 122.364 207.499 1.00129.31 C
ANISOU 78 CZ3 TRP A 35 22166 13054 13912 79 1102 1704 C
ATOM 79 CH2 TRP A 35 1.278 122.799 208.186 1.00129.53 C
ANISOU 79 CH2 TRP A 35 21919 13361 13935 -305 1119 1855 C
ATOM 80 N ALA A 36 6.940 117.119 208.453 1.00139.66 N
ANISOU 80 N ALA A 36 25895 12686 14482 1913 637 1691 N
ATOM 81 CA ALA A 36 8.336 116.926 208.029 1.00139.76 C
ANISOU 81 CA ALA A 36 26029 12670 14405 2556 649 1499 C
ATOM 82 C ALA A 36 8.428 116.410 206.593 1.00144.35 C
ANISOU 82 C ALA A 36 26981 12943 14923 2675 561 1339 C
ATOM 83 O ALA A 36 9.377 116.745 205.881 1.00142.80 O
ANISOU 83 O ALA A 36 26604 12934 14718 3101 638 1140 O
ATOM 84 CB ALA A 36 9.039 115.966 208.970 1.00143.59 C
ANISOU 84 CB ALA A 36 26936 12923 14698 2898 544 1586 C
ATOM 85 N ALA A 37 7.431 115.600 206.179 1.00142.88 N
ANISOU 85 N ALA A 37 27298 12312 14678 2277 395 1435 N
ATOM 86 CA ALA A 37 7.297 115.046 204.834 1.00144.08 C
ANISOU 86 CA ALA A 37 27857 12124 14764 2304 284 1301 C
ATOM 87 C ALA A 37 6.905 116.163 203.858 1.00143.96 C
ANISOU 87 C ALA A 37 27311 12446 14941 2092 431 1180 C
ATOM 88 O ALA A 37 7.497 116.272 202.786 1.00143.17 O
ANISOU 88 O ALA A 37 27229 12351 14819 2391 450 981 O
ATOM 89 CB ALA A 37 6.250 113.942 204.827 1.00148.23 C
ANISOU 89 CB ALA A 37 29045 12102 15175 1853 51 1473 C
ATOM 90 N ALA A 38 5.936 117.015 204.253 1.00137.60 N
ANISOU 90 N ALA A 38 26030 11946 14307 1602 533 1298 N
ATOM 91 CA ALA A 38 5.471 118.155 203.461 1.00133.94 C
ANISOU 91 CA ALA A 38 25043 11820 14028 1380 668 1203 C
ATOM 92 C ALA A 38 6.587 119.191 203.328 1.00134.91 C
ANISOU 92 C ALA A 38 24643 12380 14237 1819 837 1030 C
ATOM 93 O ALA A 38 6.706 119.848 202.293 1.00132.73 O
ANISOU 93 O ALA A 38 24113 12274 14046 1853 909 884 O
ATOM 94 CB ALA A 38 4.252 118.785 204.124 1.00132.83 C
ANISOU 94 CB ALA A 38 24540 11922 14006 828 720 1378 C
ATOM 95 N TYR A 39 7.406 119.319 204.380 1.00131.05 N
ANISOU 95 N TYR A 39 23999 12081 13714 2132 891 1061 N
ATOM 96 CA TYR A 39 8.525 120.247 204.445 1.00128.32 C
ANISOU 96 CA TYR A 39 23167 12170 13420 2525 1032 931 C
ATOM 97 C TYR A 39 9.721 119.773 203.629 1.00133.47 C
ANISOU 97 C TYR A 39 24040 12756 13916 3080 1007 761 C
ATOM 98 O TYR A 39 10.360 120.607 202.984 1.00131.64 O
ANISOU 98 O TYR A 39 23407 12882 13729 3293 1113 627 O
ATOM 99 CB TYR A 39 8.909 120.529 205.905 1.00128.62 C
ANISOU 99 CB TYR A 39 22961 12447 13463 2628 1088 1039 C
ATOM 100 CG TYR A 39 8.263 121.779 206.463 1.00126.04 C
ANISOU 100 CG TYR A 39 22076 12492 13320 2277 1193 1101 C
ATOM 101 CD1 TYR A 39 8.946 122.990 206.481 1.00124.85 C
ANISOU 101 CD1 TYR A 39 21379 12783 13276 2431 1313 1001 C
ATOM 102 CD2 TYR A 39 6.963 121.754 206.963 1.00126.38 C
ANISOU 102 CD2 TYR A 39 22149 12462 13407 1799 1157 1266 C
ATOM 103 CE1 TYR A 39 8.359 124.143 206.996 1.00122.15 C
ANISOU 103 CE1 TYR A 39 20576 12751 13084 2147 1382 1043 C
ATOM 104 CE2 TYR A 39 6.365 122.903 207.478 1.00124.25 C
ANISOU 104 CE2 TYR A 39 21377 12558 13275 1537 1244 1308 C
ATOM 105 CZ TYR A 39 7.067 124.096 207.490 1.00127.73 C
ANISOU 105 CZ TYR A 39 21322 13386 13824 1728 1350 1186 C
ATOM 106 OH TYR A 39 6.489 125.236 207.986 1.00126.18 O
ANISOU 106 OH TYR A 39 20680 13517 13746 1503 1410 1212 O
ATOM 107 N THR A 40 10.022 118.449 203.632 1.00132.84 N
ANISOU 107 N THR A 40 24599 12240 13633 3321 857 768 N
ATOM 108 CA THR A 40 11.148 117.921 202.850 1.00134.49 C
ANISOU 108 CA THR A 40 25056 12396 13648 3912 818 595 C
ATOM 109 C THR A 40 10.835 117.984 201.340 1.00137.79 C
ANISOU 109 C THR A 40 25561 12716 14078 3839 796 451 C
ATOM 110 O THR A 40 11.763 118.105 200.535 1.00137.85 O
ANISOU 110 O THR A 40 25460 12929 13987 4268 839 282 O
ATOM 111 CB THR A 40 11.630 116.546 203.346 1.00142.95 C
ANISOU 111 CB THR A 40 26778 13057 14479 4267 655 636 C
ATOM 112 OG1 THR A 40 12.919 116.273 202.787 1.00141.82 O
ANISOU 112 OG1 THR A 40 26689 13060 14137 4950 662 465 O
ATOM 113 CG2 THR A 40 10.668 115.419 203.016 1.00144.18 C
ANISOU 113 CG2 THR A 40 27654 12578 14548 3989 442 701 C
ATOM 114 N VAL A 41 9.525 117.952 200.976 1.00132.85 N
ANISOU 114 N VAL A 41 25074 11837 13566 3278 738 526 N
ATOM 115 CA VAL A 41 9.028 118.075 199.603 1.00131.59 C
ANISOU 115 CA VAL A 41 24960 11589 13449 3096 720 416 C
ATOM 116 C VAL A 41 9.592 119.377 199.033 1.00131.79 C
ANISOU 116 C VAL A 41 24309 12163 13603 3197 903 297 C
ATOM 117 O VAL A 41 10.140 119.356 197.928 1.00131.58 O
ANISOU 117 O VAL A 41 24293 12195 13507 3437 910 138 O
ATOM 118 CB VAL A 41 7.471 118.012 199.549 1.00134.67 C
ANISOU 118 CB VAL A 41 25488 11726 13954 2411 649 562 C
ATOM 119 CG1 VAL A 41 6.903 118.710 198.310 1.00131.76 C
ANISOU 119 CG1 VAL A 41 24796 11532 13735 2109 723 479 C
ATOM 120 CG2 VAL A 41 6.976 116.573 199.631 1.00138.61 C
ANISOU 120 CG2 VAL A 41 26784 11608 14273 2322 417 629 C
ATOM 121 N ILE A 42 9.529 120.482 199.835 1.00125.11 N
ANISOU 121 N ILE A 42 22896 11718 12922 3033 1036 377 N
ATOM 122 CA ILE A 42 10.046 121.814 199.481 1.00121.54 C
ANISOU 122 CA ILE A 42 21805 11782 12593 3079 1185 296 C
ATOM 123 C ILE A 42 11.545 121.734 199.131 1.00127.08 C
ANISOU 123 C ILE A 42 22427 12737 13121 3679 1221 163 C
ATOM 124 O ILE A 42 11.938 122.158 198.039 1.00126.80 O
ANISOU 124 O ILE A 42 22210 12901 13068 3791 1263 41 O
ATOM 125 CB ILE A 42 9.779 122.914 200.567 1.00121.10 C
ANISOU 125 CB ILE A 42 21240 12060 12713 2828 1283 407 C
ATOM 126 CG1 ILE A 42 8.286 123.070 200.931 1.00119.35 C
ANISOU 126 CG1 ILE A 42 21007 11700 12640 2256 1261 533 C
ATOM 127 CG2 ILE A 42 10.388 124.264 200.146 1.00119.47 C
ANISOU 127 CG2 ILE A 42 20442 12353 12600 2912 1400 323 C
ATOM 128 CD1 ILE A 42 8.038 124.109 202.063 1.00118.73 C
ANISOU 128 CD1 ILE A 42 20483 11938 12691 2082 1337 634 C
ATOM 129 N VAL A 43 12.363 121.181 200.050 1.00124.29 N
ANISOU 129 N VAL A 43 22197 12403 12623 4061 1203 195 N
ATOM 130 CA VAL A 43 13.816 121.078 199.888 1.00125.28 C
ANISOU 130 CA VAL A 43 22212 12839 12548 4658 1239 88 C
ATOM 131 C VAL A 43 14.223 120.346 198.597 1.00132.56 C
ANISOU 131 C VAL A 43 23462 13633 13273 5009 1174 -74 C
ATOM 132 O VAL A 43 15.062 120.859 197.856 1.00132.65 O
ANISOU 132 O VAL A 43 23129 14066 13205 5275 1251 -179 O
ATOM 133 CB VAL A 43 14.532 120.485 201.125 1.00130.41 C
ANISOU 133 CB VAL A 43 23025 13472 13052 5016 1209 155 C
ATOM 134 CG1 VAL A 43 15.892 121.144 201.329 1.00129.86 C
ANISOU 134 CG1 VAL A 43 22489 13979 12872 5448 1311 100 C
ATOM 135 CG2 VAL A 43 13.683 120.623 202.380 1.00128.63 C
ANISOU 135 CG2 VAL A 43 22759 13124 12991 4610 1210 331 C
ATOM 136 N VAL A 44 13.605 119.183 198.316 1.00130.83 N
ANISOU 136 N VAL A 44 23901 12847 12961 4988 1022 -87 N
ATOM 137 CA VAL A 44 13.900 118.348 197.146 1.00132.86 C
ANISOU 137 CA VAL A 44 24578 12895 13009 5332 924 -250 C
ATOM 138 C VAL A 44 13.523 119.036 195.814 1.00135.46 C
ANISOU 138 C VAL A 44 24625 13394 13449 5084 987 -341 C
ATOM 139 O VAL A 44 14.377 119.139 194.928 1.00135.93 O
ANISOU 139 O VAL A 44 24514 13773 13362 5470 1031 -480 O
ATOM 140 CB VAL A 44 13.265 116.943 197.292 1.00139.16 C
ANISOU 140 CB VAL A 44 26206 12990 13680 5321 710 -226 C
ATOM 141 CG1 VAL A 44 13.499 116.089 196.050 1.00142.02 C
ANISOU 141 CG1 VAL A 44 27041 13116 13805 5717 587 -416 C
ATOM 142 CG2 VAL A 44 13.790 116.241 198.535 1.00140.98 C
ANISOU 142 CG2 VAL A 44 26720 13066 13779 5602 641 -135 C
ATOM 143 N THR A 45 12.259 119.504 195.681 1.00129.51 N
ANISOU 143 N THR A 45 23804 12469 12935 4457 993 -256 N
ATOM 144 CA THR A 45 11.753 120.154 194.462 1.00127.39 C
ANISOU 144 CA THR A 45 23297 12322 12785 4174 1042 -327 C
ATOM 145 C THR A 45 12.443 121.508 194.169 1.00129.11 C
ANISOU 145 C THR A 45 22788 13181 13086 4223 1209 -361 C
ATOM 146 O THR A 45 12.570 121.883 192.999 1.00128.10 O
ANISOU 146 O THR A 45 22500 13235 12939 4252 1242 -464 O
ATOM 147 CB THR A 45 10.217 120.272 194.485 1.00132.09 C
ANISOU 147 CB THR A 45 23981 12615 13594 3506 1004 -214 C
ATOM 148 OG1 THR A 45 9.800 120.837 195.724 1.00132.39 O
ANISOU 148 OG1 THR A 45 23704 12798 13800 3214 1072 -57 O
ATOM 149 CG2 THR A 45 9.515 118.940 194.276 1.00131.43 C
ANISOU 149 CG2 THR A 45 24635 11907 13397 3400 813 -193 C
ATOM 150 N SER A 46 12.890 122.233 195.220 1.00124.29 N
ANISOU 150 N SER A 46 21762 12908 12555 4224 1298 -267 N
ATOM 151 CA SER A 46 13.569 123.521 195.054 1.00121.49 C
ANISOU 151 CA SER A 46 20750 13139 12270 4226 1425 -271 C
ATOM 152 C SER A 46 15.035 123.380 194.631 1.00127.64 C
ANISOU 152 C SER A 46 21368 14336 12792 4804 1461 -367 C
ATOM 153 O SER A 46 15.514 124.214 193.865 1.00126.35 O
ANISOU 153 O SER A 46 20743 14630 12635 4791 1537 -394 O
ATOM 154 CB SER A 46 13.450 124.374 196.309 1.00121.70 C
ANISOU 154 CB SER A 46 20426 13340 12473 3969 1482 -135 C
ATOM 155 OG SER A 46 14.291 125.512 196.227 1.00127.32 O
ANISOU 155 OG SER A 46 20574 14604 13196 4045 1571 -132 O
ATOM 156 N VAL A 47 15.752 122.357 195.126 1.00127.27 N
ANISOU 156 N VAL A 47 21678 14171 12506 5304 1401 -405 N
ATOM 157 CA VAL A 47 17.156 122.162 194.750 1.00129.48 C
ANISOU 157 CA VAL A 47 21803 14896 12497 5907 1432 -498 C
ATOM 158 C VAL A 47 17.247 121.578 193.328 1.00136.83 C
ANISOU 158 C VAL A 47 23020 15738 13233 6190 1376 -660 C
ATOM 159 O VAL A 47 17.943 122.146 192.486 1.00136.50 O
ANISOU 159 O VAL A 47 22600 16192 13073 6371 1444 -725 O
ATOM 160 CB VAL A 47 17.993 121.379 195.799 1.00135.32 C
ANISOU 160 CB VAL A 47 22722 15651 13041 6377 1401 -472 C
ATOM 161 CG1 VAL A 47 19.432 121.186 195.325 1.00137.76 C
ANISOU 161 CG1 VAL A 47 22862 16471 13008 7038 1430 -577 C
ATOM 162 CG2 VAL A 47 17.984 122.097 197.145 1.00132.65 C
ANISOU 162 CG2 VAL A 47 22020 15489 12891 6097 1468 -318 C
ATOM 163 N VAL A 48 16.509 120.484 193.054 1.00135.83 N
ANISOU 163 N VAL A 48 23557 14989 13065 6197 1242 -715 N
ATOM 164 CA VAL A 48 16.488 119.826 191.742 1.00138.25 C
ANISOU 164 CA VAL A 48 24228 15117 13183 6454 1159 -881 C
ATOM 165 C VAL A 48 16.106 120.833 190.641 1.00139.25 C
ANISOU 165 C VAL A 48 23940 15502 13466 6078 1244 -903 C
ATOM 166 O VAL A 48 16.953 121.167 189.816 1.00139.22 O
ANISOU 166 O VAL A 48 23618 15984 13296 6375 1307 -989 O
ATOM 167 CB VAL A 48 15.610 118.534 191.740 1.00144.58 C
ANISOU 167 CB VAL A 48 25849 15139 13947 6403 970 -909 C
ATOM 168 CG1 VAL A 48 15.440 117.962 190.331 1.00146.85 C
ANISOU 168 CG1 VAL A 48 26519 15221 14056 6617 870 -1087 C
ATOM 169 CG2 VAL A 48 16.184 117.477 192.681 1.00147.43 C
ANISOU 169 CG2 VAL A 48 26650 15255 14111 6835 867 -891 C
ATOM 170 N GLY A 49 14.880 121.355 190.715 1.00133.10 N
ANISOU 170 N GLY A 49 23122 14457 12992 5434 1250 -808 N
ATOM 171 CA GLY A 49 14.306 122.307 189.770 1.00130.11 C
ANISOU 171 CA GLY A 49 22400 14240 12797 5007 1316 -810 C
ATOM 172 C GLY A 49 15.160 123.514 189.446 1.00131.88 C
ANISOU 172 C GLY A 49 21927 15148 13035 5019 1449 -789 C
ATOM 173 O GLY A 49 15.460 123.750 188.272 1.00131.22 O
ANISOU 173 O GLY A 49 21665 15294 12900 5024 1477 -865 O
ATOM 174 N ASN A 50 15.575 124.273 190.480 1.00127.24 N
ANISOU 174 N ASN A 50 20946 14893 12505 5006 1519 -680 N
ATOM 175 CA ASN A 50 16.385 125.483 190.303 1.00125.66 C
ANISOU 175 CA ASN A 50 20091 15340 12315 4956 1620 -632 C
ATOM 176 C ASN A 50 17.806 125.218 189.778 1.00133.05 C
ANISOU 176 C ASN A 50 20847 16797 12908 5538 1650 -710 C
ATOM 177 O ASN A 50 18.350 126.087 189.092 1.00132.25 O
ANISOU 177 O ASN A 50 20270 17215 12763 5479 1712 -694 O
ATOM 178 CB ASN A 50 16.415 126.339 191.565 1.00123.04 C
ANISOU 178 CB ASN A 50 19403 15171 12175 4669 1666 -485 C
ATOM 179 CG ASN A 50 15.123 127.087 191.796 1.00140.30 C
ANISOU 179 CG ASN A 50 21532 17088 14689 4053 1662 -409 C
ATOM 180 OD1 ASN A 50 14.882 128.166 191.239 1.00129.93 O
ANISOU 180 OD1 ASN A 50 19884 15978 13504 3730 1691 -389 O
ATOM 181 ND2 ASN A 50 14.247 126.511 192.600 1.00132.44 N
ANISOU 181 ND2 ASN A 50 20870 15639 13812 3885 1617 -361 N
ATOM 182 N VAL A 51 18.401 124.037 190.075 1.00132.92 N
ANISOU 182 N VAL A 51 21205 16671 12629 6100 1598 -789 N
ATOM 183 CA VAL A 51 19.739 123.697 189.568 1.00136.03 C
ANISOU 183 CA VAL A 51 21449 17590 12646 6728 1619 -877 C
ATOM 184 C VAL A 51 19.634 123.397 188.064 1.00142.49 C
ANISOU 184 C VAL A 51 22410 18417 13311 6887 1592 -1023 C
ATOM 185 O VAL A 51 20.485 123.849 187.296 1.00143.98 O
ANISOU 185 O VAL A 51 22213 19221 13273 7151 1649 -1058 O
ATOM 186 CB VAL A 51 20.471 122.594 190.390 1.00142.70 C
ANISOU 186 CB VAL A 51 22619 18366 13235 7325 1567 -917 C
ATOM 187 CG1 VAL A 51 21.714 122.078 189.670 1.00146.45 C
ANISOU 187 CG1 VAL A 51 23025 19346 13273 8044 1571 -1044 C
ATOM 188 CG2 VAL A 51 20.852 123.111 191.770 1.00140.76 C
ANISOU 188 CG2 VAL A 51 22052 18328 13104 7189 1622 -764 C
ATOM 189 N VAL A 52 18.552 122.699 187.647 1.00138.61 N
ANISOU 189 N VAL A 52 22433 17282 12952 6666 1506 -1092 N
ATOM 190 CA VAL A 52 18.265 122.378 186.240 1.00139.44 C
ANISOU 190 CA VAL A 52 22717 17317 12948 6745 1468 -1232 C
ATOM 191 C VAL A 52 18.046 123.697 185.466 1.00139.70 C
ANISOU 191 C VAL A 52 22165 17760 13154 6281 1567 -1161 C
ATOM 192 O VAL A 52 18.606 123.854 184.378 1.00141.15 O
ANISOU 192 O VAL A 52 22094 18413 13123 6526 1604 -1229 O
ATOM 193 CB VAL A 52 17.089 121.366 186.074 1.00144.08 C
ANISOU 193 CB VAL A 52 24035 17096 13614 6609 1328 -1314 C
ATOM 194 CG1 VAL A 52 16.769 121.111 184.602 1.00145.24 C
ANISOU 194 CG1 VAL A 52 24342 17197 13644 6684 1287 -1463 C
ATOM 195 CG2 VAL A 52 17.389 120.046 186.777 1.00147.37 C
ANISOU 195 CG2 VAL A 52 25063 17108 13823 7089 1202 -1378 C
ATOM 196 N VAL A 53 17.287 124.653 186.057 1.00131.36 N
ANISOU 196 N VAL A 53 20892 16562 12458 5643 1603 -1019 N
ATOM 197 CA VAL A 53 17.047 125.980 185.476 1.00128.01 C
ANISOU 197 CA VAL A 53 19944 16475 12220 5168 1676 -934 C
ATOM 198 C VAL A 53 18.397 126.719 185.339 1.00134.24 C
ANISOU 198 C VAL A 53 20132 18056 12817 5375 1754 -870 C
ATOM 199 O VAL A 53 18.689 127.234 184.255 1.00133.96 O
ANISOU 199 O VAL A 53 19763 18421 12716 5291 1790 -869 O
ATOM 200 CB VAL A 53 15.969 126.806 186.245 1.00127.18 C
ANISOU 200 CB VAL A 53 19752 16071 12501 4529 1681 -800 C
ATOM 201 CG1 VAL A 53 15.920 128.259 185.779 1.00123.94 C
ANISOU 201 CG1 VAL A 53 18783 16058 12251 4103 1737 -700 C
ATOM 202 CG2 VAL A 53 14.592 126.176 186.104 1.00126.21 C
ANISOU 202 CG2 VAL A 53 20126 15286 12542 4250 1608 -846 C
ATOM 203 N MET A 54 19.234 126.712 186.410 1.00132.54 N
ANISOU 203 N MET A 54 19784 18083 12494 5636 1774 -810 N
ATOM 204 CA MET A 54 20.564 127.339 186.407 1.00134.05 C
ANISOU 204 CA MET A 54 19411 19053 12468 5834 1836 -733 C
ATOM 205 C MET A 54 21.418 126.761 185.282 1.00143.19 C
ANISOU 205 C MET A 54 20526 20647 13234 6375 1848 -853 C
ATOM 206 O MET A 54 22.064 127.514 184.550 1.00143.48 O
ANISOU 206 O MET A 54 20062 21313 13139 6318 1896 -793 O
ATOM 207 CB MET A 54 21.276 127.126 187.748 1.00137.24 C
ANISOU 207 CB MET A 54 19776 19570 12799 6082 1843 -669 C
ATOM 208 CG MET A 54 21.061 128.240 188.729 1.00137.69 C
ANISOU 208 CG MET A 54 19523 19650 13144 5571 1860 -503 C
ATOM 209 SD MET A 54 22.058 127.994 190.214 1.00143.33 S
ANISOU 209 SD MET A 54 20051 20711 13695 5907 1879 -421 S
ATOM 210 CE MET A 54 23.330 129.203 189.946 1.00141.02 C
ANISOU 210 CE MET A 54 19019 21388 13175 5892 1927 -310 C
ATOM 211 N TRP A 55 21.371 125.420 185.127 1.00143.68 N
ANISOU 211 N TRP A 55 21137 20360 13095 6892 1787 -1021 N
ATOM 212 CA TRP A 55 22.087 124.657 184.111 1.00148.15 C
ANISOU 212 CA TRP A 55 21790 21246 13253 7513 1774 -1178 C
ATOM 213 C TRP A 55 21.648 125.048 182.694 1.00150.17 C
ANISOU 213 C TRP A 55 21947 21583 13528 7294 1784 -1231 C
ATOM 214 O TRP A 55 22.499 125.481 181.926 1.00151.53 O
ANISOU 214 O TRP A 55 21678 22456 13442 7486 1838 -1222 O
ATOM 215 CB TRP A 55 21.934 123.150 184.368 1.00150.78 C
ANISOU 215 CB TRP A 55 22845 21036 13410 8061 1668 -1348 C
ATOM 216 CG TRP A 55 22.641 122.281 183.373 1.00156.82 C
ANISOU 216 CG TRP A 55 23803 22037 13744 8750 1625 -1543 C
ATOM 217 CD1 TRP A 55 23.935 121.849 183.429 1.00163.82 C
ANISOU 217 CD1 TRP A 55 24505 23545 14194 9448 1645 -1603 C
ATOM 218 CD2 TRP A 55 22.081 121.722 182.179 1.00158.12 C
ANISOU 218 CD2 TRP A 55 24410 21819 13850 8841 1544 -1713 C
ATOM 219 NE1 TRP A 55 24.219 121.061 182.337 1.00167.10 N
ANISOU 219 NE1 TRP A 55 25221 23998 14273 9995 1580 -1809 N
ATOM 220 CE2 TRP A 55 23.099 120.966 181.552 1.00166.91 C
ANISOU 220 CE2 TRP A 55 25595 23345 14478 9629 1514 -1882 C
ATOM 221 CE3 TRP A 55 20.811 121.781 181.577 1.00157.16 C
ANISOU 221 CE3 TRP A 55 24625 21066 14022 8338 1489 -1741 C
ATOM 222 CZ2 TRP A 55 22.888 120.280 180.350 1.00168.74 C
ANISOU 222 CZ2 TRP A 55 26245 23351 14517 9931 1424 -2086 C
ATOM 223 CZ3 TRP A 55 20.605 121.107 180.384 1.00161.26 C
ANISOU 223 CZ3 TRP A 55 25548 21363 14360 8604 1403 -1932 C
ATOM 224 CH2 TRP A 55 21.635 120.367 179.783 1.00166.68 C
ANISOU 224 CH2 TRP A 55 26319 22441 14569 9394 1367 -2106 C
ATOM 225 N ILE A 56 20.329 124.952 182.374 1.00143.52 N
ANISOU 225 N ILE A 56 21475 20076 12981 6868 1733 -1268 N
ATOM 226 CA ILE A 56 19.731 125.300 181.071 1.00142.09 C
ANISOU 226 CA ILE A 56 21250 19879 12857 6608 1735 -1319 C
ATOM 227 C ILE A 56 20.300 126.622 180.509 1.00146.72 C
ANISOU 227 C ILE A 56 21109 21215 13423 6340 1826 -1183 C
ATOM 228 O ILE A 56 20.822 126.624 179.394 1.00148.19 O
ANISOU 228 O ILE A 56 21111 21848 13346 6587 1847 -1248 O
ATOM 229 CB ILE A 56 18.167 125.285 181.143 1.00141.23 C
ANISOU 229 CB ILE A 56 21530 18997 13134 6043 1679 -1316 C
ATOM 230 CG1 ILE A 56 17.638 123.839 181.211 1.00143.26 C
ANISOU 230 CG1 ILE A 56 22556 18554 13323 6334 1558 -1466 C
ATOM 231 CG2 ILE A 56 17.516 126.055 179.975 1.00139.43 C
ANISOU 231 CG2 ILE A 56 21122 18831 13025 5651 1699 -1320 C
ATOM 232 CD1 ILE A 56 16.235 123.696 181.686 1.00143.50 C
ANISOU 232 CD1 ILE A 56 22958 17871 13693 5802 1497 -1425 C
ATOM 233 N ILE A 57 20.258 127.712 181.307 1.00142.06 N
ANISOU 233 N ILE A 57 20122 20778 13078 5861 1866 -991 N
ATOM 234 CA ILE A 57 20.733 129.046 180.915 1.00141.24 C
ANISOU 234 CA ILE A 57 19370 21312 12984 5511 1918 -829 C
ATOM 235 C ILE A 57 22.281 129.156 180.875 1.00151.22 C
ANISOU 235 C ILE A 57 20169 23447 13841 5944 1965 -778 C
ATOM 236 O ILE A 57 22.816 129.436 179.800 1.00152.64 O
ANISOU 236 O ILE A 57 20037 24169 13789 6032 1992 -774 O
ATOM 237 CB ILE A 57 20.081 130.158 181.787 1.00139.74 C
ANISOU 237 CB ILE A 57 18984 20928 13181 4861 1911 -655 C
ATOM 238 CG1 ILE A 57 18.550 130.167 181.607 1.00137.23 C
ANISOU 238 CG1 ILE A 57 19048 19872 13223 4430 1871 -700 C
ATOM 239 CG2 ILE A 57 20.676 131.547 181.492 1.00138.66 C
ANISOU 239 CG2 ILE A 57 18219 21434 13032 4494 1930 -473 C
ATOM 240 CD1 ILE A 57 17.752 130.303 182.899 1.00143.20 C
ANISOU 240 CD1 ILE A 57 19939 20171 14301 4084 1846 -621 C
ATOM 241 N LEU A 58 22.979 128.971 182.029 1.00150.79 N
ANISOU 241 N LEU A 58 20042 23562 13690 6192 1975 -726 N
ATOM 242 CA LEU A 58 24.442 129.109 182.174 1.00154.60 C
ANISOU 242 CA LEU A 58 20058 24900 13784 6583 2017 -656 C
ATOM 243 C LEU A 58 25.295 128.353 181.116 1.00166.88 C
ANISOU 243 C LEU A 58 21588 26957 14861 7252 2037 -798 C
ATOM 244 O LEU A 58 26.359 128.846 180.725 1.00169.03 O
ANISOU 244 O LEU A 58 21310 28095 14817 7385 2080 -701 O
ATOM 245 CB LEU A 58 24.900 128.735 183.590 1.00154.78 C
ANISOU 245 CB LEU A 58 20165 24862 13783 6828 2014 -627 C
ATOM 246 CG LEU A 58 24.731 129.826 184.630 1.00155.70 C
ANISOU 246 CG LEU A 58 20012 24942 14205 6261 2009 -432 C
ATOM 247 N ALA A 59 24.837 127.169 180.672 1.00167.80 N
ANISOU 247 N ALA A 59 22303 26553 14902 7677 1992 -1021 N
ATOM 248 CA ALA A 59 25.491 126.326 179.659 1.00173.33 C
ANISOU 248 CA ALA A 59 23108 27595 15154 8366 1986 -1202 C
ATOM 249 C ALA A 59 24.422 125.353 179.139 1.00179.82 C
ANISOU 249 C ALA A 59 24647 27568 16107 8439 1904 -1410 C
ATOM 250 O ALA A 59 23.818 124.679 179.968 1.00178.52 O
ANISOU 250 O ALA A 59 25007 26660 16161 8394 1841 -1461 O
ATOM 251 CB ALA A 59 26.659 125.553 180.275 1.00178.15 C
ANISOU 251 CB ALA A 59 23748 28577 15365 9120 1984 -1269 C
ATOM 252 N HIS A 60 24.063 125.305 177.839 1.00178.54 N
ANISOU 252 N HIS A 60 24529 27457 15852 8459 1895 -1512 N
ATOM 253 CA HIS A 60 24.558 125.870 176.574 1.00180.96 C
ANISOU 253 CA HIS A 60 24347 28531 15879 8540 1950 -1495 C
ATOM 254 C HIS A 60 25.121 127.308 176.544 1.00185.33 C
ANISOU 254 C HIS A 60 24101 29842 16474 8031 2034 -1230 C
ATOM 255 O HIS A 60 26.176 127.493 175.933 1.00188.24 O
ANISOU 255 O HIS A 60 24005 30955 16563 8163 2080 -1195 O
ATOM 256 CB HIS A 60 23.455 125.784 175.499 1.00180.55 C
ANISOU 256 CB HIS A 60 24625 28013 15963 8334 1907 -1621 C
ATOM 257 CG HIS A 60 22.074 125.614 176.046 1.00180.60 C
ANISOU 257 CG HIS A 60 25252 26982 16385 7974 1830 -1679 C
ATOM 258 ND1 HIS A 60 21.650 124.401 176.559 1.00184.35 N
ANISOU 258 ND1 HIS A 60 26456 26818 16771 8413 1722 -1891 N
ATOM 259 CD2 HIS A 60 21.067 126.509 176.146 1.00177.64 C
ANISOU 259 CD2 HIS A 60 24856 26161 16479 7236 1837 -1540 C
ATOM 260 CE1 HIS A 60 20.404 124.596 176.952 1.00180.56 C
ANISOU 260 CE1 HIS A 60 26347 25552 16706 7888 1673 -1860 C
ATOM 261 NE2 HIS A 60 20.009 125.849 176.723 1.00176.80 N
ANISOU 261 NE2 HIS A 60 25428 25178 16570 7195 1746 -1657 N
ATOM 262 N LYS A 61 24.408 128.316 177.103 1.00176.65 N
ANISOU 262 N LYS A 61 22868 28428 15822 7278 2038 -1051 N
ATOM 263 CA LYS A 61 24.789 129.744 177.049 1.00174.33 C
ANISOU 263 CA LYS A 61 21910 28713 15614 6704 2077 -794 C
ATOM 264 C LYS A 61 24.604 130.316 175.619 1.00176.81 C
ANISOU 264 C LYS A 61 21993 29290 15896 6428 2087 -769 C
ATOM 265 O LYS A 61 25.174 131.353 175.261 1.00176.65 O
ANISOU 265 O LYS A 61 21388 29962 15769 6125 2111 -573 O
ATOM 266 CB LYS A 61 26.188 130.034 177.641 1.00179.50 C
ANISOU 266 CB LYS A 61 22016 30252 15935 6940 2117 -646 C
ATOM 267 N ARG A 62 23.776 129.618 174.818 1.00171.36 N
ANISOU 267 N ARG A 62 21787 28023 15299 6509 2058 -961 N
ATOM 268 CA ARG A 62 23.322 129.998 173.484 1.00169.78 C
ANISOU 268 CA ARG A 62 21502 27877 15128 6244 2058 -973 C
ATOM 269 C ARG A 62 21.915 130.591 173.722 1.00167.36 C
ANISOU 269 C ARG A 62 21434 26802 15355 5540 2020 -918 C
ATOM 270 O ARG A 62 21.244 131.047 172.797 1.00164.79 O
ANISOU 270 O ARG A 62 21096 26350 15168 5189 2010 -913 O
ATOM 271 CB ARG A 62 23.255 128.757 172.581 1.00172.80 C
ANISOU 271 CB ARG A 62 22306 28117 15234 6852 2037 -1242 C
ATOM 272 N MET A 63 21.504 130.572 175.013 1.00161.56 N
ANISOU 272 N MET A 63 20898 25593 14896 5363 1999 -874 N
ATOM 273 CA MET A 63 20.259 131.060 175.608 1.00156.52 C
ANISOU 273 CA MET A 63 20474 24261 14734 4769 1962 -815 C
ATOM 274 C MET A 63 20.570 132.095 176.701 1.00155.66 C
ANISOU 274 C MET A 63 20005 24347 14793 4393 1961 -600 C
ATOM 275 O MET A 63 19.660 132.520 177.418 1.00151.89 O
ANISOU 275 O MET A 63 19681 23350 14680 3963 1928 -547 O
ATOM 276 CB MET A 63 19.499 129.885 176.244 1.00158.67 C
ANISOU 276 CB MET A 63 21409 23738 15142 4979 1920 -987 C
ATOM 277 CG MET A 63 18.268 129.492 175.487 1.00161.57 C
ANISOU 277 CG MET A 63 22186 23547 15656 4826 1880 -1120 C
ATOM 278 SD MET A 63 16.958 128.997 176.619 1.00163.24 S
ANISOU 278 SD MET A 63 22967 22799 16258 4522 1819 -1156 S
ATOM 279 CE MET A 63 16.084 130.565 176.798 1.00155.38 C
ANISOU 279 CE MET A 63 21592 21775 15669 3715 1832 -951 C
ATOM 280 N ARG A 64 21.853 132.484 176.837 1.00152.43 N
ANISOU 280 N ARG A 64 19111 24709 14095 4557 1990 -477 N
ATOM 281 CA ARG A 64 22.302 133.453 177.831 1.00150.34 C
ANISOU 281 CA ARG A 64 18472 24733 13919 4233 1974 -268 C
ATOM 282 C ARG A 64 21.891 134.901 177.473 1.00150.24 C
ANISOU 282 C ARG A 64 18144 24796 14143 3513 1922 -74 C
ATOM 283 O ARG A 64 22.674 135.636 176.866 1.00151.44 O
ANISOU 283 O ARG A 64 17805 25640 14096 3351 1911 94 O
ATOM 284 CB ARG A 64 23.815 133.312 178.077 1.00153.96 C
ANISOU 284 CB ARG A 64 18526 26030 13941 4671 2013 -202 C
ATOM 285 N THR A 65 20.643 135.294 177.841 1.00141.94 N
ANISOU 285 N THR A 65 17391 23038 13500 3087 1878 -95 N
ATOM 286 CA THR A 65 20.073 136.642 177.611 1.00138.25 C
ANISOU 286 CA THR A 65 16735 22500 13292 2429 1805 61 C
ATOM 287 C THR A 65 20.035 137.455 178.922 1.00138.22 C
ANISOU 287 C THR A 65 16671 22323 13525 2087 1739 190 C
ATOM 288 O THR A 65 20.223 136.881 179.999 1.00137.63 O
ANISOU 288 O THR A 65 16793 22010 13491 2327 1762 129 O
ATOM 289 CB THR A 65 18.692 136.592 176.891 1.00141.61 C
ANISOU 289 CB THR A 65 17482 22361 13963 2199 1793 -47 C
ATOM 290 OG1 THR A 65 17.630 136.332 177.816 1.00136.98 O
ANISOU 290 OG1 THR A 65 17329 21046 13670 2148 1783 -149 O
ATOM 291 CG2 THR A 65 18.652 135.605 175.733 1.00142.68 C
ANISOU 291 CG2 THR A 65 17718 22630 13862 2553 1847 -192 C
ATOM 292 N VAL A 66 19.786 138.779 178.831 1.00131.48 N
ANISOU 292 N VAL A 66 15572 21571 12815 1539 1645 365 N
ATOM 293 CA VAL A 66 19.738 139.672 179.996 1.00128.65 C
ANISOU 293 CA VAL A 66 15150 21069 12661 1187 1552 491 C
ATOM 294 C VAL A 66 18.623 139.246 180.961 1.00127.12 C
ANISOU 294 C VAL A 66 15387 20135 12776 1205 1559 361 C
ATOM 295 O VAL A 66 18.865 139.211 182.166 1.00126.44 O
ANISOU 295 O VAL A 66 15321 19989 12733 1275 1548 385 O
ATOM 296 CB VAL A 66 19.682 141.177 179.608 1.00132.00 C
ANISOU 296 CB VAL A 66 15323 21652 13179 595 1416 683 C
ATOM 297 CG1 VAL A 66 19.647 142.080 180.842 1.00130.07 C
ANISOU 297 CG1 VAL A 66 15088 21186 13148 258 1294 786 C
ATOM 298 CG2 VAL A 66 20.865 141.555 178.713 1.00134.97 C
ANISOU 298 CG2 VAL A 66 15232 22841 13209 554 1399 852 C
ATOM 299 N THR A 67 17.446 138.851 180.433 1.00120.05 N
ANISOU 299 N THR A 67 14822 18726 12065 1161 1581 229 N
ATOM 300 CA THR A 67 16.321 138.375 181.247 1.00116.94 C
ANISOU 300 CA THR A 67 14826 17674 11933 1161 1589 118 C
ATOM 301 C THR A 67 16.666 137.048 181.942 1.00121.39 C
ANISOU 301 C THR A 67 15624 18125 12375 1654 1670 4 C
ATOM 302 O THR A 67 16.419 136.916 183.146 1.00120.89 O
ANISOU 302 O THR A 67 15697 17799 12438 1666 1660 6 O
ATOM 303 CB THR A 67 15.024 138.337 180.419 1.00121.45 C
ANISOU 303 CB THR A 67 15643 17811 12690 957 1583 29 C
ATOM 304 OG1 THR A 67 14.448 139.646 180.424 1.00121.00 O
ANISOU 304 OG1 THR A 67 15465 17674 12836 480 1481 134 O
ATOM 305 CG2 THR A 67 13.997 137.335 180.947 1.00116.00 C
ANISOU 305 CG2 THR A 67 15392 16531 12153 1087 1622 -113 C
ATOM 306 N ASN A 68 17.262 136.095 181.202 1.00118.68 N
ANISOU 306 N ASN A 68 15336 17988 11769 2072 1738 -93 N
ATOM 307 CA ASN A 68 17.634 134.784 181.736 1.00119.57 C
ANISOU 307 CA ASN A 68 15717 17991 11722 2591 1793 -213 C
ATOM 308 C ASN A 68 18.817 134.826 182.725 1.00123.30 C
ANISOU 308 C ASN A 68 15947 18880 12022 2825 1804 -127 C
ATOM 309 O ASN A 68 18.793 134.081 183.711 1.00123.43 O
ANISOU 309 O ASN A 68 16217 18656 12024 3119 1824 -192 O
ATOM 310 CB ASN A 68 17.872 133.778 180.612 1.00121.43 C
ANISOU 310 CB ASN A 68 16112 18319 11706 2997 1837 -357 C
ATOM 311 CG ASN A 68 16.637 133.453 179.805 1.00141.51 C
ANISOU 311 CG ASN A 68 18990 20366 14412 2827 1823 -468 C
ATOM 312 OD1 ASN A 68 16.691 133.345 178.578 1.00142.29 O
ANISOU 312 OD1 ASN A 68 19014 20658 14390 2850 1833 -510 O
ATOM 313 ND2 ASN A 68 15.492 133.299 180.462 1.00127.32 N
ANISOU 313 ND2 ASN A 68 17552 17951 12873 2648 1797 -511 N
ATOM 314 N TYR A 69 19.824 135.708 182.489 1.00118.86 N
ANISOU 314 N TYR A 69 14901 18934 11326 2662 1781 30 N
ATOM 315 CA TYR A 69 20.979 135.876 183.385 1.00119.14 C
ANISOU 315 CA TYR A 69 14644 19435 11190 2807 1779 139 C
ATOM 316 C TYR A 69 20.521 136.347 184.774 1.00118.27 C
ANISOU 316 C TYR A 69 14640 18951 11347 2571 1731 190 C
ATOM 317 O TYR A 69 21.105 135.931 185.771 1.00119.01 O
ANISOU 317 O TYR A 69 14719 19160 11340 2838 1751 200 O
ATOM 318 CB TYR A 69 22.033 136.818 182.786 1.00121.66 C
ANISOU 318 CB TYR A 69 14425 20482 11320 2567 1739 324 C
ATOM 319 N PHE A 70 19.438 137.159 184.840 1.00109.92 N
ANISOU 319 N PHE A 70 13685 17467 10611 2095 1665 218 N
ATOM 320 CA PHE A 70 18.832 137.597 186.100 1.00106.30 C
ANISOU 320 CA PHE A 70 13350 16629 10410 1871 1612 250 C
ATOM 321 C PHE A 70 18.086 136.446 186.736 1.00107.96 C
ANISOU 321 C PHE A 70 14002 16292 10725 2126 1667 111 C
ATOM 322 O PHE A 70 18.206 136.255 187.943 1.00107.00 O
ANISOU 322 O PHE A 70 13958 16026 10672 2186 1661 128 O
ATOM 323 CB PHE A 70 17.885 138.782 185.900 1.00105.18 C
ANISOU 323 CB PHE A 70 13182 16247 10536 1334 1513 312 C
ATOM 324 CG PHE A 70 18.603 140.100 185.888 1.00107.17 C
ANISOU 324 CG PHE A 70 13044 16951 10726 1000 1407 486 C
ATOM 325 CD1 PHE A 70 19.349 140.514 186.986 1.00111.08 C
ANISOU 325 CD1 PHE A 70 13339 17707 11159 968 1351 594 C
ATOM 326 CD2 PHE A 70 18.540 140.932 184.779 1.00109.00 C
ANISOU 326 CD2 PHE A 70 13123 17336 10955 688 1346 553 C
ATOM 327 CE1 PHE A 70 20.043 141.725 186.961 1.00112.83 C
ANISOU 327 CE1 PHE A 70 13225 18341 11305 616 1226 770 C
ATOM 328 CE2 PHE A 70 19.225 142.146 184.758 1.00112.65 C
ANISOU 328 CE2 PHE A 70 13255 18201 11345 337 1221 736 C
ATOM 329 CZ PHE A 70 19.972 142.535 185.849 1.00111.79 C
ANISOU 329 CZ PHE A 70 12963 18347 11167 292 1155 846 C
ATOM 330 N LEU A 71 17.344 135.654 185.918 1.00103.40 N
ANISOU 330 N LEU A 71 13724 15417 10146 2265 1711 -17 N
ATOM 331 CA LEU A 71 16.605 134.468 186.367 1.00102.21 C
ANISOU 331 CA LEU A 71 14034 14739 10062 2482 1741 -137 C
ATOM 332 C LEU A 71 17.532 133.447 187.045 1.00108.88 C
ANISOU 332 C LEU A 71 14974 15729 10668 3003 1783 -176 C
ATOM 333 O LEU A 71 17.085 132.756 187.965 1.00107.32 O
ANISOU 333 O LEU A 71 15119 15123 10534 3141 1785 -226 O
ATOM 334 CB LEU A 71 15.843 133.800 185.207 1.00101.56 C
ANISOU 334 CB LEU A 71 14250 14341 9996 2494 1755 -257 C
ATOM 335 CG LEU A 71 14.591 134.475 184.655 1.00102.05 C
ANISOU 335 CG LEU A 71 14301 14180 10295 2022 1717 -242 C
ATOM 336 CD1 LEU A 71 13.760 133.475 183.898 1.00102.01 C
ANISOU 336 CD1 LEU A 71 14646 13829 10284 2087 1730 -370 C
ATOM 337 CD2 LEU A 71 13.737 135.076 185.748 1.00100.52 C
ANISOU 337 CD2 LEU A 71 14163 13655 10375 1683 1673 -186 C
ATOM 338 N VAL A 72 18.817 133.363 186.585 1.00108.82 N
ANISOU 338 N VAL A 72 14649 16328 10369 3284 1810 -142 N
ATOM 339 CA VAL A 72 19.859 132.494 187.146 1.00112.08 C
ANISOU 339 CA VAL A 72 15074 17006 10507 3814 1846 -169 C
ATOM 340 C VAL A 72 20.171 132.933 188.576 1.00115.81 C
ANISOU 340 C VAL A 72 15416 17512 11075 3715 1827 -64 C
ATOM 341 O VAL A 72 20.338 132.073 189.450 1.00116.79 O
ANISOU 341 O VAL A 72 15782 17451 11141 4041 1842 -108 O
ATOM 342 CB VAL A 72 21.125 132.388 186.237 1.00119.36 C
ANISOU 342 CB VAL A 72 15648 18646 11059 4138 1880 -159 C
ATOM 343 CG1 VAL A 72 22.414 132.159 187.037 1.00121.64 C
ANISOU 343 CG1 VAL A 72 15715 19424 11077 4530 1904 -109 C
ATOM 344 CG2 VAL A 72 20.953 131.283 185.213 1.00121.31 C
ANISOU 344 CG2 VAL A 72 16191 18775 11126 4511 1904 -325 C
ATOM 345 N ASN A 73 20.230 134.267 188.813 1.00110.63 N
ANISOU 345 N ASN A 73 14412 17057 10566 3258 1779 72 N
ATOM 346 CA ASN A 73 20.494 134.835 190.143 1.00109.50 C
ANISOU 346 CA ASN A 73 14133 16948 10525 3108 1741 172 C
ATOM 347 C ASN A 73 19.358 134.499 191.115 1.00109.96 C
ANISOU 347 C ASN A 73 14562 16354 10862 2972 1726 125 C
ATOM 348 O ASN A 73 19.615 134.152 192.267 1.00109.44 O
ANISOU 348 O ASN A 73 14540 16221 10820 3071 1724 154 O
ATOM 349 CB ASN A 73 20.742 136.349 190.079 1.00109.20 C
ANISOU 349 CB ASN A 73 13682 17257 10551 2645 1660 321 C
ATOM 350 CG ASN A 73 21.218 136.925 191.392 1.00121.04 C
ANISOU 350 CG ASN A 73 14990 18938 12062 2563 1609 427 C
ATOM 351 OD1 ASN A 73 22.137 136.398 192.029 1.00109.46 O
ANISOU 351 OD1 ASN A 73 13462 17731 10397 2929 1653 433 O
ATOM 352 ND2 ASN A 73 20.587 138.003 191.836 1.00109.53 N
ANISOU 352 ND2 ASN A 73 13450 17343 10825 2101 1507 505 N
ATOM 353 N LEU A 74 18.115 134.565 190.616 1.00104.07 N
ANISOU 353 N LEU A 74 14063 15167 10310 2741 1717 61 N
ATOM 354 CA LEU A 74 16.883 134.225 191.315 1.00101.88 C
ANISOU 354 CA LEU A 74 14131 14308 10269 2589 1705 21 C
ATOM 355 C LEU A 74 16.821 132.702 191.582 1.00108.26 C
ANISOU 355 C LEU A 74 15350 14822 10963 2999 1747 -69 C
ATOM 356 O LEU A 74 16.318 132.295 192.624 1.00107.02 O
ANISOU 356 O LEU A 74 15406 14349 10906 2996 1739 -58 O
ATOM 357 CB LEU A 74 15.683 134.721 190.470 1.00 99.73 C
ANISOU 357 CB LEU A 74 13941 13752 10198 2207 1676 -7 C
ATOM 358 CG LEU A 74 14.282 134.172 190.756 1.00102.76 C
ANISOU 358 CG LEU A 74 14711 13568 10766 2075 1674 -65 C
ATOM 359 CD1 LEU A 74 13.677 134.803 191.985 1.00101.20 C
ANISOU 359 CD1 LEU A 74 14516 13191 10745 1882 1640 -5 C
ATOM 360 CD2 LEU A 74 13.381 134.405 189.579 1.00104.07 C
ANISOU 360 CD2 LEU A 74 14911 13578 11053 1777 1655 -100 C
ATOM 361 N ALA A 75 17.344 131.874 190.655 1.00108.55 N
ANISOU 361 N ALA A 75 15504 14970 10769 3361 1778 -156 N
ATOM 362 CA ALA A 75 17.383 130.415 190.807 1.00111.17 C
ANISOU 362 CA ALA A 75 16273 15018 10950 3794 1786 -250 C
ATOM 363 C ALA A 75 18.383 130.023 191.895 1.00117.99 C
ANISOU 363 C ALA A 75 17070 16113 11646 4160 1801 -212 C
ATOM 364 O ALA A 75 18.110 129.098 192.664 1.00118.21 O
ANISOU 364 O ALA A 75 17467 15784 11665 4355 1785 -237 O
ATOM 365 CB ALA A 75 17.747 129.750 189.489 1.00114.23 C
ANISOU 365 CB ALA A 75 16791 15501 11111 4112 1797 -366 C
ATOM 366 N PHE A 76 19.524 130.751 191.976 1.00116.36 N
ANISOU 366 N PHE A 76 16394 16518 11300 4228 1823 -138 N
ATOM 367 CA PHE A 76 20.548 130.527 192.993 1.00118.48 C
ANISOU 367 CA PHE A 76 16520 17100 11396 4549 1838 -88 C
ATOM 368 C PHE A 76 19.982 130.852 194.370 1.00121.02 C
ANISOU 368 C PHE A 76 16903 17133 11945 4305 1814 -13 C
ATOM 369 O PHE A 76 20.006 129.994 195.248 1.00121.44 O
ANISOU 369 O PHE A 76 17236 16961 11944 4584 1815 -32 O
ATOM 370 CB PHE A 76 21.829 131.350 192.726 1.00121.81 C
ANISOU 370 CB PHE A 76 16384 18278 11620 4579 1853 1 C
ATOM 371 CG PHE A 76 22.852 131.197 193.834 1.00125.56 C
ANISOU 371 CG PHE A 76 16682 19096 11928 4860 1864 66 C
ATOM 372 CD1 PHE A 76 23.668 130.069 193.901 1.00132.21 C
ANISOU 372 CD1 PHE A 76 17668 20105 12462 5478 1895 -5 C
ATOM 373 CD2 PHE A 76 22.954 132.147 194.846 1.00126.48 C
ANISOU 373 CD2 PHE A 76 16524 19343 12191 4526 1831 190 C
ATOM 374 CE1 PHE A 76 24.577 129.902 194.954 1.00134.56 C
ANISOU 374 CE1 PHE A 76 17806 20722 12600 5750 1905 55 C
ATOM 375 CE2 PHE A 76 23.863 131.980 195.898 1.00130.72 C
ANISOU 375 CE2 PHE A 76 16904 20189 12573 4778 1838 249 C
ATOM 376 CZ PHE A 76 24.672 130.861 195.940 1.00131.88 C
ANISOU 376 CZ PHE A 76 17167 20526 12415 5385 1881 186 C
ATOM 377 N ALA A 77 19.477 132.094 194.547 1.00115.69 N
ANISOU 377 N ALA A 77 15982 16465 11510 3800 1782 69 N
ATOM 378 CA ALA A 77 18.878 132.608 195.783 1.00113.57 C
ANISOU 378 CA ALA A 77 15727 15963 11461 3533 1750 135 C
ATOM 379 C ALA A 77 17.809 131.657 196.338 1.00117.90 C
ANISOU 379 C ALA A 77 16748 15914 12134 3548 1750 88 C
ATOM 380 O ALA A 77 17.822 131.363 197.537 1.00117.36 O
ANISOU 380 O ALA A 77 16779 15722 12091 3628 1747 128 O
ATOM 381 CB ALA A 77 18.289 133.992 195.542 1.00111.52 C
ANISOU 381 CB ALA A 77 15214 15739 11419 3016 1694 194 C
ATOM 382 N ASP A 78 16.927 131.137 195.446 1.00115.00 N
ANISOU 382 N ASP A 78 16670 15199 11827 3464 1748 14 N
ATOM 383 CA ASP A 78 15.862 130.191 195.776 1.00114.86 C
ANISOU 383 CA ASP A 78 17121 14623 11899 3428 1731 -19 C
ATOM 384 C ASP A 78 16.445 128.875 196.295 1.00121.53 C
ANISOU 384 C ASP A 78 18290 15345 12540 3895 1731 -45 C
ATOM 385 O ASP A 78 16.266 128.577 197.473 1.00121.34 O
ANISOU 385 O ASP A 78 18391 15150 12563 3902 1719 14 O
ATOM 386 CB ASP A 78 14.894 129.976 194.585 1.00116.52 C
ANISOU 386 CB ASP A 78 17550 14554 12167 3258 1718 -94 C
ATOM 387 CG ASP A 78 13.868 131.087 194.328 1.00124.71 C
ANISOU 387 CG ASP A 78 18441 15490 13454 2749 1701 -64 C
ATOM 388 OD1 ASP A 78 13.835 132.071 195.110 1.00123.58 O
ANISOU 388 OD1 ASP A 78 18099 15395 13460 2508 1686 9 O
ATOM 389 OD2 ASP A 78 13.096 130.969 193.348 1.00129.73 O
ANISOU 389 OD2 ASP A 78 19177 15992 14121 2611 1694 -122 O
ATOM 390 N ALA A 79 17.211 128.138 195.467 1.00120.69 N
ANISOU 390 N ALA A 79 18307 15362 12189 4310 1738 -132 N
ATOM 391 CA ALA A 79 17.838 126.869 195.872 1.00123.54 C
ANISOU 391 CA ALA A 79 19014 15612 12315 4826 1718 -176 C
ATOM 392 C ALA A 79 18.700 126.985 197.162 1.00127.62 C
ANISOU 392 C ALA A 79 19324 16416 12751 5039 1739 -97 C
ATOM 393 O ALA A 79 18.754 126.040 197.953 1.00128.60 O
ANISOU 393 O ALA A 79 19788 16277 12797 5286 1708 -89 O
ATOM 394 CB ALA A 79 18.663 126.306 194.724 1.00127.05 C
ANISOU 394 CB ALA A 79 19531 16264 12478 5271 1719 -294 C
ATOM 395 N SER A 80 19.322 128.162 197.377 1.00122.85 N
ANISOU 395 N SER A 80 18180 16328 12168 4906 1779 -30 N
ATOM 396 CA SER A 80 20.171 128.502 198.515 1.00123.21 C
ANISOU 396 CA SER A 80 17949 16724 12141 5045 1796 51 C
ATOM 397 C SER A 80 19.394 128.553 199.848 1.00126.85 C
ANISOU 397 C SER A 80 18548 16845 12803 4816 1774 128 C
ATOM 398 O SER A 80 19.793 127.871 200.798 1.00128.08 O
ANISOU 398 O SER A 80 18827 16991 12845 5111 1773 155 O
ATOM 399 CB SER A 80 20.862 129.835 198.260 1.00125.69 C
ANISOU 399 CB SER A 80 17686 17613 12459 4828 1812 117 C
ATOM 400 OG SER A 80 22.145 129.853 198.855 1.00137.89 O
ANISOU 400 OG SER A 80 18955 19636 13800 5119 1828 171 O
ATOM 401 N MET A 81 18.295 129.361 199.915 1.00120.71 N
ANISOU 401 N MET A 81 17742 15820 12304 4310 1756 162 N
ATOM 402 CA MET A 81 17.435 129.519 201.094 1.00118.80 C
ANISOU 402 CA MET A 81 17594 15297 12246 4060 1736 233 C
ATOM 403 C MET A 81 16.840 128.179 201.512 1.00123.98 C
ANISOU 403 C MET A 81 18774 15464 12867 4203 1712 230 C
ATOM 404 O MET A 81 16.805 127.884 202.707 1.00124.58 O
ANISOU 404 O MET A 81 18941 15457 12937 4278 1704 297 O
ATOM 405 CB MET A 81 16.307 130.533 200.832 1.00118.43 C
ANISOU 405 CB MET A 81 17409 15130 12458 3541 1716 251 C
ATOM 406 CG MET A 81 15.890 131.339 202.083 1.00120.76 C
ANISOU 406 CG MET A 81 17482 15504 12899 3303 1694 327 C
ATOM 407 SD MET A 81 14.297 132.264 202.068 1.00122.38 S
ANISOU 407 SD MET A 81 17691 15430 13379 2780 1657 340 S
ATOM 408 CE MET A 81 14.203 132.791 200.329 1.00118.45 C
ANISOU 408 CE MET A 81 17056 15024 12924 2590 1648 274 C
ATOM 409 N ALA A 82 16.400 127.359 200.531 1.00121.04 N
ANISOU 409 N ALA A 82 18761 14766 12461 4228 1688 161 N
ATOM 410 CA ALA A 82 15.815 126.035 200.765 1.00122.77 C
ANISOU 410 CA ALA A 82 19541 14480 12627 4326 1631 166 C
ATOM 411 C ALA A 82 16.792 125.049 201.416 1.00129.89 C
ANISOU 411 C ALA A 82 20670 15395 13288 4849 1611 165 C
ATOM 412 O ALA A 82 16.405 124.326 202.327 1.00130.72 O
ANISOU 412 O ALA A 82 21113 15170 13385 4863 1562 232 O
ATOM 413 CB ALA A 82 15.278 125.456 199.469 1.00124.44 C
ANISOU 413 CB ALA A 82 20080 14390 12811 4285 1591 78 C
ATOM 414 N ALA A 83 18.053 125.022 200.957 1.00127.60 N
ANISOU 414 N ALA A 83 20187 15513 12783 5279 1642 97 N
ATOM 415 CA ALA A 83 19.063 124.126 201.505 1.00129.96 C
ANISOU 415 CA ALA A 83 20656 15904 12818 5836 1624 83 C
ATOM 416 C ALA A 83 19.371 124.462 202.967 1.00132.66 C
ANISOU 416 C ALA A 83 20786 16415 13205 5819 1649 195 C
ATOM 417 O ALA A 83 19.188 123.608 203.836 1.00133.48 O
ANISOU 417 O ALA A 83 21249 16205 13261 5951 1601 246 O
ATOM 418 CB ALA A 83 20.328 124.186 200.660 1.00132.48 C
ANISOU 418 CB ALA A 83 20717 16733 12885 6268 1662 -8 C
ATOM 419 N PHE A 84 19.754 125.724 203.238 1.00127.32 N
ANISOU 419 N PHE A 84 19547 16208 12621 5620 1709 239 N
ATOM 420 CA PHE A 84 20.150 126.217 204.561 1.00126.54 C
ANISOU 420 CA PHE A 84 19168 16355 12556 5593 1731 334 C
ATOM 421 C PHE A 84 19.030 126.322 205.624 1.00128.56 C
ANISOU 421 C PHE A 84 19544 16266 13038 5214 1709 427 C
ATOM 422 O PHE A 84 19.175 125.757 206.712 1.00128.70 O
ANISOU 422 O PHE A 84 19653 16247 13002 5369 1700 494 O
ATOM 423 CB PHE A 84 20.869 127.587 204.445 1.00126.80 C
ANISOU 423 CB PHE A 84 18592 16971 12616 5437 1770 353 C
ATOM 424 CG PHE A 84 22.100 127.662 203.565 1.00130.45 C
ANISOU 424 CG PHE A 84 18790 17950 12824 5778 1798 302 C
ATOM 425 CD1 PHE A 84 23.118 126.717 203.674 1.00137.10 C
ANISOU 425 CD1 PHE A 84 19779 18952 13362 6368 1804 263 C
ATOM 426 CD2 PHE A 84 22.278 128.720 202.683 1.00131.14 C
ANISOU 426 CD2 PHE A 84 18459 18413 12954 5518 1811 304 C
ATOM 427 CE1 PHE A 84 24.264 126.799 202.874 1.00139.98 C
ANISOU 427 CE1 PHE A 84 19853 19878 13454 6706 1834 221 C
ATOM 428 CE2 PHE A 84 23.424 128.800 201.883 1.00135.94 C
ANISOU 428 CE2 PHE A 84 18782 19569 13300 5811 1837 279 C
ATOM 429 CZ PHE A 84 24.411 127.844 201.988 1.00137.46 C
ANISOU 429 CZ PHE A 84 19094 19956 13177 6410 1854 236 C
ATOM 430 N ASN A 85 17.947 127.066 205.324 1.00122.46 N
ANISOU 430 N ASN A 85 18740 15292 12498 4735 1702 434 N
ATOM 431 CA ASN A 85 16.903 127.400 206.285 1.00120.06 C
ANISOU 431 CA ASN A 85 18435 14790 12394 4357 1688 519 C
ATOM 432 C ASN A 85 15.763 126.393 206.522 1.00123.65 C
ANISOU 432 C ASN A 85 19362 14719 12901 4189 1643 569 C
ATOM 433 O ASN A 85 15.328 126.320 207.670 1.00122.88 O
ANISOU 433 O ASN A 85 19264 14539 12887 4004 1635 662 O
ATOM 434 CB ASN A 85 16.305 128.744 205.940 1.00119.09 C
ANISOU 434 CB ASN A 85 17943 14833 12473 3937 1696 507 C
ATOM 435 CG ASN A 85 17.199 129.863 206.391 1.00150.48 C
ANISOU 435 CG ASN A 85 21454 19290 16432 3971 1707 519 C
ATOM 436 OD1 ASN A 85 17.155 130.288 207.552 1.00150.83 O
ANISOU 436 OD1 ASN A 85 21357 19431 16522 3914 1697 579 O
ATOM 437 ND2 ASN A 85 18.075 130.320 205.506 1.00141.27 N
ANISOU 437 ND2 ASN A 85 20051 18455 15170 4081 1720 470 N
ATOM 438 N THR A 86 15.243 125.671 205.500 1.00120.17 N
ANISOU 438 N THR A 86 19309 13945 12405 4221 1605 518 N
ATOM 439 CA THR A 86 14.104 124.743 205.699 1.00119.78 C
ANISOU 439 CA THR A 86 19707 13404 12399 3981 1541 591 C
ATOM 440 C THR A 86 14.293 123.731 206.830 1.00123.09 C
ANISOU 440 C THR A 86 20458 13614 12696 4174 1492 691 C
ATOM 441 O THR A 86 13.353 123.484 207.589 1.00121.96 O
ANISOU 441 O THR A 86 20455 13254 12629 3869 1459 809 O
ATOM 442 CB THR A 86 13.712 123.988 204.421 1.00129.93 C
ANISOU 442 CB THR A 86 21375 14353 13638 3956 1486 518 C
ATOM 443 OG1 THR A 86 14.782 123.116 204.047 1.00135.82 O
ANISOU 443 OG1 THR A 86 22389 15068 14150 4474 1453 436 O
ATOM 444 CG2 THR A 86 13.274 124.906 203.282 1.00122.96 C
ANISOU 444 CG2 THR A 86 20210 13609 12899 3672 1525 442 C
ATOM 445 N VAL A 87 15.495 123.139 206.923 1.00120.55 N
ANISOU 445 N VAL A 87 20255 13382 12166 4685 1482 650 N
ATOM 446 CA VAL A 87 15.813 122.124 207.931 1.00122.36 C
ANISOU 446 CA VAL A 87 20833 13412 12245 4946 1424 735 C
ATOM 447 C VAL A 87 15.767 122.731 209.342 1.00121.53 C
ANISOU 447 C VAL A 87 20400 13552 12224 4825 1473 846 C
ATOM 448 O VAL A 87 14.905 122.365 210.138 1.00120.64 O
ANISOU 448 O VAL A 87 20478 13201 12157 4584 1433 975 O
ATOM 449 CB VAL A 87 17.154 121.396 207.636 1.00129.79 C
ANISOU 449 CB VAL A 87 21969 14432 12915 5584 1399 642 C
ATOM 450 CG1 VAL A 87 17.262 120.105 208.438 1.00132.82 C
ANISOU 450 CG1 VAL A 87 22921 14419 13124 5837 1290 718 C
ATOM 451 CG2 VAL A 87 17.327 121.116 206.141 1.00130.68 C
ANISOU 451 CG2 VAL A 87 22216 14490 12945 5737 1379 495 C
ATOM 452 N VAL A 88 16.655 123.700 209.602 1.00115.16 N
ANISOU 452 N VAL A 88 19089 13239 11427 4966 1552 800 N
ATOM 453 CA VAL A 88 16.815 124.445 210.844 1.00113.06 C
ANISOU 453 CA VAL A 88 18454 13282 11223 4906 1595 872 C
ATOM 454 C VAL A 88 15.504 125.120 211.320 1.00115.33 C
ANISOU 454 C VAL A 88 18582 13507 11730 4385 1601 947 C
ATOM 455 O VAL A 88 15.166 124.989 212.493 1.00114.72 O
ANISOU 455 O VAL A 88 18474 13450 11665 4323 1598 1048 O
ATOM 456 CB VAL A 88 18.000 125.432 210.675 1.00115.72 C
ANISOU 456 CB VAL A 88 18306 14154 11509 5119 1653 792 C
ATOM 457 CG1 VAL A 88 17.618 126.886 210.911 1.00112.22 C
ANISOU 457 CG1 VAL A 88 17376 14003 11261 4749 1685 796 C
ATOM 458 CG2 VAL A 88 19.171 125.032 211.540 1.00117.65 C
ANISOU 458 CG2 VAL A 88 18529 14629 11542 5589 1660 814 C
ATOM 459 N ASN A 89 14.766 125.816 210.422 1.00111.21 N
ANISOU 459 N ASN A 89 17962 12931 11361 4038 1607 898 N
ATOM 460 CA ASN A 89 13.522 126.512 210.778 1.00109.40 C
ANISOU 460 CA ASN A 89 17573 12681 11313 3583 1608 954 C
ATOM 461 C ASN A 89 12.388 125.553 211.140 1.00115.28 C
ANISOU 461 C ASN A 89 18716 13041 12045 3361 1557 1075 C
ATOM 462 O ASN A 89 11.531 125.908 211.956 1.00113.92 O
ANISOU 462 O ASN A 89 18422 12915 11946 3089 1558 1166 O
ATOM 463 CB ASN A 89 13.087 127.508 209.692 1.00109.49 C
ANISOU 463 CB ASN A 89 17346 12782 11472 3311 1623 862 C
ATOM 464 CG ASN A 89 13.822 128.833 209.715 1.00136.32 C
ANISOU 464 CG ASN A 89 20258 16593 14944 3302 1649 798 C
ATOM 465 OD1 ASN A 89 14.933 128.968 209.192 1.00128.86 O
ANISOU 465 OD1 ASN A 89 19153 15893 13916 3556 1665 739 O
ATOM 466 ND2 ASN A 89 13.188 129.858 210.276 1.00130.03 N
ANISOU 466 ND2 ASN A 89 19225 15891 14291 2997 1637 810 N
ATOM 467 N PHE A 90 12.386 124.340 210.557 1.00114.74 N
ANISOU 467 N PHE A 90 19125 12606 11864 3467 1499 1082 N
ATOM 468 CA PHE A 90 11.354 123.368 210.880 1.00116.70 C
ANISOU 468 CA PHE A 90 19794 12472 12076 3215 1422 1220 C
ATOM 469 C PHE A 90 11.587 122.742 212.255 1.00124.30 C
ANISOU 469 C PHE A 90 20913 13392 12923 3362 1393 1356 C
ATOM 470 O PHE A 90 10.638 122.655 213.040 1.00125.07 O
ANISOU 470 O PHE A 90 21051 13426 13043 3046 1368 1504 O
ATOM 471 CB PHE A 90 11.210 122.292 209.798 1.00120.62 C
ANISOU 471 CB PHE A 90 20801 12550 12481 3253 1338 1184 C
ATOM 472 CG PHE A 90 10.138 121.274 210.122 1.00124.51 C
ANISOU 472 CG PHE A 90 21777 12623 12909 2959 1226 1345 C
ATOM 473 CD1 PHE A 90 8.789 121.594 209.997 1.00126.74 C
ANISOU 473 CD1 PHE A 90 22004 12854 13297 2436 1213 1431 C
ATOM 474 CD2 PHE A 90 10.475 120.004 210.577 1.00129.82 C
ANISOU 474 CD2 PHE A 90 22966 12965 13395 3200 1121 1422 C
ATOM 475 CE1 PHE A 90 7.799 120.654 210.304 1.00129.89 C
ANISOU 475 CE1 PHE A 90 22835 12906 13613 2117 1098 1606 C
ATOM 476 CE2 PHE A 90 9.484 119.066 210.885 1.00134.90 C
ANISOU 476 CE2 PHE A 90 24082 13209 13965 2879 992 1595 C
ATOM 477 CZ PHE A 90 8.153 119.396 210.744 1.00132.04 C
ANISOU 477 CZ PHE A 90 23636 12828 13705 2319 982 1693 C
ATOM 478 N THR A 91 12.840 122.305 212.540 1.00121.90 N
ANISOU 478 N THR A 91 20687 13152 12477 3845 1393 1314 N
ATOM 479 CA THR A 91 13.251 121.661 213.798 1.00122.90 C
ANISOU 479 CA THR A 91 20977 13246 12473 4060 1363 1431 C
ATOM 480 C THR A 91 12.896 122.508 215.014 1.00122.72 C
ANISOU 480 C THR A 91 20533 13551 12544 3874 1424 1515 C
ATOM 481 O THR A 91 12.267 122.001 215.946 1.00123.74 O
ANISOU 481 O THR A 91 20826 13566 12623 3740 1384 1675 O
ATOM 482 CB THR A 91 14.755 121.334 213.801 1.00133.47 C
ANISOU 482 CB THR A 91 22387 14689 13638 4648 1366 1341 C
ATOM 483 OG1 THR A 91 15.207 121.028 212.482 1.00134.38 O
ANISOU 483 OG1 THR A 91 22759 14624 13677 4847 1328 1215 O
ATOM 484 CG2 THR A 91 15.093 120.192 214.741 1.00136.25 C
ANISOU 484 CG2 THR A 91 23117 14841 13812 4901 1292 1463 C
ATOM 485 N TYR A 92 13.288 123.798 214.986 1.00114.63 N
ANISOU 485 N TYR A 92 18985 12930 11640 3863 1507 1409 N
ATOM 486 CA TYR A 92 13.055 124.782 216.046 1.00111.56 C
ANISOU 486 CA TYR A 92 18176 12874 11338 3717 1552 1449 C
ATOM 487 C TYR A 92 11.562 124.965 216.337 1.00113.49 C
ANISOU 487 C TYR A 92 18399 13045 11678 3249 1537 1549 C
ATOM 488 O TYR A 92 11.178 125.003 217.503 1.00112.67 O
ANISOU 488 O TYR A 92 18180 13073 11558 3157 1540 1655 O
ATOM 489 CB TYR A 92 13.723 126.120 215.674 1.00109.72 C
ANISOU 489 CB TYR A 92 17458 13032 11198 3793 1606 1305 C
ATOM 490 CG TYR A 92 14.024 127.062 216.822 1.00109.36 C
ANISOU 490 CG TYR A 92 17023 13344 11185 3804 1629 1318 C
ATOM 491 CD1 TYR A 92 14.347 128.395 216.588 1.00108.69 C
ANISOU 491 CD1 TYR A 92 16520 13573 11203 3734 1643 1212 C
ATOM 492 CD2 TYR A 92 14.018 126.615 218.143 1.00111.47 C
ANISOU 492 CD2 TYR A 92 17361 13628 11365 3889 1622 1439 C
ATOM 493 CE1 TYR A 92 14.653 129.262 217.636 1.00107.59 C
ANISOU 493 CE1 TYR A 92 16062 13736 11080 3747 1638 1215 C
ATOM 494 CE2 TYR A 92 14.304 127.477 219.200 1.00111.21 C
ANISOU 494 CE2 TYR A 92 16979 13924 11350 3913 1635 1441 C
ATOM 495 CZ TYR A 92 14.627 128.799 218.939 1.00115.07 C
ANISOU 495 CZ TYR A 92 17075 14705 11943 3847 1639 1323 C
ATOM 496 OH TYR A 92 14.917 129.656 219.969 1.00115.31 O
ANISOU 496 OH TYR A 92 16803 15032 11979 3870 1628 1317 O
ATOM 497 N ALA A 93 10.728 125.032 215.278 1.00109.21 N
ANISOU 497 N ALA A 93 17962 12321 11213 2967 1520 1520 N
ATOM 498 CA ALA A 93 9.274 125.172 215.366 1.00108.27 C
ANISOU 498 CA ALA A 93 17817 12165 11157 2520 1503 1612 C
ATOM 499 C ALA A 93 8.638 123.965 216.076 1.00116.05 C
ANISOU 499 C ALA A 93 19184 12896 12013 2363 1436 1819 C
ATOM 500 O ALA A 93 7.852 124.137 217.007 1.00115.05 O
ANISOU 500 O ALA A 93 18912 12926 11875 2119 1438 1944 O
ATOM 501 CB ALA A 93 8.690 125.325 213.969 1.00107.90 C
ANISOU 501 CB ALA A 93 17821 11976 11199 2300 1495 1527 C
ATOM 502 N VAL A 94 9.012 122.748 215.654 1.00116.89 N
ANISOU 502 N VAL A 94 19787 12626 12001 2517 1364 1857 N
ATOM 503 CA VAL A 94 8.486 121.502 216.190 1.00120.34 C
ANISOU 503 CA VAL A 94 20690 12740 12295 2365 1263 2060 C
ATOM 504 C VAL A 94 8.915 121.233 217.635 1.00128.43 C
ANISOU 504 C VAL A 94 21694 13887 13216 2526 1262 2190 C
ATOM 505 O VAL A 94 8.054 120.986 218.481 1.00128.82 O
ANISOU 505 O VAL A 94 21764 13968 13212 2218 1230 2381 O
ATOM 506 CB VAL A 94 8.827 120.314 215.262 1.00126.19 C
ANISOU 506 CB VAL A 94 22018 13001 12928 2525 1157 2033 C
ATOM 507 N HIS A 95 10.232 121.317 217.915 1.00127.54 N
ANISOU 507 N HIS A 95 21522 13878 13059 3005 1296 2095 N
ATOM 508 CA HIS A 95 10.862 120.970 219.194 1.00129.92 C
ANISOU 508 CA HIS A 95 21843 14277 13245 3246 1292 2198 C
ATOM 509 C HIS A 95 11.019 122.090 220.254 1.00132.34 C
ANISOU 509 C HIS A 95 21591 15072 13620 3281 1388 2179 C
ATOM 510 O HIS A 95 11.125 121.762 221.446 1.00133.34 O
ANISOU 510 O HIS A 95 21730 15283 13652 3351 1377 2309 O
ATOM 511 CB HIS A 95 12.236 120.350 218.923 1.00132.99 C
ANISOU 511 CB HIS A 95 22502 14522 13508 3780 1264 2111 C
ATOM 512 CG HIS A 95 12.164 118.998 218.289 1.00139.85 C
ANISOU 512 CG HIS A 95 24016 14869 14252 3826 1135 2146 C
ATOM 513 ND1 HIS A 95 12.082 118.849 216.916 1.00141.69 N
ANISOU 513 ND1 HIS A 95 24386 14929 14521 3862 1118 1998 N
ATOM 514 CD2 HIS A 95 12.170 117.772 218.863 1.00145.32 C
ANISOU 514 CD2 HIS A 95 25264 15174 14777 3839 1001 2312 C
ATOM 515 CE1 HIS A 95 12.045 117.544 216.697 1.00144.54 C
ANISOU 515 CE1 HIS A 95 25387 14800 14733 3914 973 2064 C
ATOM 516 NE2 HIS A 95 12.099 116.855 217.839 1.00147.26 N
ANISOU 516 NE2 HIS A 95 26018 14984 14950 3894 890 2256 N
ATOM 517 N ASN A 96 11.065 123.377 219.836 1.00125.61 N
ANISOU 517 N ASN A 96 20283 14523 12919 3242 1464 2017 N
ATOM 518 CA ASN A 96 11.254 124.557 220.707 1.00122.95 C
ANISOU 518 CA ASN A 96 19440 14628 12649 3288 1529 1963 C
ATOM 519 C ASN A 96 12.570 124.483 221.510 1.00125.51 C
ANISOU 519 C ASN A 96 19696 15114 12878 3723 1547 1941 C
ATOM 520 O ASN A 96 12.629 124.792 222.703 1.00123.95 O
ANISOU 520 O ASN A 96 19293 15158 12644 3772 1564 2001 O
ATOM 521 CB ASN A 96 10.027 124.853 221.591 1.00125.33 C
ANISOU 521 CB ASN A 96 19570 15094 12956 2948 1529 2094 C
ATOM 522 CG ASN A 96 9.058 125.832 220.956 1.00157.21 C
ANISOU 522 CG ASN A 96 23377 19235 17119 2610 1543 2028 C
ATOM 523 OD1 ASN A 96 9.440 126.888 220.418 1.00150.50 O
ANISOU 523 OD1 ASN A 96 22242 18551 16392 2661 1573 1854 O
ATOM 524 ND2 ASN A 96 7.773 125.504 221.010 1.00152.47 N
ANISOU 524 ND2 ASN A 96 22894 18562 16476 2248 1513 2178 N
ATOM 525 N GLU A 97 13.629 124.076 220.804 1.00122.84 N
ANISOU 525 N GLU A 97 19529 14663 12482 4051 1542 1850 N
ATOM 526 CA GLU A 97 14.993 123.969 221.295 1.00123.41 C
ANISOU 526 CA GLU A 97 19535 14915 12440 4500 1559 1811 C
ATOM 527 C GLU A 97 15.950 124.165 220.123 1.00126.58 C
ANISOU 527 C GLU A 97 19873 15387 12833 4762 1580 1646 C
ATOM 528 O GLU A 97 15.761 123.569 219.057 1.00126.58 O
ANISOU 528 O GLU A 97 20166 15105 12824 4750 1551 1606 O
ATOM 529 CB GLU A 97 15.250 122.624 222.000 1.00127.90 C
ANISOU 529 CB GLU A 97 20540 15232 12825 4718 1502 1957 C
ATOM 530 CG GLU A 97 16.650 122.550 222.595 1.00139.56 C
ANISOU 530 CG GLU A 97 21869 16980 14176 5165 1527 1934 C
ATOM 531 CD GLU A 97 17.001 121.360 223.463 1.00164.04 C
ANISOU 531 CD GLU A 97 25393 19858 17076 5457 1465 2062 C
ATOM 532 OE1 GLU A 97 16.072 120.693 223.975 1.00161.06 O
ANISOU 532 OE1 GLU A 97 25356 19177 16664 5221 1399 2230 O
ATOM 533 OE2 GLU A 97 18.214 121.133 223.680 1.00157.53 O
ANISOU 533 OE2 GLU A 97 24544 19195 16115 5916 1475 2006 O
ATOM 534 N TRP A 98 16.963 125.022 220.322 1.00122.29 N
ANISOU 534 N TRP A 98 18935 15248 12281 4978 1623 1557 N
ATOM 535 CA TRP A 98 17.987 125.290 219.319 1.00122.09 C
ANISOU 535 CA TRP A 98 18767 15408 12215 5227 1645 1421 C
ATOM 536 C TRP A 98 19.136 124.287 219.488 1.00128.47 C
ANISOU 536 C TRP A 98 19779 16242 12791 5744 1636 1430 C
ATOM 537 O TRP A 98 19.694 124.165 220.580 1.00128.88 O
ANISOU 537 O TRP A 98 19723 16499 12746 5954 1643 1486 O
ATOM 538 CB TRP A 98 18.472 126.745 219.392 1.00118.35 C
ANISOU 538 CB TRP A 98 17754 15372 11842 5118 1675 1332 C
ATOM 539 CG TRP A 98 19.342 127.118 218.236 1.00119.25 C
ANISOU 539 CG TRP A 98 17705 15685 11918 5269 1690 1215 C
ATOM 540 CD1 TRP A 98 20.683 127.358 218.265 1.00123.24 C
ANISOU 540 CD1 TRP A 98 17980 16570 12277 5596 1706 1176 C
ATOM 541 CD2 TRP A 98 18.941 127.237 216.867 1.00118.42 C
ANISOU 541 CD2 TRP A 98 17668 15433 11893 5111 1690 1136 C
ATOM 542 NE1 TRP A 98 21.143 127.630 217.000 1.00122.88 N
ANISOU 542 NE1 TRP A 98 17840 16646 12204 5649 1717 1085 N
ATOM 543 CE2 TRP A 98 20.096 127.557 216.119 1.00123.27 C
ANISOU 543 CE2 TRP A 98 18078 16361 12397 5360 1708 1054 C
ATOM 544 CE3 TRP A 98 17.712 127.112 216.194 1.00118.66 C
ANISOU 544 CE3 TRP A 98 17900 15122 12062 4779 1676 1133 C
ATOM 545 CZ2 TRP A 98 20.065 127.733 214.729 1.00122.24 C
ANISOU 545 CZ2 TRP A 98 17941 16208 12295 5293 1714 967 C
ATOM 546 CZ3 TRP A 98 17.680 127.306 214.821 1.00119.72 C
ANISOU 546 CZ3 TRP A 98 18041 15212 12235 4717 1681 1040 C
ATOM 547 CH2 TRP A 98 18.845 127.622 214.106 1.00121.04 C
ANISOU 547 CH2 TRP A 98 18005 15688 12297 4973 1700 957 C
ATOM 548 N TYR A 99 19.460 123.551 218.413 1.00125.98 N
ANISOU 548 N TYR A 99 19774 15720 12374 5966 1612 1370 N
ATOM 549 CA TYR A 99 20.467 122.493 218.439 1.00128.63 C
ANISOU 549 CA TYR A 99 20386 16028 12460 6503 1584 1361 C
ATOM 550 C TYR A 99 21.779 122.819 217.749 1.00132.41 C
ANISOU 550 C TYR A 99 20580 16925 12804 6871 1625 1235 C
ATOM 551 O TYR A 99 22.724 122.044 217.881 1.00135.43 O
ANISOU 551 O TYR A 99 21108 17401 12948 7372 1609 1222 O
ATOM 552 CB TYR A 99 19.888 121.233 217.762 1.00132.20 C
ANISOU 552 CB TYR A 99 21466 15924 12840 6548 1499 1376 C
ATOM 553 CG TYR A 99 18.627 120.694 218.397 1.00135.00 C
ANISOU 553 CG TYR A 99 22166 15848 13281 6167 1437 1527 C
ATOM 554 CD1 TYR A 99 18.646 120.158 219.682 1.00139.11 C
ANISOU 554 CD1 TYR A 99 22852 16289 13713 6240 1401 1673 C
ATOM 555 CD2 TYR A 99 17.426 120.665 217.695 1.00134.90 C
ANISOU 555 CD2 TYR A 99 22325 15520 13410 5738 1406 1537 C
ATOM 556 CE1 TYR A 99 17.489 119.654 220.274 1.00141.20 C
ANISOU 556 CE1 TYR A 99 23420 16202 14029 5864 1336 1837 C
ATOM 557 CE2 TYR A 99 16.263 120.151 218.271 1.00136.62 C
ANISOU 557 CE2 TYR A 99 22840 15396 13675 5362 1342 1697 C
ATOM 558 CZ TYR A 99 16.300 119.644 219.563 1.00147.90 C
ANISOU 558 CZ TYR A 99 24416 16773 15008 5420 1306 1853 C
ATOM 559 OH TYR A 99 15.168 119.136 220.157 1.00151.40 O
ANISOU 559 OH TYR A 99 25131 16925 15469 5026 1236 2036 O
ATOM 560 N TYR A 100 21.849 123.937 217.022 1.00125.55 N
ANISOU 560 N TYR A 100 19322 16319 12062 6637 1668 1150 N
ATOM 561 CA TYR A 100 22.954 124.251 216.124 1.00125.68 C
ANISOU 561 CA TYR A 100 19081 16724 11948 6905 1699 1042 C
ATOM 562 C TYR A 100 23.950 125.358 216.561 1.00128.16 C
ANISOU 562 C TYR A 100 18808 17670 12216 6951 1740 1036 C
ATOM 563 O TYR A 100 24.781 125.775 215.747 1.00128.01 O
ANISOU 563 O TYR A 100 18523 18033 12082 7106 1762 967 O
ATOM 564 CB TYR A 100 22.351 124.580 214.748 1.00125.53 C
ANISOU 564 CB TYR A 100 19071 16555 12069 6611 1702 961 C
ATOM 565 CG TYR A 100 21.219 123.645 214.363 1.00127.97 C
ANISOU 565 CG TYR A 100 19926 16250 12446 6461 1649 980 C
ATOM 566 CD1 TYR A 100 21.474 122.443 213.710 1.00132.39 C
ANISOU 566 CD1 TYR A 100 20959 16526 12816 6828 1596 934 C
ATOM 567 CD2 TYR A 100 19.898 123.934 214.706 1.00127.13 C
ANISOU 567 CD2 TYR A 100 19880 15860 12565 5965 1635 1051 C
ATOM 568 CE1 TYR A 100 20.443 121.567 213.375 1.00133.16 C
ANISOU 568 CE1 TYR A 100 21593 16041 12960 6659 1520 965 C
ATOM 569 CE2 TYR A 100 18.858 123.060 214.383 1.00129.01 C
ANISOU 569 CE2 TYR A 100 20607 15570 12841 5788 1575 1094 C
ATOM 570 CZ TYR A 100 19.136 121.885 213.701 1.00137.98 C
ANISOU 570 CZ TYR A 100 22225 16401 13799 6113 1512 1053 C
ATOM 571 OH TYR A 100 18.125 121.024 213.355 1.00138.88 O
ANISOU 571 OH TYR A 100 22850 15981 13938 5908 1428 1101 O
ATOM 572 N GLY A 101 23.911 125.770 217.825 1.00124.32 N
ANISOU 572 N GLY A 101 18141 17307 11787 6836 1741 1113 N
ATOM 573 CA GLY A 101 24.844 126.761 218.362 1.00124.46 C
ANISOU 573 CA GLY A 101 17649 17893 11747 6864 1755 1119 C
ATOM 574 C GLY A 101 24.684 128.192 217.879 1.00127.73 C
ANISOU 574 C GLY A 101 17649 18539 12342 6417 1743 1083 C
ATOM 575 O GLY A 101 23.973 128.447 216.901 1.00126.12 O
ANISOU 575 O GLY A 101 17516 18097 12305 6111 1736 1039 O
ATOM 576 N LEU A 102 25.381 129.136 218.569 1.00124.86 N
ANISOU 576 N LEU A 102 16865 18643 11934 6378 1726 1107 N
ATOM 577 CA LEU A 102 25.373 130.591 218.342 1.00122.71 C
ANISOU 577 CA LEU A 102 16204 18620 11801 5963 1677 1087 C
ATOM 578 C LEU A 102 25.695 131.024 216.894 1.00127.03 C
ANISOU 578 C LEU A 102 16588 19337 12340 5842 1672 1031 C
ATOM 579 O LEU A 102 25.124 132.028 216.447 1.00124.95 O
ANISOU 579 O LEU A 102 16190 19023 12262 5424 1622 1006 O
ATOM 580 CB LEU A 102 26.281 131.339 219.344 1.00123.27 C
ANISOU 580 CB LEU A 102 15902 19161 11774 5983 1636 1132 C
ATOM 581 CG LEU A 102 27.795 131.136 219.207 1.00131.58 C
ANISOU 581 CG LEU A 102 16699 20766 12531 6352 1655 1156 C
ATOM 582 CD1 LEU A 102 28.461 132.350 218.580 1.00132.03 C
ANISOU 582 CD1 LEU A 102 16338 21278 12549 6100 1601 1151 C
ATOM 583 CD2 LEU A 102 28.433 130.809 220.541 1.00136.37 C
ANISOU 583 CD2 LEU A 102 17196 21613 13006 6570 1648 1218 C
ATOM 584 N PHE A 103 26.608 130.305 216.173 1.00125.15 N
ANISOU 584 N PHE A 103 16357 19323 11873 6217 1716 1012 N
ATOM 585 CA PHE A 103 26.917 130.692 214.798 1.00124.44 C
ANISOU 585 CA PHE A 103 16100 19435 11748 6122 1716 967 C
ATOM 586 C PHE A 103 25.715 130.491 213.891 1.00126.57 C
ANISOU 586 C PHE A 103 16684 19189 12218 5901 1725 908 C
ATOM 587 O PHE A 103 25.285 131.449 213.237 1.00124.29 O
ANISOU 587 O PHE A 103 16239 18895 12090 5502 1688 887 O
ATOM 588 CB PHE A 103 28.154 129.991 214.217 1.00129.24 C
ANISOU 588 CB PHE A 103 16607 20475 12025 6611 1760 957 C
ATOM 589 CG PHE A 103 28.340 130.355 212.756 1.00130.99 C
ANISOU 589 CG PHE A 103 16698 20864 12207 6519 1767 910 C
ATOM 590 CD1 PHE A 103 28.917 131.568 212.392 1.00133.47 C
ANISOU 590 CD1 PHE A 103 16566 21619 12528 6171 1719 950 C
ATOM 591 CD2 PHE A 103 27.863 129.523 211.746 1.00133.95 C
ANISOU 591 CD2 PHE A 103 17423 20926 12544 6743 1804 832 C
ATOM 592 CE1 PHE A 103 29.042 131.926 211.043 1.00134.39 C
ANISOU 592 CE1 PHE A 103 16563 21889 12609 6057 1722 920 C
ATOM 593 CE2 PHE A 103 27.979 129.888 210.399 1.00136.55 C
ANISOU 593 CE2 PHE A 103 17631 21408 12842 6647 1811 787 C
ATOM 594 CZ PHE A 103 28.572 131.083 210.057 1.00133.86 C
ANISOU 594 CZ PHE A 103 16821 21533 12506 6307 1776 836 C
ATOM 595 N TYR A 104 25.173 129.253 213.846 1.00123.65 N
ANISOU 595 N TYR A 104 16771 18383 11827 6147 1759 885 N
ATOM 596 CA TYR A 104 24.017 128.961 213.004 1.00121.92 C
ANISOU 596 CA TYR A 104 16875 17673 11776 5938 1759 836 C
ATOM 597 C TYR A 104 22.739 129.639 213.505 1.00123.01 C
ANISOU 597 C TYR A 104 17054 17485 12201 5456 1728 860 C
ATOM 598 O TYR A 104 21.774 129.755 212.752 1.00121.53 O
ANISOU 598 O TYR A 104 17030 16977 12168 5196 1723 824 O
ATOM 599 CB TYR A 104 23.824 127.462 212.761 1.00125.00 C
ANISOU 599 CB TYR A 104 17770 17685 12041 6308 1773 812 C
ATOM 600 CG TYR A 104 23.391 127.201 211.337 1.00126.77 C
ANISOU 600 CG TYR A 104 18176 17703 12287 6259 1775 731 C
ATOM 601 CD1 TYR A 104 24.329 127.073 210.315 1.00130.26 C
ANISOU 601 CD1 TYR A 104 18449 18513 12531 6525 1796 667 C
ATOM 602 CD2 TYR A 104 22.044 127.186 210.990 1.00126.21 C
ANISOU 602 CD2 TYR A 104 18396 17129 12430 5914 1756 722 C
ATOM 603 CE1 TYR A 104 23.935 126.883 208.989 1.00130.25 C
ANISOU 603 CE1 TYR A 104 18591 18349 12549 6470 1797 588 C
ATOM 604 CE2 TYR A 104 21.639 127.016 209.667 1.00127.11 C
ANISOU 604 CE2 TYR A 104 18659 17068 12570 5844 1754 645 C
ATOM 605 CZ TYR A 104 22.588 126.854 208.672 1.00133.95 C
ANISOU 605 CZ TYR A 104 19376 18275 13243 6129 1774 574 C
ATOM 606 OH TYR A 104 22.180 126.681 207.375 1.00132.39 O
ANISOU 606 OH TYR A 104 19328 17910 13063 6069 1771 495 O
ATOM 607 N CYS A 105 22.756 130.145 214.747 1.00118.70 N
ANISOU 607 N CYS A 105 16333 17061 11708 5349 1704 914 N
ATOM 608 CA CYS A 105 21.659 130.924 215.316 1.00116.10 C
ANISOU 608 CA CYS A 105 15972 16534 11608 4941 1665 929 C
ATOM 609 C CYS A 105 21.676 132.257 214.560 1.00118.45 C
ANISOU 609 C CYS A 105 15956 17037 12013 4610 1615 880 C
ATOM 610 O CYS A 105 20.699 132.605 213.894 1.00116.08 O
ANISOU 610 O CYS A 105 15745 16484 11876 4324 1600 841 O
ATOM 611 CB CYS A 105 21.862 131.111 216.818 1.00116.41 C
ANISOU 611 CB CYS A 105 15893 16719 11618 5000 1645 989 C
ATOM 612 SG CYS A 105 20.662 132.210 217.620 1.00117.68 S
ANISOU 612 SG CYS A 105 15979 16726 12008 4576 1586 995 S
ATOM 613 N LYS A 106 22.840 132.924 214.564 1.00116.02 N
ANISOU 613 N LYS A 106 15298 17199 11584 4662 1583 891 N
ATOM 614 CA LYS A 106 23.083 134.176 213.855 1.00114.78 C
ANISOU 614 CA LYS A 106 14841 17286 11484 4350 1511 871 C
ATOM 615 C LYS A 106 22.826 134.037 212.350 1.00117.36 C
ANISOU 615 C LYS A 106 15243 17514 11833 4282 1539 823 C
ATOM 616 O LYS A 106 22.114 134.865 211.793 1.00115.19 O
ANISOU 616 O LYS A 106 14922 17122 11722 3925 1484 793 O
ATOM 617 CB LYS A 106 24.514 134.674 214.127 1.00119.07 C
ANISOU 617 CB LYS A 106 15013 18396 11833 4447 1470 922 C
ATOM 618 CG LYS A 106 24.730 135.177 215.552 1.00124.29 C
ANISOU 618 CG LYS A 106 15553 19186 12484 4438 1415 963 C
ATOM 619 CD LYS A 106 26.188 135.493 215.831 1.00128.53 C
ANISOU 619 CD LYS A 106 15739 20306 12791 4568 1382 1025 C
ATOM 620 CE LYS A 106 26.355 136.394 217.028 1.00134.25 C
ANISOU 620 CE LYS A 106 16292 21176 13541 4404 1279 1057 C
ATOM 621 NZ LYS A 106 26.214 137.828 216.665 1.00141.24 N
ANISOU 621 NZ LYS A 106 16996 22130 14537 3940 1126 1050 N
ATOM 622 N PHE A 107 23.344 132.963 211.714 1.00115.28 N
ANISOU 622 N PHE A 107 15122 17282 11398 4643 1617 809 N
ATOM 623 CA PHE A 107 23.208 132.718 210.273 1.00114.89 C
ANISOU 623 CA PHE A 107 15155 17164 11335 4638 1646 755 C
ATOM 624 C PHE A 107 21.778 132.440 209.787 1.00117.92 C
ANISOU 624 C PHE A 107 15880 16999 11925 4427 1656 707 C
ATOM 625 O PHE A 107 21.426 132.915 208.711 1.00116.86 O
ANISOU 625 O PHE A 107 15707 16824 11869 4211 1644 667 O
ATOM 626 CB PHE A 107 24.152 131.607 209.791 1.00119.10 C
ANISOU 626 CB PHE A 107 15762 17898 11592 5136 1710 737 C
ATOM 627 CG PHE A 107 24.183 131.497 208.286 1.00120.86 C
ANISOU 627 CG PHE A 107 16016 18142 11764 5155 1733 677 C
ATOM 628 CD1 PHE A 107 24.917 132.396 207.522 1.00123.91 C
ANISOU 628 CD1 PHE A 107 16015 18990 12076 5000 1708 695 C
ATOM 629 CD2 PHE A 107 23.432 130.531 207.627 1.00123.48 C
ANISOU 629 CD2 PHE A 107 16771 18027 12118 5293 1764 610 C
ATOM 630 CE1 PHE A 107 24.907 132.325 206.125 1.00125.22 C
ANISOU 630 CE1 PHE A 107 16196 19194 12189 5012 1730 643 C
ATOM 631 CE2 PHE A 107 23.427 130.455 206.229 1.00126.64 C
ANISOU 631 CE2 PHE A 107 17204 18447 12468 5314 1780 545 C
ATOM 632 CZ PHE A 107 24.167 131.351 205.488 1.00124.60 C
ANISOU 632 CZ PHE A 107 16537 18670 12135 5185 1770 560 C
ATOM 633 N HIS A 108 20.975 131.665 210.540 1.00114.77 N
ANISOU 633 N HIS A 108 15804 16208 11595 4478 1675 721 N
ATOM 634 CA HIS A 108 19.592 131.324 210.164 1.00113.17 C
ANISOU 634 CA HIS A 108 15919 15519 11560 4257 1679 697 C
ATOM 635 C HIS A 108 18.632 132.538 210.227 1.00111.34 C
ANISOU 635 C HIS A 108 15535 15212 11559 3798 1625 689 C
ATOM 636 O HIS A 108 17.517 132.475 209.693 1.00109.02 O
ANISOU 636 O HIS A 108 15423 14600 11398 3571 1624 665 O
ATOM 637 CB HIS A 108 19.077 130.119 210.987 1.00115.62 C
ANISOU 637 CB HIS A 108 16619 15476 11834 4434 1699 742 C
ATOM 638 CG HIS A 108 18.105 130.439 212.090 1.00117.79 C
ANISOU 638 CG HIS A 108 16928 15573 12255 4183 1677 800 C
ATOM 639 ND1 HIS A 108 16.754 130.138 211.972 1.00118.93 N
ANISOU 639 ND1 HIS A 108 17346 15325 12518 3944 1671 821 N
ATOM 640 CD2 HIS A 108 18.320 131.005 213.300 1.00118.84 C
ANISOU 640 CD2 HIS A 108 16850 15901 12404 4155 1656 844 C
ATOM 641 CE1 HIS A 108 16.196 130.535 213.106 1.00117.32 C
ANISOU 641 CE1 HIS A 108 17065 15122 12388 3791 1654 878 C
ATOM 642 NE2 HIS A 108 17.097 131.071 213.932 1.00117.61 N
ANISOU 642 NE2 HIS A 108 16824 15491 12373 3918 1643 886 N
ATOM 643 N ASN A 109 19.065 133.620 210.901 1.00105.69 N
ANISOU 643 N ASN A 109 14499 14793 10866 3677 1568 707 N
ATOM 644 CA ASN A 109 18.313 134.866 211.029 1.00102.69 C
ANISOU 644 CA ASN A 109 13972 14382 10664 3304 1488 689 C
ATOM 645 C ASN A 109 18.857 135.918 210.060 1.00106.23 C
ANISOU 645 C ASN A 109 14167 15073 11122 3113 1424 663 C
ATOM 646 O ASN A 109 18.197 136.924 209.806 1.00104.85 O
ANISOU 646 O ASN A 109 13955 14788 11094 2803 1355 628 O
ATOM 647 CB ASN A 109 18.329 135.389 212.474 1.00100.52 C
ANISOU 647 CB ASN A 109 13575 14220 10399 3293 1436 722 C
ATOM 648 CG ASN A 109 17.505 134.585 213.465 1.00118.93 C
ANISOU 648 CG ASN A 109 16138 16283 12766 3350 1476 756 C
ATOM 649 OD1 ASN A 109 16.400 134.111 213.176 1.00110.34 O
ANISOU 649 OD1 ASN A 109 15271 14887 11768 3222 1503 751 O
ATOM 650 ND2 ASN A 109 17.994 134.472 214.691 1.00111.71 N
ANISOU 650 ND2 ASN A 109 15162 15509 11773 3512 1471 802 N
ATOM 651 N PHE A 110 20.053 135.679 209.509 1.00103.86 N
ANISOU 651 N PHE A 110 13695 15122 10644 3306 1443 686 N
ATOM 652 CA PHE A 110 20.694 136.596 208.583 1.00103.42 C
ANISOU 652 CA PHE A 110 13379 15368 10548 3134 1385 691 C
ATOM 653 C PHE A 110 20.314 136.269 207.145 1.00107.68 C
ANISOU 653 C PHE A 110 14046 15758 11110 3106 1436 644 C
ATOM 654 O PHE A 110 19.695 137.106 206.490 1.00106.39 O
ANISOU 654 O PHE A 110 13841 15503 11079 2786 1374 622 O
ATOM 655 CB PHE A 110 22.221 136.590 208.790 1.00107.37 C
ANISOU 655 CB PHE A 110 13603 16384 10809 3354 1386 753 C
ATOM 656 CG PHE A 110 23.027 137.228 207.681 1.00110.02 C
ANISOU 656 CG PHE A 110 13656 17105 11042 3205 1338 786 C
ATOM 657 CD1 PHE A 110 23.260 138.598 207.669 1.00112.62 C
ANISOU 657 CD1 PHE A 110 13724 17668 11397 2852 1196 840 C
ATOM 658 CD2 PHE A 110 23.577 136.454 206.660 1.00113.43 C
ANISOU 658 CD2 PHE A 110 14095 17675 11330 3415 1421 768 C
ATOM 659 CE1 PHE A 110 24.003 139.187 206.642 1.00114.21 C
ANISOU 659 CE1 PHE A 110 13668 18236 11491 2667 1138 897 C
ATOM 660 CE2 PHE A 110 24.310 137.044 205.631 1.00116.84 C
ANISOU 660 CE2 PHE A 110 14242 18500 11650 3260 1379 812 C
ATOM 661 CZ PHE A 110 24.522 138.407 205.633 1.00114.46 C
ANISOU 661 CZ PHE A 110 13673 18435 11381 2869 1238 887 C
ATOM 662 N PHE A 111 20.677 135.050 206.658 1.00105.52 N
ANISOU 662 N PHE A 111 13942 15460 10692 3454 1535 624 N
ATOM 663 CA PHE A 111 20.474 134.597 205.276 1.00105.26 C
ANISOU 663 CA PHE A 111 14028 15333 10633 3488 1580 572 C
ATOM 664 C PHE A 111 19.020 134.736 204.721 1.00106.72 C
ANISOU 664 C PHE A 111 14428 15079 11042 3178 1567 521 C
ATOM 665 O PHE A 111 18.931 135.221 203.588 1.00105.90 O
ANISOU 665 O PHE A 111 14229 15048 10962 3010 1550 498 O
ATOM 666 CB PHE A 111 21.002 133.170 205.040 1.00109.14 C
ANISOU 666 CB PHE A 111 14747 15800 10921 3958 1665 540 C
ATOM 667 CG PHE A 111 21.202 132.867 203.569 1.00111.30 C
ANISOU 667 CG PHE A 111 15040 16157 11093 4050 1696 485 C
ATOM 668 CD1 PHE A 111 22.199 133.504 202.839 1.00114.59 C
ANISOU 668 CD1 PHE A 111 15087 17088 11363 4038 1682 513 C
ATOM 669 CD2 PHE A 111 20.371 131.967 202.907 1.00113.35 C
ANISOU 669 CD2 PHE A 111 15683 15995 11390 4125 1728 413 C
ATOM 670 CE1 PHE A 111 22.358 133.253 201.474 1.00116.28 C
ANISOU 670 CE1 PHE A 111 15300 17409 11473 4122 1711 463 C
ATOM 671 CE2 PHE A 111 20.537 131.710 201.541 1.00116.66 C
ANISOU 671 CE2 PHE A 111 16123 16492 11709 4216 1749 352 C
ATOM 672 CZ PHE A 111 21.525 132.359 200.835 1.00115.40 C
ANISOU 672 CZ PHE A 111 15578 16860 11407 4224 1747 374 C
ATOM 673 N PRO A 112 17.891 134.376 205.422 1.00101.03 N
ANISOU 673 N PRO A 112 13965 13953 10467 3084 1573 512 N
ATOM 674 CA PRO A 112 16.559 134.550 204.793 1.00 98.61 C
ANISOU 674 CA PRO A 112 13816 13312 10338 2789 1561 471 C
ATOM 675 C PRO A 112 16.268 135.956 204.269 1.00 99.28 C
ANISOU 675 C PRO A 112 13668 13499 10554 2431 1476 459 C
ATOM 676 O PRO A 112 15.694 136.065 203.191 1.00 97.71 O
ANISOU 676 O PRO A 112 13530 13166 10430 2261 1475 419 O
ATOM 677 CB PRO A 112 15.571 134.144 205.892 1.00 99.63 C
ANISOU 677 CB PRO A 112 14170 13127 10557 2745 1569 495 C
ATOM 678 CG PRO A 112 16.331 133.321 206.813 1.00105.65 C
ANISOU 678 CG PRO A 112 15018 13953 11172 3082 1607 537 C
ATOM 679 CD PRO A 112 17.762 133.774 206.765 1.00102.36 C
ANISOU 679 CD PRO A 112 14285 13982 10625 3235 1592 550 C
ATOM 680 N ILE A 113 16.687 137.018 205.006 1.00 94.87 N
ANISOU 680 N ILE A 113 12865 13172 10011 2320 1392 494 N
ATOM 681 CA ILE A 113 16.494 138.423 204.611 1.00 93.12 C
ANISOU 681 CA ILE A 113 12458 13034 9890 1988 1273 488 C
ATOM 682 C ILE A 113 17.322 138.736 203.372 1.00 98.51 C
ANISOU 682 C ILE A 113 12963 13989 10478 1937 1259 506 C
ATOM 683 O ILE A 113 16.819 139.397 202.460 1.00 97.41 O
ANISOU 683 O ILE A 113 12800 13780 10431 1677 1200 486 O
ATOM 684 CB ILE A 113 16.733 139.417 205.786 1.00 95.42 C
ANISOU 684 CB ILE A 113 12595 13456 10205 1889 1157 516 C
ATOM 685 CG1 ILE A 113 15.647 139.252 206.861 1.00 94.50 C
ANISOU 685 CG1 ILE A 113 12651 13071 10184 1916 1171 492 C
ATOM 686 CG2 ILE A 113 16.789 140.875 205.305 1.00 95.15 C
ANISOU 686 CG2 ILE A 113 12408 13505 10241 1556 995 516 C
ATOM 687 CD1 ILE A 113 16.134 139.420 208.246 1.00104.03 C
ANISOU 687 CD1 ILE A 113 13757 14417 11354 1982 1109 518 C
ATOM 688 N ALA A 114 18.567 138.225 203.315 1.00 97.22 N
ANISOU 688 N ALA A 114 12679 14146 10114 2203 1317 543 N
ATOM 689 CA ALA A 114 19.447 138.417 202.158 1.00 98.48 C
ANISOU 689 CA ALA A 114 12634 14653 10130 2200 1318 573 C
ATOM 690 C ALA A 114 18.916 137.700 200.900 1.00101.49 C
ANISOU 690 C ALA A 114 13194 14852 10516 2264 1399 508 C
ATOM 691 O ALA A 114 18.959 138.270 199.809 1.00101.23 O
ANISOU 691 O ALA A 114 13031 14954 10477 2074 1364 517 O
ATOM 692 CB ALA A 114 20.860 137.946 202.481 1.00101.66 C
ANISOU 692 CB ALA A 114 12839 15506 10282 2509 1358 630 C
ATOM 693 N ALA A 115 18.393 136.472 201.069 1.00 97.54 N
ANISOU 693 N ALA A 115 13003 14043 10015 2517 1494 449 N
ATOM 694 CA ALA A 115 17.868 135.638 199.987 1.00 97.36 C
ANISOU 694 CA ALA A 115 13204 13805 9983 2596 1558 379 C
ATOM 695 C ALA A 115 16.568 136.149 199.412 1.00 98.00 C
ANISOU 695 C ALA A 115 13417 13534 10283 2249 1524 341 C
ATOM 696 O ALA A 115 16.377 136.043 198.196 1.00 97.56 O
ANISOU 696 O ALA A 115 13422 13422 10223 2202 1545 298 O
ATOM 697 CB ALA A 115 17.700 134.204 200.456 1.00 99.69 C
ANISOU 697 CB ALA A 115 13826 13873 10178 2969 1636 339 C
ATOM 698 N VAL A 116 15.665 136.685 200.270 1.00 91.96 N
ANISOU 698 N VAL A 116 12695 12555 9692 2029 1472 352 N
ATOM 699 CA VAL A 116 14.381 137.221 199.804 1.00 89.38 C
ANISOU 699 CA VAL A 116 12461 11947 9551 1715 1432 317 C
ATOM 700 C VAL A 116 14.605 138.547 199.055 1.00 94.23 C
ANISOU 700 C VAL A 116 12830 12763 10212 1438 1334 333 C
ATOM 701 O VAL A 116 14.008 138.739 197.990 1.00 93.59 O
ANISOU 701 O VAL A 116 12799 12553 10208 1257 1323 298 O
ATOM 702 CB VAL A 116 13.276 137.301 200.884 1.00 90.67 C
ANISOU 702 CB VAL A 116 12760 11843 9847 1610 1412 317 C
ATOM 703 CG1 VAL A 116 11.976 137.851 200.308 1.00 88.67 C
ANISOU 703 CG1 VAL A 116 12567 11376 9749 1314 1370 278 C
ATOM 704 CG2 VAL A 116 13.017 135.936 201.498 1.00 91.30 C
ANISOU 704 CG2 VAL A 116 13114 11705 9870 1832 1496 323 C
ATOM 705 N PHE A 117 15.515 139.415 199.563 1.00 91.43 N
ANISOU 705 N PHE A 117 12219 12729 9791 1397 1254 395 N
ATOM 706 CA PHE A 117 15.847 140.688 198.916 1.00 91.06 C
ANISOU 706 CA PHE A 117 11955 12886 9756 1110 1130 437 C
ATOM 707 C PHE A 117 16.377 140.475 197.508 1.00 95.98 C
ANISOU 707 C PHE A 117 12482 13722 10264 1130 1176 450 C
ATOM 708 O PHE A 117 15.876 141.098 196.572 1.00 94.45 O
ANISOU 708 O PHE A 117 12258 13490 10140 876 1114 449 O
ATOM 709 CB PHE A 117 16.863 141.491 199.736 1.00 93.72 C
ANISOU 709 CB PHE A 117 12060 13534 10014 1052 1021 518 C
ATOM 710 CG PHE A 117 17.074 142.899 199.226 1.00 95.37 C
ANISOU 710 CG PHE A 117 12102 13891 10242 696 849 577 C
ATOM 711 CD1 PHE A 117 16.285 143.948 199.685 1.00 97.64 C
ANISOU 711 CD1 PHE A 117 12472 13950 10678 449 696 553 C
ATOM 712 CD2 PHE A 117 18.076 143.181 198.308 1.00 98.62 C
ANISOU 712 CD2 PHE A 117 12287 14683 10500 615 826 661 C
ATOM 713 CE1 PHE A 117 16.498 145.253 199.237 1.00 98.57 C
ANISOU 713 CE1 PHE A 117 12490 14162 10801 118 506 612 C
ATOM 714 CE2 PHE A 117 18.283 144.483 197.856 1.00101.57 C
ANISOU 714 CE2 PHE A 117 12531 15182 10880 245 646 738 C
ATOM 715 CZ PHE A 117 17.491 145.510 198.321 1.00 98.52 C
ANISOU 715 CZ PHE A 117 12272 14509 10653 -5 479 713 C
ATOM 716 N ALA A 118 17.390 139.601 197.369 1.00 95.25 N
ANISOU 716 N ALA A 118 12330 13885 9975 1447 1275 463 N
ATOM 717 CA ALA A 118 18.027 139.279 196.099 1.00 97.03 C
ANISOU 717 CA ALA A 118 12446 14381 10040 1542 1327 468 C
ATOM 718 C ALA A 118 17.053 138.681 195.086 1.00102.26 C
ANISOU 718 C ALA A 118 13354 14716 10786 1538 1390 376 C
ATOM 719 O ALA A 118 17.164 138.993 193.904 1.00103.21 O
ANISOU 719 O ALA A 118 13370 14986 10860 1427 1381 383 O
ATOM 720 CB ALA A 118 19.201 138.350 196.320 1.00100.10 C
ANISOU 720 CB ALA A 118 12756 15099 10180 1957 1416 480 C
ATOM 721 N SER A 119 16.073 137.874 195.545 1.00 97.93 N
ANISOU 721 N SER A 119 13122 13736 10351 1629 1444 303 N
ATOM 722 CA SER A 119 15.061 137.257 194.683 1.00 96.77 C
ANISOU 722 CA SER A 119 13238 13246 10283 1596 1492 221 C
ATOM 723 C SER A 119 14.070 138.290 194.122 1.00 97.49 C
ANISOU 723 C SER A 119 13298 13183 10559 1203 1416 217 C
ATOM 724 O SER A 119 13.894 138.366 192.908 1.00 96.92 O
ANISOU 724 O SER A 119 13245 13097 10484 1120 1428 185 O
ATOM 725 CB SER A 119 14.304 136.172 195.441 1.00100.79 C
ANISOU 725 CB SER A 119 14082 13370 10843 1747 1546 177 C
ATOM 726 OG SER A 119 15.166 135.157 195.925 1.00113.68 O
ANISOU 726 OG SER A 119 15814 15086 12293 2141 1607 169 O
ATOM 727 N ILE A 120 13.435 139.091 195.006 1.00 91.81 N
ANISOU 727 N ILE A 120 12546 12351 9987 990 1332 242 N
ATOM 728 CA ILE A 120 12.433 140.083 194.618 1.00 89.18 C
ANISOU 728 CA ILE A 120 12212 11856 9816 662 1243 228 C
ATOM 729 C ILE A 120 13.048 141.188 193.752 1.00 94.14 C
ANISOU 729 C ILE A 120 12604 12754 10410 447 1143 284 C
ATOM 730 O ILE A 120 12.406 141.619 192.790 1.00 93.74 O
ANISOU 730 O ILE A 120 12577 12604 10435 242 1104 264 O
ATOM 731 CB ILE A 120 11.597 140.621 195.829 1.00 90.23 C
ANISOU 731 CB ILE A 120 12407 11795 10082 560 1176 222 C
ATOM 732 CG1 ILE A 120 10.309 141.364 195.380 1.00 89.04 C
ANISOU 732 CG1 ILE A 120 12328 11424 10078 303 1106 179 C
ATOM 733 CG2 ILE A 120 12.410 141.466 196.809 1.00 90.20 C
ANISOU 733 CG2 ILE A 120 12223 12000 10048 539 1073 280 C
ATOM 734 CD1 ILE A 120 9.289 140.597 194.492 1.00 94.78 C
ANISOU 734 CD1 ILE A 120 13228 11941 10843 264 1189 124 C
ATOM 735 N TRP A 121 14.299 141.589 194.031 1.00 91.69 N
ANISOU 735 N TRP A 121 12067 12801 9969 485 1099 366 N
ATOM 736 CA TRP A 121 14.937 142.630 193.229 1.00 91.91 C
ANISOU 736 CA TRP A 121 11864 13124 9935 243 987 452 C
ATOM 737 C TRP A 121 15.518 142.083 191.932 1.00 96.33 C
ANISOU 737 C TRP A 121 12319 13945 10337 342 1073 464 C
ATOM 738 O TRP A 121 15.757 142.864 191.019 1.00 96.11 O
ANISOU 738 O TRP A 121 12130 14119 10269 106 991 533 O
ATOM 739 CB TRP A 121 15.940 143.450 194.042 1.00 91.68 C
ANISOU 739 CB TRP A 121 11629 13375 9829 154 866 553 C
ATOM 740 CG TRP A 121 15.231 144.353 195.005 1.00 91.42 C
ANISOU 740 CG TRP A 121 11702 13074 9958 -37 723 536 C
ATOM 741 CD1 TRP A 121 14.964 144.096 196.317 1.00 93.71 C
ANISOU 741 CD1 TRP A 121 12104 13187 10313 102 736 490 C
ATOM 742 CD2 TRP A 121 14.537 145.571 194.685 1.00 90.36 C
ANISOU 742 CD2 TRP A 121 11617 12777 9938 -361 551 542 C
ATOM 743 NE1 TRP A 121 14.197 145.106 196.851 1.00 92.12 N
ANISOU 743 NE1 TRP A 121 11993 12767 10242 -101 578 465 N
ATOM 744 CE2 TRP A 121 13.927 146.030 195.874 1.00 93.38 C
ANISOU 744 CE2 TRP A 121 12134 12914 10434 -377 457 491 C
ATOM 745 CE3 TRP A 121 14.403 146.340 193.516 1.00 91.51 C
ANISOU 745 CE3 TRP A 121 11712 12972 10084 -629 455 588 C
ATOM 746 CZ2 TRP A 121 13.217 147.236 195.936 1.00 91.86 C
ANISOU 746 CZ2 TRP A 121 12039 12521 10342 -619 262 472 C
ATOM 747 CZ3 TRP A 121 13.684 147.523 193.574 1.00 92.10 C
ANISOU 747 CZ3 TRP A 121 11896 12824 10273 -892 261 580 C
ATOM 748 CH2 TRP A 121 13.099 147.959 194.773 1.00 91.90 C
ANISOU 748 CH2 TRP A 121 12021 12548 10349 -869 163 515 C
ATOM 749 N SER A 122 15.669 140.751 191.806 1.00 93.78 N
ANISOU 749 N SER A 122 12119 13593 9921 688 1224 394 N
ATOM 750 CA SER A 122 16.096 140.162 190.540 1.00 95.11 C
ANISOU 750 CA SER A 122 12239 13968 9929 840 1306 372 C
ATOM 751 C SER A 122 14.872 140.122 189.635 1.00 99.64 C
ANISOU 751 C SER A 122 13010 14203 10646 685 1318 294 C
ATOM 752 O SER A 122 14.991 140.324 188.426 1.00100.22 O
ANISOU 752 O SER A 122 12988 14444 10647 612 1321 303 O
ATOM 753 CB SER A 122 16.672 138.768 190.737 1.00 98.89 C
ANISOU 753 CB SER A 122 12831 14505 10239 1299 1433 311 C
ATOM 754 OG SER A 122 17.989 138.874 191.249 1.00107.12 O
ANISOU 754 OG SER A 122 13611 16006 11084 1458 1428 395 O
ATOM 755 N MET A 123 13.684 139.921 190.240 1.00 95.79 N
ANISOU 755 N MET A 123 12775 13272 10347 621 1320 227 N
ATOM 756 CA MET A 123 12.407 139.915 189.533 1.00 95.06 C
ANISOU 756 CA MET A 123 12869 12853 10397 451 1324 159 C
ATOM 757 C MET A 123 12.152 141.308 188.938 1.00 98.72 C
ANISOU 757 C MET A 123 13179 13381 10949 93 1200 212 C
ATOM 758 O MET A 123 11.770 141.417 187.759 1.00 99.08 O
ANISOU 758 O MET A 123 13257 13370 11020 -29 1204 183 O
ATOM 759 CB MET A 123 11.268 139.517 190.472 1.00 96.29 C
ANISOU 759 CB MET A 123 13269 12615 10701 443 1339 107 C
ATOM 760 CG MET A 123 11.192 138.051 190.729 1.00101.59 C
ANISOU 760 CG MET A 123 14193 13103 11302 723 1446 47 C
ATOM 761 SD MET A 123 9.795 137.743 191.818 1.00105.88 S
ANISOU 761 SD MET A 123 14992 13229 12007 614 1447 21 S
ATOM 762 CE MET A 123 9.993 136.008 192.095 1.00104.78 C
ANISOU 762 CE MET A 123 15154 12919 11738 950 1539 -13 C
ATOM 763 N THR A 124 12.427 142.369 189.746 1.00 92.93 N
ANISOU 763 N THR A 124 12301 12755 10254 -71 1076 290 N
ATOM 764 CA THR A 124 12.284 143.781 189.371 1.00 90.89 C
ANISOU 764 CA THR A 124 11939 12529 10065 -411 912 352 C
ATOM 765 C THR A 124 13.207 144.097 188.199 1.00 94.22 C
ANISOU 765 C THR A 124 12148 13308 10342 -517 890 436 C
ATOM 766 O THR A 124 12.818 144.835 187.296 1.00 92.96 O
ANISOU 766 O THR A 124 11984 13103 10232 -752 818 452 O
ATOM 767 CB THR A 124 12.537 144.710 190.588 1.00 94.92 C
ANISOU 767 CB THR A 124 12404 13039 10624 -518 770 404 C
ATOM 768 OG1 THR A 124 12.005 144.135 191.785 1.00 94.14 O
ANISOU 768 OG1 THR A 124 12468 12694 10608 -342 829 330 O
ATOM 769 CG2 THR A 124 11.954 146.094 190.400 1.00 88.94 C
ANISOU 769 CG2 THR A 124 11667 12159 9967 -839 574 432 C
ATOM 770 N ALA A 125 14.414 143.501 188.201 1.00 92.29 N
ANISOU 770 N ALA A 125 11725 13442 9900 -320 959 490 N
ATOM 771 CA ALA A 125 15.423 143.692 187.161 1.00 93.85 C
ANISOU 771 CA ALA A 125 11670 14091 9899 -366 957 582 C
ATOM 772 C ALA A 125 14.937 143.171 185.810 1.00 97.41 C
ANISOU 772 C ALA A 125 12202 14475 10334 -312 1049 507 C
ATOM 773 O ALA A 125 15.170 143.814 184.784 1.00 97.47 O
ANISOU 773 O ALA A 125 12047 14723 10265 -510 996 584 O
ATOM 774 CB ALA A 125 16.724 143.023 187.566 1.00 96.59 C
ANISOU 774 CB ALA A 125 11830 14854 10015 -70 1039 625 C
ATOM 775 N VAL A 126 14.217 142.040 185.821 1.00 93.23 N
ANISOU 775 N VAL A 126 11935 13619 9870 -67 1174 366 N
ATOM 776 CA VAL A 126 13.637 141.456 184.623 1.00 93.35 C
ANISOU 776 CA VAL A 126 12084 13504 9880 -8 1253 275 C
ATOM 777 C VAL A 126 12.516 142.368 184.122 1.00 98.27 C
ANISOU 777 C VAL A 126 12782 13865 10692 -357 1163 271 C
ATOM 778 O VAL A 126 12.419 142.597 182.920 1.00 97.50 O
ANISOU 778 O VAL A 126 12628 13867 10552 -461 1162 277 O
ATOM 779 CB VAL A 126 13.165 140.013 184.892 1.00 97.01 C
ANISOU 779 CB VAL A 126 12840 13678 10340 328 1380 139 C
ATOM 780 CG1 VAL A 126 12.321 139.475 183.735 1.00 96.51 C
ANISOU 780 CG1 VAL A 126 12977 13384 10307 324 1432 38 C
ATOM 781 CG2 VAL A 126 14.357 139.099 185.164 1.00 98.91 C
ANISOU 781 CG2 VAL A 126 13011 14226 10343 722 1461 135 C
ATOM 782 N ALA A 127 11.706 142.921 185.055 1.00 96.40 N
ANISOU 782 N ALA A 127 12658 13329 10642 -519 1080 265 N
ATOM 783 CA ALA A 127 10.605 143.845 184.763 1.00 95.59 C
ANISOU 783 CA ALA A 127 12632 12984 10704 -812 975 257 C
ATOM 784 C ALA A 127 11.127 145.140 184.153 1.00102.14 C
ANISOU 784 C ALA A 127 13261 14058 11489 -1103 823 383 C
ATOM 785 O ALA A 127 10.571 145.598 183.158 1.00101.90 O
ANISOU 785 O ALA A 127 13245 13976 11498 -1289 776 386 O
ATOM 786 CB ALA A 127 9.805 144.136 186.025 1.00 94.85 C
ANISOU 786 CB ALA A 127 12681 12590 10767 -850 916 220 C
ATOM 787 N PHE A 128 12.216 145.701 184.705 1.00101.02 N
ANISOU 787 N PHE A 128 12939 14189 11255 -1159 735 498 N
ATOM 788 CA PHE A 128 12.823 146.906 184.159 1.00102.91 C
ANISOU 788 CA PHE A 128 12995 14686 11422 -1474 565 649 C
ATOM 789 C PHE A 128 13.302 146.647 182.721 1.00106.52 C
ANISOU 789 C PHE A 128 13280 15476 11717 -1487 634 699 C
ATOM 790 O PHE A 128 13.008 147.454 181.843 1.00106.28 O
ANISOU 790 O PHE A 128 13205 15486 11692 -1772 521 775 O
ATOM 791 CB PHE A 128 13.963 147.406 185.064 1.00107.28 C
ANISOU 791 CB PHE A 128 13382 15507 11873 -1524 468 768 C
ATOM 792 CG PHE A 128 14.877 148.449 184.452 1.00112.53 C
ANISOU 792 CG PHE A 128 13824 16533 12401 -1864 294 960 C
ATOM 793 CD1 PHE A 128 16.072 148.079 183.832 1.00119.37 C
ANISOU 793 CD1 PHE A 128 14391 17945 13021 -1820 355 1076 C
ATOM 794 CD2 PHE A 128 14.562 149.804 184.520 1.00115.81 C
ANISOU 794 CD2 PHE A 128 14336 16759 12907 -2227 53 1034 C
ATOM 795 CE1 PHE A 128 16.921 149.043 183.262 1.00122.85 C
ANISOU 795 CE1 PHE A 128 14604 18764 13308 -2181 183 1283 C
ATOM 796 CE2 PHE A 128 15.420 150.771 183.966 1.00121.36 C
ANISOU 796 CE2 PHE A 128 14861 17781 13468 -2588 -136 1236 C
ATOM 797 CZ PHE A 128 16.596 150.384 183.344 1.00121.89 C
ANISOU 797 CZ PHE A 128 14604 18418 13290 -2586 -67 1370 C
ATOM 798 N ASP A 129 14.005 145.513 182.484 1.00103.18 N
ANISOU 798 N ASP A 129 12779 15283 11140 -1158 812 650 N
ATOM 799 CA ASP A 129 14.545 145.112 181.175 1.00104.14 C
ANISOU 799 CA ASP A 129 12735 15763 11069 -1085 894 675 C
ATOM 800 C ASP A 129 13.477 144.991 180.079 1.00105.62 C
ANISOU 800 C ASP A 129 13078 15698 11353 -1154 928 585 C
ATOM 801 O ASP A 129 13.726 145.402 178.942 1.00105.88 O
ANISOU 801 O ASP A 129 12954 16000 11274 -1293 905 657 O
ATOM 802 CB ASP A 129 15.361 143.808 181.282 1.00107.62 C
ANISOU 802 CB ASP A 129 13116 16464 11311 -645 1063 611 C
ATOM 803 CG ASP A 129 15.978 143.366 179.965 1.00121.65 C
ANISOU 803 CG ASP A 129 14663 18730 12828 -537 1128 652 C
ATOM 804 OD1 ASP A 129 17.038 143.920 179.588 1.00123.46 O
ANISOU 804 OD1 ASP A 129 14572 19453 12884 -730 1046 827 O
ATOM 805 OD2 ASP A 129 15.373 142.504 179.288 1.00129.34 O
ANISOU 805 OD2 ASP A 129 15780 19606 13758 -276 1248 516 O
ATOM 806 N ARG A 130 12.305 144.415 180.419 1.00 99.37 N
ANISOU 806 N ARG A 130 12578 14426 10751 -1064 983 438 N
ATOM 807 CA ARG A 130 11.201 144.239 179.478 1.00 97.39 C
ANISOU 807 CA ARG A 130 12484 13924 10595 -1139 1012 349 C
ATOM 808 C ARG A 130 10.578 145.574 179.167 1.00100.27 C
ANISOU 808 C ARG A 130 12829 14191 11077 -1520 842 432 C
ATOM 809 O ARG A 130 10.316 145.846 178.000 1.00100.74 O
ANISOU 809 O ARG A 130 12827 14352 11097 -1666 820 462 O
ATOM 810 CB ARG A 130 10.149 143.231 179.982 1.00 94.94 C
ANISOU 810 CB ARG A 130 12474 13174 10423 -966 1106 191 C
ATOM 811 CG ARG A 130 10.668 141.821 180.303 1.00102.10 C
ANISOU 811 CG ARG A 130 13487 14087 11220 -584 1248 103 C
ATOM 812 CD ARG A 130 11.094 140.992 179.103 1.00106.47 C
ANISOU 812 CD ARG A 130 14043 14819 11590 -361 1349 38 C
ATOM 813 NE ARG A 130 12.399 141.412 178.594 1.00114.82 N
ANISOU 813 NE ARG A 130 14796 16408 12422 -281 1347 139 N
ATOM 814 CZ ARG A 130 12.634 141.738 177.328 1.00129.53 C
ANISOU 814 CZ ARG A 130 16466 18594 14156 -377 1333 194 C
ATOM 815 NH1 ARG A 130 11.665 141.660 176.422 1.00108.79 N
ANISOU 815 NH1 ARG A 130 13941 15784 11612 -534 1326 144 N
ATOM 816 NH2 ARG A 130 13.845 142.132 176.955 1.00121.35 N
ANISOU 816 NH2 ARG A 130 15120 18098 12890 -318 1327 308 N
ATOM 817 N TYR A 131 10.412 146.436 180.195 1.00 95.45 N
ANISOU 817 N TYR A 131 12272 13405 10588 -1667 708 472 N
ATOM 818 CA TYR A 131 9.866 147.789 180.060 1.00 94.66 C
ANISOU 818 CA TYR A 131 12209 13168 10590 -1997 505 544 C
ATOM 819 C TYR A 131 10.742 148.627 179.111 1.00103.71 C
ANISOU 819 C TYR A 131 13138 14675 11591 -2260 389 716 C
ATOM 820 O TYR A 131 10.233 149.199 178.148 1.00103.45 O
ANISOU 820 O TYR A 131 13134 14587 11587 -2470 307 747 O
ATOM 821 CB TYR A 131 9.732 148.442 181.444 1.00 94.02 C
ANISOU 821 CB TYR A 131 12218 12900 10607 -2035 378 554 C
ATOM 822 CG TYR A 131 9.119 149.823 181.438 1.00 93.98 C
ANISOU 822 CG TYR A 131 12327 12680 10701 -2310 146 595 C
ATOM 823 CD1 TYR A 131 7.750 149.999 181.610 1.00 94.34 C
ANISOU 823 CD1 TYR A 131 12582 12368 10896 -2285 125 476 C
ATOM 824 CD2 TYR A 131 9.918 150.961 181.350 1.00 95.84 C
ANISOU 824 CD2 TYR A 131 12478 13074 10863 -2588 -70 755 C
ATOM 825 CE1 TYR A 131 7.185 151.273 181.648 1.00 95.58 C
ANISOU 825 CE1 TYR A 131 12870 12326 11119 -2481 -102 498 C
ATOM 826 CE2 TYR A 131 9.363 152.239 181.368 1.00 96.55 C
ANISOU 826 CE2 TYR A 131 12732 12924 11028 -2823 -315 786 C
ATOM 827 CZ TYR A 131 7.995 152.392 181.516 1.00102.75 C
ANISOU 827 CZ TYR A 131 13737 13347 11958 -2742 -329 648 C
ATOM 828 OH TYR A 131 7.448 153.654 181.520 1.00103.20 O
ANISOU 828 OH TYR A 131 13978 13170 12065 -2923 -585 666 O
ATOM 829 N MET A 132 12.064 148.620 179.338 1.00103.77 N
ANISOU 829 N MET A 132 12916 15091 11421 -2241 391 834 N
ATOM 830 CA MET A 132 13.037 149.351 178.531 1.00106.46 C
ANISOU 830 CA MET A 132 13003 15870 11578 -2504 285 1029 C
ATOM 831 C MET A 132 13.143 148.850 177.086 1.00111.14 C
ANISOU 831 C MET A 132 13471 16713 12043 -2453 403 1024 C
ATOM 832 O MET A 132 13.703 149.546 176.236 1.00112.89 O
ANISOU 832 O MET A 132 13523 17227 12144 -2734 296 1184 O
ATOM 833 CB MET A 132 14.415 149.333 179.213 1.00111.17 C
ANISOU 833 CB MET A 132 13358 16892 11990 -2469 273 1153 C
ATOM 834 CG MET A 132 14.495 150.212 180.442 1.00115.18 C
ANISOU 834 CG MET A 132 13951 17227 12585 -2644 85 1215 C
ATOM 835 SD MET A 132 14.105 151.955 180.137 1.00120.26 S
ANISOU 835 SD MET A 132 14733 17644 13315 -3159 -247 1353 S
ATOM 836 CE MET A 132 15.573 152.469 179.262 1.00120.27 C
ANISOU 836 CE MET A 132 14373 18299 13024 -3492 -341 1628 C
ATOM 837 N ALA A 133 12.645 147.640 176.816 1.00105.47 N
ANISOU 837 N ALA A 133 12849 15890 11336 -2108 609 849 N
ATOM 838 CA ALA A 133 12.713 147.060 175.485 1.00105.58 C
ANISOU 838 CA ALA A 133 12775 16120 11219 -2011 723 816 C
ATOM 839 C ALA A 133 11.415 147.291 174.737 1.00107.08 C
ANISOU 839 C ALA A 133 13169 15940 11576 -2141 704 729 C
ATOM 840 O ALA A 133 11.446 147.587 173.539 1.00107.68 O
ANISOU 840 O ALA A 133 13143 16209 11563 -2263 696 779 O
ATOM 841 CB ALA A 133 13.017 145.575 175.582 1.00106.96 C
ANISOU 841 CB ALA A 133 12970 16394 11275 -1554 930 674 C
ATOM 842 N ILE A 134 10.271 147.145 175.442 1.00100.42 N
ANISOU 842 N ILE A 134 12597 14603 10956 -2106 700 603 N
ATOM 843 CA ILE A 134 8.934 147.309 174.871 1.00 97.60 C
ANISOU 843 CA ILE A 134 12436 13893 10756 -2207 684 511 C
ATOM 844 C ILE A 134 8.590 148.789 174.723 1.00101.85 C
ANISOU 844 C ILE A 134 12984 14342 11373 -2570 462 631 C
ATOM 845 O ILE A 134 8.101 149.193 173.666 1.00102.16 O
ANISOU 845 O ILE A 134 13032 14368 11418 -2733 417 651 O
ATOM 846 CB ILE A 134 7.847 146.558 175.701 1.00 97.79 C
ANISOU 846 CB ILE A 134 12721 13486 10949 -2021 767 341 C
ATOM 847 CG1 ILE A 134 8.244 145.079 176.067 1.00 97.97 C
ANISOU 847 CG1 ILE A 134 12795 13537 10893 -1662 948 236 C
ATOM 848 CG2 ILE A 134 6.468 146.627 175.040 1.00 96.69 C
ANISOU 848 CG2 ILE A 134 12748 13061 10929 -2107 771 247 C
ATOM 849 CD1 ILE A 134 8.584 144.066 175.005 1.00103.53 C
ANISOU 849 CD1 ILE A 134 13482 14415 11438 -1448 1088 164 C
ATOM 850 N ILE A 135 8.857 149.588 175.776 1.00 97.40 N
ANISOU 850 N ILE A 135 12445 13702 10862 -2687 311 706 N
ATOM 851 CA ILE A 135 8.485 151.001 175.857 1.00 96.20 C
ANISOU 851 CA ILE A 135 12388 13377 10788 -2996 65 799 C
ATOM 852 C ILE A 135 9.574 151.944 175.284 1.00102.29 C
ANISOU 852 C ILE A 135 12968 14499 11400 -3320 -107 1028 C
ATOM 853 O ILE A 135 9.206 152.859 174.549 1.00101.19 O
ANISOU 853 O ILE A 135 12885 14291 11271 -3578 -261 1105 O
ATOM 854 CB ILE A 135 8.024 151.388 177.310 1.00 97.16 C
ANISOU 854 CB ILE A 135 12693 13178 11046 -2942 -36 738 C
ATOM 855 CG1 ILE A 135 7.094 150.326 177.948 1.00 94.79 C
ANISOU 855 CG1 ILE A 135 12533 12620 10862 -2633 149 543 C
ATOM 856 CG2 ILE A 135 7.386 152.772 177.392 1.00 97.68 C
ANISOU 856 CG2 ILE A 135 12939 12980 11194 -3183 -302 783 C
ATOM 857 CD1 ILE A 135 5.824 149.886 177.136 1.00 99.02 C
ANISOU 857 CD1 ILE A 135 13198 12940 11485 -2579 237 416 C
ATOM 858 N HIS A 136 10.878 151.723 175.577 1.00102.13 N
ANISOU 858 N HIS A 136 12722 14864 11217 -3318 -89 1145 N
ATOM 859 CA HIS A 136 11.958 152.600 175.065 1.00105.30 C
ANISOU 859 CA HIS A 136 12913 15661 11435 -3664 -260 1391 C
ATOM 860 C HIS A 136 13.032 151.837 174.246 1.00112.72 C
ANISOU 860 C HIS A 136 13512 17189 12128 -3556 -90 1466 C
ATOM 861 O HIS A 136 14.140 151.605 174.757 1.00112.61 O
ANISOU 861 O HIS A 136 13286 17545 11956 -3510 -69 1558 O
ATOM 862 CB HIS A 136 12.590 153.423 176.201 1.00107.12 C
ANISOU 862 CB HIS A 136 13163 15881 11655 -3839 -459 1506 C
ATOM 863 CG HIS A 136 11.597 153.944 177.194 1.00108.97 C
ANISOU 863 CG HIS A 136 13725 15573 12107 -3803 -583 1384 C
ATOM 864 ND1 HIS A 136 10.735 154.979 176.877 1.00110.53 N
ANISOU 864 ND1 HIS A 136 14163 15432 12400 -4041 -817 1407 N
ATOM 865 CD2 HIS A 136 11.354 153.542 178.465 1.00109.41 C
ANISOU 865 CD2 HIS A 136 13895 15403 12274 -3534 -505 1240 C
ATOM 866 CE1 HIS A 136 10.005 155.178 177.963 1.00108.56 C
ANISOU 866 CE1 HIS A 136 14154 14786 12306 -3887 -870 1266 C
ATOM 867 NE2 HIS A 136 10.343 154.340 178.945 1.00108.14 N
ANISOU 867 NE2 HIS A 136 14026 14793 12270 -3597 -685 1169 N
ATOM 868 N PRO A 137 12.723 151.442 172.974 1.00111.82 N
ANISOU 868 N PRO A 137 13335 17195 11955 -3492 30 1423 N
ATOM 869 CA PRO A 137 13.679 150.633 172.197 1.00114.59 C
ANISOU 869 CA PRO A 137 13377 18115 12048 -3315 197 1464 C
ATOM 870 C PRO A 137 14.859 151.382 171.608 1.00125.44 C
ANISOU 870 C PRO A 137 14427 20070 13166 -3653 65 1740 C
ATOM 871 O PRO A 137 15.874 150.746 171.306 1.00126.97 O
ANISOU 871 O PRO A 137 14315 20823 13103 -3485 187 1796 O
ATOM 872 CB PRO A 137 12.816 149.997 171.099 1.00114.92 C
ANISOU 872 CB PRO A 137 13513 18021 12130 -3119 354 1299 C
ATOM 873 CG PRO A 137 11.401 150.375 171.412 1.00116.50 C
ANISOU 873 CG PRO A 137 14049 17606 12611 -3214 275 1185 C
ATOM 874 CD PRO A 137 11.471 151.622 172.217 1.00111.90 C
ANISOU 874 CD PRO A 137 13549 16853 12114 -3538 26 1322 C
ATOM 875 N LEU A 138 14.727 152.713 171.430 1.00125.75 N
ANISOU 875 N LEU A 138 14536 19992 13250 -4121 -192 1917 N
ATOM 876 CA LEU A 138 15.785 153.564 170.877 1.00129.90 C
ANISOU 876 CA LEU A 138 14784 21042 13531 -4542 -365 2220 C
ATOM 877 C LEU A 138 16.946 153.710 171.873 1.00138.57 C
ANISOU 877 C LEU A 138 15677 22501 14473 -4611 -428 2366 C
ATOM 878 O LEU A 138 18.103 153.761 171.451 1.00140.72 O
ANISOU 878 O LEU A 138 15575 23447 14447 -4732 -425 2565 O
ATOM 879 CB LEU A 138 15.245 154.933 170.428 1.00130.05 C
ANISOU 879 CB LEU A 138 15014 20750 13650 -5028 -658 2367 C
ATOM 880 CG LEU A 138 14.060 154.912 169.463 1.00132.76 C
ANISOU 880 CG LEU A 138 15568 20729 14145 -5002 -631 2243 C
ATOM 881 CD1 LEU A 138 12.982 155.873 169.910 1.00132.42 C
ANISOU 881 CD1 LEU A 138 15889 20126 14299 -5295 -910 2271 C
ATOM 882 CD2 LEU A 138 14.492 155.215 168.063 1.00135.91 C
ANISOU 882 CD2 LEU A 138 15705 21608 14328 -5156 -598 2388 C
ATOM 883 N GLN A 139 16.645 153.739 173.188 1.00136.38 N
ANISOU 883 N GLN A 139 15623 21817 14380 -4516 -477 2264 N
ATOM 884 CA GLN A 139 17.696 153.806 174.200 1.00139.45 C
ANISOU 884 CA GLN A 139 15844 22498 14642 -4547 -529 2373 C
ATOM 885 C GLN A 139 18.001 152.405 174.751 1.00146.37 C
ANISOU 885 C GLN A 139 16617 23517 15480 -3991 -243 2181 C
ATOM 886 O GLN A 139 17.144 151.807 175.404 1.00144.00 O
ANISOU 886 O GLN A 139 16590 22713 15409 -3687 -142 1951 O
ATOM 887 CB GLN A 139 17.434 154.858 175.305 1.00140.48 C
ANISOU 887 CB GLN A 139 16257 22179 14941 -4837 -805 2424 C
ATOM 888 CG GLN A 139 16.113 154.735 176.077 1.00160.37 C
ANISOU 888 CG GLN A 139 19195 23952 17787 -4604 -790 2165 C
ATOM 889 CD GLN A 139 15.930 155.803 177.139 1.00186.10 C
ANISOU 889 CD GLN A 139 22716 26828 21164 -4839 -1068 2208 C
ATOM 890 OE1 GLN A 139 16.567 156.866 177.125 1.00186.88 O
ANISOU 890 OE1 GLN A 139 22801 27055 21149 -5288 -1349 2439 O
ATOM 891 NE2 GLN A 139 15.020 155.561 178.071 1.00175.44 N
ANISOU 891 NE2 GLN A 139 21633 24990 20035 -4549 -1014 1986 N
ATOM 892 N PRO A 140 19.187 151.833 174.443 1.00147.78 N
ANISOU 892 N PRO A 140 16406 24392 15351 -3836 -112 2272 N
ATOM 893 CA PRO A 140 19.492 150.483 174.932 1.00148.08 C
ANISOU 893 CA PRO A 140 16383 24549 15331 -3276 140 2085 C
ATOM 894 C PRO A 140 20.219 150.486 176.281 1.00155.01 C
ANISOU 894 C PRO A 140 17184 25549 16163 -3241 92 2141 C
ATOM 895 O PRO A 140 21.322 151.027 176.395 1.00157.33 O
ANISOU 895 O PRO A 140 17176 26378 16223 -3521 -33 2382 O
ATOM 896 CB PRO A 140 20.342 149.891 173.802 1.00152.31 C
ANISOU 896 CB PRO A 140 16553 25785 15532 -3085 292 2141 C
ATOM 897 CG PRO A 140 20.920 151.107 173.059 1.00159.08 C
ANISOU 897 CG PRO A 140 17148 27096 16200 -3648 85 2454 C
ATOM 898 CD PRO A 140 20.302 152.360 173.629 1.00153.20 C
ANISOU 898 CD PRO A 140 16687 25819 15702 -4145 -192 2552 C
ATOM 899 N ARG A 141 19.583 149.903 177.312 1.00151.20 N
ANISOU 899 N ARG A 141 16976 24575 15900 -2924 181 1929 N
ATOM 900 CA ARG A 141 20.156 149.797 178.664 1.00152.23 C
ANISOU 900 CA ARG A 141 17075 24751 16016 -2824 160 1941 C
ATOM 901 C ARG A 141 20.584 148.340 178.984 1.00156.58 C
ANISOU 901 C ARG A 141 17539 25516 16440 -2229 420 1782 C
ATOM 902 O ARG A 141 20.851 147.984 180.144 1.00156.12 O
ANISOU 902 O ARG A 141 17520 25391 16407 -2027 453 1729 O
ATOM 903 CB ARG A 141 19.213 150.400 179.731 1.00151.14 C
ANISOU 903 CB ARG A 141 17315 23910 16201 -2948 25 1848 C
ATOM 904 CG ARG A 141 19.255 151.928 179.779 1.00162.98 C
ANISOU 904 CG ARG A 141 18882 25295 17749 -3518 -290 2042 C
ATOM 905 CD ARG A 141 18.800 152.466 181.122 1.00173.15 C
ANISOU 905 CD ARG A 141 20462 26075 19254 -3570 -434 1972 C
ATOM 906 NE ARG A 141 18.446 153.886 181.047 1.00182.09 N
ANISOU 906 NE ARG A 141 21776 26949 20462 -4065 -754 2105 N
ATOM 907 CZ ARG A 141 17.995 154.608 182.069 1.00192.80 C
ANISOU 907 CZ ARG A 141 23406 27878 21972 -4184 -952 2072 C
ATOM 908 NH1 ARG A 141 17.841 154.054 183.267 1.00176.74 N
ANISOU 908 NH1 ARG A 141 21463 25651 20039 -3863 -851 1920 N
ATOM 909 NH2 ARG A 141 17.695 155.889 181.903 1.00178.02 N
ANISOU 909 NH2 ARG A 141 21734 25765 20139 -4614 -1265 2191 N
ATOM 910 N LEU A 142 20.675 147.515 177.921 1.00152.90 N
ANISOU 910 N LEU A 142 16967 25309 15818 -1944 590 1706 N
ATOM 911 CA LEU A 142 21.077 146.116 177.986 1.00152.64 C
ANISOU 911 CA LEU A 142 16891 25482 15624 -1354 816 1547 C
ATOM 912 C LEU A 142 22.568 146.008 177.695 1.00156.96 C
ANISOU 912 C LEU A 142 16966 26913 15758 -1265 842 1717 C
ATOM 913 O LEU A 142 23.016 146.404 176.612 1.00159.47 O
ANISOU 913 O LEU A 142 17001 27733 15859 -1461 808 1867 O
ATOM 914 CB LEU A 142 20.268 145.290 176.972 1.00151.87 C
ANISOU 914 CB LEU A 142 16983 25148 15571 -1084 959 1355 C
ATOM 915 N SER A 143 23.335 145.509 178.672 1.00150.83 N
ANISOU 915 N SER A 143 16088 26360 14859 -983 897 1707 N
ATOM 916 CA SER A 143 24.782 145.313 178.551 1.00153.08 C
ANISOU 916 CA SER A 143 15910 27527 14726 -835 932 1858 C
ATOM 917 C SER A 143 25.189 144.056 179.315 1.00155.84 C
ANISOU 917 C SER A 143 16318 27928 14965 -192 1104 1682 C
ATOM 918 O SER A 143 24.698 143.825 180.424 1.00153.74 O
ANISOU 918 O SER A 143 16372 27088 14953 -67 1117 1549 O
ATOM 919 CB SER A 143 25.547 146.538 179.054 1.00156.46 C
ANISOU 919 CB SER A 143 16066 28309 15074 -1371 724 2143 C
ATOM 920 OG SER A 143 26.953 146.362 178.992 1.00163.58 O
ANISOU 920 OG SER A 143 16478 30128 15546 -1265 752 2313 O
ATOM 921 N ALA A 144 26.065 143.235 178.709 1.00153.27 N
ANISOU 921 N ALA A 144 15697 28291 14247 236 1229 1676 N
ATOM 922 CA ALA A 144 26.546 141.982 179.297 1.00153.16 C
ANISOU 922 CA ALA A 144 15734 28400 14058 911 1382 1508 C
ATOM 923 C ALA A 144 27.330 142.228 180.575 1.00153.91 C
ANISOU 923 C ALA A 144 15670 28716 14093 893 1332 1616 C
ATOM 924 O ALA A 144 26.990 141.648 181.600 1.00151.39 O
ANISOU 924 O ALA A 144 15661 27907 13955 1163 1380 1464 O
ATOM 925 CB ALA A 144 27.395 141.221 178.293 1.00157.87 C
ANISOU 925 CB ALA A 144 16021 29760 14203 1361 1499 1492 C
ATOM 926 N THR A 145 28.336 143.124 180.525 1.00150.78 N
ANISOU 926 N THR A 145 14798 29049 13443 536 1224 1889 N
ATOM 927 CA THR A 145 29.171 143.494 181.665 1.00150.79 C
ANISOU 927 CA THR A 145 14588 29360 13346 446 1153 2028 C
ATOM 928 C THR A 145 28.345 144.103 182.803 1.00149.56 C
ANISOU 928 C THR A 145 14767 28447 13613 51 1017 2023 C
ATOM 929 O THR A 145 28.566 143.744 183.959 1.00149.79 O
ANISOU 929 O THR A 145 14826 28423 13663 192 1015 2006 O
ATOM 930 CB THR A 145 30.307 144.418 181.220 1.00161.20 C
ANISOU 930 CB THR A 145 15313 31661 14273 88 1049 2343 C
ATOM 931 N ALA A 146 27.375 144.986 182.475 1.00141.06 N
ANISOU 931 N ALA A 146 13946 26797 12855 -408 902 2029 N
ATOM 932 CA ALA A 146 26.518 145.663 183.455 1.00136.46 C
ANISOU 932 CA ALA A 146 13696 25496 12655 -761 760 2010 C
ATOM 933 C ALA A 146 25.612 144.724 184.257 1.00134.36 C
ANISOU 933 C ALA A 146 13871 24512 12669 -342 883 1742 C
ATOM 934 O ALA A 146 25.406 144.976 185.445 1.00132.65 O
ANISOU 934 O ALA A 146 13789 24002 12611 -408 817 1732 O
ATOM 935 CB ALA A 146 25.694 146.744 182.781 1.00135.58 C
ANISOU 935 CB ALA A 146 13727 25028 12760 -1314 596 2088 C
ATOM 936 N THR A 147 25.080 143.647 183.621 1.00127.57 N
ANISOU 936 N THR A 147 13235 23387 11848 76 1052 1533 N
ATOM 937 CA THR A 147 24.197 142.654 184.263 1.00123.70 C
ANISOU 937 CA THR A 147 13179 22231 11590 465 1168 1290 C
ATOM 938 C THR A 147 24.879 142.064 185.500 1.00126.99 C
ANISOU 938 C THR A 147 13568 22776 11907 815 1222 1263 C
ATOM 939 O THR A 147 24.254 141.955 186.561 1.00123.85 O
ANISOU 939 O THR A 147 13461 21839 11759 841 1212 1174 O
ATOM 940 CB THR A 147 23.762 141.580 183.250 1.00125.49 C
ANISOU 940 CB THR A 147 13586 22334 11761 867 1322 1106 C
ATOM 941 OG1 THR A 147 23.242 142.222 182.089 1.00121.27 O
ANISOU 941 OG1 THR A 147 13043 21726 11307 518 1265 1147 O
ATOM 942 CG2 THR A 147 22.717 140.618 183.815 1.00120.40 C
ANISOU 942 CG2 THR A 147 13424 20968 11354 1188 1414 876 C
ATOM 943 N LYS A 148 26.178 141.735 185.360 1.00126.18 N
ANISOU 943 N LYS A 148 13090 23433 11420 1077 1274 1353 N
ATOM 944 CA LYS A 148 27.019 141.210 186.429 1.00127.09 C
ANISOU 944 CA LYS A 148 13103 23820 11367 1433 1324 1352 C
ATOM 945 C LYS A 148 27.209 142.244 187.548 1.00130.63 C
ANISOU 945 C LYS A 148 13471 24213 11949 1012 1171 1496 C
ATOM 946 O LYS A 148 27.242 141.855 188.716 1.00130.52 O
ANISOU 946 O LYS A 148 13617 23953 12021 1232 1200 1422 O
ATOM 947 CB LYS A 148 28.364 140.720 185.882 1.00132.86 C
ANISOU 947 CB LYS A 148 13398 25470 11613 1784 1400 1431 C
ATOM 948 CG LYS A 148 28.253 139.407 185.127 1.00142.44 C
ANISOU 948 CG LYS A 148 14780 26683 12659 2418 1564 1226 C
ATOM 949 CD LYS A 148 28.458 139.612 183.646 1.00154.47 C
ANISOU 949 CD LYS A 148 16066 28650 13976 2341 1576 1279 C
ATOM 950 CE LYS A 148 27.696 138.605 182.822 1.00169.23 C
ANISOU 950 CE LYS A 148 18295 30135 15871 2773 1690 1039 C
ATOM 951 NZ LYS A 148 27.696 138.959 181.374 1.00180.78 N
ANISOU 951 NZ LYS A 148 19569 31910 17210 2595 1685 1091 N
ATOM 952 N VAL A 149 27.291 143.553 187.201 1.00126.04 N
ANISOU 952 N VAL A 149 12681 23823 11387 405 993 1697 N
ATOM 953 CA VAL A 149 27.425 144.654 188.171 1.00124.63 C
ANISOU 953 CA VAL A 149 12469 23552 11332 -49 804 1836 C
ATOM 954 C VAL A 149 26.104 144.817 188.950 1.00124.05 C
ANISOU 954 C VAL A 149 12878 22565 11692 -156 758 1683 C
ATOM 955 O VAL A 149 26.139 145.050 190.164 1.00123.09 O
ANISOU 955 O VAL A 149 12850 22233 11685 -207 688 1681 O
ATOM 956 CB VAL A 149 27.900 145.981 187.510 1.00129.99 C
ANISOU 956 CB VAL A 149 12828 24689 11875 -676 597 2105 C
ATOM 957 CG1 VAL A 149 28.005 147.119 188.527 1.00129.17 C
ANISOU 957 CG1 VAL A 149 12762 24416 11899 -1150 367 2234 C
ATOM 958 CG2 VAL A 149 29.233 145.789 186.798 1.00133.98 C
ANISOU 958 CG2 VAL A 149 12810 26184 11913 -561 650 2273 C
ATOM 959 N VAL A 150 24.947 144.665 188.256 1.00117.26 N
ANISOU 959 N VAL A 150 12308 21195 11049 -163 804 1550 N
ATOM 960 CA VAL A 150 23.617 144.767 188.873 1.00112.90 C
ANISOU 960 CA VAL A 150 12188 19836 10874 -230 776 1400 C
ATOM 961 C VAL A 150 23.450 143.641 189.890 1.00117.01 C
ANISOU 961 C VAL A 150 12907 20106 11444 249 919 1245 C
ATOM 962 O VAL A 150 23.189 143.927 191.058 1.00115.46 O
ANISOU 962 O VAL A 150 12853 19604 11412 172 849 1228 O
ATOM 963 CB VAL A 150 22.458 144.841 187.846 1.00113.60 C
ANISOU 963 CB VAL A 150 12515 19502 11146 -307 809 1294 C
ATOM 964 CG1 VAL A 150 21.103 144.858 188.545 1.00109.67 C
ANISOU 964 CG1 VAL A 150 12416 18255 10999 -385 772 1159 C
ATOM 965 CG2 VAL A 150 22.604 146.067 186.954 1.00114.16 C
ANISOU 965 CG2 VAL A 150 12388 19843 11145 -768 668 1459 C
ATOM 966 N ILE A 151 23.697 142.379 189.467 1.00115.18 N
ANISOU 966 N ILE A 151 12684 20038 11041 749 1102 1142 N
ATOM 967 CA ILE A 151 23.648 141.186 190.321 1.00114.95 C
ANISOU 967 CA ILE A 151 12862 19803 11009 1242 1233 1004 C
ATOM 968 C ILE A 151 24.606 141.358 191.524 1.00121.71 C
ANISOU 968 C ILE A 151 13510 21002 11734 1305 1191 1102 C
ATOM 969 O ILE A 151 24.251 140.986 192.644 1.00119.57 O
ANISOU 969 O ILE A 151 13452 20385 11593 1471 1216 1025 O
ATOM 970 CB ILE A 151 23.900 139.904 189.469 1.00119.35 C
ANISOU 970 CB ILE A 151 13479 20509 11359 1750 1396 884 C
ATOM 971 CG1 ILE A 151 22.650 139.556 188.628 1.00117.30 C
ANISOU 971 CG1 ILE A 151 13563 19692 11312 1710 1436 745 C
ATOM 972 CG2 ILE A 151 24.320 138.705 190.324 1.00121.23 C
ANISOU 972 CG2 ILE A 151 13850 20739 11471 2301 1504 788 C
ATOM 973 CD1 ILE A 151 22.927 138.898 187.287 1.00124.00 C
ANISOU 973 CD1 ILE A 151 14412 20754 11949 2030 1537 663 C
ATOM 974 N CYS A 152 25.776 141.997 191.291 1.00123.19 N
ANISOU 974 N CYS A 152 13271 21873 11661 1126 1115 1284 N
ATOM 975 CA CYS A 152 26.792 142.308 192.305 1.00126.13 C
ANISOU 975 CA CYS A 152 13378 22677 11868 1106 1051 1411 C
ATOM 976 C CYS A 152 26.254 143.304 193.348 1.00126.09 C
ANISOU 976 C CYS A 152 13522 22252 12136 696 884 1449 C
ATOM 977 O CYS A 152 26.393 143.058 194.551 1.00124.58 O
ANISOU 977 O CYS A 152 13393 21967 11973 867 894 1419 O
ATOM 978 CB CYS A 152 28.081 142.808 191.650 1.00131.21 C
ANISOU 978 CB CYS A 152 13520 24178 12155 935 993 1618 C
ATOM 979 SG CYS A 152 29.312 143.481 192.807 1.00138.08 S
ANISOU 979 SG CYS A 152 14028 25590 12847 642 833 1838 S
ATOM 980 N VAL A 153 25.634 144.414 192.884 1.00120.68 N
ANISOU 980 N VAL A 153 12911 21305 11636 186 725 1506 N
ATOM 981 CA VAL A 153 25.050 145.447 193.750 1.00118.19 C
ANISOU 981 CA VAL A 153 12774 20566 11565 -200 535 1527 C
ATOM 982 C VAL A 153 23.884 144.873 194.560 1.00117.86 C
ANISOU 982 C VAL A 153 13137 19835 11810 36 615 1329 C
ATOM 983 O VAL A 153 23.852 145.082 195.775 1.00116.54 O
ANISOU 983 O VAL A 153 13062 19477 11740 5 541 1317 O
ATOM 984 CB VAL A 153 24.689 146.737 192.972 1.00121.62 C
ANISOU 984 CB VAL A 153 13207 20919 12084 -766 328 1639 C
ATOM 985 CG1 VAL A 153 23.778 147.655 193.783 1.00119.19 C
ANISOU 985 CG1 VAL A 153 13203 20027 12058 -1060 141 1594 C
ATOM 986 CG2 VAL A 153 25.950 147.480 192.545 1.00124.63 C
ANISOU 986 CG2 VAL A 153 13178 22009 12168 -1099 192 1884 C
ATOM 987 N ILE A 154 22.974 144.102 193.891 1.00112.20 N
ANISOU 987 N ILE A 154 12649 18778 11204 269 763 1183 N
ATOM 988 CA ILE A 154 21.818 143.404 194.484 1.00109.36 C
ANISOU 988 CA ILE A 154 12661 17809 11081 490 855 1010 C
ATOM 989 C ILE A 154 22.238 142.649 195.760 1.00115.36 C
ANISOU 989 C ILE A 154 13447 18599 11784 831 930 977 C
ATOM 990 O ILE A 154 21.610 142.823 196.813 1.00114.10 O
ANISOU 990 O ILE A 154 13473 18075 11804 784 881 929 O
ATOM 991 CB ILE A 154 21.121 142.460 193.447 1.00111.23 C
ANISOU 991 CB ILE A 154 13093 17811 11358 716 1008 884 C
ATOM 992 CG1 ILE A 154 20.227 143.260 192.468 1.00109.98 C
ANISOU 992 CG1 ILE A 154 13014 17416 11357 346 921 883 C
ATOM 993 CG2 ILE A 154 20.316 141.335 194.134 1.00109.85 C
ANISOU 993 CG2 ILE A 154 13259 17158 11321 1040 1131 734 C
ATOM 994 CD1 ILE A 154 19.658 142.473 191.243 1.00112.78 C
ANISOU 994 CD1 ILE A 154 13471 17690 11690 502 1048 794 C
ATOM 995 N TRP A 155 23.329 141.856 195.661 1.00113.90 N
ANISOU 995 N TRP A 155 13061 18888 11327 1175 1036 1010 N
ATOM 996 CA TRP A 155 23.859 141.050 196.754 1.00114.27 C
ANISOU 996 CA TRP A 155 13114 19028 11275 1545 1112 987 C
ATOM 997 C TRP A 155 24.558 141.840 197.852 1.00118.64 C
ANISOU 997 C TRP A 155 13456 19846 11777 1348 980 1105 C
ATOM 998 O TRP A 155 24.474 141.441 199.012 1.00117.65 O
ANISOU 998 O TRP A 155 13439 19568 11694 1544 1007 1065 O
ATOM 999 CB TRP A 155 24.767 139.957 196.214 1.00115.39 C
ANISOU 999 CB TRP A 155 13132 19593 11119 2022 1258 970 C
ATOM 1000 CG TRP A 155 24.001 138.761 195.750 1.00115.55 C
ANISOU 1000 CG TRP A 155 13499 19205 11198 2365 1394 810 C
ATOM 1001 CD1 TRP A 155 23.805 138.364 194.462 1.00119.02 C
ANISOU 1001 CD1 TRP A 155 13974 19687 11561 2460 1456 757 C
ATOM 1002 CD2 TRP A 155 23.280 137.831 196.573 1.00114.12 C
ANISOU 1002 CD2 TRP A 155 13699 18502 11158 2628 1467 692 C
ATOM 1003 NE1 TRP A 155 23.039 137.223 194.430 1.00117.81 N
ANISOU 1003 NE1 TRP A 155 14217 19059 11486 2773 1554 607 N
ATOM 1004 CE2 TRP A 155 22.697 136.875 195.711 1.00118.08 C
ANISOU 1004 CE2 TRP A 155 14470 18740 11654 2864 1559 574 C
ATOM 1005 CE3 TRP A 155 23.089 137.698 197.961 1.00114.42 C
ANISOU 1005 CE3 TRP A 155 13877 18290 11309 2684 1455 683 C
ATOM 1006 CZ2 TRP A 155 21.950 135.790 196.188 1.00116.66 C
ANISOU 1006 CZ2 TRP A 155 14707 18046 11573 3119 1626 461 C
ATOM 1007 CZ3 TRP A 155 22.338 136.631 198.432 1.00115.28 C
ANISOU 1007 CZ3 TRP A 155 14373 17914 11515 2945 1535 576 C
ATOM 1008 CH2 TRP A 155 21.786 135.686 197.552 1.00116.18 C
ANISOU 1008 CH2 TRP A 155 14763 17762 11617 3143 1612 473 C
ATOM 1009 N VAL A 156 25.252 142.941 197.497 1.00116.26 N
ANISOU 1009 N VAL A 156 12862 19941 11370 953 828 1259 N
ATOM 1010 CA VAL A 156 25.935 143.817 198.458 1.00116.65 C
ANISOU 1010 CA VAL A 156 12722 20240 11358 695 664 1385 C
ATOM 1011 C VAL A 156 24.861 144.441 199.364 1.00115.82 C
ANISOU 1011 C VAL A 156 12923 19528 11556 483 545 1309 C
ATOM 1012 O VAL A 156 24.935 144.313 200.590 1.00115.09 O
ANISOU 1012 O VAL A 156 12882 19356 11491 608 534 1285 O
ATOM 1013 CB VAL A 156 26.820 144.877 197.730 1.00123.13 C
ANISOU 1013 CB VAL A 156 13192 21607 11983 260 502 1586 C
ATOM 1014 CG1 VAL A 156 27.116 146.087 198.615 1.00123.45 C
ANISOU 1014 CG1 VAL A 156 13156 21715 12035 -152 264 1708 C
ATOM 1015 CG2 VAL A 156 28.118 144.255 197.213 1.00126.20 C
ANISOU 1015 CG2 VAL A 156 13202 22745 12003 528 619 1678 C
ATOM 1016 N LEU A 157 23.826 145.036 198.737 1.00108.73 N
ANISOU 1016 N LEU A 157 12231 18212 10870 209 468 1260 N
ATOM 1017 CA LEU A 157 22.698 145.657 199.413 1.00105.44 C
ANISOU 1017 CA LEU A 157 12110 17232 10721 37 354 1172 C
ATOM 1018 C LEU A 157 21.911 144.641 200.256 1.00108.60 C
ANISOU 1018 C LEU A 157 12766 17237 11260 418 516 1019 C
ATOM 1019 O LEU A 157 21.526 144.962 201.383 1.00106.43 O
ANISOU 1019 O LEU A 157 12635 16693 11110 389 439 972 O
ATOM 1020 CB LEU A 157 21.790 146.357 198.392 1.00103.56 C
ANISOU 1020 CB LEU A 157 12017 16694 10638 -280 256 1152 C
ATOM 1021 CG LEU A 157 22.409 147.509 197.594 1.00109.07 C
ANISOU 1021 CG LEU A 157 12532 17678 11232 -741 44 1314 C
ATOM 1022 CD1 LEU A 157 21.434 148.046 196.592 1.00107.80 C
ANISOU 1022 CD1 LEU A 157 12544 17193 11222 -970 -15 1275 C
ATOM 1023 CD2 LEU A 157 22.857 148.640 198.491 1.00111.56 C
ANISOU 1023 CD2 LEU A 157 12852 17991 11544 -1053 -213 1394 C
ATOM 1024 N ALA A 158 21.720 143.407 199.725 1.00106.26 N
ANISOU 1024 N ALA A 158 12535 16919 10920 772 725 949 N
ATOM 1025 CA ALA A 158 21.004 142.313 200.396 1.00105.14 C
ANISOU 1025 CA ALA A 158 12654 16416 10877 1117 875 828 C
ATOM 1026 C ALA A 158 21.670 141.880 201.708 1.00110.82 C
ANISOU 1026 C ALA A 158 13320 17284 11501 1370 907 847 C
ATOM 1027 O ALA A 158 20.974 141.755 202.719 1.00108.93 O
ANISOU 1027 O ALA A 158 13273 16714 11402 1426 906 786 O
ATOM 1028 CB ALA A 158 20.853 141.118 199.459 1.00106.19 C
ANISOU 1028 CB ALA A 158 12887 16515 10944 1410 1051 763 C
ATOM 1029 N LEU A 159 23.013 141.667 201.694 1.00110.39 N
ANISOU 1029 N LEU A 159 12991 17760 11192 1531 935 936 N
ATOM 1030 CA LEU A 159 23.794 141.239 202.868 1.00111.24 C
ANISOU 1030 CA LEU A 159 13010 18087 11170 1792 967 965 C
ATOM 1031 C LEU A 159 23.933 142.348 203.909 1.00114.13 C
ANISOU 1031 C LEU A 159 13290 18479 11594 1499 787 1024 C
ATOM 1032 O LEU A 159 24.092 142.048 205.093 1.00113.40 O
ANISOU 1032 O LEU A 159 13229 18370 11489 1683 804 1012 O
ATOM 1033 CB LEU A 159 25.174 140.678 202.480 1.00114.18 C
ANISOU 1033 CB LEU A 159 13094 19069 11222 2073 1047 1041 C
ATOM 1034 CG LEU A 159 25.213 139.530 201.459 1.00119.93 C
ANISOU 1034 CG LEU A 159 13904 19835 11830 2435 1209 973 C
ATOM 1035 CD1 LEU A 159 26.558 139.454 200.798 1.00123.21 C
ANISOU 1035 CD1 LEU A 159 13962 20956 11897 2639 1246 1063 C
ATOM 1036 CD2 LEU A 159 24.849 138.188 202.078 1.00122.09 C
ANISOU 1036 CD2 LEU A 159 14529 19697 12163 2852 1342 855 C
ATOM 1037 N LEU A 160 23.856 143.623 203.471 1.00110.24 N
ANISOU 1037 N LEU A 160 12721 18003 11161 1049 602 1084 N
ATOM 1038 CA LEU A 160 23.919 144.789 204.354 1.00109.91 C
ANISOU 1038 CA LEU A 160 12660 17926 11174 739 387 1128 C
ATOM 1039 C LEU A 160 22.629 144.934 205.194 1.00111.61 C
ANISOU 1039 C LEU A 160 13195 17572 11638 749 355 999 C
ATOM 1040 O LEU A 160 22.709 145.152 206.405 1.00111.71 O
ANISOU 1040 O LEU A 160 13233 17546 11664 771 277 989 O
ATOM 1041 CB LEU A 160 24.182 146.069 203.544 1.00110.69 C
ANISOU 1041 CB LEU A 160 12633 18182 11242 255 174 1236 C
ATOM 1042 CG LEU A 160 25.642 146.435 203.283 1.00118.22 C
ANISOU 1042 CG LEU A 160 13209 19796 11912 101 98 1416 C
ATOM 1043 CD1 LEU A 160 25.771 147.271 202.026 1.00119.23 C
ANISOU 1043 CD1 LEU A 160 13231 20077 11995 -316 -38 1525 C
ATOM 1044 CD2 LEU A 160 26.240 147.201 204.456 1.00121.50 C
ANISOU 1044 CD2 LEU A 160 13538 20369 12257 -66 -83 1489 C
ATOM 1045 N LEU A 161 21.451 144.813 204.546 1.00105.88 N
ANISOU 1045 N LEU A 161 12696 16446 11089 740 415 903 N
ATOM 1046 CA LEU A 161 20.119 144.912 205.164 1.00103.13 C
ANISOU 1046 CA LEU A 161 12628 15606 10952 757 402 784 C
ATOM 1047 C LEU A 161 19.857 143.746 206.125 1.00107.31 C
ANISOU 1047 C LEU A 161 13266 16020 11488 1132 573 729 C
ATOM 1048 O LEU A 161 19.164 143.916 207.128 1.00105.63 O
ANISOU 1048 O LEU A 161 13186 15576 11372 1160 530 671 O
ATOM 1049 CB LEU A 161 19.038 144.954 204.059 1.00101.15 C
ANISOU 1049 CB LEU A 161 12539 15050 10842 644 435 719 C
ATOM 1050 CG LEU A 161 17.569 145.093 204.471 1.00102.86 C
ANISOU 1050 CG LEU A 161 13016 14813 11255 632 418 604 C
ATOM 1051 CD1 LEU A 161 17.266 146.477 205.025 1.00102.45 C
ANISOU 1051 CD1 LEU A 161 13019 14638 11268 374 169 585 C
ATOM 1052 CD2 LEU A 161 16.669 144.814 203.307 1.00103.65 C
ANISOU 1052 CD2 LEU A 161 13237 14696 11450 588 503 553 C
ATOM 1053 N ALA A 162 20.405 142.570 205.805 1.00105.28 N
ANISOU 1053 N ALA A 162 12962 15933 11108 1428 752 748 N
ATOM 1054 CA ALA A 162 20.248 141.367 206.607 1.00105.23 C
ANISOU 1054 CA ALA A 162 13086 15818 11080 1788 902 714 C
ATOM 1055 C ALA A 162 21.171 141.360 207.833 1.00110.66 C
ANISOU 1055 C ALA A 162 13624 16782 11640 1927 870 769 C
ATOM 1056 O ALA A 162 20.895 140.637 208.796 1.00109.53 O
ANISOU 1056 O ALA A 162 13605 16505 11505 2170 951 744 O
ATOM 1057 CB ALA A 162 20.515 140.152 205.739 1.00106.89 C
ANISOU 1057 CB ALA A 162 13346 16084 11184 2070 1072 706 C
ATOM 1058 N PHE A 163 22.259 142.168 207.796 1.00109.59 N
ANISOU 1058 N PHE A 163 13218 17047 11373 1756 746 856 N
ATOM 1059 CA PHE A 163 23.286 142.238 208.841 1.00111.24 C
ANISOU 1059 CA PHE A 163 13239 17600 11428 1856 702 924 C
ATOM 1060 C PHE A 163 22.753 142.518 210.265 1.00114.41 C
ANISOU 1060 C PHE A 163 13766 17772 11931 1875 637 877 C
ATOM 1061 O PHE A 163 23.121 141.729 211.140 1.00115.31 O
ANISOU 1061 O PHE A 163 13868 17991 11955 2176 732 889 O
ATOM 1062 CB PHE A 163 24.426 143.211 208.489 1.00114.85 C
ANISOU 1062 CB PHE A 163 13390 18517 11729 1566 542 1041 C
ATOM 1063 CG PHE A 163 25.487 143.279 209.563 1.00118.39 C
ANISOU 1063 CG PHE A 163 13628 19358 11998 1664 499 1118 C
ATOM 1064 CD1 PHE A 163 26.434 142.271 209.692 1.00123.36 C
ANISOU 1064 CD1 PHE A 163 14078 20391 12402 2022 645 1169 C
ATOM 1065 CD2 PHE A 163 25.511 144.330 210.474 1.00120.71 C
ANISOU 1065 CD2 PHE A 163 13921 19608 12335 1429 305 1130 C
ATOM 1066 CE1 PHE A 163 27.397 142.319 210.704 1.00126.08 C
ANISOU 1066 CE1 PHE A 163 14216 21118 12569 2125 609 1241 C
ATOM 1067 CE2 PHE A 163 26.470 144.373 211.491 1.00125.23 C
ANISOU 1067 CE2 PHE A 163 14300 20544 12738 1515 264 1200 C
ATOM 1068 CZ PHE A 163 27.414 143.373 211.592 1.00125.04 C
ANISOU 1068 CZ PHE A 163 14071 20945 12493 1854 420 1260 C
ATOM 1069 N PRO A 164 21.965 143.594 210.563 1.00109.10 N
ANISOU 1069 N PRO A 164 13211 16826 11417 1596 472 825 N
ATOM 1070 CA PRO A 164 21.519 143.810 211.958 1.00108.31 C
ANISOU 1070 CA PRO A 164 13213 16565 11376 1665 414 775 C
ATOM 1071 C PRO A 164 20.792 142.623 212.598 1.00111.88 C
ANISOU 1071 C PRO A 164 13845 16780 11883 1989 599 723 C
ATOM 1072 O PRO A 164 21.062 142.324 213.768 1.00111.02 O
ANISOU 1072 O PRO A 164 13730 16723 11728 2160 611 727 O
ATOM 1073 CB PRO A 164 20.636 145.056 211.861 1.00108.69 C
ANISOU 1073 CB PRO A 164 13391 16340 11567 1353 212 708 C
ATOM 1074 CG PRO A 164 21.130 145.758 210.658 1.00113.77 C
ANISOU 1074 CG PRO A 164 13928 17123 12176 1057 107 769 C
ATOM 1075 CD PRO A 164 21.457 144.670 209.688 1.00109.57 C
ANISOU 1075 CD PRO A 164 13326 16721 11585 1236 320 806 C
ATOM 1076 N ALA A 165 19.924 141.910 211.817 1.00108.42 N
ANISOU 1076 N ALA A 165 13568 16100 11527 2061 737 687 N
ATOM 1077 CA ALA A 165 19.181 140.723 212.276 1.00107.99 C
ANISOU 1077 CA ALA A 165 13716 15804 11510 2316 900 661 C
ATOM 1078 C ALA A 165 20.107 139.557 212.641 1.00114.55 C
ANISOU 1078 C ALA A 165 14513 16834 12175 2665 1033 720 C
ATOM 1079 O ALA A 165 19.773 138.767 213.521 1.00114.21 O
ANISOU 1079 O ALA A 165 14633 16627 12133 2876 1127 722 O
ATOM 1080 CB ALA A 165 18.163 140.283 211.239 1.00107.54 C
ANISOU 1080 CB ALA A 165 13837 15462 11560 2252 980 619 C
ATOM 1081 N GLY A 166 21.255 139.473 211.966 1.00113.18 N
ANISOU 1081 N GLY A 166 14133 17027 11844 2724 1033 775 N
ATOM 1082 CA GLY A 166 22.283 138.473 212.223 1.00114.95 C
ANISOU 1082 CA GLY A 166 14290 17518 11869 3085 1140 826 C
ATOM 1083 C GLY A 166 23.128 138.851 213.425 1.00120.05 C
ANISOU 1083 C GLY A 166 14738 18473 12404 3138 1068 878 C
ATOM 1084 O GLY A 166 23.420 138.004 214.276 1.00120.97 O
ANISOU 1084 O GLY A 166 14905 18629 12429 3443 1147 899 O
ATOM 1085 N TYR A 167 23.496 140.147 213.513 1.00116.00 N
ANISOU 1085 N TYR A 167 14022 18158 11896 2822 900 901 N
ATOM 1086 CA TYR A 167 24.310 140.752 214.568 1.00116.75 C
ANISOU 1086 CA TYR A 167 13920 18553 11887 2782 786 951 C
ATOM 1087 C TYR A 167 23.768 140.525 215.982 1.00119.24 C
ANISOU 1087 C TYR A 167 14381 18650 12273 2915 792 911 C
ATOM 1088 O TYR A 167 24.532 140.112 216.851 1.00119.82 O
ANISOU 1088 O TYR A 167 14349 18967 12210 3126 815 956 O
ATOM 1089 CB TYR A 167 24.487 142.261 214.287 1.00118.19 C
ANISOU 1089 CB TYR A 167 13965 18841 12101 2341 563 971 C
ATOM 1090 CG TYR A 167 25.487 142.978 215.175 1.00121.72 C
ANISOU 1090 CG TYR A 167 14200 19634 12414 2228 407 1036 C
ATOM 1091 CD1 TYR A 167 26.850 142.698 215.095 1.00126.01 C
ANISOU 1091 CD1 TYR A 167 14453 20711 12713 2337 433 1144 C
ATOM 1092 CD2 TYR A 167 25.083 144.000 216.028 1.00121.95 C
ANISOU 1092 CD2 TYR A 167 14313 19483 12539 1995 211 990 C
ATOM 1093 CE1 TYR A 167 27.778 143.376 215.886 1.00128.48 C
ANISOU 1093 CE1 TYR A 167 14560 21368 12889 2195 278 1215 C
ATOM 1094 CE2 TYR A 167 26.001 144.684 216.827 1.00124.61 C
ANISOU 1094 CE2 TYR A 167 14482 20120 12746 1866 44 1047 C
ATOM 1095 CZ TYR A 167 27.350 144.370 216.751 1.00134.29 C
ANISOU 1095 CZ TYR A 167 15411 21876 13736 1945 78 1167 C
ATOM 1096 OH TYR A 167 28.267 145.035 217.537 1.00136.33 O
ANISOU 1096 OH TYR A 167 15493 22454 13852 1791 -95 1234 O
ATOM 1097 N TYR A 168 22.455 140.763 216.199 1.00113.88 N
ANISOU 1097 N TYR A 168 13931 17549 11789 2808 777 832 N
ATOM 1098 CA TYR A 168 21.789 140.672 217.506 1.00112.79 C
ANISOU 1098 CA TYR A 168 13921 17219 11715 2899 771 794 C
ATOM 1099 C TYR A 168 21.249 139.281 217.909 1.00116.23 C
ANISOU 1099 C TYR A 168 14561 17442 12159 3194 955 803 C
ATOM 1100 O TYR A 168 20.794 139.114 219.046 1.00115.57 O
ANISOU 1100 O TYR A 168 14563 17245 12104 3272 958 793 O
ATOM 1101 CB TYR A 168 20.680 141.722 217.592 1.00112.43 C
ANISOU 1101 CB TYR A 168 13978 16909 11830 2626 627 708 C
ATOM 1102 CG TYR A 168 21.235 143.127 217.564 1.00115.40 C
ANISOU 1102 CG TYR A 168 14214 17455 12179 2348 399 702 C
ATOM 1103 CD1 TYR A 168 22.154 143.553 218.518 1.00119.33 C
ANISOU 1103 CD1 TYR A 168 14558 18233 12549 2370 297 740 C
ATOM 1104 CD2 TYR A 168 20.859 144.026 216.573 1.00115.62 C
ANISOU 1104 CD2 TYR A 168 14281 17352 12296 2047 268 666 C
ATOM 1105 CE1 TYR A 168 22.694 144.836 218.482 1.00121.53 C
ANISOU 1105 CE1 TYR A 168 14737 18653 12785 2075 59 748 C
ATOM 1106 CE2 TYR A 168 21.372 145.321 216.542 1.00117.57 C
ANISOU 1106 CE2 TYR A 168 14446 17721 12505 1761 26 674 C
ATOM 1107 CZ TYR A 168 22.294 145.721 217.497 1.00127.05 C
ANISOU 1107 CZ TYR A 168 15507 19195 13573 1763 -84 719 C
ATOM 1108 OH TYR A 168 22.807 146.995 217.489 1.00129.50 O
ANISOU 1108 OH TYR A 168 15767 19608 13830 1446 -350 738 O
ATOM 1109 N SER A 169 21.339 138.285 217.015 1.00112.82 N
ANISOU 1109 N SER A 169 14215 16972 11679 3362 1090 830 N
ATOM 1110 CA SER A 169 20.910 136.922 217.312 1.00112.62 C
ANISOU 1110 CA SER A 169 14430 16727 11635 3628 1234 854 C
ATOM 1111 C SER A 169 21.891 136.297 218.294 1.00117.46 C
ANISOU 1111 C SER A 169 14972 17585 12073 3944 1275 917 C
ATOM 1112 O SER A 169 23.094 136.447 218.100 1.00118.71 O
ANISOU 1112 O SER A 169 14906 18115 12084 4035 1253 947 O
ATOM 1113 CB SER A 169 20.877 136.092 216.034 1.00116.53 C
ANISOU 1113 CB SER A 169 15070 17096 12109 3721 1332 850 C
ATOM 1114 OG SER A 169 19.902 136.587 215.136 1.00124.40 O
ANISOU 1114 OG SER A 169 16154 17844 13268 3442 1305 795 O
ATOM 1115 N THR A 170 21.392 135.631 219.354 1.00113.78 N
ANISOU 1115 N THR A 170 14678 16946 11608 4098 1329 946 N
ATOM 1116 CA THR A 170 22.235 134.957 220.360 1.00115.54 C
ANISOU 1116 CA THR A 170 14868 17367 11665 4416 1370 1010 C
ATOM 1117 C THR A 170 21.522 133.754 221.017 1.00119.38 C
ANISOU 1117 C THR A 170 15653 17555 12151 4588 1453 1062 C
ATOM 1118 O THR A 170 20.297 133.662 220.978 1.00118.04 O
ANISOU 1118 O THR A 170 15645 17090 12114 4401 1454 1054 O
ATOM 1119 CB THR A 170 22.811 135.952 221.402 1.00123.63 C
ANISOU 1119 CB THR A 170 15620 18710 12644 4348 1262 1012 C
ATOM 1120 OG1 THR A 170 23.888 135.327 222.102 1.00126.31 O
ANISOU 1120 OG1 THR A 170 15898 19296 12798 4677 1310 1077 O
ATOM 1121 CG2 THR A 170 21.779 136.447 222.389 1.00118.29 C
ANISOU 1121 CG2 THR A 170 14983 17861 12100 4150 1188 974 C
ATOM 1122 N THR A 171 22.292 132.838 221.614 1.00117.03 N
ANISOU 1122 N THR A 171 15425 17359 11682 4941 1513 1125 N
ATOM 1123 CA THR A 171 21.727 131.663 222.265 1.00117.40 C
ANISOU 1123 CA THR A 171 15779 17132 11695 5112 1572 1197 C
ATOM 1124 C THR A 171 21.802 131.790 223.771 1.00121.32 C
ANISOU 1124 C THR A 171 16181 17757 12158 5155 1547 1247 C
ATOM 1125 O THR A 171 22.895 131.956 224.319 1.00122.43 O
ANISOU 1125 O THR A 171 16064 18254 12199 5268 1513 1244 O
ATOM 1126 CB THR A 171 22.386 130.364 221.786 1.00126.63 C
ANISOU 1126 CB THR A 171 17164 18262 12686 5498 1636 1232 C
ATOM 1127 OG1 THR A 171 23.795 130.463 221.967 1.00129.53 O
ANISOU 1127 OG1 THR A 171 17278 19066 12871 5771 1633 1238 O
ATOM 1128 CG2 THR A 171 22.052 130.021 220.345 1.00123.33 C
ANISOU 1128 CG2 THR A 171 16913 17650 12297 5470 1660 1179 C
ATOM 1129 N GLU A 172 20.642 131.705 224.441 1.00116.18 N
ANISOU 1129 N GLU A 172 15724 16846 11575 5051 1560 1299 N
ATOM 1130 CA GLU A 172 20.527 131.767 225.897 1.00115.37 C
ANISOU 1130 CA GLU A 172 15554 16852 11431 5095 1543 1354 C
ATOM 1131 C GLU A 172 20.516 130.357 226.461 1.00119.73 C
ANISOU 1131 C GLU A 172 16390 17248 11853 5354 1601 1476 C
ATOM 1132 O GLU A 172 19.656 129.552 226.094 1.00119.86 O
ANISOU 1132 O GLU A 172 16726 16923 11894 5297 1631 1536 O
ATOM 1133 CB GLU A 172 19.266 132.535 226.327 1.00114.87 C
ANISOU 1133 CB GLU A 172 15443 16697 11504 4786 1499 1328 C
ATOM 1134 CG GLU A 172 19.331 134.032 226.067 1.00123.28 C
ANISOU 1134 CG GLU A 172 16236 17935 12669 4569 1403 1204 C
ATOM 1135 CD GLU A 172 20.300 134.852 226.900 1.00142.43 C
ANISOU 1135 CD GLU A 172 18385 20711 15022 4642 1320 1166 C
ATOM 1136 OE1 GLU A 172 20.434 136.063 226.612 1.00131.88 O
ANISOU 1136 OE1 GLU A 172 16872 19483 13753 4447 1213 1071 O
ATOM 1137 OE2 GLU A 172 20.917 134.300 227.839 1.00142.01 O
ANISOU 1137 OE2 GLU A 172 18305 20817 14836 4883 1348 1233 O
ATOM 1138 N THR A 173 21.486 130.047 227.328 1.00116.50 N
ANISOU 1138 N THR A 173 15882 17087 11294 5637 1605 1518 N
ATOM 1139 CA THR A 173 21.605 128.718 227.920 1.00118.17 C
ANISOU 1139 CA THR A 173 16373 17168 11358 5924 1643 1636 C
ATOM 1140 C THR A 173 20.765 128.627 229.197 1.00121.44 C
ANISOU 1140 C THR A 173 16835 17522 11786 5807 1636 1732 C
ATOM 1141 O THR A 173 20.894 129.467 230.090 1.00120.33 O
ANISOU 1141 O THR A 173 16417 17651 11652 5758 1605 1707 O
ATOM 1142 CB THR A 173 23.083 128.335 228.083 1.00127.59 C
ANISOU 1142 CB THR A 173 17454 18668 12356 6327 1655 1634 C
ATOM 1143 OG1 THR A 173 23.749 128.482 226.820 1.00124.73 O
ANISOU 1143 OG1 THR A 173 16982 18427 11981 6372 1659 1542 O
ATOM 1144 CG2 THR A 173 23.272 126.916 228.604 1.00128.89 C
ANISOU 1144 CG2 THR A 173 17971 18654 12346 6683 1682 1744 C
ATOM 1145 N MET A 174 19.893 127.608 229.262 1.00118.43 N
ANISOU 1145 N MET A 174 16811 16789 11397 5742 1652 1845 N
ATOM 1146 CA MET A 174 18.985 127.365 230.384 1.00118.20 C
ANISOU 1146 CA MET A 174 16863 16692 11355 5600 1647 1970 C
ATOM 1147 C MET A 174 19.113 125.930 230.915 1.00124.38 C
ANISOU 1147 C MET A 174 18029 17252 11978 5815 1651 2136 C
ATOM 1148 O MET A 174 19.778 125.126 230.260 1.00125.83 O
ANISOU 1148 O MET A 174 18466 17265 12080 6059 1650 2132 O
ATOM 1149 CB MET A 174 17.554 127.666 229.954 1.00119.13 C
ANISOU 1149 CB MET A 174 17026 16622 11615 5202 1639 1971 C
ATOM 1150 CG MET A 174 17.231 129.124 230.025 1.00120.73 C
ANISOU 1150 CG MET A 174 16855 17078 11939 5005 1612 1839 C
ATOM 1151 SD MET A 174 15.922 129.524 228.873 1.00123.54 S
ANISOU 1151 SD MET A 174 17262 17217 12461 4620 1604 1783 S
ATOM 1152 CE MET A 174 14.486 128.803 229.750 1.00121.19 C
ANISOU 1152 CE MET A 174 17110 16834 12101 4402 1612 1968 C
ATOM 1153 N PRO A 175 18.501 125.574 232.079 1.00120.74 N
ANISOU 1153 N PRO A 175 17628 16797 11449 5751 1643 2283 N
ATOM 1154 CA PRO A 175 18.671 124.210 232.618 1.00122.72 C
ANISOU 1154 CA PRO A 175 18273 16823 11532 5951 1625 2457 C
ATOM 1155 C PRO A 175 18.181 123.057 231.731 1.00125.49 C
ANISOU 1155 C PRO A 175 19126 16692 11862 5881 1588 2536 C
ATOM 1156 O PRO A 175 18.893 122.067 231.573 1.00126.79 O
ANISOU 1156 O PRO A 175 19609 16670 11896 6207 1560 2559 O
ATOM 1157 CB PRO A 175 17.909 124.264 233.950 1.00124.96 C
ANISOU 1157 CB PRO A 175 18478 17231 11772 5780 1620 2603 C
ATOM 1158 CG PRO A 175 16.952 125.392 233.800 1.00127.02 C
ANISOU 1158 CG PRO A 175 18413 17664 12183 5437 1631 2515 C
ATOM 1159 CD PRO A 175 17.697 126.401 233.002 1.00120.83 C
ANISOU 1159 CD PRO A 175 17356 17046 11507 5524 1640 2299 C
ATOM 1160 N SER A 176 16.978 123.184 231.160 1.00120.02 N
ANISOU 1160 N SER A 176 18511 15809 11281 5472 1576 2571 N
ATOM 1161 CA SER A 176 16.382 122.148 230.321 1.00120.89 C
ANISOU 1161 CA SER A 176 19102 15455 11376 5325 1523 2656 C
ATOM 1162 C SER A 176 16.767 122.209 228.824 1.00122.35 C
ANISOU 1162 C SER A 176 19379 15474 11636 5408 1526 2491 C
ATOM 1163 O SER A 176 16.731 121.172 228.160 1.00124.09 O
ANISOU 1163 O SER A 176 20066 15300 11782 5475 1466 2537 O
ATOM 1164 CB SER A 176 14.863 122.165 230.473 1.00124.05 C
ANISOU 1164 CB SER A 176 19524 15773 11837 4829 1506 2784 C
ATOM 1165 N ARG A 177 17.116 123.406 228.291 1.00114.68 N
ANISOU 1165 N ARG A 177 17989 14790 10796 5397 1580 2304 N
ATOM 1166 CA ARG A 177 17.392 123.593 226.863 1.00113.20 C
ANISOU 1166 CA ARG A 177 17833 14493 10685 5420 1587 2155 C
ATOM 1167 C ARG A 177 18.231 124.833 226.491 1.00114.71 C
ANISOU 1167 C ARG A 177 17556 15070 10957 5519 1633 1970 C
ATOM 1168 O ARG A 177 18.505 125.683 227.340 1.00112.53 O
ANISOU 1168 O ARG A 177 16917 15142 10698 5528 1649 1944 O
ATOM 1169 CB ARG A 177 16.048 123.632 226.097 1.00112.30 C
ANISOU 1169 CB ARG A 177 17847 14122 10700 4973 1569 2181 C
ATOM 1170 CG ARG A 177 15.217 124.895 226.337 1.00115.03 C
ANISOU 1170 CG ARG A 177 17767 14737 11202 4637 1602 2125 C
ATOM 1171 CD ARG A 177 13.748 124.659 226.068 1.00120.48 C
ANISOU 1171 CD ARG A 177 18609 15217 11950 4210 1579 2222 C
ATOM 1172 NE ARG A 177 13.083 125.867 225.579 1.00128.22 N
ANISOU 1172 NE ARG A 177 19233 16400 13085 3947 1603 2108 N
ATOM 1173 CZ ARG A 177 12.601 126.833 226.356 1.00141.54 C
ANISOU 1173 CZ ARG A 177 20580 18399 14799 3832 1613 2103 C
ATOM 1174 NH1 ARG A 177 12.717 126.755 227.677 1.00131.39 N
ANISOU 1174 NH1 ARG A 177 19236 17284 13404 3941 1614 2208 N
ATOM 1175 NH2 ARG A 177 12.005 127.888 225.818 1.00124.33 N
ANISOU 1175 NH2 ARG A 177 18132 16365 12744 3628 1615 1987 N
ATOM 1176 N VAL A 178 18.597 124.928 225.187 1.00111.73 N
ANISOU 1176 N VAL A 178 17207 14624 10621 5563 1639 1848 N
ATOM 1177 CA VAL A 178 19.328 126.035 224.564 1.00110.41 C
ANISOU 1177 CA VAL A 178 16639 14785 10525 5586 1665 1692 C
ATOM 1178 C VAL A 178 18.342 126.758 223.635 1.00114.98 C
ANISOU 1178 C VAL A 178 17129 15260 11298 5185 1662 1620 C
ATOM 1179 O VAL A 178 17.649 126.102 222.850 1.00115.12 O
ANISOU 1179 O VAL A 178 17456 14936 11349 5046 1651 1641 O
ATOM 1180 CB VAL A 178 20.578 125.537 223.809 1.00115.60 C
ANISOU 1180 CB VAL A 178 17345 15538 11038 5989 1675 1618 C
ATOM 1181 N VAL A 179 18.226 128.098 223.774 1.00111.25 N
ANISOU 1181 N VAL A 179 16255 15073 10941 4997 1658 1537 N
ATOM 1182 CA VAL A 179 17.257 128.923 223.027 1.00109.17 C
ANISOU 1182 CA VAL A 179 15871 14754 10854 4631 1643 1462 C
ATOM 1183 C VAL A 179 17.949 129.974 222.148 1.00114.34 C
ANISOU 1183 C VAL A 179 16252 15627 11566 4625 1630 1326 C
ATOM 1184 O VAL A 179 18.792 130.712 222.642 1.00113.98 O
ANISOU 1184 O VAL A 179 15941 15905 11463 4769 1613 1290 O
ATOM 1185 CB VAL A 179 16.207 129.570 223.984 1.00111.02 C
ANISOU 1185 CB VAL A 179 15925 15097 11160 4391 1620 1490 C
ATOM 1186 CG1 VAL A 179 15.179 130.396 223.221 1.00108.74 C
ANISOU 1186 CG1 VAL A 179 15506 14781 11030 4060 1593 1403 C
ATOM 1187 CG2 VAL A 179 15.503 128.520 224.832 1.00112.19 C
ANISOU 1187 CG2 VAL A 179 16329 15064 11234 4348 1631 1651 C
ATOM 1188 N CYS A 180 17.553 130.063 220.865 1.00112.14 N
ANISOU 1188 N CYS A 180 16034 15184 11389 4434 1629 1263 N
ATOM 1189 CA CYS A 180 18.063 131.042 219.903 1.00112.17 C
ANISOU 1189 CA CYS A 180 15792 15375 11451 4363 1607 1151 C
ATOM 1190 C CYS A 180 17.043 132.202 219.736 1.00115.78 C
ANISOU 1190 C CYS A 180 16083 15829 12081 3998 1556 1091 C
ATOM 1191 O CYS A 180 15.956 132.000 219.183 1.00114.89 O
ANISOU 1191 O CYS A 180 16131 15464 12057 3785 1565 1098 O
ATOM 1192 CB CYS A 180 18.385 130.358 218.574 1.00113.64 C
ANISOU 1192 CB CYS A 180 16174 15402 11602 4460 1639 1118 C
ATOM 1193 SG CYS A 180 18.804 131.480 217.212 1.00116.43 S
ANISOU 1193 SG CYS A 180 16241 15978 12020 4325 1614 1003 S
ATOM 1194 N MET A 181 17.395 133.406 220.248 1.00112.30 N
ANISOU 1194 N MET A 181 15335 15668 11666 3934 1488 1035 N
ATOM 1195 CA MET A 181 16.567 134.612 220.165 1.00110.66 C
ANISOU 1195 CA MET A 181 14986 15466 11593 3643 1410 961 C
ATOM 1196 C MET A 181 17.395 135.869 219.854 1.00113.70 C
ANISOU 1196 C MET A 181 15103 16104 11995 3565 1312 881 C
ATOM 1197 O MET A 181 18.578 135.934 220.185 1.00113.35 O
ANISOU 1197 O MET A 181 14906 16318 11844 3722 1292 898 O
ATOM 1198 CB MET A 181 15.660 134.791 221.400 1.00113.04 C
ANISOU 1198 CB MET A 181 15280 15764 11905 3583 1387 989 C
ATOM 1199 CG MET A 181 16.371 135.125 222.693 1.00118.12 C
ANISOU 1199 CG MET A 181 15772 16657 12451 3758 1353 1010 C
ATOM 1200 SD MET A 181 15.189 135.082 224.064 1.00122.97 S
ANISOU 1200 SD MET A 181 16379 17284 13059 3692 1332 1040 S
ATOM 1201 CE MET A 181 15.985 136.184 225.232 1.00120.49 C
ANISOU 1201 CE MET A 181 15832 17296 12653 3861 1250 1009 C
ATOM 1202 N ILE A 182 16.776 136.843 219.173 1.00110.42 N
ANISOU 1202 N ILE A 182 14641 15614 11701 3306 1241 804 N
ATOM 1203 CA ILE A 182 17.450 138.079 218.765 1.00110.51 C
ANISOU 1203 CA ILE A 182 14445 15808 11736 3158 1117 739 C
ATOM 1204 C ILE A 182 17.096 139.221 219.747 1.00115.77 C
ANISOU 1204 C ILE A 182 15007 16553 12427 3062 979 683 C
ATOM 1205 O ILE A 182 15.923 139.586 219.923 1.00114.42 O
ANISOU 1205 O ILE A 182 14912 16231 12333 2959 948 637 O
ATOM 1206 CB ILE A 182 17.260 138.428 217.241 1.00112.34 C
ANISOU 1206 CB ILE A 182 14704 15919 12062 2952 1102 693 C
ATOM 1207 CG1 ILE A 182 17.355 139.953 216.972 1.00111.84 C
ANISOU 1207 CG1 ILE A 182 14491 15944 12059 2703 929 622 C
ATOM 1208 CG2 ILE A 182 15.979 137.815 216.641 1.00111.82 C
ANISOU 1208 CG2 ILE A 182 14856 15541 12091 2869 1181 686 C
ATOM 1209 CD1 ILE A 182 17.662 140.331 215.583 1.00120.89 C
ANISOU 1209 CD1 ILE A 182 15544 17194 13195 2586 899 626 C
ATOM 1210 N GLU A 183 18.145 139.761 220.392 1.00114.10 N
ANISOU 1210 N GLU A 183 14623 16602 12126 3117 891 688 N
ATOM 1211 CA GLU A 183 18.023 140.820 221.389 1.00114.27 C
ANISOU 1211 CA GLU A 183 14566 16708 12142 3058 736 628 C
ATOM 1212 C GLU A 183 18.845 142.080 221.063 1.00119.02 C
ANISOU 1212 C GLU A 183 15021 17477 12723 2870 546 590 C
ATOM 1213 O GLU A 183 20.082 142.071 221.102 1.00119.10 O
ANISOU 1213 O GLU A 183 14880 17748 12626 2909 530 649 O
ATOM 1214 CB GLU A 183 18.334 140.284 222.802 1.00116.62 C
ANISOU 1214 CB GLU A 183 14838 17137 12336 3293 784 677 C
ATOM 1215 CG GLU A 183 19.501 139.316 222.898 1.00125.55 C
ANISOU 1215 CG GLU A 183 15893 18473 13338 3510 879 771 C
ATOM 1216 CD GLU A 183 19.351 138.310 224.021 1.00139.35 C
ANISOU 1216 CD GLU A 183 17730 20206 15012 3762 998 844 C
ATOM 1217 OE1 GLU A 183 19.829 138.591 225.144 1.00139.03 O
ANISOU 1217 OE1 GLU A 183 17592 20342 14890 3866 948 851 O
ATOM 1218 OE2 GLU A 183 18.775 137.227 223.772 1.00123.65 O
ANISOU 1218 OE2 GLU A 183 15923 18022 13038 3844 1130 900 O
ATOM 1219 N TRP A 184 18.119 143.167 220.752 1.00115.98 N
ANISOU 1219 N TRP A 184 14693 16948 12426 2659 388 497 N
ATOM 1220 CA TRP A 184 18.653 144.487 220.410 1.00117.24 C
ANISOU 1220 CA TRP A 184 14791 17176 12580 2419 159 455 C
ATOM 1221 C TRP A 184 18.992 145.266 221.695 1.00126.87 C
ANISOU 1221 C TRP A 184 15967 18523 13714 2450 -17 413 C
ATOM 1222 O TRP A 184 18.427 144.931 222.737 1.00126.00 O
ANISOU 1222 O TRP A 184 15898 18393 13583 2648 37 385 O
ATOM 1223 CB TRP A 184 17.609 145.261 219.580 1.00114.36 C
ANISOU 1223 CB TRP A 184 14565 16549 12338 2221 58 364 C
ATOM 1224 CG TRP A 184 17.522 144.855 218.135 1.00114.15 C
ANISOU 1224 CG TRP A 184 14555 16433 12382 2111 167 403 C
ATOM 1225 CD1 TRP A 184 17.177 143.630 217.644 1.00116.35 C
ANISOU 1225 CD1 TRP A 184 14876 16642 12688 2243 393 452 C
ATOM 1226 CD2 TRP A 184 17.717 145.703 216.994 1.00113.75 C
ANISOU 1226 CD2 TRP A 184 14499 16346 12373 1841 39 396 C
ATOM 1227 NE1 TRP A 184 17.194 143.650 216.272 1.00115.09 N
ANISOU 1227 NE1 TRP A 184 14727 16418 12583 2093 420 465 N
ATOM 1228 CE2 TRP A 184 17.501 144.913 215.845 1.00116.62 C
ANISOU 1228 CE2 TRP A 184 14880 16642 12790 1842 213 436 C
ATOM 1229 CE3 TRP A 184 18.066 147.053 216.829 1.00115.50 C
ANISOU 1229 CE3 TRP A 184 14726 16577 12583 1586 -223 367 C
ATOM 1230 CZ2 TRP A 184 17.631 145.424 214.552 1.00115.65 C
ANISOU 1230 CZ2 TRP A 184 14743 16493 12706 1611 152 448 C
ATOM 1231 CZ3 TRP A 184 18.170 147.563 215.546 1.00116.69 C
ANISOU 1231 CZ3 TRP A 184 14880 16681 12774 1335 -292 390 C
ATOM 1232 CH2 TRP A 184 17.953 146.753 214.426 1.00116.42 C
ANISOU 1232 CH2 TRP A 184 14829 16613 12794 1354 -97 430 C
ATOM 1233 N PRO A 185 19.871 146.310 221.663 1.00128.83 N
ANISOU 1233 N PRO A 185 16143 18905 13900 2243 -238 414 N
ATOM 1234 CA PRO A 185 20.188 147.050 222.904 1.00131.44 C
ANISOU 1234 CA PRO A 185 16464 19339 14140 2267 -426 367 C
ATOM 1235 C PRO A 185 18.974 147.643 223.615 1.00139.96 C
ANISOU 1235 C PRO A 185 17723 20196 15261 2353 -537 224 C
ATOM 1236 O PRO A 185 17.998 148.006 222.957 1.00138.76 O
ANISOU 1236 O PRO A 185 17711 19806 15205 2280 -573 148 O
ATOM 1237 CB PRO A 185 21.158 148.142 222.433 1.00134.36 C
ANISOU 1237 CB PRO A 185 16779 19824 14449 1944 -675 399 C
ATOM 1238 CG PRO A 185 20.960 148.240 220.957 1.00137.41 C
ANISOU 1238 CG PRO A 185 17201 20084 14926 1736 -656 423 C
ATOM 1239 CD PRO A 185 20.641 146.850 220.524 1.00131.39 C
ANISOU 1239 CD PRO A 185 16395 19313 14216 1959 -341 470 C
ATOM 1240 N GLU A 186 19.030 147.715 224.960 1.00141.48 N
ANISOU 1240 N GLU A 186 17897 20496 15363 2533 -583 188 N
ATOM 1241 CA GLU A 186 17.939 148.220 225.793 1.00143.32 C
ANISOU 1241 CA GLU A 186 18269 20598 15588 2678 -683 50 C
ATOM 1242 C GLU A 186 17.726 149.738 225.650 1.00153.77 C
ANISOU 1242 C GLU A 186 19768 21754 16904 2500 -1018 -83 C
ATOM 1243 O GLU A 186 18.378 150.541 226.327 1.00155.21 O
ANISOU 1243 O GLU A 186 19976 22008 16988 2437 -1250 -120 O
ATOM 1244 CB GLU A 186 18.124 147.796 227.259 1.00145.45 C
ANISOU 1244 CB GLU A 186 18455 21063 15745 2932 -629 60 C
ATOM 1245 N HIS A 187 16.813 150.116 224.740 1.00153.74 N
ANISOU 1245 N HIS A 187 19905 21515 16995 2416 -1056 -152 N
ATOM 1246 CA HIS A 187 16.438 151.506 224.474 1.00156.54 C
ANISOU 1246 CA HIS A 187 20480 21653 17344 2273 -1376 -285 C
ATOM 1247 C HIS A 187 15.159 151.880 225.251 1.00163.02 C
ANISOU 1247 C HIS A 187 21446 22376 18117 2545 -1454 -456 C
ATOM 1248 O HIS A 187 14.430 150.962 225.640 1.00162.55 O
ANISOU 1248 O HIS A 187 21287 22421 18055 2781 -1217 -439 O
ATOM 1249 CB HIS A 187 16.285 151.757 222.964 1.00157.29 C
ANISOU 1249 CB HIS A 187 20637 21575 17551 2015 -1391 -252 C
ATOM 1250 CG HIS A 187 17.514 152.355 222.355 1.00162.55 C
ANISOU 1250 CG HIS A 187 21268 22302 18191 1678 -1557 -154 C
ATOM 1251 ND1 HIS A 187 17.840 153.690 222.547 1.00166.37 N
ANISOU 1251 ND1 HIS A 187 21946 22658 18610 1470 -1929 -220 N
ATOM 1252 CD2 HIS A 187 18.482 151.773 221.608 1.00164.76 C
ANISOU 1252 CD2 HIS A 187 21339 22790 18472 1530 -1409 9 C
ATOM 1253 CE1 HIS A 187 18.984 153.876 221.908 1.00166.94 C
ANISOU 1253 CE1 HIS A 187 21902 22878 18649 1158 -1992 -76 C
ATOM 1254 NE2 HIS A 187 19.409 152.752 221.326 1.00166.30 N
ANISOU 1254 NE2 HIS A 187 21560 23028 18600 1200 -1679 61 N
ATOM 1255 N PRO A 188 14.861 153.190 225.504 1.00161.48 N
ANISOU 1255 N PRO A 188 21492 22004 17860 2532 -1789 -615 N
ATOM 1256 CA PRO A 188 13.653 153.544 226.293 1.00161.55 C
ANISOU 1256 CA PRO A 188 21620 21981 17781 2857 -1862 -789 C
ATOM 1257 C PRO A 188 12.309 152.974 225.804 1.00161.89 C
ANISOU 1257 C PRO A 188 21632 21998 17879 3006 -1656 -814 C
ATOM 1258 O PRO A 188 11.398 152.796 226.623 1.00162.07 O
ANISOU 1258 O PRO A 188 21660 22116 17803 3305 -1638 -917 O
ATOM 1259 CB PRO A 188 13.644 155.082 226.276 1.00165.43 C
ANISOU 1259 CB PRO A 188 22423 22238 18194 2784 -2289 -949 C
ATOM 1260 CG PRO A 188 14.593 155.477 225.175 1.00170.10 C
ANISOU 1260 CG PRO A 188 23069 22685 18878 2372 -2399 -845 C
ATOM 1261 CD PRO A 188 15.631 154.403 225.153 1.00164.74 C
ANISOU 1261 CD PRO A 188 22093 22252 18250 2235 -2135 -641 C
ATOM 1262 N ASN A 189 12.188 152.689 224.488 1.00154.36 N
ANISOU 1262 N ASN A 189 20635 20950 17066 2797 -1506 -716 N
ATOM 1263 CA ASN A 189 10.981 152.127 223.879 1.00151.44 C
ANISOU 1263 CA ASN A 189 20234 20551 16757 2870 -1314 -718 C
ATOM 1264 C ASN A 189 11.334 151.070 222.819 1.00150.65 C
ANISOU 1264 C ASN A 189 20003 20436 16801 2656 -1054 -549 C
ATOM 1265 O ASN A 189 10.429 150.424 222.272 1.00148.94 O
ANISOU 1265 O ASN A 189 19756 20194 16642 2673 -880 -527 O
ATOM 1266 CB ASN A 189 10.108 153.243 223.291 1.00151.71 C
ANISOU 1266 CB ASN A 189 20494 20380 16767 2898 -1555 -884 C
ATOM 1267 N LYS A 190 12.660 150.868 222.570 1.00144.75 N
ANISOU 1267 N LYS A 190 19174 19734 16090 2467 -1034 -431 N
ATOM 1268 CA LYS A 190 13.229 149.933 221.583 1.00142.07 C
ANISOU 1268 CA LYS A 190 18715 19412 15853 2294 -817 -278 C
ATOM 1269 C LYS A 190 12.586 150.133 220.189 1.00141.04 C
ANISOU 1269 C LYS A 190 18673 19086 15828 2124 -818 -296 C
ATOM 1270 O LYS A 190 12.059 149.195 219.585 1.00139.17 O
ANISOU 1270 O LYS A 190 18381 18834 15662 2132 -587 -235 O
ATOM 1271 CB LYS A 190 13.164 148.474 222.078 1.00143.92 C
ANISOU 1271 CB LYS A 190 18798 19802 16083 2464 -506 -167 C
ATOM 1272 N ILE A 191 12.596 151.394 219.720 1.00135.36 N
ANISOU 1272 N ILE A 191 18116 18205 15108 1969 -1102 -382 N
ATOM 1273 CA ILE A 191 12.015 151.816 218.453 1.00133.31 C
ANISOU 1273 CA ILE A 191 17972 17747 14931 1801 -1169 -414 C
ATOM 1274 C ILE A 191 12.790 151.316 217.241 1.00135.03 C
ANISOU 1274 C ILE A 191 18080 17987 15237 1548 -1034 -268 C
ATOM 1275 O ILE A 191 12.171 151.031 216.218 1.00134.44 O
ANISOU 1275 O ILE A 191 18017 17816 15249 1482 -919 -256 O
ATOM 1276 CB ILE A 191 11.835 153.346 218.424 1.00137.57 C
ANISOU 1276 CB ILE A 191 18764 18093 15414 1730 -1554 -549 C
ATOM 1277 N TYR A 192 14.131 151.205 217.351 1.00129.94 N
ANISOU 1277 N TYR A 192 17317 17502 14553 1423 -1048 -160 N
ATOM 1278 CA TYR A 192 15.027 150.757 216.273 1.00128.44 C
ANISOU 1278 CA TYR A 192 16991 17412 14398 1213 -937 -20 C
ATOM 1279 C TYR A 192 14.709 149.351 215.748 1.00124.78 C
ANISOU 1279 C TYR A 192 16417 16992 14000 1333 -602 48 C
ATOM 1280 O TYR A 192 14.667 149.170 214.533 1.00124.06 O
ANISOU 1280 O TYR A 192 16312 16855 13972 1183 -536 95 O
ATOM 1281 CB TYR A 192 16.508 150.873 216.681 1.00132.50 C
ANISOU 1281 CB TYR A 192 17363 18171 14810 1109 -1011 83 C
ATOM 1282 CG TYR A 192 16.903 152.260 217.142 1.00138.41 C
ANISOU 1282 CG TYR A 192 18247 18859 15482 924 -1373 36 C
ATOM 1283 CD1 TYR A 192 17.403 153.201 216.245 1.00141.64 C
ANISOU 1283 CD1 TYR A 192 18736 19192 15887 576 -1600 81 C
ATOM 1284 CD2 TYR A 192 16.782 152.633 218.479 1.00141.13 C
ANISOU 1284 CD2 TYR A 192 18664 19214 15746 1085 -1508 -49 C
ATOM 1285 CE1 TYR A 192 17.751 154.486 216.663 1.00145.35 C
ANISOU 1285 CE1 TYR A 192 19386 19565 16276 376 -1969 46 C
ATOM 1286 CE2 TYR A 192 17.123 153.914 218.908 1.00144.44 C
ANISOU 1286 CE2 TYR A 192 19257 19540 16082 915 -1871 -103 C
ATOM 1287 CZ TYR A 192 17.613 154.835 217.998 1.00155.36 C
ANISOU 1287 CZ TYR A 192 20748 20818 17462 550 -2110 -52 C
ATOM 1288 OH TYR A 192 17.958 156.090 218.439 1.00161.60 O
ANISOU 1288 OH TYR A 192 21757 21485 18158 355 -2499 -94 O
ATOM 1289 N GLU A 193 14.458 148.375 216.647 1.00115.70 N
ANISOU 1289 N GLU A 193 15214 15919 12828 1590 -410 54 N
ATOM 1290 CA GLU A 193 14.102 147.001 216.286 1.00112.22 C
ANISOU 1290 CA GLU A 193 14726 15482 12432 1705 -121 121 C
ATOM 1291 C GLU A 193 12.819 146.990 215.442 1.00110.87 C
ANISOU 1291 C GLU A 193 14665 15108 12354 1655 -73 64 C
ATOM 1292 O GLU A 193 12.768 146.296 214.429 1.00109.05 O
ANISOU 1292 O GLU A 193 14426 14829 12179 1595 81 120 O
ATOM 1293 CB GLU A 193 13.951 146.129 217.552 1.00113.71 C
ANISOU 1293 CB GLU A 193 14872 15775 12559 1965 23 146 C
ATOM 1294 CG GLU A 193 13.805 144.632 217.281 1.00122.76 C
ANISOU 1294 CG GLU A 193 16002 16921 13721 2073 292 241 C
ATOM 1295 CD GLU A 193 13.768 143.653 218.448 1.00135.39 C
ANISOU 1295 CD GLU A 193 17587 18604 15251 2305 433 294 C
ATOM 1296 OE1 GLU A 193 14.055 144.054 219.599 1.00118.26 O
ANISOU 1296 OE1 GLU A 193 15379 16542 13012 2411 343 261 O
ATOM 1297 OE2 GLU A 193 13.465 142.463 218.198 1.00129.18 O
ANISOU 1297 OE2 GLU A 193 16846 17765 14472 2376 623 372 O
ATOM 1298 N LYS A 194 11.808 147.792 215.844 1.00105.90 N
ANISOU 1298 N LYS A 194 14139 14377 11721 1697 -215 -52 N
ATOM 1299 CA LYS A 194 10.514 147.925 215.158 1.00104.20 C
ANISOU 1299 CA LYS A 194 14015 14012 11563 1673 -198 -119 C
ATOM 1300 C LYS A 194 10.644 148.621 213.788 1.00106.30 C
ANISOU 1300 C LYS A 194 14349 14139 11901 1435 -319 -136 C
ATOM 1301 O LYS A 194 10.074 148.140 212.804 1.00105.30 O
ANISOU 1301 O LYS A 194 14243 13924 11844 1366 -205 -124 O
ATOM 1302 CB LYS A 194 9.476 148.627 216.056 1.00106.60 C
ANISOU 1302 CB LYS A 194 14390 14315 11798 1844 -327 -245 C
ATOM 1303 N VAL A 195 11.410 149.731 213.726 1.00101.60 N
ANISOU 1303 N VAL A 195 13796 13528 11280 1291 -559 -152 N
ATOM 1304 CA VAL A 195 11.674 150.499 212.505 1.00100.46 C
ANISOU 1304 CA VAL A 195 13721 13267 11182 1028 -710 -144 C
ATOM 1305 C VAL A 195 12.359 149.596 211.462 1.00100.87 C
ANISOU 1305 C VAL A 195 13638 13408 11279 899 -512 -16 C
ATOM 1306 O VAL A 195 11.872 149.479 210.339 1.00 98.61 O
ANISOU 1306 O VAL A 195 13386 13018 11063 792 -458 -14 O
ATOM 1307 CB VAL A 195 12.473 151.795 212.830 1.00106.04 C
ANISOU 1307 CB VAL A 195 14523 13947 11821 877 -1038 -167 C
ATOM 1308 CG1 VAL A 195 13.153 152.380 211.592 1.00106.35 C
ANISOU 1308 CG1 VAL A 195 14562 13968 11880 544 -1159 -77 C
ATOM 1309 CG2 VAL A 195 11.574 152.836 213.492 1.00106.44 C
ANISOU 1309 CG2 VAL A 195 14792 13817 11833 992 -1279 -328 C
ATOM 1310 N TYR A 196 13.448 148.921 211.869 1.00 97.44 N
ANISOU 1310 N TYR A 196 13053 13180 10788 947 -400 82 N
ATOM 1311 CA TYR A 196 14.201 147.972 211.050 1.00 97.04 C
ANISOU 1311 CA TYR A 196 12868 13266 10736 910 -207 194 C
ATOM 1312 C TYR A 196 13.266 146.885 210.511 1.00100.62 C
ANISOU 1312 C TYR A 196 13366 13603 11263 1019 28 184 C
ATOM 1313 O TYR A 196 13.255 146.660 209.300 1.00100.20 O
ANISOU 1313 O TYR A 196 13306 13516 11250 902 90 214 O
ATOM 1314 CB TYR A 196 15.357 147.362 211.867 1.00 98.59 C
ANISOU 1314 CB TYR A 196 12911 13719 10830 1041 -126 277 C
ATOM 1315 CG TYR A 196 16.077 146.209 211.206 1.00 99.76 C
ANISOU 1315 CG TYR A 196 12937 14028 10940 1116 92 374 C
ATOM 1316 CD1 TYR A 196 16.999 146.428 210.189 1.00102.19 C
ANISOU 1316 CD1 TYR A 196 13122 14507 11197 940 59 453 C
ATOM 1317 CD2 TYR A 196 15.878 144.900 211.636 1.00100.35 C
ANISOU 1317 CD2 TYR A 196 13022 14105 11000 1378 313 391 C
ATOM 1318 CE1 TYR A 196 17.679 145.370 209.591 1.00103.10 C
ANISOU 1318 CE1 TYR A 196 13123 14807 11243 1064 250 527 C
ATOM 1319 CE2 TYR A 196 16.566 143.835 211.055 1.00101.63 C
ANISOU 1319 CE2 TYR A 196 13114 14400 11101 1496 488 465 C
ATOM 1320 CZ TYR A 196 17.468 144.076 210.035 1.00108.47 C
ANISOU 1320 CZ TYR A 196 13851 15451 11910 1360 459 523 C
ATOM 1321 OH TYR A 196 18.142 143.031 209.458 1.00109.75 O
ANISOU 1321 OH TYR A 196 13947 15770 11984 1525 625 579 O
ATOM 1322 N HIS A 197 12.449 146.256 211.395 1.00 96.57 N
ANISOU 1322 N HIS A 197 12902 13036 10753 1222 142 149 N
ATOM 1323 CA HIS A 197 11.495 145.221 210.998 1.00 95.46 C
ANISOU 1323 CA HIS A 197 12826 12783 10663 1290 341 155 C
ATOM 1324 C HIS A 197 10.556 145.735 209.911 1.00 96.86 C
ANISOU 1324 C HIS A 197 13085 12796 10921 1128 288 96 C
ATOM 1325 O HIS A 197 10.311 145.022 208.937 1.00 95.76 O
ANISOU 1325 O HIS A 197 12969 12589 10825 1071 421 128 O
ATOM 1326 CB HIS A 197 10.696 144.700 212.200 1.00 96.85 C
ANISOU 1326 CB HIS A 197 13035 12960 10805 1477 417 139 C
ATOM 1327 CG HIS A 197 9.584 143.772 211.805 1.00100.49 C
ANISOU 1327 CG HIS A 197 13573 13309 11300 1485 580 157 C
ATOM 1328 ND1 HIS A 197 9.805 142.429 211.613 1.00102.99 N
ANISOU 1328 ND1 HIS A 197 13926 13598 11606 1538 764 244 N
ATOM 1329 CD2 HIS A 197 8.289 144.042 211.520 1.00102.48 C
ANISOU 1329 CD2 HIS A 197 13878 13480 11578 1437 565 102 C
ATOM 1330 CE1 HIS A 197 8.641 141.919 211.242 1.00102.21 C
ANISOU 1330 CE1 HIS A 197 13915 13387 11535 1484 848 248 C
ATOM 1331 NE2 HIS A 197 7.703 142.851 211.165 1.00102.10 N
ANISOU 1331 NE2 HIS A 197 13890 13362 11540 1420 742 169 N
ATOM 1332 N ILE A 198 10.038 146.969 210.087 1.00 92.53 N
ANISOU 1332 N ILE A 198 12596 12180 10380 1070 82 5 N
ATOM 1333 CA ILE A 198 9.120 147.638 209.162 1.00 91.53 C
ANISOU 1333 CA ILE A 198 12561 11904 10313 940 -10 -63 C
ATOM 1334 C ILE A 198 9.807 147.937 207.800 1.00 95.03 C
ANISOU 1334 C ILE A 198 12985 12323 10798 714 -50 -12 C
ATOM 1335 O ILE A 198 9.230 147.650 206.748 1.00 92.93 O
ANISOU 1335 O ILE A 198 12747 11972 10591 632 39 -10 O
ATOM 1336 CB ILE A 198 8.488 148.884 209.852 1.00 95.14 C
ANISOU 1336 CB ILE A 198 13115 12303 10731 995 -250 -181 C
ATOM 1337 CG1 ILE A 198 7.473 148.445 210.934 1.00 95.66 C
ANISOU 1337 CG1 ILE A 198 13179 12425 10744 1221 -168 -235 C
ATOM 1338 CG2 ILE A 198 7.833 149.838 208.847 1.00 95.70 C
ANISOU 1338 CG2 ILE A 198 13301 12217 10843 847 -416 -248 C
ATOM 1339 CD1 ILE A 198 7.012 149.540 211.893 1.00103.97 C
ANISOU 1339 CD1 ILE A 198 14306 13488 11710 1371 -392 -356 C
ATOM 1340 N CYS A 199 11.044 148.466 207.833 1.00 93.19 N
ANISOU 1340 N CYS A 199 12691 12196 10520 607 -178 41 N
ATOM 1341 CA CYS A 199 11.833 148.779 206.645 1.00 93.81 C
ANISOU 1341 CA CYS A 199 12713 12330 10602 378 -229 116 C
ATOM 1342 C CYS A 199 12.104 147.556 205.791 1.00 99.32 C
ANISOU 1342 C CYS A 199 13321 13104 11311 407 15 185 C
ATOM 1343 O CYS A 199 11.909 147.605 204.570 1.00 99.43 O
ANISOU 1343 O CYS A 199 13350 13061 11367 263 27 194 O
ATOM 1344 CB CYS A 199 13.126 149.478 207.033 1.00 95.71 C
ANISOU 1344 CB CYS A 199 12872 12740 10754 258 -401 185 C
ATOM 1345 SG CYS A 199 12.891 151.191 207.551 1.00101.00 S
ANISOU 1345 SG CYS A 199 13725 13247 11405 93 -784 112 S
ATOM 1346 N VAL A 200 12.540 146.454 206.439 1.00 96.28 N
ANISOU 1346 N VAL A 200 12867 12838 10878 610 198 227 N
ATOM 1347 CA VAL A 200 12.833 145.172 205.799 1.00 95.80 C
ANISOU 1347 CA VAL A 200 12770 12832 10799 709 419 279 C
ATOM 1348 C VAL A 200 11.571 144.720 205.067 1.00 99.81 C
ANISOU 1348 C VAL A 200 13406 13121 11396 683 515 228 C
ATOM 1349 O VAL A 200 11.644 144.465 203.866 1.00 99.39 O
ANISOU 1349 O VAL A 200 13349 13060 11356 599 574 245 O
ATOM 1350 CB VAL A 200 13.388 144.131 206.814 1.00 99.53 C
ANISOU 1350 CB VAL A 200 13207 13416 11194 967 563 320 C
ATOM 1351 CG1 VAL A 200 13.341 142.712 206.260 1.00 99.36 C
ANISOU 1351 CG1 VAL A 200 13237 13368 11148 1111 772 350 C
ATOM 1352 CG2 VAL A 200 14.807 144.490 207.249 1.00100.33 C
ANISOU 1352 CG2 VAL A 200 13145 13790 11186 981 479 384 C
ATOM 1353 N THR A 201 10.403 144.752 205.760 1.00 96.46 N
ANISOU 1353 N THR A 201 13081 12553 11017 740 514 166 N
ATOM 1354 CA THR A 201 9.084 144.400 205.213 1.00 95.79 C
ANISOU 1354 CA THR A 201 13102 12297 10995 700 592 124 C
ATOM 1355 C THR A 201 8.757 145.248 203.945 1.00100.43 C
ANISOU 1355 C THR A 201 13709 12808 11643 494 486 87 C
ATOM 1356 O THR A 201 8.136 144.731 203.010 1.00100.36 O
ANISOU 1356 O THR A 201 13752 12706 11674 431 582 81 O
ATOM 1357 CB THR A 201 8.011 144.465 206.330 1.00100.19 C
ANISOU 1357 CB THR A 201 13708 12815 11546 803 586 79 C
ATOM 1358 OG1 THR A 201 8.293 143.471 207.322 1.00101.98 O
ANISOU 1358 OG1 THR A 201 13919 13117 11711 976 691 134 O
ATOM 1359 CG2 THR A 201 6.607 144.240 205.821 1.00 96.15 C
ANISOU 1359 CG2 THR A 201 13273 12191 11067 749 668 56 C
ATOM 1360 N VAL A 202 9.227 146.512 203.890 1.00 96.27 N
ANISOU 1360 N VAL A 202 13155 12313 11112 379 279 70 N
ATOM 1361 CA VAL A 202 8.990 147.379 202.737 1.00 95.54 C
ANISOU 1361 CA VAL A 202 13097 12141 11063 173 153 50 C
ATOM 1362 C VAL A 202 9.900 147.011 201.567 1.00101.41 C
ANISOU 1362 C VAL A 202 13749 12994 11788 55 220 133 C
ATOM 1363 O VAL A 202 9.391 146.765 200.469 1.00101.58 O
ANISOU 1363 O VAL A 202 13801 12944 11852 -34 281 125 O
ATOM 1364 CB VAL A 202 9.049 148.884 203.094 1.00 99.49 C
ANISOU 1364 CB VAL A 202 13659 12593 11550 78 -128 6 C
ATOM 1365 CG1 VAL A 202 8.892 149.758 201.852 1.00 99.00 C
ANISOU 1365 CG1 VAL A 202 13659 12434 11522 -149 -274 3 C
ATOM 1366 CG2 VAL A 202 7.987 149.240 204.132 1.00 99.14 C
ANISOU 1366 CG2 VAL A 202 13708 12462 11497 246 -191 -97 C
ATOM 1367 N LEU A 203 11.233 146.964 201.796 1.00 98.81 N
ANISOU 1367 N LEU A 203 13295 12873 11377 68 213 212 N
ATOM 1368 CA LEU A 203 12.232 146.649 200.762 1.00 99.24 C
ANISOU 1368 CA LEU A 203 13220 13121 11367 -12 272 298 C
ATOM 1369 C LEU A 203 12.139 145.243 200.185 1.00103.05 C
ANISOU 1369 C LEU A 203 13708 13611 11834 153 512 300 C
ATOM 1370 O LEU A 203 12.518 145.039 199.039 1.00102.57 O
ANISOU 1370 O LEU A 203 13576 13667 11730 91 559 340 O
ATOM 1371 CB LEU A 203 13.656 146.906 201.265 1.00100.74 C
ANISOU 1371 CB LEU A 203 13245 13593 11438 -33 193 390 C
ATOM 1372 CG LEU A 203 14.012 148.359 201.588 1.00106.60 C
ANISOU 1372 CG LEU A 203 13986 14356 12162 -287 -89 421 C
ATOM 1373 CD1 LEU A 203 15.251 148.427 202.445 1.00108.39 C
ANISOU 1373 CD1 LEU A 203 14078 14834 12273 -268 -160 496 C
ATOM 1374 CD2 LEU A 203 14.225 149.184 200.321 1.00109.72 C
ANISOU 1374 CD2 LEU A 203 14342 14806 12542 -581 -206 489 C
ATOM 1375 N ILE A 204 11.630 144.286 200.969 1.00100.22 N
ANISOU 1375 N ILE A 204 13453 13128 11499 353 647 260 N
ATOM 1376 CA ILE A 204 11.503 142.878 200.590 1.00100.52 C
ANISOU 1376 CA ILE A 204 13565 13120 11508 520 846 261 C
ATOM 1377 C ILE A 204 10.112 142.541 200.016 1.00101.96 C
ANISOU 1377 C ILE A 204 13910 13051 11780 459 910 203 C
ATOM 1378 O ILE A 204 9.964 141.493 199.379 1.00101.63 O
ANISOU 1378 O ILE A 204 13967 12933 11715 541 1043 201 O
ATOM 1379 CB ILE A 204 11.916 142.011 201.830 1.00104.90 C
ANISOU 1379 CB ILE A 204 14133 13733 11991 771 933 288 C
ATOM 1380 CG1 ILE A 204 13.341 141.508 201.667 1.00107.80 C
ANISOU 1380 CG1 ILE A 204 14384 14355 12220 925 998 346 C
ATOM 1381 CG2 ILE A 204 10.956 140.879 202.250 1.00104.73 C
ANISOU 1381 CG2 ILE A 204 14299 13495 11997 898 1056 266 C
ATOM 1382 CD1 ILE A 204 14.298 142.157 202.623 1.00121.13 C
ANISOU 1382 CD1 ILE A 204 15904 16287 13833 955 907 398 C
ATOM 1383 N TYR A 205 9.106 143.419 200.210 1.00 96.55 N
ANISOU 1383 N TYR A 205 13260 12249 11177 321 803 155 N
ATOM 1384 CA TYR A 205 7.768 143.081 199.740 1.00 95.32 C
ANISOU 1384 CA TYR A 205 13225 11909 11084 259 859 109 C
ATOM 1385 C TYR A 205 6.995 144.206 199.058 1.00 98.36 C
ANISOU 1385 C TYR A 205 13608 12229 11534 72 728 59 C
ATOM 1386 O TYR A 205 6.770 144.114 197.854 1.00 98.36 O
ANISOU 1386 O TYR A 205 13626 12189 11558 -41 753 53 O
ATOM 1387 CB TYR A 205 6.939 142.494 200.895 1.00 96.08 C
ANISOU 1387 CB TYR A 205 13398 11935 11173 369 916 102 C
ATOM 1388 CG TYR A 205 5.631 141.875 200.467 1.00 96.46 C
ANISOU 1388 CG TYR A 205 13561 11843 11248 296 998 86 C
ATOM 1389 CD1 TYR A 205 5.579 140.565 199.995 1.00 98.85 C
ANISOU 1389 CD1 TYR A 205 13991 12046 11523 321 1134 120 C
ATOM 1390 CD2 TYR A 205 4.438 142.582 200.569 1.00 96.23 C
ANISOU 1390 CD2 TYR A 205 13523 11790 11249 207 925 39 C
ATOM 1391 CE1 TYR A 205 4.373 139.985 199.608 1.00 99.66 C
ANISOU 1391 CE1 TYR A 205 14207 12022 11636 208 1190 119 C
ATOM 1392 CE2 TYR A 205 3.227 142.016 200.179 1.00 96.98 C
ANISOU 1392 CE2 TYR A 205 13694 11808 11346 115 997 38 C
ATOM 1393 CZ TYR A 205 3.199 140.717 199.698 1.00105.59 C
ANISOU 1393 CZ TYR A 205 14909 12795 12417 92 1127 85 C
ATOM 1394 OH TYR A 205 2.005 140.165 199.310 1.00106.81 O
ANISOU 1394 OH TYR A 205 15146 12877 12559 -39 1180 98 O
ATOM 1395 N PHE A 206 6.523 145.208 199.820 1.00 93.55 N
ANISOU 1395 N PHE A 206 12996 11607 10941 63 584 17 N
ATOM 1396 CA PHE A 206 5.657 146.275 199.320 1.00 92.61 C
ANISOU 1396 CA PHE A 206 12915 11410 10864 -58 436 -45 C
ATOM 1397 C PHE A 206 6.280 147.164 198.231 1.00 95.19 C
ANISOU 1397 C PHE A 206 13216 11746 11206 -241 307 -24 C
ATOM 1398 O PHE A 206 5.665 147.315 197.165 1.00 94.32 O
ANISOU 1398 O PHE A 206 13145 11557 11134 -357 294 -49 O
ATOM 1399 CB PHE A 206 5.106 147.124 200.479 1.00 94.91 C
ANISOU 1399 CB PHE A 206 13230 11699 11131 40 291 -105 C
ATOM 1400 CG PHE A 206 4.284 146.322 201.467 1.00 97.07 C
ANISOU 1400 CG PHE A 206 13512 12000 11372 194 412 -118 C
ATOM 1401 CD1 PHE A 206 3.015 145.855 201.128 1.00 99.95 C
ANISOU 1401 CD1 PHE A 206 13907 12332 11738 172 495 -141 C
ATOM 1402 CD2 PHE A 206 4.788 146.011 202.730 1.00 99.83 C
ANISOU 1402 CD2 PHE A 206 13827 12431 11674 342 441 -91 C
ATOM 1403 CE1 PHE A 206 2.267 145.093 202.036 1.00101.06 C
ANISOU 1403 CE1 PHE A 206 14038 12537 11823 272 598 -124 C
ATOM 1404 CE2 PHE A 206 4.036 145.255 203.638 1.00102.43 C
ANISOU 1404 CE2 PHE A 206 14158 12803 11958 461 549 -81 C
ATOM 1405 CZ PHE A 206 2.785 144.797 203.284 1.00100.33 C
ANISOU 1405 CZ PHE A 206 13917 12518 11684 413 624 -91 C
ATOM 1406 N LEU A 207 7.476 147.745 198.485 1.00 91.00 N
ANISOU 1406 N LEU A 207 12613 11328 10633 -286 204 33 N
ATOM 1407 CA LEU A 207 8.143 148.627 197.521 1.00 90.56 C
ANISOU 1407 CA LEU A 207 12523 11319 10568 -505 61 84 C
ATOM 1408 C LEU A 207 8.416 147.946 196.149 1.00 93.86 C
ANISOU 1408 C LEU A 207 12876 11803 10982 -581 204 129 C
ATOM 1409 O LEU A 207 7.884 148.451 195.159 1.00 92.27 O
ANISOU 1409 O LEU A 207 12722 11516 10821 -727 144 112 O
ATOM 1410 CB LEU A 207 9.417 149.266 198.105 1.00 91.43 C
ANISOU 1410 CB LEU A 207 12554 11580 10607 -575 -89 158 C
ATOM 1411 CG LEU A 207 10.281 150.056 197.117 1.00 96.25 C
ANISOU 1411 CG LEU A 207 13119 12272 11179 -852 -259 245 C
ATOM 1412 CD1 LEU A 207 9.671 151.412 196.805 1.00 95.93 C
ANISOU 1412 CD1 LEU A 207 13250 12032 11168 -997 -533 200 C
ATOM 1413 CD2 LEU A 207 11.688 150.206 197.633 1.00100.01 C
ANISOU 1413 CD2 LEU A 207 13435 13018 11548 -916 -297 360 C
ATOM 1414 N PRO A 208 9.186 146.825 196.045 1.00 91.06 N
ANISOU 1414 N PRO A 208 12433 11595 10570 -464 384 177 N
ATOM 1415 CA PRO A 208 9.413 146.223 194.720 1.00 91.11 C
ANISOU 1415 CA PRO A 208 12398 11668 10551 -506 500 201 C
ATOM 1416 C PRO A 208 8.167 145.687 194.023 1.00 94.70 C
ANISOU 1416 C PRO A 208 12977 11927 11077 -507 602 130 C
ATOM 1417 O PRO A 208 8.107 145.785 192.798 1.00 94.22 O
ANISOU 1417 O PRO A 208 12896 11893 11009 -609 627 140 O
ATOM 1418 CB PRO A 208 10.441 145.127 194.987 1.00 93.71 C
ANISOU 1418 CB PRO A 208 12644 12182 10778 -304 650 244 C
ATOM 1419 CG PRO A 208 10.335 144.839 196.405 1.00 98.07 C
ANISOU 1419 CG PRO A 208 13243 12680 11339 -141 669 224 C
ATOM 1420 CD PRO A 208 9.921 146.086 197.091 1.00 93.26 C
ANISOU 1420 CD PRO A 208 12655 11996 10785 -267 473 206 C
ATOM 1421 N LEU A 209 7.169 145.153 194.775 1.00 91.18 N
ANISOU 1421 N LEU A 209 12644 11317 10682 -411 656 68 N
ATOM 1422 CA LEU A 209 5.919 144.654 194.170 1.00 90.51 C
ANISOU 1422 CA LEU A 209 12665 11078 10645 -447 740 15 C
ATOM 1423 C LEU A 209 5.125 145.781 193.513 1.00 94.90 C
ANISOU 1423 C LEU A 209 13236 11565 11256 -620 604 -21 C
ATOM 1424 O LEU A 209 4.475 145.569 192.486 1.00 94.36 O
ANISOU 1424 O LEU A 209 13209 11432 11212 -706 655 -46 O
ATOM 1425 CB LEU A 209 5.031 143.867 195.153 1.00 90.02 C
ANISOU 1425 CB LEU A 209 12696 10917 10590 -328 832 -13 C
ATOM 1426 CG LEU A 209 5.421 142.410 195.440 1.00 94.84 C
ANISOU 1426 CG LEU A 209 13377 11512 11146 -175 994 18 C
ATOM 1427 CD1 LEU A 209 4.571 141.845 196.536 1.00 94.52 C
ANISOU 1427 CD1 LEU A 209 13424 11386 11103 -117 1047 16 C
ATOM 1428 CD2 LEU A 209 5.320 141.528 194.196 1.00 96.83 C
ANISOU 1428 CD2 LEU A 209 13711 11704 11375 -199 1098 12 C
ATOM 1429 N LEU A 210 5.220 146.985 194.083 1.00 91.91 N
ANISOU 1429 N LEU A 210 12844 11193 10886 -666 416 -26 N
ATOM 1430 CA LEU A 210 4.584 148.169 193.534 1.00 91.96 C
ANISOU 1430 CA LEU A 210 12900 11117 10924 -804 244 -61 C
ATOM 1431 C LEU A 210 5.247 148.524 192.192 1.00 96.44 C
ANISOU 1431 C LEU A 210 13414 11747 11481 -994 196 3 C
ATOM 1432 O LEU A 210 4.539 148.707 191.204 1.00 96.88 O
ANISOU 1432 O LEU A 210 13509 11735 11566 -1103 174 -20 O
ATOM 1433 CB LEU A 210 4.743 149.319 194.526 1.00 92.75 C
ANISOU 1433 CB LEU A 210 13043 11188 11008 -776 31 -82 C
ATOM 1434 CG LEU A 210 3.662 150.365 194.488 1.00 97.68 C
ANISOU 1434 CG LEU A 210 13782 11687 11645 -772 -131 -167 C
ATOM 1435 CD1 LEU A 210 2.437 149.912 195.297 1.00 97.73 C
ANISOU 1435 CD1 LEU A 210 13804 11690 11639 -581 -30 -244 C
ATOM 1436 CD2 LEU A 210 4.196 151.696 194.984 1.00100.21 C
ANISOU 1436 CD2 LEU A 210 14191 11950 11934 -815 -409 -171 C
ATOM 1437 N VAL A 211 6.604 148.555 192.154 1.00 91.99 N
ANISOU 1437 N VAL A 211 12742 11352 10859 -1029 189 91 N
ATOM 1438 CA VAL A 211 7.450 148.853 190.987 1.00 91.23 C
ANISOU 1438 CA VAL A 211 12545 11405 10712 -1208 151 179 C
ATOM 1439 C VAL A 211 7.210 147.837 189.861 1.00 92.86 C
ANISOU 1439 C VAL A 211 12732 11634 10915 -1177 343 160 C
ATOM 1440 O VAL A 211 6.954 148.245 188.729 1.00 91.27 O
ANISOU 1440 O VAL A 211 12527 11431 10722 -1336 297 175 O
ATOM 1441 CB VAL A 211 8.950 148.963 191.394 1.00 96.19 C
ANISOU 1441 CB VAL A 211 13026 12280 11241 -1224 115 283 C
ATOM 1442 CG1 VAL A 211 9.857 149.123 190.180 1.00 97.12 C
ANISOU 1442 CG1 VAL A 211 12996 12636 11269 -1401 98 392 C
ATOM 1443 CG2 VAL A 211 9.176 150.113 192.372 1.00 96.46 C
ANISOU 1443 CG2 VAL A 211 13110 12266 11273 -1303 -115 302 C
ATOM 1444 N ILE A 212 7.260 146.522 190.185 1.00 89.90 N
ANISOU 1444 N ILE A 212 12373 11260 10524 -975 540 124 N
ATOM 1445 CA ILE A 212 7.009 145.418 189.241 1.00 89.73 C
ANISOU 1445 CA ILE A 212 12389 11220 10486 -916 710 91 C
ATOM 1446 C ILE A 212 5.579 145.540 188.703 1.00 93.75 C
ANISOU 1446 C ILE A 212 13014 11528 11079 -1011 705 21 C
ATOM 1447 O ILE A 212 5.367 145.374 187.501 1.00 94.20 O
ANISOU 1447 O ILE A 212 13077 11586 11129 -1089 751 10 O
ATOM 1448 CB ILE A 212 7.277 144.014 189.867 1.00 92.78 C
ANISOU 1448 CB ILE A 212 12830 11599 10822 -671 880 70 C
ATOM 1449 CG1 ILE A 212 8.761 143.834 190.244 1.00 94.36 C
ANISOU 1449 CG1 ILE A 212 12891 12059 10903 -548 902 139 C
ATOM 1450 CG2 ILE A 212 6.836 142.909 188.916 1.00 92.82 C
ANISOU 1450 CG2 ILE A 212 12958 11495 10814 -618 1020 17 C
ATOM 1451 CD1 ILE A 212 9.091 142.667 191.216 1.00100.13 C
ANISOU 1451 CD1 ILE A 212 13688 12780 11575 -278 1026 125 C
ATOM 1452 N GLY A 213 4.635 145.863 189.590 1.00 89.01 N
ANISOU 1452 N GLY A 213 12489 10793 10538 -992 650 -26 N
ATOM 1453 CA GLY A 213 3.239 146.073 189.236 1.00 88.26 C
ANISOU 1453 CA GLY A 213 12474 10564 10495 -1063 636 -88 C
ATOM 1454 C GLY A 213 3.069 147.121 188.155 1.00 93.21 C
ANISOU 1454 C GLY A 213 13084 11188 11142 -1240 506 -83 C
ATOM 1455 O GLY A 213 2.399 146.863 187.149 1.00 92.31 O
ANISOU 1455 O GLY A 213 13003 11028 11043 -1314 558 -114 O
ATOM 1456 N TYR A 214 3.740 148.289 188.334 1.00 91.22 N
ANISOU 1456 N TYR A 214 12796 10984 10880 -1323 325 -35 N
ATOM 1457 CA TYR A 214 3.735 149.420 187.403 1.00 91.87 C
ANISOU 1457 CA TYR A 214 12886 11056 10966 -1515 153 -2 C
ATOM 1458 C TYR A 214 4.282 149.073 186.000 1.00 97.23 C
ANISOU 1458 C TYR A 214 13476 11860 11607 -1635 232 57 C
ATOM 1459 O TYR A 214 3.661 149.438 184.995 1.00 96.52 O
ANISOU 1459 O TYR A 214 13415 11724 11535 -1753 198 45 O
ATOM 1460 CB TYR A 214 4.475 150.645 187.989 1.00 94.29 C
ANISOU 1460 CB TYR A 214 13201 11379 11246 -1599 -77 59 C
ATOM 1461 CG TYR A 214 4.781 151.687 186.934 1.00 98.40 C
ANISOU 1461 CG TYR A 214 13731 11914 11743 -1843 -259 136 C
ATOM 1462 CD1 TYR A 214 3.799 152.568 186.491 1.00100.63 C
ANISOU 1462 CD1 TYR A 214 14153 12027 12056 -1912 -419 90 C
ATOM 1463 CD2 TYR A 214 6.023 151.725 186.303 1.00100.82 C
ANISOU 1463 CD2 TYR A 214 13899 12431 11978 -2001 -263 262 C
ATOM 1464 CE1 TYR A 214 4.054 153.484 185.467 1.00102.55 C
ANISOU 1464 CE1 TYR A 214 14426 12267 12272 -2149 -588 172 C
ATOM 1465 CE2 TYR A 214 6.281 152.617 185.259 1.00102.79 C
ANISOU 1465 CE2 TYR A 214 14146 12719 12191 -2258 -423 355 C
ATOM 1466 CZ TYR A 214 5.295 153.499 184.849 1.00110.03 C
ANISOU 1466 CZ TYR A 214 15232 13422 13153 -2340 -590 312 C
ATOM 1467 OH TYR A 214 5.558 154.394 183.840 1.00112.26 O
ANISOU 1467 OH TYR A 214 15538 13724 13393 -2606 -766 417 O
ATOM 1468 N ALA A 215 5.479 148.453 185.933 1.00 94.70 N
ANISOU 1468 N ALA A 215 13038 11728 11217 -1592 324 122 N
ATOM 1469 CA ALA A 215 6.115 148.143 184.656 1.00 95.16 C
ANISOU 1469 CA ALA A 215 12986 11971 11200 -1666 396 179 C
ATOM 1470 C ALA A 215 5.278 147.207 183.821 1.00 98.51 C
ANISOU 1470 C ALA A 215 13476 12310 11645 -1609 554 98 C
ATOM 1471 O ALA A 215 4.896 147.598 182.725 1.00 98.32 O
ANISOU 1471 O ALA A 215 13437 12305 11617 -1750 522 110 O
ATOM 1472 CB ALA A 215 7.508 147.580 184.867 1.00 97.06 C
ANISOU 1472 CB ALA A 215 13084 12465 11330 -1559 476 246 C
ATOM 1473 N TYR A 216 4.917 146.022 184.364 1.00 95.21 N
ANISOU 1473 N TYR A 216 13148 11784 11243 -1425 705 23 N
ATOM 1474 CA TYR A 216 4.122 145.008 183.660 1.00 95.06 C
ANISOU 1474 CA TYR A 216 13228 11662 11230 -1389 841 -50 C
ATOM 1475 C TYR A 216 2.705 145.476 183.326 1.00 99.04 C
ANISOU 1475 C TYR A 216 13810 12009 11813 -1519 786 -102 C
ATOM 1476 O TYR A 216 2.125 144.937 182.385 1.00 99.04 O
ANISOU 1476 O TYR A 216 13855 11970 11805 -1567 856 -141 O
ATOM 1477 CB TYR A 216 4.113 143.635 184.374 1.00 96.39 C
ANISOU 1477 CB TYR A 216 13505 11745 11372 -1190 988 -96 C
ATOM 1478 CG TYR A 216 5.438 142.895 184.317 1.00 99.59 C
ANISOU 1478 CG TYR A 216 13858 12316 11664 -1010 1069 -67 C
ATOM 1479 CD1 TYR A 216 6.164 142.806 183.128 1.00102.53 C
ANISOU 1479 CD1 TYR A 216 14136 12885 11937 -1002 1097 -45 C
ATOM 1480 CD2 TYR A 216 5.951 142.259 185.441 1.00100.70 C
ANISOU 1480 CD2 TYR A 216 14041 12445 11777 -822 1121 -62 C
ATOM 1481 CE1 TYR A 216 7.398 142.153 183.078 1.00103.91 C
ANISOU 1481 CE1 TYR A 216 14240 13270 11971 -794 1168 -23 C
ATOM 1482 CE2 TYR A 216 7.174 141.586 185.398 1.00103.02 C
ANISOU 1482 CE2 TYR A 216 14285 12915 11944 -618 1191 -41 C
ATOM 1483 CZ TYR A 216 7.894 141.535 184.215 1.00110.93 C
ANISOU 1483 CZ TYR A 216 15180 14137 12832 -592 1215 -25 C
ATOM 1484 OH TYR A 216 9.100 140.879 184.183 1.00114.33 O
ANISOU 1484 OH TYR A 216 15545 14792 13105 -349 1281 -9 O
ATOM 1485 N THR A 217 2.159 146.499 184.020 1.00 95.46 N
ANISOU 1485 N THR A 217 13372 11482 11416 -1561 652 -108 N
ATOM 1486 CA THR A 217 0.838 146.980 183.606 1.00 94.89 C
ANISOU 1486 CA THR A 217 13356 11310 11386 -1649 593 -159 C
ATOM 1487 C THR A 217 0.997 147.849 182.308 1.00 97.67 C
ANISOU 1487 C THR A 217 13668 11710 11732 -1820 489 -122 C
ATOM 1488 O THR A 217 0.293 147.595 181.327 1.00 97.37 O
ANISOU 1488 O THR A 217 13653 11644 11698 -1889 534 -158 O
ATOM 1489 CB THR A 217 0.002 147.606 184.750 1.00102.68 C
ANISOU 1489 CB THR A 217 14388 12224 12402 -1581 491 -198 C
ATOM 1490 OG1 THR A 217 -1.227 148.080 184.201 1.00102.96 O
ANISOU 1490 OG1 THR A 217 14460 12214 12446 -1634 459 -252 O
ATOM 1491 CG2 THR A 217 0.677 148.752 185.438 1.00102.86 C
ANISOU 1491 CG2 THR A 217 14405 12250 12426 -1595 291 -163 C
ATOM 1492 N VAL A 218 1.972 148.782 182.281 1.00 92.89 N
ANISOU 1492 N VAL A 218 12999 11192 11102 -1905 354 -38 N
ATOM 1493 CA VAL A 218 2.276 149.633 181.117 1.00 92.53 C
ANISOU 1493 CA VAL A 218 12911 11217 11031 -2099 236 31 C
ATOM 1494 C VAL A 218 2.650 148.753 179.896 1.00 97.20 C
ANISOU 1494 C VAL A 218 13420 11946 11566 -2121 393 43 C
ATOM 1495 O VAL A 218 2.133 148.955 178.793 1.00 97.45 O
ANISOU 1495 O VAL A 218 13458 11970 11597 -2231 382 35 O
ATOM 1496 CB VAL A 218 3.376 150.680 181.465 1.00 96.38 C
ANISOU 1496 CB VAL A 218 13351 11791 11478 -2216 48 145 C
ATOM 1497 CG1 VAL A 218 3.832 151.456 180.236 1.00 96.52 C
ANISOU 1497 CG1 VAL A 218 13306 11927 11439 -2453 -65 254 C
ATOM 1498 CG2 VAL A 218 2.901 151.637 182.557 1.00 95.98 C
ANISOU 1498 CG2 VAL A 218 13433 11566 11470 -2192 -148 115 C
ATOM 1499 N VAL A 219 3.514 147.759 180.123 1.00 93.62 N
ANISOU 1499 N VAL A 219 12899 11621 11052 -1991 533 54 N
ATOM 1500 CA VAL A 219 3.978 146.803 179.119 1.00 93.90 C
ANISOU 1500 CA VAL A 219 12874 11802 11000 -1936 680 48 C
ATOM 1501 C VAL A 219 2.826 145.849 178.703 1.00 98.89 C
ANISOU 1501 C VAL A 219 13639 12269 11667 -1883 804 -64 C
ATOM 1502 O VAL A 219 2.762 145.421 177.547 1.00 99.54 O
ANISOU 1502 O VAL A 219 13706 12412 11702 -1927 856 -80 O
ATOM 1503 CB VAL A 219 5.243 146.074 179.647 1.00 97.74 C
ANISOU 1503 CB VAL A 219 13277 12469 11390 -1757 771 80 C
ATOM 1504 CG1 VAL A 219 5.668 144.921 178.750 1.00 98.15 C
ANISOU 1504 CG1 VAL A 219 13350 12599 11344 -1582 942 20 C
ATOM 1505 CG2 VAL A 219 6.387 147.051 179.820 1.00 98.43 C
ANISOU 1505 CG2 VAL A 219 13181 12823 11394 -1878 651 217 C
ATOM 1506 N GLY A 220 1.917 145.564 179.631 1.00 94.86 N
ANISOU 1506 N GLY A 220 13248 11570 11225 -1811 838 -129 N
ATOM 1507 CA GLY A 220 0.769 144.706 179.356 1.00 94.99 C
ANISOU 1507 CA GLY A 220 13391 11439 11261 -1807 932 -214 C
ATOM 1508 C GLY A 220 -0.208 145.359 178.400 1.00 99.37 C
ANISOU 1508 C GLY A 220 13945 11959 11853 -1974 863 -232 C
ATOM 1509 O GLY A 220 -0.727 144.711 177.485 1.00 99.06 O
ANISOU 1509 O GLY A 220 13962 11884 11791 -2018 937 -282 O
ATOM 1510 N ILE A 221 -0.433 146.668 178.611 1.00 95.43 N
ANISOU 1510 N ILE A 221 13401 11461 11398 -2059 705 -196 N
ATOM 1511 CA ILE A 221 -1.289 147.532 177.806 1.00 94.52 C
ANISOU 1511 CA ILE A 221 13292 11317 11305 -2192 605 -207 C
ATOM 1512 C ILE A 221 -0.692 147.684 176.390 1.00 99.08 C
ANISOU 1512 C ILE A 221 13800 12012 11834 -2309 606 -163 C
ATOM 1513 O ILE A 221 -1.429 147.595 175.406 1.00 98.96 O
ANISOU 1513 O ILE A 221 13807 11981 11814 -2383 636 -202 O
ATOM 1514 CB ILE A 221 -1.492 148.883 178.551 1.00 97.11 C
ANISOU 1514 CB ILE A 221 13637 11593 11669 -2207 407 -183 C
ATOM 1515 CG1 ILE A 221 -2.569 148.743 179.643 1.00 96.84 C
ANISOU 1515 CG1 ILE A 221 13663 11475 11658 -2084 416 -254 C
ATOM 1516 CG2 ILE A 221 -1.830 150.035 177.594 1.00 97.98 C
ANISOU 1516 CG2 ILE A 221 13759 11692 11776 -2347 255 -160 C
ATOM 1517 CD1 ILE A 221 -2.404 149.677 180.828 1.00103.70 C
ANISOU 1517 CD1 ILE A 221 14571 12293 12539 -2015 232 -251 C
ATOM 1518 N ARG A 222 0.633 147.876 176.290 1.00 95.75 N
ANISOU 1518 N ARG A 222 13280 11740 11359 -2327 578 -76 N
ATOM 1519 CA ARG A 222 1.294 148.033 175.002 1.00 96.41 C
ANISOU 1519 CA ARG A 222 13263 12003 11365 -2433 579 -15 C
ATOM 1520 C ARG A 222 1.251 146.766 174.126 1.00101.37 C
ANISOU 1520 C ARG A 222 13906 12678 11932 -2346 757 -89 C
ATOM 1521 O ARG A 222 1.029 146.882 172.919 1.00101.49 O
ANISOU 1521 O ARG A 222 13896 12750 11915 -2445 759 -92 O
ATOM 1522 CB ARG A 222 2.735 148.545 175.189 1.00 97.49 C
ANISOU 1522 CB ARG A 222 13261 12355 11425 -2474 510 110 C
ATOM 1523 CG ARG A 222 3.517 148.777 173.880 1.00108.59 C
ANISOU 1523 CG ARG A 222 14516 14030 12713 -2588 511 199 C
ATOM 1524 CD ARG A 222 3.049 149.985 173.069 1.00116.54 C
ANISOU 1524 CD ARG A 222 15525 15018 13735 -2833 345 272 C
ATOM 1525 NE ARG A 222 3.810 151.197 173.380 1.00124.30 N
ANISOU 1525 NE ARG A 222 16478 16048 14703 -3016 132 415 N
ATOM 1526 CZ ARG A 222 4.990 151.498 172.845 1.00142.24 C
ANISOU 1526 CZ ARG A 222 18582 18612 16850 -3165 68 570 C
ATOM 1527 NH1 ARG A 222 5.559 150.678 171.967 1.00133.30 N
ANISOU 1527 NH1 ARG A 222 17276 17784 15588 -3110 214 593 N
ATOM 1528 NH2 ARG A 222 5.616 152.618 173.191 1.00127.99 N
ANISOU 1528 NH2 ARG A 222 16787 16816 15029 -3371 -153 708 N
ATOM 1529 N LEU A 223 1.455 145.576 174.726 1.00 98.34 N
ANISOU 1529 N LEU A 223 13585 12260 11521 -2157 890 -149 N
ATOM 1530 CA LEU A 223 1.511 144.291 174.012 1.00 98.71 C
ANISOU 1530 CA LEU A 223 13706 12314 11486 -2037 1035 -230 C
ATOM 1531 C LEU A 223 0.175 143.699 173.615 1.00103.87 C
ANISOU 1531 C LEU A 223 14515 12767 12183 -2091 1082 -325 C
ATOM 1532 O LEU A 223 0.105 142.951 172.639 1.00103.01 O
ANISOU 1532 O LEU A 223 14473 12666 12002 -2060 1156 -386 O
ATOM 1533 CB LEU A 223 2.295 143.241 174.818 1.00 98.88 C
ANISOU 1533 CB LEU A 223 13787 12336 11446 -1802 1131 -258 C
ATOM 1534 CG LEU A 223 3.800 143.416 174.936 1.00103.51 C
ANISOU 1534 CG LEU A 223 14206 13188 11934 -1697 1121 -174 C
ATOM 1535 CD1 LEU A 223 4.334 142.561 176.039 1.00104.17 C
ANISOU 1535 CD1 LEU A 223 14374 13211 11996 -1473 1189 -203 C
ATOM 1536 CD2 LEU A 223 4.502 143.042 173.657 1.00105.98 C
ANISOU 1536 CD2 LEU A 223 14410 13772 12086 -1628 1171 -166 C
ATOM 1537 N TRP A 224 -0.868 143.982 174.394 1.00102.90 N
ANISOU 1537 N TRP A 224 14453 12487 12157 -2158 1038 -340 N
ATOM 1538 CA TRP A 224 -2.182 143.398 174.158 1.00104.09 C
ANISOU 1538 CA TRP A 224 14728 12492 12328 -2231 1079 -412 C
ATOM 1539 C TRP A 224 -3.224 144.405 173.636 1.00109.92 C
ANISOU 1539 C TRP A 224 15409 13242 13115 -2396 986 -406 C
ATOM 1540 O TRP A 224 -3.858 144.125 172.619 1.00110.50 O
ANISOU 1540 O TRP A 224 15520 13305 13161 -2488 1016 -450 O
ATOM 1541 CB TRP A 224 -2.664 142.646 175.412 1.00102.91 C
ANISOU 1541 CB TRP A 224 14697 12200 12203 -2161 1124 -435 C
ATOM 1542 CG TRP A 224 -2.002 141.298 175.561 1.00105.34 C
ANISOU 1542 CG TRP A 224 15150 12436 12438 -2013 1224 -469 C
ATOM 1543 CD1 TRP A 224 -2.341 140.151 174.906 1.00109.36 C
ANISOU 1543 CD1 TRP A 224 15839 12835 12879 -2019 1287 -534 C
ATOM 1544 CD2 TRP A 224 -0.849 140.971 176.369 1.00105.72 C
ANISOU 1544 CD2 TRP A 224 15198 12516 12455 -1821 1253 -445 C
ATOM 1545 NE1 TRP A 224 -1.489 139.127 175.264 1.00110.16 N
ANISOU 1545 NE1 TRP A 224 16078 12872 12904 -1821 1345 -559 N
ATOM 1546 CE2 TRP A 224 -0.566 139.601 176.164 1.00111.01 C
ANISOU 1546 CE2 TRP A 224 16064 13083 13032 -1689 1334 -503 C
ATOM 1547 CE3 TRP A 224 -0.037 141.698 177.260 1.00106.35 C
ANISOU 1547 CE3 TRP A 224 15146 12700 12564 -1744 1208 -380 C
ATOM 1548 CZ2 TRP A 224 0.496 138.947 176.807 1.00110.81 C
ANISOU 1548 CZ2 TRP A 224 16097 13068 12939 -1457 1376 -502 C
ATOM 1549 CZ3 TRP A 224 1.015 141.046 177.895 1.00108.26 C
ANISOU 1549 CZ3 TRP A 224 15416 12974 12742 -1540 1260 -371 C
ATOM 1550 CH2 TRP A 224 1.267 139.687 177.672 1.00109.99 C
ANISOU 1550 CH2 TRP A 224 15824 13102 12867 -1386 1347 -433 C
ATOM 1551 N ALA A 225 -3.367 145.575 174.284 1.00106.73 N
ANISOU 1551 N ALA A 225 14931 12857 12766 -2420 862 -358 N
ATOM 1552 CA ALA A 225 -4.345 146.601 173.895 1.00106.39 C
ANISOU 1552 CA ALA A 225 14860 12816 12749 -2525 750 -359 C
ATOM 1553 C ALA A 225 -3.926 147.498 172.708 1.00110.96 C
ANISOU 1553 C ALA A 225 15367 13485 13308 -2638 660 -306 C
ATOM 1554 O ALA A 225 -2.735 147.604 172.397 1.00112.06 O
ANISOU 1554 O ALA A 225 15442 13722 13412 -2644 662 -244 O
ATOM 1555 CB ALA A 225 -4.702 147.461 175.103 1.00106.73 C
ANISOU 1555 CB ALA A 225 14903 12815 12834 -2462 635 -349 C
ATOM 1556 N SER A 226 -4.931 148.152 172.061 1.00106.10 N
ANISOU 1556 N SER A 226 14753 12862 12697 -2726 578 -321 N
ATOM 1557 CA SER A 226 -4.788 149.117 170.951 1.00105.39 C
ANISOU 1557 CA SER A 226 14620 12836 12586 -2850 468 -265 C
ATOM 1558 C SER A 226 -5.987 150.104 170.929 1.00106.98 C
ANISOU 1558 C SER A 226 14863 12984 12799 -2867 331 -289 C
ATOM 1559 O SER A 226 -6.812 150.073 171.849 1.00106.23 O
ANISOU 1559 O SER A 226 14806 12838 12719 -2764 317 -342 O
ATOM 1560 CB SER A 226 -4.611 148.402 169.610 1.00108.76 C
ANISOU 1560 CB SER A 226 15010 13356 12957 -2921 583 -282 C
ATOM 1561 OG SER A 226 -4.284 149.308 168.566 1.00115.69 O
ANISOU 1561 OG SER A 226 15829 14327 13802 -3049 484 -209 O
ATOM 1562 N ASN A1001 -6.066 150.990 169.915 1.00102.46 N
ANISOU 1562 N ASN A1001 14283 12445 12202 -2977 223 -248 N
ATOM 1563 CA ASN A1001 -7.145 151.977 169.803 1.00102.08 C
ANISOU 1563 CA ASN A1001 14290 12353 12141 -2960 79 -275 C
ATOM 1564 C ASN A1001 -7.508 152.294 168.344 1.00104.73 C
ANISOU 1564 C ASN A1001 14602 12753 12436 -3086 50 -254 C
ATOM 1565 O ASN A1001 -6.798 151.864 167.433 1.00103.86 O
ANISOU 1565 O ASN A1001 14428 12728 12307 -3197 129 -210 O
ATOM 1566 CB ASN A1001 -6.785 153.259 170.577 1.00104.63 C
ANISOU 1566 CB ASN A1001 14712 12567 12476 -2903 -148 -228 C
ATOM 1567 CG ASN A1001 -5.547 153.972 170.074 1.00129.35 C
ANISOU 1567 CG ASN A1001 17854 15690 15605 -3048 -272 -98 C
ATOM 1568 OD1 ASN A1001 -5.504 154.514 168.960 1.00122.08 O
ANISOU 1568 OD1 ASN A1001 16932 14804 14649 -3197 -359 -24 O
ATOM 1569 ND2 ASN A1001 -4.518 154.005 170.900 1.00123.30 N
ANISOU 1569 ND2 ASN A1001 17087 14900 14861 -3022 -288 -56 N
ATOM 1570 N ILE A1002 -8.592 153.084 168.143 1.00101.01 N
ANISOU 1570 N ILE A1002 14182 12263 11935 -3047 -72 -287 N
ATOM 1571 CA ILE A1002 -9.120 153.507 166.839 1.00101.15 C
ANISOU 1571 CA ILE A1002 14191 12336 11906 -3144 -125 -273 C
ATOM 1572 C ILE A1002 -8.112 154.310 166.017 1.00106.88 C
ANISOU 1572 C ILE A1002 14935 13054 12622 -3303 -250 -144 C
ATOM 1573 O ILE A1002 -8.045 154.112 164.804 1.00106.74 O
ANISOU 1573 O ILE A1002 14851 13138 12569 -3427 -197 -115 O
ATOM 1574 CB ILE A1002 -10.496 154.240 166.947 1.00104.41 C
ANISOU 1574 CB ILE A1002 14664 12741 12266 -3017 -254 -336 C
ATOM 1575 CG1 ILE A1002 -11.109 154.560 165.564 1.00105.06 C
ANISOU 1575 CG1 ILE A1002 14726 12902 12291 -3106 -286 -329 C
ATOM 1576 CG2 ILE A1002 -10.459 155.486 167.832 1.00105.53 C
ANISOU 1576 CG2 ILE A1002 14957 12738 12401 -2885 -495 -317 C
ATOM 1577 CD1 ILE A1002 -11.512 153.346 164.752 1.00111.84 C
ANISOU 1577 CD1 ILE A1002 15461 13908 13126 -3186 -73 -389 C
ATOM 1578 N PHE A1003 -7.334 155.198 166.661 1.00105.12 N
ANISOU 1578 N PHE A1003 14798 12728 12414 -3318 -423 -59 N
ATOM 1579 CA PHE A1003 -6.344 156.030 165.967 1.00106.27 C
ANISOU 1579 CA PHE A1003 14967 12882 12530 -3515 -578 96 C
ATOM 1580 C PHE A1003 -5.182 155.196 165.445 1.00109.74 C
ANISOU 1580 C PHE A1003 15237 13508 12950 -3640 -414 166 C
ATOM 1581 O PHE A1003 -4.651 155.494 164.372 1.00109.17 O
ANISOU 1581 O PHE A1003 15099 13562 12818 -3812 -444 269 O
ATOM 1582 CB PHE A1003 -5.871 157.184 166.850 1.00109.09 C
ANISOU 1582 CB PHE A1003 15490 13066 12892 -3514 -832 167 C
ATOM 1583 CG PHE A1003 -6.998 158.035 167.382 1.00111.35 C
ANISOU 1583 CG PHE A1003 15968 13175 13166 -3332 -1017 81 C
ATOM 1584 CD1 PHE A1003 -7.626 158.976 166.569 1.00115.80 C
ANISOU 1584 CD1 PHE A1003 16660 13668 13671 -3361 -1203 105 C
ATOM 1585 CD2 PHE A1003 -7.430 157.902 168.697 1.00113.45 C
ANISOU 1585 CD2 PHE A1003 16288 13361 13457 -3108 -1013 -24 C
ATOM 1586 CE1 PHE A1003 -8.664 159.773 167.066 1.00117.70 C
ANISOU 1586 CE1 PHE A1003 17089 13764 13869 -3138 -1386 14 C
ATOM 1587 CE2 PHE A1003 -8.466 158.701 169.195 1.00117.33 C
ANISOU 1587 CE2 PHE A1003 16947 13732 13901 -2893 -1190 -112 C
ATOM 1588 CZ PHE A1003 -9.081 159.628 168.375 1.00116.73 C
ANISOU 1588 CZ PHE A1003 17005 13590 13757 -2894 -1377 -99 C
ATOM 1589 N GLU A1004 -4.832 154.116 166.184 1.00105.89 N
ANISOU 1589 N GLU A1004 14680 13058 12496 -3531 -239 107 N
ATOM 1590 CA GLU A1004 -3.799 153.162 165.797 1.00105.91 C
ANISOU 1590 CA GLU A1004 14534 13248 12458 -3565 -68 140 C
ATOM 1591 C GLU A1004 -4.335 152.371 164.592 1.00110.27 C
ANISOU 1591 C GLU A1004 15017 13911 12968 -3574 92 70 C
ATOM 1592 O GLU A1004 -3.668 152.327 163.558 1.00111.24 O
ANISOU 1592 O GLU A1004 15030 14224 13011 -3671 132 140 O
ATOM 1593 CB GLU A1004 -3.440 152.233 166.976 1.00106.49 C
ANISOU 1593 CB GLU A1004 14599 13291 12572 -3404 64 73 C
ATOM 1594 N MET A1005 -5.580 151.840 164.712 1.00105.70 N
ANISOU 1594 N MET A1005 14499 13237 12425 -3484 165 -61 N
ATOM 1595 CA MET A1005 -6.331 151.053 163.717 1.00105.23 C
ANISOU 1595 CA MET A1005 14411 13242 12329 -3496 299 -148 C
ATOM 1596 C MET A1005 -6.466 151.795 162.388 1.00108.06 C
ANISOU 1596 C MET A1005 14728 13699 12629 -3641 212 -79 C
ATOM 1597 O MET A1005 -6.121 151.243 161.338 1.00108.04 O
ANISOU 1597 O MET A1005 14644 13848 12560 -3693 311 -77 O
ATOM 1598 CB MET A1005 -7.732 150.712 164.271 1.00107.20 C
ANISOU 1598 CB MET A1005 14730 13387 12614 -3411 332 -264 C
ATOM 1599 CG MET A1005 -8.416 149.554 163.575 1.00111.28 C
ANISOU 1599 CG MET A1005 15237 13951 13093 -3428 492 -364 C
ATOM 1600 SD MET A1005 -10.201 149.608 163.848 1.00115.80 S
ANISOU 1600 SD MET A1005 15840 14495 13662 -3398 477 -449 S
ATOM 1601 CE MET A1005 -10.635 147.911 163.636 1.00112.50 C
ANISOU 1601 CE MET A1005 15448 14096 13199 -3454 671 -546 C
ATOM 1602 N LEU A1006 -6.970 153.045 162.439 1.00103.41 N
ANISOU 1602 N LEU A1006 14213 13025 12054 -3687 17 -27 N
ATOM 1603 CA LEU A1006 -7.150 153.882 161.258 1.00103.24 C
ANISOU 1603 CA LEU A1006 14183 13068 11976 -3827 -100 53 C
ATOM 1604 C LEU A1006 -5.811 154.292 160.640 1.00111.06 C
ANISOU 1604 C LEU A1006 15090 14203 12903 -3997 -165 219 C
ATOM 1605 O LEU A1006 -5.751 154.474 159.422 1.00112.07 O
ANISOU 1605 O LEU A1006 15153 14469 12959 -4123 -177 280 O
ATOM 1606 CB LEU A1006 -8.011 155.116 161.551 1.00102.55 C
ANISOU 1606 CB LEU A1006 14237 12827 11899 -3798 -317 63 C
ATOM 1607 CG LEU A1006 -9.492 154.914 161.820 1.00105.12 C
ANISOU 1607 CG LEU A1006 14601 13104 12234 -3642 -277 -80 C
ATOM 1608 CD1 LEU A1006 -10.133 156.221 162.154 1.00105.14 C
ANISOU 1608 CD1 LEU A1006 14757 12973 12219 -3558 -519 -66 C
ATOM 1609 CD2 LEU A1006 -10.217 154.273 160.634 1.00107.03 C
ANISOU 1609 CD2 LEU A1006 14753 13485 12427 -3692 -143 -145 C
ATOM 1610 N ARG A1007 -4.735 154.427 161.461 1.00108.73 N
ANISOU 1610 N ARG A1007 14783 13912 12619 -4010 -207 300 N
ATOM 1611 CA ARG A1007 -3.406 154.756 160.936 1.00109.89 C
ANISOU 1611 CA ARG A1007 14810 14267 12676 -4185 -260 474 C
ATOM 1612 C ARG A1007 -2.889 153.594 160.061 1.00113.31 C
ANISOU 1612 C ARG A1007 15058 14973 13020 -4145 -34 436 C
ATOM 1613 O ARG A1007 -2.330 153.855 158.990 1.00114.18 O
ANISOU 1613 O ARG A1007 15037 15331 13015 -4294 -58 563 O
ATOM 1614 CB ARG A1007 -2.414 155.139 162.052 1.00111.26 C
ANISOU 1614 CB ARG A1007 15006 14399 12868 -4208 -362 565 C
ATOM 1615 CG ARG A1007 -1.735 156.501 161.804 1.00128.25 C
ANISOU 1615 CG ARG A1007 17227 16534 14967 -4462 -646 773 C
ATOM 1616 CD ARG A1007 -0.794 156.948 162.921 1.00142.01 C
ANISOU 1616 CD ARG A1007 19009 18230 16719 -4511 -769 866 C
ATOM 1617 NE ARG A1007 -1.509 157.523 164.065 1.00152.25 N
ANISOU 1617 NE ARG A1007 20535 19194 18120 -4371 -899 771 N
ATOM 1618 CZ ARG A1007 -1.704 156.903 165.227 1.00167.53 C
ANISOU 1618 CZ ARG A1007 22482 21038 20133 -4153 -781 639 C
ATOM 1619 NH1 ARG A1007 -1.222 155.682 165.428 1.00152.30 N
ANISOU 1619 NH1 ARG A1007 20379 19290 18197 -4048 -538 587 N
ATOM 1620 NH2 ARG A1007 -2.375 157.503 166.201 1.00157.53 N
ANISOU 1620 NH2 ARG A1007 21414 19506 18934 -4022 -914 560 N
ATOM 1621 N ILE A1008 -3.170 152.324 160.473 1.00107.85 N
ANISOU 1621 N ILE A1008 14377 14236 12366 -3944 170 262 N
ATOM 1622 CA ILE A1008 -2.797 151.093 159.758 1.00107.67 C
ANISOU 1622 CA ILE A1008 14251 14405 12252 -3845 373 183 C
ATOM 1623 C ILE A1008 -3.630 150.891 158.478 1.00113.24 C
ANISOU 1623 C ILE A1008 14957 15152 12917 -3889 418 116 C
ATOM 1624 O ILE A1008 -3.055 150.686 157.401 1.00113.91 O
ANISOU 1624 O ILE A1008 14917 15486 12878 -3938 461 163 O
ATOM 1625 CB ILE A1008 -2.850 149.832 160.674 1.00109.42 C
ANISOU 1625 CB ILE A1008 14540 14518 12515 -3627 536 34 C
ATOM 1626 CG1 ILE A1008 -1.911 149.972 161.890 1.00109.61 C
ANISOU 1626 CG1 ILE A1008 14542 14544 12561 -3569 506 102 C
ATOM 1627 CG2 ILE A1008 -2.535 148.553 159.873 1.00110.48 C
ANISOU 1627 CG2 ILE A1008 14637 14803 12536 -3502 713 -68 C
ATOM 1628 CD1 ILE A1008 -2.048 148.873 162.980 1.00113.91 C
ANISOU 1628 CD1 ILE A1008 15180 14945 13155 -3359 641 -31 C
ATOM 1629 N ASP A1009 -4.979 150.912 158.607 1.00109.63 N
ANISOU 1629 N ASP A1009 14624 14486 12546 -3864 414 7 N
ATOM 1630 CA ASP A1009 -5.912 150.687 157.496 1.00109.62 C
ANISOU 1630 CA ASP A1009 14630 14511 12509 -3907 453 -66 C
ATOM 1631 C ASP A1009 -5.975 151.836 156.467 1.00115.04 C
ANISOU 1631 C ASP A1009 15260 15308 13142 -4081 309 64 C
ATOM 1632 O ASP A1009 -6.352 151.585 155.318 1.00115.02 O
ANISOU 1632 O ASP A1009 15207 15430 13066 -4126 362 33 O
ATOM 1633 CB ASP A1009 -7.311 150.331 158.023 1.00110.12 C
ANISOU 1633 CB ASP A1009 14810 14377 12652 -3846 478 -196 C
ATOM 1634 CG ASP A1009 -7.417 148.923 158.584 1.00117.44 C
ANISOU 1634 CG ASP A1009 15801 15235 13585 -3726 645 -333 C
ATOM 1635 OD1 ASP A1009 -6.516 148.099 158.308 1.00118.40 O
ANISOU 1635 OD1 ASP A1009 15897 15452 13638 -3660 749 -357 O
ATOM 1636 OD2 ASP A1009 -8.419 148.632 159.256 1.00121.49 O
ANISOU 1636 OD2 ASP A1009 16394 15613 14152 -3696 663 -414 O
ATOM 1637 N GLU A1010 -5.593 153.076 156.874 1.00112.38 N
ANISOU 1637 N GLU A1010 14950 14920 12831 -4185 116 212 N
ATOM 1638 CA GLU A1010 -5.542 154.277 156.026 1.00139.50 C
ANISOU 1638 CA GLU A1010 18371 18425 16207 -4377 -64 370 C
ATOM 1639 C GLU A1010 -4.211 154.991 156.209 1.00157.26 C
ANISOU 1639 C GLU A1010 20554 20799 18400 -4526 -184 568 C
ATOM 1640 O GLU A1010 -3.772 155.697 155.308 1.00121.96 O
ANISOU 1640 O GLU A1010 16018 16487 13833 -4723 -297 730 O
ATOM 1641 CB GLU A1010 -6.701 155.241 156.335 1.00140.53 C
ANISOU 1641 CB GLU A1010 18673 18320 16403 -4376 -244 360 C
ATOM 1642 CG GLU A1010 -7.988 154.904 155.602 1.00150.07 C
ANISOU 1642 CG GLU A1010 19894 19517 17607 -4311 -168 227 C
ATOM 1643 CD GLU A1010 -9.119 155.908 155.727 1.00168.44 C
ANISOU 1643 CD GLU A1010 22361 21685 19952 -4282 -349 222 C
ATOM 1644 OE1 GLU A1010 -10.291 155.468 155.714 1.00158.05 O
ANISOU 1644 OE1 GLU A1010 21045 20375 18633 -4194 -274 95 O
ATOM 1645 OE2 GLU A1010 -8.845 157.129 155.799 1.00164.01 O
ANISOU 1645 OE2 GLU A1010 21921 21006 19389 -4348 -579 346 O
ATOM 1646 N ASP A1017 6.751 164.254 150.314 1.00171.97 N
ANISOU 1646 N ASP A1017 21227 25809 18304 -8748 -2328 4019 N
ATOM 1647 CA ASP A1017 6.208 162.957 149.914 1.00169.48 C
ANISOU 1647 CA ASP A1017 20725 25598 18072 -8230 -1935 3681 C
ATOM 1648 C ASP A1017 4.659 162.943 149.821 1.00171.56 C
ANISOU 1648 C ASP A1017 21330 25273 18583 -7936 -1907 3399 C
ATOM 1649 O ASP A1017 4.114 162.661 148.751 1.00170.59 O
ANISOU 1649 O ASP A1017 21126 25264 18426 -7846 -1790 3331 O
ATOM 1650 CB ASP A1017 6.672 161.875 150.891 1.00 20.00 C
ATOM 1651 N GLU A1018 3.971 163.241 150.952 1.00167.29 N
ANISOU 1651 N GLU A1018 21150 24142 18269 -7785 -2017 3239 N
ATOM 1652 CA GLU A1018 2.513 163.333 151.165 1.00164.91 C
ANISOU 1652 CA GLU A1018 21188 23277 18193 -7499 -2026 2979 C
ATOM 1653 C GLU A1018 2.264 163.866 152.596 1.00169.28 C
ANISOU 1653 C GLU A1018 22099 23310 18908 -7451 -2233 2918 C
ATOM 1654 O GLU A1018 3.067 163.593 153.496 1.00169.20 O
ANISOU 1654 O GLU A1018 22011 23393 18885 -7490 -2231 2966 O
ATOM 1655 CB GLU A1018 1.837 161.976 150.963 1.00 20.00 C
ATOM 1656 N ALA A1019 1.167 164.627 152.805 1.00165.76 N
ANISOU 1656 N ALA A1019 22042 22345 18595 -7348 -2416 2813 N
ATOM 1657 CA ALA A1019 0.825 165.220 154.113 1.00165.36 C
ANISOU 1657 CA ALA A1019 22363 21789 18677 -7255 -2634 2734 C
ATOM 1658 C ALA A1019 0.349 164.199 155.175 1.00166.43 C
ANISOU 1658 C ALA A1019 22456 21792 18986 -6806 -2365 2414 C
ATOM 1659 O ALA A1019 0.188 163.015 154.865 1.00164.49 O
ANISOU 1659 O ALA A1019 21945 21783 18770 -6565 -2027 2242 O
ATOM 1660 CB ALA A1019 -0.202 166.332 153.934 1.00166.81 C
ANISOU 1660 CB ALA A1019 22968 21514 18897 -7258 -2930 2729 C
ATOM 1661 N GLU A1020 0.147 164.660 156.430 1.00162.47 N
ANISOU 1661 N GLU A1020 22230 20915 18586 -6705 -2528 2343 N
ATOM 1662 CA GLU A1020 -0.295 163.824 157.552 1.00159.77 C
ANISOU 1662 CA GLU A1020 21873 20437 18397 -6315 -2314 2071 C
ATOM 1663 C GLU A1020 -1.817 163.699 157.623 1.00162.71 C
ANISOU 1663 C GLU A1020 22404 20525 18894 -5945 -2230 1801 C
ATOM 1664 O GLU A1020 -2.526 164.570 157.119 1.00163.39 O
ANISOU 1664 O GLU A1020 22666 20460 18953 -5971 -2381 1818 O
ATOM 1665 CB GLU A1020 0.240 164.387 158.870 1.00 20.00 C
ATOM 1666 N LYS A1021 -2.313 162.610 158.256 1.00157.40 N
ANISOU 1666 N LYS A1021 21656 19808 18339 -5608 -1989 1562 N
ATOM 1667 CA LYS A1021 -3.736 162.308 158.463 1.00155.25 C
ANISOU 1667 CA LYS A1021 21477 19341 18171 -5254 -1873 1303 C
ATOM 1668 C LYS A1021 -4.327 163.174 159.596 1.00159.94 C
ANISOU 1668 C LYS A1021 22442 19523 18806 -5111 -2157 1241 C
ATOM 1669 O LYS A1021 -3.594 163.618 160.486 1.00161.32 O
ANISOU 1669 O LYS A1021 22798 19531 18967 -5227 -2390 1346 O
ATOM 1670 CB LYS A1021 -3.915 160.820 158.780 1.00155.37 C
ANISOU 1670 CB LYS A1021 21278 19486 18270 -5005 -1537 1113 C
ATOM 1671 N LEU A1022 -5.649 163.413 159.559 1.00155.04 N
ANISOU 1671 N LEU A1022 21933 18761 18213 -4848 -2145 1068 N
ATOM 1672 CA LEU A1022 -6.336 164.244 160.552 1.00155.13 C
ANISOU 1672 CA LEU A1022 22292 18424 18227 -4634 -2409 979 C
ATOM 1673 C LEU A1022 -7.519 163.505 161.200 1.00154.89 C
ANISOU 1673 C LEU A1022 22211 18372 18270 -4238 -2215 719 C
ATOM 1674 O LEU A1022 -8.657 163.987 161.158 1.00155.32 O
ANISOU 1674 O LEU A1022 22467 18255 18293 -3987 -2356 604 O
ATOM 1675 CB LEU A1022 -6.784 165.567 159.898 1.00156.88 C
ANISOU 1675 CB LEU A1022 22730 18517 18361 -4667 -2642 1035 C
ATOM 1676 N PHE A1023 -7.239 162.337 161.812 1.00147.23 N
ANISOU 1676 N PHE A1023 20977 17588 17374 -4179 -1909 636 N
ATOM 1677 CA PHE A1023 -8.248 161.483 162.447 1.00144.12 C
ANISOU 1677 CA PHE A1023 20487 17233 17038 -3871 -1691 420 C
ATOM 1678 C PHE A1023 -8.868 162.074 163.699 1.00146.74 C
ANISOU 1678 C PHE A1023 21043 17343 17370 -3594 -1861 307 C
ATOM 1679 O PHE A1023 -10.084 162.016 163.849 1.00145.76 O
ANISOU 1679 O PHE A1023 20929 17236 17218 -3337 -1822 158 O
ATOM 1680 CB PHE A1023 -7.686 160.088 162.752 1.00144.01 C
ANISOU 1680 CB PHE A1023 20217 17408 17093 -3896 -1391 388 C
ATOM 1681 CG PHE A1023 -7.101 159.340 161.581 1.00144.71 C
ANISOU 1681 CG PHE A1023 20070 17752 17161 -4082 -1186 451 C
ATOM 1682 CD1 PHE A1023 -7.807 159.217 160.389 1.00147.60 C
ANISOU 1682 CD1 PHE A1023 20377 18220 17484 -4105 -1127 424 C
ATOM 1683 CD2 PHE A1023 -5.874 158.701 161.691 1.00146.28 C
ANISOU 1683 CD2 PHE A1023 20101 18112 17366 -4205 -1050 527 C
ATOM 1684 CE1 PHE A1023 -7.275 158.504 159.314 1.00148.31 C
ANISOU 1684 CE1 PHE A1023 20261 18552 17539 -4253 -946 470 C
ATOM 1685 CE2 PHE A1023 -5.348 157.977 160.620 1.00149.04 C
ANISOU 1685 CE2 PHE A1023 20239 18723 17668 -4325 -867 567 C
ATOM 1686 CZ PHE A1023 -6.050 157.885 159.437 1.00147.20 C
ANISOU 1686 CZ PHE A1023 19965 18572 17394 -4350 -819 537 C
ATOM 1687 N ASN A1024 -8.032 162.638 164.592 1.00143.50 N
ANISOU 1687 N ASN A1024 20797 16756 16971 -3642 -2050 378 N
ATOM 1688 CA ASN A1024 -8.396 163.264 165.876 1.00143.48 C
ANISOU 1688 CA ASN A1024 21031 16529 16955 -3382 -2240 278 C
ATOM 1689 C ASN A1024 -9.778 163.963 165.860 1.00145.57 C
ANISOU 1689 C ASN A1024 21478 16698 17134 -3065 -2384 139 C
ATOM 1690 O ASN A1024 -10.609 163.680 166.724 1.00144.34 O
ANISOU 1690 O ASN A1024 21259 16613 16970 -2759 -2272 -29 O
ATOM 1691 CB ASN A1024 -7.284 164.229 166.352 1.00147.43 C
ANISOU 1691 CB ASN A1024 21789 16795 17433 -3572 -2555 428 C
ATOM 1692 CG ASN A1024 -5.892 163.898 165.843 1.00174.47 C
ANISOU 1692 CG ASN A1024 25037 20370 20885 -3953 -2478 624 C
ATOM 1693 OD1 ASN A1024 -5.458 164.372 164.782 1.00170.67 O
ANISOU 1693 OD1 ASN A1024 24572 19925 20348 -4249 -2591 800 O
ATOM 1694 ND2 ASN A1024 -5.172 163.060 166.575 1.00165.41 N
ANISOU 1694 ND2 ASN A1024 23698 19349 19803 -3944 -2280 603 N
ATOM 1695 N GLN A1025 -10.028 164.822 164.841 1.00141.49 N
ANISOU 1695 N GLN A1025 21163 16060 16535 -3140 -2620 216 N
ATOM 1696 CA GLN A1025 -11.271 165.577 164.642 1.00141.02 C
ANISOU 1696 CA GLN A1025 21300 15917 16363 -2835 -2793 103 C
ATOM 1697 C GLN A1025 -12.364 164.753 163.958 1.00139.59 C
ANISOU 1697 C GLN A1025 20843 16030 16164 -2719 -2522 -3 C
ATOM 1698 O GLN A1025 -13.527 164.834 164.357 1.00138.91 O
ANISOU 1698 O GLN A1025 20783 16006 15990 -2373 -2538 -157 O
ATOM 1699 CB GLN A1025 -10.993 166.862 163.843 1.00144.80 C
ANISOU 1699 CB GLN A1025 22136 16128 16754 -2981 -3173 244 C
ATOM 1700 N ASP A1026 -11.985 163.974 162.929 1.00132.82 N
ANISOU 1700 N ASP A1026 19724 15372 15369 -3003 -2287 83 N
ATOM 1701 CA ASP A1026 -12.883 163.135 162.133 1.00130.58 C
ANISOU 1701 CA ASP A1026 19183 15361 15070 -2968 -2034 4 C
ATOM 1702 C ASP A1026 -13.502 161.979 162.907 1.00129.34 C
ANISOU 1702 C ASP A1026 18784 15412 14947 -2790 -1747 -150 C
ATOM 1703 O ASP A1026 -14.633 161.610 162.613 1.00128.63 O
ANISOU 1703 O ASP A1026 18566 15516 14792 -2646 -1632 -253 O
ATOM 1704 CB ASP A1026 -12.183 162.629 160.858 1.00132.17 C
ANISOU 1704 CB ASP A1026 19208 15699 15312 -3319 -1893 140 C
ATOM 1705 CG ASP A1026 -11.852 163.706 159.826 1.00147.42 C
ANISOU 1705 CG ASP A1026 21327 17511 17175 -3509 -2148 298 C
ATOM 1706 OD1 ASP A1026 -11.514 163.342 158.675 1.00147.48 O
ANISOU 1706 OD1 ASP A1026 21169 17686 17179 -3739 -2028 386 O
ATOM 1707 OD2 ASP A1026 -11.909 164.915 160.178 1.00156.68 O
ANISOU 1707 OD2 ASP A1026 22830 18416 18286 -3431 -2481 339 O
ATOM 1708 N VAL A1027 -12.774 161.418 163.888 1.00122.34 N
ANISOU 1708 N VAL A1027 17835 14500 14147 -2818 -1641 -154 N
ATOM 1709 CA VAL A1027 -13.210 160.304 164.738 1.00119.26 C
ANISOU 1709 CA VAL A1027 17243 14278 13791 -2684 -1387 -275 C
ATOM 1710 C VAL A1027 -14.363 160.752 165.638 1.00123.07 C
ANISOU 1710 C VAL A1027 17806 14785 14171 -2321 -1492 -411 C
ATOM 1711 O VAL A1027 -15.356 160.033 165.765 1.00122.02 O
ANISOU 1711 O VAL A1027 17487 14890 13986 -2197 -1316 -511 O
ATOM 1712 CB VAL A1027 -12.012 159.679 165.512 1.00120.91 C
ANISOU 1712 CB VAL A1027 17389 14440 14111 -2809 -1271 -227 C
ATOM 1713 CG1 VAL A1027 -12.464 158.789 166.667 1.00119.31 C
ANISOU 1713 CG1 VAL A1027 17044 14359 13928 -2644 -1068 -344 C
ATOM 1714 CG2 VAL A1027 -11.115 158.898 164.564 1.00119.80 C
ANISOU 1714 CG2 VAL A1027 17099 14388 14031 -3109 -1109 -121 C
ATOM 1715 N ASP A1028 -14.254 161.961 166.209 1.00120.76 N
ANISOU 1715 N ASP A1028 17799 14263 13823 -2153 -1795 -411 N
ATOM 1716 CA ASP A1028 -15.290 162.529 167.069 1.00121.65 C
ANISOU 1716 CA ASP A1028 18022 14397 13802 -1751 -1938 -548 C
ATOM 1717 C ASP A1028 -16.494 162.972 166.237 1.00122.56 C
ANISOU 1717 C ASP A1028 18147 14651 13770 -1573 -2011 -608 C
ATOM 1718 O ASP A1028 -17.629 162.900 166.710 1.00122.49 O
ANISOU 1718 O ASP A1028 18064 14850 13625 -1249 -1996 -736 O
ATOM 1719 CB ASP A1028 -14.719 163.662 167.941 1.00126.18 C
ANISOU 1719 CB ASP A1028 18939 14649 14353 -1618 -2260 -539 C
ATOM 1720 CG ASP A1028 -13.738 163.175 169.009 1.00146.49 C
ANISOU 1720 CG ASP A1028 21473 17145 17040 -1714 -2177 -511 C
ATOM 1721 OD1 ASP A1028 -12.654 162.659 168.638 1.00147.29 O
ANISOU 1721 OD1 ASP A1028 21459 17236 17270 -2053 -2039 -391 O
ATOM 1722 OD2 ASP A1028 -14.047 163.324 170.216 1.00157.56 O
ANISOU 1722 OD2 ASP A1028 22964 18513 18388 -1433 -2262 -611 O
ATOM 1723 N ALA A1029 -16.241 163.362 164.977 1.00116.72 N
ANISOU 1723 N ALA A1029 17465 13839 13043 -1792 -2076 -507 N
ATOM 1724 CA ALA A1029 -17.262 163.762 164.014 1.00116.62 C
ANISOU 1724 CA ALA A1029 17455 13952 12902 -1676 -2139 -539 C
ATOM 1725 C ALA A1029 -17.997 162.536 163.439 1.00116.92 C
ANISOU 1725 C ALA A1029 17123 14364 12939 -1765 -1807 -585 C
ATOM 1726 O ALA A1029 -19.165 162.647 163.046 1.00117.19 O
ANISOU 1726 O ALA A1029 17075 14622 12829 -1571 -1805 -662 O
ATOM 1727 CB ALA A1029 -16.624 164.561 162.893 1.00118.19 C
ANISOU 1727 CB ALA A1029 17857 13928 13120 -1917 -2333 -394 C
ATOM 1728 N ALA A1030 -17.304 161.375 163.380 1.00109.68 N
ANISOU 1728 N ALA A1030 15996 13512 12164 -2058 -1543 -535 N
ATOM 1729 CA ALA A1030 -17.851 160.103 162.897 1.00107.25 C
ANISOU 1729 CA ALA A1030 15383 13502 11865 -2188 -1240 -572 C
ATOM 1730 C ALA A1030 -18.825 159.560 163.930 1.00109.43 C
ANISOU 1730 C ALA A1030 15509 14020 12050 -1951 -1135 -690 C
ATOM 1731 O ALA A1030 -19.896 159.070 163.562 1.00108.74 O
ANISOU 1731 O ALA A1030 15234 14230 11851 -1905 -1023 -746 O
ATOM 1732 CB ALA A1030 -16.731 159.099 162.672 1.00106.25 C
ANISOU 1732 CB ALA A1030 15148 13325 11896 -2507 -1036 -497 C
ATOM 1733 N VAL A1031 -18.441 159.668 165.233 1.00104.71 N
ANISOU 1733 N VAL A1031 14987 13315 11483 -1809 -1181 -718 N
ATOM 1734 CA VAL A1031 -19.223 159.241 166.393 1.00103.70 C
ANISOU 1734 CA VAL A1031 14730 13412 11260 -1574 -1105 -815 C
ATOM 1735 C VAL A1031 -20.506 160.068 166.462 1.00110.53 C
ANISOU 1735 C VAL A1031 15615 14480 11901 -1206 -1266 -908 C
ATOM 1736 O VAL A1031 -21.584 159.483 166.549 1.00110.39 O
ANISOU 1736 O VAL A1031 15358 14837 11749 -1111 -1131 -966 O
ATOM 1737 CB VAL A1031 -18.392 159.245 167.705 1.00105.81 C
ANISOU 1737 CB VAL A1031 15102 13489 11612 -1504 -1144 -816 C
ATOM 1738 CG1 VAL A1031 -19.260 158.951 168.925 1.00105.89 C
ANISOU 1738 CG1 VAL A1031 14971 13762 11499 -1243 -1078 -910 C
ATOM 1739 CG2 VAL A1031 -17.244 158.242 167.624 1.00103.47 C
ANISOU 1739 CG2 VAL A1031 14746 13060 11507 -1840 -961 -729 C
ATOM 1740 N ARG A1032 -20.395 161.410 166.317 1.00110.38 N
ANISOU 1740 N ARG A1032 15884 14231 11823 -1012 -1561 -913 N
ATOM 1741 CA ARG A1032 -21.535 162.343 166.294 1.00113.56 C
ANISOU 1741 CA ARG A1032 16362 14794 11993 -612 -1755 -1008 C
ATOM 1742 C ARG A1032 -22.551 161.988 165.182 1.00119.57 C
ANISOU 1742 C ARG A1032 16899 15883 12651 -680 -1631 -1011 C
ATOM 1743 O ARG A1032 -23.763 162.065 165.413 1.00121.43 O
ANISOU 1743 O ARG A1032 16992 16479 12666 -383 -1638 -1100 O
ATOM 1744 CB ARG A1032 -21.059 163.801 166.115 1.00115.86 C
ANISOU 1744 CB ARG A1032 17074 14694 12255 -446 -2121 -995 C
ATOM 1745 CG ARG A1032 -20.784 164.552 167.415 1.00128.05 C
ANISOU 1745 CG ARG A1032 18871 16028 13753 -144 -2339 -1064 C
ATOM 1746 CD ARG A1032 -20.534 166.040 167.177 1.00139.29 C
ANISOU 1746 CD ARG A1032 20761 17057 15107 35 -2744 -1058 C
ATOM 1747 NE ARG A1032 -19.155 166.329 166.761 1.00141.50 N
ANISOU 1747 NE ARG A1032 21260 16921 15582 -358 -2846 -905 N
ATOM 1748 CZ ARG A1032 -18.813 166.973 165.646 1.00148.03 C
ANISOU 1748 CZ ARG A1032 22294 17517 16435 -566 -3016 -790 C
ATOM 1749 NH1 ARG A1032 -19.748 167.413 164.808 1.00131.43 N
ANISOU 1749 NH1 ARG A1032 20233 15518 14187 -402 -3108 -821 N
ATOM 1750 NH2 ARG A1032 -17.535 167.187 165.364 1.00129.82 N
ANISOU 1750 NH2 ARG A1032 20142 14900 14282 -943 -3098 -635 N
ATOM 1751 N GLY A1033 -22.037 161.597 164.010 1.00114.49 N
ANISOU 1751 N GLY A1033 16212 15140 12149 -1062 -1521 -912 N
ATOM 1752 CA GLY A1033 -22.831 161.223 162.847 1.00114.15 C
ANISOU 1752 CA GLY A1033 15974 15363 12036 -1191 -1401 -902 C
ATOM 1753 C GLY A1033 -23.549 159.899 162.990 1.00117.24 C
ANISOU 1753 C GLY A1033 16009 16163 12373 -1300 -1120 -936 C
ATOM 1754 O GLY A1033 -24.679 159.762 162.516 1.00117.20 O
ANISOU 1754 O GLY A1033 15824 16526 12182 -1183 -1087 -981 O
ATOM 1755 N ILE A1034 -22.886 158.905 163.627 1.00113.15 N
ANISOU 1755 N ILE A1034 15398 15591 12004 -1537 -927 -905 N
ATOM 1756 CA ILE A1034 -23.434 157.562 163.871 1.00112.43 C
ANISOU 1756 CA ILE A1034 15019 15826 11875 -1702 -675 -915 C
ATOM 1757 C ILE A1034 -24.644 157.644 164.812 1.00119.45 C
ANISOU 1757 C ILE A1034 15744 17110 12531 -1384 -696 -991 C
ATOM 1758 O ILE A1034 -25.681 157.034 164.531 1.00120.15 O
ANISOU 1758 O ILE A1034 15582 17610 12459 -1432 -587 -1000 O
ATOM 1759 CB ILE A1034 -22.332 156.567 164.352 1.00112.92 C
ANISOU 1759 CB ILE A1034 15083 15681 12139 -1981 -505 -865 C
ATOM 1760 CG1 ILE A1034 -21.597 155.960 163.150 1.00111.30 C
ANISOU 1760 CG1 ILE A1034 14948 15240 12100 -2305 -436 -796 C
ATOM 1761 CG2 ILE A1034 -22.897 155.464 165.247 1.00113.67 C
ANISOU 1761 CG2 ILE A1034 14941 16079 12170 -2108 -296 -874 C
ATOM 1762 CD1 ILE A1034 -20.443 155.025 163.494 1.00114.33 C
ANISOU 1762 CD1 ILE A1034 15357 15424 12659 -2529 -291 -754 C
ATOM 1763 N LEU A1035 -24.521 158.443 165.890 1.00117.24 N
ANISOU 1763 N LEU A1035 15604 16731 12211 -1055 -851 -1041 N
ATOM 1764 CA LEU A1035 -25.578 158.635 166.881 1.00119.49 C
ANISOU 1764 CA LEU A1035 15748 17401 12252 -687 -896 -1121 C
ATOM 1765 C LEU A1035 -26.767 159.472 166.360 1.00129.86 C
ANISOU 1765 C LEU A1035 17012 19029 13298 -352 -1041 -1188 C
ATOM 1766 O LEU A1035 -27.819 159.480 167.000 1.00132.15 O
ANISOU 1766 O LEU A1035 17090 19785 13336 -82 -1032 -1245 O
ATOM 1767 CB LEU A1035 -25.010 159.196 168.190 1.00119.19 C
ANISOU 1767 CB LEU A1035 15903 17140 12242 -414 -1035 -1167 C
ATOM 1768 CG LEU A1035 -24.019 158.272 168.922 1.00121.04 C
ANISOU 1768 CG LEU A1035 16127 17177 12684 -677 -877 -1111 C
ATOM 1769 CD1 LEU A1035 -23.123 159.051 169.863 1.00120.39 C
ANISOU 1769 CD1 LEU A1035 16327 16729 12687 -468 -1064 -1141 C
ATOM 1770 CD2 LEU A1035 -24.731 157.126 169.640 1.00123.31 C
ANISOU 1770 CD2 LEU A1035 16100 17892 12859 -743 -670 -1103 C
ATOM 1771 N ARG A1036 -26.614 160.130 165.184 1.00128.43 N
ANISOU 1771 N ARG A1036 17008 18634 13155 -375 -1170 -1173 N
ATOM 1772 CA ARG A1036 -27.664 160.900 164.498 1.00131.02 C
ANISOU 1772 CA ARG A1036 17316 19220 13244 -86 -1310 -1226 C
ATOM 1773 C ARG A1036 -28.492 159.942 163.620 1.00135.93 C
ANISOU 1773 C ARG A1036 17603 20253 13791 -370 -1097 -1184 C
ATOM 1774 O ARG A1036 -29.703 160.130 163.489 1.00138.55 O
ANISOU 1774 O ARG A1036 17757 21029 13856 -133 -1131 -1231 O
ATOM 1775 CB ARG A1036 -27.055 161.994 163.587 1.00132.23 C
ANISOU 1775 CB ARG A1036 17835 18922 13483 -36 -1551 -1207 C
ATOM 1776 CG ARG A1036 -26.763 163.341 164.241 1.00145.03 C
ANISOU 1776 CG ARG A1036 19822 20264 15017 416 -1877 -1281 C
ATOM 1777 CD ARG A1036 -26.174 164.318 163.227 1.00155.89 C
ANISOU 1777 CD ARG A1036 21559 21209 16462 386 -2121 -1230 C
ATOM 1778 NE ARG A1036 -25.567 165.492 163.865 1.00167.54 N
ANISOU 1778 NE ARG A1036 23469 22246 17943 649 -2438 -1261 N
ATOM 1779 CZ ARG A1036 -24.257 165.676 164.028 1.00177.98 C
ANISOU 1779 CZ ARG A1036 25051 23079 19493 376 -2524 -1168 C
ATOM 1780 NH1 ARG A1036 -23.391 164.770 163.589 1.00161.89 N
ANISOU 1780 NH1 ARG A1036 22873 20946 17692 -131 -2307 -1046 N
ATOM 1781 NH2 ARG A1036 -23.804 166.773 164.622 1.00162.60 N
ANISOU 1781 NH2 ARG A1036 23511 20751 17518 615 -2839 -1197 N
ATOM 1782 N ASN A1037 -27.819 158.947 162.986 1.00129.86 N
ANISOU 1782 N ASN A1037 16769 19329 13241 -866 -895 -1098 N
ATOM 1783 CA ASN A1037 -28.406 157.950 162.079 1.00128.92 C
ANISOU 1783 CA ASN A1037 16390 19506 13088 -1209 -700 -1053 C
ATOM 1784 C ASN A1037 -29.238 156.918 162.841 1.00132.17 C
ANISOU 1784 C ASN A1037 16475 20402 13343 -1291 -527 -1047 C
ATOM 1785 O ASN A1037 -28.744 156.308 163.790 1.00131.35 O
ANISOU 1785 O ASN A1037 16366 20220 13321 -1354 -450 -1033 O
ATOM 1786 CB ASN A1037 -27.302 157.254 161.276 1.00126.73 C
ANISOU 1786 CB ASN A1037 16216 18847 13089 -1660 -575 -978 C
ATOM 1787 CG ASN A1037 -27.759 156.607 159.994 1.00144.96 C
ANISOU 1787 CG ASN A1037 18384 21319 15374 -1959 -462 -945 C
ATOM 1788 OD1 ASN A1037 -28.769 155.898 159.939 1.00141.54 O
ANISOU 1788 OD1 ASN A1037 17688 21301 14788 -2089 -335 -943 O
ATOM 1789 ND2 ASN A1037 -26.986 156.796 158.938 1.00133.60 N
ANISOU 1789 ND2 ASN A1037 17116 19566 14080 -2102 -507 -908 N
ATOM 1790 N ALA A1038 -30.493 156.715 162.413 1.00128.59 N
ANISOU 1790 N ALA A1038 15744 20463 12651 -1306 -472 -1047 N
ATOM 1791 CA ALA A1038 -31.420 155.778 163.053 1.00128.86 C
ANISOU 1791 CA ALA A1038 15437 21040 12484 -1422 -327 -1015 C
ATOM 1792 C ALA A1038 -31.115 154.301 162.766 1.00128.43 C
ANISOU 1792 C ALA A1038 15297 20929 12570 -1989 -116 -927 C
ATOM 1793 O ALA A1038 -31.434 153.445 163.593 1.00128.58 O
ANISOU 1793 O ALA A1038 15130 21225 12499 -2143 -6 -879 O
ATOM 1794 CB ALA A1038 -32.848 156.110 162.661 1.00132.40 C
ANISOU 1794 CB ALA A1038 15610 22105 12590 -1218 -369 -1038 C
ATOM 1795 N LYS A1039 -30.523 154.005 161.597 1.00120.96 N
ANISOU 1795 N LYS A1039 14499 19638 11823 -2289 -71 -904 N
ATOM 1796 CA LYS A1039 -30.169 152.641 161.194 1.00118.63 C
ANISOU 1796 CA LYS A1039 14192 19223 11658 -2794 101 -841 C
ATOM 1797 C LYS A1039 -28.864 152.176 161.858 1.00119.48 C
ANISOU 1797 C LYS A1039 14520 18849 12028 -2903 153 -826 C
ATOM 1798 O LYS A1039 -28.679 150.972 162.063 1.00118.82 O
ANISOU 1798 O LYS A1039 14421 18722 12002 -3236 285 -777 O
ATOM 1799 CB LYS A1039 -30.039 152.534 159.662 1.00119.61 C
ANISOU 1799 CB LYS A1039 14384 19205 11858 -3019 117 -838 C
ATOM 1800 CG LYS A1039 -31.330 152.778 158.903 1.00129.03 C
ANISOU 1800 CG LYS A1039 15350 20879 12795 -2974 84 -845 C
ATOM 1801 CD LYS A1039 -31.088 152.864 157.412 1.00135.84 C
ANISOU 1801 CD LYS A1039 16315 21552 13746 -3122 72 -851 C
ATOM 1802 CE LYS A1039 -32.384 153.050 156.666 1.00148.33 C
ANISOU 1802 CE LYS A1039 17660 23636 15064 -3082 43 -856 C
ATOM 1803 NZ LYS A1039 -32.173 153.177 155.202 1.00155.38 N
ANISOU 1803 NZ LYS A1039 18638 24371 16030 -3240 37 -859 N
ATOM 1804 N LEU A1040 -27.964 153.126 162.195 1.00113.53 N
ANISOU 1804 N LEU A1040 13986 17732 11418 -2627 35 -863 N
ATOM 1805 CA LEU A1040 -26.659 152.807 162.774 1.00110.61 C
ANISOU 1805 CA LEU A1040 13820 16916 11289 -2701 69 -848 C
ATOM 1806 C LEU A1040 -26.574 152.945 164.312 1.00114.16 C
ANISOU 1806 C LEU A1040 14258 17407 11711 -2483 46 -858 C
ATOM 1807 O LEU A1040 -25.882 152.138 164.941 1.00111.85 O
ANISOU 1807 O LEU A1040 14032 16908 11557 -2652 142 -826 O
ATOM 1808 CB LEU A1040 -25.556 153.626 162.080 1.00108.84 C
ANISOU 1808 CB LEU A1040 13849 16256 11250 -2623 -42 -856 C
ATOM 1809 CG LEU A1040 -25.379 153.380 160.567 1.00111.89 C
ANISOU 1809 CG LEU A1040 14275 16535 11705 -2872 -2 -835 C
ATOM 1810 CD1 LEU A1040 -24.427 154.368 159.966 1.00110.50 C
ANISOU 1810 CD1 LEU A1040 14318 16005 11662 -2770 -139 -821 C
ATOM 1811 CD2 LEU A1040 -24.901 151.963 160.271 1.00113.17 C
ANISOU 1811 CD2 LEU A1040 14443 16574 11983 -3247 177 -805 C
ATOM 1812 N LYS A1041 -27.284 153.935 164.907 1.00112.56 N
ANISOU 1812 N LYS A1041 13977 17475 11314 -2090 -85 -908 N
ATOM 1813 CA LYS A1041 -27.297 154.206 166.354 1.00112.89 C
ANISOU 1813 CA LYS A1041 14003 17596 11294 -1820 -128 -933 C
ATOM 1814 C LYS A1041 -27.609 152.976 167.237 1.00116.92 C
ANISOU 1814 C LYS A1041 14317 18362 11745 -2051 39 -872 C
ATOM 1815 O LYS A1041 -26.816 152.736 168.149 1.00115.06 O
ANISOU 1815 O LYS A1041 14190 17884 11644 -2056 67 -859 O
ATOM 1816 CB LYS A1041 -28.233 155.377 166.713 1.00117.73 C
ANISOU 1816 CB LYS A1041 14550 18531 11651 -1329 -302 -1011 C
ATOM 1817 CG LYS A1041 -28.000 155.956 168.110 1.00130.18 C
ANISOU 1817 CG LYS A1041 16212 20053 13196 -973 -403 -1063 C
ATOM 1818 CD LYS A1041 -29.303 156.264 168.828 1.00137.25 C
ANISOU 1818 CD LYS A1041 16874 21532 13744 -581 -469 -1120 C
ATOM 1819 CE LYS A1041 -29.050 156.628 170.265 1.00143.23 C
ANISOU 1819 CE LYS A1041 17665 22301 14455 -289 -523 -1162 C
ATOM 1820 NZ LYS A1041 -29.899 155.833 171.189 1.00153.62 N
ANISOU 1820 NZ LYS A1041 18610 24273 15484 -235 -419 -1135 N
ATOM 1821 N PRO A1042 -28.712 152.194 167.029 1.00115.66 N
ANISOU 1821 N PRO A1042 13882 18685 11378 -2258 138 -821 N
ATOM 1822 CA PRO A1042 -28.977 151.048 167.927 1.00116.09 C
ANISOU 1822 CA PRO A1042 13780 18963 11365 -2511 270 -738 C
ATOM 1823 C PRO A1042 -27.884 149.978 167.950 1.00118.50 C
ANISOU 1823 C PRO A1042 14285 18808 11931 -2881 384 -686 C
ATOM 1824 O PRO A1042 -27.577 149.448 169.023 1.00117.78 O
ANISOU 1824 O PRO A1042 14202 18678 11871 -2933 439 -644 O
ATOM 1825 CB PRO A1042 -30.320 150.503 167.428 1.00119.76 C
ANISOU 1825 CB PRO A1042 13943 20000 11561 -2723 327 -679 C
ATOM 1826 CG PRO A1042 -30.432 150.979 166.032 1.00123.94 C
ANISOU 1826 CG PRO A1042 14530 20443 12117 -2722 275 -725 C
ATOM 1827 CD PRO A1042 -29.786 152.323 166.022 1.00118.70 C
ANISOU 1827 CD PRO A1042 14080 19460 11561 -2286 123 -822 C
ATOM 1828 N VAL A1043 -27.276 149.696 166.780 1.00114.03 N
ANISOU 1828 N VAL A1043 13885 17903 11538 -3104 412 -693 N
ATOM 1829 CA VAL A1043 -26.204 148.710 166.636 1.00112.57 C
ANISOU 1829 CA VAL A1043 13909 17285 11579 -3405 508 -663 C
ATOM 1830 C VAL A1043 -25.019 149.150 167.482 1.00116.82 C
ANISOU 1830 C VAL A1043 14637 17438 12310 -3192 472 -690 C
ATOM 1831 O VAL A1043 -24.574 148.399 168.346 1.00116.50 O
ANISOU 1831 O VAL A1043 14654 17271 12338 -3307 545 -650 O
ATOM 1832 CB VAL A1043 -25.776 148.490 165.159 1.00115.41 C
ANISOU 1832 CB VAL A1043 14391 17411 12047 -3622 531 -680 C
ATOM 1833 CG1 VAL A1043 -24.997 147.182 165.002 1.00113.76 C
ANISOU 1833 CG1 VAL A1043 14382 16830 12010 -3918 632 -655 C
ATOM 1834 CG2 VAL A1043 -26.976 148.529 164.211 1.00117.16 C
ANISOU 1834 CG2 VAL A1043 14416 18036 12063 -3788 540 -663 C
ATOM 1835 N TYR A1044 -24.553 150.393 167.251 1.00113.51 N
ANISOU 1835 N TYR A1044 14322 16848 11960 -2887 343 -750 N
ATOM 1836 CA TYR A1044 -23.416 151.042 167.899 1.00111.98 C
ANISOU 1836 CA TYR A1044 14320 16291 11935 -2680 268 -775 C
ATOM 1837 C TYR A1044 -23.469 151.028 169.431 1.00116.22 C
ANISOU 1837 C TYR A1044 14811 16926 12421 -2498 262 -773 C
ATOM 1838 O TYR A1044 -22.434 150.827 170.079 1.00115.03 O
ANISOU 1838 O TYR A1044 14801 16474 12430 -2503 282 -761 O
ATOM 1839 CB TYR A1044 -23.259 152.471 167.365 1.00113.19 C
ANISOU 1839 CB TYR A1044 14585 16319 12102 -2410 90 -825 C
ATOM 1840 CG TYR A1044 -21.943 153.103 167.753 1.00114.32 C
ANISOU 1840 CG TYR A1044 14960 16045 12432 -2295 -3 -829 C
ATOM 1841 CD1 TYR A1044 -20.754 152.714 167.142 1.00115.10 C
ANISOU 1841 CD1 TYR A1044 15198 15810 12726 -2515 48 -789 C
ATOM 1842 CD2 TYR A1044 -21.881 154.084 168.740 1.00115.44 C
ANISOU 1842 CD2 TYR A1044 15176 16152 12534 -1964 -150 -869 C
ATOM 1843 CE1 TYR A1044 -19.534 153.265 167.521 1.00115.00 C
ANISOU 1843 CE1 TYR A1044 15366 15468 12860 -2440 -38 -773 C
ATOM 1844 CE2 TYR A1044 -20.665 154.655 169.116 1.00115.21 C
ANISOU 1844 CE2 TYR A1044 15364 15746 12665 -1896 -250 -861 C
ATOM 1845 CZ TYR A1044 -19.494 154.243 168.502 1.00121.29 C
ANISOU 1845 CZ TYR A1044 16243 16218 13625 -2151 -191 -804 C
ATOM 1846 OH TYR A1044 -18.290 154.795 168.860 1.00121.63 O
ANISOU 1846 OH TYR A1044 16469 15943 13802 -2113 -291 -778 O
ATOM 1847 N ASP A1045 -24.671 151.236 170.002 1.00113.69 N
ANISOU 1847 N ASP A1045 14278 17058 11860 -2321 231 -785 N
ATOM 1848 CA ASP A1045 -24.893 151.235 171.447 1.00113.47 C
ANISOU 1848 CA ASP A1045 14163 17218 11733 -2121 223 -784 C
ATOM 1849 C ASP A1045 -24.683 149.840 172.049 1.00115.36 C
ANISOU 1849 C ASP A1045 14369 17440 12023 -2436 380 -697 C
ATOM 1850 O ASP A1045 -24.108 149.730 173.130 1.00114.68 O
ANISOU 1850 O ASP A1045 14338 17239 11995 -2330 384 -692 O
ATOM 1851 CB ASP A1045 -26.289 151.787 171.780 1.00117.72 C
ANISOU 1851 CB ASP A1045 14443 18330 11956 -1863 162 -811 C
ATOM 1852 CG ASP A1045 -26.463 153.276 171.518 1.00129.58 C
ANISOU 1852 CG ASP A1045 16021 19844 13368 -1413 -37 -916 C
ATOM 1853 OD1 ASP A1045 -25.535 154.056 171.851 1.00129.76 O
ANISOU 1853 OD1 ASP A1045 16311 19428 13562 -1240 -158 -966 O
ATOM 1854 OD2 ASP A1045 -27.553 153.671 171.045 1.00135.99 O
ANISOU 1854 OD2 ASP A1045 16632 21121 13916 -1221 -86 -945 O
ATOM 1855 N SER A1046 -25.115 148.779 171.329 1.00110.87 N
ANISOU 1855 N SER A1046 13736 16961 11427 -2824 494 -630 N
ATOM 1856 CA SER A1046 -24.973 147.375 171.743 1.00109.78 C
ANISOU 1856 CA SER A1046 13616 16777 11318 -3171 620 -538 C
ATOM 1857 C SER A1046 -23.510 146.890 171.724 1.00110.78 C
ANISOU 1857 C SER A1046 14023 16352 11716 -3274 667 -543 C
ATOM 1858 O SER A1046 -23.162 145.930 172.421 1.00110.92 O
ANISOU 1858 O SER A1046 14104 16272 11768 -3453 745 -480 O
ATOM 1859 CB SER A1046 -25.838 146.470 170.864 1.00112.65 C
ANISOU 1859 CB SER A1046 13873 17378 11552 -3555 688 -471 C
ATOM 1860 OG SER A1046 -25.167 145.976 169.715 1.00114.41 O
ANISOU 1860 OG SER A1046 14298 17233 11941 -3788 724 -489 O
ATOM 1861 N LEU A1047 -22.670 147.537 170.906 1.00104.28 N
ANISOU 1861 N LEU A1047 13362 15197 11062 -3171 616 -606 N
ATOM 1862 CA LEU A1047 -21.284 147.134 170.718 1.00101.84 C
ANISOU 1862 CA LEU A1047 13283 14434 10976 -3259 660 -609 C
ATOM 1863 C LEU A1047 -20.343 147.602 171.800 1.00103.85 C
ANISOU 1863 C LEU A1047 13633 14478 11346 -3031 621 -621 C
ATOM 1864 O LEU A1047 -20.495 148.709 172.311 1.00104.15 O
ANISOU 1864 O LEU A1047 13622 14614 11338 -2743 514 -659 O
ATOM 1865 CB LEU A1047 -20.757 147.576 169.337 1.00100.68 C
ANISOU 1865 CB LEU A1047 13240 14078 10934 -3292 628 -649 C
ATOM 1866 CG LEU A1047 -21.533 147.121 168.107 1.00105.17 C
ANISOU 1866 CG LEU A1047 13747 14801 11412 -3526 665 -646 C
ATOM 1867 CD1 LEU A1047 -21.191 147.986 166.920 1.00104.88 C
ANISOU 1867 CD1 LEU A1047 13752 14664 11432 -3442 590 -688 C
ATOM 1868 CD2 LEU A1047 -21.305 145.649 167.808 1.00105.99 C
ANISOU 1868 CD2 LEU A1047 13970 14751 11552 -3849 777 -615 C
ATOM 1869 N ASP A1048 -19.336 146.760 172.110 1.00 98.22 N
ANISOU 1869 N ASP A1048 13074 13473 10772 -3149 699 -595 N
ATOM 1870 CA ASP A1048 -18.252 147.040 173.049 1.00 96.39 C
ANISOU 1870 CA ASP A1048 12945 13016 10663 -2975 677 -599 C
ATOM 1871 C ASP A1048 -17.218 147.916 172.337 1.00 99.95 C
ANISOU 1871 C ASP A1048 13509 13216 11250 -2871 597 -633 C
ATOM 1872 O ASP A1048 -17.246 148.019 171.108 1.00 99.97 O
ANISOU 1872 O ASP A1048 13529 13190 11266 -2975 592 -645 O
ATOM 1873 CB ASP A1048 -17.601 145.736 173.528 1.00 97.53 C
ANISOU 1873 CB ASP A1048 13206 12978 10874 -3142 792 -553 C
ATOM 1874 CG ASP A1048 -17.033 144.888 172.410 1.00108.18 C
ANISOU 1874 CG ASP A1048 14691 14128 12284 -3365 863 -555 C
ATOM 1875 OD1 ASP A1048 -17.808 144.130 171.792 1.00110.58 O
ANISOU 1875 OD1 ASP A1048 14966 14561 12490 -3581 898 -542 O
ATOM 1876 OD2 ASP A1048 -15.815 144.993 172.146 1.00113.03 O
ANISOU 1876 OD2 ASP A1048 15441 14478 13026 -3317 879 -570 O
ATOM 1877 N ALA A1049 -16.302 148.519 173.100 1.00 95.85 N
ANISOU 1877 N ALA A1049 13065 12533 10820 -2688 528 -638 N
ATOM 1878 CA ALA A1049 -15.255 149.409 172.609 1.00 95.30 C
ANISOU 1878 CA ALA A1049 13102 12246 10862 -2614 426 -643 C
ATOM 1879 C ALA A1049 -14.487 148.918 171.365 1.00 99.23 C
ANISOU 1879 C ALA A1049 13665 12597 11440 -2806 493 -624 C
ATOM 1880 O ALA A1049 -14.273 149.705 170.434 1.00 98.36 O
ANISOU 1880 O ALA A1049 13577 12449 11347 -2811 406 -622 O
ATOM 1881 CB ALA A1049 -14.287 149.717 173.733 1.00 95.81 C
ANISOU 1881 CB ALA A1049 13242 12156 11007 -2472 379 -631 C
ATOM 1882 N VAL A1050 -14.078 147.629 171.351 1.00 96.27 N
ANISOU 1882 N VAL A1050 13334 12148 11097 -2949 636 -609 N
ATOM 1883 CA VAL A1050 -13.322 147.026 170.243 1.00 96.42 C
ANISOU 1883 CA VAL A1050 13424 12048 11163 -3088 707 -606 C
ATOM 1884 C VAL A1050 -14.187 146.926 168.972 1.00102.79 C
ANISOU 1884 C VAL A1050 14189 12970 11898 -3235 723 -630 C
ATOM 1885 O VAL A1050 -13.714 147.268 167.883 1.00103.70 O
ANISOU 1885 O VAL A1050 14321 13041 12038 -3282 705 -630 O
ATOM 1886 CB VAL A1050 -12.675 145.661 170.615 1.00100.19 C
ANISOU 1886 CB VAL A1050 14003 12396 11667 -3145 832 -600 C
ATOM 1887 CG1 VAL A1050 -11.650 145.233 169.569 1.00 99.71 C
ANISOU 1887 CG1 VAL A1050 14021 12226 11640 -3197 881 -609 C
ATOM 1888 CG2 VAL A1050 -12.028 145.711 171.992 1.00 99.64 C
ANISOU 1888 CG2 VAL A1050 13955 12252 11651 -2996 820 -576 C
ATOM 1889 N ARG A1051 -15.448 146.465 169.118 1.00 98.90 N
ANISOU 1889 N ARG A1051 13625 12652 11300 -3318 753 -639 N
ATOM 1890 CA ARG A1051 -16.387 146.319 168.003 1.00 98.70 C
ANISOU 1890 CA ARG A1051 13542 12774 11186 -3469 764 -657 C
ATOM 1891 C ARG A1051 -16.893 147.660 167.486 1.00102.64 C
ANISOU 1891 C ARG A1051 13944 13406 11647 -3353 643 -670 C
ATOM 1892 O ARG A1051 -17.161 147.795 166.285 1.00102.99 O
ANISOU 1892 O ARG A1051 13976 13487 11670 -3443 633 -682 O
ATOM 1893 CB ARG A1051 -17.532 145.366 168.355 1.00 97.38 C
ANISOU 1893 CB ARG A1051 13327 12775 10898 -3638 829 -643 C
ATOM 1894 CG ARG A1051 -17.042 143.945 168.418 1.00 99.46 C
ANISOU 1894 CG ARG A1051 13756 12847 11186 -3803 925 -634 C
ATOM 1895 CD ARG A1051 -18.133 143.016 168.796 1.00104.40 C
ANISOU 1895 CD ARG A1051 14371 13618 11680 -4034 963 -597 C
ATOM 1896 NE ARG A1051 -17.675 141.634 168.747 1.00112.92 N
ANISOU 1896 NE ARG A1051 15674 14456 12776 -4179 1023 -590 N
ATOM 1897 CZ ARG A1051 -17.206 140.965 169.791 1.00124.65 C
ANISOU 1897 CZ ARG A1051 17247 15843 14272 -4167 1049 -548 C
ATOM 1898 NH1 ARG A1051 -17.121 141.549 170.976 1.00109.56 N
ANISOU 1898 NH1 ARG A1051 15196 14071 12360 -4021 1031 -510 N
ATOM 1899 NH2 ARG A1051 -16.801 139.712 169.654 1.00114.01 N
ANISOU 1899 NH2 ARG A1051 16144 14250 12925 -4283 1084 -548 N
ATOM 1900 N ARG A1052 -16.981 148.661 168.381 1.00 97.93 N
ANISOU 1900 N ARG A1052 13308 12863 11039 -3136 537 -671 N
ATOM 1901 CA ARG A1052 -17.386 150.016 168.022 1.00 97.40 C
ANISOU 1901 CA ARG A1052 13210 12871 10927 -2968 383 -688 C
ATOM 1902 C ARG A1052 -16.371 150.592 167.027 1.00 98.23 C
ANISOU 1902 C ARG A1052 13420 12770 11134 -2997 314 -665 C
ATOM 1903 O ARG A1052 -16.771 151.232 166.055 1.00 97.40 O
ANISOU 1903 O ARG A1052 13309 12712 10987 -2973 216 -668 O
ATOM 1904 CB ARG A1052 -17.476 150.899 169.273 1.00 98.16 C
ANISOU 1904 CB ARG A1052 13311 12990 10997 -2703 268 -703 C
ATOM 1905 CG ARG A1052 -18.744 150.708 170.107 1.00107.38 C
ANISOU 1905 CG ARG A1052 14329 14469 12003 -2606 288 -725 C
ATOM 1906 CD ARG A1052 -18.793 151.784 171.172 1.00114.30 C
ANISOU 1906 CD ARG A1052 15233 15356 12839 -2290 146 -759 C
ATOM 1907 NE ARG A1052 -19.546 151.405 172.367 1.00113.76 N
ANISOU 1907 NE ARG A1052 15017 15575 12630 -2193 193 -765 N
ATOM 1908 CZ ARG A1052 -20.708 151.943 172.720 1.00128.03 C
ANISOU 1908 CZ ARG A1052 16693 17711 14240 -1972 114 -807 C
ATOM 1909 NH1 ARG A1052 -21.280 152.864 171.956 1.00114.31 N
ANISOU 1909 NH1 ARG A1052 14982 16021 12428 -1805 -26 -855 N
ATOM 1910 NH2 ARG A1052 -21.311 151.557 173.834 1.00121.47 N
ANISOU 1910 NH2 ARG A1052 15701 17186 13265 -1904 169 -797 N
ATOM 1911 N ALA A1053 -15.064 150.309 167.252 1.00 93.29 N
ANISOU 1911 N ALA A1053 12879 11943 10623 -3050 363 -633 N
ATOM 1912 CA ALA A1053 -13.945 150.749 166.410 1.00 92.44 C
ANISOU 1912 CA ALA A1053 12840 11692 10592 -3105 313 -587 C
ATOM 1913 C ALA A1053 -13.981 150.118 165.015 1.00 95.98 C
ANISOU 1913 C ALA A1053 13261 12189 11019 -3284 402 -591 C
ATOM 1914 O ALA A1053 -13.647 150.788 164.028 1.00 95.44 O
ANISOU 1914 O ALA A1053 13201 12110 10952 -3325 323 -555 O
ATOM 1915 CB ALA A1053 -12.627 150.452 167.095 1.00 92.54 C
ANISOU 1915 CB ALA A1053 12910 11555 10695 -3090 354 -552 C
ATOM 1916 N ALA A1054 -14.421 148.842 164.932 1.00 92.18 N
ANISOU 1916 N ALA A1054 12764 11757 10504 -3398 550 -631 N
ATOM 1917 CA ALA A1054 -14.581 148.119 163.667 1.00 91.59 C
ANISOU 1917 CA ALA A1054 12687 11724 10388 -3560 630 -655 C
ATOM 1918 C ALA A1054 -15.669 148.809 162.813 1.00 94.30 C
ANISOU 1918 C ALA A1054 12947 12234 10648 -3595 562 -667 C
ATOM 1919 O ALA A1054 -15.446 149.041 161.619 1.00 93.51 O
ANISOU 1919 O ALA A1054 12842 12154 10535 -3675 554 -661 O
ATOM 1920 CB ALA A1054 -14.940 146.663 163.932 1.00 92.60 C
ANISOU 1920 CB ALA A1054 12868 11834 10482 -3675 763 -695 C
ATOM 1921 N LEU A1055 -16.801 149.213 163.446 1.00 90.02 N
ANISOU 1921 N LEU A1055 12331 11837 10034 -3508 503 -681 N
ATOM 1922 CA LEU A1055 -17.879 149.921 162.759 1.00 90.23 C
ANISOU 1922 CA LEU A1055 12270 12055 9958 -3491 427 -695 C
ATOM 1923 C LEU A1055 -17.435 151.292 162.259 1.00 96.73 C
ANISOU 1923 C LEU A1055 13142 12800 10810 -3376 268 -661 C
ATOM 1924 O LEU A1055 -17.784 151.637 161.136 1.00 97.76 O
ANISOU 1924 O LEU A1055 13244 13012 10890 -3432 230 -658 O
ATOM 1925 CB LEU A1055 -19.134 150.027 163.630 1.00 90.74 C
ANISOU 1925 CB LEU A1055 12224 12350 9902 -3388 404 -718 C
ATOM 1926 CG LEU A1055 -20.419 150.563 162.970 1.00 95.82 C
ANISOU 1926 CG LEU A1055 12742 13270 10395 -3371 351 -739 C
ATOM 1927 CD1 LEU A1055 -20.953 149.609 161.917 1.00 95.82 C
ANISOU 1927 CD1 LEU A1055 12684 13391 10334 -3641 467 -747 C
ATOM 1928 CD2 LEU A1055 -21.497 150.799 164.013 1.00 99.79 C
ANISOU 1928 CD2 LEU A1055 13121 14037 10757 -3190 302 -756 C
ATOM 1929 N ILE A1056 -16.643 152.054 163.055 1.00 94.03 N
ANISOU 1929 N ILE A1056 12890 12297 10542 -3235 161 -627 N
ATOM 1930 CA ILE A1056 -16.149 153.376 162.648 1.00 94.43 C
ANISOU 1930 CA ILE A1056 13035 12232 10612 -3161 -27 -575 C
ATOM 1931 C ILE A1056 -15.144 153.247 161.513 1.00 98.59 C
ANISOU 1931 C ILE A1056 13584 12678 11196 -3343 2 -509 C
ATOM 1932 O ILE A1056 -15.169 154.077 160.602 1.00 98.59 O
ANISOU 1932 O ILE A1056 13617 12676 11167 -3374 -117 -462 O
ATOM 1933 CB ILE A1056 -15.643 154.233 163.844 1.00 97.92 C
ANISOU 1933 CB ILE A1056 13587 12528 11091 -2975 -174 -559 C
ATOM 1934 CG1 ILE A1056 -16.784 155.115 164.347 1.00 99.60 C
ANISOU 1934 CG1 ILE A1056 13792 12868 11185 -2736 -288 -623 C
ATOM 1935 CG2 ILE A1056 -14.428 155.126 163.500 1.00 98.74 C
ANISOU 1935 CG2 ILE A1056 13834 12435 11248 -3006 -355 -467 C
ATOM 1936 CD1 ILE A1056 -17.208 154.816 165.655 1.00109.08 C
ANISOU 1936 CD1 ILE A1056 15017 14043 12384 -2559 -317 -655 C
ATOM 1937 N ASN A1057 -14.310 152.183 161.538 1.00 95.47 N
ANISOU 1937 N ASN A1057 13170 12244 10860 -3451 159 -508 N
ATOM 1938 CA ASN A1057 -13.309 151.876 160.501 1.00 95.91 C
ANISOU 1938 CA ASN A1057 13217 12288 10938 -3594 216 -459 C
ATOM 1939 C ASN A1057 -13.964 151.772 159.088 1.00100.75 C
ANISOU 1939 C ASN A1057 13772 13033 11476 -3703 241 -477 C
ATOM 1940 O ASN A1057 -13.398 152.242 158.095 1.00100.28 O
ANISOU 1940 O ASN A1057 13707 12993 11401 -3780 177 -407 O
ATOM 1941 CB ASN A1057 -12.582 150.571 160.863 1.00 96.17 C
ANISOU 1941 CB ASN A1057 13249 12285 11006 -3625 389 -494 C
ATOM 1942 CG ASN A1057 -11.353 150.249 160.046 1.00120.20 C
ANISOU 1942 CG ASN A1057 16280 15339 14053 -3697 440 -445 C
ATOM 1943 OD1 ASN A1057 -11.382 150.138 158.814 1.00117.01 O
ANISOU 1943 OD1 ASN A1057 15834 15031 13595 -3789 460 -437 O
ATOM 1944 ND2 ASN A1057 -10.263 149.989 160.733 1.00111.52 N
ANISOU 1944 ND2 ASN A1057 15201 14174 12998 -3642 474 -417 N
ATOM 1945 N MET A1058 -15.165 151.166 159.030 1.00 97.55 N
ANISOU 1945 N MET A1058 13318 12738 11010 -3724 325 -559 N
ATOM 1946 CA MET A1058 -15.966 150.983 157.823 1.00 97.39 C
ANISOU 1946 CA MET A1058 13235 12865 10905 -3827 356 -592 C
ATOM 1947 C MET A1058 -16.547 152.311 157.359 1.00100.98 C
ANISOU 1947 C MET A1058 13677 13383 11307 -3760 191 -554 C
ATOM 1948 O MET A1058 -16.488 152.603 156.169 1.00101.20 O
ANISOU 1948 O MET A1058 13680 13478 11293 -3849 170 -528 O
ATOM 1949 CB MET A1058 -17.093 149.977 158.078 1.00 99.78 C
ANISOU 1949 CB MET A1058 13489 13283 11140 -3878 458 -671 C
ATOM 1950 CG MET A1058 -16.632 148.555 158.045 1.00103.01 C
ANISOU 1950 CG MET A1058 13952 13622 11564 -3994 608 -716 C
ATOM 1951 SD MET A1058 -17.955 147.428 158.488 1.00107.83 S
ANISOU 1951 SD MET A1058 14530 14371 12071 -4130 690 -776 S
ATOM 1952 CE MET A1058 -18.961 147.498 157.005 1.00105.32 C
ANISOU 1952 CE MET A1058 14121 14255 11640 -4249 665 -797 C
ATOM 1953 N VAL A1059 -17.108 153.113 158.292 1.00 96.72 N
ANISOU 1953 N VAL A1059 13167 12829 10752 -3585 66 -555 N
ATOM 1954 CA VAL A1059 -17.677 154.437 158.008 1.00 96.99 C
ANISOU 1954 CA VAL A1059 13242 12891 10718 -3459 -127 -531 C
ATOM 1955 C VAL A1059 -16.569 155.339 157.403 1.00101.73 C
ANISOU 1955 C VAL A1059 13951 13335 11367 -3524 -264 -421 C
ATOM 1956 O VAL A1059 -16.858 156.182 156.550 1.00102.84 O
ANISOU 1956 O VAL A1059 14115 13513 11446 -3544 -374 -381 O
ATOM 1957 CB VAL A1059 -18.356 155.050 159.267 1.00100.49 C
ANISOU 1957 CB VAL A1059 13722 13344 11116 -3209 -238 -572 C
ATOM 1958 CG1 VAL A1059 -18.910 156.443 158.990 1.00101.40 C
ANISOU 1958 CG1 VAL A1059 13945 13434 11150 -3027 -475 -553 C
ATOM 1959 CG2 VAL A1059 -19.468 154.149 159.775 1.00100.27 C
ANISOU 1959 CG2 VAL A1059 13544 13559 10996 -3180 -110 -654 C
ATOM 1960 N PHE A1060 -15.299 155.103 157.798 1.00 96.40 N
ANISOU 1960 N PHE A1060 13328 12512 10786 -3581 -254 -361 N
ATOM 1961 CA PHE A1060 -14.152 155.833 157.279 1.00 96.05 C
ANISOU 1961 CA PHE A1060 13359 12366 10771 -3693 -376 -231 C
ATOM 1962 C PHE A1060 -13.838 155.447 155.817 1.00102.66 C
ANISOU 1962 C PHE A1060 14100 13336 11571 -3881 -289 -188 C
ATOM 1963 O PHE A1060 -13.383 156.291 155.043 1.00104.82 O
ANISOU 1963 O PHE A1060 14415 13599 11811 -3979 -425 -74 O
ATOM 1964 CB PHE A1060 -12.935 155.659 158.209 1.00 96.78 C
ANISOU 1964 CB PHE A1060 13488 12335 10948 -3710 -366 -179 C
ATOM 1965 CG PHE A1060 -12.746 156.806 159.183 1.00 98.52 C
ANISOU 1965 CG PHE A1060 13875 12370 11189 -3598 -590 -132 C
ATOM 1966 CD1 PHE A1060 -13.473 156.864 160.368 1.00101.40 C
ANISOU 1966 CD1 PHE A1060 14286 12682 11559 -3387 -611 -226 C
ATOM 1967 CD2 PHE A1060 -11.843 157.830 158.912 1.00101.03 C
ANISOU 1967 CD2 PHE A1060 14309 12574 11502 -3713 -793 14 C
ATOM 1968 CE1 PHE A1060 -13.312 157.934 161.257 1.00102.75 C
ANISOU 1968 CE1 PHE A1060 14637 12672 11733 -3257 -835 -198 C
ATOM 1969 CE2 PHE A1060 -11.675 158.895 159.807 1.00104.40 C
ANISOU 1969 CE2 PHE A1060 14935 12795 11936 -3621 -1029 54 C
ATOM 1970 CZ PHE A1060 -12.410 158.940 160.972 1.00102.39 C
ANISOU 1970 CZ PHE A1060 14742 12472 11690 -3376 -1049 -63 C
ATOM 1971 N GLN A1061 -14.137 154.201 155.429 1.00 98.36 N
ANISOU 1971 N GLN A1061 13444 12914 11015 -3931 -77 -278 N
ATOM 1972 CA GLN A1061 -13.886 153.671 154.094 1.00 98.37 C
ANISOU 1972 CA GLN A1061 13357 13053 10965 -4073 26 -273 C
ATOM 1973 C GLN A1061 -15.081 153.844 153.122 1.00105.54 C
ANISOU 1973 C GLN A1061 14221 14092 11786 -4095 9 -316 C
ATOM 1974 O GLN A1061 -14.871 154.213 151.971 1.00106.83 O
ANISOU 1974 O GLN A1061 14351 14343 11897 -4197 -23 -255 O
ATOM 1975 CB GLN A1061 -13.447 152.207 154.240 1.00 98.81 C
ANISOU 1975 CB GLN A1061 13370 13134 11038 -4094 236 -362 C
ATOM 1976 CG GLN A1061 -13.404 151.355 152.975 1.00107.84 C
ANISOU 1976 CG GLN A1061 14449 14416 12111 -4199 355 -396 C
ATOM 1977 CD GLN A1061 -12.983 149.924 153.247 1.00122.80 C
ANISOU 1977 CD GLN A1061 16365 16288 14005 -4183 528 -496 C
ATOM 1978 OE1 GLN A1061 -13.102 149.391 154.364 1.00120.49 O
ANISOU 1978 OE1 GLN A1061 16130 15883 13766 -4117 576 -547 O
ATOM 1979 NE2 GLN A1061 -12.513 149.253 152.212 1.00110.53 N
ANISOU 1979 NE2 GLN A1061 14783 14839 12375 -4233 613 -530 N
ATOM 1980 N MET A1062 -16.314 153.591 153.580 1.00103.19 N
ANISOU 1980 N MET A1062 13906 13846 11457 -4006 34 -413 N
ATOM 1981 CA MET A1062 -17.537 153.659 152.763 1.00104.39 C
ANISOU 1981 CA MET A1062 13988 14170 11507 -4022 34 -462 C
ATOM 1982 C MET A1062 -18.439 154.859 153.047 1.00110.14 C
ANISOU 1982 C MET A1062 14751 14927 12169 -3860 -144 -450 C
ATOM 1983 O MET A1062 -19.184 155.288 152.169 1.00109.88 O
ANISOU 1983 O MET A1062 14684 15018 12048 -3869 -202 -444 O
ATOM 1984 CB MET A1062 -18.363 152.375 152.959 1.00106.92 C
ANISOU 1984 CB MET A1062 14231 14604 11790 -4077 202 -576 C
ATOM 1985 CG MET A1062 -17.733 151.155 152.334 1.00110.88 C
ANISOU 1985 CG MET A1062 14728 15097 12303 -4227 357 -612 C
ATOM 1986 SD MET A1062 -18.194 149.617 153.158 1.00115.33 S
ANISOU 1986 SD MET A1062 15307 15657 12857 -4292 512 -719 S
ATOM 1987 CE MET A1062 -16.930 149.525 154.383 1.00111.43 C
ANISOU 1987 CE MET A1062 14904 14948 12485 -4197 536 -690 C
ATOM 1988 N GLY A1063 -18.428 155.335 154.283 1.00108.66 N
ANISOU 1988 N GLY A1063 14634 14644 12009 -3690 -228 -462 N
ATOM 1989 CA GLY A1063 -19.290 156.429 154.703 1.00110.45 C
ANISOU 1989 CA GLY A1063 14918 14898 12149 -3466 -408 -475 C
ATOM 1990 C GLY A1063 -20.563 155.930 155.350 1.00116.63 C
ANISOU 1990 C GLY A1063 15581 15890 12843 -3339 -330 -578 C
ATOM 1991 O GLY A1063 -21.004 154.807 155.083 1.00116.73 O
ANISOU 1991 O GLY A1063 15456 16065 12832 -3485 -150 -628 O
ATOM 1992 N GLU A1064 -21.159 156.779 156.204 1.00114.17 N
ANISOU 1992 N GLU A1064 15332 15589 12460 -3068 -482 -605 N
ATOM 1993 CA GLU A1064 -22.396 156.547 156.954 1.00114.51 C
ANISOU 1993 CA GLU A1064 15247 15886 12374 -2887 -449 -689 C
ATOM 1994 C GLU A1064 -23.511 155.885 156.123 1.00118.72 C
ANISOU 1994 C GLU A1064 15574 16764 12772 -2988 -334 -729 C
ATOM 1995 O GLU A1064 -24.051 154.867 156.546 1.00118.42 O
ANISOU 1995 O GLU A1064 15377 16942 12674 -3057 -195 -770 O
ATOM 1996 CB GLU A1064 -22.890 157.879 157.545 1.00117.13 C
ANISOU 1996 CB GLU A1064 15708 16195 12601 -2529 -688 -711 C
ATOM 1997 CG GLU A1064 -23.569 157.757 158.894 1.00125.99 C
ANISOU 1997 CG GLU A1064 16767 17466 13638 -2286 -687 -783 C
ATOM 1998 CD GLU A1064 -24.117 159.068 159.414 1.00142.33 C
ANISOU 1998 CD GLU A1064 18962 19568 15550 -1879 -931 -830 C
ATOM 1999 OE1 GLU A1064 -25.356 159.245 159.388 1.00134.57 O
ANISOU 1999 OE1 GLU A1064 17821 18950 14361 -1681 -935 -893 O
ATOM 2000 OE2 GLU A1064 -23.307 159.935 159.812 1.00133.72 O
ANISOU 2000 OE2 GLU A1064 18140 18145 14524 -1759 -1135 -802 O
ATOM 2001 N THR A1065 -23.823 156.443 154.941 1.00115.99 N
ANISOU 2001 N THR A1065 15234 16469 12369 -3022 -400 -706 N
ATOM 2002 CA THR A1065 -24.880 155.970 154.041 1.00116.88 C
ANISOU 2002 CA THR A1065 15164 16903 12342 -3121 -320 -736 C
ATOM 2003 C THR A1065 -24.558 154.574 153.467 1.00119.56 C
ANISOU 2003 C THR A1065 15419 17256 12753 -3473 -112 -738 C
ATOM 2004 O THR A1065 -25.457 153.726 153.402 1.00120.39 O
ANISOU 2004 O THR A1065 15358 17637 12749 -3598 -2 -777 O
ATOM 2005 CB THR A1065 -25.172 157.059 152.991 1.00127.77 C
ANISOU 2005 CB THR A1065 16616 18289 13640 -3004 -488 -706 C
ATOM 2006 OG1 THR A1065 -25.877 158.114 153.657 1.00131.01 O
ANISOU 2006 OG1 THR A1065 17110 18733 13933 -2635 -684 -733 O
ATOM 2007 CG2 THR A1065 -25.995 156.562 151.794 1.00125.15 C
ANISOU 2007 CG2 THR A1065 16105 18272 13176 -3130 -410 -727 C
ATOM 2008 N GLY A1066 -23.294 154.349 153.103 1.00113.82 N
ANISOU 2008 N GLY A1066 14813 16249 12185 -3623 -76 -695 N
ATOM 2009 CA GLY A1066 -22.818 153.068 152.582 1.00112.30 C
ANISOU 2009 CA GLY A1066 14593 16021 12054 -3899 98 -710 C
ATOM 2010 C GLY A1066 -22.887 151.946 153.603 1.00113.68 C
ANISOU 2010 C GLY A1066 14746 16187 12261 -3983 229 -751 C
ATOM 2011 O GLY A1066 -23.391 150.859 153.302 1.00113.37 O
ANISOU 2011 O GLY A1066 14650 16253 12173 -4189 350 -789 O
ATOM 2012 N VAL A1067 -22.405 152.223 154.834 1.00107.89 N
ANISOU 2012 N VAL A1067 14076 15317 11599 -3831 190 -738 N
ATOM 2013 CA VAL A1067 -22.400 151.302 155.974 1.00106.27 C
ANISOU 2013 CA VAL A1067 13864 15090 11425 -3879 293 -762 C
ATOM 2014 C VAL A1067 -23.838 150.949 156.411 1.00109.87 C
ANISOU 2014 C VAL A1067 14152 15882 11713 -3887 322 -791 C
ATOM 2015 O VAL A1067 -24.099 149.792 156.741 1.00110.33 O
ANISOU 2015 O VAL A1067 14180 15994 11748 -4071 433 -801 O
ATOM 2016 CB VAL A1067 -21.511 151.850 157.121 1.00108.91 C
ANISOU 2016 CB VAL A1067 14310 15192 11878 -3706 231 -734 C
ATOM 2017 CG1 VAL A1067 -21.653 151.034 158.401 1.00108.38 C
ANISOU 2017 CG1 VAL A1067 14224 15133 11824 -3722 323 -754 C
ATOM 2018 CG2 VAL A1067 -20.053 151.897 156.686 1.00107.85 C
ANISOU 2018 CG2 VAL A1067 14302 14792 11883 -3774 232 -690 C
ATOM 2019 N ALA A1068 -24.775 151.925 156.340 1.00105.52 N
ANISOU 2019 N ALA A1068 13495 15578 11020 -3700 214 -797 N
ATOM 2020 CA ALA A1068 -26.198 151.764 156.675 1.00105.75 C
ANISOU 2020 CA ALA A1068 13316 16022 10841 -3677 227 -814 C
ATOM 2021 C ALA A1068 -26.893 150.737 155.774 1.00108.69 C
ANISOU 2021 C ALA A1068 13574 16611 11112 -3991 329 -818 C
ATOM 2022 O ALA A1068 -27.978 150.253 156.110 1.00109.90 O
ANISOU 2022 O ALA A1068 13542 17131 11085 -4070 362 -811 O
ATOM 2023 CB ALA A1068 -26.911 153.103 156.584 1.00107.51 C
ANISOU 2023 CB ALA A1068 13480 16445 10924 -3343 69 -829 C
ATOM 2024 N GLY A1069 -26.246 150.409 154.656 1.00102.99 N
ANISOU 2024 N GLY A1069 12961 15680 10489 -4172 370 -823 N
ATOM 2025 CA GLY A1069 -26.725 149.428 153.693 1.00103.08 C
ANISOU 2025 CA GLY A1069 12921 15823 10420 -4474 451 -838 C
ATOM 2026 C GLY A1069 -26.669 147.985 154.167 1.00105.48 C
ANISOU 2026 C GLY A1069 13288 16049 10740 -4760 561 -842 C
ATOM 2027 O GLY A1069 -27.540 147.194 153.797 1.00106.87 O
ANISOU 2027 O GLY A1069 13397 16424 10786 -5022 601 -845 O
ATOM 2028 N PHE A1070 -25.647 147.621 154.979 1.00 99.27 N
ANISOU 2028 N PHE A1070 12649 14969 10100 -4723 597 -838 N
ATOM 2029 CA PHE A1070 -25.437 146.262 155.512 1.00 99.21 C
ANISOU 2029 CA PHE A1070 12756 14829 10112 -4964 682 -839 C
ATOM 2030 C PHE A1070 -26.465 145.880 156.622 1.00105.18 C
ANISOU 2030 C PHE A1070 13370 15862 10731 -5034 689 -791 C
ATOM 2031 O PHE A1070 -26.087 145.334 157.662 1.00104.08 O
ANISOU 2031 O PHE A1070 13310 15583 10651 -5037 720 -769 O
ATOM 2032 CB PHE A1070 -23.994 146.118 156.044 1.00 99.20 C
ANISOU 2032 CB PHE A1070 12956 14433 10304 -4864 714 -849 C
ATOM 2033 CG PHE A1070 -22.873 146.311 155.052 1.00 99.36 C
ANISOU 2033 CG PHE A1070 13099 14214 10439 -4806 716 -878 C
ATOM 2034 CD1 PHE A1070 -22.409 145.248 154.288 1.00102.10 C
ANISOU 2034 CD1 PHE A1070 13592 14409 10791 -4983 776 -926 C
ATOM 2035 CD2 PHE A1070 -22.229 147.536 154.935 1.00100.53 C
ANISOU 2035 CD2 PHE A1070 13234 14284 10678 -4573 647 -852 C
ATOM 2036 CE1 PHE A1070 -21.350 145.419 153.390 1.00102.04 C
ANISOU 2036 CE1 PHE A1070 13670 14238 10862 -4907 784 -948 C
ATOM 2037 CE2 PHE A1070 -21.167 147.703 154.039 1.00102.11 C
ANISOU 2037 CE2 PHE A1070 13523 14313 10962 -4549 647 -854 C
ATOM 2038 CZ PHE A1070 -20.736 146.642 153.273 1.00100.06 C
ANISOU 2038 CZ PHE A1070 13364 13961 10694 -4705 725 -902 C
ATOM 2039 N THR A1071 -27.760 146.141 156.365 1.00104.01 N
ANISOU 2039 N THR A1071 12998 16141 10381 -5094 659 -769 N
ATOM 2040 CA THR A1071 -28.917 145.956 157.250 1.00105.87 C
ANISOU 2040 CA THR A1071 13020 16781 10423 -5146 654 -708 C
ATOM 2041 C THR A1071 -28.934 144.603 157.990 1.00110.42 C
ANISOU 2041 C THR A1071 13690 17285 10979 -5463 711 -655 C
ATOM 2042 O THR A1071 -29.120 144.579 159.220 1.00110.21 O
ANISOU 2042 O THR A1071 13589 17369 10917 -5387 716 -605 O
ATOM 2043 CB THR A1071 -30.198 146.214 156.451 1.00118.24 C
ANISOU 2043 CB THR A1071 14337 18832 11755 -5217 620 -693 C
ATOM 2044 OG1 THR A1071 -30.133 147.552 155.947 1.00120.11 O
ANISOU 2044 OG1 THR A1071 14527 19094 12015 -4881 550 -739 O
ATOM 2045 CG2 THR A1071 -31.473 146.034 157.283 1.00118.85 C
ANISOU 2045 CG2 THR A1071 14136 19436 11585 -5250 612 -619 C
ATOM 2046 N ASN A1072 -28.728 143.500 157.249 1.00107.25 N
ANISOU 2046 N ASN A1072 13471 16692 10589 -5804 740 -665 N
ATOM 2047 CA ASN A1072 -28.715 142.151 157.810 1.00108.25 C
ANISOU 2047 CA ASN A1072 13757 16688 10684 -6133 763 -614 C
ATOM 2048 C ASN A1072 -27.515 141.941 158.725 1.00110.37 C
ANISOU 2048 C ASN A1072 14237 16552 11148 -5973 796 -627 C
ATOM 2049 O ASN A1072 -27.690 141.597 159.892 1.00110.41 O
ANISOU 2049 O ASN A1072 14214 16626 11111 -6023 804 -556 O
ATOM 2050 CB ASN A1072 -28.756 141.103 156.703 1.00110.86 C
ANISOU 2050 CB ASN A1072 14295 16853 10975 -6490 754 -643 C
ATOM 2051 CG ASN A1072 -30.046 141.080 155.934 1.00132.46 C
ANISOU 2051 CG ASN A1072 16830 19999 13500 -6711 718 -620 C
ATOM 2052 OD1 ASN A1072 -31.133 140.897 156.496 1.00140.18 O
ANISOU 2052 OD1 ASN A1072 17565 21430 14267 -6879 696 -525 O
ATOM 2053 ND2 ASN A1072 -29.948 141.219 154.627 1.00115.36 N
ANISOU 2053 ND2 ASN A1072 14755 17707 11368 -6730 711 -701 N
ATOM 2054 N SER A1073 -26.303 142.206 158.212 1.00105.38 N
ANISOU 2054 N SER A1073 13786 15542 10711 -5769 813 -709 N
ATOM 2055 CA SER A1073 -25.051 142.091 158.964 1.00103.57 C
ANISOU 2055 CA SER A1073 13746 14940 10667 -5587 843 -728 C
ATOM 2056 C SER A1073 -25.105 142.942 160.267 1.00106.34 C
ANISOU 2056 C SER A1073 13936 15424 11046 -5320 833 -685 C
ATOM 2057 O SER A1073 -24.654 142.481 161.318 1.00106.01 O
ANISOU 2057 O SER A1073 13996 15214 11068 -5295 857 -658 O
ATOM 2058 CB SER A1073 -23.872 142.484 158.077 1.00104.58 C
ANISOU 2058 CB SER A1073 14019 14765 10951 -5413 855 -809 C
ATOM 2059 OG SER A1073 -24.025 141.961 156.765 1.00113.12 O
ANISOU 2059 OG SER A1073 15214 15789 11977 -5615 856 -860 O
ATOM 2060 N LEU A1074 -25.739 144.139 160.202 1.00101.62 N
ANISOU 2060 N LEU A1074 13097 15141 10374 -5117 786 -682 N
ATOM 2061 CA LEU A1074 -25.936 145.047 161.337 1.00100.24 C
ANISOU 2061 CA LEU A1074 12770 15134 10183 -4823 749 -659 C
ATOM 2062 C LEU A1074 -26.958 144.488 162.354 1.00105.76 C
ANISOU 2062 C LEU A1074 13310 16171 10703 -4962 764 -579 C
ATOM 2063 O LEU A1074 -26.765 144.647 163.567 1.00104.93 O
ANISOU 2063 O LEU A1074 13185 16061 10624 -4801 765 -554 O
ATOM 2064 CB LEU A1074 -26.360 146.444 160.854 1.00 99.66 C
ANISOU 2064 CB LEU A1074 12530 15293 10045 -4557 669 -691 C
ATOM 2065 CG LEU A1074 -25.300 147.277 160.157 1.00101.55 C
ANISOU 2065 CG LEU A1074 12900 15233 10451 -4346 620 -742 C
ATOM 2066 CD1 LEU A1074 -25.936 148.364 159.338 1.00101.82 C
ANISOU 2066 CD1 LEU A1074 12797 15515 10375 -4197 536 -762 C
ATOM 2067 CD2 LEU A1074 -24.310 147.851 161.143 1.00101.93 C
ANISOU 2067 CD2 LEU A1074 13043 15045 10639 -4075 578 -746 C
ATOM 2068 N ARG A1075 -28.033 143.829 161.871 1.00103.68 N
ANISOU 2068 N ARG A1075 12924 16228 10243 -5276 770 -528 N
ATOM 2069 CA ARG A1075 -28.994 143.215 162.787 1.00105.70 C
ANISOU 2069 CA ARG A1075 13011 16854 10295 -5479 779 -422 C
ATOM 2070 C ARG A1075 -28.373 141.982 163.474 1.00109.42 C
ANISOU 2070 C ARG A1075 13727 17007 10841 -5752 817 -368 C
ATOM 2071 O ARG A1075 -28.798 141.633 164.567 1.00110.77 O
ANISOU 2071 O ARG A1075 13798 17406 10883 -5883 822 -268 O
ATOM 2072 CB ARG A1075 -30.306 142.845 162.081 1.00108.85 C
ANISOU 2072 CB ARG A1075 13192 17727 10438 -5764 759 -366 C
ATOM 2073 N MET A1076 -27.357 141.346 162.844 1.00104.09 N
ANISOU 2073 N MET A1076 13372 15826 10351 -5824 837 -430 N
ATOM 2074 CA MET A1076 -26.660 140.167 163.373 1.00103.66 C
ANISOU 2074 CA MET A1076 13609 15409 10369 -6031 856 -399 C
ATOM 2075 C MET A1076 -25.730 140.540 164.505 1.00104.68 C
ANISOU 2075 C MET A1076 13794 15329 10650 -5735 884 -407 C
ATOM 2076 O MET A1076 -25.692 139.830 165.510 1.00103.98 O
ANISOU 2076 O MET A1076 13788 15189 10531 -5871 893 -331 O
ATOM 2077 CB MET A1076 -25.882 139.431 162.266 1.00105.70 C
ANISOU 2077 CB MET A1076 14187 15239 10734 -6153 858 -483 C
ATOM 2078 CG MET A1076 -26.751 138.565 161.373 1.00111.61 C
ANISOU 2078 CG MET A1076 14993 16099 11313 -6568 815 -456 C
ATOM 2079 SD MET A1076 -25.867 138.033 159.889 1.00115.39 S
ANISOU 2079 SD MET A1076 15808 16136 11898 -6602 807 -590 S
ATOM 2080 CE MET A1076 -27.232 137.457 158.898 1.00114.65 C
ANISOU 2080 CE MET A1076 15687 16318 11557 -7091 736 -542 C
ATOM 2081 N LEU A1077 -24.964 141.643 164.331 1.00100.31 N
ANISOU 2081 N LEU A1077 13210 14652 10253 -5352 886 -490 N
ATOM 2082 CA LEU A1077 -24.023 142.165 165.329 1.00 99.28 C
ANISOU 2082 CA LEU A1077 13120 14335 10267 -5048 896 -504 C
ATOM 2083 C LEU A1077 -24.771 142.597 166.580 1.00106.27 C
ANISOU 2083 C LEU A1077 13760 15599 11017 -4943 880 -436 C
ATOM 2084 O LEU A1077 -24.331 142.286 167.685 1.00106.83 O
ANISOU 2084 O LEU A1077 13882 15578 11130 -4883 899 -398 O
ATOM 2085 CB LEU A1077 -23.193 143.343 164.783 1.00 97.10 C
ANISOU 2085 CB LEU A1077 12853 13895 10146 -4720 870 -588 C
ATOM 2086 CG LEU A1077 -22.195 143.026 163.675 1.00100.76 C
ANISOU 2086 CG LEU A1077 13507 14046 10731 -4755 886 -655 C
ATOM 2087 CD1 LEU A1077 -21.754 144.289 162.975 1.00 99.63 C
ANISOU 2087 CD1 LEU A1077 13297 13884 10673 -4487 834 -699 C
ATOM 2088 CD2 LEU A1077 -20.994 142.256 164.199 1.00101.88 C
ANISOU 2088 CD2 LEU A1077 13908 13799 11001 -4767 933 -671 C
ATOM 2089 N GLN A1078 -25.912 143.300 166.399 1.00103.66 N
ANISOU 2089 N GLN A1078 13158 15721 10508 -4902 842 -423 N
ATOM 2090 CA GLN A1078 -26.786 143.779 167.470 1.00104.43 C
ANISOU 2090 CA GLN A1078 12979 16282 10417 -4772 820 -366 C
ATOM 2091 C GLN A1078 -27.228 142.584 168.324 1.00110.05 C
ANISOU 2091 C GLN A1078 13673 17145 10995 -5117 857 -238 C
ATOM 2092 O GLN A1078 -27.040 142.599 169.540 1.00109.95 O
ANISOU 2092 O GLN A1078 13597 17225 10954 -5000 866 -191 O
ATOM 2093 CB GLN A1078 -27.996 144.494 166.853 1.00107.04 C
ANISOU 2093 CB GLN A1078 13036 17092 10542 -4706 774 -376 C
ATOM 2094 CG GLN A1078 -28.799 145.351 167.821 1.00120.94 C
ANISOU 2094 CG GLN A1078 14509 19333 12109 -4390 729 -364 C
ATOM 2095 CD GLN A1078 -29.887 146.148 167.138 1.00145.11 C
ANISOU 2095 CD GLN A1078 17323 22849 14965 -4249 673 -393 C
ATOM 2096 OE1 GLN A1078 -29.958 146.257 165.901 1.00143.21 O
ANISOU 2096 OE1 GLN A1078 17132 22522 14759 -4341 661 -433 O
ATOM 2097 NE2 GLN A1078 -30.754 146.746 167.938 1.00138.39 N
ANISOU 2097 NE2 GLN A1078 16196 22508 13878 -3987 632 -380 N
ATOM 2098 N GLN A1079 -27.722 141.515 167.657 1.00108.07 N
ANISOU 2098 N GLN A1079 13511 16886 10664 -5554 866 -179 N
ATOM 2099 CA GLN A1079 -28.165 140.244 168.244 1.00109.56 C
ANISOU 2099 CA GLN A1079 13748 17164 10715 -5974 871 -39 C
ATOM 2100 C GLN A1079 -26.985 139.444 168.863 1.00111.37 C
ANISOU 2100 C GLN A1079 14323 16860 11134 -6008 895 -36 C
ATOM 2101 O GLN A1079 -27.230 138.430 169.527 1.00113.16 O
ANISOU 2101 O GLN A1079 14649 17084 11264 -6336 884 84 O
ATOM 2102 CB GLN A1079 -28.887 139.389 167.183 1.00112.75 C
ANISOU 2102 CB GLN A1079 14205 17652 10983 -6430 841 11 C
ATOM 2103 CG GLN A1079 -30.276 139.876 166.777 1.00127.99 C
ANISOU 2103 CG GLN A1079 15760 20215 12654 -6502 816 57 C
ATOM 2104 CD GLN A1079 -30.880 139.007 165.692 1.00150.57 C
ANISOU 2104 CD GLN A1079 18706 23109 15394 -6975 778 101 C
ATOM 2105 OE1 GLN A1079 -30.365 138.910 164.567 1.00145.13 O
ANISOU 2105 OE1 GLN A1079 18273 22018 14852 -7015 772 1 O
ATOM 2106 NE2 GLN A1079 -32.008 138.372 165.997 1.00145.84 N
ANISOU 2106 NE2 GLN A1079 17885 23023 14505 -7349 743 258 N
ATOM 2107 N LYS A1080 -25.719 139.905 168.636 1.00103.64 N
ANISOU 2107 N LYS A1080 13525 15448 10405 -5678 918 -160 N
ATOM 2108 CA LYS A1080 -24.450 139.338 169.126 1.00101.93 C
ANISOU 2108 CA LYS A1080 13612 14737 10380 -5599 944 -186 C
ATOM 2109 C LYS A1080 -24.063 138.001 168.437 1.00106.39 C
ANISOU 2109 C LYS A1080 14538 14910 10976 -5916 934 -188 C
ATOM 2110 O LYS A1080 -23.349 137.182 169.029 1.00106.36 O
ANISOU 2110 O LYS A1080 14784 14602 11026 -5979 937 -156 O
ATOM 2111 CB LYS A1080 -24.413 139.223 170.672 1.00104.87 C
ANISOU 2111 CB LYS A1080 13913 15213 10718 -5523 958 -100 C
ATOM 2112 CG LYS A1080 -24.570 140.565 171.387 1.00120.12 C
ANISOU 2112 CG LYS A1080 15573 17413 12656 -5111 954 -141 C
ATOM 2113 CD LYS A1080 -23.855 140.622 172.737 1.00129.04 C
ANISOU 2113 CD LYS A1080 16745 18420 13865 -4908 973 -120 C
ATOM 2114 CE LYS A1080 -23.676 142.047 173.220 1.00142.67 C
ANISOU 2114 CE LYS A1080 18287 20294 15628 -4462 944 -196 C
ATOM 2115 NZ LYS A1080 -22.673 142.811 172.410 1.00151.18 N
ANISOU 2115 NZ LYS A1080 19505 21022 16916 -4216 923 -319 N
ATOM 2116 N ARG A1081 -24.490 137.808 167.170 1.00102.82 N
ANISOU 2116 N ARG A1081 14133 14448 10486 -6077 911 -237 N
ATOM 2117 CA ARG A1081 -24.171 136.610 166.389 1.00103.55 C
ANISOU 2117 CA ARG A1081 14585 14176 10583 -6342 880 -266 C
ATOM 2118 C ARG A1081 -22.930 136.917 165.556 1.00108.85 C
ANISOU 2118 C ARG A1081 15421 14488 11448 -6046 911 -414 C
ATOM 2119 O ARG A1081 -23.027 137.080 164.334 1.00108.83 O
ANISOU 2119 O ARG A1081 15390 14515 11447 -6045 905 -488 O
ATOM 2120 CB ARG A1081 -25.346 136.238 165.489 1.00103.30 C
ANISOU 2120 CB ARG A1081 14488 14401 10359 -6720 826 -223 C
ATOM 2121 CG ARG A1081 -26.579 135.774 166.232 1.00112.55 C
ANISOU 2121 CG ARG A1081 15485 15982 11297 -7078 785 -51 C
ATOM 2122 CD ARG A1081 -27.815 136.211 165.490 1.00118.42 C
ANISOU 2122 CD ARG A1081 15945 17198 11852 -7277 758 -17 C
ATOM 2123 NE ARG A1081 -29.032 135.922 166.238 1.00129.37 N
ANISOU 2123 NE ARG A1081 17079 19094 12982 -7590 725 162 N
ATOM 2124 CZ ARG A1081 -29.699 134.779 166.157 1.00148.90 C
ANISOU 2124 CZ ARG A1081 19688 21619 15268 -8117 644 294 C
ATOM 2125 NH1 ARG A1081 -29.264 133.804 165.370 1.00140.02 N
ANISOU 2125 NH1 ARG A1081 18991 20022 14190 -8366 576 248 N
ATOM 2126 NH2 ARG A1081 -30.808 134.602 166.859 1.00139.31 N
ANISOU 2126 NH2 ARG A1081 18189 20944 13797 -8402 615 475 N
ATOM 2127 N TRP A1082 -21.762 137.030 166.236 1.00105.67 N
ANISOU 2127 N TRP A1082 15162 13790 11196 -5789 946 -448 N
ATOM 2128 CA TRP A1082 -20.462 137.409 165.671 1.00104.24 C
ANISOU 2128 CA TRP A1082 15095 13324 11186 -5479 980 -563 C
ATOM 2129 C TRP A1082 -20.020 136.565 164.466 1.00109.15 C
ANISOU 2129 C TRP A1082 16005 13670 11796 -5575 961 -652 C
ATOM 2130 O TRP A1082 -19.809 137.132 163.395 1.00107.51 O
ANISOU 2130 O TRP A1082 15724 13500 11625 -5471 971 -728 O
ATOM 2131 CB TRP A1082 -19.359 137.449 166.752 1.00102.56 C
ANISOU 2131 CB TRP A1082 14973 12901 11096 -5233 1014 -557 C
ATOM 2132 CG TRP A1082 -19.760 138.060 168.074 1.00103.56 C
ANISOU 2132 CG TRP A1082 14858 13275 11215 -5139 1023 -474 C
ATOM 2133 CD1 TRP A1082 -19.684 137.465 169.299 1.00107.04 C
ANISOU 2133 CD1 TRP A1082 15367 13665 11638 -5172 1028 -397 C
ATOM 2134 CD2 TRP A1082 -20.271 139.392 168.307 1.00102.66 C
ANISOU 2134 CD2 TRP A1082 14414 13499 11095 -4972 1016 -468 C
ATOM 2135 NE1 TRP A1082 -20.124 138.330 170.278 1.00105.93 N
ANISOU 2135 NE1 TRP A1082 14941 13829 11477 -5034 1033 -346 N
ATOM 2136 CE2 TRP A1082 -20.501 139.514 169.697 1.00106.49 C
ANISOU 2136 CE2 TRP A1082 14777 14137 11549 -4899 1019 -394 C
ATOM 2137 CE3 TRP A1082 -20.592 140.482 167.470 1.00103.19 C
ANISOU 2137 CE3 TRP A1082 14292 13752 11162 -4867 995 -518 C
ATOM 2138 CZ2 TRP A1082 -21.025 140.681 170.273 1.00105.21 C
ANISOU 2138 CZ2 TRP A1082 14325 14302 11348 -4696 998 -385 C
ATOM 2139 CZ3 TRP A1082 -21.141 141.625 168.039 1.00104.17 C
ANISOU 2139 CZ3 TRP A1082 14147 14185 11247 -4681 966 -502 C
ATOM 2140 CH2 TRP A1082 -21.342 141.721 169.426 1.00104.98 C
ANISOU 2140 CH2 TRP A1082 14145 14429 11312 -4581 965 -443 C
ATOM 2141 N ASP A1083 -19.901 135.235 164.629 1.00109.32 N
ANISOU 2141 N ASP A1083 16365 13421 11750 -5772 919 -641 N
ATOM 2142 CA ASP A1083 -19.494 134.278 163.586 1.00111.58 C
ANISOU 2142 CA ASP A1083 16997 13408 11990 -5855 873 -736 C
ATOM 2143 C ASP A1083 -20.384 134.355 162.340 1.00117.56 C
ANISOU 2143 C ASP A1083 17683 14344 12639 -6092 834 -762 C
ATOM 2144 O ASP A1083 -19.869 134.346 161.218 1.00117.30 O
ANISOU 2144 O ASP A1083 17782 14171 12615 -6002 830 -875 O
ATOM 2145 CB ASP A1083 -19.472 132.841 164.139 1.00116.62 C
ANISOU 2145 CB ASP A1083 18039 13731 12539 -6062 797 -696 C
ATOM 2146 CG ASP A1083 -18.707 132.697 165.442 1.00136.28 C
ANISOU 2146 CG ASP A1083 20602 16061 15117 -5850 831 -659 C
ATOM 2147 OD1 ASP A1083 -17.455 132.686 165.396 1.00137.35 O
ANISOU 2147 OD1 ASP A1083 20846 15986 15355 -5506 874 -753 O
ATOM 2148 OD2 ASP A1083 -19.361 132.620 166.514 1.00145.94 O
ANISOU 2148 OD2 ASP A1083 21744 17414 16294 -6023 817 -527 O
ATOM 2149 N GLU A1084 -21.718 134.449 162.555 1.00115.69 N
ANISOU 2149 N GLU A1084 17221 14451 12285 -6383 807 -654 N
ATOM 2150 CA GLU A1084 -22.785 134.575 161.550 1.00116.64 C
ANISOU 2150 CA GLU A1084 17208 14833 12277 -6641 768 -649 C
ATOM 2151 C GLU A1084 -22.571 135.872 160.729 1.00117.89 C
ANISOU 2151 C GLU A1084 17092 15175 12526 -6361 828 -730 C
ATOM 2152 O GLU A1084 -22.536 135.825 159.498 1.00118.19 O
ANISOU 2152 O GLU A1084 17200 15170 12535 -6401 810 -812 O
ATOM 2153 CB GLU A1084 -24.148 134.608 162.281 1.00119.50 C
ANISOU 2153 CB GLU A1084 17319 15603 12481 -6951 739 -493 C
ATOM 2154 CG GLU A1084 -25.382 134.251 161.465 1.00132.16 C
ANISOU 2154 CG GLU A1084 18895 17434 13884 -7372 663 -446 C
ATOM 2155 CD GLU A1084 -26.682 134.147 162.254 1.00153.37 C
ANISOU 2155 CD GLU A1084 21325 20573 16374 -7705 628 -270 C
ATOM 2156 OE1 GLU A1084 -27.752 134.444 161.673 1.00151.65 O
ANISOU 2156 OE1 GLU A1084 20861 20753 16005 -7905 606 -231 O
ATOM 2157 OE2 GLU A1084 -26.640 133.751 163.443 1.00142.47 O
ANISOU 2157 OE2 GLU A1084 19984 19178 14972 -7776 621 -164 O
ATOM 2158 N ALA A1085 -22.386 137.009 161.425 1.00111.42 N
ANISOU 2158 N ALA A1085 15990 14536 11808 -6078 883 -705 N
ATOM 2159 CA ALA A1085 -22.145 138.323 160.839 1.00108.97 C
ANISOU 2159 CA ALA A1085 15448 14374 11583 -5810 914 -759 C
ATOM 2160 C ALA A1085 -20.853 138.339 160.018 1.00111.09 C
ANISOU 2160 C ALA A1085 15897 14340 11974 -5586 941 -866 C
ATOM 2161 O ALA A1085 -20.843 138.904 158.925 1.00110.71 O
ANISOU 2161 O ALA A1085 15747 14378 11940 -5504 943 -917 O
ATOM 2162 CB ALA A1085 -22.079 139.372 161.939 1.00108.27 C
ANISOU 2162 CB ALA A1085 15103 14474 11561 -5564 934 -707 C
ATOM 2163 N ALA A1086 -19.779 137.699 160.535 1.00106.27 N
ANISOU 2163 N ALA A1086 15539 13407 11430 -5480 958 -894 N
ATOM 2164 CA ALA A1086 -18.457 137.579 159.900 1.00104.85 C
ANISOU 2164 CA ALA A1086 15527 12981 11329 -5246 986 -990 C
ATOM 2165 C ALA A1086 -18.506 136.844 158.528 1.00109.27 C
ANISOU 2165 C ALA A1086 16283 13442 11792 -5366 956 -1084 C
ATOM 2166 O ALA A1086 -17.764 137.185 157.598 1.00107.43 O
ANISOU 2166 O ALA A1086 16042 13188 11590 -5182 980 -1158 O
ATOM 2167 CB ALA A1086 -17.510 136.853 160.846 1.00105.55 C
ANISOU 2167 CB ALA A1086 15850 12788 11466 -5121 1000 -993 C
ATOM 2168 N VAL A1087 -19.383 135.834 158.430 1.00107.49 N
ANISOU 2168 N VAL A1087 16240 13169 11434 -5688 893 -1074 N
ATOM 2169 CA VAL A1087 -19.603 134.992 157.256 1.00108.85 C
ANISOU 2169 CA VAL A1087 16650 13223 11485 -5855 835 -1162 C
ATOM 2170 C VAL A1087 -20.272 135.794 156.125 1.00112.29 C
ANISOU 2170 C VAL A1087 16824 13955 11886 -5919 842 -1176 C
ATOM 2171 O VAL A1087 -19.879 135.689 154.956 1.00112.15 O
ANISOU 2171 O VAL A1087 16889 13883 11840 -5837 840 -1276 O
ATOM 2172 CB VAL A1087 -20.420 133.742 157.700 1.00114.90 C
ANISOU 2172 CB VAL A1087 17700 13844 12112 -6229 739 -1116 C
ATOM 2173 CG1 VAL A1087 -21.266 133.150 156.571 1.00116.80 C
ANISOU 2173 CG1 VAL A1087 18113 14068 12198 -6514 652 -1173 C
ATOM 2174 CG2 VAL A1087 -19.506 132.690 158.314 1.00115.47 C
ANISOU 2174 CG2 VAL A1087 18151 13525 12199 -6119 709 -1144 C
ATOM 2175 N ASN A1088 -21.278 136.595 156.503 1.00107.70 N
ANISOU 2175 N ASN A1088 15927 13705 11290 -6041 848 -1077 N
ATOM 2176 CA ASN A1088 -22.106 137.414 155.633 1.00106.48 C
ANISOU 2176 CA ASN A1088 15497 13874 11086 -6100 846 -1070 C
ATOM 2177 C ASN A1088 -21.363 138.593 155.026 1.00106.98 C
ANISOU 2177 C ASN A1088 15377 14005 11265 -5781 893 -1107 C
ATOM 2178 O ASN A1088 -21.512 138.851 153.836 1.00105.44 O
ANISOU 2178 O ASN A1088 15083 13954 11025 -5803 884 -1143 O
ATOM 2179 CB ASN A1088 -23.306 137.897 156.422 1.00106.65 C
ANISOU 2179 CB ASN A1088 15239 14244 11038 -6252 833 -954 C
ATOM 2180 CG ASN A1088 -24.482 138.183 155.558 1.00127.12 C
ANISOU 2180 CG ASN A1088 17682 17143 13473 -6510 792 -937 C
ATOM 2181 OD1 ASN A1088 -24.788 139.346 155.263 1.00125.20 O
ANISOU 2181 OD1 ASN A1088 17139 17213 13218 -6403 803 -916 O
ATOM 2182 ND2 ASN A1088 -25.156 137.121 155.131 1.00115.95 N
ANISOU 2182 ND2 ASN A1088 16492 15642 11922 -6858 729 -943 N
ATOM 2183 N LEU A1089 -20.573 139.311 155.844 1.00102.44 N
ANISOU 2183 N LEU A1089 14751 13345 10828 -5509 932 -1085 N
ATOM 2184 CA LEU A1089 -19.797 140.475 155.423 1.00100.65 C
ANISOU 2184 CA LEU A1089 14366 13176 10700 -5246 954 -1092 C
ATOM 2185 C LEU A1089 -18.695 140.092 154.447 1.00106.01 C
ANISOU 2185 C LEU A1089 15212 13682 11385 -5127 977 -1181 C
ATOM 2186 O LEU A1089 -18.264 140.936 153.658 1.00105.85 O
ANISOU 2186 O LEU A1089 15060 13770 11388 -5009 982 -1185 O
ATOM 2187 CB LEU A1089 -19.193 141.196 156.634 1.00 99.04 C
ANISOU 2187 CB LEU A1089 14048 12961 10621 -5028 966 -1028 C
ATOM 2188 CG LEU A1089 -20.141 142.015 157.500 1.00103.40 C
ANISOU 2188 CG LEU A1089 14384 13747 11157 -5047 936 -949 C
ATOM 2189 CD1 LEU A1089 -19.514 142.300 158.850 1.00102.65 C
ANISOU 2189 CD1 LEU A1089 14273 13562 11167 -4857 943 -904 C
ATOM 2190 CD2 LEU A1089 -20.501 143.330 156.833 1.00104.92 C
ANISOU 2190 CD2 LEU A1089 14354 14182 11329 -4976 892 -932 C
ATOM 2191 N ALA A1090 -18.249 138.819 154.493 1.00103.46 N
ANISOU 2191 N ALA A1090 15187 13106 11017 -5155 980 -1250 N
ATOM 2192 CA ALA A1090 -17.210 138.272 153.616 1.00103.85 C
ANISOU 2192 CA ALA A1090 15419 13013 11028 -5002 996 -1353 C
ATOM 2193 C ALA A1090 -17.731 138.000 152.177 1.00108.63 C
ANISOU 2193 C ALA A1090 16066 13700 11508 -5147 964 -1428 C
ATOM 2194 O ALA A1090 -16.939 137.800 151.246 1.00109.54 O
ANISOU 2194 O ALA A1090 16288 13768 11565 -5007 974 -1520 O
ATOM 2195 CB ALA A1090 -16.639 137.006 154.232 1.00105.85 C
ANISOU 2195 CB ALA A1090 16008 12960 11251 -4945 988 -1411 C
ATOM 2196 N LYS A1091 -19.060 138.012 152.006 1.00104.04 N
ANISOU 2196 N LYS A1091 15376 13284 10871 -5415 927 -1386 N
ATOM 2197 CA LYS A1091 -19.727 137.792 150.723 1.00104.19 C
ANISOU 2197 CA LYS A1091 15396 13425 10768 -5602 889 -1438 C
ATOM 2198 C LYS A1091 -19.991 139.125 149.979 1.00105.30 C
ANISOU 2198 C LYS A1091 15202 13870 10939 -5541 906 -1389 C
ATOM 2199 O LYS A1091 -20.458 139.106 148.838 1.00104.58 O
ANISOU 2199 O LYS A1091 15072 13913 10751 -5662 883 -1428 O
ATOM 2200 CB LYS A1091 -21.038 136.989 150.933 1.00107.62 C
ANISOU 2200 CB LYS A1091 15913 13886 11093 -5966 825 -1405 C
ATOM 2201 CG LYS A1091 -20.827 135.587 151.497 1.00110.53 C
ANISOU 2201 CG LYS A1091 16683 13920 11392 -6088 768 -1456 C
ATOM 2202 CD LYS A1091 -22.128 134.937 151.917 1.00118.80 C
ANISOU 2202 CD LYS A1091 17791 15027 12320 -6496 690 -1386 C
ATOM 2203 CE LYS A1091 -21.882 133.696 152.747 1.00130.54 C
ANISOU 2203 CE LYS A1091 19704 16148 13746 -6626 613 -1408 C
ATOM 2204 NZ LYS A1091 -23.144 133.071 153.230 1.00137.86 N
ANISOU 2204 NZ LYS A1091 20664 17163 14554 -7064 530 -1293 N
ATOM 2205 N SER A1092 -19.677 140.271 150.624 1.00100.78 N
ANISOU 2205 N SER A1092 14415 13389 10489 -5358 932 -1304 N
ATOM 2206 CA SER A1092 -19.903 141.623 150.091 1.00100.27 C
ANISOU 2206 CA SER A1092 14076 13569 10453 -5285 920 -1242 C
ATOM 2207 C SER A1092 -18.992 142.025 148.919 1.00106.39 C
ANISOU 2207 C SER A1092 14821 14373 11230 -5137 935 -1270 C
ATOM 2208 O SER A1092 -18.008 141.334 148.634 1.00107.35 O
ANISOU 2208 O SER A1092 15105 14345 11338 -5031 967 -1337 O
ATOM 2209 CB SER A1092 -19.787 142.657 151.208 1.00101.55 C
ANISOU 2209 CB SER A1092 14079 13777 10728 -5147 910 -1145 C
ATOM 2210 OG SER A1092 -18.452 142.781 151.671 1.00107.04 O
ANISOU 2210 OG SER A1092 14836 14304 11530 -4943 937 -1131 O
ATOM 2211 N ARG A1093 -19.323 143.160 148.250 1.00103.09 N
ANISOU 2211 N ARG A1093 14191 14169 10808 -5119 904 -1213 N
ATOM 2212 CA ARG A1093 -18.509 143.762 147.183 1.00103.23 C
ANISOU 2212 CA ARG A1093 14135 14270 10819 -5005 905 -1200 C
ATOM 2213 C ARG A1093 -17.344 144.503 147.863 1.00106.21 C
ANISOU 2213 C ARG A1093 14464 14580 11311 -4813 904 -1116 C
ATOM 2214 O ARG A1093 -16.283 144.671 147.265 1.00105.09 O
ANISOU 2214 O ARG A1093 14307 14467 11155 -4709 922 -1104 O
ATOM 2215 CB ARG A1093 -19.336 144.745 146.336 1.00104.61 C
ANISOU 2215 CB ARG A1093 14121 14679 10947 -5066 851 -1148 C
ATOM 2216 CG ARG A1093 -19.289 144.464 144.845 1.00121.95 C
ANISOU 2216 CG ARG A1093 16331 16984 13019 -5152 862 -1220 C
ATOM 2217 CD ARG A1093 -20.242 145.359 144.078 1.00144.42 C
ANISOU 2217 CD ARG A1093 18994 20067 15812 -5212 807 -1166 C
ATOM 2218 NE ARG A1093 -19.601 146.606 143.646 1.00166.61 N
ANISOU 2218 NE ARG A1093 21688 22955 18663 -5086 768 -1066 N
ATOM 2219 CZ ARG A1093 -19.381 146.944 142.376 1.00187.11 C
ANISOU 2219 CZ ARG A1093 24201 25713 21179 -5108 749 -1049 C
ATOM 2220 NH1 ARG A1093 -19.758 146.136 141.389 1.00178.68 N
ANISOU 2220 NH1 ARG A1093 23151 24748 19991 -5231 771 -1141 N
ATOM 2221 NH2 ARG A1093 -18.794 148.098 142.083 1.00171.46 N
ANISOU 2221 NH2 ARG A1093 22127 23794 19227 -5025 697 -931 N
ATOM 2222 N TRP A1094 -17.557 144.924 149.129 1.00103.31 N
ANISOU 2222 N TRP A1094 14065 14149 11038 -4773 879 -1055 N
ATOM 2223 CA TRP A1094 -16.575 145.580 149.982 1.00103.06 C
ANISOU 2223 CA TRP A1094 14009 14035 11115 -4617 864 -976 C
ATOM 2224 C TRP A1094 -15.396 144.638 150.190 1.00108.39 C
ANISOU 2224 C TRP A1094 14825 14565 11794 -4525 936 -1029 C
ATOM 2225 O TRP A1094 -14.251 145.083 150.115 1.00108.49 O
ANISOU 2225 O TRP A1094 14793 14602 11828 -4406 939 -977 O
ATOM 2226 CB TRP A1094 -17.213 145.984 151.334 1.00101.33 C
ANISOU 2226 CB TRP A1094 13751 13779 10970 -4592 820 -927 C
ATOM 2227 CG TRP A1094 -16.250 146.240 152.470 1.00101.51 C
ANISOU 2227 CG TRP A1094 13812 13657 11099 -4455 819 -880 C
ATOM 2228 CD1 TRP A1094 -15.194 147.103 152.473 1.00103.74 C
ANISOU 2228 CD1 TRP A1094 14051 13924 11441 -4348 775 -795 C
ATOM 2229 CD2 TRP A1094 -16.301 145.663 153.790 1.00101.25 C
ANISOU 2229 CD2 TRP A1094 13861 13495 11113 -4431 853 -900 C
ATOM 2230 NE1 TRP A1094 -14.558 147.069 153.693 1.00102.58 N
ANISOU 2230 NE1 TRP A1094 13955 13644 11378 -4251 783 -773 N
ATOM 2231 CE2 TRP A1094 -15.219 146.198 154.523 1.00104.20 C
ANISOU 2231 CE2 TRP A1094 14238 13773 11580 -4287 835 -839 C
ATOM 2232 CE3 TRP A1094 -17.146 144.726 154.420 1.00103.00 C
ANISOU 2232 CE3 TRP A1094 14156 13685 11294 -4541 889 -951 C
ATOM 2233 CZ2 TRP A1094 -14.961 145.833 155.853 1.00102.98 C
ANISOU 2233 CZ2 TRP A1094 14153 13486 11487 -4223 862 -841 C
ATOM 2234 CZ3 TRP A1094 -16.888 144.369 155.737 1.00103.81 C
ANISOU 2234 CZ3 TRP A1094 14331 13658 11454 -4489 912 -941 C
ATOM 2235 CH2 TRP A1094 -15.802 144.912 156.435 1.00103.36 C
ANISOU 2235 CH2 TRP A1094 14275 13500 11498 -4318 904 -893 C
ATOM 2236 N TYR A1095 -15.675 143.349 150.438 1.00106.05 N
ANISOU 2236 N TYR A1095 14705 14134 11455 -4582 982 -1128 N
ATOM 2237 CA TYR A1095 -14.640 142.346 150.647 1.00107.24 C
ANISOU 2237 CA TYR A1095 15037 14127 11583 -4463 1036 -1198 C
ATOM 2238 C TYR A1095 -13.926 142.006 149.338 1.00114.57 C
ANISOU 2238 C TYR A1095 15993 15142 12395 -4382 1062 -1265 C
ATOM 2239 O TYR A1095 -12.704 141.866 149.332 1.00115.06 O
ANISOU 2239 O TYR A1095 16080 15202 12434 -4197 1097 -1273 O
ATOM 2240 CB TYR A1095 -15.222 141.082 151.299 1.00109.27 C
ANISOU 2240 CB TYR A1095 15523 14187 11807 -4567 1046 -1278 C
ATOM 2241 CG TYR A1095 -14.168 140.087 151.732 1.00111.69 C
ANISOU 2241 CG TYR A1095 16052 14295 12091 -4406 1082 -1347 C
ATOM 2242 CD1 TYR A1095 -13.622 140.133 153.009 1.00113.06 C
ANISOU 2242 CD1 TYR A1095 16248 14351 12357 -4296 1099 -1298 C
ATOM 2243 CD2 TYR A1095 -13.716 139.095 150.864 1.00114.15 C
ANISOU 2243 CD2 TYR A1095 16562 14538 12271 -4336 1092 -1469 C
ATOM 2244 CE1 TYR A1095 -12.638 139.232 153.410 1.00115.02 C
ANISOU 2244 CE1 TYR A1095 16701 14431 12572 -4118 1129 -1362 C
ATOM 2245 CE2 TYR A1095 -12.729 138.190 151.251 1.00116.14 C
ANISOU 2245 CE2 TYR A1095 17033 14618 12477 -4132 1113 -1543 C
ATOM 2246 CZ TYR A1095 -12.204 138.252 152.533 1.00123.38 C
ANISOU 2246 CZ TYR A1095 17961 15428 13490 -4025 1134 -1486 C
ATOM 2247 OH TYR A1095 -11.251 137.352 152.944 1.00126.25 O
ANISOU 2247 OH TYR A1095 18547 15627 13794 -3806 1150 -1559 O
ATOM 2248 N ASN A1096 -14.684 141.866 148.237 1.00112.92 N
ANISOU 2248 N ASN A1096 15769 15039 12095 -4510 1045 -1313 N
ATOM 2249 CA ASN A1096 -14.155 141.521 146.912 1.00114.28 C
ANISOU 2249 CA ASN A1096 15964 15324 12135 -4442 1064 -1387 C
ATOM 2250 C ASN A1096 -13.124 142.531 146.380 1.00117.78 C
ANISOU 2250 C ASN A1096 16188 15989 12574 -4314 1070 -1285 C
ATOM 2251 O ASN A1096 -12.172 142.119 145.712 1.00118.89 O
ANISOU 2251 O ASN A1096 16348 16223 12602 -4158 1106 -1335 O
ATOM 2252 CB ASN A1096 -15.304 141.325 145.912 1.00116.37 C
ANISOU 2252 CB ASN A1096 16235 15668 12313 -4637 1033 -1443 C
ATOM 2253 CG ASN A1096 -14.925 140.623 144.635 1.00141.60 C
ANISOU 2253 CG ASN A1096 19523 18932 15346 -4581 1044 -1559 C
ATOM 2254 OD1 ASN A1096 -14.202 139.617 144.630 1.00138.52 O
ANISOU 2254 OD1 ASN A1096 19338 18424 14868 -4423 1065 -1669 O
ATOM 2255 ND2 ASN A1096 -15.452 141.116 143.524 1.00133.64 N
ANISOU 2255 ND2 ASN A1096 18382 18118 14278 -4693 1022 -1547 N
ATOM 2256 N GLN A1097 -13.306 143.837 146.697 1.00112.41 N
ANISOU 2256 N GLN A1097 15311 15403 11996 -4378 1022 -1139 N
ATOM 2257 CA GLN A1097 -12.443 144.948 146.270 1.00111.61 C
ANISOU 2257 CA GLN A1097 15012 15501 11895 -4328 991 -1002 C
ATOM 2258 C GLN A1097 -11.243 145.186 147.201 1.00114.10 C
ANISOU 2258 C GLN A1097 15296 15788 12270 -4197 999 -920 C
ATOM 2259 O GLN A1097 -10.154 145.481 146.710 1.00114.23 O
ANISOU 2259 O GLN A1097 15192 15997 12213 -4124 1004 -846 O
ATOM 2260 CB GLN A1097 -13.256 146.246 146.107 1.00112.16 C
ANISOU 2260 CB GLN A1097 14943 15649 12024 -4462 900 -886 C
ATOM 2261 CG GLN A1097 -14.337 146.193 145.022 1.00127.38 C
ANISOU 2261 CG GLN A1097 16856 17672 13870 -4587 888 -947 C
ATOM 2262 CD GLN A1097 -15.419 147.244 145.184 1.00148.94 C
ANISOU 2262 CD GLN A1097 19499 20436 16657 -4682 798 -867 C
ATOM 2263 OE1 GLN A1097 -15.655 147.795 146.271 1.00145.39 O
ANISOU 2263 OE1 GLN A1097 19049 19884 16310 -4655 746 -808 O
ATOM 2264 NE2 GLN A1097 -16.137 147.513 144.104 1.00140.96 N
ANISOU 2264 NE2 GLN A1097 18418 19577 15562 -4772 772 -874 N
ATOM 2265 N THR A1098 -11.451 145.101 148.534 1.00109.28 N
ANISOU 2265 N THR A1098 14771 14972 11777 -4179 995 -921 N
ATOM 2266 CA THR A1098 -10.410 145.299 149.559 1.00108.41 C
ANISOU 2266 CA THR A1098 14645 14813 11734 -4061 1000 -850 C
ATOM 2267 C THR A1098 -10.403 144.110 150.547 1.00111.65 C
ANISOU 2267 C THR A1098 15254 15000 12168 -3966 1063 -964 C
ATOM 2268 O THR A1098 -10.836 144.271 151.689 1.00109.47 O
ANISOU 2268 O THR A1098 15017 14571 12005 -3993 1041 -938 O
ATOM 2269 CB THR A1098 -10.580 146.655 150.271 1.00115.15 C
ANISOU 2269 CB THR A1098 15401 15639 12712 -4131 899 -706 C
ATOM 2270 OG1 THR A1098 -11.933 146.789 150.708 1.00115.22 O
ANISOU 2270 OG1 THR A1098 15468 15522 12788 -4214 868 -747 O
ATOM 2271 CG2 THR A1098 -10.214 147.827 149.394 1.00114.03 C
ANISOU 2271 CG2 THR A1098 15100 15692 12534 -4213 810 -563 C
ATOM 2272 N PRO A1099 -9.927 142.907 150.129 1.00109.84 N
ANISOU 2272 N PRO A1099 15167 14747 11820 -3841 1129 -1090 N
ATOM 2273 CA PRO A1099 -9.965 141.744 151.035 1.00109.86 C
ANISOU 2273 CA PRO A1099 15407 14502 11834 -3759 1165 -1192 C
ATOM 2274 C PRO A1099 -9.123 141.835 152.308 1.00113.18 C
ANISOU 2274 C PRO A1099 15819 14849 12337 -3628 1179 -1130 C
ATOM 2275 O PRO A1099 -9.579 141.363 153.350 1.00112.29 O
ANISOU 2275 O PRO A1099 15847 14518 12299 -3652 1180 -1155 O
ATOM 2276 CB PRO A1099 -9.507 140.584 150.144 1.00113.39 C
ANISOU 2276 CB PRO A1099 16021 14958 12104 -3610 1204 -1338 C
ATOM 2277 CG PRO A1099 -8.731 141.219 149.061 1.00118.43 C
ANISOU 2277 CG PRO A1099 16440 15916 12642 -3536 1214 -1282 C
ATOM 2278 CD PRO A1099 -9.411 142.520 148.798 1.00112.78 C
ANISOU 2278 CD PRO A1099 15517 15312 12024 -3756 1160 -1151 C
ATOM 2279 N ASN A1100 -7.908 142.418 152.227 1.00109.92 N
ANISOU 2279 N ASN A1100 15232 14636 11895 -3506 1185 -1038 N
ATOM 2280 CA ASN A1100 -6.971 142.528 153.355 1.00109.14 C
ANISOU 2280 CA ASN A1100 15100 14518 11852 -3377 1195 -971 C
ATOM 2281 C ASN A1100 -7.524 143.368 154.515 1.00109.61 C
ANISOU 2281 C ASN A1100 15115 14444 12087 -3500 1137 -874 C
ATOM 2282 O ASN A1100 -7.498 142.902 155.666 1.00108.64 O
ANISOU 2282 O ASN A1100 15105 14144 12029 -3433 1156 -898 O
ATOM 2283 CB ASN A1100 -5.600 143.025 152.887 1.00112.43 C
ANISOU 2283 CB ASN A1100 15307 15245 12167 -3268 1202 -874 C
ATOM 2284 CG ASN A1100 -4.939 142.113 151.876 1.00137.48 C
ANISOU 2284 CG ASN A1100 18519 18585 15132 -3070 1265 -983 C
ATOM 2285 OD1 ASN A1100 -4.175 141.209 152.231 1.00133.34 O
ANISOU 2285 OD1 ASN A1100 18111 18033 14520 -2830 1316 -1067 O
ATOM 2286 ND2 ASN A1100 -5.226 142.325 150.593 1.00128.24 N
ANISOU 2286 ND2 ASN A1100 17264 17595 13865 -3142 1257 -991 N
ATOM 2287 N ARG A1101 -8.061 144.581 154.203 1.00103.50 N
ANISOU 2287 N ARG A1101 14197 13754 11374 -3661 1058 -773 N
ATOM 2288 CA ARG A1101 -8.683 145.477 155.186 1.00100.84 C
ANISOU 2288 CA ARG A1101 13831 13308 11175 -3746 978 -695 C
ATOM 2289 C ARG A1101 -9.961 144.833 155.716 1.00104.09 C
ANISOU 2289 C ARG A1101 14381 13538 11630 -3801 1001 -790 C
ATOM 2290 O ARG A1101 -10.105 144.706 156.932 1.00103.32 O
ANISOU 2290 O ARG A1101 14345 13304 11606 -3758 1005 -788 O
ATOM 2291 CB ARG A1101 -8.989 146.857 154.577 1.00 97.80 C
ANISOU 2291 CB ARG A1101 13309 13043 10806 -3876 868 -584 C
ATOM 2292 CG ARG A1101 -9.610 147.859 155.554 1.00 98.44 C
ANISOU 2292 CG ARG A1101 13389 13012 11000 -3916 760 -520 C
ATOM 2293 CD ARG A1101 -9.701 149.238 154.935 1.00105.25 C
ANISOU 2293 CD ARG A1101 14159 13970 11863 -4005 618 -386 C
ATOM 2294 NE ARG A1101 -10.155 150.251 155.889 1.00110.45 N
ANISOU 2294 NE ARG A1101 14858 14501 12606 -3995 491 -343 N
ATOM 2295 CZ ARG A1101 -10.207 151.554 155.630 1.00123.16 C
ANISOU 2295 CZ ARG A1101 16458 16117 14221 -4052 325 -236 C
ATOM 2296 NH1 ARG A1101 -9.834 152.018 154.445 1.00114.02 N
ANISOU 2296 NH1 ARG A1101 15233 15095 12995 -4161 269 -140 N
ATOM 2297 NH2 ARG A1101 -10.635 152.402 156.554 1.00108.10 N
ANISOU 2297 NH2 ARG A1101 14624 14080 12370 -3993 202 -224 N
ATOM 2298 N ALA A1102 -10.868 144.398 154.802 1.00100.35 N
ANISOU 2298 N ALA A1102 13949 13086 11092 -3908 1016 -864 N
ATOM 2299 CA ALA A1102 -12.134 143.767 155.160 1.00 99.73 C
ANISOU 2299 CA ALA A1102 13983 12897 11014 -4018 1028 -938 C
ATOM 2300 C ALA A1102 -11.928 142.561 156.058 1.00104.87 C
ANISOU 2300 C ALA A1102 14826 13355 11663 -3962 1083 -1004 C
ATOM 2301 O ALA A1102 -12.667 142.434 157.032 1.00104.80 O
ANISOU 2301 O ALA A1102 14855 13265 11701 -4035 1071 -995 O
ATOM 2302 CB ALA A1102 -12.917 143.395 153.923 1.00101.19 C
ANISOU 2302 CB ALA A1102 14189 13159 11098 -4142 1034 -1007 C
ATOM 2303 N LYS A1103 -10.875 141.735 155.801 1.00101.93 N
ANISOU 2303 N LYS A1103 14575 12927 11226 -3818 1135 -1065 N
ATOM 2304 CA LYS A1103 -10.544 140.581 156.641 1.00102.36 C
ANISOU 2304 CA LYS A1103 14852 12773 11268 -3735 1171 -1127 C
ATOM 2305 C LYS A1103 -10.216 141.028 158.095 1.00107.63 C
ANISOU 2305 C LYS A1103 15466 13378 12049 -3656 1168 -1046 C
ATOM 2306 O LYS A1103 -10.700 140.393 159.043 1.00107.52 O
ANISOU 2306 O LYS A1103 15597 13197 12057 -3688 1175 -1063 O
ATOM 2307 CB LYS A1103 -9.419 139.731 156.024 1.00105.06 C
ANISOU 2307 CB LYS A1103 15345 13089 11484 -3540 1212 -1222 C
ATOM 2308 N ARG A1104 -9.473 142.165 158.255 1.00104.09 N
ANISOU 2308 N ARG A1104 14816 13070 11664 -3579 1144 -948 N
ATOM 2309 CA ARG A1104 -9.092 142.758 159.556 1.00103.01 C
ANISOU 2309 CA ARG A1104 14617 12892 11630 -3507 1122 -868 C
ATOM 2310 C ARG A1104 -10.289 143.318 160.366 1.00105.73 C
ANISOU 2310 C ARG A1104 14920 13197 12056 -3627 1070 -832 C
ATOM 2311 O ARG A1104 -10.334 143.150 161.593 1.00105.60 O
ANISOU 2311 O ARG A1104 14951 13080 12093 -3587 1075 -818 O
ATOM 2312 CB ARG A1104 -8.015 143.843 159.389 1.00102.69 C
ANISOU 2312 CB ARG A1104 14392 13015 11609 -3436 1080 -765 C
ATOM 2313 CG ARG A1104 -6.631 143.309 159.052 1.00114.40 C
ANISOU 2313 CG ARG A1104 15870 14598 12997 -3267 1137 -776 C
ATOM 2314 CD ARG A1104 -5.538 144.361 159.245 1.00118.33 C
ANISOU 2314 CD ARG A1104 16175 15276 13508 -3236 1085 -641 C
ATOM 2315 NE ARG A1104 -5.608 145.442 158.258 1.00112.73 N
ANISOU 2315 NE ARG A1104 15312 14739 12783 -3378 1007 -551 N
ATOM 2316 CZ ARG A1104 -5.070 145.390 157.043 1.00120.60 C
ANISOU 2316 CZ ARG A1104 16218 15948 13655 -3380 1028 -541 C
ATOM 2317 NH1 ARG A1104 -4.417 144.304 156.644 1.00106.69 N
ANISOU 2317 NH1 ARG A1104 14508 14264 11765 -3215 1123 -634 N
ATOM 2318 NH2 ARG A1104 -5.188 146.417 156.215 1.00106.35 N
ANISOU 2318 NH2 ARG A1104 14285 14284 11840 -3532 944 -442 N
ATOM 2319 N VAL A1105 -11.229 144.012 159.679 1.00100.04 N
ANISOU 2319 N VAL A1105 14097 12586 11326 -3751 1017 -816 N
ATOM 2320 CA VAL A1105 -12.441 144.593 160.271 1.00 98.02 C
ANISOU 2320 CA VAL A1105 13776 12366 11102 -3830 960 -790 C
ATOM 2321 C VAL A1105 -13.361 143.444 160.742 1.00102.63 C
ANISOU 2321 C VAL A1105 14473 12885 11636 -3944 1008 -846 C
ATOM 2322 O VAL A1105 -13.838 143.466 161.882 1.00101.69 O
ANISOU 2322 O VAL A1105 14332 12766 11539 -3952 993 -820 O
ATOM 2323 CB VAL A1105 -13.157 145.552 159.279 1.00100.43 C
ANISOU 2323 CB VAL A1105 13955 12823 11379 -3905 888 -765 C
ATOM 2324 CG1 VAL A1105 -14.387 146.196 159.914 1.00 99.54 C
ANISOU 2324 CG1 VAL A1105 13766 12787 11269 -3926 819 -746 C
ATOM 2325 CG2 VAL A1105 -12.201 146.620 158.750 1.00 99.58 C
ANISOU 2325 CG2 VAL A1105 13765 12769 11301 -3842 822 -687 C
ATOM 2326 N ILE A1106 -13.566 142.433 159.859 1.00100.30 N
ANISOU 2326 N ILE A1106 14310 12541 11258 -4036 1054 -918 N
ATOM 2327 CA ILE A1106 -14.384 141.237 160.090 1.00101.40 C
ANISOU 2327 CA ILE A1106 14607 12595 11326 -4198 1075 -961 C
ATOM 2328 C ILE A1106 -13.872 140.447 161.300 1.00106.92 C
ANISOU 2328 C ILE A1106 15463 13108 12052 -4128 1105 -956 C
ATOM 2329 O ILE A1106 -14.670 140.132 162.191 1.00106.51 O
ANISOU 2329 O ILE A1106 15435 13049 11986 -4245 1095 -922 O
ATOM 2330 CB ILE A1106 -14.519 140.377 158.784 1.00105.32 C
ANISOU 2330 CB ILE A1106 15242 13059 11714 -4310 1087 -1046 C
ATOM 2331 CG1 ILE A1106 -15.561 141.005 157.825 1.00105.34 C
ANISOU 2331 CG1 ILE A1106 15086 13270 11670 -4463 1051 -1038 C
ATOM 2332 CG2 ILE A1106 -14.851 138.898 159.071 1.00106.78 C
ANISOU 2332 CG2 ILE A1106 15708 13046 11817 -4441 1090 -1098 C
ATOM 2333 CD1 ILE A1106 -15.369 140.711 156.337 1.00109.83 C
ANISOU 2333 CD1 ILE A1106 15699 13873 12159 -4488 1056 -1110 C
ATOM 2334 N THR A1107 -12.541 140.168 161.352 1.00104.53 N
ANISOU 2334 N THR A1107 15247 12694 11777 -3931 1138 -979 N
ATOM 2335 CA THR A1107 -11.952 139.408 162.460 1.00104.95 C
ANISOU 2335 CA THR A1107 15457 12570 11849 -3833 1163 -976 C
ATOM 2336 C THR A1107 -12.020 140.192 163.775 1.00107.26 C
ANISOU 2336 C THR A1107 15597 12916 12240 -3773 1149 -891 C
ATOM 2337 O THR A1107 -11.992 139.573 164.837 1.00106.93 O
ANISOU 2337 O THR A1107 15663 12751 12213 -3730 1166 -874 O
ATOM 2338 CB THR A1107 -10.556 138.847 162.149 1.00114.17 C
ANISOU 2338 CB THR A1107 16761 13640 12980 -3615 1200 -1035 C
ATOM 2339 OG1 THR A1107 -10.107 138.110 163.284 1.00112.55 O
ANISOU 2339 OG1 THR A1107 16770 13231 12762 -3544 1213 -1047 O
ATOM 2340 CG2 THR A1107 -9.549 139.906 161.841 1.00113.49 C
ANISOU 2340 CG2 THR A1107 16470 13699 12951 -3436 1208 -985 C
ATOM 2341 N THR A1108 -12.165 141.528 163.708 1.00102.91 N
ANISOU 2341 N THR A1108 14822 12537 11743 -3765 1106 -842 N
ATOM 2342 CA THR A1108 -12.326 142.345 164.913 1.00101.62 C
ANISOU 2342 CA THR A1108 14535 12424 11652 -3692 1068 -777 C
ATOM 2343 C THR A1108 -13.771 142.153 165.435 1.00104.43 C
ANISOU 2343 C THR A1108 14855 12869 11954 -3844 1054 -760 C
ATOM 2344 O THR A1108 -13.940 141.880 166.621 1.00103.87 O
ANISOU 2344 O THR A1108 14788 12781 11895 -3816 1058 -725 O
ATOM 2345 CB THR A1108 -11.851 143.798 164.684 1.00105.97 C
ANISOU 2345 CB THR A1108 14921 13078 12264 -3589 999 -733 C
ATOM 2346 OG1 THR A1108 -10.423 143.783 164.525 1.00102.27 O
ANISOU 2346 OG1 THR A1108 14479 12557 11822 -3466 1020 -723 O
ATOM 2347 CG2 THR A1108 -12.236 144.739 165.837 1.00101.69 C
ANISOU 2347 CG2 THR A1108 14280 12583 11773 -3507 928 -684 C
ATOM 2348 N PHE A1109 -14.787 142.212 164.539 1.00100.23 N
ANISOU 2348 N PHE A1109 14277 12461 11343 -4011 1039 -778 N
ATOM 2349 CA PHE A1109 -16.198 141.989 164.886 1.00100.26 C
ANISOU 2349 CA PHE A1109 14214 12623 11256 -4182 1025 -750 C
ATOM 2350 C PHE A1109 -16.433 140.573 165.461 1.00106.94 C
ANISOU 2350 C PHE A1109 15256 13337 12041 -4348 1061 -740 C
ATOM 2351 O PHE A1109 -17.292 140.391 166.328 1.00107.24 O
ANISOU 2351 O PHE A1109 15237 13496 12013 -4460 1052 -682 O
ATOM 2352 CB PHE A1109 -17.104 142.185 163.653 1.00101.77 C
ANISOU 2352 CB PHE A1109 14318 12988 11362 -4334 1000 -772 C
ATOM 2353 CG PHE A1109 -17.472 143.603 163.278 1.00101.50 C
ANISOU 2353 CG PHE A1109 14087 13138 11341 -4220 938 -764 C
ATOM 2354 CD1 PHE A1109 -18.183 144.410 164.156 1.00103.50 C
ANISOU 2354 CD1 PHE A1109 14180 13571 11573 -4111 883 -728 C
ATOM 2355 CD2 PHE A1109 -17.191 144.099 162.012 1.00102.59 C
ANISOU 2355 CD2 PHE A1109 14211 13288 11482 -4228 922 -795 C
ATOM 2356 CE1 PHE A1109 -18.554 145.708 163.793 1.00103.71 C
ANISOU 2356 CE1 PHE A1109 14073 13745 11588 -3990 799 -729 C
ATOM 2357 CE2 PHE A1109 -17.572 145.395 161.647 1.00104.30 C
ANISOU 2357 CE2 PHE A1109 14277 13659 11694 -4140 846 -779 C
ATOM 2358 CZ PHE A1109 -18.256 146.187 162.537 1.00102.10 C
ANISOU 2358 CZ PHE A1109 13875 13521 11396 -4017 778 -749 C
ATOM 2359 N ARG A1110 -15.683 139.574 164.960 1.00104.41 N
ANISOU 2359 N ARG A1110 15172 12780 11718 -4358 1089 -793 N
ATOM 2360 CA ARG A1110 -15.818 138.195 165.406 1.00105.87 C
ANISOU 2360 CA ARG A1110 15614 12777 11833 -4509 1093 -789 C
ATOM 2361 C ARG A1110 -15.169 137.939 166.769 1.00110.56 C
ANISOU 2361 C ARG A1110 16280 13243 12483 -4377 1113 -746 C
ATOM 2362 O ARG A1110 -15.799 137.325 167.636 1.00111.10 O
ANISOU 2362 O ARG A1110 16420 13303 12489 -4540 1098 -681 O
ATOM 2363 CB ARG A1110 -15.270 137.230 164.347 1.00106.87 C
ANISOU 2363 CB ARG A1110 16009 12685 11913 -4519 1093 -880 C
ATOM 2364 CG ARG A1110 -15.686 135.775 164.572 1.00120.27 C
ANISOU 2364 CG ARG A1110 18021 14182 13495 -4755 1051 -879 C
ATOM 2365 CD ARG A1110 -14.996 134.823 163.617 1.00133.71 C
ANISOU 2365 CD ARG A1110 20039 15626 15137 -4687 1032 -991 C
ATOM 2366 NE ARG A1110 -13.616 134.542 164.019 1.00145.19 N
ANISOU 2366 NE ARG A1110 21649 16879 16636 -4384 1062 -1033 N
ATOM 2367 CZ ARG A1110 -12.540 135.091 163.462 1.00160.57 C
ANISOU 2367 CZ ARG A1110 23510 18868 18633 -4092 1110 -1094 C
ATOM 2368 NH1 ARG A1110 -12.667 135.962 162.468 1.00143.67 N
ANISOU 2368 NH1 ARG A1110 21145 16931 16511 -4074 1127 -1115 N
ATOM 2369 NH2 ARG A1110 -11.328 134.771 163.895 1.00152.09 N
ANISOU 2369 NH2 ARG A1110 22563 17654 17572 -3823 1135 -1122 N
ATOM 2370 N THR A1111 -13.912 138.387 166.951 1.00106.92 N
ANISOU 2370 N THR A1111 15794 12707 12125 -4101 1140 -770 N
ATOM 2371 CA THR A1111 -13.144 138.143 168.178 1.00107.04 C
ANISOU 2371 CA THR A1111 15879 12599 12193 -3949 1161 -737 C
ATOM 2372 C THR A1111 -13.358 139.158 169.312 1.00112.21 C
ANISOU 2372 C THR A1111 16295 13425 12913 -3854 1151 -670 C
ATOM 2373 O THR A1111 -13.193 138.795 170.477 1.00112.07 O
ANISOU 2373 O THR A1111 16325 13351 12905 -3816 1161 -625 O
ATOM 2374 CB THR A1111 -11.645 138.014 167.871 1.00110.55 C
ANISOU 2374 CB THR A1111 16438 12887 12679 -3703 1193 -795 C
ATOM 2375 OG1 THR A1111 -11.137 139.264 167.405 1.00107.60 O
ANISOU 2375 OG1 THR A1111 15846 12662 12375 -3564 1190 -798 O
ATOM 2376 CG2 THR A1111 -11.331 136.898 166.888 1.00109.96 C
ANISOU 2376 CG2 THR A1111 16642 12627 12510 -3730 1193 -878 C
ATOM 2377 N GLY A1112 -13.664 140.409 168.969 1.00109.53 N
ANISOU 2377 N GLY A1112 15731 13277 12610 -3801 1118 -670 N
ATOM 2378 CA GLY A1112 -13.821 141.496 169.932 1.00109.16 C
ANISOU 2378 CA GLY A1112 15492 13375 12609 -3668 1080 -628 C
ATOM 2379 C GLY A1112 -12.499 141.891 170.563 1.00114.03 C
ANISOU 2379 C GLY A1112 16123 13875 13327 -3443 1080 -623 C
ATOM 2380 O GLY A1112 -12.474 142.381 171.696 1.00112.96 O
ANISOU 2380 O GLY A1112 15911 13787 13223 -3333 1054 -590 O
ATOM 2381 N THR A1113 -11.388 141.660 169.822 1.00112.38 N
ANISOU 2381 N THR A1113 16006 13542 13150 -3372 1107 -657 N
ATOM 2382 CA THR A1113 -9.999 141.913 170.224 1.00112.49 C
ANISOU 2382 CA THR A1113 16029 13481 13232 -3178 1114 -646 C
ATOM 2383 C THR A1113 -9.187 142.646 169.137 1.00118.25 C
ANISOU 2383 C THR A1113 16674 14274 13983 -3125 1084 -651 C
ATOM 2384 O THR A1113 -9.567 142.645 167.957 1.00119.06 O
ANISOU 2384 O THR A1113 16749 14440 14049 -3228 1074 -675 O
ATOM 2385 CB THR A1113 -9.280 140.585 170.569 1.00120.24 C
ANISOU 2385 CB THR A1113 17219 14285 14180 -3120 1183 -669 C
ATOM 2386 OG1 THR A1113 -9.347 139.688 169.457 1.00119.62 O
ANISOU 2386 OG1 THR A1113 17285 14138 14028 -3195 1211 -730 O
ATOM 2387 CG2 THR A1113 -9.803 139.928 171.835 1.00119.44 C
ANISOU 2387 CG2 THR A1113 17214 14107 14059 -3168 1199 -637 C
ATOM 2388 N TRP A1114 -8.027 143.209 169.542 1.00114.42 N
ANISOU 2388 N TRP A1114 16144 13789 13542 -2981 1069 -616 N
ATOM 2389 CA TRP A1114 -7.088 143.913 168.669 1.00114.07 C
ANISOU 2389 CA TRP A1114 16006 13840 13497 -2950 1034 -589 C
ATOM 2390 C TRP A1114 -6.061 142.963 168.026 1.00120.44 C
ANISOU 2390 C TRP A1114 16889 14640 14233 -2855 1116 -622 C
ATOM 2391 O TRP A1114 -5.086 143.433 167.435 1.00120.26 O
ANISOU 2391 O TRP A1114 16766 14742 14185 -2797 1101 -581 O
ATOM 2392 CB TRP A1114 -6.373 145.014 169.454 1.00111.66 C
ANISOU 2392 CB TRP A1114 15594 13578 13254 -2879 942 -512 C
ATOM 2393 CG TRP A1114 -7.294 146.028 170.052 1.00111.62 C
ANISOU 2393 CG TRP A1114 15544 13572 13295 -2904 840 -496 C
ATOM 2394 CD1 TRP A1114 -7.617 146.169 171.371 1.00114.19 C
ANISOU 2394 CD1 TRP A1114 15882 13852 13653 -2824 817 -492 C
ATOM 2395 CD2 TRP A1114 -8.010 147.044 169.350 1.00111.11 C
ANISOU 2395 CD2 TRP A1114 15420 13570 13225 -2982 738 -487 C
ATOM 2396 NE1 TRP A1114 -8.479 147.227 171.536 1.00113.27 N
ANISOU 2396 NE1 TRP A1114 15717 13778 13542 -2825 704 -490 N
ATOM 2397 CE2 TRP A1114 -8.739 147.783 170.309 1.00114.85 C
ANISOU 2397 CE2 TRP A1114 15882 14035 13719 -2916 650 -488 C
ATOM 2398 CE3 TRP A1114 -8.109 147.407 167.997 1.00112.44 C
ANISOU 2398 CE3 TRP A1114 15550 13811 13362 -3083 708 -481 C
ATOM 2399 CZ2 TRP A1114 -9.550 148.868 169.957 1.00114.23 C
ANISOU 2399 CZ2 TRP A1114 15771 14010 13621 -2922 524 -490 C
ATOM 2400 CZ3 TRP A1114 -8.908 148.485 167.651 1.00113.87 C
ANISOU 2400 CZ3 TRP A1114 15696 14032 13537 -3117 587 -472 C
ATOM 2401 CH2 TRP A1114 -9.612 149.206 168.624 1.00114.38 C
ANISOU 2401 CH2 TRP A1114 15766 14078 13614 -3025 493 -480 C
ATOM 2402 N ASP A1115 -6.303 141.638 168.112 1.00119.05 N
ANISOU 2402 N ASP A1115 16899 14333 14003 -2839 1190 -692 N
ATOM 2403 CA ASP A1115 -5.461 140.558 167.580 1.00121.03 C
ANISOU 2403 CA ASP A1115 17286 14543 14156 -2699 1255 -752 C
ATOM 2404 C ASP A1115 -5.019 140.736 166.118 1.00125.54 C
ANISOU 2404 C ASP A1115 17789 15264 14646 -2693 1261 -779 C
ATOM 2405 O ASP A1115 -3.917 140.313 165.761 1.00126.12 O
ANISOU 2405 O ASP A1115 17868 15424 14627 -2514 1298 -800 O
ATOM 2406 CB ASP A1115 -6.160 139.191 167.758 1.00124.67 C
ANISOU 2406 CB ASP A1115 18019 14788 14563 -2736 1288 -824 C
ATOM 2407 CG ASP A1115 -6.295 138.677 169.187 1.00136.76 C
ANISOU 2407 CG ASP A1115 19653 16175 16136 -2724 1293 -793 C
ATOM 2408 OD1 ASP A1115 -7.151 137.795 169.420 1.00137.90 O
ANISOU 2408 OD1 ASP A1115 19972 16174 16248 -2866 1288 -810 O
ATOM 2409 OD2 ASP A1115 -5.527 139.137 170.067 1.00142.77 O
ANISOU 2409 OD2 ASP A1115 20321 16979 16946 -2586 1295 -744 O
ATOM 2410 N ALA A1116 -5.881 141.351 165.284 1.00121.72 N
ANISOU 2410 N ALA A1116 17230 14840 14178 -2871 1223 -777 N
ATOM 2411 CA ALA A1116 -5.646 141.618 163.859 1.00122.03 C
ANISOU 2411 CA ALA A1116 17189 15036 14141 -2896 1222 -792 C
ATOM 2412 C ALA A1116 -4.635 142.752 163.610 1.00124.83 C
ANISOU 2412 C ALA A1116 17316 15616 14499 -2863 1179 -689 C
ATOM 2413 O ALA A1116 -4.105 142.886 162.501 1.00124.58 O
ANISOU 2413 O ALA A1116 17198 15764 14373 -2844 1189 -684 O
ATOM 2414 CB ALA A1116 -6.965 141.959 163.186 1.00122.47 C
ANISOU 2414 CB ALA A1116 17230 15088 14214 -3103 1187 -809 C
ATOM 2415 N TYR A1117 -4.394 143.580 164.631 1.00120.54 N
ANISOU 2415 N TYR A1117 16679 15071 14048 -2874 1120 -600 N
ATOM 2416 CA TYR A1117 -3.507 144.729 164.531 1.00120.39 C
ANISOU 2416 CA TYR A1117 16473 15237 14033 -2900 1042 -480 C
ATOM 2417 C TYR A1117 -2.273 144.594 165.464 1.00126.05 C
ANISOU 2417 C TYR A1117 17145 16020 14727 -2747 1061 -431 C
ATOM 2418 O TYR A1117 -1.751 145.585 165.983 1.00125.34 O
ANISOU 2418 O TYR A1117 16926 16035 14662 -2798 974 -316 O
ATOM 2419 CB TYR A1117 -4.318 146.025 164.749 1.00120.11 C
ANISOU 2419 CB TYR A1117 16384 15153 14099 -3055 914 -412 C
ATOM 2420 CG TYR A1117 -5.471 146.202 163.774 1.00120.91 C
ANISOU 2420 CG TYR A1117 16499 15244 14196 -3186 892 -452 C
ATOM 2421 CD1 TYR A1117 -6.730 145.675 164.048 1.00122.48 C
ANISOU 2421 CD1 TYR A1117 16806 15312 14417 -3215 935 -542 C
ATOM 2422 CD2 TYR A1117 -5.310 146.921 162.592 1.00121.48 C
ANISOU 2422 CD2 TYR A1117 16468 15461 14228 -3297 822 -386 C
ATOM 2423 CE1 TYR A1117 -7.790 145.827 163.153 1.00122.70 C
ANISOU 2423 CE1 TYR A1117 16828 15368 14425 -3338 915 -574 C
ATOM 2424 CE2 TYR A1117 -6.368 147.097 161.699 1.00121.78 C
ANISOU 2424 CE2 TYR A1117 16514 15500 14255 -3406 801 -423 C
ATOM 2425 CZ TYR A1117 -7.606 146.547 161.983 1.00126.27 C
ANISOU 2425 CZ TYR A1117 17181 15952 14845 -3419 851 -521 C
ATOM 2426 OH TYR A1117 -8.657 146.722 161.119 1.00123.94 O
ANISOU 2426 OH TYR A1117 16877 15692 14524 -3527 830 -554 O
ATOM 2427 N HIS A 237 -1.799 143.343 165.625 1.00124.71 N
ANISOU 2427 N HIS A 237 17099 15794 14493 -2561 1164 -516 N
ATOM 2428 CA HIS A 237 -0.648 142.922 166.433 1.00125.98 C
ANISOU 2428 CA HIS A 237 17241 16025 14602 -2365 1203 -496 C
ATOM 2429 C HIS A 237 -0.085 141.640 165.811 1.00133.87 C
ANISOU 2429 C HIS A 237 18343 17081 15440 -2144 1300 -597 C
ATOM 2430 O HIS A 237 -0.869 140.827 165.313 1.00133.71 O
ANISOU 2430 O HIS A 237 18506 16903 15393 -2150 1334 -706 O
ATOM 2431 CB HIS A 237 -1.089 142.628 167.881 1.00125.90 C
ANISOU 2431 CB HIS A 237 17356 15783 14697 -2323 1207 -513 C
ATOM 2432 CG HIS A 237 -1.239 143.836 168.755 1.00127.98 C
ANISOU 2432 CG HIS A 237 17514 16035 15079 -2439 1105 -417 C
ATOM 2433 ND1 HIS A 237 -0.139 144.480 169.292 1.00129.83 N
ANISOU 2433 ND1 HIS A 237 17604 16426 15299 -2406 1052 -315 N
ATOM 2434 CD2 HIS A 237 -2.362 144.440 169.208 1.00128.44 C
ANISOU 2434 CD2 HIS A 237 17608 15948 15247 -2564 1039 -416 C
ATOM 2435 CE1 HIS A 237 -0.625 145.475 170.016 1.00128.17 C
ANISOU 2435 CE1 HIS A 237 17377 16122 15198 -2518 944 -262 C
ATOM 2436 NE2 HIS A 237 -1.957 145.490 169.996 1.00127.68 N
ANISOU 2436 NE2 HIS A 237 17417 15889 15208 -2592 935 -326 N
ATOM 2437 N GLU A 238 1.255 141.442 165.857 1.00133.92 N
ANISOU 2437 N GLU A 238 18245 17320 15320 -1940 1333 -565 N
ATOM 2438 CA GLU A 238 1.913 140.249 165.290 1.00136.86 C
ANISOU 2438 CA GLU A 238 18716 17785 15499 -1656 1413 -671 C
ATOM 2439 C GLU A 238 1.353 138.925 165.857 1.00143.15 C
ANISOU 2439 C GLU A 238 19856 18232 16301 -1506 1452 -806 C
ATOM 2440 O GLU A 238 1.055 138.840 167.052 1.00142.22 O
ANISOU 2440 O GLU A 238 19824 17928 16285 -1503 1447 -786 O
ATOM 2441 CB GLU A 238 3.457 140.311 165.393 1.00139.84 C
ANISOU 2441 CB GLU A 238 18876 18545 15713 -1447 1436 -599 C
ATOM 2442 CG GLU A 238 4.046 140.377 166.798 1.00152.24 C
ANISOU 2442 CG GLU A 238 20406 20104 17336 -1367 1429 -531 C
ATOM 2443 CD GLU A 238 5.554 140.208 166.919 1.00180.48 C
ANISOU 2443 CD GLU A 238 23817 24051 20706 -1090 1470 -494 C
ATOM 2444 OE1 GLU A 238 6.271 140.380 165.905 1.00173.78 O
ANISOU 2444 OE1 GLU A 238 22778 23583 19667 -1013 1487 -468 O
ATOM 2445 OE2 GLU A 238 6.020 139.924 168.047 1.00179.05 O
ANISOU 2445 OE2 GLU A 238 23678 23813 20541 -946 1484 -485 O
ATOM 2446 N GLN A 239 1.174 137.920 164.975 1.00142.21 N
ANISOU 2446 N GLN A 239 19949 18019 16065 -1400 1477 -939 N
ATOM 2447 CA GLN A 239 0.616 136.599 165.307 1.00143.50 C
ANISOU 2447 CA GLN A 239 20499 17825 16199 -1294 1483 -1068 C
ATOM 2448 C GLN A 239 1.457 135.826 166.348 1.00149.03 C
ANISOU 2448 C GLN A 239 21338 18457 16828 -996 1506 -1092 C
ATOM 2449 O GLN A 239 1.016 135.695 167.495 1.00147.73 O
ANISOU 2449 O GLN A 239 21315 18036 16781 -1071 1492 -1068 O
ATOM 2450 CB GLN A 239 0.347 135.755 164.036 1.00146.77 C
ANISOU 2450 CB GLN A 239 21116 18191 16458 -1208 1481 -1208 C
ATOM 2451 CG GLN A 239 1.487 135.747 163.006 1.00165.59 C
ANISOU 2451 CG GLN A 239 23336 20957 18622 -931 1515 -1240 C
ATOM 2452 CD GLN A 239 1.136 134.982 161.759 1.00184.85 C
ANISOU 2452 CD GLN A 239 25961 23361 20913 -859 1502 -1381 C
ATOM 2453 OE1 GLN A 239 0.410 135.472 160.887 1.00179.98 O
ANISOU 2453 OE1 GLN A 239 25242 22794 20347 -1104 1488 -1364 O
ATOM 2454 NE2 GLN A 239 1.675 133.776 161.631 1.00176.36 N
ANISOU 2454 NE2 GLN A 239 25165 22211 19631 -497 1499 -1526 N
ATOM 2455 N VAL A 240 2.665 135.351 165.959 1.00147.97 N
ANISOU 2455 N VAL A 240 21143 18589 16489 -651 1540 -1130 N
ATOM 2456 CA VAL A 240 3.591 134.596 166.815 1.00149.29 C
ANISOU 2456 CA VAL A 240 21425 18753 16546 -306 1561 -1161 C
ATOM 2457 C VAL A 240 4.490 135.599 167.579 1.00151.92 C
ANISOU 2457 C VAL A 240 21389 19414 16921 -309 1582 -1008 C
ATOM 2458 O VAL A 240 5.512 136.051 167.037 1.00152.26 O
ANISOU 2458 O VAL A 240 21138 19894 16819 -191 1605 -955 O
ATOM 2459 CB VAL A 240 4.408 133.528 166.011 1.00156.29 C
ANISOU 2459 CB VAL A 240 22496 19743 17144 125 1573 -1310 C
ATOM 2460 CG1 VAL A 240 5.215 132.624 166.942 1.00157.76 C
ANISOU 2460 CG1 VAL A 240 22853 19884 17203 511 1582 -1354 C
ATOM 2461 CG2 VAL A 240 3.503 132.687 165.111 1.00157.16 C
ANISOU 2461 CG2 VAL A 240 22989 19513 17211 84 1525 -1458 C
ATOM 2462 N SER A 241 4.082 135.968 168.824 1.00146.09 N
ANISOU 2462 N SER A 241 20660 18480 16368 -465 1565 -931 N
ATOM 2463 CA SER A 241 4.827 136.927 169.645 1.00144.41 C
ANISOU 2463 CA SER A 241 20143 18515 16210 -501 1562 -790 C
ATOM 2464 C SER A 241 5.543 136.285 170.833 1.00147.29 C
ANISOU 2464 C SER A 241 20612 18831 16521 -226 1586 -799 C
ATOM 2465 O SER A 241 4.900 135.760 171.753 1.00145.81 O
ANISOU 2465 O SER A 241 20680 18284 16438 -253 1576 -830 O
ATOM 2466 CB SER A 241 3.942 138.088 170.088 1.00145.31 C
ANISOU 2466 CB SER A 241 20133 18519 16561 -884 1508 -686 C
ATOM 2467 OG SER A 241 4.734 139.164 170.565 1.00152.52 O
ANISOU 2467 OG SER A 241 20741 19714 17496 -953 1476 -547 O
ATOM 2468 N ALA A 242 6.892 136.331 170.784 1.00144.19 N
ANISOU 2468 N ALA A 242 20006 18837 15944 37 1616 -762 N
ATOM 2469 CA ALA A 242 7.806 135.800 171.799 1.00144.34 C
ANISOU 2469 CA ALA A 242 20059 18917 15867 344 1641 -761 C
ATOM 2470 C ALA A 242 7.858 136.717 173.019 1.00144.05 C
ANISOU 2470 C ALA A 242 19847 18877 16009 133 1612 -625 C
ATOM 2471 O ALA A 242 8.079 136.236 174.132 1.00143.87 O
ANISOU 2471 O ALA A 242 19954 18705 16005 283 1622 -632 O
ATOM 2472 CB ALA A 242 9.199 135.628 171.212 1.00147.52 C
ANISOU 2472 CB ALA A 242 20234 19834 15981 681 1680 -757 C
ATOM 2473 N LYS A 243 7.650 138.034 172.805 1.00136.95 N
ANISOU 2473 N LYS A 243 18676 18129 15231 -208 1563 -504 N
ATOM 2474 CA LYS A 243 7.629 139.049 173.857 1.00133.99 C
ANISOU 2474 CA LYS A 243 18148 17740 15022 -437 1504 -381 C
ATOM 2475 C LYS A 243 6.404 138.859 174.761 1.00134.41 C
ANISOU 2475 C LYS A 243 18453 17332 15285 -578 1486 -424 C
ATOM 2476 O LYS A 243 6.496 139.084 175.967 1.00132.94 O
ANISOU 2476 O LYS A 243 18257 17066 15189 -596 1464 -374 O
ATOM 2477 CB LYS A 243 7.637 140.456 173.244 1.00135.37 C
ANISOU 2477 CB LYS A 243 18042 18147 15246 -760 1425 -255 C
ATOM 2478 N ARG A 244 5.271 138.412 174.181 1.00129.50 N
ANISOU 2478 N ARG A 244 18045 16440 14720 -679 1493 -512 N
ATOM 2479 CA ARG A 244 4.019 138.161 174.907 1.00127.49 C
ANISOU 2479 CA ARG A 244 18011 15805 14626 -835 1477 -543 C
ATOM 2480 C ARG A 244 4.099 136.923 175.823 1.00129.16 C
ANISOU 2480 C ARG A 244 18501 15777 14796 -619 1515 -601 C
ATOM 2481 O ARG A 244 3.464 136.905 176.883 1.00127.00 O
ANISOU 2481 O ARG A 244 18329 15283 14643 -733 1498 -578 O
ATOM 2482 CB ARG A 244 2.831 138.038 173.933 1.00128.91 C
ANISOU 2482 CB ARG A 244 18313 15820 14847 -1029 1467 -606 C
ATOM 2483 CG ARG A 244 2.415 139.349 173.267 1.00139.60 C
ANISOU 2483 CG ARG A 244 19444 17298 16300 -1310 1407 -539 C
ATOM 2484 CD ARG A 244 0.928 139.370 172.986 1.00150.33 C
ANISOU 2484 CD ARG A 244 20942 18420 17757 -1532 1388 -583 C
ATOM 2485 NE ARG A 244 0.612 139.985 171.700 1.00164.26 N
ANISOU 2485 NE ARG A 244 22599 20299 19512 -1688 1362 -584 N
ATOM 2486 CZ ARG A 244 0.438 139.309 170.568 1.00185.54 C
ANISOU 2486 CZ ARG A 244 25400 22989 22106 -1648 1397 -666 C
ATOM 2487 NH1 ARG A 244 0.547 137.985 170.553 1.00177.34 N
ANISOU 2487 NH1 ARG A 244 24608 21814 20960 -1448 1445 -760 N
ATOM 2488 NH2 ARG A 244 0.150 139.948 169.446 1.00175.31 N
ANISOU 2488 NH2 ARG A 244 23989 21814 20808 -1799 1371 -657 N
ATOM 2489 N LYS A 245 4.864 135.889 175.396 1.00125.75 N
ANISOU 2489 N LYS A 245 18204 15399 14178 -296 1556 -675 N
ATOM 2490 CA LYS A 245 5.061 134.637 176.135 1.00125.41 C
ANISOU 2490 CA LYS A 245 18473 15115 14061 -53 1572 -734 C
ATOM 2491 C LYS A 245 5.838 134.848 177.430 1.00124.25 C
ANISOU 2491 C LYS A 245 18207 15074 13928 81 1582 -658 C
ATOM 2492 O LYS A 245 5.447 134.299 178.457 1.00123.58 O
ANISOU 2492 O LYS A 245 18332 14727 13894 98 1576 -654 O
ATOM 2493 CB LYS A 245 5.761 133.578 175.257 1.00131.00 C
ANISOU 2493 CB LYS A 245 19388 15849 14536 298 1591 -853 C
ATOM 2494 CG LYS A 245 4.814 132.604 174.550 1.00152.63 C
ANISOU 2494 CG LYS A 245 22498 18245 17249 228 1557 -963 C
ATOM 2495 CD LYS A 245 4.335 131.462 175.465 1.00165.54 C
ANISOU 2495 CD LYS A 245 24542 19436 18920 200 1516 -983 C
ATOM 2496 CE LYS A 245 3.568 130.394 174.718 1.00175.24 C
ANISOU 2496 CE LYS A 245 26197 20332 20053 192 1457 -1097 C
ATOM 2497 NZ LYS A 245 4.326 129.114 174.646 1.00183.08 N
ANISOU 2497 NZ LYS A 245 27489 21272 20801 652 1433 -1218 N
ATOM 2498 N VAL A 246 6.926 135.644 177.380 1.00117.62 N
ANISOU 2498 N VAL A 246 17030 14633 13027 160 1592 -587 N
ATOM 2499 CA VAL A 246 7.800 135.939 178.522 1.00116.35 C
ANISOU 2499 CA VAL A 246 16710 14642 12855 283 1595 -508 C
ATOM 2500 C VAL A 246 7.086 136.787 179.594 1.00117.00 C
ANISOU 2500 C VAL A 246 16718 14582 13154 -2 1549 -425 C
ATOM 2501 O VAL A 246 7.222 136.502 180.790 1.00116.30 O
ANISOU 2501 O VAL A 246 16704 14388 13096 89 1553 -402 O
ATOM 2502 CB VAL A 246 9.152 136.558 178.075 1.00120.56 C
ANISOU 2502 CB VAL A 246 16890 15688 13230 406 1604 -441 C
ATOM 2503 CG1 VAL A 246 10.045 136.891 179.269 1.00120.29 C
ANISOU 2503 CG1 VAL A 246 16685 15846 13172 512 1598 -353 C
ATOM 2504 CG2 VAL A 246 9.883 135.638 177.107 1.00122.76 C
ANISOU 2504 CG2 VAL A 246 17233 16154 13255 751 1652 -534 C
ATOM 2505 N VAL A 247 6.325 137.814 179.164 1.00110.77 N
ANISOU 2505 N VAL A 247 15795 13795 12499 -323 1498 -386 N
ATOM 2506 CA VAL A 247 5.584 138.703 180.065 1.00108.00 C
ANISOU 2506 CA VAL A 247 15376 13331 12329 -567 1436 -324 C
ATOM 2507 C VAL A 247 4.517 137.893 180.839 1.00111.13 C
ANISOU 2507 C VAL A 247 16043 13378 12805 -593 1455 -367 C
ATOM 2508 O VAL A 247 4.435 138.045 182.055 1.00110.07 O
ANISOU 2508 O VAL A 247 15895 13186 12739 -599 1437 -325 O
ATOM 2509 CB VAL A 247 5.048 139.975 179.347 1.00110.18 C
ANISOU 2509 CB VAL A 247 15480 13688 12696 -858 1361 -283 C
ATOM 2510 CG1 VAL A 247 4.214 140.846 180.277 1.00108.19 C
ANISOU 2510 CG1 VAL A 247 15209 13292 12605 -1057 1283 -247 C
ATOM 2511 CG2 VAL A 247 6.202 140.792 178.785 1.00110.58 C
ANISOU 2511 CG2 VAL A 247 15256 14104 12656 -869 1320 -198 C
ATOM 2512 N LYS A 248 3.797 136.964 180.165 1.00108.77 N
ANISOU 2512 N LYS A 248 15991 12865 12470 -602 1485 -444 N
ATOM 2513 CA LYS A 248 2.808 136.066 180.800 1.00109.01 C
ANISOU 2513 CA LYS A 248 16301 12581 12537 -664 1491 -466 C
ATOM 2514 C LYS A 248 3.490 135.191 181.878 1.00113.09 C
ANISOU 2514 C LYS A 248 16972 13013 12985 -417 1516 -455 C
ATOM 2515 O LYS A 248 2.919 134.981 182.955 1.00112.28 O
ANISOU 2515 O LYS A 248 16954 12761 12945 -494 1506 -412 O
ATOM 2516 CB LYS A 248 2.129 135.149 179.756 1.00113.08 C
ANISOU 2516 CB LYS A 248 17078 12900 12989 -717 1497 -546 C
ATOM 2517 CG LYS A 248 0.854 135.704 179.124 1.00131.56 C
ANISOU 2517 CG LYS A 248 19363 15202 15422 -1034 1467 -547 C
ATOM 2518 CD LYS A 248 0.350 134.772 178.009 1.00146.75 C
ANISOU 2518 CD LYS A 248 21550 16946 17261 -1079 1466 -629 C
ATOM 2519 CE LYS A 248 -0.861 135.291 177.265 1.00155.42 C
ANISOU 2519 CE LYS A 248 22590 18031 18433 -1389 1439 -629 C
ATOM 2520 NZ LYS A 248 -1.166 134.462 176.066 1.00162.60 N
ANISOU 2520 NZ LYS A 248 23731 18803 19245 -1420 1431 -714 N
ATOM 2521 N MET A 249 4.720 134.702 181.583 1.00109.64 N
ANISOU 2521 N MET A 249 16555 12704 12399 -108 1547 -490 N
ATOM 2522 CA MET A 249 5.506 133.873 182.491 1.00110.02 C
ANISOU 2522 CA MET A 249 16751 12705 12347 186 1567 -490 C
ATOM 2523 C MET A 249 5.813 134.663 183.757 1.00111.92 C
ANISOU 2523 C MET A 249 16774 13080 12671 173 1562 -400 C
ATOM 2524 O MET A 249 5.362 134.275 184.834 1.00111.46 O
ANISOU 2524 O MET A 249 16869 12839 12640 194 1560 -371 O
ATOM 2525 CB MET A 249 6.794 133.395 181.802 1.00114.17 C
ANISOU 2525 CB MET A 249 17275 13435 12668 545 1597 -552 C
ATOM 2526 CG MET A 249 7.543 132.337 182.574 1.00119.87 C
ANISOU 2526 CG MET A 249 18247 14051 13246 903 1608 -582 C
ATOM 2527 SD MET A 249 8.634 131.353 181.518 1.00127.33 S
ANISOU 2527 SD MET A 249 19336 15139 13903 1367 1624 -704 S
ATOM 2528 CE MET A 249 10.104 132.368 181.496 1.00123.87 C
ANISOU 2528 CE MET A 249 18387 15315 13364 1544 1670 -631 C
ATOM 2529 N MET A 250 6.491 135.817 183.593 1.00106.90 N
ANISOU 2529 N MET A 250 15793 12757 12068 111 1546 -349 N
ATOM 2530 CA MET A 250 6.939 136.728 184.649 1.00105.23 C
ANISOU 2530 CA MET A 250 15354 12708 11919 87 1517 -267 C
ATOM 2531 C MET A 250 5.823 137.271 185.535 1.00105.43 C
ANISOU 2531 C MET A 250 15386 12563 12109 -153 1473 -232 C
ATOM 2532 O MET A 250 6.046 137.411 186.739 1.00103.91 O
ANISOU 2532 O MET A 250 15152 12383 11946 -99 1461 -187 O
ATOM 2533 CB MET A 250 7.782 137.867 184.063 1.00107.51 C
ANISOU 2533 CB MET A 250 15312 13361 12175 37 1481 -212 C
ATOM 2534 CG MET A 250 9.064 137.390 183.375 1.00113.50 C
ANISOU 2534 CG MET A 250 15999 14397 12728 303 1528 -232 C
ATOM 2535 SD MET A 250 10.252 136.553 184.467 1.00120.09 S
ANISOU 2535 SD MET A 250 16881 15354 13395 715 1579 -229 S
ATOM 2536 CE MET A 250 9.860 134.845 184.180 1.00118.42 C
ANISOU 2536 CE MET A 250 17111 14789 13095 958 1628 -351 C
ATOM 2537 N ILE A 251 4.634 137.557 184.962 1.00100.73 N
ANISOU 2537 N ILE A 251 14832 11837 11603 -397 1449 -255 N
ATOM 2538 CA ILE A 251 3.480 138.043 185.730 1.00 99.04 C
ANISOU 2538 CA ILE A 251 14615 11504 11511 -600 1408 -230 C
ATOM 2539 C ILE A 251 3.041 136.961 186.729 1.00105.52 C
ANISOU 2539 C ILE A 251 15669 12117 12306 -535 1446 -221 C
ATOM 2540 O ILE A 251 2.851 137.267 187.909 1.00105.77 O
ANISOU 2540 O ILE A 251 15653 12154 12382 -541 1428 -176 O
ATOM 2541 CB ILE A 251 2.308 138.581 184.844 1.00100.30 C
ANISOU 2541 CB ILE A 251 14755 11616 11740 -853 1373 -256 C
ATOM 2542 CG1 ILE A 251 2.734 139.841 184.069 1.00 99.46 C
ANISOU 2542 CG1 ILE A 251 14416 11708 11665 -940 1307 -241 C
ATOM 2543 CG2 ILE A 251 1.043 138.868 185.688 1.00 99.32 C
ANISOU 2543 CG2 ILE A 251 14652 11394 11690 -1015 1344 -238 C
ATOM 2544 CD1 ILE A 251 1.708 140.352 183.035 1.00105.57 C
ANISOU 2544 CD1 ILE A 251 15176 12453 12481 -1146 1276 -271 C
ATOM 2545 N VAL A 252 2.937 135.698 186.262 1.00103.03 N
ANISOU 2545 N VAL A 252 15621 11622 11903 -464 1485 -260 N
ATOM 2546 CA VAL A 252 2.548 134.548 187.084 1.00103.81 C
ANISOU 2546 CA VAL A 252 16005 11486 11951 -423 1499 -239 C
ATOM 2547 C VAL A 252 3.499 134.368 188.286 1.00107.68 C
ANISOU 2547 C VAL A 252 16486 12031 12397 -173 1516 -200 C
ATOM 2548 O VAL A 252 3.024 134.294 189.422 1.00106.88 O
ANISOU 2548 O VAL A 252 16432 11856 12323 -224 1509 -140 O
ATOM 2549 CB VAL A 252 2.395 133.274 186.221 1.00109.60 C
ANISOU 2549 CB VAL A 252 17067 11995 12581 -389 1503 -299 C
ATOM 2550 CG1 VAL A 252 2.125 132.044 187.086 1.00111.48 C
ANISOU 2550 CG1 VAL A 252 17658 11966 12734 -310 1490 -270 C
ATOM 2551 CG2 VAL A 252 1.289 133.457 185.189 1.00108.75 C
ANISOU 2551 CG2 VAL A 252 16979 11818 12524 -690 1481 -319 C
ATOM 2552 N VAL A 253 4.832 134.378 188.023 1.00104.71 N
ANISOU 2552 N VAL A 253 16011 11832 11941 86 1538 -226 N
ATOM 2553 CA VAL A 253 5.949 134.272 188.982 1.00104.78 C
ANISOU 2553 CA VAL A 253 15960 11969 11883 354 1555 -194 C
ATOM 2554 C VAL A 253 5.830 135.322 190.121 1.00107.59 C
ANISOU 2554 C VAL A 253 16078 12456 12347 250 1527 -125 C
ATOM 2555 O VAL A 253 6.006 134.983 191.294 1.00107.95 O
ANISOU 2555 O VAL A 253 16178 12466 12372 367 1535 -84 O
ATOM 2556 CB VAL A 253 7.319 134.361 188.242 1.00109.11 C
ANISOU 2556 CB VAL A 253 16366 12785 12304 604 1578 -229 C
ATOM 2557 CG1 VAL A 253 8.493 134.285 189.208 1.00109.19 C
ANISOU 2557 CG1 VAL A 253 16185 13044 12257 815 1586 -179 C
ATOM 2558 CG2 VAL A 253 7.448 133.275 187.184 1.00111.05 C
ANISOU 2558 CG2 VAL A 253 16909 12891 12393 838 1601 -309 C
ATOM 2559 N VAL A 254 5.513 136.578 189.761 1.00102.60 N
ANISOU 2559 N VAL A 254 15206 11962 11816 44 1481 -118 N
ATOM 2560 CA VAL A 254 5.345 137.716 190.677 1.00101.19 C
ANISOU 2560 CA VAL A 254 14820 11897 11729 -56 1422 -74 C
ATOM 2561 C VAL A 254 4.120 137.533 191.573 1.00104.58 C
ANISOU 2561 C VAL A 254 15347 12168 12221 -188 1413 -54 C
ATOM 2562 O VAL A 254 4.204 137.732 192.787 1.00104.05 O
ANISOU 2562 O VAL A 254 15228 12140 12165 -131 1397 -16 O
ATOM 2563 CB VAL A 254 5.333 139.046 189.876 1.00104.08 C
ANISOU 2563 CB VAL A 254 14962 12428 12157 -224 1347 -78 C
ATOM 2564 CG1 VAL A 254 4.710 140.200 190.658 1.00102.31 C
ANISOU 2564 CG1 VAL A 254 14616 12228 12031 -362 1254 -59 C
ATOM 2565 CG2 VAL A 254 6.743 139.399 189.417 1.00104.94 C
ANISOU 2565 CG2 VAL A 254 14899 12793 12180 -104 1338 -55 C
ATOM 2566 N CYS A 255 2.998 137.123 190.971 1.00101.21 N
ANISOU 2566 N CYS A 255 15047 11592 11815 -367 1422 -74 N
ATOM 2567 CA CYS A 255 1.739 136.888 191.673 1.00100.80 C
ANISOU 2567 CA CYS A 255 15065 11448 11788 -523 1415 -39 C
ATOM 2568 C CYS A 255 1.833 135.729 192.671 1.00101.83 C
ANISOU 2568 C CYS A 255 15393 11450 11847 -426 1453 18 C
ATOM 2569 O CYS A 255 1.161 135.751 193.703 1.00100.77 O
ANISOU 2569 O CYS A 255 15236 11335 11717 -503 1442 73 O
ATOM 2570 CB CYS A 255 0.596 136.708 190.680 1.00101.79 C
ANISOU 2570 CB CYS A 255 15267 11484 11924 -750 1412 -62 C
ATOM 2571 SG CYS A 255 0.211 138.208 189.735 1.00104.57 S
ANISOU 2571 SG CYS A 255 15375 11993 12363 -894 1346 -110 S
ATOM 2572 N THR A 256 2.725 134.764 192.389 1.00 96.69 N
ANISOU 2572 N THR A 256 14931 10692 11113 -233 1488 6 N
ATOM 2573 CA THR A 256 3.004 133.620 193.241 1.00 96.70 C
ANISOU 2573 CA THR A 256 15165 10547 11030 -92 1509 57 C
ATOM 2574 C THR A 256 3.754 134.114 194.471 1.00 99.25 C
ANISOU 2574 C THR A 256 15309 11037 11363 73 1510 95 C
ATOM 2575 O THR A 256 3.374 133.761 195.594 1.00 99.39 O
ANISOU 2575 O THR A 256 15386 11012 11366 49 1508 164 O
ATOM 2576 CB THR A 256 3.797 132.600 192.454 1.00102.60 C
ANISOU 2576 CB THR A 256 16158 11156 11668 123 1527 6 C
ATOM 2577 OG1 THR A 256 3.061 132.289 191.276 1.00104.07 O
ANISOU 2577 OG1 THR A 256 16505 11191 11845 -45 1514 -37 O
ATOM 2578 CG2 THR A 256 4.059 131.339 193.237 1.00102.12 C
ANISOU 2578 CG2 THR A 256 16398 10903 11501 294 1526 52 C
ATOM 2579 N PHE A 257 4.787 134.968 194.259 1.00 93.70 N
ANISOU 2579 N PHE A 257 14378 10547 10678 215 1504 59 N
ATOM 2580 CA PHE A 257 5.595 135.561 195.324 1.00 92.37 C
ANISOU 2580 CA PHE A 257 14022 10563 10513 357 1489 91 C
ATOM 2581 C PHE A 257 4.698 136.320 196.297 1.00 95.91 C
ANISOU 2581 C PHE A 257 14340 11064 11039 202 1445 122 C
ATOM 2582 O PHE A 257 4.754 136.059 197.505 1.00 95.96 O
ANISOU 2582 O PHE A 257 14352 11088 11020 288 1449 171 O
ATOM 2583 CB PHE A 257 6.673 136.490 194.737 1.00 93.24 C
ANISOU 2583 CB PHE A 257 13894 10912 10620 434 1464 61 C
ATOM 2584 CG PHE A 257 7.601 137.109 195.759 1.00 94.39 C
ANISOU 2584 CG PHE A 257 13846 11266 10752 559 1432 97 C
ATOM 2585 CD1 PHE A 257 8.830 136.528 196.048 1.00 98.82 C
ANISOU 2585 CD1 PHE A 257 14410 11941 11197 826 1471 115 C
ATOM 2586 CD2 PHE A 257 7.248 138.273 196.431 1.00 95.01 C
ANISOU 2586 CD2 PHE A 257 13746 11437 10916 423 1350 106 C
ATOM 2587 CE1 PHE A 257 9.685 137.094 196.999 1.00 99.55 C
ANISOU 2587 CE1 PHE A 257 14309 12249 11265 923 1436 153 C
ATOM 2588 CE2 PHE A 257 8.094 138.827 197.394 1.00 97.99 C
ANISOU 2588 CE2 PHE A 257 13966 11993 11272 523 1302 137 C
ATOM 2589 CZ PHE A 257 9.314 138.243 197.662 1.00 97.33 C
ANISOU 2589 CZ PHE A 257 13867 12035 11080 755 1349 166 C
ATOM 2590 N ALA A 258 3.857 137.236 195.757 1.00 91.51 N
ANISOU 2590 N ALA A 258 13666 10545 10560 -3 1398 89 N
ATOM 2591 CA ALA A 258 2.915 138.083 196.499 1.00 90.33 C
ANISOU 2591 CA ALA A 258 13388 10473 10460 -123 1341 95 C
ATOM 2592 C ALA A 258 1.970 137.267 197.392 1.00 94.89 C
ANISOU 2592 C ALA A 258 14087 10978 10989 -184 1377 160 C
ATOM 2593 O ALA A 258 1.772 137.620 198.556 1.00 92.85 O
ANISOU 2593 O ALA A 258 13733 10826 10718 -141 1352 188 O
ATOM 2594 CB ALA A 258 2.121 138.948 195.527 1.00 89.96 C
ANISOU 2594 CB ALA A 258 13258 10449 10474 -306 1289 43 C
ATOM 2595 N ILE A 259 1.430 136.150 196.850 1.00 94.02 N
ANISOU 2595 N ILE A 259 14197 10692 10834 -286 1425 190 N
ATOM 2596 CA ILE A 259 0.518 135.234 197.545 1.00 95.26 C
ANISOU 2596 CA ILE A 259 14502 10771 10921 -403 1445 281 C
ATOM 2597 C ILE A 259 1.245 134.495 198.674 1.00102.70 C
ANISOU 2597 C ILE A 259 15553 11668 11801 -219 1469 347 C
ATOM 2598 O ILE A 259 0.740 134.446 199.799 1.00102.71 O
ANISOU 2598 O ILE A 259 15507 11755 11762 -250 1464 421 O
ATOM 2599 CB ILE A 259 -0.213 134.292 196.534 1.00 98.66 C
ANISOU 2599 CB ILE A 259 15168 11006 11312 -607 1457 299 C
ATOM 2600 CG1 ILE A 259 -1.397 135.044 195.878 1.00 98.00 C
ANISOU 2600 CG1 ILE A 259 14931 11037 11266 -835 1431 269 C
ATOM 2601 CG2 ILE A 259 -0.704 133.004 197.198 1.00100.76 C
ANISOU 2601 CG2 ILE A 259 15682 11128 11476 -714 1462 417 C
ATOM 2602 CD1 ILE A 259 -1.823 134.588 194.481 1.00103.87 C
ANISOU 2602 CD1 ILE A 259 15840 11625 12001 -1008 1434 242 C
ATOM 2603 N CYS A 260 2.444 133.968 198.378 1.00101.27 N
ANISOU 2603 N CYS A 260 15497 11387 11594 -7 1492 319 N
ATOM 2604 CA CYS A 260 3.257 133.206 199.322 1.00102.74 C
ANISOU 2604 CA CYS A 260 15809 11522 11706 212 1512 371 C
ATOM 2605 C CYS A 260 3.746 133.999 200.528 1.00106.83 C
ANISOU 2605 C CYS A 260 16091 12255 12243 348 1502 386 C
ATOM 2606 O CYS A 260 3.814 133.431 201.624 1.00108.54 O
ANISOU 2606 O CYS A 260 16388 12453 12399 421 1513 464 O
ATOM 2607 CB CYS A 260 4.423 132.538 198.605 1.00103.94 C
ANISOU 2607 CB CYS A 260 16122 11570 11801 447 1534 319 C
ATOM 2608 SG CYS A 260 3.930 131.212 197.479 1.00109.65 S
ANISOU 2608 SG CYS A 260 17265 11954 12444 361 1525 315 S
ATOM 2609 N TRP A 261 4.126 135.277 200.335 1.00101.08 N
ANISOU 2609 N TRP A 261 15098 11719 11588 378 1469 316 N
ATOM 2610 CA TRP A 261 4.718 136.060 201.416 1.00100.01 C
ANISOU 2610 CA TRP A 261 14760 11776 11462 510 1436 318 C
ATOM 2611 C TRP A 261 3.724 136.887 202.244 1.00101.71 C
ANISOU 2611 C TRP A 261 14817 12119 11709 396 1383 321 C
ATOM 2612 O TRP A 261 4.049 137.225 203.384 1.00100.86 O
ANISOU 2612 O TRP A 261 14588 12147 11588 513 1350 327 O
ATOM 2613 CB TRP A 261 5.881 136.925 200.888 1.00 98.25 C
ANISOU 2613 CB TRP A 261 14370 11692 11267 615 1401 258 C
ATOM 2614 CG TRP A 261 7.108 136.090 200.661 1.00100.54 C
ANISOU 2614 CG TRP A 261 14760 11968 11473 836 1454 269 C
ATOM 2615 CD1 TRP A 261 7.525 135.557 199.474 1.00104.12 C
ANISOU 2615 CD1 TRP A 261 15330 12345 11886 884 1491 236 C
ATOM 2616 CD2 TRP A 261 7.937 135.497 201.679 1.00101.46 C
ANISOU 2616 CD2 TRP A 261 14908 12136 11505 1070 1481 315 C
ATOM 2617 NE1 TRP A 261 8.605 134.722 199.680 1.00105.04 N
ANISOU 2617 NE1 TRP A 261 15537 12485 11888 1160 1532 251 N
ATOM 2618 CE2 TRP A 261 8.879 134.668 201.025 1.00106.89 C
ANISOU 2618 CE2 TRP A 261 15724 12793 12097 1274 1528 303 C
ATOM 2619 CE3 TRP A 261 7.987 135.601 203.084 1.00102.44 C
ANISOU 2619 CE3 TRP A 261 14959 12349 11614 1147 1466 361 C
ATOM 2620 CZ2 TRP A 261 9.879 133.974 201.724 1.00107.59 C
ANISOU 2620 CZ2 TRP A 261 15868 12942 12071 1561 1558 336 C
ATOM 2621 CZ3 TRP A 261 8.982 134.921 203.772 1.00105.04 C
ANISOU 2621 CZ3 TRP A 261 15334 12730 11845 1403 1499 400 C
ATOM 2622 CH2 TRP A 261 9.909 134.114 203.097 1.00107.14 C
ANISOU 2622 CH2 TRP A 261 15730 12966 12014 1611 1544 388 C
ATOM 2623 N LEU A 262 2.511 137.149 201.729 1.00 97.49 N
ANISOU 2623 N LEU A 262 14286 11564 11192 190 1373 316 N
ATOM 2624 CA LEU A 262 1.521 137.949 202.457 1.00 96.59 C
ANISOU 2624 CA LEU A 262 14012 11618 11069 128 1320 310 C
ATOM 2625 C LEU A 262 1.162 137.397 203.867 1.00101.99 C
ANISOU 2625 C LEU A 262 14701 12387 11663 180 1345 401 C
ATOM 2626 O LEU A 262 1.255 138.184 204.818 1.00102.11 O
ANISOU 2626 O LEU A 262 14559 12573 11667 298 1292 373 O
ATOM 2627 CB LEU A 262 0.253 138.208 201.622 1.00 95.90 C
ANISOU 2627 CB LEU A 262 13904 11544 10991 -85 1306 290 C
ATOM 2628 CG LEU A 262 -0.756 139.194 202.216 1.00 99.22 C
ANISOU 2628 CG LEU A 262 14135 12183 11380 -100 1235 254 C
ATOM 2629 CD1 LEU A 262 -0.118 140.551 202.508 1.00 98.17 C
ANISOU 2629 CD1 LEU A 262 13867 12141 11291 72 1130 161 C
ATOM 2630 CD2 LEU A 262 -1.965 139.337 201.327 1.00100.58 C
ANISOU 2630 CD2 LEU A 262 14282 12379 11555 -283 1221 224 C
ATOM 2631 N PRO A 263 0.775 136.103 204.055 1.00 98.79 N
ANISOU 2631 N PRO A 263 14483 11869 11184 95 1408 512 N
ATOM 2632 CA PRO A 263 0.445 135.632 205.416 1.00 98.94 C
ANISOU 2632 CA PRO A 263 14489 11999 11106 124 1422 615 C
ATOM 2633 C PRO A 263 1.614 135.728 206.382 1.00100.67 C
ANISOU 2633 C PRO A 263 14679 12251 11319 379 1423 614 C
ATOM 2634 O PRO A 263 1.406 136.000 207.562 1.00 99.49 O
ANISOU 2634 O PRO A 263 14433 12265 11103 445 1414 663 O
ATOM 2635 CB PRO A 263 0.028 134.173 205.200 1.00102.62 C
ANISOU 2635 CB PRO A 263 15218 12281 11493 -59 1464 744 C
ATOM 2636 CG PRO A 263 -0.298 134.062 203.755 1.00107.06 C
ANISOU 2636 CG PRO A 263 15889 12681 12107 -215 1464 693 C
ATOM 2637 CD PRO A 263 0.612 135.014 203.068 1.00101.32 C
ANISOU 2637 CD PRO A 263 15056 11952 11489 -45 1449 554 C
ATOM 2638 N PHE A 264 2.842 135.513 205.869 1.00 96.87 N
ANISOU 2638 N PHE A 264 14264 11652 10889 526 1432 560 N
ATOM 2639 CA PHE A 264 4.069 135.588 206.652 1.00 96.64 C
ANISOU 2639 CA PHE A 264 14188 11684 10845 770 1431 556 C
ATOM 2640 C PHE A 264 4.267 137.000 207.185 1.00100.00 C
ANISOU 2640 C PHE A 264 14360 12329 11307 842 1352 479 C
ATOM 2641 O PHE A 264 4.449 137.163 208.393 1.00100.31 O
ANISOU 2641 O PHE A 264 14323 12496 11295 958 1337 509 O
ATOM 2642 CB PHE A 264 5.283 135.114 205.831 1.00 98.23 C
ANISOU 2642 CB PHE A 264 14490 11773 11060 906 1456 519 C
ATOM 2643 CG PHE A 264 6.583 135.038 206.604 1.00 99.61 C
ANISOU 2643 CG PHE A 264 14631 12033 11182 1165 1466 534 C
ATOM 2644 CD1 PHE A 264 6.974 133.857 207.220 1.00103.74 C
ANISOU 2644 CD1 PHE A 264 15361 12443 11611 1305 1514 618 C
ATOM 2645 CD2 PHE A 264 7.422 136.142 206.699 1.00100.34 C
ANISOU 2645 CD2 PHE A 264 14500 12319 11307 1261 1412 472 C
ATOM 2646 CE1 PHE A 264 8.168 133.790 207.939 1.00105.23 C
ANISOU 2646 CE1 PHE A 264 15507 12736 11738 1565 1524 631 C
ATOM 2647 CE2 PHE A 264 8.615 136.072 207.415 1.00103.73 C
ANISOU 2647 CE2 PHE A 264 14877 12864 11670 1488 1419 494 C
ATOM 2648 CZ PHE A 264 8.980 134.897 208.030 1.00103.32 C
ANISOU 2648 CZ PHE A 264 15008 12723 11525 1653 1482 569 C
ATOM 2649 N HIS A 265 4.193 138.014 206.303 1.00 95.49 N
ANISOU 2649 N HIS A 265 13682 11787 10813 768 1287 383 N
ATOM 2650 CA HIS A 265 4.363 139.406 206.703 1.00 95.09 C
ANISOU 2650 CA HIS A 265 13449 11892 10790 820 1172 301 C
ATOM 2651 C HIS A 265 3.275 139.882 207.661 1.00100.66 C
ANISOU 2651 C HIS A 265 14067 12738 11440 813 1131 295 C
ATOM 2652 O HIS A 265 3.597 140.585 208.614 1.00100.40 O
ANISOU 2652 O HIS A 265 13930 12838 11378 943 1050 254 O
ATOM 2653 CB HIS A 265 4.512 140.327 205.493 1.00 94.87 C
ANISOU 2653 CB HIS A 265 13373 11830 10843 723 1096 216 C
ATOM 2654 CG HIS A 265 5.801 140.110 204.762 1.00 98.37 C
ANISOU 2654 CG HIS A 265 13843 12226 11307 762 1125 225 C
ATOM 2655 ND1 HIS A 265 7.024 140.165 205.414 1.00100.53 N
ANISOU 2655 ND1 HIS A 265 14045 12605 11547 908 1101 240 N
ATOM 2656 CD2 HIS A 265 6.017 139.846 203.453 1.00100.00 C
ANISOU 2656 CD2 HIS A 265 14123 12331 11540 684 1174 221 C
ATOM 2657 CE1 HIS A 265 7.935 139.931 204.486 1.00100.12 C
ANISOU 2657 CE1 HIS A 265 14009 12543 11490 922 1140 250 C
ATOM 2658 NE2 HIS A 265 7.378 139.737 203.289 1.00100.20 N
ANISOU 2658 NE2 HIS A 265 14110 12424 11536 799 1184 234 N
ATOM 2659 N ILE A 266 2.015 139.443 207.452 1.00 98.55 N
ANISOU 2659 N ILE A 266 13841 12469 11135 668 1181 340 N
ATOM 2660 CA ILE A 266 0.865 139.755 208.315 1.00 99.18 C
ANISOU 2660 CA ILE A 266 13810 12755 11117 663 1157 354 C
ATOM 2661 C ILE A 266 1.067 139.147 209.718 1.00103.71 C
ANISOU 2661 C ILE A 266 14372 13436 11596 779 1199 446 C
ATOM 2662 O ILE A 266 0.788 139.811 210.724 1.00103.22 O
ANISOU 2662 O ILE A 266 14173 13586 11460 904 1140 414 O
ATOM 2663 CB ILE A 266 -0.467 139.296 207.645 1.00102.78 C
ANISOU 2663 CB ILE A 266 14294 13224 11533 441 1205 405 C
ATOM 2664 CG1 ILE A 266 -0.880 140.284 206.519 1.00102.09 C
ANISOU 2664 CG1 ILE A 266 14163 13107 11520 368 1136 291 C
ATOM 2665 CG2 ILE A 266 -1.597 139.095 208.683 1.00104.62 C
ANISOU 2665 CG2 ILE A 266 14411 13727 11613 420 1217 481 C
ATOM 2666 CD1 ILE A 266 -2.076 139.850 205.638 1.00109.40 C
ANISOU 2666 CD1 ILE A 266 15103 14056 12407 145 1177 331 C
ATOM 2667 N PHE A 267 1.564 137.889 209.764 1.00100.70 N
ANISOU 2667 N PHE A 267 14151 12904 11206 760 1289 554 N
ATOM 2668 CA PHE A 267 1.847 137.150 210.992 1.00101.29 C
ANISOU 2668 CA PHE A 267 14254 13041 11192 867 1330 658 C
ATOM 2669 C PHE A 267 2.777 137.938 211.912 1.00106.15 C
ANISOU 2669 C PHE A 267 14744 13772 11815 1105 1268 585 C
ATOM 2670 O PHE A 267 2.456 138.111 213.087 1.00107.03 O
ANISOU 2670 O PHE A 267 14751 14078 11836 1200 1249 609 O
ATOM 2671 CB PHE A 267 2.457 135.779 210.671 1.00103.42 C
ANISOU 2671 CB PHE A 267 14771 13068 11455 839 1409 762 C
ATOM 2672 CG PHE A 267 2.638 134.885 211.873 1.00105.85 C
ANISOU 2672 CG PHE A 267 15159 13401 11658 916 1448 894 C
ATOM 2673 CD1 PHE A 267 1.657 133.970 212.232 1.00109.92 C
ANISOU 2673 CD1 PHE A 267 15778 13920 12066 727 1478 1046 C
ATOM 2674 CD2 PHE A 267 3.801 134.938 212.633 1.00107.51 C
ANISOU 2674 CD2 PHE A 267 15351 13634 11863 1158 1447 881 C
ATOM 2675 CE1 PHE A 267 1.831 133.130 213.335 1.00112.06 C
ANISOU 2675 CE1 PHE A 267 16147 14200 12231 779 1502 1185 C
ATOM 2676 CE2 PHE A 267 3.964 134.113 213.747 1.00111.47 C
ANISOU 2676 CE2 PHE A 267 15937 14153 12262 1237 1479 1007 C
ATOM 2677 CZ PHE A 267 2.981 133.209 214.086 1.00110.88 C
ANISOU 2677 CZ PHE A 267 15983 14060 12086 1047 1505 1160 C
ATOM 2678 N PHE A 268 3.916 138.416 211.377 1.00102.01 N
ANISOU 2678 N PHE A 268 14220 13158 11381 1186 1229 501 N
ATOM 2679 CA PHE A 268 4.903 139.179 212.138 1.00101.78 C
ANISOU 2679 CA PHE A 268 14081 13238 11351 1369 1152 442 C
ATOM 2680 C PHE A 268 4.517 140.640 212.355 1.00106.48 C
ANISOU 2680 C PHE A 268 14537 13966 11953 1398 1008 318 C
ATOM 2681 O PHE A 268 5.116 141.307 213.200 1.00106.36 O
ANISOU 2681 O PHE A 268 14447 14052 11914 1539 920 270 O
ATOM 2682 CB PHE A 268 6.287 139.054 211.495 1.00103.21 C
ANISOU 2682 CB PHE A 268 14305 13321 11589 1425 1161 429 C
ATOM 2683 CG PHE A 268 6.903 137.695 211.700 1.00105.71 C
ANISOU 2683 CG PHE A 268 14762 13549 11853 1519 1274 535 C
ATOM 2684 CD1 PHE A 268 7.701 137.437 212.806 1.00109.43 C
ANISOU 2684 CD1 PHE A 268 15205 14120 12252 1705 1286 583 C
ATOM 2685 CD2 PHE A 268 6.669 136.664 210.800 1.00108.53 C
ANISOU 2685 CD2 PHE A 268 15306 13713 12218 1433 1354 583 C
ATOM 2686 CE1 PHE A 268 8.255 136.174 213.009 1.00111.58 C
ANISOU 2686 CE1 PHE A 268 15638 14297 12459 1818 1375 679 C
ATOM 2687 CE2 PHE A 268 7.221 135.399 211.005 1.00112.85 C
ANISOU 2687 CE2 PHE A 268 16038 14145 12696 1548 1430 672 C
ATOM 2688 CZ PHE A 268 8.019 135.165 212.102 1.00111.66 C
ANISOU 2688 CZ PHE A 268 15861 14092 12472 1748 1440 720 C
ATOM 2689 N LEU A 269 3.507 141.128 211.615 1.00103.87 N
ANISOU 2689 N LEU A 269 14191 13638 11637 1280 973 265 N
ATOM 2690 CA LEU A 269 3.021 142.502 211.702 1.00104.20 C
ANISOU 2690 CA LEU A 269 14147 13780 11665 1332 819 136 C
ATOM 2691 C LEU A 269 1.954 142.686 212.778 1.00113.87 C
ANISOU 2691 C LEU A 269 15274 15238 12752 1434 802 131 C
ATOM 2692 O LEU A 269 1.792 143.795 213.282 1.00113.97 O
ANISOU 2692 O LEU A 269 15229 15361 12713 1571 657 14 O
ATOM 2693 CB LEU A 269 2.501 142.966 210.331 1.00102.81 C
ANISOU 2693 CB LEU A 269 14008 13489 11567 1179 776 73 C
ATOM 2694 CG LEU A 269 3.303 144.041 209.555 1.00105.52 C
ANISOU 2694 CG LEU A 269 14381 13705 12005 1140 647 -10 C
ATOM 2695 CD1 LEU A 269 4.794 144.044 209.888 1.00105.10 C
ANISOU 2695 CD1 LEU A 269 14336 13610 11986 1172 670 40 C
ATOM 2696 CD2 LEU A 269 3.078 143.919 208.055 1.00105.55 C
ANISOU 2696 CD2 LEU A 269 14437 13579 12087 959 667 -23 C
ATOM 2697 N LEU A 270 1.250 141.601 213.146 1.00114.65 N
ANISOU 2697 N LEU A 270 15366 15425 12772 1371 936 262 N
ATOM 2698 CA LEU A 270 0.184 141.604 214.155 1.00116.94 C
ANISOU 2698 CA LEU A 270 15529 16007 12897 1446 939 293 C
ATOM 2699 C LEU A 270 0.612 141.917 215.604 1.00125.34 C
ANISOU 2699 C LEU A 270 16514 17239 13870 1676 891 276 C
ATOM 2700 O LEU A 270 -0.182 142.587 216.261 1.00125.26 O
ANISOU 2700 O LEU A 270 16381 17486 13727 1817 818 212 O
ATOM 2701 CB LEU A 270 -0.611 140.302 214.133 1.00117.73 C
ANISOU 2701 CB LEU A 270 15647 16164 12920 1250 1078 465 C
ATOM 2702 CG LEU A 270 -1.690 140.233 213.079 1.00121.76 C
ANISOU 2702 CG LEU A 270 16165 16655 13442 1045 1097 467 C
ATOM 2703 CD1 LEU A 270 -2.125 138.805 212.861 1.00122.92 C
ANISOU 2703 CD1 LEU A 270 16438 16690 13576 789 1220 645 C
ATOM 2704 CD2 LEU A 270 -2.863 141.122 213.440 1.00123.69 C
ANISOU 2704 CD2 LEU A 270 16222 17236 13539 1119 1031 404 C
ATOM 2705 N PRO A 271 1.790 141.500 216.159 1.00125.95 N
ANISOU 2705 N PRO A 271 16647 17215 13992 1747 919 321 N
ATOM 2706 CA PRO A 271 2.106 141.868 217.562 1.00128.33 C
ANISOU 2706 CA PRO A 271 16863 17700 14197 1970 860 294 C
ATOM 2707 C PRO A 271 2.114 143.376 217.864 1.00137.53 C
ANISOU 2707 C PRO A 271 17973 18952 15329 2151 666 107 C
ATOM 2708 O PRO A 271 2.156 143.770 219.032 1.00138.43 O
ANISOU 2708 O PRO A 271 18012 19256 15330 2350 601 67 O
ATOM 2709 CB PRO A 271 3.478 141.223 217.808 1.00129.51 C
ANISOU 2709 CB PRO A 271 17095 17692 14422 1998 909 356 C
ATOM 2710 CG PRO A 271 3.586 140.148 216.786 1.00133.00 C
ANISOU 2710 CG PRO A 271 17667 17925 14942 1810 1035 463 C
ATOM 2711 CD PRO A 271 2.869 140.672 215.582 1.00127.43 C
ANISOU 2711 CD PRO A 271 16971 17152 14295 1660 1001 393 C
ATOM 2712 N TYR A 272 2.047 144.212 216.807 1.00136.85 N
ANISOU 2712 N TYR A 272 17947 18719 15332 2083 561 -6 N
ATOM 2713 CA TYR A 272 1.995 145.670 216.893 1.00138.50 C
ANISOU 2713 CA TYR A 272 18174 18939 15511 2229 342 -187 C
ATOM 2714 C TYR A 272 0.548 146.149 217.084 1.00146.67 C
ANISOU 2714 C TYR A 272 19133 20194 16402 2342 288 -265 C
ATOM 2715 O TYR A 272 0.338 147.221 217.649 1.00146.82 O
ANISOU 2715 O TYR A 272 19174 20276 16334 2548 96 -422 O
ATOM 2716 CB TYR A 272 2.653 146.324 215.653 1.00138.82 C
ANISOU 2716 CB TYR A 272 18336 18705 15706 2086 237 -251 C
ATOM 2717 CG TYR A 272 4.107 145.941 215.456 1.00140.15 C
ANISOU 2717 CG TYR A 272 18541 18731 15977 1996 279 -177 C
ATOM 2718 CD1 TYR A 272 5.064 146.228 216.428 1.00143.03 C
ANISOU 2718 CD1 TYR A 272 18892 19150 16302 2121 193 -196 C
ATOM 2719 CD2 TYR A 272 4.531 145.302 214.293 1.00139.72 C
ANISOU 2719 CD2 TYR A 272 18529 18519 16040 1802 398 -91 C
ATOM 2720 CE1 TYR A 272 6.399 145.861 216.261 1.00143.93 C
ANISOU 2720 CE1 TYR A 272 19008 19195 16482 2053 234 -120 C
ATOM 2721 CE2 TYR A 272 5.866 144.938 214.112 1.00140.27 C
ANISOU 2721 CE2 TYR A 272 18609 18519 16169 1760 437 -26 C
ATOM 2722 CZ TYR A 272 6.797 145.223 215.099 1.00148.01 C
ANISOU 2722 CZ TYR A 272 19552 19586 17100 1884 358 -36 C
ATOM 2723 OH TYR A 272 8.116 144.877 214.941 1.00148.02 O
ANISOU 2723 OH TYR A 272 19534 19576 17131 1857 396 33 O
ATOM 2724 N ILE A 273 -0.442 145.343 216.626 1.00146.37 N
ANISOU 2724 N ILE A 273 19014 20285 16316 2213 445 -154 N
ATOM 2725 CA ILE A 273 -1.878 145.619 216.741 1.00148.62 C
ANISOU 2725 CA ILE A 273 19176 20861 16432 2295 430 -191 C
ATOM 2726 C ILE A 273 -2.465 145.020 218.043 1.00158.68 C
ANISOU 2726 C ILE A 273 20282 22507 17504 2418 512 -97 C
ATOM 2727 O ILE A 273 -2.995 145.773 218.865 1.00159.95 O
ANISOU 2727 O ILE A 273 20356 22926 17492 2698 397 -209 O
ATOM 2728 CB ILE A 273 -2.647 145.186 215.466 1.00150.84 C
ANISOU 2728 CB ILE A 273 19459 21085 16768 2038 532 -118 C
ATOM 2729 N ASN A 274 -2.342 143.684 218.243 1.00158.23 N
ANISOU 2729 N ASN A 274 20198 22469 17455 2216 695 109 N
ATOM 2730 CA ASN A 274 -2.826 142.974 219.440 1.00160.76 C
ANISOU 2730 CA ASN A 274 20371 23122 17588 2264 784 246 C
ATOM 2731 C ASN A 274 -1.756 141.976 219.956 1.00166.29 C
ANISOU 2731 C ASN A 274 21171 23633 18379 2178 884 387 C
ATOM 2732 O ASN A 274 -1.696 140.843 219.468 1.00165.72 O
ANISOU 2732 O ASN A 274 21193 23394 18379 1925 1009 546 O
ATOM 2733 CB ASN A 274 -4.170 142.282 219.166 1.00163.22 C
ANISOU 2733 CB ASN A 274 20544 23726 17746 2076 887 389 C
ATOM 2734 N PRO A 275 -0.889 142.390 220.918 1.00164.48 N
ANISOU 2734 N PRO A 275 20942 23412 18140 2399 818 323 N
ATOM 2735 CA PRO A 275 0.190 141.492 221.387 1.00165.04 C
ANISOU 2735 CA PRO A 275 21104 23317 18286 2354 906 448 C
ATOM 2736 C PRO A 275 -0.246 140.167 222.025 1.00173.25 C
ANISOU 2736 C PRO A 275 22104 24520 19202 2231 1050 678 C
ATOM 2737 O PRO A 275 0.449 139.159 221.859 1.00172.37 O
ANISOU 2737 O PRO A 275 22136 24184 19172 2111 1140 810 O
ATOM 2738 CB PRO A 275 0.971 142.362 222.380 1.00166.61 C
ANISOU 2738 CB PRO A 275 21276 23565 18462 2628 781 316 C
ATOM 2739 CG PRO A 275 0.028 143.444 222.777 1.00171.43 C
ANISOU 2739 CG PRO A 275 21760 24465 18909 2838 653 169 C
ATOM 2740 CD PRO A 275 -0.802 143.713 221.570 1.00166.40 C
ANISOU 2740 CD PRO A 275 21127 23801 18295 2710 643 127 C
ATOM 2741 N ASP A 276 -1.383 140.173 222.752 1.00173.85 N
ANISOU 2741 N ASP A 276 21993 25000 19062 2266 1058 731 N
ATOM 2742 CA ASP A 276 -1.941 139.003 223.443 1.00176.36 C
ANISOU 2742 CA ASP A 276 22243 25551 19215 2119 1170 969 C
ATOM 2743 C ASP A 276 -2.529 137.949 222.493 1.00181.86 C
ANISOU 2743 C ASP A 276 23049 26106 19942 1747 1266 1147 C
ATOM 2744 O ASP A 276 -2.484 136.760 222.821 1.00182.65 O
ANISOU 2744 O ASP A 276 23232 26183 19982 1560 1348 1367 O
ATOM 2745 CB ASP A 276 -3.000 139.427 224.482 1.00180.25 C
ANISOU 2745 CB ASP A 276 22460 26594 19432 2276 1137 965 C
ATOM 2746 CG ASP A 276 -2.496 140.288 225.629 1.00191.19 C
ANISOU 2746 CG ASP A 276 23745 28175 20725 2633 1052 841 C
ATOM 2747 OD1 ASP A 276 -1.319 140.117 226.035 1.00190.43 O
ANISOU 2747 OD1 ASP A 276 23780 27813 20760 2719 1040 812 O
ATOM 2748 OD2 ASP A 276 -3.293 141.098 226.157 1.00199.51 O
ANISOU 2748 OD2 ASP A 276 24587 29661 21558 2844 991 765 O
ATOM 2749 N LEU A 277 -3.091 138.384 221.335 1.00178.44 N
ANISOU 2749 N LEU A 277 22632 25578 19588 1638 1239 1055 N
ATOM 2750 CA LEU A 277 -3.699 137.527 220.302 1.00178.91 C
ANISOU 2750 CA LEU A 277 22800 25497 19682 1288 1307 1187 C
ATOM 2751 C LEU A 277 -2.752 136.415 219.801 1.00183.18 C
ANISOU 2751 C LEU A 277 23642 25569 20389 1124 1369 1290 C
ATOM 2752 O LEU A 277 -3.201 135.282 219.588 1.00184.07 O
ANISOU 2752 O LEU A 277 23884 25601 20453 834 1428 1486 O
ATOM 2753 CB LEU A 277 -4.208 138.378 219.125 1.00177.79 C
ANISOU 2753 CB LEU A 277 22616 25324 19612 1278 1249 1020 C
ATOM 2754 N TYR A 278 -1.444 136.741 219.648 1.00178.27 N
ANISOU 2754 N TYR A 278 23136 24661 19938 1319 1341 1160 N
ATOM 2755 CA TYR A 278 -0.397 135.816 219.203 1.00177.36 C
ANISOU 2755 CA TYR A 278 23286 24145 19958 1261 1389 1222 C
ATOM 2756 C TYR A 278 -0.067 134.738 220.260 1.00181.46 C
ANISOU 2756 C TYR A 278 23902 24670 20376 1264 1441 1411 C
ATOM 2757 O TYR A 278 -0.157 133.551 219.949 1.00181.78 O
ANISOU 2757 O TYR A 278 24187 24452 20429 1091 1486 1553 O
ATOM 2758 CB TYR A 278 0.861 136.581 218.755 1.00176.72 C
ANISOU 2758 CB TYR A 278 23241 23856 20048 1470 1337 1034 C
ATOM 2759 N LEU A 279 0.275 135.138 221.508 1.00177.34 N
ANISOU 2759 N LEU A 279 23210 24428 19743 1467 1422 1409 N
ATOM 2760 CA LEU A 279 0.600 134.197 222.593 1.00177.93 C
ANISOU 2760 CA LEU A 279 23353 24547 19707 1490 1464 1589 C
ATOM 2761 C LEU A 279 -0.675 133.616 223.259 1.00181.63 C
ANISOU 2761 C LEU A 279 23703 25357 19951 1281 1489 1791 C
ATOM 2762 O LEU A 279 -0.864 133.717 224.476 1.00182.00 O
ANISOU 2762 O LEU A 279 23541 25773 19839 1410 1480 1824 O
ATOM 2763 CB LEU A 279 1.553 134.844 223.617 1.00177.47 C
ANISOU 2763 CB LEU A 279 23186 24591 19654 1825 1429 1479 C
ATOM 2764 N LYS A 280 -1.550 133.008 222.428 1.00177.01 N
ANISOU 2764 N LYS A 280 23247 24667 19340 942 1512 1929 N
ATOM 2765 CA LYS A 280 -2.821 132.396 222.821 1.00177.98 C
ANISOU 2765 CA LYS A 280 23281 25098 19244 642 1526 2155 C
ATOM 2766 C LYS A 280 -3.234 131.331 221.806 1.00180.04 C
ANISOU 2766 C LYS A 280 23838 25035 19534 259 1533 2312 C
ATOM 2767 O LYS A 280 -2.897 131.447 220.624 1.00177.85 O
ANISOU 2767 O LYS A 280 23736 24399 19439 252 1529 2186 O
ATOM 2768 CB LYS A 280 -3.920 133.463 222.944 1.00180.43 C
ANISOU 2768 CB LYS A 280 23235 25887 19434 677 1504 2059 C
ATOM 2769 N LYS A 281 -3.987 130.308 222.276 1.00177.42 N
ANISOU 2769 N LYS A 281 23565 24844 19004 -71 1532 2593 N
ATOM 2770 CA LYS A 281 -4.499 129.155 221.515 1.00177.88 C
ANISOU 2770 CA LYS A 281 23933 24622 19032 -496 1508 2790 C
ATOM 2771 C LYS A 281 -3.361 128.194 221.101 1.00178.77 C
ANISOU 2771 C LYS A 281 24518 24118 19289 -450 1489 2802 C
ATOM 2772 O LYS A 281 -2.469 127.934 221.916 1.00178.41 O
ANISOU 2772 O LYS A 281 24564 23981 19241 -226 1495 2827 O
ATOM 2773 CB LYS A 281 -5.388 129.587 220.322 1.00179.74 C
ANISOU 2773 CB LYS A 281 24075 24917 19301 -705 1501 2713 C
ATOM 2774 N PHE A 282 -3.410 127.647 219.865 1.00172.87 N
ANISOU 2774 N PHE A 282 24069 22972 18642 -646 1461 2788 N
ATOM 2775 CA PHE A 282 -2.401 126.733 219.326 1.00171.53 C
ANISOU 2775 CA PHE A 282 24363 22229 18581 -574 1431 2780 C
ATOM 2776 C PHE A 282 -1.803 127.306 218.021 1.00168.96 C
ANISOU 2776 C PHE A 282 24083 21637 18478 -382 1452 2516 C
ATOM 2777 O PHE A 282 -1.987 126.754 216.927 1.00168.83 O
ANISOU 2777 O PHE A 282 24363 21274 18511 -554 1417 2517 O
ATOM 2778 CB PHE A 282 -2.974 125.315 219.154 1.00176.52 C
ANISOU 2778 CB PHE A 282 25403 22590 19077 -999 1348 3046 C
ATOM 2779 N ILE A 283 -1.082 128.436 218.166 1.00159.68 N
ANISOU 2779 N ILE A 283 22617 20633 17420 -30 1496 2296 N
ATOM 2780 CA ILE A 283 -0.417 129.178 217.088 1.00155.22 C
ANISOU 2780 CA ILE A 283 22022 19903 17053 175 1512 2049 C
ATOM 2781 C ILE A 283 0.697 128.398 216.390 1.00154.35 C
ANISOU 2781 C ILE A 283 22286 19327 17032 312 1503 2006 C
ATOM 2782 O ILE A 283 1.065 128.776 215.283 1.00152.96 O
ANISOU 2782 O ILE A 283 22135 18992 16989 382 1510 1844 O
ATOM 2783 CB ILE A 283 0.100 130.571 217.546 1.00156.38 C
ANISOU 2783 CB ILE A 283 21815 20329 17273 502 1530 1855 C
ATOM 2784 CG1 ILE A 283 0.711 130.545 218.975 1.00157.55 C
ANISOU 2784 CG1 ILE A 283 21894 20630 17339 730 1539 1916 C
ATOM 2785 CG2 ILE A 283 -0.988 131.627 217.403 1.00156.65 C
ANISOU 2785 CG2 ILE A 283 21516 20728 17277 412 1520 1782 C
ATOM 2786 CD1 ILE A 283 2.226 130.210 219.058 1.00164.79 C
ANISOU 2786 CD1 ILE A 283 23010 21269 18333 1018 1547 1861 C
ATOM 2787 N GLN A 284 1.256 127.352 217.033 1.00148.36 N
ANISOU 2787 N GLN A 284 21811 18374 16186 378 1484 2145 N
ATOM 2788 CA GLN A 284 2.333 126.527 216.469 1.00146.81 C
ANISOU 2788 CA GLN A 284 22000 17757 16026 566 1463 2112 C
ATOM 2789 C GLN A 284 1.897 125.822 215.177 1.00145.78 C
ANISOU 2789 C GLN A 284 22203 17277 15908 329 1416 2127 C
ATOM 2790 O GLN A 284 2.680 125.743 214.227 1.00143.91 O
ANISOU 2790 O GLN A 284 22126 16796 15758 519 1417 1984 O
ATOM 2791 CB GLN A 284 2.846 125.513 217.505 1.00150.72 C
ANISOU 2791 CB GLN A 284 22746 18133 16387 671 1433 2280 C
ATOM 2792 CG GLN A 284 3.707 126.142 218.596 1.00168.03 C
ANISOU 2792 CG GLN A 284 24672 20583 18587 1019 1480 2217 C
ATOM 2793 CD GLN A 284 5.173 125.878 218.381 1.00183.98 C
ANISOU 2793 CD GLN A 284 26874 22384 20646 1408 1487 2111 C
ATOM 2794 OE1 GLN A 284 5.693 124.822 218.757 1.00180.44 O
ANISOU 2794 OE1 GLN A 284 26781 21684 20095 1513 1446 2222 O
ATOM 2795 NE2 GLN A 284 5.875 126.841 217.793 1.00171.35 N
ANISOU 2795 NE2 GLN A 284 25033 20899 19174 1632 1527 1903 N
ATOM 2796 N GLN A 285 0.633 125.350 215.140 1.00140.28 N
ANISOU 2796 N GLN A 285 21591 16599 15111 -92 1370 2300 N
ATOM 2797 CA GLN A 285 0.027 124.674 213.990 1.00139.40 C
ANISOU 2797 CA GLN A 285 21796 16181 14988 -390 1306 2338 C
ATOM 2798 C GLN A 285 -0.220 125.677 212.857 1.00135.72 C
ANISOU 2798 C GLN A 285 21084 15818 14667 -410 1351 2144 C
ATOM 2799 O GLN A 285 -0.156 125.306 211.682 1.00135.42 O
ANISOU 2799 O GLN A 285 21301 15478 14675 -477 1318 2078 O
ATOM 2800 CB GLN A 285 -1.281 123.979 214.409 1.00143.38 C
ANISOU 2800 CB GLN A 285 22399 16760 15318 -874 1236 2605 C
ATOM 2801 CG GLN A 285 -1.404 122.525 213.941 1.00159.67 C
ANISOU 2801 CG GLN A 285 25046 18333 17287 -1131 1110 2744 C
ATOM 2802 CD GLN A 285 -0.556 121.547 214.727 1.00181.21 C
ANISOU 2802 CD GLN A 285 28206 20732 19914 -969 1033 2862 C
ATOM 2803 OE1 GLN A 285 -0.446 121.614 215.958 1.00177.13 O
ANISOU 2803 OE1 GLN A 285 27551 20415 19336 -831 1062 2949 O
ATOM 2804 NE2 GLN A 285 0.038 120.592 214.030 1.00175.72 N
ANISOU 2804 NE2 GLN A 285 28068 19517 19180 -980 920 2871 N
ATOM 2805 N VAL A 286 -0.483 126.948 213.228 1.00126.16 N
ANISOU 2805 N VAL A 286 19396 15025 13513 -336 1415 2049 N
ATOM 2806 CA VAL A 286 -0.702 128.082 212.326 1.00121.56 C
ANISOU 2806 CA VAL A 286 18533 14594 13061 -319 1450 1862 C
ATOM 2807 C VAL A 286 0.647 128.534 211.754 1.00119.49 C
ANISOU 2807 C VAL A 286 18282 14171 12948 44 1477 1654 C
ATOM 2808 O VAL A 286 0.787 128.576 210.536 1.00117.37 O
ANISOU 2808 O VAL A 286 18102 13728 12766 18 1474 1545 O
ATOM 2809 CB VAL A 286 -1.470 129.243 213.019 1.00123.95 C
ANISOU 2809 CB VAL A 286 18373 15389 13335 -336 1478 1840 C
ATOM 2810 CG1 VAL A 286 -1.485 130.508 212.157 1.00121.08 C
ANISOU 2810 CG1 VAL A 286 17755 15142 13109 -245 1493 1627 C
ATOM 2811 CG2 VAL A 286 -2.889 128.820 213.389 1.00125.73 C
ANISOU 2811 CG2 VAL A 286 18540 15847 13383 -719 1454 2048 C
ATOM 2812 N TYR A 287 1.642 128.842 212.626 1.00113.60 N
ANISOU 2812 N TYR A 287 17441 13508 12214 367 1501 1611 N
ATOM 2813 CA TYR A 287 2.974 129.247 212.190 1.00111.30 C
ANISOU 2813 CA TYR A 287 17133 13130 12027 698 1522 1443 C
ATOM 2814 C TYR A 287 3.555 128.232 211.224 1.00117.26 C
ANISOU 2814 C TYR A 287 18290 13497 12767 756 1503 1439 C
ATOM 2815 O TYR A 287 4.142 128.639 210.229 1.00116.84 O
ANISOU 2815 O TYR A 287 18220 13376 12798 894 1516 1294 O
ATOM 2816 CB TYR A 287 3.951 129.562 213.345 1.00111.37 C
ANISOU 2816 CB TYR A 287 16985 13312 12019 1007 1541 1425 C
ATOM 2817 CG TYR A 287 5.286 130.085 212.843 1.00111.76 C
ANISOU 2817 CG TYR A 287 16965 13346 12152 1312 1556 1267 C
ATOM 2818 CD1 TYR A 287 5.355 131.217 212.030 1.00112.12 C
ANISOU 2818 CD1 TYR A 287 16773 13511 12315 1308 1553 1114 C
ATOM 2819 CD2 TYR A 287 6.470 129.406 213.113 1.00113.38 C
ANISOU 2819 CD2 TYR A 287 17349 13433 12298 1595 1565 1282 C
ATOM 2820 CE1 TYR A 287 6.570 131.665 211.507 1.00112.72 C
ANISOU 2820 CE1 TYR A 287 16772 13612 12444 1541 1557 997 C
ATOM 2821 CE2 TYR A 287 7.696 129.856 212.613 1.00113.52 C
ANISOU 2821 CE2 TYR A 287 17268 13507 12358 1864 1579 1153 C
ATOM 2822 CZ TYR A 287 7.742 130.986 211.806 1.00120.96 C
ANISOU 2822 CZ TYR A 287 17956 14590 13414 1816 1575 1019 C
ATOM 2823 OH TYR A 287 8.944 131.444 211.299 1.00121.29 O
ANISOU 2823 OH TYR A 287 17883 14727 13476 2037 1580 917 O
ATOM 2824 N LEU A 288 3.322 126.927 211.462 1.00115.67 N
ANISOU 2824 N LEU A 288 18462 13044 12444 635 1456 1600 N
ATOM 2825 CA LEU A 288 3.777 125.874 210.559 1.00116.81 C
ANISOU 2825 CA LEU A 288 19058 12781 12544 696 1407 1593 C
ATOM 2826 C LEU A 288 3.106 125.961 209.190 1.00120.83 C
ANISOU 2826 C LEU A 288 19636 13159 13113 463 1389 1522 C
ATOM 2827 O LEU A 288 3.776 125.761 208.176 1.00121.42 O
ANISOU 2827 O LEU A 288 19913 13015 13207 632 1378 1409 O
ATOM 2828 CB LEU A 288 3.605 124.484 211.170 1.00119.70 C
ANISOU 2828 CB LEU A 288 19855 12875 12751 593 1326 1791 C
ATOM 2829 CG LEU A 288 4.725 124.038 212.104 1.00125.27 C
ANISOU 2829 CG LEU A 288 20697 13525 13375 957 1322 1824 C
ATOM 2830 CD1 LEU A 288 4.321 122.799 212.860 1.00128.81 C
ANISOU 2830 CD1 LEU A 288 21584 13698 13661 791 1222 2042 C
ATOM 2831 CD2 LEU A 288 6.036 123.793 211.346 1.00127.09 C
ANISOU 2831 CD2 LEU A 288 21080 13593 13615 1384 1331 1658 C
ATOM 2832 N ALA A 289 1.810 126.307 209.151 1.00116.30 N
ANISOU 2832 N ALA A 289 18874 12758 12556 101 1389 1581 N
ATOM 2833 CA ALA A 289 1.084 126.466 207.893 1.00115.70 C
ANISOU 2833 CA ALA A 289 18816 12608 12536 -137 1375 1517 C
ATOM 2834 C ALA A 289 1.552 127.735 207.134 1.00118.16 C
ANISOU 2834 C ALA A 289 18796 13101 13000 50 1437 1308 C
ATOM 2835 O ALA A 289 1.745 127.680 205.916 1.00117.22 O
ANISOU 2835 O ALA A 289 18795 12813 12931 69 1431 1202 O
ATOM 2836 CB ALA A 289 -0.410 126.521 208.161 1.00116.86 C
ANISOU 2836 CB ALA A 289 18833 12945 12623 -565 1355 1657 C
ATOM 2837 N ILE A 290 1.766 128.856 207.874 1.00113.53 N
ANISOU 2837 N ILE A 290 17815 12850 12473 186 1481 1254 N
ATOM 2838 CA ILE A 290 2.213 130.168 207.379 1.00110.56 C
ANISOU 2838 CA ILE A 290 17120 12662 12224 339 1511 1081 C
ATOM 2839 C ILE A 290 3.659 130.106 206.853 1.00114.91 C
ANISOU 2839 C ILE A 290 17760 13092 12809 661 1527 971 C
ATOM 2840 O ILE A 290 3.941 130.632 205.769 1.00113.57 O
ANISOU 2840 O ILE A 290 17529 12908 12715 684 1532 853 O
ATOM 2841 CB ILE A 290 1.990 131.271 208.465 1.00112.16 C
ANISOU 2841 CB ILE A 290 16947 13221 12446 394 1519 1067 C
ATOM 2842 CG1 ILE A 290 0.507 131.371 208.929 1.00113.09 C
ANISOU 2842 CG1 ILE A 290 16928 13542 12499 107 1505 1162 C
ATOM 2843 CG2 ILE A 290 2.521 132.633 208.049 1.00110.59 C
ANISOU 2843 CG2 ILE A 290 16478 13179 12364 551 1514 901 C
ATOM 2844 CD1 ILE A 290 -0.625 131.547 207.821 1.00120.08 C
ANISOU 2844 CD1 ILE A 290 17820 14402 13402 -187 1492 1148 C
ATOM 2845 N MET A 291 4.560 129.448 207.610 1.00113.33 N
ANISOU 2845 N MET A 291 17694 12835 12533 910 1532 1018 N
ATOM 2846 CA MET A 291 5.967 129.268 207.238 1.00113.94 C
ANISOU 2846 CA MET A 291 17844 12856 12592 1252 1547 932 C
ATOM 2847 C MET A 291 6.128 128.292 206.055 1.00119.64 C
ANISOU 2847 C MET A 291 18932 13264 13263 1281 1525 899 C
ATOM 2848 O MET A 291 7.099 128.426 205.306 1.00118.90 O
ANISOU 2848 O MET A 291 18815 13196 13167 1516 1542 789 O
ATOM 2849 CB MET A 291 6.813 128.838 208.448 1.00117.52 C
ANISOU 2849 CB MET A 291 18343 13356 12955 1519 1554 998 C
ATOM 2850 CG MET A 291 8.308 128.996 208.243 1.00121.46 C
ANISOU 2850 CG MET A 291 18770 13953 13425 1892 1577 903 C
ATOM 2851 SD MET A 291 9.301 128.444 209.654 1.00127.64 S
ANISOU 2851 SD MET A 291 19605 14809 14084 2222 1583 982 S
ATOM 2852 CE MET A 291 9.048 126.673 209.586 1.00127.40 C
ANISOU 2852 CE MET A 291 20161 14338 13907 2258 1532 1087 C
ATOM 2853 N TRP A 292 5.182 127.334 205.872 1.00118.20 N
ANISOU 2853 N TRP A 292 19082 12807 13020 1033 1476 997 N
ATOM 2854 CA TRP A 292 5.242 126.392 204.749 1.00119.82 C
ANISOU 2854 CA TRP A 292 19680 12681 13166 1041 1429 959 C
ATOM 2855 C TRP A 292 5.010 127.111 203.422 1.00122.15 C
ANISOU 2855 C TRP A 292 19808 13042 13560 943 1452 830 C
ATOM 2856 O TRP A 292 5.762 126.868 202.478 1.00122.28 O
ANISOU 2856 O TRP A 292 19949 12966 13544 1166 1452 723 O
ATOM 2857 CB TRP A 292 4.273 125.205 204.904 1.00121.08 C
ANISOU 2857 CB TRP A 292 20256 12520 13228 746 1343 1107 C
ATOM 2858 CG TRP A 292 4.552 124.107 203.915 1.00124.42 C
ANISOU 2858 CG TRP A 292 21165 12553 13556 845 1266 1057 C
ATOM 2859 CD1 TRP A 292 5.355 123.020 204.106 1.00129.97 C
ANISOU 2859 CD1 TRP A 292 22280 12986 14118 1159 1203 1062 C
ATOM 2860 CD2 TRP A 292 4.110 124.043 202.551 1.00124.13 C
ANISOU 2860 CD2 TRP A 292 21238 12376 13549 700 1241 966 C
ATOM 2861 NE1 TRP A 292 5.417 122.266 202.957 1.00131.00 N
ANISOU 2861 NE1 TRP A 292 22795 12802 14177 1222 1129 976 N
ATOM 2862 CE2 TRP A 292 4.670 122.876 201.983 1.00130.76 C
ANISOU 2862 CE2 TRP A 292 22580 12850 14254 936 1156 917 C
ATOM 2863 CE3 TRP A 292 3.269 124.847 201.758 1.00123.36 C
ANISOU 2863 CE3 TRP A 292 20880 12426 13566 404 1274 920 C
ATOM 2864 CZ2 TRP A 292 4.428 122.498 200.656 1.00130.82 C
ANISOU 2864 CZ2 TRP A 292 22829 12638 14240 879 1104 820 C
ATOM 2865 CZ3 TRP A 292 3.034 124.474 200.443 1.00125.47 C
ANISOU 2865 CZ3 TRP A 292 21372 12480 13819 328 1231 835 C
ATOM 2866 CH2 TRP A 292 3.605 123.312 199.905 1.00128.77 C
ANISOU 2866 CH2 TRP A 292 22285 12538 14105 559 1148 785 C
ATOM 2867 N LEU A 293 3.968 127.975 203.347 1.00117.03 N
ANISOU 2867 N LEU A 293 18888 12566 13012 626 1467 842 N
ATOM 2868 CA LEU A 293 3.614 128.759 202.158 1.00115.34 C
ANISOU 2868 CA LEU A 293 18490 12435 12898 491 1483 735 C
ATOM 2869 C LEU A 293 4.776 129.660 201.724 1.00118.68 C
ANISOU 2869 C LEU A 293 18658 13055 13380 769 1524 601 C
ATOM 2870 O LEU A 293 5.147 129.638 200.550 1.00118.64 O
ANISOU 2870 O LEU A 293 18738 12971 13367 854 1525 511 O
ATOM 2871 CB LEU A 293 2.378 129.638 202.434 1.00113.86 C
ANISOU 2871 CB LEU A 293 18007 12470 12784 184 1488 775 C
ATOM 2872 CG LEU A 293 1.193 129.596 201.455 1.00118.12 C
ANISOU 2872 CG LEU A 293 18557 12966 13356 -141 1469 763 C
ATOM 2873 CD1 LEU A 293 0.293 130.797 201.672 1.00116.35 C
ANISOU 2873 CD1 LEU A 293 17929 13055 13223 -250 1484 719 C
ATOM 2874 CD2 LEU A 293 1.636 129.581 200.000 1.00120.35 C
ANISOU 2874 CD2 LEU A 293 19019 13055 13653 -79 1462 655 C
ATOM 2875 N ALA A 294 5.340 130.454 202.673 1.00114.13 N
ANISOU 2875 N ALA A 294 17768 12749 12846 894 1546 597 N
ATOM 2876 CA ALA A 294 6.465 131.370 202.447 1.00112.35 C
ANISOU 2876 CA ALA A 294 17272 12756 12659 1108 1565 504 C
ATOM 2877 C ALA A 294 7.650 130.644 201.811 1.00117.40 C
ANISOU 2877 C ALA A 294 18087 13324 13194 1415 1581 454 C
ATOM 2878 O ALA A 294 8.163 131.089 200.784 1.00117.23 O
ANISOU 2878 O ALA A 294 17961 13397 13183 1473 1590 369 O
ATOM 2879 CB ALA A 294 6.887 132.009 203.758 1.00112.27 C
ANISOU 2879 CB ALA A 294 17020 12976 12660 1214 1564 537 C
ATOM 2880 N MET A 295 8.029 129.493 202.379 1.00114.97 N
ANISOU 2880 N MET A 295 18063 12854 12766 1616 1576 510 N
ATOM 2881 CA MET A 295 9.137 128.676 201.895 1.00116.45 C
ANISOU 2881 CA MET A 295 18462 12972 12812 1977 1579 460 C
ATOM 2882 C MET A 295 8.833 127.928 200.585 1.00120.67 C
ANISOU 2882 C MET A 295 19327 13232 13292 1955 1550 399 C
ATOM 2883 O MET A 295 9.776 127.553 199.888 1.00121.83 O
ANISOU 2883 O MET A 295 19578 13394 13318 2272 1553 320 O
ATOM 2884 CB MET A 295 9.630 127.710 202.991 1.00120.72 C
ANISOU 2884 CB MET A 295 19223 13417 13230 2223 1566 537 C
ATOM 2885 CG MET A 295 10.247 128.421 204.186 1.00123.37 C
ANISOU 2885 CG MET A 295 19216 14072 13586 2342 1598 570 C
ATOM 2886 SD MET A 295 11.992 128.041 204.455 1.00129.45 S
ANISOU 2886 SD MET A 295 19965 15043 14176 2871 1620 538 S
ATOM 2887 CE MET A 295 12.750 128.974 203.138 1.00125.56 C
ANISOU 2887 CE MET A 295 19238 14805 13665 2974 1646 412 C
ATOM 2888 N SER A 296 7.542 127.699 200.241 1.00115.40 N
ANISOU 2888 N SER A 296 18813 12343 12691 1595 1517 434 N
ATOM 2889 CA SER A 296 7.214 126.986 199.002 1.00115.58 C
ANISOU 2889 CA SER A 296 19159 12095 12660 1546 1475 375 C
ATOM 2890 C SER A 296 7.431 127.849 197.748 1.00118.85 C
ANISOU 2890 C SER A 296 19314 12702 13142 1519 1511 260 C
ATOM 2891 O SER A 296 7.629 127.285 196.671 1.00120.03 O
ANISOU 2891 O SER A 296 19687 12706 13212 1621 1488 179 O
ATOM 2892 CB SER A 296 5.819 126.371 199.047 1.00117.70 C
ANISOU 2892 CB SER A 296 19716 12063 12940 1165 1411 470 C
ATOM 2893 OG SER A 296 4.784 127.321 199.225 1.00120.02 O
ANISOU 2893 OG SER A 296 19722 12510 13372 785 1433 506 O
ATOM 2894 N SER A 297 7.477 129.211 197.902 1.00112.95 N
ANISOU 2894 N SER A 297 18111 12283 12520 1411 1555 252 N
ATOM 2895 CA SER A 297 7.742 130.203 196.838 1.00111.02 C
ANISOU 2895 CA SER A 297 17587 12255 12339 1365 1577 166 C
ATOM 2896 C SER A 297 9.052 129.868 196.093 1.00117.89 C
ANISOU 2896 C SER A 297 18474 13250 13067 1737 1597 84 C
ATOM 2897 O SER A 297 9.217 130.170 194.908 1.00117.51 O
ANISOU 2897 O SER A 297 18354 13285 13011 1729 1605 10 O
ATOM 2898 CB SER A 297 7.839 131.605 197.437 1.00110.41 C
ANISOU 2898 CB SER A 297 17083 12483 12386 1240 1587 188 C
ATOM 2899 OG SER A 297 8.965 131.766 198.284 1.00114.79 O
ANISOU 2899 OG SER A 297 17469 13262 12884 1496 1603 206 O
ATOM 2900 N THR A 298 9.951 129.204 196.825 1.00116.70 N
ANISOU 2900 N THR A 298 18423 13131 12787 2074 1603 102 N
ATOM 2901 CA THR A 298 11.275 128.707 196.479 1.00118.54 C
ANISOU 2901 CA THR A 298 18686 13523 12830 2514 1620 40 C
ATOM 2902 C THR A 298 11.229 127.541 195.450 1.00124.91 C
ANISOU 2902 C THR A 298 19915 14054 13492 2700 1583 -47 C
ATOM 2903 O THR A 298 12.234 127.296 194.778 1.00126.34 O
ANISOU 2903 O THR A 298 20069 14427 13507 3048 1598 -128 O
ATOM 2904 CB THR A 298 11.937 128.255 197.806 1.00127.10 C
ANISOU 2904 CB THR A 298 19832 14636 13824 2778 1621 103 C
ATOM 2905 OG1 THR A 298 11.662 129.201 198.837 1.00127.11 O
ANISOU 2905 OG1 THR A 298 19556 14769 13971 2547 1633 187 O
ATOM 2906 CG2 THR A 298 13.394 128.095 197.711 1.00125.90 C
ANISOU 2906 CG2 THR A 298 19536 14812 13489 3211 1650 62 C
ATOM 2907 N MET A 299 10.095 126.815 195.338 1.00121.51 N
ANISOU 2907 N MET A 299 19875 13195 13098 2476 1525 -27 N
ATOM 2908 CA MET A 299 10.026 125.660 194.439 1.00123.86 C
ANISOU 2908 CA MET A 299 20643 13169 13248 2635 1458 -109 C
ATOM 2909 C MET A 299 9.138 125.846 193.178 1.00128.79 C
ANISOU 2909 C MET A 299 21312 13674 13950 2336 1440 -167 C
ATOM 2910 O MET A 299 9.353 125.133 192.189 1.00130.38 O
ANISOU 2910 O MET A 299 21805 13722 14010 2535 1395 -270 O
ATOM 2911 CB MET A 299 9.610 124.396 195.216 1.00128.07 C
ANISOU 2911 CB MET A 299 21698 13260 13703 2651 1366 -41 C
ATOM 2912 CG MET A 299 8.147 124.369 195.600 1.00130.37 C
ANISOU 2912 CG MET A 299 22085 13306 14144 2129 1328 74 C
ATOM 2913 SD MET A 299 7.691 122.973 196.639 1.00137.50 S
ANISOU 2913 SD MET A 299 23610 13703 14930 2077 1196 188 S
ATOM 2914 CE MET A 299 5.944 123.296 196.848 1.00132.24 C
ANISOU 2914 CE MET A 299 22843 12964 14440 1403 1184 329 C
ATOM 2915 N TYR A 300 8.155 126.775 193.212 1.00123.35 N
ANISOU 2915 N TYR A 300 20347 13057 13463 1890 1468 -109 N
ATOM 2916 CA TYR A 300 7.206 126.988 192.110 1.00122.41 C
ANISOU 2916 CA TYR A 300 20249 12836 13426 1570 1451 -148 C
ATOM 2917 C TYR A 300 7.805 127.456 190.767 1.00125.79 C
ANISOU 2917 C TYR A 300 20477 13501 13817 1701 1487 -262 C
ATOM 2918 O TYR A 300 7.286 127.053 189.725 1.00125.52 O
ANISOU 2918 O TYR A 300 20630 13294 13768 1576 1453 -324 O
ATOM 2919 CB TYR A 300 6.079 127.944 192.522 1.00121.06 C
ANISOU 2919 CB TYR A 300 19803 12740 13453 1118 1471 -60 C
ATOM 2920 CG TYR A 300 5.294 127.497 193.735 1.00123.68 C
ANISOU 2920 CG TYR A 300 20306 12876 13811 918 1434 65 C
ATOM 2921 CD1 TYR A 300 4.611 126.284 193.742 1.00127.88 C
ANISOU 2921 CD1 TYR A 300 21319 13017 14253 803 1348 107 C
ATOM 2922 CD2 TYR A 300 5.182 128.315 194.855 1.00123.08 C
ANISOU 2922 CD2 TYR A 300 19913 13012 13838 808 1471 148 C
ATOM 2923 CE1 TYR A 300 3.872 125.876 194.853 1.00129.63 C
ANISOU 2923 CE1 TYR A 300 21680 13096 14479 574 1307 248 C
ATOM 2924 CE2 TYR A 300 4.436 127.924 195.967 1.00124.64 C
ANISOU 2924 CE2 TYR A 300 20235 13083 14040 618 1441 271 C
ATOM 2925 CZ TYR A 300 3.788 126.700 195.965 1.00134.89 C
ANISOU 2925 CZ TYR A 300 21989 14022 15241 490 1363 331 C
ATOM 2926 OH TYR A 300 3.063 126.312 197.066 1.00136.61 O
ANISOU 2926 OH TYR A 300 22310 14152 15442 273 1328 478 O
ATOM 2927 N ASN A 301 8.856 128.309 190.782 1.00121.74 N
ANISOU 2927 N ASN A 301 19579 13397 13279 1919 1549 -277 N
ATOM 2928 CA ASN A 301 9.489 128.885 189.576 1.00121.14 C
ANISOU 2928 CA ASN A 301 19244 13630 13153 2015 1585 -354 C
ATOM 2929 C ASN A 301 9.852 127.868 188.446 1.00125.45 C
ANISOU 2929 C ASN A 301 20107 14061 13497 2315 1556 -478 C
ATOM 2930 O ASN A 301 9.383 128.105 187.332 1.00124.13 O
ANISOU 2930 O ASN A 301 19900 13899 13363 2146 1554 -531 O
ATOM 2931 CB ASN A 301 10.703 129.744 189.933 1.00122.41 C
ANISOU 2931 CB ASN A 301 18972 14263 13275 2198 1636 -320 C
ATOM 2932 CG ASN A 301 10.371 131.016 190.666 1.00136.70 C
ANISOU 2932 CG ASN A 301 20405 16248 15285 1855 1645 -232 C
ATOM 2933 OD1 ASN A 301 9.202 131.383 190.863 1.00128.23 O
ANISOU 2933 OD1 ASN A 301 19374 14968 14381 1509 1623 -196 O
ATOM 2934 ND2 ASN A 301 11.408 131.710 191.101 1.00126.95 N
ANISOU 2934 ND2 ASN A 301 18801 15419 14016 1948 1666 -195 N
ATOM 2935 N PRO A 302 10.623 126.759 188.653 1.00123.93 N
ANISOU 2935 N PRO A 302 20241 13761 13087 2762 1523 -536 N
ATOM 2936 CA PRO A 302 10.891 125.837 187.526 1.00126.28 C
ANISOU 2936 CA PRO A 302 20864 13940 13176 3065 1476 -674 C
ATOM 2937 C PRO A 302 9.628 125.229 186.899 1.00130.17 C
ANISOU 2937 C PRO A 302 21771 13960 13728 2768 1393 -711 C
ATOM 2938 O PRO A 302 9.605 124.998 185.690 1.00130.76 O
ANISOU 2938 O PRO A 302 21948 14023 13711 2843 1371 -819 O
ATOM 2939 CB PRO A 302 11.789 124.761 188.145 1.00131.20 C
ANISOU 2939 CB PRO A 302 21806 14478 13565 3586 1432 -715 C
ATOM 2940 CG PRO A 302 11.539 124.845 189.608 1.00134.79 C
ANISOU 2940 CG PRO A 302 22270 14799 14146 3427 1431 -585 C
ATOM 2941 CD PRO A 302 11.292 126.288 189.884 1.00126.71 C
ANISOU 2941 CD PRO A 302 20697 14095 13352 3041 1516 -487 C
ATOM 2942 N ILE A 303 8.576 125.005 187.720 1.00125.54 N
ANISOU 2942 N ILE A 303 21397 13020 13282 2416 1344 -612 N
ATOM 2943 CA ILE A 303 7.268 124.471 187.309 1.00125.11 C
ANISOU 2943 CA ILE A 303 21708 12539 13290 2040 1256 -603 C
ATOM 2944 C ILE A 303 6.572 125.484 186.388 1.00126.68 C
ANISOU 2944 C ILE A 303 21571 12913 13647 1666 1307 -610 C
ATOM 2945 O ILE A 303 6.046 125.094 185.342 1.00126.99 O
ANISOU 2945 O ILE A 303 21851 12754 13647 1555 1251 -683 O
ATOM 2946 CB ILE A 303 6.400 124.085 188.543 1.00127.49 C
ANISOU 2946 CB ILE A 303 22210 12549 13682 1743 1205 -457 C
ATOM 2947 CG1 ILE A 303 7.147 123.103 189.469 1.00130.15 C
ANISOU 2947 CG1 ILE A 303 22918 12684 13848 2123 1140 -446 C
ATOM 2948 CG2 ILE A 303 5.030 123.530 188.127 1.00128.28 C
ANISOU 2948 CG2 ILE A 303 22630 12277 13835 1282 1111 -415 C
ATOM 2949 CD1 ILE A 303 6.850 123.270 190.939 1.00134.63 C
ANISOU 2949 CD1 ILE A 303 23410 13233 14512 1953 1153 -288 C
ATOM 2950 N ILE A 304 6.601 126.781 186.765 1.00120.65 N
ANISOU 2950 N ILE A 304 20279 12510 13052 1483 1400 -538 N
ATOM 2951 CA ILE A 304 6.028 127.869 185.963 1.00118.34 C
ANISOU 2951 CA ILE A 304 19644 12414 12906 1158 1442 -537 C
ATOM 2952 C ILE A 304 6.746 127.928 184.595 1.00123.33 C
ANISOU 2952 C ILE A 304 20207 13237 13416 1385 1460 -659 C
ATOM 2953 O ILE A 304 6.067 128.026 183.570 1.00123.02 O
ANISOU 2953 O ILE A 304 20194 13131 13416 1165 1444 -702 O
ATOM 2954 CB ILE A 304 6.025 129.259 186.701 1.00118.45 C
ANISOU 2954 CB ILE A 304 19155 12755 13096 973 1506 -442 C
ATOM 2955 CG1 ILE A 304 5.344 129.183 188.088 1.00118.02 C
ANISOU 2955 CG1 ILE A 304 19155 12540 13149 742 1488 -328 C
ATOM 2956 CG2 ILE A 304 5.363 130.357 185.845 1.00116.73 C
ANISOU 2956 CG2 ILE A 304 18621 12727 13004 683 1528 -450 C
ATOM 2957 CD1 ILE A 304 5.703 130.339 189.063 1.00122.36 C
ANISOU 2957 CD1 ILE A 304 19298 13386 13806 724 1533 -251 C
ATOM 2958 N TYR A 305 8.099 127.815 184.581 1.00120.81 N
ANISOU 2958 N TYR A 305 19794 13181 12928 1830 1492 -709 N
ATOM 2959 CA TYR A 305 8.898 127.871 183.348 1.00121.75 C
ANISOU 2959 CA TYR A 305 19794 13578 12888 2095 1516 -813 C
ATOM 2960 C TYR A 305 8.577 126.730 182.370 1.00130.29 C
ANISOU 2960 C TYR A 305 21350 14338 13816 2236 1440 -946 C
ATOM 2961 O TYR A 305 8.563 126.956 181.159 1.00129.27 O
ANISOU 2961 O TYR A 305 21125 14353 13637 2229 1451 -1020 O
ATOM 2962 CB TYR A 305 10.416 127.963 183.628 1.00123.38 C
ANISOU 2962 CB TYR A 305 19766 14201 12913 2548 1566 -820 C
ATOM 2963 CG TYR A 305 10.872 129.111 184.513 1.00122.04 C
ANISOU 2963 CG TYR A 305 19117 14386 12865 2415 1625 -694 C
ATOM 2964 CD1 TYR A 305 10.133 130.290 184.606 1.00120.39 C
ANISOU 2964 CD1 TYR A 305 18637 14204 12902 1946 1635 -604 C
ATOM 2965 CD2 TYR A 305 12.069 129.039 185.217 1.00124.10 C
ANISOU 2965 CD2 TYR A 305 19203 14973 12976 2772 1657 -670 C
ATOM 2966 CE1 TYR A 305 10.544 131.342 185.425 1.00118.54 C
ANISOU 2966 CE1 TYR A 305 18019 14254 12768 1830 1660 -497 C
ATOM 2967 CE2 TYR A 305 12.494 130.087 186.035 1.00123.20 C
ANISOU 2967 CE2 TYR A 305 18674 15172 12966 2629 1692 -552 C
ATOM 2968 CZ TYR A 305 11.727 131.236 186.137 1.00125.85 C
ANISOU 2968 CZ TYR A 305 18789 15479 13551 2155 1686 -469 C
ATOM 2969 OH TYR A 305 12.153 132.266 186.941 1.00123.77 O
ANISOU 2969 OH TYR A 305 18162 15493 13373 2024 1694 -364 O
ATOM 2970 N CYS A 306 8.281 125.525 182.894 1.00131.57 N
ANISOU 2970 N CYS A 306 22040 14055 13895 2346 1347 -970 N
ATOM 2971 CA CYS A 306 7.922 124.372 182.063 1.00135.25 C
ANISOU 2971 CA CYS A 306 23046 14138 14203 2464 1235 -1095 C
ATOM 2972 C CYS A 306 6.479 124.436 181.599 1.00141.35 C
ANISOU 2972 C CYS A 306 23954 14616 15137 1932 1186 -1064 C
ATOM 2973 O CYS A 306 6.213 124.200 180.419 1.00142.40 O
ANISOU 2973 O CYS A 306 24229 14679 15198 1919 1146 -1168 O
ATOM 2974 CB CYS A 306 8.225 123.059 182.773 1.00138.46 C
ANISOU 2974 CB CYS A 306 24004 14166 14438 2787 1126 -1125 C
ATOM 2975 SG CYS A 306 9.989 122.728 182.969 1.00144.53 S
ANISOU 2975 SG CYS A 306 24672 15302 14942 3517 1168 -1198 S
ATOM 2976 N CYS A 307 5.548 124.769 182.517 1.00137.81 N
ANISOU 2976 N CYS A 307 23441 14032 14887 1504 1188 -921 N
ATOM 2977 CA CYS A 307 4.124 124.878 182.212 1.00137.38 C
ANISOU 2977 CA CYS A 307 23464 13761 14974 975 1146 -865 C
ATOM 2978 C CYS A 307 3.811 125.924 181.115 1.00142.09 C
ANISOU 2978 C CYS A 307 23655 14651 15681 754 1218 -892 C
ATOM 2979 O CYS A 307 2.884 125.715 180.330 1.00141.83 O
ANISOU 2979 O CYS A 307 23764 14439 15687 430 1167 -903 O
ATOM 2980 CB CYS A 307 3.314 125.125 183.482 1.00136.01 C
ANISOU 2980 CB CYS A 307 23228 13498 14953 626 1147 -700 C
ATOM 2981 N LEU A 308 4.605 127.009 181.022 1.00139.17 N
ANISOU 2981 N LEU A 308 22804 14731 15345 919 1323 -898 N
ATOM 2982 CA LEU A 308 4.334 128.061 180.043 1.00138.13 C
ANISOU 2982 CA LEU A 308 22291 14880 15314 705 1379 -906 C
ATOM 2983 C LEU A 308 5.332 128.148 178.868 1.00146.04 C
ANISOU 2983 C LEU A 308 23164 16170 16154 1037 1412 -1018 C
ATOM 2984 O LEU A 308 4.885 128.194 177.714 1.00146.28 O
ANISOU 2984 O LEU A 308 23237 16179 16162 924 1394 -1088 O
ATOM 2985 CB LEU A 308 4.192 129.433 180.736 1.00135.03 C
ANISOU 2985 CB LEU A 308 21412 14774 15120 472 1449 -783 C
ATOM 2986 CG LEU A 308 3.013 129.585 181.717 1.00138.41 C
ANISOU 2986 CG LEU A 308 21876 15012 15702 124 1426 -671 C
ATOM 2987 CD1 LEU A 308 3.240 130.737 182.667 1.00136.33 C
ANISOU 2987 CD1 LEU A 308 21186 15035 15579 49 1480 -578 C
ATOM 2988 CD2 LEU A 308 1.690 129.777 180.989 1.00140.36 C
ANISOU 2988 CD2 LEU A 308 22202 15100 16028 -282 1387 -662 C
ATOM 2989 N ASN A 309 6.658 128.189 179.142 1.00144.69 N
ANISOU 2989 N ASN A 309 22816 16304 15856 1435 1459 -1030 N
ATOM 2990 CA ASN A 309 7.666 128.338 178.085 1.00146.25 C
ANISOU 2990 CA ASN A 309 22827 16876 15866 1762 1496 -1115 C
ATOM 2991 C ASN A 309 8.067 127.041 177.388 1.00155.55 C
ANISOU 2991 C ASN A 309 24454 17868 16779 2177 1430 -1277 C
ATOM 2992 O ASN A 309 8.330 126.028 178.039 1.00157.04 O
ANISOU 2992 O ASN A 309 25039 17774 16856 2438 1367 -1317 O
ATOM 2993 CB ASN A 309 8.895 129.072 178.582 1.00145.16 C
ANISOU 2993 CB ASN A 309 22263 17217 15673 1984 1569 -1045 C
ATOM 2994 CG ASN A 309 9.274 130.220 177.690 1.00156.28 C
ANISOU 2994 CG ASN A 309 23193 19107 17080 1885 1623 -1008 C
ATOM 2995 OD1 ASN A 309 8.513 131.184 177.514 1.00140.98 O
ANISOU 2995 OD1 ASN A 309 21038 17188 15341 1466 1628 -936 O
ATOM 2996 ND2 ASN A 309 10.457 130.132 177.102 1.00149.23 N
ANISOU 2996 ND2 ASN A 309 22125 18633 15941 2275 1657 -1049 N
ATOM 2997 N ASP A 310 8.149 127.114 176.045 1.00154.76 N
ANISOU 2997 N ASP A 310 24294 17941 16566 2253 1435 -1372 N
ATOM 2998 CA ASP A 310 8.467 126.027 175.108 1.00158.80 C
ANISOU 2998 CA ASP A 310 25208 18320 16809 2649 1362 -1550 C
ATOM 2999 C ASP A 310 9.893 125.455 175.241 1.00164.50 C
ANISOU 2999 C ASP A 310 25946 19326 17231 3294 1373 -1631 C
ATOM 3000 O ASP A 310 10.060 124.233 175.202 1.00167.05 O
ANISOU 3000 O ASP A 310 26787 19334 17352 3666 1273 -1759 O
ATOM 3001 CB ASP A 310 8.219 126.480 173.647 1.00161.28 C
ANISOU 3001 CB ASP A 310 25367 18818 17093 2527 1378 -1616 C
ATOM 3002 CG ASP A 310 6.873 127.140 173.387 1.00175.08 C
ANISOU 3002 CG ASP A 310 27040 20369 19112 1922 1375 -1539 C
ATOM 3003 OD1 ASP A 310 5.912 126.414 173.048 1.00177.60 O
ANISOU 3003 OD1 ASP A 310 27799 20218 19463 1731 1280 -1591 O
ATOM 3004 OD2 ASP A 310 6.792 128.386 173.493 1.00179.62 O
ANISOU 3004 OD2 ASP A 310 27125 21273 19848 1641 1454 -1426 O
ATOM 3005 N ARG A 311 10.916 126.333 175.340 1.00159.40 N
ANISOU 3005 N ARG A 311 24747 19283 16533 3427 1479 -1555 N
ATOM 3006 CA ARG A 311 12.330 125.934 175.421 1.00161.43 C
ANISOU 3006 CA ARG A 311 24911 19947 16478 4035 1504 -1613 C
ATOM 3007 C ARG A 311 12.718 125.353 176.776 1.00164.61 C
ANISOU 3007 C ARG A 311 25516 20173 16857 4266 1480 -1580 C
ATOM 3008 O ARG A 311 13.471 124.376 176.815 1.00167.33 O
ANISOU 3008 O ARG A 311 26119 20549 16908 4840 1436 -1695 O
ATOM 3009 CB ARG A 311 13.292 127.069 175.006 1.00160.91 C
ANISOU 3009 CB ARG A 311 24167 20634 16336 4053 1613 -1519 C
ATOM 3010 CG ARG A 311 12.832 128.489 175.352 1.00167.05 C
ANISOU 3010 CG ARG A 311 24488 21555 17428 3468 1671 -1324 C
ATOM 3011 CD ARG A 311 12.982 129.457 174.181 1.00174.62 C
ANISOU 3011 CD ARG A 311 24975 23003 18369 3265 1721 -1264 C
ATOM 3012 NE ARG A 311 12.234 129.035 172.992 1.00181.90 N
ANISOU 3012 NE ARG A 311 26115 23764 19236 3247 1689 -1391 N
ATOM 3013 CZ ARG A 311 10.956 129.324 172.757 1.00195.16 C
ANISOU 3013 CZ ARG A 311 27953 25043 21156 2803 1655 -1390 C
ATOM 3014 NH1 ARG A 311 10.260 130.049 173.626 1.00180.20 N
ANISOU 3014 NH1 ARG A 311 26019 22880 19567 2356 1651 -1272 N
ATOM 3015 NH2 ARG A 311 10.364 128.889 171.652 1.00183.28 N
ANISOU 3015 NH2 ARG A 311 26641 23428 19569 2820 1623 -1510 N
ATOM 3016 N PHE A 312 12.207 125.947 177.879 1.00157.16 N
ANISOU 3016 N PHE A 312 24461 19053 16200 3849 1502 -1429 N
ATOM 3017 CA PHE A 312 12.471 125.495 179.249 1.00156.58 C
ANISOU 3017 CA PHE A 312 24559 18801 16135 4002 1482 -1376 C
ATOM 3018 C PHE A 312 11.947 124.080 179.475 1.00161.56 C
ANISOU 3018 C PHE A 312 25909 18799 16679 4179 1349 -1481 C
ATOM 3019 O PHE A 312 12.645 123.271 180.093 1.00163.06 O
ANISOU 3019 O PHE A 312 26349 18924 16684 4618 1307 -1522 O
ATOM 3020 CB PHE A 312 11.879 126.469 180.284 1.00154.46 C
ANISOU 3020 CB PHE A 312 24004 18494 16188 3494 1529 -1197 C
ATOM 3021 CG PHE A 312 12.718 127.695 180.565 1.00153.98 C
ANISOU 3021 CG PHE A 312 23317 19027 16162 3443 1624 -1076 C
ATOM 3022 CD1 PHE A 312 13.797 127.635 181.440 1.00157.95 C
ANISOU 3022 CD1 PHE A 312 23668 19830 16517 3797 1655 -1038 C
ATOM 3023 CD2 PHE A 312 12.408 128.918 179.983 1.00153.22 C
ANISOU 3023 CD2 PHE A 312 22804 19174 16240 3020 1667 -990 C
ATOM 3024 CE1 PHE A 312 14.565 128.771 181.709 1.00157.42 C
ANISOU 3024 CE1 PHE A 312 23033 20313 16467 3707 1723 -914 C
ATOM 3025 CE2 PHE A 312 13.174 130.055 180.258 1.00154.69 C
ANISOU 3025 CE2 PHE A 312 22457 19872 16445 2934 1722 -866 C
ATOM 3026 CZ PHE A 312 14.248 129.974 181.118 1.00153.98 C
ANISOU 3026 CZ PHE A 312 22217 20087 16203 3262 1748 -825 C
ATOM 3027 N ARG A 313 10.738 123.771 178.939 1.00157.57 N
ANISOU 3027 N ARG A 313 25748 17835 16285 3836 1270 -1521 N
ATOM 3028 CA ARG A 313 10.128 122.441 179.052 1.00160.01 C
ANISOU 3028 CA ARG A 313 26782 17505 16508 3913 1111 -1605 C
ATOM 3029 C ARG A 313 10.870 121.403 178.199 1.00167.69 C
ANISOU 3029 C ARG A 313 28148 18448 17119 4539 1019 -1812 C
ATOM 3030 O ARG A 313 10.855 120.219 178.539 1.00170.37 O
ANISOU 3030 O ARG A 313 29096 18335 17301 4811 874 -1887 O
ATOM 3031 CB ARG A 313 8.601 122.450 178.792 1.00158.65 C
ANISOU 3031 CB ARG A 313 26838 16886 16557 3305 1044 -1559 C
ATOM 3032 CG ARG A 313 8.140 122.693 177.358 1.00165.76 C
ANISOU 3032 CG ARG A 313 27710 17831 17441 3161 1036 -1655 C
ATOM 3033 CD ARG A 313 6.680 122.309 177.181 1.00170.14 C
ANISOU 3033 CD ARG A 313 28647 17863 18135 2650 926 -1627 C
ATOM 3034 NE ARG A 313 5.768 123.431 177.414 1.00169.45 N
ANISOU 3034 NE ARG A 313 28130 17903 18349 2061 1017 -1472 N
ATOM 3035 CZ ARG A 313 5.149 124.110 176.451 1.00179.59 C
ANISOU 3035 CZ ARG A 313 29126 19372 19739 1768 1068 -1477 C
ATOM 3036 NH1 ARG A 313 5.335 123.789 175.176 1.00164.40 N
ANISOU 3036 NH1 ARG A 313 27276 17538 17651 1985 1047 -1623 N
ATOM 3037 NH2 ARG A 313 4.337 125.114 176.756 1.00165.23 N
ANISOU 3037 NH2 ARG A 313 26949 17658 18173 1280 1136 -1341 N
ATOM 3038 N LEU A 314 11.539 121.855 177.116 1.00164.19 N
ANISOU 3038 N LEU A 314 27360 18500 16523 4781 1092 -1899 N
ATOM 3039 CA LEU A 314 12.356 121.007 176.246 1.00167.97 C
ANISOU 3039 CA LEU A 314 28120 19080 16620 5440 1020 -2104 C
ATOM 3040 C LEU A 314 13.721 120.774 176.913 1.00172.75 C
ANISOU 3040 C LEU A 314 28584 20073 16982 6045 1061 -2116 C
ATOM 3041 O LEU A 314 14.334 119.724 176.708 1.00176.23 O
ANISOU 3041 O LEU A 314 29461 20403 17096 6659 954 -2279 O
ATOM 3042 CB LEU A 314 12.528 121.650 174.860 1.00167.86 C
ANISOU 3042 CB LEU A 314 27747 19513 16518 5458 1090 -2178 C
ATOM 3043 N GLY A 315 14.156 121.751 177.718 1.00166.06 N
ANISOU 3043 N GLY A 315 27149 19661 16286 5865 1202 -1945 N
ATOM 3044 CA GLY A 315 15.406 121.725 178.476 1.00166.94 C
ANISOU 3044 CA GLY A 315 27019 20206 16203 6336 1259 -1915 C
ATOM 3045 C GLY A 315 15.386 120.738 179.627 1.00170.78 C
ANISOU 3045 C GLY A 315 28012 20215 16661 6542 1158 -1913 C
ATOM 3046 O GLY A 315 16.366 120.016 179.849 1.00173.21 O
ANISOU 3046 O GLY A 315 28449 20698 16665 7173 1127 -1994 O
ATOM 3047 N PHE A 316 14.260 120.704 180.368 1.00164.36 N
ANISOU 3047 N PHE A 316 27480 18822 16148 6012 1102 -1813 N
ATOM 3048 CA PHE A 316 14.033 119.769 181.469 1.00165.12 C
ANISOU 3048 CA PHE A 316 28099 18394 16246 6092 989 -1783 C
ATOM 3049 C PHE A 316 13.859 118.359 180.900 1.00172.80 C
ANISOU 3049 C PHE A 316 29874 18819 16963 6466 785 -1966 C
ATOM 3050 O PHE A 316 14.311 117.392 181.517 1.00174.99 O
ANISOU 3050 O PHE A 316 30614 18814 17062 6864 671 -2006 O
ATOM 3051 CB PHE A 316 12.800 120.183 182.284 1.00163.25 C
ANISOU 3051 CB PHE A 316 27859 17782 16387 5368 994 -1606 C
ATOM 3052 CG PHE A 316 13.094 121.069 183.474 1.00161.74 C
ANISOU 3052 CG PHE A 316 27157 17918 16380 5180 1122 -1430 C
ATOM 3053 CD1 PHE A 316 13.065 120.558 184.766 1.00165.32 C
ANISOU 3053 CD1 PHE A 316 27853 18111 16850 5243 1075 -1348 C
ATOM 3054 CD2 PHE A 316 13.378 122.419 183.305 1.00160.52 C
ANISOU 3054 CD2 PHE A 316 26301 18317 16374 4932 1273 -1344 C
ATOM 3055 CE1 PHE A 316 13.319 121.381 185.866 1.00163.65 C
ANISOU 3055 CE1 PHE A 316 27177 18200 16801 5074 1186 -1194 C
ATOM 3056 CE2 PHE A 316 13.635 123.239 184.404 1.00160.75 C
ANISOU 3056 CE2 PHE A 316 25898 18617 16562 4755 1366 -1190 C
ATOM 3057 CZ PHE A 316 13.605 122.715 185.677 1.00159.45 C
ANISOU 3057 CZ PHE A 316 25968 18205 16412 4838 1326 -1122 C
ATOM 3058 N LYS A 317 13.233 118.259 179.698 1.00169.72 N
ANISOU 3058 N LYS A 317 29665 18275 16545 6346 726 -2080 N
ATOM 3059 CA LYS A 317 13.019 117.019 178.945 1.00173.44 C
ANISOU 3059 CA LYS A 317 30900 18238 16763 6674 515 -2275 C
ATOM 3060 C LYS A 317 14.371 116.422 178.552 1.00181.79 C
ANISOU 3060 C LYS A 317 32051 19635 17385 7570 484 -2464 C
ATOM 3061 O LYS A 317 14.543 115.208 178.641 1.00182.61 O
ANISOU 3061 O LYS A 317 32176 19506 17703 7476 341 -2577 O
ATOM 3062 CB LYS A 317 12.161 117.275 177.695 1.00174.56 C
ANISOU 3062 CB LYS A 317 31076 18262 16988 6310 490 -2343 C
ATOM 3063 N HIS A 318 15.342 117.284 178.173 1.00177.21 N
ANISOU 3063 N HIS A 318 30755 19868 16708 7822 669 -2457 N
ATOM 3064 CA HIS A 318 16.709 116.892 177.812 1.00180.48 C
ANISOU 3064 CA HIS A 318 31021 20812 16740 8599 683 -2607 C
ATOM 3065 C HIS A 318 17.509 116.407 179.040 1.00181.70 C
ANISOU 3065 C HIS A 318 30617 21124 17297 8322 714 -2538 C
ATOM 3066 O HIS A 318 18.499 115.687 178.877 1.00181.90 O
ANISOU 3066 O HIS A 318 30275 21469 17371 8476 724 -2650 O
ATOM 3067 CB HIS A 318 17.433 118.045 177.099 1.00180.01 C
ANISOU 3067 CB HIS A 318 30174 21641 16581 8680 882 -2569 C
ATOM 3068 N ALA A 319 17.067 116.791 180.260 1.00179.98 N
ANISOU 3068 N ALA A 319 31071 20511 16803 8616 693 -2373 N
ATOM 3069 CA ALA A 319 17.678 116.395 181.531 1.00179.69 C
ANISOU 3069 CA ALA A 319 30939 20490 16844 8717 687 -2299 C
ATOM 3070 C ALA A 319 16.906 115.204 182.135 1.00181.73 C
ANISOU 3070 C ALA A 319 31362 20045 17641 8047 508 -2300 C
ATOM 3071 O ALA A 319 16.389 115.283 183.254 1.00180.77 O
ANISOU 3071 O ALA A 319 31583 19585 17518 8005 476 -2153 O
ATOM 3072 CB ALA A 319 17.699 117.579 182.489 1.00176.98 C
ANISOU 3072 CB ALA A 319 30122 20448 16676 8398 859 -2067 C
ATOM 3073 N PHE A 320 16.825 114.099 181.361 1.00180.82 N
ANISOU 3073 N PHE A 320 31497 19621 17587 8018 361 -2475 N
ATOM 3074 CA PHE A 320 16.141 112.850 181.723 1.00181.36 C
ANISOU 3074 CA PHE A 320 31959 19020 17930 7691 160 -2494 C
ATOM 3075 C PHE A 320 16.893 111.605 181.202 1.00184.71 C
ANISOU 3075 C PHE A 320 31922 19600 18658 7627 125 -2667 C
ATOM 3076 O PHE A 320 16.995 111.393 179.985 1.00184.38 O
ANISOU 3076 O PHE A 320 31739 19751 18565 7710 146 -2831 O
ATOM 3077 CB PHE A 320 14.676 112.865 181.246 1.00182.62 C
ANISOU 3077 CB PHE A 320 32523 18645 18220 7190 52 -2468 C
ATOM 3078 N ARG A 321 17.429 110.797 182.146 1.00182.61 N
ANISOU 3078 N ARG A 321 31823 19129 18432 7794 40 -2643 N
ATOM 3079 CA ARG A 321 18.188 109.573 181.875 1.00200.05 C
ANISOU 3079 CA ARG A 321 32543 21753 21715 6791 180 -2697 C
ATOM 3080 C ARG A 321 17.773 108.453 182.824 1.00205.60 C
ANISOU 3080 C ARG A 321 33027 22093 22997 6239 97 -2588 C
ATOM 3081 O ARG A 321 16.595 108.112 182.903 1.00174.17 O
ANISOU 3081 O ARG A 321 31966 16742 17469 7820 -412 -2695 O
ATOM 3082 CB ARG A 321 19.695 109.838 182.003 1.00200.17 C
ANISOU 3082 CB ARG A 321 32087 22351 21619 7090 333 -2729 C
TER 3083 ARG A 321
HETATM 3084 C13 GBQ A1201 12.083 137.184 205.492 1.00112.12 C
HETATM 3085 C21 GBQ A1201 12.138 137.707 213.867 1.00 98.68 C
HETATM 3086 C22 GBQ A1201 12.755 136.375 213.449 1.00 99.45 C
HETATM 3087 C24 GBQ A1201 11.514 139.913 213.255 1.00 98.65 C
HETATM 3088 C01 GBQ A1201 15.121 135.625 209.844 1.00106.72 C
HETATM 3089 C02 GBQ A1201 13.602 135.620 209.885 1.00107.35 C
HETATM 3090 C03 GBQ A1201 13.071 135.379 208.604 1.00111.63 C
HETATM 3091 C04 GBQ A1201 12.858 136.405 207.668 1.00113.42 C
HETATM 3092 C05 GBQ A1201 12.298 136.133 206.412 1.00114.39 C
HETATM 3093 C06 GBQ A1201 11.967 134.801 206.099 1.00117.18 C
HETATM 3094 C07 GBQ A1201 12.164 133.756 207.023 1.00118.59 C
HETATM 3095 C08 GBQ A1201 12.718 134.068 208.271 1.00114.79 C
HETATM 3096 C09 GBQ A1201 11.836 132.403 206.726 1.00123.39 C
HETATM 3097 C18 GBQ A1201 11.829 136.660 211.182 1.00102.52 C
HETATM 3098 C19 GBQ A1201 11.162 138.028 211.599 1.00100.35 C
HETATM 3099 C25 GBQ A1201 12.810 140.672 213.528 1.00101.68 C
HETATM 3100 C27 GBQ A1201 14.353 141.764 214.431 1.00103.47 C
HETATM 3101 C31 GBQ A1201 10.994 138.842 210.443 1.00 99.78 C
HETATM 3102 C32 GBQ A1201 12.001 139.697 209.958 1.00 99.85 C
HETATM 3103 C33 GBQ A1201 11.779 140.475 208.819 1.00100.62 C
HETATM 3104 C34 GBQ A1201 10.542 140.413 208.166 1.00101.99 C
HETATM 3105 C35 GBQ A1201 9.526 139.568 208.634 1.00100.38 C
HETATM 3106 C36 GBQ A1201 9.760 138.787 209.772 1.00 99.78 C
HETATM 3107 F10 GBQ A1201 12.990 131.649 206.697 1.00125.38 F
HETATM 3108 F11 GBQ A1201 10.985 131.879 207.726 1.00124.94 F
HETATM 3109 F12 GBQ A1201 11.180 132.265 205.463 1.00123.67 F
HETATM 3110 F14 GBQ A1201 11.355 138.139 206.022 1.00111.50 F
HETATM 3111 F15 GBQ A1201 11.469 136.765 204.460 1.00111.49 F
HETATM 3112 F16 GBQ A1201 13.203 137.684 205.135 1.00111.95 F
HETATM 3113 F37 GBQ A1201 10.330 141.192 207.065 1.00104.28 F
HETATM 3114 N20 GBQ A1201 11.939 138.618 212.717 1.00 98.47 N
HETATM 3115 N26 GBQ A1201 13.112 141.332 214.638 1.00101.94 N
HETATM 3116 N29 GBQ A1201 14.835 141.362 213.266 1.00103.99 N
HETATM 3117 N30 GBQ A1201 13.854 140.647 212.700 1.00104.53 N
HETATM 3118 O17 GBQ A1201 13.127 136.844 210.491 1.00104.38 O
HETATM 3119 O23 GBQ A1201 11.952 135.794 212.373 1.00101.06 O
HETATM 3120 O28 GBQ A1201 14.991 142.449 215.212 1.00105.45 O
HETATM 3121 C10 OLC A1202 2.068 142.827 190.476 1.00108.59 C
HETATM 3122 C9 OLC A1202 2.115 142.637 188.932 1.00108.89 C
HETATM 3123 C11 OLC A1202 0.932 142.193 191.297 1.00106.78 C
HETATM 3124 C8 OLC A1202 1.016 141.828 188.223 1.00107.85 C
HETATM 3125 C24 OLC A1202 -6.039 146.634 178.959 1.00138.44 C
HETATM 3126 C12 OLC A1202 1.544 141.441 192.479 1.00105.94 C
HETATM 3127 C7 OLC A1202 0.096 142.803 187.492 1.00108.16 C
HETATM 3128 C6 OLC A1202 0.157 142.558 185.987 1.00110.27 C
HETATM 3129 C5 OLC A1202 -0.509 143.726 185.259 1.00113.75 C
HETATM 3130 C4 OLC A1202 -1.669 143.232 184.386 1.00117.61 C
HETATM 3131 C3 OLC A1202 -1.263 143.295 182.908 1.00122.32 C
HETATM 3132 C2 OLC A1202 -1.952 144.477 182.203 1.00127.24 C
HETATM 3133 C21 OLC A1202 -4.011 145.125 179.273 1.00136.88 C
HETATM 3134 C1 OLC A1202 -2.634 144.036 180.889 1.00132.34 C
HETATM 3135 C22 OLC A1202 -5.521 145.174 178.957 1.00137.74 C
HETATM 3136 O19 OLC A1202 -2.147 143.153 180.175 1.00132.99 O
HETATM 3137 O25 OLC A1202 -6.224 147.146 180.296 1.00138.02 O
HETATM 3138 O23 OLC A1202 -5.780 144.548 177.684 1.00136.51 O
HETATM 3139 O20 OLC A1202 -3.820 144.672 180.630 1.00135.48 O
CONECT 612 1193
CONECT 1193 612
CONECT 3084 3092 3110 3111 3112
CONECT 3085 3086 3114
CONECT 3086 3085 3119
CONECT 3087 3099 3114
CONECT 3088 3089
CONECT 3089 3088 3090 3118
CONECT 3090 3089 3091 3095
CONECT 3091 3090 3092
CONECT 3092 3084 3091 3093
CONECT 3093 3092 3094
CONECT 3094 3093 3095 3096
CONECT 3095 3090 3094
CONECT 3096 3094 3107 3108 3109
CONECT 3097 3098 3118 3119
CONECT 3098 3097 3101 3114
CONECT 3099 3087 3115 3117
CONECT 3100 3115 3116 3120
CONECT 3101 3098 3102 3106
CONECT 3102 3101 3103
CONECT 3103 3102 3104
CONECT 3104 3103 3105 3113
CONECT 3105 3104 3106
CONECT 3106 3101 3105
CONECT 3107 3096
CONECT 3108 3096
CONECT 3109 3096
CONECT 3110 3084
CONECT 3111 3084
CONECT 3112 3084
CONECT 3113 3104
CONECT 3114 3085 3087 3098
CONECT 3115 3099 3100
CONECT 3116 3100 3117
CONECT 3117 3099 3116
CONECT 3118 3089 3097
CONECT 3119 3086 3097
CONECT 3120 3100
CONECT 3121 3122 3123
CONECT 3122 3121 3124
CONECT 3123 3121 3126
CONECT 3124 3122 3127
CONECT 3125 3135 3137
CONECT 3126 3123
CONECT 3127 3124 3128
CONECT 3128 3127 3129
CONECT 3129 3128 3130
CONECT 3130 3129 3131
CONECT 3131 3130 3132
CONECT 3132 3131 3134
CONECT 3133 3135 3139
CONECT 3134 3132 3136 3139
CONECT 3135 3125 3133 3138
CONECT 3136 3134
CONECT 3137 3125
CONECT 3138 3135
CONECT 3139 3133 3134
MASTER 386 0 2 21 2 0 5 6 3138 1 58 34
END