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*** eliza ***elNémo ID: 230809184619996707Job options:ID = 230809184619996707 JOBID = eliza USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:
HEADER eliza
HEADER APOPTOSIS 07-JAN-17 5UG6
TITLE PERFORIN C2 DOMAIN - T431D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERFORIN-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2 DOMAIN (UNP RESIDUES 410-535);
COMPND 5 SYNONYM: P1,CYTOLYSIN,LYMPHOCYTE PORE-FORMING PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PRF1, PFP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10F';
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PHAGEMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCOMB3X
KEYWDS C2, PERFORIN, CALCIUM, PROTEOSTASIS, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR R.H.P.LAW,P.J.CONROY,I.VOSKOBOINIK,J.C.WHISSTOCK
REVDAT 4 12-SEP-18 5UG6 1 JRNL
REVDAT 3 18-APR-18 5UG6 1 REMARK
REVDAT 2 21-FEB-18 5UG6 1 JRNL
REVDAT 1 07-FEB-18 5UG6 0
JRNL AUTH A.J.BRENNAN,R.H.P.LAW,P.J.CONROY,T.NOORI,N.LUKOYANOVA,
JRNL AUTH 2 H.SAIBIL,H.YAGITA,A.CICCONE,S.VERSCHOOR,J.C.WHISSTOCK,
JRNL AUTH 3 J.A.TRAPANI,I.VOSKOBOINIK
JRNL TITL PERFORIN PROTEOSTASIS IS REGULATED THROUGH ITS C2 DOMAIN:
JRNL TITL 2 SUPRA-PHYSIOLOGICAL CELL DEATH MEDIATED BY T431D-PERFORIN.
JRNL REF CELL DEATH DIFFER. V. 25 1517 2018
JRNL REFN ISSN 1476-5403
JRNL PMID 29416110
JRNL DOI 10.1038/S41418-018-0057-Z
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 9810
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.780
REMARK 3 FREE R VALUE TEST SET COUNT : 469
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 : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2702
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1910
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2587
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE : 0.2250
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.26
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 115
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 : 956
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.79010
REMARK 3 B22 (A**2) : 6.88780
REMARK 3 B33 (A**2) : 0.90230
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) : 0.280
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.174
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.148
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.162
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.143
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 982 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 1333 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 324 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 24 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 147 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 982 ; 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 : 119 ; 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 : 1154 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.12
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.85
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.79
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|410 - A|419 }
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6092 -29.1146 -9.4360
REMARK 3 T TENSOR
REMARK 3 T11: 0.0456 T22: 0.0786
REMARK 3 T33: 0.0552 T12: 0.0366
REMARK 3 T13: -0.0178 T23: -0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 7.4925 L22: 5.3489
REMARK 3 L33: 0.0000 L12: -4.3810
REMARK 3 L13: 2.5297 L23: -0.7956
REMARK 3 S TENSOR
REMARK 3 S11: -0.1963 S12: -0.1114 S13: 0.2663
REMARK 3 S21: -0.0648 S22: 0.1555 S23: -0.4640
REMARK 3 S31: -0.0841 S32: 0.2237 S33: 0.0407
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|420 - A|442 }
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7468 -10.6473 -14.1672
REMARK 3 T TENSOR
REMARK 3 T11: 0.0216 T22: -0.0695
REMARK 3 T33: -0.0371 T12: 0.0035
REMARK 3 T13: 0.0133 T23: 0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 3.0980 L22: 0.6203
REMARK 3 L33: 2.9156 L12: 0.8167
REMARK 3 L13: 0.9830 L23: -0.6373
REMARK 3 S TENSOR
REMARK 3 S11: 0.0747 S12: 0.3139 S13: -0.1320
REMARK 3 S21: 0.0643 S22: -0.1139 S23: 0.2020
REMARK 3 S31: -0.2996 S32: -0.1083 S33: 0.0392
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|443 - A|448 }
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0261 -16.3372 -17.5807
REMARK 3 T TENSOR
REMARK 3 T11: 0.0737 T22: 0.0633
REMARK 3 T33: 0.1562 T12: -0.0110
REMARK 3 T13: -0.0417 T23: 0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 10.0841 L22: 5.8572
REMARK 3 L33: 13.1505 L12: -7.3542
REMARK 3 L13: 2.3106 L23: -3.3193
REMARK 3 S TENSOR
REMARK 3 S11: 0.0190 S12: 1.0017 S13: 0.5597
REMARK 3 S21: 0.0019 S22: -0.5110 S23: -0.9391
REMARK 3 S31: -0.4606 S32: 0.7283 S33: 0.4919
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|449 - A|462 }
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6694 -11.3153 -19.7414
REMARK 3 T TENSOR
REMARK 3 T11: 0.1082 T22: 0.0468
REMARK 3 T33: 0.0439 T12: -0.0143
REMARK 3 T13: -0.0102 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 6.1884 L22: 4.1981
REMARK 3 L33: 6.0142 L12: -2.4642
REMARK 3 L13: -0.1741 L23: -0.3410
REMARK 3 S TENSOR
REMARK 3 S11: 0.0889 S12: 0.3186 S13: -0.1956
REMARK 3 S21: -0.2473 S22: -0.0766 S23: 0.3010
REMARK 3 S31: -0.0628 S32: 0.1927 S33: -0.0122
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|463 - A|470 }
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0783 -25.3668 -14.2855
REMARK 3 T TENSOR
REMARK 3 T11: 0.1360 T22: 0.0482
REMARK 3 T33: 0.0622 T12: -0.0145
REMARK 3 T13: -0.0174 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 2.9119 L22: 2.7029
REMARK 3 L33: 4.2962 L12: -1.7697
REMARK 3 L13: 0.3449 L23: -2.2191
REMARK 3 S TENSOR
REMARK 3 S11: 0.1749 S12: 0.0267 S13: -0.2141
REMARK 3 S21: -0.1688 S22: 0.0347 S23: -0.0044
REMARK 3 S31: 0.0797 S32: 0.0092 S33: -0.2096
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { A|471 - A|476 }
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9208 -22.0329 -4.5010
REMARK 3 T TENSOR
REMARK 3 T11: 0.3205 T22: 0.1472
REMARK 3 T33: 0.1991 T12: -0.0341
REMARK 3 T13: -0.1587 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 2.1279 L22: 1.0415
REMARK 3 L33: 0.0000 L12: 2.0871
REMARK 3 L13: 2.0274 L23: -0.2282
REMARK 3 S TENSOR
REMARK 3 S11: 0.1711 S12: -0.1327 S13: 0.0919
REMARK 3 S21: 0.2045 S22: -0.0039 S23: -0.3191
REMARK 3 S31: -0.4747 S32: 0.2304 S33: -0.1672
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { A|477 - A|498 }
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8515 -6.2083 -13.0952
REMARK 3 T TENSOR
REMARK 3 T11: 0.1876 T22: 0.0821
REMARK 3 T33: 0.1096 T12: 0.0147
REMARK 3 T13: -0.0246 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 2.5884 L22: 2.5213
REMARK 3 L33: 6.3353 L12: -0.7537
REMARK 3 L13: 3.7142 L23: -4.0772
REMARK 3 S TENSOR
REMARK 3 S11: -0.2486 S12: 0.1198 S13: 0.2945
REMARK 3 S21: 0.2973 S22: -0.1384 S23: -0.2595
REMARK 3 S31: -0.4131 S32: -0.0021 S33: 0.3870
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { A|499 - A|510 }
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1379 -21.6059 -3.5405
REMARK 3 T TENSOR
REMARK 3 T11: 0.1329 T22: 0.0014
REMARK 3 T33: 0.0087 T12: 0.0077
REMARK 3 T13: -0.0203 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 4.4718 L22: 1.3386
REMARK 3 L33: 0.0000 L12: -4.2025
REMARK 3 L13: -0.0946 L23: 0.5995
REMARK 3 S TENSOR
REMARK 3 S11: -0.1749 S12: -0.2960 S13: -0.0929
REMARK 3 S21: 0.3564 S22: 0.2599 S23: 0.0944
REMARK 3 S31: -0.1446 S32: 0.0378 S33: -0.0850
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { A|511 - A|535 }
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9819 -24.7503 -5.4289
REMARK 3 T TENSOR
REMARK 3 T11: 0.0736 T22: -0.0150
REMARK 3 T33: -0.0101 T12: -0.0233
REMARK 3 T13: 0.0189 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 2.7552 L22: 4.4052
REMARK 3 L33: 2.1011 L12: -1.8506
REMARK 3 L13: 0.4503 L23: 0.7530
REMARK 3 S TENSOR
REMARK 3 S11: 0.1721 S12: 0.0697 S13: -0.1876
REMARK 3 S21: 0.1001 S22: -0.0018 S23: 0.1235
REMARK 3 S31: 0.1123 S32: 0.1154 S33: -0.1702
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5UG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225371.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9857
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 49.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.32500
REMARK 200 FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 1.51400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: 3NSJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM IODIDE, 20% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 13.88700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.43350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.01350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.43350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 13.88700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.01350
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 GLY A 428
REMARK 465 ASP A 429
REMARK 465 ALA A 430
REMARK 465 GLY A 536
REMARK 465 GLN A 537
REMARK 465 ALA A 538
REMARK 465 GLY A 539
REMARK 465 GLN A 540
REMARK 465 HIS A 541
REMARK 465 HIS A 542
REMARK 465 HIS A 543
REMARK 465 HIS A 544
REMARK 465 HIS A 545
REMARK 465 HIS A 546
REMARK 465 GLY A 547
REMARK 465 ALA A 548
REMARK 465 TYR A 549
REMARK 465 PRO A 550
REMARK 465 TYR A 551
REMARK 465 ASP A 552
REMARK 465 VAL A 553
REMARK 465 PRO A 554
REMARK 465 ASP A 555
REMARK 465 TYR A 556
REMARK 465 ALA A 557
REMARK 465 SER A 558
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 ASP A 431 CG OD1 OD2
REMARK 470 ASP A 489 CG OD1 OD2
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 GLU A 467 -141.62 64.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 770 DISTANCE = 5.84 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UG7 RELATED DB: PDB
DBREF 5UG6 A 410 535 UNP P10820 PERF_MOUSE 410 535
SEQADV 5UG6 ALA A 427 UNP P10820 TRP 427 ENGINEERED MUTATION
SEQADV 5UG6 ALA A 430 UNP P10820 TYR 430 ENGINEERED MUTATION
SEQADV 5UG6 ASP A 431 UNP P10820 THR 431 ENGINEERED MUTATION
SEQADV 5UG6 ALA A 486 UNP P10820 TYR 486 ENGINEERED MUTATION
SEQADV 5UG6 ALA A 488 UNP P10820 TRP 488 ENGINEERED MUTATION
SEQADV 5UG6 GLY A 536 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 GLN A 537 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 ALA A 538 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 GLY A 539 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 GLN A 540 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 HIS A 541 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 HIS A 542 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 HIS A 543 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 HIS A 544 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 HIS A 545 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 HIS A 546 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 GLY A 547 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 ALA A 548 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 TYR A 549 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 PRO A 550 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 TYR A 551 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 ASP A 552 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 VAL A 553 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 PRO A 554 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 ASP A 555 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 TYR A 556 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 ALA A 557 UNP P10820 EXPRESSION TAG
SEQADV 5UG6 SER A 558 UNP P10820 EXPRESSION TAG
SEQRES 1 A 149 GLN ARG GLY LEU ALA HIS LEU VAL VAL SER ASN PHE ARG
SEQRES 2 A 149 ALA GLU HIS LEU ALA GLY ASP ALA ASP THR ALA THR ASP
SEQRES 3 A 149 ALA TYR LEU LYS VAL PHE PHE GLY GLY GLN GLU PHE ARG
SEQRES 4 A 149 THR GLY VAL VAL TRP ASN ASN ASN ASN PRO ARG TRP THR
SEQRES 5 A 149 ASP LYS MET ASP PHE GLU ASN VAL LEU LEU SER THR GLY
SEQRES 6 A 149 GLY PRO LEU ARG VAL GLN VAL TRP ASP ALA ASP ALA GLY
SEQRES 7 A 149 ALA ASP ASP ASP LEU LEU GLY SER CYS ASP ARG SER PRO
SEQRES 8 A 149 HIS SER GLY PHE HIS GLU VAL THR CYS GLU LEU ASN HIS
SEQRES 9 A 149 GLY ARG VAL LYS PHE SER TYR HIS ALA LYS CYS LEU PRO
SEQRES 10 A 149 HIS LEU THR GLY GLY THR CYS LEU GLU GLY GLN ALA GLY
SEQRES 11 A 149 GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR PRO TYR ASP
SEQRES 12 A 149 VAL PRO ASP TYR ALA SER
HET IOD A 601 1
HETNAM IOD IODIDE ION
FORMUL 2 IOD I 1-
FORMUL 3 HOH *70(H2 O)
HELIX 1 AA1 ASP A 485 ALA A 488 5 4
SHEET 1 AA1 4 MET A 464 LEU A 470 0
SHEET 2 AA1 4 LEU A 413 GLU A 424 -1 N VAL A 418 O MET A 464
SHEET 3 AA1 4 ARG A 515 CYS A 524 -1 O LYS A 517 N ARG A 422
SHEET 4 AA1 4 GLY A 503 GLU A 510 -1 N VAL A 507 O PHE A 518
SHEET 1 AA2 4 GLN A 445 ARG A 448 0
SHEET 2 AA2 4 ALA A 436 PHE A 442 -1 N VAL A 440 O PHE A 447
SHEET 3 AA2 4 LEU A 477 ASP A 483 -1 O TRP A 482 N TYR A 437
SHEET 4 AA2 4 ASP A 491 ARG A 498 -1 O GLY A 494 N VAL A 481
SSBOND 1 CYS A 496 CYS A 509 1555 1555 2.04
SSBOND 2 CYS A 524 CYS A 533 1555 1555 2.07
SITE 1 AC1 6 ASP A 465 ASP A 485 HOH A 701 HOH A 722
SITE 2 AC1 6 HOH A 728 HOH A 764
CRYST1 27.774 66.027 74.867 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.036005 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015145 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013357 0.00000
ATOM 1 N GLN A 410 19.689 -35.070 -8.617 1.00 35.85 N
ANISOU 1 N GLN A 410 3506 4683 5434 469 -94 -904 N
ATOM 2 CA GLN A 410 20.033 -34.525 -7.306 1.00 35.29 C
ANISOU 2 CA GLN A 410 3406 4537 5468 493 -296 -960 C
ATOM 3 C GLN A 410 18.815 -34.208 -6.448 1.00 35.22 C
ANISOU 3 C GLN A 410 3551 4609 5221 571 -412 -938 C
ATOM 4 O GLN A 410 17.700 -34.040 -6.961 1.00 34.37 O
ANISOU 4 O GLN A 410 3555 4564 4940 552 -321 -860 O
ATOM 5 CB GLN A 410 20.987 -33.308 -7.396 1.00 38.42 C
ANISOU 5 CB GLN A 410 3647 4778 6171 441 -315 -978 C
ATOM 6 CG GLN A 410 20.525 -32.141 -8.270 1.00 49.63 C
ANISOU 6 CG GLN A 410 5067 6180 7610 373 -173 -855 C
ATOM 7 CD GLN A 410 21.550 -31.022 -8.388 1.00 73.93 C
ANISOU 7 CD GLN A 410 7901 9046 11142 315 -197 -803 C
ATOM 8 OE1 GLN A 410 21.211 -29.841 -8.267 1.00 76.44 O
ANISOU 8 OE1 GLN A 410 8187 9258 11601 293 -303 -783 O
ATOM 9 NE2 GLN A 410 22.814 -31.346 -8.686 1.00 56.62 N
ANISOU 9 NE2 GLN A 410 5494 6762 9258 291 -102 -759 N
ATOM 10 N ARG A 411 19.052 -34.159 -5.122 1.00 29.23 N
ANISOU 10 N ARG A 411 2796 3864 4445 696 -620 -1012 N
ATOM 11 CA ARG A 411 18.102 -33.845 -4.062 1.00 27.58 C
ANISOU 11 CA ARG A 411 2714 3789 3977 863 -737 -998 C
ATOM 12 C ARG A 411 17.519 -32.451 -4.284 1.00 25.78 C
ANISOU 12 C ARG A 411 2539 3531 3726 847 -761 -1054 C
ATOM 13 O ARG A 411 18.233 -31.562 -4.750 1.00 25.30 O
ANISOU 13 O ARG A 411 2372 3305 3937 755 -799 -1136 O
ATOM 14 CB ARG A 411 18.876 -33.811 -2.721 1.00 31.81 C
ANISOU 14 CB ARG A 411 3227 4344 4516 1065 -995 -1138 C
ATOM 15 CG ARG A 411 18.657 -34.994 -1.785 1.00 43.65 C
ANISOU 15 CG ARG A 411 4764 6017 5803 1235 -1020 -1002 C
ATOM 16 CD ARG A 411 19.554 -34.876 -0.552 1.00 57.03 C
ANISOU 16 CD ARG A 411 6456 7739 7474 1476 -1303 -1172 C
ATOM 17 NE ARG A 411 19.285 -33.663 0.230 1.00 68.16 N
ANISOU 17 NE ARG A 411 7953 9215 8728 1713 -1523 -1375 N
ATOM 18 CZ ARG A 411 20.208 -32.955 0.878 1.00 85.44 C
ANISOU 18 CZ ARG A 411 10106 11291 11066 1884 -1861 -1676 C
ATOM 19 NH1 ARG A 411 21.482 -33.334 0.860 1.00 77.50 N
ANISOU 19 NH1 ARG A 411 8978 10097 10373 1824 -1990 -1777 N
ATOM 20 NH2 ARG A 411 19.866 -31.863 1.549 1.00 71.32 N
ANISOU 20 NH2 ARG A 411 8388 9555 9158 2135 -2109 -1906 N
ATOM 21 N GLY A 412 16.256 -32.259 -3.902 1.00 19.93 N
ANISOU 21 N GLY A 412 1925 2931 2717 946 -744 -985 N
ATOM 22 CA GLY A 412 15.601 -30.960 -3.926 1.00 18.83 C
ANISOU 22 CA GLY A 412 1838 2775 2542 964 -809 -1062 C
ATOM 23 C GLY A 412 14.920 -30.551 -5.209 1.00 19.33 C
ANISOU 23 C GLY A 412 1931 2765 2651 767 -630 -958 C
ATOM 24 O GLY A 412 14.322 -29.471 -5.270 1.00 17.18 O
ANISOU 24 O GLY A 412 1692 2461 2374 765 -689 -1006 O
ATOM 25 N LEU A 413 14.993 -31.415 -6.227 1.00 15.59 N
ANISOU 25 N LEU A 413 1444 2268 2210 635 -441 -839 N
ATOM 26 CA LEU A 413 14.412 -31.184 -7.539 1.00 14.99 C
ANISOU 26 CA LEU A 413 1418 2153 2126 508 -283 -752 C
ATOM 27 C LEU A 413 12.931 -31.520 -7.598 1.00 18.02 C
ANISOU 27 C LEU A 413 1925 2598 2323 540 -244 -667 C
ATOM 28 O LEU A 413 12.483 -32.550 -7.075 1.00 16.39 O
ANISOU 28 O LEU A 413 1720 2451 2057 619 -246 -592 O
ATOM 29 CB LEU A 413 15.166 -31.930 -8.672 1.00 14.78 C
ANISOU 29 CB LEU A 413 1329 2105 2180 438 -130 -713 C
ATOM 30 CG LEU A 413 16.569 -31.398 -9.075 1.00 20.17 C
ANISOU 30 CG LEU A 413 1849 2705 3111 379 -76 -715 C
ATOM 31 CD1 LEU A 413 17.218 -32.316 -10.158 1.00 19.80 C
ANISOU 31 CD1 LEU A 413 1752 2713 3059 386 107 -677 C
ATOM 32 CD2 LEU A 413 16.487 -29.969 -9.640 1.00 21.59 C
ANISOU 32 CD2 LEU A 413 1984 2803 3418 305 -35 -628 C
ATOM 33 N ALA A 414 12.191 -30.666 -8.306 1.00 13.15 N
ANISOU 33 N ALA A 414 1381 1939 1677 472 -206 -646 N
ATOM 34 CA ALA A 414 10.764 -30.862 -8.503 1.00 12.35 C
ANISOU 34 CA ALA A 414 1380 1843 1468 489 -184 -575 C
ATOM 35 C ALA A 414 10.346 -30.316 -9.858 1.00 16.04 C
ANISOU 35 C ALA A 414 1925 2241 1929 397 -118 -558 C
ATOM 36 O ALA A 414 10.851 -29.283 -10.294 1.00 18.03 O
ANISOU 36 O ALA A 414 2150 2458 2241 328 -98 -558 O
ATOM 37 CB ALA A 414 9.971 -30.169 -7.387 1.00 12.76 C
ANISOU 37 CB ALA A 414 1463 1959 1426 586 -268 -584 C
ATOM 38 N HIS A 415 9.385 -30.981 -10.500 1.00 12.17 N
ANISOU 38 N HIS A 415 1510 1712 1402 419 -110 -526 N
ATOM 39 CA HIS A 415 8.834 -30.527 -11.762 1.00 11.54 C
ANISOU 39 CA HIS A 415 1537 1583 1263 392 -85 -527 C
ATOM 40 C HIS A 415 7.750 -29.519 -11.352 1.00 17.23 C
ANISOU 40 C HIS A 415 2314 2251 1982 348 -143 -503 C
ATOM 41 O HIS A 415 6.833 -29.873 -10.594 1.00 16.10 O
ANISOU 41 O HIS A 415 2163 2085 1868 395 -191 -472 O
ATOM 42 CB HIS A 415 8.318 -31.723 -12.592 1.00 11.72 C
ANISOU 42 CB HIS A 415 1606 1555 1292 486 -135 -577 C
ATOM 43 CG HIS A 415 7.598 -31.357 -13.860 1.00 15.08 C
ANISOU 43 CG HIS A 415 2175 1940 1616 531 -165 -615 C
ATOM 44 ND1 HIS A 415 6.844 -32.284 -14.540 1.00 16.51 N
ANISOU 44 ND1 HIS A 415 2406 2019 1850 657 -310 -720 N
ATOM 45 CD2 HIS A 415 7.598 -30.197 -14.562 1.00 16.35 C
ANISOU 45 CD2 HIS A 415 2421 2140 1653 492 -94 -560 C
ATOM 46 CE1 HIS A 415 6.424 -31.676 -15.631 1.00 16.53 C
ANISOU 46 CE1 HIS A 415 2559 2032 1692 718 -327 -755 C
ATOM 47 NE2 HIS A 415 6.814 -30.402 -15.657 1.00 16.77 N
ANISOU 47 NE2 HIS A 415 2613 2153 1606 609 -179 -629 N
ATOM 48 N LEU A 416 7.939 -28.233 -11.738 1.00 13.37 N
ANISOU 48 N LEU A 416 1838 1743 1501 270 -133 -489 N
ATOM 49 CA LEU A 416 7.061 -27.134 -11.335 1.00 12.15 C
ANISOU 49 CA LEU A 416 1709 1525 1380 228 -220 -503 C
ATOM 50 C LEU A 416 6.242 -26.590 -12.510 1.00 15.98 C
ANISOU 50 C LEU A 416 2310 1928 1834 177 -221 -455 C
ATOM 51 O LEU A 416 6.798 -26.151 -13.519 1.00 14.21 O
ANISOU 51 O LEU A 416 2094 1716 1591 147 -146 -371 O
ATOM 52 CB LEU A 416 7.882 -25.989 -10.670 1.00 12.75 C
ANISOU 52 CB LEU A 416 1661 1588 1596 191 -297 -549 C
ATOM 53 CG LEU A 416 7.117 -24.690 -10.248 1.00 14.80 C
ANISOU 53 CG LEU A 416 1912 1768 1944 170 -448 -620 C
ATOM 54 CD1 LEU A 416 6.088 -24.976 -9.199 1.00 10.88 C
ANISOU 54 CD1 LEU A 416 1466 1349 1317 297 -502 -699 C
ATOM 55 CD2 LEU A 416 8.078 -23.616 -9.722 1.00 16.69 C
ANISOU 55 CD2 LEU A 416 1978 1930 2435 160 -602 -706 C
ATOM 56 N VAL A 417 4.911 -26.620 -12.365 1.00 11.52 N
ANISOU 56 N VAL A 417 1820 1286 1272 191 -297 -480 N
ATOM 57 CA VAL A 417 3.999 -26.121 -13.394 1.00 10.26 C
ANISOU 57 CA VAL A 417 1781 1020 1097 158 -346 -462 C
ATOM 58 C VAL A 417 3.097 -25.131 -12.701 1.00 14.78 C
ANISOU 58 C VAL A 417 2335 1515 1765 103 -440 -495 C
ATOM 59 O VAL A 417 2.425 -25.480 -11.724 1.00 14.65 O
ANISOU 59 O VAL A 417 2279 1508 1782 164 -460 -523 O
ATOM 60 CB VAL A 417 3.199 -27.270 -14.070 1.00 13.76 C
ANISOU 60 CB VAL A 417 2319 1383 1526 256 -402 -503 C
ATOM 61 CG1 VAL A 417 2.204 -26.730 -15.117 1.00 13.85 C
ANISOU 61 CG1 VAL A 417 2475 1270 1518 259 -505 -521 C
ATOM 62 CG2 VAL A 417 4.146 -28.263 -14.729 1.00 14.04 C
ANISOU 62 CG2 VAL A 417 2361 1513 1461 359 -348 -532 C
ATOM 63 N VAL A 418 3.034 -23.910 -13.236 1.00 11.23 N
ANISOU 63 N VAL A 418 1898 997 1373 11 -490 -466 N
ATOM 64 CA VAL A 418 2.176 -22.857 -12.679 1.00 10.73 C
ANISOU 64 CA VAL A 418 1806 840 1431 -36 -619 -533 C
ATOM 65 C VAL A 418 1.063 -22.655 -13.703 1.00 16.93 C
ANISOU 65 C VAL A 418 2728 1485 2220 -76 -676 -500 C
ATOM 66 O VAL A 418 1.336 -22.520 -14.892 1.00 16.98 O
ANISOU 66 O VAL A 418 2816 1481 2156 -93 -646 -401 O
ATOM 67 CB VAL A 418 3.018 -21.580 -12.400 1.00 15.16 C
ANISOU 67 CB VAL A 418 2219 1372 2171 -107 -704 -545 C
ATOM 68 CG1 VAL A 418 2.223 -20.524 -11.626 1.00 15.35 C
ANISOU 68 CG1 VAL A 418 2183 1310 2338 -106 -894 -694 C
ATOM 69 CG2 VAL A 418 4.302 -21.933 -11.643 1.00 14.60 C
ANISOU 69 CG2 VAL A 418 2023 1408 2117 -47 -672 -584 C
ATOM 70 N SER A 419 -0.197 -22.632 -13.246 1.00 13.93 N
ANISOU 70 N SER A 419 2369 1010 1915 -58 -756 -570 N
ATOM 71 CA SER A 419 -1.290 -22.505 -14.175 1.00 14.53 C
ANISOU 71 CA SER A 419 2568 912 2039 -86 -849 -566 C
ATOM 72 C SER A 419 -2.513 -21.885 -13.535 1.00 16.32 C
ANISOU 72 C SER A 419 2754 1019 2427 -109 -948 -638 C
ATOM 73 O SER A 419 -2.441 -21.389 -12.415 1.00 14.91 O
ANISOU 73 O SER A 419 2459 930 2277 -80 -946 -703 O
ATOM 74 CB SER A 419 -1.631 -23.886 -14.738 1.00 20.45 C
ANISOU 74 CB SER A 419 3399 1613 2759 21 -847 -569 C
ATOM 75 OG SER A 419 -2.083 -24.733 -13.693 1.00 24.87 O
ANISOU 75 OG SER A 419 3842 2167 3441 88 -803 -562 O
ATOM 76 N ASN A 420 -3.659 -21.925 -14.255 1.00 13.70 N
ANISOU 76 N ASN A 420 1607 795 2803 -216 -328 -306 N
ATOM 77 CA ASN A 420 -4.955 -21.446 -13.787 1.00 12.44 C
ANISOU 77 CA ASN A 420 1429 710 2588 -289 -300 -209 C
ATOM 78 C ASN A 420 -4.923 -19.960 -13.370 1.00 16.88 C
ANISOU 78 C ASN A 420 2041 1397 2977 -254 -186 -99 C
ATOM 79 O ASN A 420 -5.543 -19.564 -12.365 1.00 17.75 O
ANISOU 79 O ASN A 420 2156 1526 3061 -315 -144 23 O
ATOM 80 CB ASN A 420 -5.461 -22.344 -12.637 1.00 17.02 C
ANISOU 80 CB ASN A 420 1987 1162 3317 -428 -363 -94 C
ATOM 81 CG ASN A 420 -6.963 -22.253 -12.409 1.00 51.36 C
ANISOU 81 CG ASN A 420 6273 5610 7633 -512 -366 -37 C
ATOM 82 OD1 ASN A 420 -7.721 -21.611 -13.174 1.00 45.65 O
ANISOU 82 OD1 ASN A 420 5514 5036 6795 -457 -330 -95 O
ATOM 83 ND2 ASN A 420 -7.423 -22.879 -11.334 1.00 40.96 N
ANISOU 83 ND2 ASN A 420 4924 4233 6406 -652 -411 95 N
ATOM 84 N PHE A 421 -4.224 -19.132 -14.156 1.00 12.26 N
ANISOU 84 N PHE A 421 1489 901 2267 -160 -143 -146 N
ATOM 85 CA PHE A 421 -4.123 -17.680 -13.878 1.00 11.08 C
ANISOU 85 CA PHE A 421 1410 837 1964 -127 -56 -49 C
ATOM 86 C PHE A 421 -5.417 -16.962 -14.200 1.00 16.09 C
ANISOU 86 C PHE A 421 2015 1578 2520 -93 -29 -40 C
ATOM 87 O PHE A 421 -6.029 -17.165 -15.266 1.00 15.17 O
ANISOU 87 O PHE A 421 1829 1548 2388 -59 -67 -128 O
ATOM 88 CB PHE A 421 -3.035 -17.023 -14.717 1.00 12.36 C
ANISOU 88 CB PHE A 421 1608 1075 2014 -59 -39 -81 C
ATOM 89 CG PHE A 421 -1.656 -17.613 -14.518 1.00 15.03 C
ANISOU 89 CG PHE A 421 1954 1351 2405 -67 -58 -90 C
ATOM 90 CD1 PHE A 421 -0.845 -17.184 -13.473 1.00 16.03 C
ANISOU 90 CD1 PHE A 421 2153 1428 2511 -118 -22 40 C
ATOM 91 CD2 PHE A 421 -1.143 -18.527 -15.422 1.00 19.50 C
ANISOU 91 CD2 PHE A 421 2452 1928 3028 -14 -111 -234 C
ATOM 92 CE1 PHE A 421 0.437 -17.683 -13.324 1.00 16.95 C
ANISOU 92 CE1 PHE A 421 2258 1514 2669 -118 -42 49 C
ATOM 93 CE2 PHE A 421 0.153 -19.009 -15.279 1.00 22.20 C
ANISOU 93 CE2 PHE A 421 2785 2234 3416 9 -124 -244 C
ATOM 94 CZ PHE A 421 0.914 -18.608 -14.213 1.00 18.23 C
ANISOU 94 CZ PHE A 421 2340 1686 2901 -44 -91 -91 C
ATOM 95 N ARG A 422 -5.783 -16.059 -13.294 1.00 13.19 N
ANISOU 95 N ARG A 422 1701 1218 2093 -94 38 63 N
ATOM 96 CA ARG A 422 -6.940 -15.194 -13.409 1.00 13.64 C
ANISOU 96 CA ARG A 422 1737 1370 2076 -32 77 88 C
ATOM 97 C ARG A 422 -6.791 -14.039 -12.409 1.00 17.77 C
ANISOU 97 C ARG A 422 2366 1863 2522 -9 157 174 C
ATOM 98 O ARG A 422 -6.058 -14.147 -11.419 1.00 18.86 O
ANISOU 98 O ARG A 422 2569 1925 2674 -82 180 223 O
ATOM 99 CB ARG A 422 -8.288 -15.952 -13.256 1.00 10.33 C
ANISOU 99 CB ARG A 422 1196 1008 1722 -73 51 78 C
ATOM 100 CG ARG A 422 -8.679 -16.338 -11.826 1.00 12.38 C
ANISOU 100 CG ARG A 422 1436 1237 2030 -165 78 159 C
ATOM 101 CD ARG A 422 -8.207 -17.720 -11.503 1.00 13.32 C
ANISOU 101 CD ARG A 422 1529 1247 2284 -289 0 158 C
ATOM 102 NE ARG A 422 -8.776 -18.235 -10.256 1.00 16.13 N
ANISOU 102 NE ARG A 422 1832 1610 2685 -409 1 257 N
ATOM 103 CZ ARG A 422 -8.210 -19.186 -9.533 1.00 29.04 C
ANISOU 103 CZ ARG A 422 3471 3133 4429 -530 -55 315 C
ATOM 104 NH1 ARG A 422 -7.061 -19.738 -9.930 1.00 16.98 N
ANISOU 104 NH1 ARG A 422 1996 1465 2989 -523 -110 270 N
ATOM 105 NH2 ARG A 422 -8.769 -19.584 -8.398 1.00 19.75 N
ANISOU 105 NH2 ARG A 422 2235 1997 3273 -656 -58 428 N
ATOM 106 N ALA A 423 -7.456 -12.936 -12.693 1.00 12.16 N
ANISOU 106 N ALA A 423 1677 1210 1733 92 192 188 N
ATOM 107 CA ALA A 423 -7.421 -11.764 -11.841 1.00 11.22 C
ANISOU 107 CA ALA A 423 1672 1047 1546 135 261 239 C
ATOM 108 C ALA A 423 -8.806 -11.209 -11.776 1.00 16.26 C
ANISOU 108 C ALA A 423 2247 1767 2165 242 299 236 C
ATOM 109 O ALA A 423 -9.647 -11.572 -12.590 1.00 14.86 O
ANISOU 109 O ALA A 423 1946 1690 2009 280 262 215 O
ATOM 110 CB ALA A 423 -6.469 -10.735 -12.402 1.00 11.40 C
ANISOU 110 CB ALA A 423 1823 1016 1491 172 248 265 C
ATOM 111 N GLU A 424 -9.079 -10.398 -10.759 1.00 14.72 N
ANISOU 111 N GLU A 424 2121 1544 1926 288 372 250 N
ATOM 112 CA GLU A 424 -10.398 -9.818 -10.598 1.00 16.33 C
ANISOU 112 CA GLU A 424 2256 1839 2111 420 420 237 C
ATOM 113 C GLU A 424 -10.291 -8.421 -10.040 1.00 18.95 C
ANISOU 113 C GLU A 424 2740 2078 2383 530 477 227 C
ATOM 114 O GLU A 424 -9.307 -8.110 -9.354 1.00 16.28 O
ANISOU 114 O GLU A 424 2548 1627 2010 456 496 230 O
ATOM 115 CB GLU A 424 -11.331 -10.710 -9.757 1.00 18.48 C
ANISOU 115 CB GLU A 424 2375 2242 2404 357 455 237 C
ATOM 116 CG GLU A 424 -10.854 -11.006 -8.352 1.00 32.96 C
ANISOU 116 CG GLU A 424 4257 4050 4218 236 506 252 C
ATOM 117 CD GLU A 424 -11.646 -12.029 -7.552 1.00 50.99 C
ANISOU 117 CD GLU A 424 6377 6478 6518 125 517 285 C
ATOM 118 OE1 GLU A 424 -12.016 -11.706 -6.403 1.00 35.35 O
ANISOU 118 OE1 GLU A 424 4383 4581 4467 123 599 283 O
ATOM 119 OE2 GLU A 424 -11.812 -13.177 -8.022 1.00 50.27 O
ANISOU 119 OE2 GLU A 424 6178 6414 6506 23 440 313 O
ATOM 120 N HIS A 425 -11.264 -7.572 -10.403 1.00 18.07 N
ANISOU 120 N HIS A 425 2598 2005 2264 709 492 217 N
ATOM 121 CA HIS A 425 -11.410 -6.179 -9.934 1.00 21.49 C
ANISOU 121 CA HIS A 425 3170 2331 2664 860 539 186 C
ATOM 122 C HIS A 425 -10.127 -5.377 -10.050 1.00 24.51 C
ANISOU 122 C HIS A 425 3779 2514 3020 812 497 211 C
ATOM 123 O HIS A 425 -9.761 -4.640 -9.128 1.00 26.39 O
ANISOU 123 O HIS A 425 4173 2635 3219 821 543 169 O
ATOM 124 CB HIS A 425 -11.896 -6.178 -8.469 1.00 24.81 C
ANISOU 124 CB HIS A 425 3572 2813 3042 870 646 117 C
ATOM 125 CG HIS A 425 -13.127 -6.989 -8.219 1.00 30.77 C
ANISOU 125 CG HIS A 425 4093 3798 3802 885 686 112 C
ATOM 126 ND1 HIS A 425 -13.402 -7.497 -6.964 1.00 34.53 N
ANISOU 126 ND1 HIS A 425 4497 4394 4227 799 762 85 N
ATOM 127 CD2 HIS A 425 -14.146 -7.303 -9.050 1.00 35.11 C
ANISOU 127 CD2 HIS A 425 4463 4493 4386 965 656 143 C
ATOM 128 CE1 HIS A 425 -14.567 -8.113 -7.070 1.00 35.65 C
ANISOU 128 CE1 HIS A 425 4418 4750 4376 824 773 106 C
ATOM 129 NE2 HIS A 425 -15.058 -8.019 -8.306 1.00 36.20 N
ANISOU 129 NE2 HIS A 425 4416 4840 4497 924 711 138 N
ATOM 130 N LEU A 426 -9.442 -5.513 -11.186 1.00 18.24 N
ANISOU 130 N LEU A 426 2997 1699 2235 751 409 277 N
ATOM 131 CA LEU A 426 -8.173 -4.851 -11.415 1.00 17.29 C
ANISOU 131 CA LEU A 426 3062 1433 2076 675 355 327 C
ATOM 132 C LEU A 426 -8.258 -3.338 -11.498 1.00 19.92 C
ANISOU 132 C LEU A 426 3563 1605 2402 801 329 348 C
ATOM 133 O LEU A 426 -7.241 -2.677 -11.339 1.00 19.73 O
ANISOU 133 O LEU A 426 3722 1438 2336 719 292 385 O
ATOM 134 CB LEU A 426 -7.475 -5.416 -12.650 1.00 16.05 C
ANISOU 134 CB LEU A 426 2842 1346 1910 583 271 388 C
ATOM 135 CG LEU A 426 -6.885 -6.832 -12.486 1.00 17.38 C
ANISOU 135 CG LEU A 426 2912 1598 2093 435 278 361 C
ATOM 136 CD1 LEU A 426 -6.047 -7.193 -13.679 1.00 15.92 C
ANISOU 136 CD1 LEU A 426 2690 1476 1882 367 202 395 C
ATOM 137 CD2 LEU A 426 -5.995 -6.928 -11.238 1.00 15.27 C
ANISOU 137 CD2 LEU A 426 2756 1244 1801 316 323 358 C
ATOM 138 N ALA A 427 -9.450 -2.789 -11.706 1.00 18.39 N
ANISOU 138 N ALA A 427 3308 1427 2251 997 341 330 N
ATOM 139 CA ALA A 427 -9.610 -1.335 -11.817 1.00 46.81 C
ANISOU 139 CA ALA A 427 7071 4841 5875 1145 300 350 C
ATOM 140 C ALA A 427 -10.188 -0.712 -10.555 1.00 75.73 C
ANISOU 140 C ALA A 427 10821 8411 9544 1277 394 225 C
ATOM 141 O ALA A 427 -11.212 -1.172 -10.066 1.00 45.70 O
ANISOU 141 O ALA A 427 6859 4756 5749 1376 481 148 O
ATOM 142 CB ALA A 427 -10.473 -0.993 -13.014 1.00 48.64 C
ANISOU 142 CB ALA A 427 7187 5136 6159 1297 232 428 C
ATOM 143 N ASP A 431 -15.841 1.176 -15.763 1.00 47.77 N
ANISOU 143 N ASP A 431 6510 5305 6336 2269 96 671 N
ATOM 144 CA ASP A 431 -15.603 2.035 -16.918 1.00 48.06 C
ANISOU 144 CA ASP A 431 6605 5245 6411 2291 -57 850 C
ATOM 145 C ASP A 431 -14.117 2.166 -17.276 1.00 47.86 C
ANISOU 145 C ASP A 431 6776 5080 6329 2054 -142 919 C
ATOM 146 O ASP A 431 -13.806 2.604 -18.381 1.00 48.61 O
ANISOU 146 O ASP A 431 6881 5170 6416 1999 -275 1088 O
ATOM 147 CB ASP A 431 -16.241 3.416 -16.712 1.00 53.41 C
ANISOU 147 CB ASP A 431 7376 5704 7212 2583 -97 880 C
ATOM 148 N THR A 432 -13.203 1.784 -16.359 1.00 39.72 N
ANISOU 148 N THR A 432 5883 3963 5246 1904 -70 802 N
ATOM 149 CA THR A 432 -11.757 1.842 -16.598 1.00 36.70 C
ANISOU 149 CA THR A 432 5666 3482 4795 1673 -139 864 C
ATOM 150 C THR A 432 -11.336 0.632 -17.446 1.00 36.42 C
ANISOU 150 C THR A 432 5458 3711 4667 1473 -154 900 C
ATOM 151 O THR A 432 -11.622 -0.494 -17.070 1.00 34.45 O
ANISOU 151 O THR A 432 5068 3626 4396 1426 -62 793 O
ATOM 152 CB THR A 432 -10.991 1.949 -15.262 1.00 40.84 C
ANISOU 152 CB THR A 432 6394 3825 5299 1601 -59 733 C
ATOM 153 OG1 THR A 432 -11.269 3.208 -14.649 1.00 43.50 O
ANISOU 153 OG1 THR A 432 6919 3892 5716 1781 -72 696 O
ATOM 154 CG2 THR A 432 -9.490 1.789 -15.421 1.00 37.24 C
ANISOU 154 CG2 THR A 432 6069 3326 4757 1343 -113 792 C
ATOM 155 N ALA A 433 -10.643 0.879 -18.571 1.00 31.73 N
ANISOU 155 N ALA A 433 4879 3157 4018 1352 -275 1048 N
ATOM 156 CA ALA A 433 -10.140 -0.153 -19.479 1.00 29.00 C
ANISOU 156 CA ALA A 433 4384 3064 3573 1171 -298 1068 C
ATOM 157 C ALA A 433 -8.844 -0.812 -18.927 1.00 30.48 C
ANISOU 157 C ALA A 433 4659 3232 3691 977 -249 987 C
ATOM 158 O ALA A 433 -7.859 -0.123 -18.718 1.00 31.58 O
ANISOU 158 O ALA A 433 4983 3216 3801 892 -293 1048 O
ATOM 159 CB ALA A 433 -9.899 0.458 -20.858 1.00 29.99 C
ANISOU 159 CB ALA A 433 4484 3269 3644 1118 -444 1260 C
ATOM 160 N THR A 434 -8.856 -2.124 -18.638 1.00 23.93 N
ANISOU 160 N THR A 434 3701 2547 2844 909 -166 860 N
ATOM 161 CA THR A 434 -7.666 -2.831 -18.133 1.00 20.11 C
ANISOU 161 CA THR A 434 3276 2054 2310 743 -125 794 C
ATOM 162 C THR A 434 -7.148 -3.791 -19.189 1.00 22.17 C
ANISOU 162 C THR A 434 3391 2540 2494 620 -162 785 C
ATOM 163 O THR A 434 -7.930 -4.570 -19.718 1.00 23.29 O
ANISOU 163 O THR A 434 3358 2844 2646 650 -155 730 O
ATOM 164 CB THR A 434 -7.925 -3.493 -16.776 1.00 23.75 C
ANISOU 164 CB THR A 434 3742 2455 2826 758 -10 659 C
ATOM 165 OG1 THR A 434 -8.254 -2.473 -15.845 1.00 25.24 O
ANISOU 165 OG1 THR A 434 4083 2448 3060 867 23 653 O
ATOM 166 CG2 THR A 434 -6.696 -4.282 -16.231 1.00 16.32 C
ANISOU 166 CG2 THR A 434 2844 1509 1847 589 24 609 C
ATOM 167 N ASP A 435 -5.841 -3.721 -19.490 1.00 17.37 N
ANISOU 167 N ASP A 435 2850 1952 1798 481 -202 833 N
ATOM 168 CA ASP A 435 -5.116 -4.515 -20.494 1.00 16.87 C
ANISOU 168 CA ASP A 435 2661 2112 1638 367 -235 813 C
ATOM 169 C ASP A 435 -3.999 -5.262 -19.790 1.00 20.49 C
ANISOU 169 C ASP A 435 3157 2544 2084 264 -180 733 C
ATOM 170 O ASP A 435 -2.817 -4.988 -20.011 1.00 18.71 O
ANISOU 170 O ASP A 435 2986 2357 1766 157 -215 801 O
ATOM 171 CB ASP A 435 -4.553 -3.585 -21.589 1.00 19.10 C
ANISOU 171 CB ASP A 435 2964 2489 1804 300 -345 979 C
ATOM 172 CG ASP A 435 -5.627 -2.712 -22.215 1.00 23.65 C
ANISOU 172 CG ASP A 435 3517 3062 2408 405 -416 1096 C
ATOM 173 OD1 ASP A 435 -6.778 -3.168 -22.304 1.00 23.12 O
ANISOU 173 OD1 ASP A 435 3327 3053 2404 511 -385 1027 O
ATOM 174 OD2 ASP A 435 -5.305 -1.581 -22.632 1.00 29.39 O
ANISOU 174 OD2 ASP A 435 4340 3733 3093 374 -514 1270 O
ATOM 175 N ALA A 436 -4.375 -6.238 -18.963 1.00 16.33 N
ANISOU 175 N ALA A 436 2586 1970 1648 290 -102 605 N
ATOM 176 CA ALA A 436 -3.413 -6.935 -18.128 1.00 15.26 C
ANISOU 176 CA ALA A 436 2489 1780 1528 205 -54 548 C
ATOM 177 C ALA A 436 -2.707 -8.116 -18.737 1.00 17.92 C
ANISOU 177 C ALA A 436 2699 2271 1839 144 -60 459 C
ATOM 178 O ALA A 436 -3.247 -8.828 -19.571 1.00 16.10 O
ANISOU 178 O ALA A 436 2329 2175 1615 174 -78 374 O
ATOM 179 CB ALA A 436 -4.077 -7.373 -16.832 1.00 15.33 C
ANISOU 179 CB ALA A 436 2519 1659 1647 243 23 478 C
ATOM 180 N TYR A 437 -1.475 -8.350 -18.238 1.00 14.66 N
ANISOU 180 N TYR A 437 2336 1834 1400 61 -45 469 N
ATOM 181 CA TYR A 437 -0.672 -9.516 -18.536 1.00 13.48 C
ANISOU 181 CA TYR A 437 2078 1792 1252 26 -41 372 C
ATOM 182 C TYR A 437 0.215 -9.783 -17.338 1.00 16.93 C
ANISOU 182 C TYR A 437 2591 2110 1732 -37 -3 396 C
ATOM 183 O TYR A 437 0.428 -8.895 -16.507 1.00 14.38 O
ANISOU 183 O TYR A 437 2409 1668 1386 -82 10 498 O
ATOM 184 CB TYR A 437 0.133 -9.376 -19.847 1.00 13.33 C
ANISOU 184 CB TYR A 437 1976 2002 1087 -7 -90 386 C
ATOM 185 CG TYR A 437 1.258 -8.378 -19.764 1.00 16.24 C
ANISOU 185 CG TYR A 437 2441 2398 1333 -100 -117 540 C
ATOM 186 CD1 TYR A 437 1.037 -7.022 -20.017 1.00 17.26 C
ANISOU 186 CD1 TYR A 437 2672 2498 1387 -129 -170 694 C
ATOM 187 CD2 TYR A 437 2.557 -8.784 -19.464 1.00 16.85 C
ANISOU 187 CD2 TYR A 437 2501 2532 1369 -165 -103 545 C
ATOM 188 CE1 TYR A 437 2.087 -6.113 -20.031 1.00 17.17 C
ANISOU 188 CE1 TYR A 437 2750 2517 1256 -244 -217 849 C
ATOM 189 CE2 TYR A 437 3.602 -7.866 -19.404 1.00 17.76 C
ANISOU 189 CE2 TYR A 437 2694 2697 1355 -276 -137 703 C
ATOM 190 CZ TYR A 437 3.362 -6.534 -19.692 1.00 25.31 C
ANISOU 190 CZ TYR A 437 3762 3623 2234 -326 -197 855 C
ATOM 191 OH TYR A 437 4.394 -5.632 -19.675 1.00 30.67 O
ANISOU 191 OH TYR A 437 4523 4348 2782 -462 -250 1023 O
ATOM 192 N LEU A 438 0.692 -11.025 -17.228 1.00 13.57 N
ANISOU 192 N LEU A 438 2073 1709 1376 -39 9 298 N
ATOM 193 CA LEU A 438 1.538 -11.421 -16.119 1.00 13.15 C
ANISOU 193 CA LEU A 438 2064 1560 1373 -99 36 334 C
ATOM 194 C LEU A 438 2.922 -11.694 -16.560 1.00 17.83 C
ANISOU 194 C LEU A 438 2597 2287 1892 -130 19 342 C
ATOM 195 O LEU A 438 3.128 -12.144 -17.684 1.00 18.59 O
ANISOU 195 O LEU A 438 2575 2545 1944 -82 -3 249 O
ATOM 196 CB LEU A 438 0.978 -12.707 -15.448 1.00 12.76 C
ANISOU 196 CB LEU A 438 1952 1401 1495 -75 51 240 C
ATOM 197 CG LEU A 438 -0.463 -12.648 -15.011 1.00 17.03 C
ANISOU 197 CG LEU A 438 2510 1852 2108 -48 71 225 C
ATOM 198 CD1 LEU A 438 -0.906 -13.973 -14.476 1.00 17.31 C
ANISOU 198 CD1 LEU A 438 2468 1809 2298 -56 64 153 C
ATOM 199 CD2 LEU A 438 -0.715 -11.497 -14.022 1.00 17.21 C
ANISOU 199 CD2 LEU A 438 2674 1781 2084 -80 111 333 C
ATOM 200 N LYS A 439 3.865 -11.471 -15.651 1.00 14.45 N
ANISOU 200 N LYS A 439 2237 1810 1442 -212 32 446 N
ATOM 201 CA LYS A 439 5.274 -11.856 -15.752 1.00 13.73 C
ANISOU 201 CA LYS A 439 2076 1843 1299 -245 23 473 C
ATOM 202 C LYS A 439 5.501 -12.785 -14.553 1.00 15.65 C
ANISOU 202 C LYS A 439 2312 1944 1689 -259 42 473 C
ATOM 203 O LYS A 439 5.163 -12.430 -13.430 1.00 14.95 O
ANISOU 203 O LYS A 439 2332 1713 1634 -328 63 552 O
ATOM 204 CB LYS A 439 6.208 -10.646 -15.674 1.00 17.49 C
ANISOU 204 CB LYS A 439 2641 2401 1603 -363 5 642 C
ATOM 205 CG LYS A 439 6.363 -9.917 -16.987 1.00 28.89 C
ANISOU 205 CG LYS A 439 4047 4042 2887 -370 -35 670 C
ATOM 206 CD LYS A 439 7.358 -8.791 -16.847 1.00 34.50 C
ANISOU 206 CD LYS A 439 4848 4827 3436 -517 -71 859 C
ATOM 207 CE LYS A 439 7.214 -7.792 -17.979 1.00 40.35 C
ANISOU 207 CE LYS A 439 5600 5703 4029 -555 -131 938 C
ATOM 208 NZ LYS A 439 8.135 -6.630 -17.807 1.00 40.48 N
ANISOU 208 NZ LYS A 439 5726 5761 3893 -728 -187 1144 N
ATOM 209 N VAL A 440 5.935 -14.017 -14.805 1.00 12.83 N
ANISOU 209 N VAL A 440 1824 1619 1432 -185 31 373 N
ATOM 210 CA VAL A 440 6.135 -15.016 -13.748 1.00 11.82 C
ANISOU 210 CA VAL A 440 1674 1347 1469 -194 28 387 C
ATOM 211 C VAL A 440 7.590 -15.466 -13.767 1.00 14.28 C
ANISOU 211 C VAL A 440 1892 1769 1763 -181 16 423 C
ATOM 212 O VAL A 440 8.123 -15.799 -14.825 1.00 17.13 O
ANISOU 212 O VAL A 440 2139 2290 2079 -88 7 320 O
ATOM 213 CB VAL A 440 5.123 -16.174 -13.931 1.00 16.39 C
ANISOU 213 CB VAL A 440 2192 1804 2233 -110 5 235 C
ATOM 214 CG1 VAL A 440 5.354 -17.303 -12.928 1.00 15.54 C
ANISOU 214 CG1 VAL A 440 2052 1539 2313 -126 -23 266 C
ATOM 215 CG2 VAL A 440 3.673 -15.648 -13.813 1.00 15.97 C
ANISOU 215 CG2 VAL A 440 2213 1677 2177 -131 21 226 C
ATOM 216 N PHE A 441 8.220 -15.478 -12.616 1.00 10.30 N
ANISOU 216 N PHE A 441 1423 1205 1284 -271 17 567 N
ATOM 217 CA PHE A 441 9.640 -15.821 -12.501 1.00 11.21 C
ANISOU 217 CA PHE A 441 1442 1441 1376 -268 5 639 C
ATOM 218 C PHE A 441 9.894 -16.909 -11.523 1.00 16.60 C
ANISOU 218 C PHE A 441 2075 1981 2250 -259 -22 683 C
ATOM 219 O PHE A 441 9.332 -16.898 -10.426 1.00 16.84 O
ANISOU 219 O PHE A 441 2191 1858 2348 -359 -23 771 O
ATOM 220 CB PHE A 441 10.468 -14.587 -12.079 1.00 13.11 C
ANISOU 220 CB PHE A 441 1762 1804 1414 -425 16 830 C
ATOM 221 CG PHE A 441 10.310 -13.325 -12.905 1.00 15.68 C
ANISOU 221 CG PHE A 441 2163 2251 1543 -475 21 846 C
ATOM 222 CD1 PHE A 441 9.219 -12.476 -12.712 1.00 19.41 C
ANISOU 222 CD1 PHE A 441 2791 2592 1993 -525 32 849 C
ATOM 223 CD2 PHE A 441 11.308 -12.925 -13.794 1.00 19.54 C
ANISOU 223 CD2 PHE A 441 2565 2995 1863 -483 9 883 C
ATOM 224 CE1 PHE A 441 9.098 -11.285 -13.443 1.00 20.70 C
ANISOU 224 CE1 PHE A 441 3031 2840 1994 -572 18 889 C
ATOM 225 CE2 PHE A 441 11.184 -11.734 -14.523 1.00 23.30 C
ANISOU 225 CE2 PHE A 441 3114 3580 2159 -556 -6 935 C
ATOM 226 CZ PHE A 441 10.071 -10.932 -14.359 1.00 21.04 C
ANISOU 226 CZ PHE A 441 2991 3124 1878 -597 -7 939 C
ATOM 227 N PHE A 442 10.857 -17.778 -11.856 1.00 14.36 N
ANISOU 227 N PHE A 442 1647 1772 2038 -149 -47 644 N
ATOM 228 CA PHE A 442 11.358 -18.814 -10.964 1.00 14.47 C
ANISOU 228 CA PHE A 442 1594 1665 2239 -131 -89 719 C
ATOM 229 C PHE A 442 12.692 -19.334 -11.452 1.00 17.99 C
ANISOU 229 C PHE A 442 1876 2275 2685 -5 -102 703 C
ATOM 230 O PHE A 442 12.814 -19.710 -12.615 1.00 18.94 O
ANISOU 230 O PHE A 442 1901 2494 2801 156 -96 512 O
ATOM 231 CB PHE A 442 10.353 -19.971 -10.716 1.00 16.58 C
ANISOU 231 CB PHE A 442 1863 1674 2762 -68 -139 617 C
ATOM 232 CG PHE A 442 10.749 -20.810 -9.527 1.00 18.76 C
ANISOU 232 CG PHE A 442 2104 1806 3218 -113 -196 770 C
ATOM 233 CD1 PHE A 442 11.644 -21.863 -9.665 1.00 22.32 C
ANISOU 233 CD1 PHE A 442 2421 2231 3829 29 -250 746 C
ATOM 234 CD2 PHE A 442 10.311 -20.482 -8.245 1.00 20.20 C
ANISOU 234 CD2 PHE A 442 2378 1903 3394 -299 -197 949 C
ATOM 235 CE1 PHE A 442 12.082 -22.575 -8.548 1.00 24.22 C
ANISOU 235 CE1 PHE A 442 2622 2347 4234 -21 -316 925 C
ATOM 236 CE2 PHE A 442 10.750 -21.193 -7.136 1.00 22.51 C
ANISOU 236 CE2 PHE A 442 2626 2102 3826 -366 -256 1123 C
ATOM 237 CZ PHE A 442 11.595 -22.266 -7.296 1.00 22.83 C
ANISOU 237 CZ PHE A 442 2535 2095 4045 -228 -323 1119 C
ATOM 238 N GLY A 443 13.672 -19.377 -10.550 1.00 22.45 N
ANISOU 238 N GLY A 443 2564 2284 3681 473 -1252 23 N
ATOM 239 CA GLY A 443 15.020 -19.867 -10.839 1.00 23.85 C
ANISOU 239 CA GLY A 443 2349 2815 3897 528 -1209 168 C
ATOM 240 C GLY A 443 15.696 -19.159 -12.002 1.00 29.57 C
ANISOU 240 C GLY A 443 2674 3754 4806 180 -1208 407 C
ATOM 241 O GLY A 443 16.532 -19.749 -12.688 1.00 32.85 O
ANISOU 241 O GLY A 443 2751 4570 5161 327 -996 603 O
ATOM 242 N GLY A 444 15.329 -17.899 -12.226 1.00 24.05 N
ANISOU 242 N GLY A 444 2027 2810 4299 -208 -1422 443 N
ATOM 243 CA GLY A 444 15.870 -17.103 -13.315 1.00 26.72 C
ANISOU 243 CA GLY A 444 1999 3298 4856 -569 -1388 792 C
ATOM 244 C GLY A 444 15.108 -17.177 -14.621 1.00 29.53 C
ANISOU 244 C GLY A 444 2454 3696 5071 -490 -1010 889 C
ATOM 245 O GLY A 444 15.419 -16.415 -15.540 1.00 31.51 O
ANISOU 245 O GLY A 444 2441 4072 5459 -725 -935 1245 O
ATOM 246 N GLN A 445 14.096 -18.084 -14.720 1.00 22.24 N
ANISOU 246 N GLN A 445 1886 2678 3888 -166 -789 602 N
ATOM 247 CA GLN A 445 13.287 -18.240 -15.934 1.00 20.11 C
ANISOU 247 CA GLN A 445 1720 2480 3442 -51 -520 583 C
ATOM 248 C GLN A 445 12.140 -17.250 -15.856 1.00 22.27 C
ANISOU 248 C GLN A 445 2290 2430 3740 -228 -642 504 C
ATOM 249 O GLN A 445 11.525 -17.134 -14.813 1.00 21.23 O
ANISOU 249 O GLN A 445 2435 2020 3613 -225 -825 307 O
ATOM 250 CB GLN A 445 12.674 -19.668 -16.041 1.00 18.64 C
ANISOU 250 CB GLN A 445 1777 2261 3045 287 -342 272 C
ATOM 251 CG GLN A 445 13.632 -20.851 -16.157 1.00 34.76 C
ANISOU 251 CG GLN A 445 3707 4534 4965 641 -207 267 C
ATOM 252 CD GLN A 445 12.839 -22.156 -16.274 1.00 45.03 C
ANISOU 252 CD GLN A 445 5391 5564 6153 884 -121 -72 C
ATOM 253 OE1 GLN A 445 12.041 -22.354 -17.194 1.00 45.47 O
ANISOU 253 OE1 GLN A 445 5590 5583 6105 921 -79 -262 O
ATOM 254 NE2 GLN A 445 12.986 -23.056 -15.318 1.00 22.37 N
ANISOU 254 NE2 GLN A 445 2708 2462 3331 1031 -131 -148 N
ATOM 255 N GLU A 446 11.811 -16.584 -16.956 1.00 19.25 N
ANISOU 255 N GLU A 446 1867 2150 3298 -266 -513 680 N
ATOM 256 CA GLU A 446 10.716 -15.619 -16.991 1.00 17.78 C
ANISOU 256 CA GLU A 446 1981 1711 3064 -325 -601 637 C
ATOM 257 C GLU A 446 9.717 -16.073 -18.044 1.00 20.01 C
ANISOU 257 C GLU A 446 2314 2249 3041 -71 -365 501 C
ATOM 258 O GLU A 446 10.120 -16.421 -19.139 1.00 20.45 O
ANISOU 258 O GLU A 446 2153 2657 2960 92 -157 617 O
ATOM 259 CB GLU A 446 11.248 -14.204 -17.337 1.00 22.16 C
ANISOU 259 CB GLU A 446 2467 2100 3851 -604 -711 1035 C
ATOM 260 CG GLU A 446 10.174 -13.119 -17.391 1.00 27.12 C
ANISOU 260 CG GLU A 446 3498 2415 4391 -562 -807 1017 C
ATOM 261 CD GLU A 446 10.548 -11.778 -18.008 1.00 54.52 C
ANISOU 261 CD GLU A 446 6980 5648 8087 -794 -846 1480 C
ATOM 262 OE1 GLU A 446 11.722 -11.350 -17.885 1.00 45.12 O
ANISOU 262 OE1 GLU A 446 5521 4318 7303 -1193 -993 1813 O
ATOM 263 OE2 GLU A 446 9.645 -11.143 -18.602 1.00 45.83 O
ANISOU 263 OE2 GLU A 446 6140 4502 6771 -583 -735 1550 O
ATOM 264 N PHE A 447 8.429 -16.087 -17.701 1.00 14.42 N
ANISOU 264 N PHE A 447 1853 1438 2189 12 -418 258 N
ATOM 265 CA PHE A 447 7.356 -16.352 -18.630 1.00 15.56 C
ANISOU 265 CA PHE A 447 2003 1848 2061 198 -294 105 C
ATOM 266 C PHE A 447 6.469 -15.132 -18.604 1.00 20.48 C
ANISOU 266 C PHE A 447 2821 2410 2549 267 -353 206 C
ATOM 267 O PHE A 447 6.352 -14.470 -17.567 1.00 21.08 O
ANISOU 267 O PHE A 447 3122 2178 2709 222 -528 233 O
ATOM 268 CB PHE A 447 6.504 -17.543 -18.195 1.00 17.42 C
ANISOU 268 CB PHE A 447 2268 2077 2272 206 -324 -220 C
ATOM 269 CG PHE A 447 7.106 -18.905 -18.410 1.00 20.97 C
ANISOU 269 CG PHE A 447 2650 2516 2801 233 -282 -396 C
ATOM 270 CD1 PHE A 447 7.885 -19.499 -17.428 1.00 23.19 C
ANISOU 270 CD1 PHE A 447 2964 2569 3279 179 -303 -361 C
ATOM 271 CD2 PHE A 447 6.811 -19.637 -19.547 1.00 26.13 C
ANISOU 271 CD2 PHE A 447 3270 3373 3287 391 -265 -647 C
ATOM 272 CE1 PHE A 447 8.434 -20.766 -17.621 1.00 26.44 C
ANISOU 272 CE1 PHE A 447 3396 2927 3722 302 -259 -514 C
ATOM 273 CE2 PHE A 447 7.332 -20.924 -19.721 1.00 31.83 C
ANISOU 273 CE2 PHE A 447 4059 3981 4052 503 -284 -871 C
ATOM 274 CZ PHE A 447 8.148 -21.473 -18.757 1.00 28.64 C
ANISOU 274 CZ PHE A 447 3714 3319 3850 466 -258 -778 C
ATOM 275 N ARG A 448 5.808 -14.857 -19.728 1.00 16.93 N
ANISOU 275 N ARG A 448 2329 2283 1822 478 -230 225 N
ATOM 276 CA ARG A 448 4.916 -13.734 -19.843 1.00 17.81 C
ANISOU 276 CA ARG A 448 2642 2407 1718 668 -248 339 C
ATOM 277 C ARG A 448 3.635 -14.257 -20.476 1.00 22.92 C
ANISOU 277 C ARG A 448 3153 3534 2021 898 -204 83 C
ATOM 278 O ARG A 448 3.695 -15.047 -21.416 1.00 25.15 O
ANISOU 278 O ARG A 448 3227 4134 2197 965 -145 -87 O
ATOM 279 CB ARG A 448 5.594 -12.662 -20.715 1.00 23.65 C
ANISOU 279 CB ARG A 448 3417 3099 2472 719 -126 765 C
ATOM 280 CG ARG A 448 4.918 -11.297 -20.683 1.00 47.78 C
ANISOU 280 CG ARG A 448 6828 5951 5375 926 -172 964 C
ATOM 281 CD ARG A 448 5.655 -10.253 -21.519 1.00 69.22 C
ANISOU 281 CD ARG A 448 9589 8503 8209 902 -33 1506 C
ATOM 282 NE ARG A 448 5.550 -10.497 -22.960 1.00 83.79 N
ANISOU 282 NE ARG A 448 11156 10969 9712 1234 284 1676 N
ATOM 283 CZ ARG A 448 6.374 -9.985 -23.871 1.00107.95 C
ANISOU 283 CZ ARG A 448 14055 14121 12841 1256 528 2240 C
ATOM 284 NH1 ARG A 448 7.373 -9.191 -23.502 1.00102.04 N
ANISOU 284 NH1 ARG A 448 13348 12823 12598 824 465 2717 N
ATOM 285 NH2 ARG A 448 6.209 -10.266 -25.157 1.00 96.17 N
ANISOU 285 NH2 ARG A 448 12326 13304 10911 1719 817 2355 N
ATOM 286 N THR A 449 2.475 -13.872 -19.944 1.00 22.84 N
ANISOU 286 N THR A 449 2626 4097 1956 279 284 145 N
ATOM 287 CA THR A 449 1.212 -14.280 -20.566 1.00 20.74 C
ANISOU 287 CA THR A 449 2584 3553 1744 333 236 62 C
ATOM 288 C THR A 449 0.943 -13.310 -21.728 1.00 22.73 C
ANISOU 288 C THR A 449 2879 3857 1901 221 268 100 C
ATOM 289 O THR A 449 1.672 -12.325 -21.906 1.00 20.25 O
ANISOU 289 O THR A 449 2442 3726 1526 72 350 221 O
ATOM 290 CB THR A 449 0.027 -14.229 -19.573 1.00 23.12 C
ANISOU 290 CB THR A 449 3001 3565 2219 233 158 64 C
ATOM 291 OG1 THR A 449 -0.269 -12.873 -19.198 1.00 17.76 O
ANISOU 291 OG1 THR A 449 2317 2869 1563 5 149 129 O
ATOM 292 CG2 THR A 449 0.215 -15.120 -18.372 1.00 16.92 C
ANISOU 292 CG2 THR A 449 2196 2731 1500 356 153 91 C
ATOM 293 N GLY A 450 -0.128 -13.569 -22.483 1.00 19.70 N
ANISOU 293 N GLY A 450 2661 3307 1518 283 197 12 N
ATOM 294 CA GLY A 450 -0.561 -12.640 -23.510 1.00 19.30 C
ANISOU 294 CA GLY A 450 2678 3300 1354 220 206 75 C
ATOM 295 C GLY A 450 -1.319 -11.536 -22.789 1.00 21.06 C
ANISOU 295 C GLY A 450 2944 3332 1725 2 170 171 C
ATOM 296 O GLY A 450 -1.589 -11.645 -21.581 1.00 18.57 O
ANISOU 296 O GLY A 450 2612 2874 1568 -69 132 150 O
ATOM 297 N VAL A 451 -1.701 -10.488 -23.508 1.00 18.30 N
ANISOU 297 N VAL A 451 2669 2977 1308 -64 188 283 N
ATOM 298 CA VAL A 451 -2.483 -9.403 -22.902 1.00 16.02 C
ANISOU 298 CA VAL A 451 2455 2473 1159 -216 154 360 C
ATOM 299 C VAL A 451 -3.956 -9.751 -23.050 1.00 18.01 C
ANISOU 299 C VAL A 451 2797 2572 1473 -113 19 262 C
ATOM 300 O VAL A 451 -4.403 -10.110 -24.135 1.00 16.92 O
ANISOU 300 O VAL A 451 2706 2513 1209 27 -49 208 O
ATOM 301 CB VAL A 451 -2.202 -7.998 -23.542 1.00 20.13 C
ANISOU 301 CB VAL A 451 3032 3000 1618 -332 252 570 C
ATOM 302 CG1 VAL A 451 -3.127 -6.926 -22.947 1.00 18.99 C
ANISOU 302 CG1 VAL A 451 3011 2576 1627 -426 205 617 C
ATOM 303 CG2 VAL A 451 -0.731 -7.580 -23.423 1.00 20.99 C
ANISOU 303 CG2 VAL A 451 2992 3266 1717 -501 394 684 C
ATOM 304 N VAL A 452 -4.729 -9.604 -21.976 1.00 15.70 N
ANISOU 304 N VAL A 452 2511 2095 1361 -174 -23 235 N
ATOM 305 CA VAL A 452 -6.172 -9.748 -22.120 1.00 14.81 C
ANISOU 305 CA VAL A 452 2424 1869 1334 -101 -134 178 C
ATOM 306 C VAL A 452 -6.623 -8.287 -22.245 1.00 15.85 C
ANISOU 306 C VAL A 452 2648 1920 1454 -124 -115 315 C
ATOM 307 O VAL A 452 -6.528 -7.532 -21.291 1.00 14.25 O
ANISOU 307 O VAL A 452 2478 1595 1342 -215 -57 359 O
ATOM 308 CB VAL A 452 -6.883 -10.557 -20.994 1.00 18.11 C
ANISOU 308 CB VAL A 452 2769 2157 1953 -115 -159 101 C
ATOM 309 CG1 VAL A 452 -8.404 -10.547 -21.196 1.00 18.69 C
ANISOU 309 CG1 VAL A 452 2803 2153 2143 -70 -261 68 C
ATOM 310 CG2 VAL A 452 -6.362 -11.999 -20.947 1.00 17.48 C
ANISOU 310 CG2 VAL A 452 2643 2095 1905 -74 -164 0 C
ATOM 311 N TRP A 453 -7.002 -7.866 -23.447 1.00 15.45 N
ANISOU 311 N TRP A 453 2664 1940 1265 -18 -162 382 N
ATOM 312 CA TRP A 453 -7.378 -6.468 -23.671 1.00 16.67 C
ANISOU 312 CA TRP A 453 2941 1986 1405 1 -129 556 C
ATOM 313 C TRP A 453 -8.780 -6.147 -23.132 1.00 20.93 C
ANISOU 313 C TRP A 453 3472 2393 2088 92 -214 523 C
ATOM 314 O TRP A 453 -9.707 -6.951 -23.284 1.00 20.13 O
ANISOU 314 O TRP A 453 3253 2366 2029 180 -339 403 O
ATOM 315 CB TRP A 453 -7.299 -6.135 -25.159 1.00 18.28 C
ANISOU 315 CB TRP A 453 3228 2349 1369 136 -136 691 C
ATOM 316 CG TRP A 453 -5.927 -6.335 -25.749 1.00 19.81 C
ANISOU 316 CG TRP A 453 3410 2719 1397 77 -5 766 C
ATOM 317 CD1 TRP A 453 -5.467 -7.443 -26.399 1.00 22.91 C
ANISOU 317 CD1 TRP A 453 3733 3348 1622 174 -30 636 C
ATOM 318 CD2 TRP A 453 -4.814 -5.441 -25.643 1.00 19.91 C
ANISOU 318 CD2 TRP A 453 3453 2685 1428 -101 181 969 C
ATOM 319 NE1 TRP A 453 -4.137 -7.289 -26.714 1.00 23.04 N
ANISOU 319 NE1 TRP A 453 3717 3515 1522 106 149 768 N
ATOM 320 CE2 TRP A 453 -3.717 -6.058 -26.286 1.00 24.43 C
ANISOU 320 CE2 TRP A 453 3931 3529 1822 -89 281 987 C
ATOM 321 CE3 TRP A 453 -4.653 -4.143 -25.126 1.00 21.64 C
ANISOU 321 CE3 TRP A 453 3768 2644 1808 -269 272 1133 C
ATOM 322 CZ2 TRP A 453 -2.463 -5.444 -26.386 1.00 24.85 C
ANISOU 322 CZ2 TRP A 453 3926 3645 1870 -267 479 1188 C
ATOM 323 CZ3 TRP A 453 -3.408 -3.542 -25.210 1.00 24.63 C
ANISOU 323 CZ3 TRP A 453 4117 3029 2214 -483 444 1305 C
ATOM 324 CH2 TRP A 453 -2.331 -4.190 -25.841 1.00 25.98 C
ANISOU 324 CH2 TRP A 453 4137 3516 2216 -492 552 1348 C
ATOM 325 N ASN A 454 -8.935 -4.958 -22.518 1.00 16.39 N
ANISOU 325 N ASN A 454 3010 1617 1601 73 -145 620 N
ATOM 326 CA ASN A 454 -10.227 -4.431 -22.071 1.00 17.17 C
ANISOU 326 CA ASN A 454 3113 1606 1805 221 -192 618 C
ATOM 327 C ASN A 454 -11.023 -5.381 -21.139 1.00 19.15 C
ANISOU 327 C ASN A 454 3173 1908 2196 232 -229 465 C
ATOM 328 O ASN A 454 -12.167 -5.730 -21.419 1.00 18.39 O
ANISOU 328 O ASN A 454 2937 1901 2148 357 -328 435 O
ATOM 329 CB ASN A 454 -11.074 -4.009 -23.295 1.00 16.12 C
ANISOU 329 CB ASN A 454 3014 1558 1554 445 -294 732 C
ATOM 330 CG ASN A 454 -12.273 -3.196 -22.923 1.00 33.28 C
ANISOU 330 CG ASN A 454 5206 3617 3821 642 -319 778 C
ATOM 331 OD1 ASN A 454 -12.158 -2.202 -22.234 1.00 30.62 O
ANISOU 331 OD1 ASN A 454 5029 3035 3568 643 -217 833 O
ATOM 332 ND2 ASN A 454 -13.457 -3.644 -23.307 1.00 33.65 N
ANISOU 332 ND2 ASN A 454 5068 3843 3874 815 -465 725 N
ATOM 333 N ASN A 455 -10.437 -5.755 -20.015 1.00 15.49 N
ANISOU 333 N ASN A 455 2686 1401 1800 104 -144 392 N
ATOM 334 CA ASN A 455 -11.113 -6.660 -19.079 1.00 15.12 C
ANISOU 334 CA ASN A 455 2472 1397 1874 114 -129 315 C
ATOM 335 C ASN A 455 -10.559 -6.473 -17.666 1.00 15.63 C
ANISOU 335 C ASN A 455 2591 1401 1946 57 -15 281 C
ATOM 336 O ASN A 455 -9.368 -6.634 -17.466 1.00 12.54 O
ANISOU 336 O ASN A 455 2249 1028 1490 -66 7 255 O
ATOM 337 CB ASN A 455 -10.899 -8.137 -19.526 1.00 16.51 C
ANISOU 337 CB ASN A 455 2514 1680 2077 38 -191 244 C
ATOM 338 CG ASN A 455 -11.899 -9.110 -18.963 1.00 25.60 C
ANISOU 338 CG ASN A 455 3471 2845 3413 37 -194 211 C
ATOM 339 OD1 ASN A 455 -12.444 -8.931 -17.868 1.00 17.34 O
ANISOU 339 OD1 ASN A 455 2368 1774 2447 74 -89 258 O
ATOM 340 ND2 ASN A 455 -12.134 -10.192 -19.698 1.00 18.07 N
ANISOU 340 ND2 ASN A 455 2409 1925 2532 -9 -306 125 N
ATOM 341 N ASN A 456 -11.420 -6.141 -16.699 1.00 13.87 N
ANISOU 341 N ASN A 456 2343 1150 1777 174 51 274 N
ATOM 342 CA ASN A 456 -11.031 -5.990 -15.284 1.00 13.91 C
ANISOU 342 CA ASN A 456 2405 1149 1730 179 148 217 C
ATOM 343 C ASN A 456 -10.944 -7.333 -14.535 1.00 16.99 C
ANISOU 343 C ASN A 456 2646 1670 2139 147 213 243 C
ATOM 344 O ASN A 456 -10.334 -7.402 -13.468 1.00 15.89 O
ANISOU 344 O ASN A 456 2556 1583 1897 153 271 210 O
ATOM 345 CB ASN A 456 -11.994 -5.036 -14.568 1.00 17.60 C
ANISOU 345 CB ASN A 456 2931 1555 2199 380 215 195 C
ATOM 346 CG ASN A 456 -11.812 -3.621 -15.077 1.00 39.67 C
ANISOU 346 CG ASN A 456 5951 4140 4982 415 167 170 C
ATOM 347 OD1 ASN A 456 -10.739 -3.245 -15.541 1.00 23.18 O
ANISOU 347 OD1 ASN A 456 3990 1950 2869 245 118 160 O
ATOM 348 ND2 ASN A 456 -12.848 -2.809 -15.034 1.00 29.11 N
ANISOU 348 ND2 ASN A 456 4656 2725 3679 643 193 185 N
ATOM 349 N ASN A 457 -11.507 -8.401 -15.119 1.00 14.36 N
ANISOU 349 N ASN A 457 2144 1377 1937 114 188 299 N
ATOM 350 CA ASN A 457 -11.525 -9.749 -14.521 1.00 14.91 C
ANISOU 350 CA ASN A 457 2087 1491 2087 73 263 363 C
ATOM 351 C ASN A 457 -10.927 -10.745 -15.505 1.00 15.06 C
ANISOU 351 C ASN A 457 2082 1475 2163 -41 162 326 C
ATOM 352 O ASN A 457 -11.622 -11.682 -15.905 1.00 14.49 O
ANISOU 352 O ASN A 457 1874 1359 2272 -90 131 336 O
ATOM 353 CB ASN A 457 -12.968 -10.122 -14.181 1.00 16.12 C
ANISOU 353 CB ASN A 457 2037 1673 2415 128 347 456 C
ATOM 354 CG ASN A 457 -13.600 -9.129 -13.264 1.00 30.11 C
ANISOU 354 CG ASN A 457 3830 3510 4099 305 464 480 C
ATOM 355 OD1 ASN A 457 -13.158 -8.942 -12.131 1.00 28.49 O
ANISOU 355 OD1 ASN A 457 3724 3363 3738 388 576 489 O
ATOM 356 ND2 ASN A 457 -14.625 -8.450 -13.739 1.00 26.13 N
ANISOU 356 ND2 ASN A 457 3245 3018 3664 404 429 473 N
ATOM 357 N PRO A 458 -9.665 -10.537 -15.951 1.00 10.18 N
ANISOU 357 N PRO A 458 1584 880 1404 -85 108 267 N
ATOM 358 CA PRO A 458 -9.115 -11.393 -16.996 1.00 9.42 C
ANISOU 358 CA PRO A 458 1478 782 1320 -133 23 210 C
ATOM 359 C PRO A 458 -8.824 -12.822 -16.563 1.00 13.36 C
ANISOU 359 C PRO A 458 1929 1232 1914 -134 67 234 C
ATOM 360 O PRO A 458 -8.625 -13.085 -15.385 1.00 10.81 O
ANISOU 360 O PRO A 458 1604 924 1579 -96 177 328 O
ATOM 361 CB PRO A 458 -7.815 -10.660 -17.379 1.00 10.70 C
ANISOU 361 CB PRO A 458 1744 1024 1298 -163 9 185 C
ATOM 362 CG PRO A 458 -7.390 -10.021 -16.120 1.00 14.80 C
ANISOU 362 CG PRO A 458 2304 1569 1750 -167 81 208 C
ATOM 363 CD PRO A 458 -8.683 -9.486 -15.585 1.00 11.84 C
ANISOU 363 CD PRO A 458 1924 1125 1449 -100 118 235 C
ATOM 364 N ARG A 459 -8.788 -13.737 -17.545 1.00 12.90 N
ANISOU 364 N ARG A 459 1857 1110 1933 -152 -23 142 N
ATOM 365 CA ARG A 459 -8.356 -15.108 -17.350 1.00 15.55 C
ANISOU 365 CA ARG A 459 2201 1335 2371 -131 5 140 C
ATOM 366 C ARG A 459 -7.347 -15.398 -18.449 1.00 19.00 C
ANISOU 366 C ARG A 459 2715 1836 2670 -70 -79 2 C
ATOM 367 O ARG A 459 -7.526 -14.952 -19.574 1.00 20.02 O
ANISOU 367 O ARG A 459 2859 2035 2713 -72 -185 -108 O
ATOM 368 CB ARG A 459 -9.525 -16.119 -17.327 1.00 21.06 C
ANISOU 368 CB ARG A 459 2803 1822 3375 -214 -10 143 C
ATOM 369 CG ARG A 459 -10.173 -16.415 -18.674 1.00 39.83 C
ANISOU 369 CG ARG A 459 5138 4139 5855 -277 -203 -64 C
ATOM 370 CD ARG A 459 -11.381 -17.342 -18.592 1.00 54.57 C
ANISOU 370 CD ARG A 459 6857 5792 8085 -424 -238 -79 C
ATOM 371 NE ARG A 459 -11.063 -18.650 -18.019 1.00 64.32 N
ANISOU 371 NE ARG A 459 8146 6764 9529 -453 -140 -7 N
ATOM 372 CZ ARG A 459 -10.747 -19.727 -18.730 1.00 83.80 C
ANISOU 372 CZ ARG A 459 10710 9013 12119 -459 -250 -194 C
ATOM 373 NH1 ARG A 459 -10.683 -19.661 -20.055 1.00 71.89 N
ANISOU 373 NH1 ARG A 459 9246 7570 10500 -428 -468 -485 N
ATOM 374 NH2 ARG A 459 -10.487 -20.876 -18.122 1.00 74.01 N
ANISOU 374 NH2 ARG A 459 9544 7482 11094 -463 -138 -88 N
ATOM 375 N TRP A 460 -6.266 -16.065 -18.109 1.00 15.09 N
ANISOU 375 N TRP A 460 2261 1361 2112 24 -19 26 N
ATOM 376 CA TRP A 460 -5.244 -16.449 -19.065 1.00 16.36 C
ANISOU 376 CA TRP A 460 2470 1614 2130 133 -60 -94 C
ATOM 377 C TRP A 460 -5.283 -17.977 -19.086 1.00 24.89 C
ANISOU 377 C TRP A 460 3611 2456 3392 221 -71 -162 C
ATOM 378 O TRP A 460 -5.542 -18.580 -18.047 1.00 26.41 O
ANISOU 378 O TRP A 460 3801 2482 3750 217 12 -23 O
ATOM 379 CB TRP A 460 -3.877 -15.961 -18.615 1.00 13.95 C
ANISOU 379 CB TRP A 460 2130 1548 1621 197 20 -10 C
ATOM 380 CG TRP A 460 -3.770 -14.477 -18.572 1.00 14.05 C
ANISOU 380 CG TRP A 460 2106 1719 1511 74 28 43 C
ATOM 381 CD1 TRP A 460 -3.448 -13.649 -19.607 1.00 17.31 C
ANISOU 381 CD1 TRP A 460 2523 2265 1788 33 11 17 C
ATOM 382 CD2 TRP A 460 -3.998 -13.639 -17.439 1.00 12.84 C
ANISOU 382 CD2 TRP A 460 1935 1577 1365 -11 64 133 C
ATOM 383 NE1 TRP A 460 -3.390 -12.345 -19.167 1.00 16.90 N
ANISOU 383 NE1 TRP A 460 2461 2258 1702 -99 36 97 N
ATOM 384 CE2 TRP A 460 -3.752 -12.306 -17.846 1.00 16.60 C
ANISOU 384 CE2 TRP A 460 2417 2144 1746 -121 53 135 C
ATOM 385 CE3 TRP A 460 -4.353 -13.885 -16.101 1.00 13.77 C
ANISOU 385 CE3 TRP A 460 2048 1642 1541 18 116 217 C
ATOM 386 CZ2 TRP A 460 -3.884 -11.222 -16.976 1.00 15.30 C
ANISOU 386 CZ2 TRP A 460 2272 1969 1572 -212 65 164 C
ATOM 387 CZ3 TRP A 460 -4.425 -12.816 -15.219 1.00 15.06 C
ANISOU 387 CZ3 TRP A 460 2217 1874 1632 -39 132 243 C
ATOM 388 CH2 TRP A 460 -4.211 -11.498 -15.662 1.00 15.73 C
ANISOU 388 CH2 TRP A 460 2324 2001 1652 -158 93 190 C
ATOM 389 N THR A 461 -5.094 -18.590 -20.258 1.00 23.39 N
ANISOU 389 N THR A 461 3491 2227 3169 311 -167 -373 N
ATOM 390 CA THR A 461 -5.146 -20.055 -20.413 1.00 26.16 C
ANISOU 390 CA THR A 461 3943 2276 3719 401 -202 -499 C
ATOM 391 C THR A 461 -3.766 -20.734 -20.265 1.00 30.58 C
ANISOU 391 C THR A 461 4571 2895 4155 661 -113 -481 C
ATOM 392 O THR A 461 -3.687 -21.953 -20.183 1.00 31.90 O
ANISOU 392 O THR A 461 4854 2768 4499 780 -111 -543 O
ATOM 393 CB THR A 461 -5.778 -20.422 -21.760 1.00 40.80 C
ANISOU 393 CB THR A 461 5858 4040 5605 386 -393 -807 C
ATOM 394 OG1 THR A 461 -5.065 -19.738 -22.795 1.00 42.34 O
ANISOU 394 OG1 THR A 461 6068 4577 5443 520 -420 -904 O
ATOM 395 CG2 THR A 461 -7.266 -20.096 -21.825 1.00 42.28 C
ANISOU 395 CG2 THR A 461 5944 4115 6004 147 -510 -837 C
ATOM 396 N ASP A 462 -2.694 -19.941 -20.265 1.00 26.29 N
ANISOU 396 N ASP A 462 3942 2718 3327 750 -41 -399 N
ATOM 397 CA ASP A 462 -1.300 -20.390 -20.176 1.00 25.90 C
ANISOU 397 CA ASP A 462 3875 2845 3120 1011 42 -371 C
ATOM 398 C ASP A 462 -1.034 -21.353 -19.034 1.00 27.03 C
ANISOU 398 C ASP A 462 4064 2791 3415 1152 116 -215 C
ATOM 399 O ASP A 462 -1.592 -21.208 -17.949 1.00 24.28 O
ANISOU 399 O ASP A 462 3695 2343 3189 1026 158 -24 O
ATOM 400 CB ASP A 462 -0.376 -19.171 -19.928 1.00 26.98 C
ANISOU 400 CB ASP A 462 3829 3409 3012 965 110 -235 C
ATOM 401 CG ASP A 462 -0.581 -18.000 -20.880 1.00 38.33 C
ANISOU 401 CG ASP A 462 5224 5040 4301 808 81 -286 C
ATOM 402 OD1 ASP A 462 -1.699 -17.412 -20.869 1.00 34.79 O
ANISOU 402 OD1 ASP A 462 4812 4456 3951 607 18 -278 O
ATOM 403 OD2 ASP A 462 0.380 -17.664 -21.628 1.00 40.40 O
ANISOU 403 OD2 ASP A 462 5405 5600 4344 907 138 -306 O
ATOM 404 N LYS A 463 -0.151 -22.309 -19.291 1.00 18.17 N
ANISOU 404 N LYS A 463 2562 2610 1731 20 -355 443 N
ATOM 405 CA LYS A 463 0.479 -23.201 -18.342 1.00 18.05 C
ANISOU 405 CA LYS A 463 2554 2470 1835 -81 -398 385 C
ATOM 406 C LYS A 463 1.932 -22.801 -18.465 1.00 21.72 C
ANISOU 406 C LYS A 463 3178 2817 2259 -25 -281 210 C
ATOM 407 O LYS A 463 2.431 -22.606 -19.575 1.00 22.95 O
ANISOU 407 O LYS A 463 3424 2960 2336 25 -277 107 O
ATOM 408 CB LYS A 463 0.320 -24.681 -18.714 1.00 22.81 C
ANISOU 408 CB LYS A 463 3134 2998 2535 -241 -646 331 C
ATOM 409 CG LYS A 463 -0.969 -25.308 -18.202 1.00 31.14 C
ANISOU 409 CG LYS A 463 3989 4139 3706 -365 -781 545 C
ATOM 410 CD LYS A 463 -0.799 -26.804 -17.964 1.00 30.89 C
ANISOU 410 CD LYS A 463 3964 3944 3829 -543 -984 500 C
ATOM 411 CE LYS A 463 -0.893 -27.650 -19.206 1.00 37.19 C
ANISOU 411 CE LYS A 463 4867 4642 4621 -645 -1239 351 C
ATOM 412 NZ LYS A 463 -0.669 -29.074 -18.869 1.00 34.40 N
ANISOU 412 NZ LYS A 463 4562 4080 4429 -808 -1426 308 N
ATOM 413 N MET A 464 2.594 -22.622 -17.352 1.00 16.42 N
ANISOU 413 N MET A 464 2527 2082 1628 -24 -185 197 N
ATOM 414 CA MET A 464 3.991 -22.225 -17.362 1.00 14.90 C
ANISOU 414 CA MET A 464 2444 1798 1421 -1 -91 65 C
ATOM 415 C MET A 464 4.743 -23.329 -16.724 1.00 18.69 C
ANISOU 415 C MET A 464 2914 2198 1990 -78 -169 -3 C
ATOM 416 O MET A 464 4.677 -23.500 -15.510 1.00 17.70 O
ANISOU 416 O MET A 464 2742 2070 1913 -102 -159 54 O
ATOM 417 CB MET A 464 4.171 -20.941 -16.587 1.00 16.18 C
ANISOU 417 CB MET A 464 2657 1947 1543 62 68 101 C
ATOM 418 CG MET A 464 3.586 -19.765 -17.322 1.00 20.42 C
ANISOU 418 CG MET A 464 3238 2532 1988 166 172 168 C
ATOM 419 SD MET A 464 3.678 -18.413 -16.210 1.00 24.66 S
ANISOU 419 SD MET A 464 3887 2999 2482 243 324 200 S
ATOM 420 CE MET A 464 2.975 -17.123 -17.243 1.00 21.68 C
ANISOU 420 CE MET A 464 3577 2656 2003 388 453 295 C
ATOM 421 N ASP A 465 5.402 -24.126 -17.543 1.00 15.88 N
ANISOU 421 N ASP A 465 2610 1786 1639 -86 -244 -113 N
ATOM 422 CA ASP A 465 6.131 -25.258 -17.026 1.00 16.09 C
ANISOU 422 CA ASP A 465 2642 1727 1744 -129 -315 -170 C
ATOM 423 C ASP A 465 7.570 -24.847 -16.880 1.00 19.83 C
ANISOU 423 C ASP A 465 3145 2188 2200 -85 -202 -236 C
ATOM 424 O ASP A 465 8.250 -24.592 -17.884 1.00 19.43 O
ANISOU 424 O ASP A 465 3147 2150 2087 -14 -150 -294 O
ATOM 425 CB ASP A 465 6.016 -26.451 -17.982 1.00 18.40 C
ANISOU 425 CB ASP A 465 3007 1944 2040 -137 -473 -253 C
ATOM 426 CG ASP A 465 6.508 -27.739 -17.358 1.00 19.57 C
ANISOU 426 CG ASP A 465 3176 1974 2284 -176 -558 -284 C
ATOM 427 OD1 ASP A 465 7.348 -27.680 -16.437 1.00 19.04 O
ANISOU 427 OD1 ASP A 465 3070 1912 2251 -159 -469 -269 O
ATOM 428 OD2 ASP A 465 5.953 -28.760 -17.650 1.00 16.75 O
ANISOU 428 OD2 ASP A 465 2864 1521 1979 -236 -723 -301 O
ATOM 429 N PHE A 466 8.042 -24.799 -15.633 1.00 16.18 N
ANISOU 429 N PHE A 466 2637 1723 1789 -120 -170 -209 N
ATOM 430 CA PHE A 466 9.417 -24.425 -15.347 1.00 15.03 C
ANISOU 430 CA PHE A 466 2483 1584 1644 -112 -95 -250 C
ATOM 431 C PHE A 466 10.357 -25.634 -15.419 1.00 16.49 C
ANISOU 431 C PHE A 466 2660 1742 1864 -77 -141 -294 C
ATOM 432 O PHE A 466 11.563 -25.495 -15.242 1.00 15.60 O
ANISOU 432 O PHE A 466 2503 1666 1756 -61 -88 -301 O
ATOM 433 CB PHE A 466 9.497 -23.731 -13.982 1.00 16.38 C
ANISOU 433 CB PHE A 466 2629 1773 1823 -158 -63 -214 C
ATOM 434 CG PHE A 466 8.897 -22.348 -13.986 1.00 16.83 C
ANISOU 434 CG PHE A 466 2741 1830 1823 -151 12 -187 C
ATOM 435 CD1 PHE A 466 7.541 -22.156 -13.715 1.00 18.05 C
ANISOU 435 CD1 PHE A 466 2904 2012 1944 -112 15 -111 C
ATOM 436 CD2 PHE A 466 9.679 -21.234 -14.286 1.00 17.83 C
ANISOU 436 CD2 PHE A 466 2909 1929 1936 -175 86 -213 C
ATOM 437 CE1 PHE A 466 6.988 -20.861 -13.710 1.00 19.63 C
ANISOU 437 CE1 PHE A 466 3179 2208 2073 -60 103 -77 C
ATOM 438 CE2 PHE A 466 9.131 -19.943 -14.258 1.00 20.37 C
ANISOU 438 CE2 PHE A 466 3322 2210 2209 -157 157 -188 C
ATOM 439 CZ PHE A 466 7.790 -19.768 -13.983 1.00 18.71 C
ANISOU 439 CZ PHE A 466 3145 2024 1942 -80 172 -129 C
ATOM 440 N GLU A 467 9.811 -26.799 -15.713 1.00 13.83 N
ANISOU 440 N GLU A 467 2366 1335 1552 -63 -245 -313 N
ATOM 441 CA GLU A 467 10.524 -28.083 -15.804 1.00 14.90 C
ANISOU 441 CA GLU A 467 2545 1402 1716 0 -298 -357 C
ATOM 442 C GLU A 467 11.082 -28.449 -14.437 1.00 17.31 C
ANISOU 442 C GLU A 467 2766 1724 2087 -24 -290 -299 C
ATOM 443 O GLU A 467 10.402 -28.202 -13.443 1.00 15.07 O
ANISOU 443 O GLU A 467 2426 1463 1839 -99 -305 -226 O
ATOM 444 CB GLU A 467 11.565 -28.128 -16.972 1.00 17.49 C
ANISOU 444 CB GLU A 467 2935 1754 1957 142 -231 -426 C
ATOM 445 CG GLU A 467 10.990 -27.635 -18.313 1.00 22.44 C
ANISOU 445 CG GLU A 467 3647 2394 2484 191 -230 -474 C
ATOM 446 CD GLU A 467 9.767 -28.392 -18.806 1.00 40.08 C
ANISOU 446 CD GLU A 467 5987 4524 4718 152 -398 -526 C
ATOM 447 OE1 GLU A 467 9.603 -29.564 -18.401 1.00 25.74 O
ANISOU 447 OE1 GLU A 467 4222 2582 2976 120 -517 -547 O
ATOM 448 OE2 GLU A 467 8.975 -27.823 -19.592 1.00 23.86 O
ANISOU 448 OE2 GLU A 467 3959 2511 2595 144 -422 -534 O
ATOM 449 N ASN A 468 12.280 -29.019 -14.365 1.00 15.54 N
ANISOU 449 N ASN A 468 2530 1512 1861 63 -260 -312 N
ATOM 450 CA ASN A 468 12.858 -29.454 -13.097 1.00 16.01 C
ANISOU 450 CA ASN A 468 2505 1610 1970 60 -262 -248 C
ATOM 451 C ASN A 468 13.623 -28.342 -12.456 1.00 19.25 C
ANISOU 451 C ASN A 468 2802 2159 2352 12 -199 -221 C
ATOM 452 O ASN A 468 14.521 -27.771 -13.066 1.00 20.06 O
ANISOU 452 O ASN A 468 2863 2335 2425 36 -133 -232 O
ATOM 453 CB ASN A 468 13.651 -30.736 -13.253 1.00 14.05 C
ANISOU 453 CB ASN A 468 2302 1303 1736 192 -274 -253 C
ATOM 454 CG ASN A 468 12.798 -31.890 -13.733 1.00 28.39 C
ANISOU 454 CG ASN A 468 4270 2920 3596 207 -381 -290 C
ATOM 455 OD1 ASN A 468 11.582 -31.905 -13.543 1.00 19.99 O
ANISOU 455 OD1 ASN A 468 3218 1788 2591 83 -463 -262 O
ATOM 456 ND2 ASN A 468 13.397 -32.854 -14.436 1.00 20.43 N
ANISOU 456 ND2 ASN A 468 3393 1811 2558 361 -390 -349 N
ATOM 457 N VAL A 469 13.183 -27.956 -11.261 1.00 15.83 N
ANISOU 457 N VAL A 469 2329 1760 1924 -61 -225 -180 N
ATOM 458 CA VAL A 469 13.734 -26.809 -10.519 1.00 16.80 C
ANISOU 458 CA VAL A 469 2394 1980 2007 -129 -209 -182 C
ATOM 459 C VAL A 469 14.076 -27.175 -9.077 1.00 20.10 C
ANISOU 459 C VAL A 469 2752 2472 2412 -121 -259 -135 C
ATOM 460 O VAL A 469 13.499 -28.110 -8.531 1.00 18.42 O
ANISOU 460 O VAL A 469 2547 2231 2223 -71 -283 -75 O
ATOM 461 CB VAL A 469 12.786 -25.572 -10.592 1.00 21.28 C
ANISOU 461 CB VAL A 469 3036 2517 2534 -193 -185 -207 C
ATOM 462 CG1 VAL A 469 12.481 -25.184 -12.040 1.00 20.51 C
ANISOU 462 CG1 VAL A 469 2987 2370 2434 -185 -133 -238 C
ATOM 463 CG2 VAL A 469 11.486 -25.812 -9.824 1.00 21.36 C
ANISOU 463 CG2 VAL A 469 3079 2508 2527 -173 -207 -152 C
ATOM 464 N LEU A 470 15.007 -26.434 -8.456 1.00 18.98 N
ANISOU 464 N LEU A 470 2549 2428 2235 -177 -285 -151 N
ATOM 465 CA LEU A 470 15.374 -26.620 -7.055 1.00 19.40 C
ANISOU 465 CA LEU A 470 2554 2579 2239 -164 -353 -121 C
ATOM 466 C LEU A 470 14.346 -25.809 -6.248 1.00 22.40 C
ANISOU 466 C LEU A 470 3047 2934 2531 -179 -369 -149 C
ATOM 467 O LEU A 470 14.432 -24.582 -6.220 1.00 22.78 O
ANISOU 467 O LEU A 470 3165 2960 2531 -258 -390 -225 O
ATOM 468 CB LEU A 470 16.774 -26.032 -6.806 1.00 21.03 C
ANISOU 468 CB LEU A 470 2652 2904 2436 -245 -411 -134 C
ATOM 469 CG LEU A 470 18.008 -26.933 -6.713 1.00 28.20 C
ANISOU 469 CG LEU A 470 3394 3944 3375 -180 -422 -51 C
ATOM 470 CD1 LEU A 470 17.665 -28.407 -6.491 1.00 28.93 C
ANISOU 470 CD1 LEU A 470 3498 4011 3484 -18 -386 20 C
ATOM 471 CD2 LEU A 470 18.933 -26.701 -7.881 1.00 31.52 C
ANISOU 471 CD2 LEU A 470 3712 4406 3859 -206 -365 -20 C
ATOM 472 N LEU A 471 13.362 -26.473 -5.631 1.00 24.50 N
ANISOU 472 N LEU A 471 3615 2592 3100 -58 -1859 151 N
ATOM 473 CA LEU A 471 12.302 -25.781 -4.884 1.00 24.09 C
ANISOU 473 CA LEU A 471 3746 2506 2901 -36 -1813 200 C
ATOM 474 C LEU A 471 12.779 -24.824 -3.806 1.00 30.04 C
ANISOU 474 C LEU A 471 4593 3229 3591 -169 -1810 141 C
ATOM 475 O LEU A 471 12.356 -23.683 -3.809 1.00 31.02 O
ANISOU 475 O LEU A 471 4865 3280 3641 -175 -1690 117 O
ATOM 476 CB LEU A 471 11.275 -26.750 -4.275 1.00 22.44 C
ANISOU 476 CB LEU A 471 3522 2364 2639 56 -1935 293 C
ATOM 477 CG LEU A 471 10.164 -27.290 -5.166 1.00 24.21 C
ANISOU 477 CG LEU A 471 3766 2585 2850 220 -1896 391 C
ATOM 478 CD1 LEU A 471 9.128 -27.997 -4.315 1.00 22.87 C
ANISOU 478 CD1 LEU A 471 3611 2490 2588 285 -2022 493 C
ATOM 479 CD2 LEU A 471 9.489 -26.185 -6.059 1.00 24.51 C
ANISOU 479 CD2 LEU A 471 3960 2512 2842 261 -1686 403 C
ATOM 480 N SER A 472 13.629 -25.285 -2.889 1.00 28.55 N
ANISOU 480 N SER A 472 4318 3084 3447 -283 -1956 122 N
ATOM 481 CA SER A 472 14.106 -24.496 -1.760 1.00 29.75 C
ANISOU 481 CA SER A 472 4561 3212 3531 -429 -1973 79 C
ATOM 482 C SER A 472 15.150 -23.415 -2.076 1.00 34.59 C
ANISOU 482 C SER A 472 5220 3743 4179 -520 -1889 16 C
ATOM 483 O SER A 472 15.503 -22.663 -1.161 1.00 37.78 O
ANISOU 483 O SER A 472 5722 4113 4520 -635 -1899 -14 O
ATOM 484 CB SER A 472 14.648 -25.421 -0.677 1.00 33.20 C
ANISOU 484 CB SER A 472 4889 3714 4013 -555 -2186 111 C
ATOM 485 OG SER A 472 15.727 -26.191 -1.182 1.00 43.76 O
ANISOU 485 OG SER A 472 6040 5041 5546 -583 -2291 103 O
ATOM 486 N THR A 473 15.707 -23.352 -3.308 1.00 27.30 N
ANISOU 486 N THR A 473 4222 2803 3347 -491 -1821 -1 N
ATOM 487 CA THR A 473 16.754 -22.350 -3.576 1.00 26.78 C
ANISOU 487 CA THR A 473 4189 2684 3301 -599 -1768 -43 C
ATOM 488 C THR A 473 16.492 -21.530 -4.827 1.00 28.99 C
ANISOU 488 C THR A 473 4523 2933 3557 -564 -1631 -45 C
ATOM 489 O THR A 473 17.160 -20.515 -5.035 1.00 26.91 O
ANISOU 489 O THR A 473 4314 2628 3283 -659 -1600 -60 O
ATOM 490 CB THR A 473 18.166 -22.978 -3.607 1.00 36.26 C
ANISOU 490 CB THR A 473 5216 3915 4648 -695 -1864 -69 C
ATOM 491 OG1 THR A 473 18.279 -23.802 -4.768 1.00 37.99 O
ANISOU 491 OG1 THR A 473 5267 4197 4970 -621 -1838 -97 O
ATOM 492 CG2 THR A 473 18.529 -23.761 -2.316 1.00 30.28 C
ANISOU 492 CG2 THR A 473 4396 3162 3947 -781 -2044 -46 C
ATOM 493 N GLY A 474 15.525 -21.973 -5.641 1.00 25.88 N
ANISOU 493 N GLY A 474 4118 2559 3158 -448 -1572 -11 N
ATOM 494 CA GLY A 474 15.109 -21.300 -6.874 1.00 25.46 C
ANISOU 494 CA GLY A 474 4115 2472 3086 -440 -1460 14 C
ATOM 495 C GLY A 474 14.483 -19.934 -6.687 1.00 31.72 C
ANISOU 495 C GLY A 474 5088 3146 3818 -462 -1414 27 C
ATOM 496 O GLY A 474 13.900 -19.384 -7.624 1.00 30.04 O
ANISOU 496 O GLY A 474 4928 2877 3608 -463 -1351 70 O
ATOM 497 N GLY A 475 14.722 -19.335 -5.512 1.00 35.30 N
ANISOU 497 N GLY A 475 5625 3553 4234 -507 -1461 -16 N
ATOM 498 CA GLY A 475 14.281 -17.986 -5.118 1.00 34.81 C
ANISOU 498 CA GLY A 475 5719 3368 4139 -532 -1443 -43 C
ATOM 499 C GLY A 475 12.780 -18.076 -4.975 1.00 34.57 C
ANISOU 499 C GLY A 475 5758 3287 4088 -404 -1393 -36 C
ATOM 500 O GLY A 475 12.233 -19.168 -5.189 1.00 31.55 O
ANISOU 500 O GLY A 475 5311 2975 3701 -311 -1382 12 O
ATOM 501 N PRO A 476 12.057 -16.998 -4.670 1.00 30.22 N
ANISOU 501 N PRO A 476 5328 2614 3541 -389 -1370 -82 N
ATOM 502 CA PRO A 476 10.600 -17.149 -4.597 1.00 28.58 C
ANISOU 502 CA PRO A 476 5167 2359 3333 -261 -1314 -78 C
ATOM 503 C PRO A 476 9.953 -17.177 -5.981 1.00 29.28 C
ANISOU 503 C PRO A 476 5249 2377 3501 -224 -1272 27 C
ATOM 504 O PRO A 476 10.495 -16.643 -6.942 1.00 27.98 O
ANISOU 504 O PRO A 476 5073 2169 3391 -324 -1287 71 O
ATOM 505 CB PRO A 476 10.139 -15.930 -3.791 1.00 31.68 C
ANISOU 505 CB PRO A 476 5667 2631 3738 -268 -1308 -195 C
ATOM 506 CG PRO A 476 11.240 -14.929 -3.908 1.00 38.65 C
ANISOU 506 CG PRO A 476 6576 3448 4661 -396 -1370 -218 C
ATOM 507 CD PRO A 476 12.496 -15.614 -4.376 1.00 33.77 C
ANISOU 507 CD PRO A 476 5865 2953 4012 -478 -1406 -146 C
ATOM 508 N LEU A 477 8.793 -17.809 -6.080 1.00 17.91 N
ANISOU 508 N LEU A 477 2823 1587 2395 -145 -386 361 N
ATOM 509 CA LEU A 477 8.007 -17.752 -7.298 1.00 18.42 C
ANISOU 509 CA LEU A 477 2975 1671 2353 -19 -340 264 C
ATOM 510 C LEU A 477 7.497 -16.311 -7.276 1.00 20.14 C
ANISOU 510 C LEU A 477 3119 1973 2560 -97 -275 269 C
ATOM 511 O LEU A 477 6.877 -15.918 -6.296 1.00 19.67 O
ANISOU 511 O LEU A 477 3055 1931 2489 -242 -326 248 O
ATOM 512 CB LEU A 477 6.832 -18.737 -7.238 1.00 18.37 C
ANISOU 512 CB LEU A 477 3118 1592 2269 -109 -495 174 C
ATOM 513 CG LEU A 477 5.784 -18.626 -8.356 1.00 23.59 C
ANISOU 513 CG LEU A 477 3882 2264 2816 -59 -500 107 C
ATOM 514 CD1 LEU A 477 6.410 -18.880 -9.753 1.00 24.25 C
ANISOU 514 CD1 LEU A 477 4088 2297 2829 223 -428 58 C
ATOM 515 CD2 LEU A 477 4.659 -19.640 -8.113 1.00 25.60 C
ANISOU 515 CD2 LEU A 477 4262 2458 3008 -233 -731 116 C
ATOM 516 N ARG A 478 7.848 -15.509 -8.280 1.00 16.18 N
ANISOU 516 N ARG A 478 2565 1532 2049 21 -175 314 N
ATOM 517 CA ARG A 478 7.444 -14.097 -8.326 1.00 16.92 C
ANISOU 517 CA ARG A 478 2627 1662 2140 -42 -162 324 C
ATOM 518 C ARG A 478 6.436 -13.880 -9.447 1.00 21.06 C
ANISOU 518 C ARG A 478 3197 2229 2575 38 -107 235 C
ATOM 519 O ARG A 478 6.674 -14.288 -10.566 1.00 20.33 O
ANISOU 519 O ARG A 478 3117 2168 2439 177 -46 237 O
ATOM 520 CB ARG A 478 8.669 -13.204 -8.524 1.00 19.40 C
ANISOU 520 CB ARG A 478 2824 2012 2534 -47 -159 518 C
ATOM 521 CG ARG A 478 8.398 -11.700 -8.445 1.00 42.28 C
ANISOU 521 CG ARG A 478 5754 4871 5440 -140 -241 548 C
ATOM 522 CD ARG A 478 9.690 -10.872 -8.382 1.00 54.27 C
ANISOU 522 CD ARG A 478 7172 6396 7053 -242 -347 820 C
ATOM 523 NE ARG A 478 10.362 -10.917 -7.074 1.00 62.40 N
ANISOU 523 NE ARG A 478 8235 7323 8149 -400 -483 917 N
ATOM 524 CZ ARG A 478 11.395 -11.707 -6.775 1.00 76.65 C
ANISOU 524 CZ ARG A 478 9905 9190 10028 -417 -462 1086 C
ATOM 525 NH1 ARG A 478 11.877 -12.555 -7.678 1.00 64.13 N
ANISOU 525 NH1 ARG A 478 8161 7773 8431 -227 -298 1155 N
ATOM 526 NH2 ARG A 478 11.943 -11.664 -5.565 1.00 57.91 N
ANISOU 526 NH2 ARG A 478 7576 6709 7719 -596 -609 1184 N
ATOM 527 N VAL A 479 5.309 -13.268 -9.127 1.00 17.55 N
ANISOU 527 N VAL A 479 2785 1802 2081 -23 -129 166 N
ATOM 528 CA VAL A 479 4.294 -12.947 -10.105 1.00 16.78 C
ANISOU 528 CA VAL A 479 2707 1756 1912 25 -89 118 C
ATOM 529 C VAL A 479 4.109 -11.449 -10.123 1.00 19.24 C
ANISOU 529 C VAL A 479 3003 2075 2233 37 -87 127 C
ATOM 530 O VAL A 479 3.903 -10.851 -9.062 1.00 20.47 O
ANISOU 530 O VAL A 479 3201 2206 2370 15 -141 103 O
ATOM 531 CB VAL A 479 2.965 -13.686 -9.838 1.00 19.60 C
ANISOU 531 CB VAL A 479 3099 2167 2182 -40 -139 83 C
ATOM 532 CG1 VAL A 479 1.874 -13.223 -10.815 1.00 18.92 C
ANISOU 532 CG1 VAL A 479 3009 2151 2028 -14 -109 82 C
ATOM 533 CG2 VAL A 479 3.166 -15.208 -9.936 1.00 19.09 C
ANISOU 533 CG2 VAL A 479 3121 2026 2106 -73 -231 84 C
ATOM 534 N GLN A 480 4.194 -10.837 -11.304 1.00 14.28 N
ANISOU 534 N GLN A 480 2344 1469 1614 87 -48 161 N
ATOM 535 CA GLN A 480 3.956 -9.389 -11.456 1.00 14.53 C
ANISOU 535 CA GLN A 480 2390 1472 1658 91 -98 178 C
ATOM 536 C GLN A 480 2.721 -9.202 -12.330 1.00 16.61 C
ANISOU 536 C GLN A 480 2651 1803 1856 139 -42 124 C
ATOM 537 O GLN A 480 2.561 -9.906 -13.323 1.00 15.94 O
ANISOU 537 O GLN A 480 2543 1770 1742 151 19 129 O
ATOM 538 CB GLN A 480 5.142 -8.679 -12.107 1.00 17.12 C
ANISOU 538 CB GLN A 480 2644 1792 2069 56 -147 338 C
ATOM 539 CG GLN A 480 6.454 -8.744 -11.336 1.00 22.68 C
ANISOU 539 CG GLN A 480 3311 2457 2851 -25 -228 479 C
ATOM 540 CD GLN A 480 7.552 -8.051 -12.106 1.00 31.11 C
ANISOU 540 CD GLN A 480 4238 3597 3984 -83 -295 735 C
ATOM 541 OE1 GLN A 480 7.557 -8.007 -13.334 1.00 21.47 O
ANISOU 541 OE1 GLN A 480 2906 2518 2735 -17 -207 800 O
ATOM 542 NE2 GLN A 480 8.521 -7.502 -11.406 1.00 32.91 N
ANISOU 542 NE2 GLN A 480 4458 3754 4291 -227 -473 929 N
ATOM 543 N VAL A 481 1.858 -8.265 -11.976 1.00 13.99 N
ANISOU 543 N VAL A 481 2367 1466 1482 191 -77 80 N
ATOM 544 CA VAL A 481 0.654 -7.968 -12.751 1.00 14.51 C
ANISOU 544 CA VAL A 481 2401 1617 1493 240 -29 69 C
ATOM 545 C VAL A 481 0.890 -6.662 -13.461 1.00 17.37 C
ANISOU 545 C VAL A 481 2787 1902 1912 258 -97 100 C
ATOM 546 O VAL A 481 1.091 -5.673 -12.792 1.00 15.00 O
ANISOU 546 O VAL A 481 2597 1485 1615 307 -216 77 O
ATOM 547 CB VAL A 481 -0.617 -7.950 -11.867 1.00 19.88 C
ANISOU 547 CB VAL A 481 3077 2420 2054 336 -1 42 C
ATOM 548 CG1 VAL A 481 -1.871 -7.827 -12.735 1.00 20.02 C
ANISOU 548 CG1 VAL A 481 3012 2573 2023 363 52 101 C
ATOM 549 CG2 VAL A 481 -0.683 -9.218 -11.021 1.00 19.76 C
ANISOU 549 CG2 VAL A 481 3022 2490 1995 266 13 63 C
ATOM 550 N TRP A 482 0.920 -6.662 -14.816 1.00 15.37 N
ANISOU 550 N TRP A 482 2458 1694 1688 211 -59 160 N
ATOM 551 CA TRP A 482 1.172 -5.456 -15.598 1.00 15.42 C
ANISOU 551 CA TRP A 482 2452 1650 1756 186 -149 231 C
ATOM 552 C TRP A 482 -0.030 -5.056 -16.422 1.00 18.21 C
ANISOU 552 C TRP A 482 2780 2060 2080 219 -113 220 C
ATOM 553 O TRP A 482 -0.790 -5.912 -16.840 1.00 16.06 O
ANISOU 553 O TRP A 482 2464 1890 1746 209 -11 210 O
ATOM 554 CB TRP A 482 2.366 -5.659 -16.540 1.00 14.70 C
ANISOU 554 CB TRP A 482 2249 1625 1712 106 -136 371 C
ATOM 555 CG TRP A 482 3.692 -5.815 -15.858 1.00 16.54 C
ANISOU 555 CG TRP A 482 2454 1835 1995 61 -195 470 C
ATOM 556 CD1 TRP A 482 4.221 -6.962 -15.339 1.00 19.22 C
ANISOU 556 CD1 TRP A 482 2779 2212 2310 93 -107 446 C
ATOM 557 CD2 TRP A 482 4.682 -4.789 -15.663 1.00 17.62 C
ANISOU 557 CD2 TRP A 482 2570 1907 2219 -52 -395 657 C
ATOM 558 NE1 TRP A 482 5.480 -6.714 -14.831 1.00 18.82 N
ANISOU 558 NE1 TRP A 482 2670 2150 2329 23 -202 610 N
ATOM 559 CE2 TRP A 482 5.782 -5.386 -15.007 1.00 21.23 C
ANISOU 559 CE2 TRP A 482 2970 2394 2701 -88 -395 761 C
ATOM 560 CE3 TRP A 482 4.737 -3.415 -15.967 1.00 20.37 C
ANISOU 560 CE3 TRP A 482 2955 2155 2627 -150 -620 776 C
ATOM 561 CZ2 TRP A 482 6.918 -4.653 -14.625 1.00 22.26 C
ANISOU 561 CZ2 TRP A 482 3062 2479 2917 -242 -614 1012 C
ATOM 562 CZ3 TRP A 482 5.884 -2.697 -15.626 1.00 23.46 C
ANISOU 562 CZ3 TRP A 482 3337 2477 3100 -316 -874 1022 C
ATOM 563 CH2 TRP A 482 6.937 -3.305 -14.928 1.00 24.12 C
ANISOU 563 CH2 TRP A 482 3352 2606 3207 -371 -872 1148 C
ATOM 564 N ASP A 483 -0.200 -3.745 -16.657 1.00 16.75 N
ANISOU 564 N ASP A 483 2640 1786 1938 240 -239 245 N
ATOM 565 CA ASP A 483 -1.241 -3.219 -17.523 1.00 16.54 C
ANISOU 565 CA ASP A 483 2573 1807 1906 265 -224 262 C
ATOM 566 C ASP A 483 -0.531 -2.663 -18.750 1.00 22.35 C
ANISOU 566 C ASP A 483 3230 2539 2725 124 -303 390 C
ATOM 567 O ASP A 483 0.346 -1.820 -18.608 1.00 24.45 O
ANISOU 567 O ASP A 483 3534 2693 3062 61 -486 473 O
ATOM 568 CB ASP A 483 -2.072 -2.115 -16.843 1.00 19.12 C
ANISOU 568 CB ASP A 483 3028 2040 2195 451 -322 193 C
ATOM 569 CG ASP A 483 -3.378 -1.820 -17.575 1.00 29.42 C
ANISOU 569 CG ASP A 483 4251 3454 3473 520 -256 228 C
ATOM 570 OD1 ASP A 483 -3.387 -1.828 -18.814 1.00 31.83 O
ANISOU 570 OD1 ASP A 483 4447 3806 3838 367 -239 317 O
ATOM 571 OD2 ASP A 483 -4.377 -1.591 -16.912 1.00 36.45 O
ANISOU 571 OD2 ASP A 483 5175 4408 4266 740 -218 188 O
ATOM 572 N ALA A 484 -0.907 -3.130 -19.943 1.00 18.48 N
ANISOU 572 N ALA A 484 2635 2177 2208 60 -195 439 N
ATOM 573 CA ALA A 484 -0.305 -2.706 -21.201 1.00 19.51 C
ANISOU 573 CA ALA A 484 2660 2379 2376 -55 -236 580 C
ATOM 574 C ALA A 484 -0.787 -1.298 -21.591 1.00 22.97 C
ANISOU 574 C ALA A 484 3104 2724 2900 -98 -410 642 C
ATOM 575 O ALA A 484 -0.120 -0.637 -22.369 1.00 24.66 O
ANISOU 575 O ALA A 484 3227 2971 3171 -226 -530 804 O
ATOM 576 CB ALA A 484 -0.613 -3.720 -22.297 1.00 20.03 C
ANISOU 576 CB ALA A 484 2683 2588 2340 -73 -80 581 C
ATOM 577 N ASP A 485 -1.937 -0.828 -21.028 1.00 18.21 N
ANISOU 577 N ASP A 485 2600 2026 2292 28 -437 540 N
ATOM 578 CA ASP A 485 -2.488 0.528 -21.245 1.00 17.69 C
ANISOU 578 CA ASP A 485 2599 1830 2292 62 -624 566 C
ATOM 579 C ASP A 485 -2.603 0.939 -22.724 1.00 19.33 C
ANISOU 579 C ASP A 485 2667 2116 2560 -109 -660 711 C
ATOM 580 O ASP A 485 -2.025 1.936 -23.139 1.00 19.24 O
ANISOU 580 O ASP A 485 2654 2016 2639 -228 -888 834 O
ATOM 581 CB ASP A 485 -1.664 1.552 -20.452 1.00 20.29 C
ANISOU 581 CB ASP A 485 3113 1921 2677 75 -911 573 C
ATOM 582 CG ASP A 485 -2.481 2.635 -19.824 1.00 22.40 C
ANISOU 582 CG ASP A 485 3612 1978 2920 301 -1086 464 C
ATOM 583 OD1 ASP A 485 -3.640 2.379 -19.514 1.00 22.71 O
ANISOU 583 OD1 ASP A 485 3648 2115 2866 525 -908 360 O
ATOM 584 OD2 ASP A 485 -1.919 3.702 -19.521 1.00 29.07 O
ANISOU 584 OD2 ASP A 485 4669 2562 3814 276 -1423 496 O
ATOM 585 N ALA A 486 -3.304 0.122 -23.530 1.00 16.07 N
ANISOU 585 N ALA A 486 2146 1870 2089 -150 -468 723 N
ATOM 586 CA ALA A 486 -3.528 0.335 -24.964 1.00 16.35 C
ANISOU 586 CA ALA A 486 2064 2002 2146 -309 -473 849 C
ATOM 587 C ALA A 486 -2.243 0.289 -25.800 1.00 22.04 C
ANISOU 587 C ALA A 486 2675 2841 2858 -455 -501 987 C
ATOM 588 O ALA A 486 -2.265 0.643 -26.954 1.00 22.23 O
ANISOU 588 O ALA A 486 2592 2966 2890 -585 -534 1116 O
ATOM 589 CB ALA A 486 -4.275 1.659 -25.200 1.00 18.40 C
ANISOU 589 CB ALA A 486 2337 2144 2508 -300 -650 898 C
ATOM 590 N GLY A 487 -1.143 -0.149 -25.215 1.00 21.76 N
ANISOU 590 N GLY A 487 2640 2835 2792 -422 -480 990 N
ATOM 591 CA GLY A 487 0.133 -0.194 -25.900 1.00 22.88 C
ANISOU 591 CA GLY A 487 2624 3170 2899 -511 -488 1182 C
ATOM 592 C GLY A 487 1.096 0.849 -25.381 1.00 27.67 C
ANISOU 592 C GLY A 487 3189 3699 3624 -622 -758 1364 C
ATOM 593 O GLY A 487 2.275 0.790 -25.722 1.00 27.55 O
ANISOU 593 O GLY A 487 2996 3892 3579 -697 -779 1595 O
ATOM 594 N ALA A 488 0.605 1.846 -24.595 1.00 26.08 N
ANISOU 594 N ALA A 488 3164 3208 3538 -624 -997 1296 N
ATOM 595 CA ALA A 488 1.466 2.927 -24.048 1.00 29.60 C
ANISOU 595 CA ALA A 488 3671 3484 4090 -760 -1366 1476 C
ATOM 596 C ALA A 488 2.393 2.341 -22.977 1.00 34.82 C
ANISOU 596 C ALA A 488 4374 4133 4721 -719 -1344 1474 C
ATOM 597 O ALA A 488 2.396 1.125 -22.822 1.00 34.08 O
ANISOU 597 O ALA A 488 4230 4188 4531 -584 -1034 1343 O
ATOM 598 CB ALA A 488 0.610 4.061 -23.479 1.00 31.08 C
ANISOU 598 CB ALA A 488 4137 3317 4354 -689 -1641 1346 C
ATOM 599 N ASP A 489 3.198 3.143 -22.262 1.00 33.97 N
ANISOU 599 N ASP A 489 4374 3839 4692 -852 -1697 1637 N
ATOM 600 CA ASP A 489 4.080 2.576 -21.224 1.00 33.45 C
ANISOU 600 CA ASP A 489 4344 3760 4603 -836 -1684 1658 C
ATOM 601 C ASP A 489 3.342 1.583 -20.315 1.00 35.19 C
ANISOU 601 C ASP A 489 4723 3913 4736 -571 -1390 1292 C
ATOM 602 O ASP A 489 2.203 1.851 -19.934 1.00 35.34 O
ANISOU 602 O ASP A 489 4949 3750 4730 -406 -1383 1048 O
ATOM 603 CB ASP A 489 4.748 3.672 -20.375 1.00 37.69 C
ANISOU 603 CB ASP A 489 5106 3987 5227 -1011 -2178 1830 C
ATOM 604 N ASP A 490 3.967 0.424 -20.017 1.00 29.31 N
ANISOU 604 N ASP A 490 3854 3351 3932 -519 -1149 1289 N
ATOM 605 CA ASP A 490 3.383 -0.603 -19.150 1.00 27.39 C
ANISOU 605 CA ASP A 490 3729 3068 3611 -322 -911 1002 C
ATOM 606 C ASP A 490 3.365 -0.123 -17.701 1.00 30.76 C
ANISOU 606 C ASP A 490 4430 3211 4049 -275 -1116 891 C
ATOM 607 O ASP A 490 4.374 0.418 -17.223 1.00 31.87 O
ANISOU 607 O ASP A 490 4624 3237 4248 -427 -1385 1079 O
ATOM 608 CB ASP A 490 4.195 -1.904 -19.203 1.00 29.44 C
ANISOU 608 CB ASP A 490 3822 3553 3812 -286 -675 1053 C
ATOM 609 CG ASP A 490 4.221 -2.649 -20.517 1.00 41.99 C
ANISOU 609 CG ASP A 490 5219 5420 5313 -235 -444 1109 C
ATOM 610 OD1 ASP A 490 3.187 -2.677 -21.203 1.00 38.90 O
ANISOU 610 OD1 ASP A 490 4863 5034 4884 -197 -360 990 O
ATOM 611 OD2 ASP A 490 5.243 -3.309 -20.798 1.00 56.60 O
ANISOU 611 OD2 ASP A 490 6910 7487 7107 -196 -336 1261 O
ATOM 612 N ASP A 491 2.234 -0.345 -16.993 1.00 24.62 N
ANISOU 612 N ASP A 491 3819 2345 3189 -64 -999 620 N
ATOM 613 CA ASP A 491 2.119 0.030 -15.573 1.00 25.19 C
ANISOU 613 CA ASP A 491 4178 2187 3206 58 -1152 480 C
ATOM 614 C ASP A 491 2.185 -1.242 -14.723 1.00 26.39 C
ANISOU 614 C ASP A 491 4280 2456 3291 130 -918 372 C
ATOM 615 O ASP A 491 1.491 -2.207 -15.045 1.00 22.84 O
ANISOU 615 O ASP A 491 3688 2200 2791 202 -648 291 O
ATOM 616 CB ASP A 491 0.769 0.710 -15.283 1.00 27.84 C
ANISOU 616 CB ASP A 491 4719 2413 3447 318 -1174 282 C
ATOM 617 CG ASP A 491 0.462 1.953 -16.089 1.00 51.73 C
ANISOU 617 CG ASP A 491 7830 5293 6531 296 -1410 348 C
ATOM 618 OD1 ASP A 491 0.958 3.039 -15.715 1.00 57.27 O
ANISOU 618 OD1 ASP A 491 8803 5699 7260 246 -1798 402 O
ATOM 619 OD2 ASP A 491 -0.352 1.859 -17.041 1.00 57.71 O
ANISOU 619 OD2 ASP A 491 8421 6207 7300 329 -1245 346 O
ATOM 620 N LEU A 492 2.952 -1.226 -13.617 1.00 24.77 N
ANISOU 620 N LEU A 492 4219 2111 3081 91 -1062 385 N
ATOM 621 CA LEU A 492 2.995 -2.340 -12.683 1.00 24.37 C
ANISOU 621 CA LEU A 492 4146 2145 2969 151 -883 284 C
ATOM 622 C LEU A 492 1.793 -2.226 -11.740 1.00 27.56 C
ANISOU 622 C LEU A 492 4735 2523 3215 414 -824 60 C
ATOM 623 O LEU A 492 1.714 -1.273 -10.984 1.00 29.75 O
ANISOU 623 O LEU A 492 5306 2584 3414 537 -1043 -17 O
ATOM 624 CB LEU A 492 4.325 -2.386 -11.899 1.00 25.03 C
ANISOU 624 CB LEU A 492 4288 2113 3111 -12 -1062 421 C
ATOM 625 CG LEU A 492 4.531 -3.585 -10.942 1.00 28.03 C
ANISOU 625 CG LEU A 492 4623 2575 3450 13 -896 346 C
ATOM 626 CD1 LEU A 492 4.381 -4.933 -11.658 1.00 27.15 C
ANISOU 626 CD1 LEU A 492 4247 2718 3352 25 -597 342 C
ATOM 627 CD2 LEU A 492 5.897 -3.518 -10.285 1.00 28.84 C
ANISOU 627 CD2 LEU A 492 4763 2564 3630 -177 -1098 533 C
ATOM 628 N LEU A 493 0.846 -3.162 -11.816 1.00 20.39 N
ANISOU 628 N LEU A 493 3666 1848 2235 513 -557 -14 N
ATOM 629 CA LEU A 493 -0.364 -3.125 -10.980 1.00 20.76 C
ANISOU 629 CA LEU A 493 3791 1994 2103 779 -465 -142 C
ATOM 630 C LEU A 493 -0.116 -3.705 -9.598 1.00 26.05 C
ANISOU 630 C LEU A 493 4539 2685 2675 828 -448 -204 C
ATOM 631 O LEU A 493 -0.822 -3.380 -8.644 1.00 28.00 O
ANISOU 631 O LEU A 493 4922 2983 2732 1090 -436 -302 O
ATOM 632 CB LEU A 493 -1.547 -3.845 -11.656 1.00 19.19 C
ANISOU 632 CB LEU A 493 3352 2075 1866 812 -239 -101 C
ATOM 633 CG LEU A 493 -2.124 -3.224 -12.961 1.00 21.88 C
ANISOU 633 CG LEU A 493 3619 2432 2264 806 -236 -47 C
ATOM 634 CD1 LEU A 493 -3.213 -4.115 -13.551 1.00 21.09 C
ANISOU 634 CD1 LEU A 493 3295 2599 2121 779 -52 41 C
ATOM 635 CD2 LEU A 493 -2.651 -1.801 -12.738 1.00 19.95 C
ANISOU 635 CD2 LEU A 493 3578 2057 1944 1058 -373 -120 C
ATOM 636 N GLY A 494 0.882 -4.564 -9.512 1.00 20.49 N
ANISOU 636 N GLY A 494 3739 1966 2080 605 -438 -134 N
ATOM 637 CA GLY A 494 1.255 -5.229 -8.280 1.00 20.72 C
ANISOU 637 CA GLY A 494 3810 2009 2053 588 -432 -164 C
ATOM 638 C GLY A 494 2.098 -6.458 -8.516 1.00 23.07 C
ANISOU 638 C GLY A 494 3924 2360 2483 364 -361 -68 C
ATOM 639 O GLY A 494 2.299 -6.890 -9.651 1.00 20.05 O
ANISOU 639 O GLY A 494 3389 2033 2196 270 -288 4 O
ATOM 640 N SER A 495 2.619 -7.008 -7.437 1.00 20.54 N
ANISOU 640 N SER A 495 3642 2013 2147 307 -392 -72 N
ATOM 641 CA SER A 495 3.432 -8.206 -7.496 1.00 20.41 C
ANISOU 641 CA SER A 495 3479 2035 2242 139 -339 11 C
ATOM 642 C SER A 495 3.335 -8.957 -6.187 1.00 25.24 C
ANISOU 642 C SER A 495 4105 2704 2781 123 -331 -23 C
ATOM 643 O SER A 495 2.838 -8.415 -5.196 1.00 25.60 O
ANISOU 643 O SER A 495 4291 2758 2679 246 -373 -100 O
ATOM 644 CB SER A 495 4.884 -7.871 -7.840 1.00 24.27 C
ANISOU 644 CB SER A 495 3958 2384 2877 -3 -457 156 C
ATOM 645 OG SER A 495 5.417 -6.893 -6.968 1.00 38.08 O
ANISOU 645 OG SER A 495 5914 3939 4616 -45 -677 184 O
ATOM 646 N CYS A 496 3.750 -10.214 -6.198 1.00 22.58 N
ANISOU 646 N CYS A 496 3640 2419 2520 3 -282 33 N
ATOM 647 CA CYS A 496 3.804 -11.030 -4.998 1.00 24.94 C
ANISOU 647 CA CYS A 496 3928 2766 2781 -66 -303 35 C
ATOM 648 C CYS A 496 4.860 -12.057 -5.145 1.00 24.05 C
ANISOU 648 C CYS A 496 3736 2591 2812 -199 -319 116 C
ATOM 649 O CYS A 496 5.150 -12.483 -6.263 1.00 22.44 O
ANISOU 649 O CYS A 496 3467 2382 2678 -184 -267 148 O
ATOM 650 CB CYS A 496 2.458 -11.671 -4.697 1.00 27.95 C
ANISOU 650 CB CYS A 496 4216 3381 3024 -22 -234 29 C
ATOM 651 SG CYS A 496 1.907 -12.847 -5.959 1.00 32.83 S
ANISOU 651 SG CYS A 496 4706 4075 3693 -106 -200 94 S
ATOM 652 N ASP A 497 5.385 -12.500 -4.006 1.00 19.59 N
ANISOU 652 N ASP A 497 3188 1992 2265 -298 -387 146 N
ATOM 653 CA ASP A 497 6.376 -13.557 -3.879 1.00 18.75 C
ANISOU 653 CA ASP A 497 3008 1831 2285 -406 -414 232 C
ATOM 654 C ASP A 497 5.785 -14.689 -3.053 1.00 21.92 C
ANISOU 654 C ASP A 497 3370 2322 2638 -491 -448 220 C
ATOM 655 O ASP A 497 5.160 -14.450 -2.011 1.00 18.59 O
ANISOU 655 O ASP A 497 2971 1996 2096 -511 -473 197 O
ATOM 656 CB ASP A 497 7.648 -13.040 -3.177 1.00 21.05 C
ANISOU 656 CB ASP A 497 3337 1992 2669 -509 -516 343 C
ATOM 657 CG ASP A 497 8.302 -11.857 -3.878 1.00 42.80 C
ANISOU 657 CG ASP A 497 6119 4667 5477 -494 -564 440 C
ATOM 658 OD1 ASP A 497 7.650 -10.788 -3.986 1.00 50.46 O
ANISOU 658 OD1 ASP A 497 7212 5605 6356 -422 -597 357 O
ATOM 659 OD2 ASP A 497 9.474 -11.977 -4.272 1.00 45.00 O
ANISOU 659 OD2 ASP A 497 6289 4930 5879 -555 -591 633 O
ATOM 660 N ARG A 498 5.950 -15.912 -3.545 1.00 21.12 N
ANISOU 660 N ARG A 498 3226 2198 2600 -521 -469 247 N
ATOM 661 CA ARG A 498 5.529 -17.138 -2.843 1.00 22.40 C
ANISOU 661 CA ARG A 498 3361 2405 2745 -655 -579 283 C
ATOM 662 C ARG A 498 6.682 -18.122 -2.823 1.00 26.74 C
ANISOU 662 C ARG A 498 3924 2804 3431 -686 -649 330 C
ATOM 663 O ARG A 498 7.536 -18.096 -3.701 1.00 24.60 O
ANISOU 663 O ARG A 498 3669 2450 3228 -547 -585 336 O
ATOM 664 CB ARG A 498 4.265 -17.761 -3.470 1.00 24.96 C
ANISOU 664 CB ARG A 498 3681 2828 2975 -674 -631 295 C
ATOM 665 CG ARG A 498 2.987 -16.941 -3.241 1.00 28.82 C
ANISOU 665 CG ARG A 498 4095 3549 3308 -638 -561 311 C
ATOM 666 CD ARG A 498 2.601 -16.784 -1.763 1.00 26.55 C
ANISOU 666 CD ARG A 498 3724 3456 2908 -696 -573 370 C
ATOM 667 NE ARG A 498 1.364 -16.023 -1.613 1.00 27.26 N
ANISOU 667 NE ARG A 498 3733 3821 2803 -568 -480 403 N
ATOM 668 CZ ARG A 498 1.303 -14.701 -1.483 1.00 36.90 C
ANISOU 668 CZ ARG A 498 5035 5057 3929 -355 -364 296 C
ATOM 669 NH1 ARG A 498 2.415 -13.979 -1.443 1.00 24.57 N
ANISOU 669 NH1 ARG A 498 3637 3237 2460 -312 -367 179 N
ATOM 670 NH2 ARG A 498 0.127 -14.093 -1.366 1.00 27.41 N
ANISOU 670 NH2 ARG A 498 3759 4131 2525 -179 -273 335 N
ATOM 671 N SER A 499 6.763 -18.918 -1.770 1.00 23.62 N
ANISOU 671 N SER A 499 3829 2482 2664 86 -701 -829 N
ATOM 672 CA SER A 499 7.801 -19.924 -1.617 1.00 22.97 C
ANISOU 672 CA SER A 499 3760 2476 2491 92 -751 -882 C
ATOM 673 C SER A 499 7.124 -21.242 -1.968 1.00 24.69 C
ANISOU 673 C SER A 499 4021 2778 2581 69 -664 -674 C
ATOM 674 O SER A 499 6.273 -21.682 -1.197 1.00 24.11 O
ANISOU 674 O SER A 499 3996 2776 2387 197 -601 -598 O
ATOM 675 CB SER A 499 8.305 -19.943 -0.174 1.00 28.22 C
ANISOU 675 CB SER A 499 4459 3241 3022 311 -839 -1097 C
ATOM 676 OG SER A 499 9.396 -19.047 -0.022 1.00 45.66 O
ANISOU 676 OG SER A 499 6583 5358 5409 311 -963 -1356 O
ATOM 677 N PRO A 500 7.364 -21.851 -3.157 1.00 20.80 N
ANISOU 677 N PRO A 500 3486 2273 2146 -67 -656 -567 N
ATOM 678 CA PRO A 500 6.641 -23.089 -3.473 1.00 19.55 C
ANISOU 678 CA PRO A 500 3323 2167 1937 -71 -601 -414 C
ATOM 679 C PRO A 500 7.118 -24.302 -2.683 1.00 18.56 C
ANISOU 679 C PRO A 500 3236 2132 1686 5 -608 -417 C
ATOM 680 O PRO A 500 8.270 -24.406 -2.281 1.00 17.36 O
ANISOU 680 O PRO A 500 3114 2029 1455 25 -680 -543 O
ATOM 681 CB PRO A 500 6.869 -23.260 -4.970 1.00 21.58 C
ANISOU 681 CB PRO A 500 3500 2410 2289 -182 -630 -354 C
ATOM 682 CG PRO A 500 8.191 -22.626 -5.197 1.00 26.82 C
ANISOU 682 CG PRO A 500 4148 3050 2993 -235 -698 -451 C
ATOM 683 CD PRO A 500 8.273 -21.467 -4.257 1.00 22.71 C
ANISOU 683 CD PRO A 500 3655 2456 2518 -187 -697 -577 C
ATOM 684 N HIS A 501 6.209 -25.203 -2.443 1.00 15.82 N
ANISOU 684 N HIS A 501 2873 1797 1342 60 -519 -276 N
ATOM 685 CA HIS A 501 6.529 -26.470 -1.788 1.00 15.69 C
ANISOU 685 CA HIS A 501 2865 1847 1248 143 -482 -220 C
ATOM 686 C HIS A 501 5.774 -27.596 -2.502 1.00 17.54 C
ANISOU 686 C HIS A 501 2989 2020 1656 80 -438 -73 C
ATOM 687 O HIS A 501 4.845 -27.302 -3.253 1.00 17.51 O
ANISOU 687 O HIS A 501 2917 1941 1796 23 -425 -33 O
ATOM 688 CB HIS A 501 6.305 -26.390 -0.277 1.00 17.60 C
ANISOU 688 CB HIS A 501 3179 2174 1335 379 -387 -199 C
ATOM 689 CG HIS A 501 4.962 -25.869 0.094 1.00 21.75 C
ANISOU 689 CG HIS A 501 3697 2664 1902 466 -281 -83 C
ATOM 690 ND1 HIS A 501 3.974 -26.707 0.545 1.00 24.51 N
ANISOU 690 ND1 HIS A 501 3999 2998 2315 572 -119 140 N
ATOM 691 CD2 HIS A 501 4.489 -24.602 0.068 1.00 25.02 C
ANISOU 691 CD2 HIS A 501 4137 3048 2323 461 -313 -154 C
ATOM 692 CE1 HIS A 501 2.929 -25.932 0.782 1.00 25.15 C
ANISOU 692 CE1 HIS A 501 4090 3056 2411 630 -63 195 C
ATOM 693 NE2 HIS A 501 3.186 -24.660 0.483 1.00 25.65 N
ANISOU 693 NE2 HIS A 501 4202 3114 2429 560 -184 15 N
ATOM 694 N SER A 502 6.200 -28.867 -2.339 1.00 13.85 N
ANISOU 694 N SER A 502 2485 1577 1200 97 -430 -22 N
ATOM 695 CA SER A 502 5.609 -29.996 -3.069 1.00 13.74 C
ANISOU 695 CA SER A 502 2319 1479 1424 39 -428 69 C
ATOM 696 C SER A 502 4.103 -30.089 -2.918 1.00 19.05 C
ANISOU 696 C SER A 502 2895 2033 2310 91 -290 209 C
ATOM 697 O SER A 502 3.550 -29.691 -1.882 1.00 20.15 O
ANISOU 697 O SER A 502 3098 2181 2377 220 -144 314 O
ATOM 698 CB SER A 502 6.265 -31.321 -2.670 1.00 16.40 C
ANISOU 698 CB SER A 502 2627 1844 1760 76 -411 122 C
ATOM 699 OG SER A 502 6.126 -31.546 -1.286 1.00 24.63 O
ANISOU 699 OG SER A 502 3731 2922 2704 261 -228 255 O
ATOM 700 N GLY A 503 3.462 -30.613 -3.955 1.00 13.75 N
ANISOU 700 N GLY A 503 2058 1264 1901 20 -349 192 N
ATOM 701 CA GLY A 503 2.020 -30.777 -3.968 1.00 14.18 C
ANISOU 701 CA GLY A 503 1983 1180 2224 58 -237 288 C
ATOM 702 C GLY A 503 1.321 -29.736 -4.809 1.00 18.34 C
ANISOU 702 C GLY A 503 2512 1701 2753 20 -293 187 C
ATOM 703 O GLY A 503 1.929 -29.032 -5.626 1.00 16.82 O
ANISOU 703 O GLY A 503 2378 1600 2413 -32 -423 56 O
ATOM 704 N PHE A 504 0.032 -29.667 -4.620 1.00 16.56 N
ANISOU 704 N PHE A 504 2214 1369 2711 65 -178 265 N
ATOM 705 CA PHE A 504 -0.875 -28.769 -5.302 1.00 15.59 C
ANISOU 705 CA PHE A 504 2084 1230 2609 56 -197 183 C
ATOM 706 C PHE A 504 -1.222 -27.619 -4.375 1.00 18.52 C
ANISOU 706 C PHE A 504 2631 1644 2761 98 -81 269 C
ATOM 707 O PHE A 504 -1.757 -27.842 -3.279 1.00 19.89 O
ANISOU 707 O PHE A 504 2817 1780 2961 187 73 437 O
ATOM 708 CB PHE A 504 -2.157 -29.529 -5.723 1.00 18.20 C
ANISOU 708 CB PHE A 504 2186 1398 3333 87 -163 175 C
ATOM 709 CG PHE A 504 -3.271 -28.605 -6.167 1.00 20.61 C
ANISOU 709 CG PHE A 504 2500 1687 3643 110 -139 109 C
ATOM 710 CD1 PHE A 504 -3.056 -27.649 -7.158 1.00 20.75 C
ANISOU 710 CD1 PHE A 504 2591 1827 3465 106 -250 -46 C
ATOM 711 CD2 PHE A 504 -4.527 -28.664 -5.566 1.00 25.26 C
ANISOU 711 CD2 PHE A 504 3026 2146 4425 154 16 224 C
ATOM 712 CE1 PHE A 504 -4.087 -26.802 -7.572 1.00 22.45 C
ANISOU 712 CE1 PHE A 504 2824 2042 3666 146 -215 -107 C
ATOM 713 CE2 PHE A 504 -5.545 -27.780 -5.957 1.00 27.38 C
ANISOU 713 CE2 PHE A 504 3324 2415 4666 174 35 150 C
ATOM 714 CZ PHE A 504 -5.322 -26.873 -6.967 1.00 22.61 C
ANISOU 714 CZ PHE A 504 2798 1939 3855 169 -85 -26 C
ATOM 715 N HIS A 505 -0.959 -26.394 -4.820 1.00 11.65 N
ANISOU 715 N HIS A 505 1878 855 1695 62 -148 166 N
ATOM 716 CA HIS A 505 -1.269 -25.223 -3.993 1.00 13.78 C
ANISOU 716 CA HIS A 505 2296 1162 1777 106 -76 208 C
ATOM 717 C HIS A 505 -1.889 -24.083 -4.791 1.00 18.04 C
ANISOU 717 C HIS A 505 2866 1703 2285 74 -97 125 C
ATOM 718 O HIS A 505 -1.493 -23.839 -5.930 1.00 17.41 O
ANISOU 718 O HIS A 505 2750 1652 2212 31 -182 25 O
ATOM 719 CB HIS A 505 -0.011 -24.774 -3.225 1.00 15.18 C
ANISOU 719 CB HIS A 505 2602 1435 1733 128 -121 171 C
ATOM 720 CG HIS A 505 0.564 -25.883 -2.388 1.00 19.43 C
ANISOU 720 CG HIS A 505 3123 2000 2259 201 -80 253 C
ATOM 721 ND1 HIS A 505 -0.090 -26.342 -1.244 1.00 22.35 N
ANISOU 721 ND1 HIS A 505 3487 2371 2634 358 73 428 N
ATOM 722 CD2 HIS A 505 1.639 -26.673 -2.620 1.00 20.59 C
ANISOU 722 CD2 HIS A 505 3245 2178 2402 157 -155 207 C
ATOM 723 CE1 HIS A 505 0.599 -27.397 -0.832 1.00 22.22 C
ANISOU 723 CE1 HIS A 505 3437 2378 2628 409 103 490 C
ATOM 724 NE2 HIS A 505 1.658 -27.627 -1.615 1.00 21.35 N
ANISOU 724 NE2 HIS A 505 3324 2288 2502 280 -43 346 N
ATOM 725 N GLU A 506 -2.891 -23.425 -4.200 1.00 15.98 N
ANISOU 725 N GLU A 506 2665 1425 1982 125 -9 184 N
ATOM 726 CA GLU A 506 -3.609 -22.294 -4.754 1.00 17.02 C
ANISOU 726 CA GLU A 506 2846 1561 2062 112 -3 124 C
ATOM 727 C GLU A 506 -3.081 -21.032 -4.064 1.00 20.21 C
ANISOU 727 C GLU A 506 3391 2018 2270 122 -27 98 C
ATOM 728 O GLU A 506 -2.834 -21.033 -2.850 1.00 20.82 O
ANISOU 728 O GLU A 506 3528 2135 2247 203 -16 144 O
ATOM 729 CB GLU A 506 -5.136 -22.455 -4.572 1.00 19.24 C
ANISOU 729 CB GLU A 506 3083 1779 2450 162 97 190 C
ATOM 730 CG GLU A 506 -5.810 -23.286 -5.669 1.00 30.09 C
ANISOU 730 CG GLU A 506 4282 3080 4072 158 81 112 C
ATOM 731 CD GLU A 506 -6.592 -22.506 -6.725 1.00 62.20 C
ANISOU 731 CD GLU A 506 8345 7172 8115 180 65 -18 C
ATOM 732 OE1 GLU A 506 -7.836 -22.664 -6.764 1.00 51.56 O
ANISOU 732 OE1 GLU A 506 6932 5758 6901 220 125 -32 O
ATOM 733 OE2 GLU A 506 -5.973 -21.740 -7.509 1.00 45.16 O
ANISOU 733 OE2 GLU A 506 6241 5101 5816 177 10 -97 O
ATOM 734 N VAL A 507 -2.875 -19.970 -4.842 1.00 13.94 N
ANISOU 734 N VAL A 507 2627 1227 1443 73 -60 18 N
ATOM 735 CA VAL A 507 -2.329 -18.706 -4.328 1.00 13.85 C
ANISOU 735 CA VAL A 507 2700 1221 1342 73 -97 -39 C
ATOM 736 C VAL A 507 -3.257 -17.554 -4.675 1.00 16.57 C
ANISOU 736 C VAL A 507 3089 1546 1661 75 -51 -49 C
ATOM 737 O VAL A 507 -3.799 -17.539 -5.770 1.00 13.47 O
ANISOU 737 O VAL A 507 2656 1150 1310 63 -3 -44 O
ATOM 738 CB VAL A 507 -0.912 -18.478 -4.953 1.00 18.60 C
ANISOU 738 CB VAL A 507 3260 1807 2000 5 -162 -103 C
ATOM 739 CG1 VAL A 507 -0.394 -17.070 -4.703 1.00 19.37 C
ANISOU 739 CG1 VAL A 507 3383 1851 2123 -8 -194 -179 C
ATOM 740 CG2 VAL A 507 0.097 -19.508 -4.452 1.00 18.66 C
ANISOU 740 CG2 VAL A 507 3248 1847 1997 6 -223 -116 C
ATOM 741 N THR A 508 -3.423 -16.590 -3.752 1.00 14.74 N
ANISOU 741 N THR A 508 2932 1318 1351 120 -78 -83 N
ATOM 742 CA THR A 508 -4.170 -15.350 -3.953 1.00 15.33 C
ANISOU 742 CA THR A 508 3057 1371 1399 119 -52 -106 C
ATOM 743 C THR A 508 -3.228 -14.213 -3.583 1.00 21.62 C
ANISOU 743 C THR A 508 3845 2111 2259 110 -136 -213 C
ATOM 744 O THR A 508 -2.731 -14.179 -2.457 1.00 23.68 O
ANISOU 744 O THR A 508 4114 2401 2481 189 -236 -294 O
ATOM 745 CB THR A 508 -5.483 -15.301 -3.117 1.00 18.63 C
ANISOU 745 CB THR A 508 3548 1841 1688 207 -23 -56 C
ATOM 746 OG1 THR A 508 -6.309 -16.370 -3.548 1.00 20.71 O
ANISOU 746 OG1 THR A 508 3772 2108 1988 205 62 29 O
ATOM 747 CG2 THR A 508 -6.251 -14.004 -3.315 1.00 18.35 C
ANISOU 747 CG2 THR A 508 3576 1794 1604 202 -9 -92 C
ATOM 748 N CYS A 509 -2.981 -13.303 -4.507 1.00 17.59 N
ANISOU 748 N CYS A 509 3294 1520 1870 48 -91 -218 N
ATOM 749 CA CYS A 509 -2.130 -12.140 -4.244 1.00 20.61 C
ANISOU 749 CA CYS A 509 3619 1792 2420 30 -156 -318 C
ATOM 750 C CYS A 509 -2.987 -10.914 -4.406 1.00 20.51 C
ANISOU 750 C CYS A 509 3637 1734 2424 37 -110 -316 C
ATOM 751 O CYS A 509 -3.415 -10.593 -5.533 1.00 16.80 O
ANISOU 751 O CYS A 509 3160 1246 1976 13 29 -212 O
ATOM 752 CB CYS A 509 -0.914 -12.089 -5.175 1.00 23.64 C
ANISOU 752 CB CYS A 509 3889 2084 3010 -41 -113 -285 C
ATOM 753 SG CYS A 509 0.212 -13.511 -5.033 1.00 29.15 S
ANISOU 753 SG CYS A 509 4555 2840 3681 -59 -184 -303 S
ATOM 754 N GLU A 510 -3.222 -10.219 -3.284 1.00 16.42 N
ANISOU 754 N GLU A 510 3144 1215 1880 105 -234 -442 N
ATOM 755 CA GLU A 510 -3.965 -8.961 -3.266 1.00 15.32 C
ANISOU 755 CA GLU A 510 3027 1026 1768 116 -230 -472 C
ATOM 756 C GLU A 510 -3.073 -7.881 -3.834 1.00 18.98 C
ANISOU 756 C GLU A 510 3348 1290 2575 50 -201 -505 C
ATOM 757 O GLU A 510 -1.864 -7.868 -3.584 1.00 19.45 O
ANISOU 757 O GLU A 510 3285 1249 2857 34 -281 -602 O
ATOM 758 CB GLU A 510 -4.423 -8.598 -1.849 1.00 16.64 C
ANISOU 758 CB GLU A 510 3243 1279 1800 251 -404 -613 C
ATOM 759 CG GLU A 510 -5.483 -9.527 -1.280 1.00 23.09 C
ANISOU 759 CG GLU A 510 4188 2282 2304 345 -384 -517 C
ATOM 760 CD GLU A 510 -6.825 -9.550 -1.982 1.00 33.63 C
ANISOU 760 CD GLU A 510 5620 3657 3500 298 -240 -381 C
ATOM 761 OE1 GLU A 510 -7.252 -8.510 -2.537 1.00 32.63 O
ANISOU 761 OE1 GLU A 510 5509 3468 3422 250 -197 -393 O
ATOM 762 OE2 GLU A 510 -7.446 -10.633 -1.993 1.00 33.29 O
ANISOU 762 OE2 GLU A 510 5624 3700 3325 318 -163 -268 O
ATOM 763 N LEU A 511 -3.667 -6.982 -4.599 1.00 14.70 N
ANISOU 763 N LEU A 511 2920 809 1857 113 660 65 N
ATOM 764 CA LEU A 511 -2.970 -5.879 -5.249 1.00 15.50 C
ANISOU 764 CA LEU A 511 3141 753 1995 87 650 133 C
ATOM 765 C LEU A 511 -3.540 -4.566 -4.749 1.00 20.27 C
ANISOU 765 C LEU A 511 3821 1212 2670 174 625 70 C
ATOM 766 O LEU A 511 -4.473 -4.573 -3.943 1.00 20.99 O
ANISOU 766 O LEU A 511 3862 1350 2762 266 624 -31 O
ATOM 767 CB LEU A 511 -3.193 -5.971 -6.770 1.00 16.14 C
ANISOU 767 CB LEU A 511 3270 833 2031 149 628 255 C
ATOM 768 CG LEU A 511 -2.934 -7.341 -7.427 1.00 20.48 C
ANISOU 768 CG LEU A 511 3749 1534 2497 120 625 294 C
ATOM 769 CD1 LEU A 511 -3.286 -7.296 -8.868 1.00 21.19 C
ANISOU 769 CD1 LEU A 511 3923 1616 2512 232 579 387 C
ATOM 770 CD2 LEU A 511 -1.467 -7.756 -7.285 1.00 24.06 C
ANISOU 770 CD2 LEU A 511 4188 2010 2942 -32 693 325 C
ATOM 771 N ASN A 512 -3.049 -3.437 -5.291 1.00 17.89 N
ANISOU 771 N ASN A 512 3641 723 2434 157 618 138 N
ATOM 772 CA ASN A 512 -3.565 -2.100 -4.962 1.00 18.74 C
ANISOU 772 CA ASN A 512 3844 651 2626 251 576 84 C
ATOM 773 C ASN A 512 -5.061 -2.076 -5.277 1.00 23.09 C
ANISOU 773 C ASN A 512 4371 1253 3149 443 529 61 C
ATOM 774 O ASN A 512 -5.849 -1.543 -4.500 1.00 21.85 O
ANISOU 774 O ASN A 512 4203 1064 3033 553 506 -57 O
ATOM 775 CB ASN A 512 -2.824 -1.025 -5.786 1.00 19.57 C
ANISOU 775 CB ASN A 512 4090 528 2817 196 590 212 C
ATOM 776 CG ASN A 512 -3.120 0.386 -5.381 1.00 43.75 C
ANISOU 776 CG ASN A 512 7264 3359 6000 263 538 152 C
ATOM 777 OD1 ASN A 512 -3.590 1.198 -6.181 1.00 42.52 O
ANISOU 777 OD1 ASN A 512 7235 3052 5868 364 515 250 O
ATOM 778 ND2 ASN A 512 -2.768 0.734 -4.156 1.00 37.81 N
ANISOU 778 ND2 ASN A 512 6489 2554 5322 217 504 -9 N
ATOM 779 N HIS A 513 -5.445 -2.697 -6.413 1.00 21.71 N
ANISOU 779 N HIS A 513 4178 1162 2909 496 504 158 N
ATOM 780 CA HIS A 513 -6.831 -2.870 -6.831 1.00 22.47 C
ANISOU 780 CA HIS A 513 4211 1324 3004 675 426 122 C
ATOM 781 C HIS A 513 -6.984 -4.324 -7.231 1.00 22.06 C
ANISOU 781 C HIS A 513 4024 1464 2893 642 419 131 C
ATOM 782 O HIS A 513 -6.235 -4.827 -8.075 1.00 20.52 O
ANISOU 782 O HIS A 513 3883 1299 2616 577 424 233 O
ATOM 783 CB HIS A 513 -7.203 -1.924 -7.990 1.00 26.20 C
ANISOU 783 CB HIS A 513 4846 1644 3464 822 338 220 C
ATOM 784 CG HIS A 513 -7.177 -0.477 -7.613 1.00 32.97 C
ANISOU 784 CG HIS A 513 5840 2280 4408 871 329 206 C
ATOM 785 ND1 HIS A 513 -8.228 0.110 -6.923 1.00 36.49 N
ANISOU 785 ND1 HIS A 513 6235 2694 4935 1023 274 68 N
ATOM 786 CD2 HIS A 513 -6.226 0.461 -7.847 1.00 36.44 C
ANISOU 786 CD2 HIS A 513 6453 2510 4884 790 370 311 C
ATOM 787 CE1 HIS A 513 -7.878 1.375 -6.753 1.00 37.46 C
ANISOU 787 CE1 HIS A 513 6519 2586 5127 1037 263 81 C
ATOM 788 NE2 HIS A 513 -6.673 1.624 -7.282 1.00 37.93 N
ANISOU 788 NE2 HIS A 513 6713 2523 5178 887 320 229 N
ATOM 789 N GLY A 514 -7.924 -5.003 -6.601 1.00 17.30 N
ANISOU 789 N GLY A 514 3243 983 2346 684 421 25 N
ATOM 790 CA GLY A 514 -8.178 -6.414 -6.881 1.00 16.64 C
ANISOU 790 CA GLY A 514 3012 1054 2257 646 406 18 C
ATOM 791 C GLY A 514 -7.103 -7.403 -6.467 1.00 18.15 C
ANISOU 791 C GLY A 514 3181 1331 2385 470 490 50 C
ATOM 792 O GLY A 514 -6.329 -7.179 -5.522 1.00 14.90 O
ANISOU 792 O GLY A 514 2811 898 1951 374 574 35 O
ATOM 793 N ARG A 515 -7.066 -8.532 -7.184 1.00 14.61 N
ANISOU 793 N ARG A 515 2667 975 1911 446 442 74 N
ATOM 794 CA ARG A 515 -6.160 -9.617 -6.851 1.00 13.53 C
ANISOU 794 CA ARG A 515 2494 921 1727 303 502 94 C
ATOM 795 C ARG A 515 -5.877 -10.487 -8.051 1.00 14.77 C
ANISOU 795 C ARG A 515 2657 1131 1822 312 420 135 C
ATOM 796 O ARG A 515 -6.635 -10.486 -9.016 1.00 15.33 O
ANISOU 796 O ARG A 515 2726 1199 1900 439 301 123 O
ATOM 797 CB ARG A 515 -6.775 -10.503 -5.715 1.00 12.73 C
ANISOU 797 CB ARG A 515 2232 902 1704 261 574 27 C
ATOM 798 CG ARG A 515 -8.097 -11.229 -6.098 1.00 18.26 C
ANISOU 798 CG ARG A 515 2752 1647 2538 332 511 -25 C
ATOM 799 CD ARG A 515 -9.030 -11.475 -4.918 1.00 21.85 C
ANISOU 799 CD ARG A 515 3052 2136 3114 331 633 -79 C
ATOM 800 NE ARG A 515 -9.160 -10.261 -4.113 1.00 27.89 N
ANISOU 800 NE ARG A 515 3893 2854 3848 393 712 -108 N
ATOM 801 CZ ARG A 515 -10.010 -9.267 -4.347 1.00 37.96 C
ANISOU 801 CZ ARG A 515 5152 4076 5196 530 665 -161 C
ATOM 802 NH1 ARG A 515 -10.912 -9.367 -5.316 1.00 27.75 N
ANISOU 802 NH1 ARG A 515 3747 2777 4020 627 535 -195 N
ATOM 803 NH2 ARG A 515 -9.986 -8.182 -3.596 1.00 27.64 N
ANISOU 803 NH2 ARG A 515 3939 2712 3851 586 727 -197 N
ATOM 804 N VAL A 516 -4.786 -11.227 -7.977 1.00 10.97 N
ANISOU 804 N VAL A 516 2189 701 1278 199 468 169 N
ATOM 805 CA VAL A 516 -4.416 -12.241 -8.970 1.00 10.28 C
ANISOU 805 CA VAL A 516 2102 679 1124 208 402 187 C
ATOM 806 C VAL A 516 -4.432 -13.589 -8.241 1.00 14.24 C
ANISOU 806 C VAL A 516 2468 1254 1688 119 416 136 C
ATOM 807 O VAL A 516 -4.037 -13.685 -7.079 1.00 11.65 O
ANISOU 807 O VAL A 516 2116 932 1378 26 509 131 O
ATOM 808 CB VAL A 516 -3.088 -11.937 -9.735 1.00 15.34 C
ANISOU 808 CB VAL A 516 2882 1308 1638 180 455 281 C
ATOM 809 CG1 VAL A 516 -1.898 -11.835 -8.776 1.00 15.00 C
ANISOU 809 CG1 VAL A 516 2830 1255 1615 29 568 295 C
ATOM 810 CG2 VAL A 516 -2.810 -12.967 -10.842 1.00 15.43 C
ANISOU 810 CG2 VAL A 516 2909 1399 1553 234 387 283 C
ATOM 811 N LYS A 517 -4.929 -14.639 -8.913 1.00 12.69 N
ANISOU 811 N LYS A 517 2195 1098 1527 162 309 92 N
ATOM 812 CA LYS A 517 -4.987 -15.970 -8.305 1.00 11.29 C
ANISOU 812 CA LYS A 517 1898 958 1435 77 319 56 C
ATOM 813 C LYS A 517 -4.413 -16.916 -9.287 1.00 14.22 C
ANISOU 813 C LYS A 517 2299 1366 1740 100 222 41 C
ATOM 814 O LYS A 517 -4.557 -16.711 -10.500 1.00 11.91 O
ANISOU 814 O LYS A 517 2075 1078 1372 220 112 25 O
ATOM 815 CB LYS A 517 -6.441 -16.382 -8.031 1.00 14.21 C
ANISOU 815 CB LYS A 517 2093 1308 1999 102 278 -10 C
ATOM 816 CG LYS A 517 -7.112 -15.611 -6.919 1.00 20.22 C
ANISOU 816 CG LYS A 517 2801 2048 2835 91 405 -6 C
ATOM 817 CD LYS A 517 -8.611 -15.896 -6.849 1.00 24.80 C
ANISOU 817 CD LYS A 517 3175 2609 3639 132 377 -74 C
ATOM 818 CE LYS A 517 -9.132 -15.577 -5.458 1.00 30.97 C
ANISOU 818 CE LYS A 517 3884 3392 4491 93 573 -56 C
ATOM 819 NZ LYS A 517 -10.619 -15.555 -5.400 1.00 36.82 N
ANISOU 819 NZ LYS A 517 4404 4114 5470 150 577 -124 N
ATOM 820 N PHE A 518 -3.773 -17.975 -8.780 1.00 11.48 N
ANISOU 820 N PHE A 518 1917 1041 1404 8 253 41 N
ATOM 821 CA PHE A 518 -3.221 -19.013 -9.641 1.00 11.39 C
ANISOU 821 CA PHE A 518 1925 1061 1341 39 157 6 C
ATOM 822 C PHE A 518 -2.989 -20.263 -8.820 1.00 13.41 C
ANISOU 822 C PHE A 518 2106 1305 1685 -59 176 -6 C
ATOM 823 O PHE A 518 -3.152 -20.236 -7.606 1.00 11.27 O
ANISOU 823 O PHE A 518 1795 1011 1475 -143 282 33 O
ATOM 824 CB PHE A 518 -1.931 -18.544 -10.337 1.00 14.18 C
ANISOU 824 CB PHE A 518 2416 1462 1511 70 203 56 C
ATOM 825 CG PHE A 518 -0.793 -18.175 -9.430 1.00 15.75 C
ANISOU 825 CG PHE A 518 2638 1670 1677 -39 341 113 C
ATOM 826 CD1 PHE A 518 -0.663 -16.878 -8.943 1.00 19.00 C
ANISOU 826 CD1 PHE A 518 3094 2045 2081 -73 433 164 C
ATOM 827 CD2 PHE A 518 0.162 -19.119 -9.069 1.00 17.24 C
ANISOU 827 CD2 PHE A 518 2804 1892 1855 -95 351 98 C
ATOM 828 CE1 PHE A 518 0.407 -16.532 -8.104 1.00 19.68 C
ANISOU 828 CE1 PHE A 518 3189 2125 2162 -167 521 184 C
ATOM 829 CE2 PHE A 518 1.234 -18.771 -8.233 1.00 19.36 C
ANISOU 829 CE2 PHE A 518 3082 2167 2108 -178 439 125 C
ATOM 830 CZ PHE A 518 1.345 -17.480 -7.754 1.00 17.67 C
ANISOU 830 CZ PHE A 518 2901 1915 1899 -217 517 161 C
ATOM 831 N SER A 519 -2.588 -21.331 -9.484 1.00 11.65 N
ANISOU 831 N SER A 519 1885 1091 1451 -29 74 -56 N
ATOM 832 CA SER A 519 -2.256 -22.624 -8.870 1.00 12.57 C
ANISOU 832 CA SER A 519 1957 1175 1645 -103 67 -65 C
ATOM 833 C SER A 519 -0.864 -23.005 -9.284 1.00 14.90 C
ANISOU 833 C SER A 519 2337 1527 1795 -75 59 -71 C
ATOM 834 O SER A 519 -0.355 -22.535 -10.293 1.00 14.30 O
ANISOU 834 O SER A 519 2335 1512 1585 13 41 -84 O
ATOM 835 CB SER A 519 -3.182 -23.712 -9.416 1.00 13.23 C
ANISOU 835 CB SER A 519 1939 1186 1901 -77 -88 -156 C
ATOM 836 OG SER A 519 -4.513 -23.459 -9.018 1.00 26.91 O
ANISOU 836 OG SER A 519 3543 2861 3820 -109 -75 -161 O
ATOM 837 N TYR A 520 -0.264 -23.878 -8.533 1.00 13.58 N
ANISOU 837 N TYR A 520 2165 1339 1657 -135 77 -59 N
ATOM 838 CA TYR A 520 0.967 -24.487 -8.976 1.00 13.45 C
ANISOU 838 CA TYR A 520 2195 1369 1545 -90 41 -93 C
ATOM 839 C TYR A 520 0.968 -25.945 -8.506 1.00 17.35 C
ANISOU 839 C TYR A 520 2661 1782 2148 -118 -35 -120 C
ATOM 840 O TYR A 520 0.296 -26.284 -7.526 1.00 18.25 O
ANISOU 840 O TYR A 520 2739 1812 2382 -200 4 -68 O
ATOM 841 CB TYR A 520 2.233 -23.669 -8.616 1.00 14.48 C
ANISOU 841 CB TYR A 520 2369 1573 1560 -115 154 -46 C
ATOM 842 CG TYR A 520 2.595 -23.704 -7.151 1.00 15.77 C
ANISOU 842 CG TYR A 520 2532 1709 1751 -200 212 -2 C
ATOM 843 CD1 TYR A 520 3.281 -24.788 -6.610 1.00 17.46 C
ANISOU 843 CD1 TYR A 520 2754 1902 1978 -201 162 -19 C
ATOM 844 CD2 TYR A 520 2.259 -22.653 -6.302 1.00 15.96 C
ANISOU 844 CD2 TYR A 520 2570 1723 1772 -254 302 48 C
ATOM 845 CE1 TYR A 520 3.572 -24.851 -5.253 1.00 16.99 C
ANISOU 845 CE1 TYR A 520 2731 1815 1911 -245 195 23 C
ATOM 846 CE2 TYR A 520 2.583 -22.687 -4.943 1.00 16.87 C
ANISOU 846 CE2 TYR A 520 2718 1818 1874 -297 338 75 C
ATOM 847 CZ TYR A 520 3.203 -23.810 -4.418 1.00 23.64 C
ANISOU 847 CZ TYR A 520 3599 2657 2728 -288 283 67 C
ATOM 848 OH TYR A 520 3.549 -23.891 -3.090 1.00 24.00 O
ANISOU 848 OH TYR A 520 3712 2684 2725 -296 299 93 O
ATOM 849 N HIS A 521 1.663 -26.806 -9.248 1.00 12.33 N
ANISOU 849 N HIS A 521 2050 1162 1474 -38 -133 -198 N
ATOM 850 CA HIS A 521 1.885 -28.201 -8.937 1.00 11.98 C
ANISOU 850 CA HIS A 521 2001 1028 1522 -42 -223 -233 C
ATOM 851 C HIS A 521 3.414 -28.359 -8.942 1.00 15.02 C
ANISOU 851 C HIS A 521 2429 1496 1781 13 -204 -252 C
ATOM 852 O HIS A 521 4.068 -27.994 -9.927 1.00 11.48 O
ANISOU 852 O HIS A 521 1997 1153 1212 105 -195 -304 O
ATOM 853 CB HIS A 521 1.250 -29.118 -9.996 1.00 15.03 C
ANISOU 853 CB HIS A 521 2363 1345 2002 38 -401 -356 C
ATOM 854 CG HIS A 521 -0.260 -29.166 -9.938 1.00 19.52 C
ANISOU 854 CG HIS A 521 2841 1805 2769 -24 -451 -362 C
ATOM 855 ND1 HIS A 521 -1.034 -28.144 -10.456 1.00 21.66 N
ANISOU 855 ND1 HIS A 521 3083 2129 3018 5 -447 -373 N
ATOM 856 CD2 HIS A 521 -1.075 -30.091 -9.388 1.00 22.60 C
ANISOU 856 CD2 HIS A 521 3153 2033 3403 -114 -492 -352 C
ATOM 857 CE1 HIS A 521 -2.290 -28.500 -10.250 1.00 22.44 C
ANISOU 857 CE1 HIS A 521 3063 2108 3355 -59 -503 -394 C
ATOM 858 NE2 HIS A 521 -2.366 -29.667 -9.614 1.00 23.68 N
ANISOU 858 NE2 HIS A 521 3179 2129 3690 -143 -518 -377 N
ATOM 859 N ALA A 522 3.984 -28.824 -7.815 1.00 12.63 N
ANISOU 859 N ALA A 522 2146 1151 1501 -33 -183 -203 N
ATOM 860 CA ALA A 522 5.406 -29.113 -7.697 1.00 12.39 C
ANISOU 860 CA ALA A 522 2129 1183 1396 26 -198 -241 C
ATOM 861 C ALA A 522 5.508 -30.569 -7.351 1.00 14.99 C
ANISOU 861 C ALA A 522 2492 1393 1810 59 -317 -268 C
ATOM 862 O ALA A 522 5.113 -30.989 -6.268 1.00 16.56 O
ANISOU 862 O ALA A 522 2736 1483 2073 -6 -308 -182 O
ATOM 863 CB ALA A 522 6.060 -28.234 -6.631 1.00 13.02 C
ANISOU 863 CB ALA A 522 2213 1313 1420 -32 -104 -178 C
ATOM 864 N LYS A 523 5.887 -31.381 -8.325 1.00 11.71 N
ANISOU 864 N LYS A 523 2073 979 1399 168 -426 -382 N
ATOM 865 CA LYS A 523 5.999 -32.816 -8.109 1.00 11.49 C
ANISOU 865 CA LYS A 523 2084 810 1470 212 -561 -422 C
ATOM 866 C LYS A 523 7.494 -33.157 -7.912 1.00 16.39 C
ANISOU 866 C LYS A 523 2711 1499 2017 312 -593 -476 C
ATOM 867 O LYS A 523 8.273 -33.018 -8.861 1.00 14.89 O
ANISOU 867 O LYS A 523 2476 1434 1747 420 -591 -579 O
ATOM 868 CB LYS A 523 5.389 -33.568 -9.310 1.00 16.54 C
ANISOU 868 CB LYS A 523 2717 1384 2182 289 -700 -549 C
ATOM 869 CG LYS A 523 5.474 -35.118 -9.250 1.00 23.17 C
ANISOU 869 CG LYS A 523 3599 2046 3159 344 -868 -617 C
ATOM 870 CD LYS A 523 4.494 -35.708 -8.251 1.00 25.52 C
ANISOU 870 CD LYS A 523 3913 2126 3655 204 -869 -497 C
ATOM 871 CE LYS A 523 4.496 -37.225 -8.252 1.00 33.11 C
ANISOU 871 CE LYS A 523 4924 2870 4787 246 -1034 -552 C
ATOM 872 NZ LYS A 523 5.817 -37.792 -7.863 1.00 34.93 N
ANISOU 872 NZ LYS A 523 5232 3118 4922 360 -1081 -569 N
ATOM 873 N CYS A 524 7.891 -33.630 -6.697 1.00 16.32 N
ANISOU 873 N CYS A 524 2760 1408 2034 295 -622 -407 N
ATOM 874 CA CYS A 524 9.274 -34.076 -6.437 1.00 17.51 C
ANISOU 874 CA CYS A 524 2907 1602 2145 410 -696 -476 C
ATOM 875 C CYS A 524 9.668 -35.114 -7.472 1.00 20.40 C
ANISOU 875 C CYS A 524 3260 1945 2547 552 -819 -621 C
ATOM 876 O CYS A 524 8.842 -35.949 -7.829 1.00 19.92 O
ANISOU 876 O CYS A 524 3250 1737 2581 551 -909 -641 O
ATOM 877 CB CYS A 524 9.419 -34.659 -5.039 1.00 19.52 C
ANISOU 877 CB CYS A 524 3273 1730 2414 406 -754 -382 C
ATOM 878 SG CYS A 524 9.115 -33.476 -3.707 1.00 23.30 S
ANISOU 878 SG CYS A 524 3800 2249 2802 294 -625 -240 S
ATOM 879 N LEU A 525 10.930 -35.093 -7.914 1.00 16.90 N
ANISOU 879 N LEU A 525 2740 1633 2048 677 -829 -733 N
ATOM 880 CA LEU A 525 11.430 -36.055 -8.885 1.00 17.99 C
ANISOU 880 CA LEU A 525 2868 1770 2197 845 -934 -889 C
ATOM 881 C LEU A 525 11.430 -37.437 -8.200 1.00 22.47 C
ANISOU 881 C LEU A 525 3541 2124 2871 901 -1118 -893 C
ATOM 882 O LEU A 525 11.426 -37.495 -6.961 1.00 20.60 O
ANISOU 882 O LEU A 525 3371 1798 2657 836 -1133 -774 O
ATOM 883 CB LEU A 525 12.861 -35.687 -9.334 1.00 18.58 C
ANISOU 883 CB LEU A 525 2812 2038 2209 966 -866 -993 C
ATOM 884 CG LEU A 525 13.083 -34.507 -10.294 1.00 22.38 C
ANISOU 884 CG LEU A 525 3194 2720 2591 954 -666 -1000 C
ATOM 885 CD1 LEU A 525 14.046 -34.852 -11.394 1.00 22.95 C
ANISOU 885 CD1 LEU A 525 3189 2921 2608 1145 -627 -1147 C
ATOM 886 CD2 LEU A 525 11.815 -33.860 -10.784 1.00 23.63 C
ANISOU 886 CD2 LEU A 525 3419 2864 2695 855 -598 -922 C
ATOM 887 N PRO A 526 11.375 -38.538 -8.976 1.00 20.84 N
ANISOU 887 N PRO A 526 3374 1820 2724 1027 -1259 -1022 N
ATOM 888 CA PRO A 526 11.332 -39.880 -8.362 1.00 22.33 C
ANISOU 888 CA PRO A 526 3677 1766 3039 1076 -1437 -1017 C
ATOM 889 C PRO A 526 12.355 -40.129 -7.267 1.00 29.65 C
ANISOU 889 C PRO A 526 4636 2680 3951 1142 -1488 -975 C
ATOM 890 O PRO A 526 13.526 -39.724 -7.391 1.00 29.45 O
ANISOU 890 O PRO A 526 4498 2838 3853 1248 -1465 -1066 O
ATOM 891 CB PRO A 526 11.572 -40.824 -9.553 1.00 24.92 C
ANISOU 891 CB PRO A 526 4008 2061 3399 1260 -1581 -1227 C
ATOM 892 CG PRO A 526 11.142 -40.086 -10.722 1.00 28.04 C
ANISOU 892 CG PRO A 526 4341 2615 3699 1263 -1490 -1301 C
ATOM 893 CD PRO A 526 11.333 -38.622 -10.457 1.00 22.70 C
ANISOU 893 CD PRO A 526 3575 2147 2902 1148 -1272 -1184 C
ATOM 894 N HIS A 527 11.896 -40.810 -6.198 1.00 29.87 N
ANISOU 894 N HIS A 527 4814 2481 4056 1088 -1559 -834 N
ATOM 895 CA HIS A 527 12.634 -41.187 -4.995 1.00 33.28 C
ANISOU 895 CA HIS A 527 5346 2842 4457 1164 -1642 -762 C
ATOM 896 C HIS A 527 12.877 -40.023 -4.021 1.00 35.58 C
ANISOU 896 C HIS A 527 5620 3279 4621 1085 -1527 -653 C
ATOM 897 O HIS A 527 13.615 -40.209 -3.055 1.00 37.06 O
ANISOU 897 O HIS A 527 5887 3440 4753 1180 -1620 -622 O
ATOM 898 CB HIS A 527 13.955 -41.928 -5.305 1.00 38.21 C
ANISOU 898 CB HIS A 527 5930 3496 5091 1401 -1811 -944 C
ATOM 899 CG HIS A 527 13.790 -43.100 -6.218 1.00 45.01 C
ANISOU 899 CG HIS A 527 6826 4207 6068 1509 -1948 -1077 C
ATOM 900 ND1 HIS A 527 14.496 -43.189 -7.406 1.00 48.48 N
ANISOU 900 ND1 HIS A 527 7133 4800 6486 1671 -1977 -1301 N
ATOM 901 CD2 HIS A 527 12.954 -44.161 -6.124 1.00 49.36 C
ANISOU 901 CD2 HIS A 527 7526 4465 6763 1472 -2048 -1019 C
ATOM 902 CE1 HIS A 527 14.104 -44.320 -7.973 1.00 50.20 C
ANISOU 902 CE1 HIS A 527 7440 4818 6817 1750 -2126 -1394 C
ATOM 903 NE2 HIS A 527 13.175 -44.939 -7.241 1.00 51.03 N
ANISOU 903 NE2 HIS A 527 7705 4638 7046 1624 -2181 -1232 N
ATOM 904 N LEU A 528 12.243 -38.847 -4.242 1.00 27.63 N
ANISOU 904 N LEU A 528 4526 2407 3567 930 -1349 -602 N
ATOM 905 CA LEU A 528 12.382 -37.716 -3.327 1.00 25.48 C
ANISOU 905 CA LEU A 528 4247 2248 3186 854 -1251 -513 C
ATOM 906 C LEU A 528 11.031 -37.442 -2.695 1.00 27.57 C
ANISOU 906 C LEU A 528 4627 2404 3445 689 -1122 -321 C
ATOM 907 O LEU A 528 10.001 -37.739 -3.294 1.00 26.55 O
ANISOU 907 O LEU A 528 4492 2180 3416 599 -1073 -290 O
ATOM 908 CB LEU A 528 12.923 -36.444 -4.034 1.00 24.84 C
ANISOU 908 CB LEU A 528 3961 2413 3063 822 -1139 -614 C
ATOM 909 CG LEU A 528 14.328 -36.523 -4.681 1.00 30.21 C
ANISOU 909 CG LEU A 528 4476 3236 3768 972 -1203 -800 C
ATOM 910 CD1 LEU A 528 14.579 -35.303 -5.577 1.00 28.57 C
ANISOU 910 CD1 LEU A 528 4078 3234 3543 906 -1027 -854 C
ATOM 911 CD2 LEU A 528 15.419 -36.649 -3.636 1.00 33.37 C
ANISOU 911 CD2 LEU A 528 4879 3638 4160 1085 -1346 -840 C
ATOM 912 N THR A 529 11.031 -36.893 -1.483 1.00 24.84 N
ANISOU 912 N THR A 529 4380 2069 2989 663 -1076 -207 N
ATOM 913 CA THR A 529 9.805 -36.566 -0.741 1.00 24.41 C
ANISOU 913 CA THR A 529 4437 1930 2907 527 -921 -18 C
ATOM 914 C THR A 529 10.041 -35.339 0.144 1.00 26.42 C
ANISOU 914 C THR A 529 4711 2324 3005 512 -851 13 C
ATOM 915 O THR A 529 11.168 -34.857 0.250 1.00 25.13 O
ANISOU 915 O THR A 529 4478 2288 2782 601 -949 -110 O
ATOM 916 CB THR A 529 9.296 -37.807 0.050 1.00 38.62 C
ANISOU 916 CB THR A 529 6452 3476 4746 550 -947 145 C
ATOM 917 OG1 THR A 529 7.990 -37.540 0.566 1.00 48.17 O
ANISOU 917 OG1 THR A 529 7724 4601 5976 401 -750 328 O
ATOM 918 CG2 THR A 529 10.212 -38.191 1.189 1.00 28.85 C
ANISOU 918 CG2 THR A 529 5401 2201 3359 714 -1072 185 C
ATOM 919 N GLY A 530 8.995 -34.917 0.838 1.00 23.73 N
ANISOU 919 N GLY A 530 4466 1937 2612 412 -692 169 N
ATOM 920 CA GLY A 530 9.029 -33.766 1.724 1.00 23.72 C
ANISOU 920 CA GLY A 530 4512 2045 2455 405 -622 197 C
ATOM 921 C GLY A 530 8.639 -32.519 0.973 1.00 24.90 C
ANISOU 921 C GLY A 530 4479 2335 2648 283 -505 133 C
ATOM 922 O GLY A 530 8.645 -32.509 -0.266 1.00 23.75 O
ANISOU 922 O GLY A 530 4170 2233 2620 240 -508 43 O
ATOM 923 N GLY A 531 8.347 -31.458 1.720 1.00 19.72 N
ANISOU 923 N GLY A 531 3868 1744 1881 252 -412 172 N
ATOM 924 CA GLY A 531 7.940 -30.178 1.156 1.00 16.53 C
ANISOU 924 CA GLY A 531 3320 1450 1509 146 -300 126 C
ATOM 925 C GLY A 531 8.892 -29.570 0.148 1.00 20.59 C
ANISOU 925 C GLY A 531 3644 2089 2092 143 -366 -32 C
ATOM 926 O GLY A 531 8.449 -28.929 -0.809 1.00 18.65 O
ANISOU 926 O GLY A 531 3276 1896 1914 59 -273 -51 O
ATOM 927 N THR A 532 10.203 -29.757 0.345 1.00 17.52 N
ANISOU 927 N THR A 532 3225 1742 1691 243 -518 -141 N
ATOM 928 CA THR A 532 11.188 -29.215 -0.586 1.00 17.79 C
ANISOU 928 CA THR A 532 3053 1890 1816 238 -545 -281 C
ATOM 929 C THR A 532 11.999 -30.309 -1.300 1.00 21.23 C
ANISOU 929 C THR A 532 3416 2324 2325 336 -652 -365 C
ATOM 930 O THR A 532 13.098 -30.050 -1.802 1.00 19.80 O
ANISOU 930 O THR A 532 3071 2237 2216 375 -693 -490 O
ATOM 931 CB THR A 532 12.084 -28.191 0.103 1.00 23.05 C
ANISOU 931 CB THR A 532 3665 2624 2470 254 -612 -375 C
ATOM 932 OG1 THR A 532 12.639 -28.811 1.252 1.00 24.25 O
ANISOU 932 OG1 THR A 532 3951 2728 2536 387 -786 -398 O
ATOM 933 CG2 THR A 532 11.342 -26.930 0.485 1.00 19.03 C
ANISOU 933 CG2 THR A 532 3191 2126 1913 157 -497 -327 C
ATOM 934 N CYS A 533 11.479 -31.540 -1.307 1.00 18.71 N
ANISOU 934 N CYS A 533 3215 1888 2006 379 -695 -300 N
ATOM 935 CA CYS A 533 12.063 -32.660 -2.047 1.00 18.59 C
ANISOU 935 CA CYS A 533 3155 1846 2063 481 -799 -384 C
ATOM 936 C CYS A 533 13.527 -33.030 -1.618 1.00 21.67 C
ANISOU 936 C CYS A 533 3499 2272 2462 632 -975 -508 C
ATOM 937 O CYS A 533 14.290 -33.557 -2.412 1.00 20.08 O
ANISOU 937 O CYS A 533 3179 2113 2336 721 -1034 -625 O
ATOM 938 CB CYS A 533 11.952 -32.373 -3.546 1.00 18.94 C
ANISOU 938 CB CYS A 533 3046 1981 2170 443 -704 -453 C
ATOM 939 SG CYS A 533 10.297 -31.822 -4.067 1.00 22.29 S
ANISOU 939 SG CYS A 533 3503 2372 2595 294 -546 -342 S
ATOM 940 N LEU A 534 13.896 -32.786 -0.358 1.00 21.34 N
ANISOU 940 N LEU A 534 3555 2213 2341 683 -1070 -493 N
ATOM 941 CA LEU A 534 15.252 -33.093 0.113 1.00 23.52 C
ANISOU 941 CA LEU A 534 3778 2520 2639 841 -1274 -629 C
ATOM 942 C LEU A 534 15.379 -34.473 0.744 1.00 29.40 C
ANISOU 942 C LEU A 534 4725 3116 3330 1001 -1446 -587 C
ATOM 943 O LEU A 534 16.499 -34.924 0.976 1.00 32.80 O
ANISOU 943 O LEU A 534 5107 3560 3795 1162 -1641 -714 O
ATOM 944 CB LEU A 534 15.745 -32.033 1.122 1.00 24.64 C
ANISOU 944 CB LEU A 534 3908 2724 2731 846 -1343 -683 C
ATOM 945 CG LEU A 534 15.864 -30.595 0.637 1.00 28.49 C
ANISOU 945 CG LEU A 534 4186 3332 3305 701 -1209 -744 C
ATOM 946 CD1 LEU A 534 16.041 -29.671 1.810 1.00 29.42 C
ANISOU 946 CD1 LEU A 534 4366 3457 3354 707 -1296 -779 C
ATOM 947 CD2 LEU A 534 17.004 -30.436 -0.388 1.00 31.02 C
ANISOU 947 CD2 LEU A 534 4206 3764 3817 713 -1203 -902 C
ATOM 948 N GLU A 535 14.253 -35.103 1.096 1.00 25.02 N
ANISOU 948 N GLU A 535 4393 2408 2706 959 -1376 -406 N
ATOM 949 CA GLU A 535 14.215 -36.397 1.789 1.00 30.91 C
ANISOU 949 CA GLU A 535 5377 2969 3398 1092 -1505 -313 C
ATOM 950 C GLU A 535 14.275 -37.555 0.806 1.00 46.48 C
ANISOU 950 C GLU A 535 7301 4848 5513 1136 -1558 -363 C
ATOM 951 O GLU A 535 13.663 -37.472 -0.254 1.00 26.45 O
ANISOU 951 O GLU A 535 4645 2331 3073 1017 -1432 -376 O
ATOM 952 CB GLU A 535 12.967 -36.465 2.700 1.00 32.40 C
ANISOU 952 CB GLU A 535 5821 3023 3466 1014 -1363 -75 C
ATOM 953 CG GLU A 535 12.904 -37.669 3.633 1.00 54.62 C
ANISOU 953 CG GLU A 535 8931 5629 6195 1150 -1459 71 C
ATOM 954 CD GLU A 535 11.880 -37.589 4.755 1.00 90.62 C
ANISOU 954 CD GLU A 535 13757 10083 10592 1108 -1295 315 C
ATOM 955 OE1 GLU A 535 10.668 -37.472 4.456 1.00 95.26 O
ANISOU 955 OE1 GLU A 535 14319 10618 11257 926 -1067 444 O
ATOM 956 OE2 GLU A 535 12.289 -37.673 5.936 1.00 86.66 O
ANISOU 956 OE2 GLU A 535 13494 9549 9883 1274 -1395 374 O
TER 957 GLU A 535
HETATM 958 I IOD A 601 5.125 -30.037 -19.696 1.00 19.28 I
HETATM 959 O HOH A 701 7.467 -30.566 -19.085 1.00 20.54 O
HETATM 960 O HOH A 702 -6.172 -0.856 -15.284 1.00 24.45 O
HETATM 961 O HOH A 703 -1.960 -15.663 -22.732 1.00 29.87 O
HETATM 962 O HOH A 704 14.426 -28.077 -2.864 1.00 20.75 O
HETATM 963 O HOH A 705 -3.872 -20.192 -16.812 1.00 29.70 O
HETATM 964 O HOH A 706 -8.190 -1.769 -24.042 1.00 28.30 O
HETATM 965 O HOH A 707 -0.476 -25.890 -11.942 1.00 18.57 O
HETATM 966 O HOH A 708 2.254 -1.496 -23.390 1.00 32.98 O
HETATM 967 O HOH A 709 -7.116 -7.486 -18.594 1.00 18.43 O
HETATM 968 O HOH A 710 -3.328 -2.438 -8.679 1.00 25.88 O
HETATM 969 O HOH A 711 8.161 -38.016 -9.390 1.00 57.58 O
HETATM 970 O HOH A 712 -6.357 -0.520 -12.659 1.00 31.56 O
HETATM 971 O HOH A 713 -0.346 -3.481 -6.005 1.00 29.97 O
HETATM 972 O HOH A 714 -13.444 -12.472 -17.729 1.00 28.71 O
HETATM 973 O HOH A 715 -5.018 -3.812 -10.266 1.00 20.87 O
HETATM 974 O HOH A 716 10.490 -22.901 -1.883 1.00 22.08 O
HETATM 975 O HOH A 717 3.991 -29.899 0.787 1.00 30.02 O
HETATM 976 O HOH A 718 16.276 -40.805 -3.172 1.00 57.77 O
HETATM 977 O HOH A 719 8.969 -25.240 -20.481 1.00 53.00 O
HETATM 978 O HOH A 720 9.548 -7.041 -14.943 1.00 37.15 O
HETATM 979 O HOH A 721 -6.654 -5.849 -2.765 1.00 22.57 O
HETATM 980 O HOH A 722 -3.068 1.985 -16.668 1.00 16.17 O
HETATM 981 O HOH A 723 14.009 -26.994 2.802 1.00 23.82 O
HETATM 982 O HOH A 724 12.639 -8.944 -16.893 1.00 26.55 O
HETATM 983 O HOH A 725 -10.374 -9.506 -24.133 1.00 26.40 O
HETATM 984 O HOH A 726 -7.382 -19.591 -15.407 1.00 25.38 O
HETATM 985 O HOH A 727 -6.011 -19.235 -6.274 1.00 24.40 O
HETATM 986 O HOH A 728 6.766 -28.325 -21.242 1.00 22.17 O
HETATM 987 O HOH A 729 12.317 -11.795 -10.350 1.00 50.44 O
HETATM 988 O HOH A 730 13.628 -16.054 -10.942 1.00 25.48 O
HETATM 989 O HOH A 731 5.529 -17.910 0.558 1.00 43.15 O
HETATM 990 O HOH A 732 5.631 -23.826 -20.359 1.00 28.94 O
HETATM 991 O HOH A 733 -2.230 -11.072 -0.754 1.00 26.38 O
HETATM 992 O HOH A 734 6.791 -16.325 -21.968 1.00 22.16 O
HETATM 993 O HOH A 735 -11.236 -17.564 -8.949 1.00 28.93 O
HETATM 994 O HOH A 736 11.134 -24.173 -19.246 1.00 39.59 O
HETATM 995 O HOH A 737 -0.694 -10.591 -26.227 1.00 28.92 O
HETATM 996 O HOH A 738 16.037 -24.194 -9.990 1.00 27.45 O
HETATM 997 O HOH A 739 4.021 -20.957 -21.366 1.00 38.89 O
HETATM 998 O HOH A 740 -14.239 -5.693 -17.337 1.00 25.22 O
HETATM 999 O HOH A 741 -4.157 -24.489 -1.764 1.00 26.19 O
HETATM 1000 O HOH A 742 12.139 -31.649 1.959 1.00 15.31 O
HETATM 1001 O HOH A 743 -10.144 -13.318 -20.157 1.00 26.68 O
HETATM 1002 O HOH A 744 -7.197 -15.055 -22.538 1.00 63.46 O
HETATM 1003 O HOH A 745 4.342 -10.996 -1.641 1.00 31.21 O
HETATM 1004 O HOH A 746 -7.929 -9.875 -25.507 1.00 29.54 O
HETATM 1005 O HOH A 747 5.678 -34.288 -4.717 1.00 15.53 O
HETATM 1006 O HOH A 748 4.508 -12.738 0.458 1.00 37.13 O
HETATM 1007 O HOH A 749 1.644 -5.272 -5.067 1.00 19.83 O
HETATM 1008 O HOH A 750 8.609 -35.820 -10.936 1.00 36.75 O
HETATM 1009 O HOH A 751 -0.273 -21.806 -1.159 1.00 49.70 O
HETATM 1010 O HOH A 752 12.164 -18.758 -19.796 1.00 52.23 O
HETATM 1011 O HOH A 753 -0.017 -0.857 -4.359 1.00 34.88 O
HETATM 1012 O HOH A 754 -1.781 -17.156 -1.066 1.00 15.85 O
HETATM 1013 O HOH A 755 13.729 -20.895 -19.509 1.00 58.56 O
HETATM 1014 O HOH A 756 7.599 -15.700 -0.142 1.00 45.06 O
HETATM 1015 O HOH A 757 3.653 -18.318 -20.754 1.00 43.97 O
HETATM 1016 O HOH A 758 -3.028 0.165 -9.342 1.00 35.04 O
HETATM 1017 O HOH A 759 -3.859 -18.928 -0.336 1.00 47.91 O
HETATM 1018 O HOH A 760 22.399 -34.919 -4.712 1.00 59.82 O
HETATM 1019 O HOH A 761 -4.634 -16.093 -22.656 1.00 45.40 O
HETATM 1020 O HOH A 762 1.604 -14.465 2.037 1.00 51.85 O
HETATM 1021 O HOH A 763 -1.970 -21.362 -23.841 1.00 52.77 O
HETATM 1022 O HOH A 764 -6.070 1.824 -15.386 1.00 29.48 O
HETATM 1023 O HOH A 765 4.946 4.512 -16.773 1.00 13.24 O
HETATM 1024 O HOH A 766 7.760 2.323 -19.282 1.00 25.77 O
HETATM 1025 O HOH A 767 7.458 3.631 -17.021 1.00 45.73 O
HETATM 1026 O HOH A 768 -4.543 1.023 -11.435 1.00 30.90 O
HETATM 1027 O HOH A 769 -18.580 5.636 -17.505 1.00 36.79 O
HETATM 1028 O HOH A 770 -19.870 5.360 -15.166 1.00 38.71 O
CONECT 651 753
CONECT 753 651
CONECT 878 939
CONECT 939 878
MASTER 437 0 1 1 8 0 2 6 1027 1 4 12
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