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fpocket/data/sample/4bdf.pdb
pschmidtke 84967334d8 fixes on alternate locations in cif & output as cif
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HEADER TRANSFERASE 05-OCT-12 4BDF
TITLE FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
TITLE 2 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 210-531;
COMPND 5 SYNONYM: CHK2 CHECKPOINT HOMOLOG, CDS1 HOMOLOG, HUCDS1, HCDS1,
COMPND 6 CHECKPOINT KINASE 2;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTHREE-E
KEYWDS TRANSFERASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.C.SILVA-SANTISTEBAN,I.M.WESTWOOD,K.BOXALL,N.BROWN,S.PEACOCK,
AUTHOR 2 C.MCANDREW,E.BARRIE,M.RICHARDS,A.MIRZA,A.W.OLIVER,R.BURKE,S.HOELDER,
AUTHOR 3 K.JONES,G.W.AHERNE,J.BLAGG,I.COLLINS,M.D.GARRETT,R.L.M.VAN MONTFORT
REVDAT 1 26-JUN-13 4BDF 0
JRNL AUTH M.C.SILVA-SANTISTEBAN,I.M.WESTWOOD,K.BOXALL,N.BROWN,
JRNL AUTH 2 S.PEACOCK,C.MCANDREW,E.BARRIE,M.RICHARDS,A.MIRZA,A.W.OLIVER,
JRNL AUTH 3 R.BURKE,S.HOELDER,K.JONES,G.W.AHERNE,J.BLAGG,I.COLLINS,
JRNL AUTH 4 M.D.GARRETT,R.L.VAN MONTFORT
JRNL TITL FRAGMENT-BASED SCREENING MAPS INHIBITOR INTERACTIONS IN THE
JRNL TITL 2 ATP-BINDING SITE OF CHECKPOINT KINASE 2.
JRNL REF PLOS ONE V. 8 65689 2013
JRNL REFN ISSN 1932-6203
JRNL PMID 23776527
JRNL DOI 10.1371/JOURNAL.PONE.0065689
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,WOMACK;
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.50
REMARK 3 NUMBER OF REFLECTIONS : 12518
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1835
REMARK 3 R VALUE (WORKING SET) : 0.1810
REMARK 3 FREE R VALUE : 0.2334
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.86
REMARK 3 FREE R VALUE TEST SET COUNT : 608
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.96
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2942
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2144
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2794
REMARK 3 BIN R VALUE (WORKING SET) : 0.2118
REMARK 3 BIN FREE R VALUE : 0.2642
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.03
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2185
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.9153
REMARK 3 B22 (A**2) : 0.9153
REMARK 3 B33 (A**2) : -1.8306
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.365
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.399
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.265
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.393
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.267
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 : 0.9516
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9329
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2249 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 3047 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 757 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 48 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 336 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2249 ; 20.00 ; 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 : 302 ; 5.00 ; 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 : 2633 ; 4.00 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.42
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.81
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 210-301
REMARK 3 ORIGIN FOR THE GROUP (A): -39.4145 42.5794 12.2710
REMARK 3 T TENSOR
REMARK 3 T11: 0.3123 T22: 0.2481
REMARK 3 T33: 0.1396 T12: 0.0959
REMARK 3 T13: -0.0021 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 7.0578 L22: 2.0348
REMARK 3 L33: 0.0000 L12: -3.9969
REMARK 3 L13: -1.1058 L23: 0.6698
REMARK 3 S TENSOR
REMARK 3 S11: -0.6104 S12: -0.6790 S13: -0.0752
REMARK 3 S21: 0.5344 S22: 0.4034 S23: 0.0187
REMARK 3 S31: 0.3152 S32: -0.1791 S33: 0.2070
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 302-375
REMARK 3 ORIGIN FOR THE GROUP (A): -26.9905 28.4498 6.1579
REMARK 3 T TENSOR
REMARK 3 T11: 0.2235 T22: 0.1455
REMARK 3 T33: 0.1377 T12: 0.0117
REMARK 3 T13: -0.0029 T23: -0.0698
REMARK 3 L TENSOR
REMARK 3 L11: 3.5893 L22: 2.5946
REMARK 3 L33: 3.5405 L12: -0.5877
REMARK 3 L13: 0.4118 L23: 0.1940
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: 0.2984 S13: -0.1893
REMARK 3 S21: -0.5250 S22: -0.1927 S23: 0.3460
REMARK 3 S31: -0.1088 S32: -0.4004 S33: 0.2236
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESID 376-445
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5239 21.1278 22.4613
REMARK 3 T TENSOR
REMARK 3 T11: 0.2384 T22: 0.2078
REMARK 3 T33: 0.3976 T12: 0.0160
REMARK 3 T13: 0.1380 T23: 0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 1.3365 L22: 0.8051
REMARK 3 L33: 3.5981 L12: -1.3899
REMARK 3 L13: 0.7902 L23: -0.2914
REMARK 3 S TENSOR
REMARK 3 S11: -0.2727 S12: 0.0536 S13: -0.4006
REMARK 3 S21: -0.2414 S22: 0.2080 S23: 0.1111
REMARK 3 S31: 0.2219 S32: 0.2050 S33: 0.0647
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESID 446-512
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1894 24.6354 0.7700
REMARK 3 T TENSOR
REMARK 3 T11: 0.4814 T22: 0.2976
REMARK 3 T33: 0.0613 T12: -0.0266
REMARK 3 T13: 0.0668 T23: -0.1247
REMARK 3 L TENSOR
REMARK 3 L11: 4.4934 L22: 2.4473
REMARK 3 L33: 1.2535 L12: -0.7257
REMARK 3 L13: 0.3141 L23: 0.0747
REMARK 3 S TENSOR
REMARK 3 S11: 0.0560 S12: 0.7136 S13: -0.2760
REMARK 3 S21: -0.8886 S22: -0.3035 S23: -0.2523
REMARK 3 S31: 0.3716 S32: 0.5392 S33: 0.2475
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
REMARK 4
REMARK 4 4BDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-OCT-12.
REMARK 100 THE PDBE ID CODE IS EBI-54368.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97280
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12578
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.70
REMARK 200 RESOLUTION RANGE LOW (A) : 78.81
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.5
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.6
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2WTJ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES 7.5, 0.2 M MG(NO3)2,
REMARK 280 10% (V/V) ETHYLENE GLYCOL, 1 MM TCEP AND 8-14% (W/V) PEG
REMARK 280 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.02000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.01000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.01000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 62.02000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.5 KCAL/MOL
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 62.02000
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 203
REMARK 465 PRO A 204
REMARK 465 LEU A 205
REMARK 465 GLY A 206
REMARK 465 SER A 207
REMARK 465 HIS A 208
REMARK 465 SER A 228
REMARK 465 GLY A 229
REMARK 465 ALA A 230
REMARK 465 CYS A 231
REMARK 465 ARG A 254
REMARK 465 LYS A 255
REMARK 465 PHE A 256
REMARK 465 ALA A 257
REMARK 465 ILE A 258
REMARK 465 GLY A 259
REMARK 465 SER A 260
REMARK 465 ALA A 261
REMARK 465 ARG A 262
REMARK 465 GLU A 263
REMARK 465 ALA A 264
REMARK 465 ASP A 265
REMARK 465 PRO A 266
REMARK 465 ALA A 267
REMARK 465 LEU A 268
REMARK 465 ALA A 513
REMARK 465 GLN A 514
REMARK 465 PRO A 515
REMARK 465 SER A 516
REMARK 465 THR A 517
REMARK 465 SER A 518
REMARK 465 ARG A 519
REMARK 465 LYS A 520
REMARK 465 ARG A 521
REMARK 465 PRO A 522
REMARK 465 ARG A 523
REMARK 465 GLU A 524
REMARK 465 GLY A 525
REMARK 465 GLU A 526
REMARK 465 ALA A 527
REMARK 465 GLU A 528
REMARK 465 GLY A 529
REMARK 465 ALA A 530
REMARK 465 GLU A 531
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 MET A 209 CG SD CE
REMARK 470 LYS A 224 CG CD CE NZ
REMARK 470 GLU A 233 CG CD OE1 OE2
REMARK 470 LYS A 235 CE NZ
REMARK 470 LYS A 241 CD CE NZ
REMARK 470 LYS A 245 CE NZ
REMARK 470 LYS A 249 CD CE NZ
REMARK 470 SER A 252 OG
REMARK 470 GLU A 271 CG CD OE1 OE2
REMARK 470 THR A 272 OG1 CG2
REMARK 470 GLU A 275 CG CD OE1 OE2
REMARK 470 ILE A 276 CG1 CG2 CD1
REMARK 470 LYS A 278 CD CE NZ
REMARK 470 LYS A 279 CG CD CE NZ
REMARK 470 GLU A 295 CG CD OE1 OE2
REMARK 470 LYS A 312 CE NZ
REMARK 470 LYS A 373 CG CD CE NZ
REMARK 470 GLU A 377 CG CD OE1 OE2
REMARK 470 ARG A 382 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 431 CG CD NE CZ NH1 NH2
REMARK 470 THR A 432 OG1 CG2
REMARK 470 GLN A 433 CG CD OE1 NE2
REMARK 470 LYS A 444 CG CD CE NZ
REMARK 470 GLU A 454 CD OE1 OE2
REMARK 470 GLU A 457 CG CD OE1 OE2
REMARK 470 LYS A 494 CD CE NZ
REMARK 470 GLU A 501 CG CD OE1 OE2
REMARK 470 GLU A 504 CG CD OE1 OE2
REMARK 470 SER A 505 OG
REMARK 470 THR A 506 OG1 CG2
REMARK 470 LEU A 512 CG CD1 CD2
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 SER A 223 -165.59 -126.03
REMARK 500 ASN A 281 89.19 -152.79
REMARK 500 ALA A 294 -148.25 -112.17
REMARK 500 ARG A 346 -3.61 71.21
REMARK 500 ASP A 347 46.27 -145.17
REMARK 500 ASP A 368 80.46 63.53
REMARK 500 ALA A 402 129.81 -38.40
REMARK 500 LEU A 467 36.00 -86.88
REMARK 500 ALA A 507 109.40 -44.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H3R A1513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A1514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1516
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GXC RELATED DB: PDB
REMARK 900 FHA DOMAIN FROM HUMAN CHK2 KINASE IN COMPLEX WITH A
REMARK 900 SYNTHETIC PHOSPHOPEPTIDE
REMARK 900 RELATED ID: 2CN5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH ADP
REMARK 900 RELATED ID: 2CN8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH
REMARK 900 DEBROMOHYMENIALDISINE
REMARK 900 RELATED ID: 2W0J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH NSC 109555
REMARK 900 , A SPECIFIC INHIBITOR
REMARK 900 RELATED ID: 2W7X RELATED DB: PDB
REMARK 900 CELLULAR INHIBITION OF CHECKPOINT KINASE 2 AND
REMARK 900 POTENTIATION OF CYTOTOXIC DRUGS BY NOVEL CHK2 INHIBITOR
REMARK 900 PV1019
REMARK 900 RELATED ID: 2WTC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 2WTD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 2WTI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 2WTJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 2XBJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 2XK9 RELATED DB: PDB
REMARK 900 STRUCTURAL ANALYSIS OF CHECKPOINT KINASE 2 (CHK2) IN
REMARK 900 COMPLEX WITH INHIBITOR PV1533
REMARK 900 RELATED ID: 2XM8 RELATED DB: PDB
REMARK 900 CO-CRYSTAL STRUCTURE OF A SMALL MOLECULE INHIBITOR
REMARK 900 BOUND TO THE KINASE DOMAIN OF CHK2
REMARK 900 RELATED ID: 2XM9 RELATED DB: PDB
REMARK 900 STRUCTURE OF A SMALL MOLECULE INHIBITOR WITH THE
REMARK 900 KINASE DOMAIN OF CHK2
REMARK 900 RELATED ID: 2YCF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 2 IN COMPLEX
REMARK 900 WITH INHIBITOR PV1531
REMARK 900 RELATED ID: 2YCQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 2 IN COMPLEX
REMARK 900 WITH INHIBITOR PV1115
REMARK 900 RELATED ID: 2YCR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 2 IN COMPLEX
REMARK 900 WITH INHIBITOR PV976
REMARK 900 RELATED ID: 2YCS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHECKPOINT KINASE 2 IN COMPLEX
REMARK 900 WITH PV788
REMARK 900 RELATED ID: 2YIQ RELATED DB: PDB
REMARK 900 STRUCTURAL ANALYSIS OF CHECKPOINT KINASE 2 IN COMPLEX
REMARK 900 WITH INHIBITOR PV1322
REMARK 900 RELATED ID: 2YIR RELATED DB: PDB
REMARK 900 STRUCTURAL ANALYSIS OF CHECKPOINT KINASE 2 IN COMPLEX
REMARK 900 WITH INHIBITOR PV1352
REMARK 900 RELATED ID: 2YIT RELATED DB: PDB
REMARK 900 STRUCTURAL ANALYSIS OF CHECKPOINT KINASE 2 IN COMPLEX
REMARK 900 WITH PV1162, A NOVEL INHIBITOR
REMARK 900 RELATED ID: 4A9R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH
REMARK 900 BENZIMIDAZOLE CARBOXAMIDE INHIBITOR
REMARK 900 RELATED ID: 4A9S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH
REMARK 900 BENZIMIDAZOLE CARBOXAMIDE INHIBITOR
REMARK 900 RELATED ID: 4A9T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH
REMARK 900 BENZIMIDAZOLE CARBOXAMIDE INHIBITOR
REMARK 900 RELATED ID: 4A9U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH
REMARK 900 BENZIMIDAZOLE CARBOXAMIDE INHIBITOR
REMARK 900 RELATED ID: 4BDA RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
REMARK 900 RELATED ID: 4BDB RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
REMARK 900 RELATED ID: 4BDC RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
REMARK 900 RELATED ID: 4BDD RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
REMARK 900 RELATED ID: 4BDE RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
REMARK 900 RELATED ID: 4BDG RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
REMARK 900 RELATED ID: 4BDH RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
REMARK 900 RELATED ID: 4BDI RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
REMARK 900 RELATED ID: 4BDJ RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
REMARK 900 RELATED ID: 4BDK RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING IDENTIFIES A NEW AREA FOR
REMARK 900 INHIBITOR BINDING TO CHECKPOINT KINASE 2 (CHK2)
DBREF 4BDF A 210 531 UNP O96017 CHK2_HUMAN 210 531
SEQADV 4BDF GLY A 203 UNP O96017 EXPRESSION TAG
SEQADV 4BDF PRO A 204 UNP O96017 EXPRESSION TAG
SEQADV 4BDF LEU A 205 UNP O96017 EXPRESSION TAG
SEQADV 4BDF GLY A 206 UNP O96017 EXPRESSION TAG
SEQADV 4BDF SER A 207 UNP O96017 EXPRESSION TAG
SEQADV 4BDF HIS A 208 UNP O96017 EXPRESSION TAG
SEQADV 4BDF MET A 209 UNP O96017 EXPRESSION TAG
SEQRES 1 A 329 GLY PRO LEU GLY SER HIS MET SER VAL TYR PRO LYS ALA
SEQRES 2 A 329 LEU ARG ASP GLU TYR ILE MET SER LYS THR LEU GLY SER
SEQRES 3 A 329 GLY ALA CYS GLY GLU VAL LYS LEU ALA PHE GLU ARG LYS
SEQRES 4 A 329 THR CYS LYS LYS VAL ALA ILE LYS ILE ILE SER LYS ARG
SEQRES 5 A 329 LYS PHE ALA ILE GLY SER ALA ARG GLU ALA ASP PRO ALA
SEQRES 6 A 329 LEU ASN VAL GLU THR GLU ILE GLU ILE LEU LYS LYS LEU
SEQRES 7 A 329 ASN HIS PRO CYS ILE ILE LYS ILE LYS ASN PHE PHE ASP
SEQRES 8 A 329 ALA GLU ASP TYR TYR ILE VAL LEU GLU LEU MET GLU GLY
SEQRES 9 A 329 GLY GLU LEU PHE ASP LYS VAL VAL GLY ASN LYS ARG LEU
SEQRES 10 A 329 LYS GLU ALA THR CYS LYS LEU TYR PHE TYR GLN MET LEU
SEQRES 11 A 329 LEU ALA VAL GLN TYR LEU HIS GLU ASN GLY ILE ILE HIS
SEQRES 12 A 329 ARG ASP LEU LYS PRO GLU ASN VAL LEU LEU SER SER GLN
SEQRES 13 A 329 GLU GLU ASP CYS LEU ILE LYS ILE THR ASP PHE GLY HIS
SEQRES 14 A 329 SER LYS ILE LEU GLY GLU THR SER LEU MET ARG THR LEU
SEQRES 15 A 329 CYS GLY THR PRO THR TYR LEU ALA PRO GLU VAL LEU VAL
SEQRES 16 A 329 SER VAL GLY THR ALA GLY TYR ASN ARG ALA VAL ASP CYS
SEQRES 17 A 329 TRP SER LEU GLY VAL ILE LEU PHE ILE CYS LEU SER GLY
SEQRES 18 A 329 TYR PRO PRO PHE SER GLU HIS ARG THR GLN VAL SER LEU
SEQRES 19 A 329 LYS ASP GLN ILE THR SER GLY LYS TYR ASN PHE ILE PRO
SEQRES 20 A 329 GLU VAL TRP ALA GLU VAL SER GLU LYS ALA LEU ASP LEU
SEQRES 21 A 329 VAL LYS LYS LEU LEU VAL VAL ASP PRO LYS ALA ARG PHE
SEQRES 22 A 329 THR THR GLU GLU ALA LEU ARG HIS PRO TRP LEU GLN ASP
SEQRES 23 A 329 GLU ASP MET LYS ARG LYS PHE GLN ASP LEU LEU SER GLU
SEQRES 24 A 329 GLU ASN GLU SER THR ALA LEU PRO GLN VAL LEU ALA GLN
SEQRES 25 A 329 PRO SER THR SER ARG LYS ARG PRO ARG GLU GLY GLU ALA
SEQRES 26 A 329 GLU GLY ALA GLU
HET H3R A1513 12
HET NO3 A1514 4
HET EDO A1515 4
HET EDO A1516 4
HETNAM H3R 5-METHYL-3-PHENYL-1H-PYRAZOLE
HETNAM NO3 NITRATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 H3R C10 H10 N2
FORMUL 3 NO3 N O3 1-
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 5 HOH *50(H2 O)
HELIX 1 1 PRO A 213 GLU A 219 1 7
HELIX 2 2 ASN A 269 LEU A 280 1 12
HELIX 3 3 LEU A 309 VAL A 314 1 6
HELIX 4 4 LYS A 320 ASN A 341 1 22
HELIX 5 5 LYS A 349 GLU A 351 5 3
HELIX 6 6 THR A 378 CYS A 385 1 8
HELIX 7 7 ALA A 392 VAL A 399 1 8
HELIX 8 8 ARG A 406 GLY A 423 1 18
HELIX 9 9 SER A 435 GLY A 443 1 9
HELIX 10 10 ILE A 448 ALA A 453 1 6
HELIX 11 11 SER A 456 LEU A 467 1 12
HELIX 12 12 THR A 476 HIS A 483 1 8
HELIX 13 13 PRO A 484 GLN A 487 5 4
HELIX 14 14 ASP A 488 GLU A 504 1 17
SHEET 1 AA 5 TYR A 220 THR A 225 0
SHEET 2 AA 5 GLU A 233 GLU A 239 -1 O LEU A 236 N SER A 223
SHEET 3 AA 5 LYS A 244 SER A 252 -1 O LYS A 244 N GLU A 239
SHEET 4 AA 5 ASP A 296 LEU A 301 -1 O TYR A 297 N ILE A 251
SHEET 5 AA 5 ILE A 288 ASP A 293 -1 N LYS A 289 O VAL A 300
SHEET 1 AB 3 GLY A 307 GLU A 308 0
SHEET 2 AB 3 VAL A 353 LEU A 355 -1 N LEU A 355 O GLY A 307
SHEET 3 AB 3 ILE A 364 ILE A 366 -1 O LYS A 365 N LEU A 354
SHEET 1 AC 2 ILE A 343 ILE A 344 0
SHEET 2 AC 2 LYS A 373 ILE A 374 -1 O LYS A 373 N ILE A 344
SITE 1 AC1 4 GLU A 302 MET A 304 GLY A 307 LEU A 354
SITE 1 AC2 4 LEU A 375 GLY A 403 ASN A 405 ARG A 406
SITE 1 AC3 4 GLU A 219 ASN A 290 PHE A 291 PHE A 292
SITE 1 AC4 5 LYS A 465 PHE A 475 GLU A 479 HIS A 483
SITE 2 AC4 5 PRO A 484
CRYST1 90.950 90.950 93.030 90.00 90.00 120.00 P 32 2 1 6
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 0.010995 0.006348 0.000000 0.00000
SCALE2 0.000000 0.012696 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010749 0.00000
ATOM 1 N MET A 209 -58.514 36.415 20.842 1.00 73.14 N
ATOM 2 CA MET A 209 -57.230 36.531 20.138 1.00 72.71 C
ATOM 3 C MET A 209 -56.343 37.723 20.691 1.00 76.61 C
ATOM 4 O MET A 209 -56.258 37.852 21.921 1.00 77.94 O
ATOM 5 CB MET A 209 -57.454 36.547 18.612 1.00 74.74 C
ATOM 6 N SER A 210 -55.658 38.545 19.822 1.00113.31 N
ANISOU 6 N SER A 210 14362 14596 14094 1824 3413 3046 N
ATOM 7 CA SER A 210 -54.807 39.708 20.214 1.00109.59 C
ANISOU 7 CA SER A 210 14099 14556 12984 2029 3005 2846 C
ATOM 8 C SER A 210 -54.424 40.623 19.019 1.00104.25 C
ANISOU 8 C SER A 210 13474 13859 12276 1664 2544 2321 C
ATOM 9 O SER A 210 -54.695 40.249 17.869 1.00104.37 O
ANISOU 9 O SER A 210 13384 13576 12697 1293 2538 2127 O
ATOM 10 CB SER A 210 -53.551 39.261 20.962 1.00115.31 C
ANISOU 10 CB SER A 210 14928 15451 13432 2381 3047 3067 C
ATOM 11 OG SER A 210 -53.223 40.192 21.983 1.00125.09 O
ANISOU 11 OG SER A 210 16287 17174 14068 2794 2837 3037 O
ATOM 12 N VAL A 211 -53.806 41.819 19.281 1.00 92.72 N
ANISOU 12 N VAL A 211 12140 12722 10368 1800 2169 2086 N
ATOM 13 CA VAL A 211 -53.416 42.775 18.208 1.00 86.25 C
ANISOU 13 CA VAL A 211 11342 11883 9546 1507 1774 1657 C
ATOM 14 C VAL A 211 -51.908 43.098 18.116 1.00 84.50 C
ANISOU 14 C VAL A 211 11217 11756 9135 1586 1493 1496 C
ATOM 15 O VAL A 211 -51.186 42.927 19.106 1.00 85.66 O
ANISOU 15 O VAL A 211 11434 12103 9010 1937 1508 1634 O
ATOM 16 CB VAL A 211 -54.275 44.086 18.136 1.00 87.09 C
ANISOU 16 CB VAL A 211 11424 12149 9519 1441 1565 1429 C
ATOM 17 CG1 VAL A 211 -55.736 43.801 17.823 1.00 87.21 C
ANISOU 17 CG1 VAL A 211 11324 12005 9806 1248 1788 1491 C
ATOM 18 CG2 VAL A 211 -54.126 44.951 19.385 1.00 87.47 C
ANISOU 18 CG2 VAL A 211 11529 12568 9137 1832 1431 1431 C
ATOM 19 N TYR A 212 -51.462 43.606 16.923 1.00 74.66 N
ANISOU 19 N TYR A 212 9954 10388 8027 1290 1242 1205 N
ATOM 20 CA TYR A 212 -50.100 44.090 16.654 1.00 71.48 C
ANISOU 20 CA TYR A 212 9607 10027 7527 1315 961 1021 C
ATOM 21 C TYR A 212 -49.971 45.520 17.192 1.00 73.06 C
ANISOU 21 C TYR A 212 9797 10467 7496 1483 672 801 C
ATOM 22 O TYR A 212 -50.977 46.255 17.218 1.00 71.85 O
ANISOU 22 O TYR A 212 9587 10386 7327 1434 641 724 O
ATOM 23 CB TYR A 212 -49.768 44.110 15.150 1.00 69.78 C
ANISOU 23 CB TYR A 212 9342 9605 7568 976 846 842 C
ATOM 24 CG TYR A 212 -49.693 42.746 14.520 1.00 72.36 C
ANISOU 24 CG TYR A 212 9640 9695 8158 813 1062 954 C
ATOM 25 CD1 TYR A 212 -48.710 41.834 14.898 1.00 75.62 C
ANISOU 25 CD1 TYR A 212 10120 10042 8569 932 1158 1109 C
ATOM 26 CD2 TYR A 212 -50.597 42.362 13.539 1.00 73.21 C
ANISOU 26 CD2 TYR A 212 9625 9650 8541 555 1156 867 C
ATOM 27 CE1 TYR A 212 -48.661 40.555 14.346 1.00 77.51 C
ANISOU 27 CE1 TYR A 212 10302 10037 9113 782 1364 1197 C
ATOM 28 CE2 TYR A 212 -50.550 41.091 12.969 1.00 75.34 C
ANISOU 28 CE2 TYR A 212 9815 9691 9120 417 1336 899 C
ATOM 29 CZ TYR A 212 -49.569 40.196 13.362 1.00 85.25 C
ANISOU 29 CZ TYR A 212 11133 10851 10406 519 1441 1068 C
ATOM 30 OH TYR A 212 -49.512 38.958 12.766 1.00 89.35 O
ANISOU 30 OH TYR A 212 11542 11121 11287 375 1612 1072 O
ATOM 31 N PRO A 213 -48.749 45.967 17.586 1.00 68.15 N
ANISOU 31 N PRO A 213 9199 9952 6741 1674 446 658 N
ATOM 32 CA PRO A 213 -48.624 47.334 18.116 1.00 66.83 C
ANISOU 32 CA PRO A 213 8960 9984 6450 1847 160 384 C
ATOM 33 C PRO A 213 -48.848 48.374 17.035 1.00 65.57 C
ANISOU 33 C PRO A 213 8694 9677 6541 1555 -8 179 C
ATOM 34 O PRO A 213 -48.540 48.148 15.848 1.00 62.54 O
ANISOU 34 O PRO A 213 8301 9079 6381 1284 10 195 O
ATOM 35 CB PRO A 213 -47.207 47.377 18.710 1.00 69.79 C
ANISOU 35 CB PRO A 213 9348 10465 6706 2115 -22 255 C
ATOM 36 CG PRO A 213 -46.732 45.965 18.711 1.00 75.18 C
ANISOU 36 CG PRO A 213 10147 11065 7355 2138 217 540 C
ATOM 37 CD PRO A 213 -47.448 45.266 17.615 1.00 69.55 C
ANISOU 37 CD PRO A 213 9443 10074 6907 1760 436 708 C
ATOM 38 N LYS A 214 -49.429 49.503 17.456 1.00 60.06 N
ANISOU 38 N LYS A 214 7902 9118 5798 1644 -155 2 N
ATOM 39 CA LYS A 214 -49.745 50.639 16.600 1.00 57.12 C
ANISOU 39 CA LYS A 214 7400 8637 5666 1429 -293 -165 C
ATOM 40 C LYS A 214 -48.524 51.079 15.762 1.00 58.15 C
ANISOU 40 C LYS A 214 7446 8578 6069 1325 -452 -286 C
ATOM 41 O LYS A 214 -48.691 51.310 14.568 1.00 55.13 O
ANISOU 41 O LYS A 214 7008 8043 5897 1081 -416 -239 O
ATOM 42 CB LYS A 214 -50.272 51.778 17.471 1.00 59.59 C
ANISOU 42 CB LYS A 214 7603 9143 5894 1623 -456 -372 C
ATOM 43 CG LYS A 214 -51.180 52.743 16.760 1.00 53.87 C
ANISOU 43 CG LYS A 214 6763 8341 5363 1408 -487 -440 C
ATOM 44 CD LYS A 214 -51.165 54.080 17.489 1.00 47.87 C
ANISOU 44 CD LYS A 214 5829 7700 4658 1601 -732 -742 C
ATOM 45 CE LYS A 214 -52.192 55.023 16.934 1.00 49.02 C
ANISOU 45 CE LYS A 214 5862 7793 4971 1419 -733 -776 C
ATOM 46 NZ LYS A 214 -52.067 56.348 17.573 1.00 64.71 N
ANISOU 46 NZ LYS A 214 7630 9836 7120 1588 -982 -1103 N
ATOM 47 N ALA A 215 -47.300 51.137 16.377 1.00 55.49 N
ANISOU 47 N ALA A 215 7089 8272 5722 1540 -612 -428 N
ATOM 48 CA ALA A 215 -46.028 51.500 15.717 1.00 54.76 C
ANISOU 48 CA ALA A 215 6903 7982 5922 1477 -751 -535 C
ATOM 49 C ALA A 215 -45.602 50.514 14.608 1.00 59.21 C
ANISOU 49 C ALA A 215 7573 8370 6554 1253 -591 -308 C
ATOM 50 O ALA A 215 -45.065 50.942 13.581 1.00 58.51 O
ANISOU 50 O ALA A 215 7388 8106 6738 1107 -628 -305 O
ATOM 51 CB ALA A 215 -44.918 51.649 16.741 1.00 56.89 C
ANISOU 51 CB ALA A 215 7123 8352 6140 1786 -952 -768 C
ATOM 52 N LEU A 216 -45.827 49.200 14.816 1.00 55.73 N
ANISOU 52 N LEU A 216 7304 7978 5892 1252 -402 -113 N
ATOM 53 CA LEU A 216 -45.540 48.190 13.803 1.00 54.86 C
ANISOU 53 CA LEU A 216 7270 7714 5861 1049 -256 57 C
ATOM 54 C LEU A 216 -46.494 48.415 12.650 1.00 57.59 C
ANISOU 54 C LEU A 216 7549 8004 6330 808 -171 102 C
ATOM 55 O LEU A 216 -46.057 48.612 11.518 1.00 56.09 O
ANISOU 55 O LEU A 216 7291 7713 6308 682 -198 109 O
ATOM 56 CB LEU A 216 -45.735 46.777 14.391 1.00 56.49 C
ANISOU 56 CB LEU A 216 7622 7959 5882 1116 -44 250 C
ATOM 57 CG LEU A 216 -45.574 45.601 13.432 1.00 59.57 C
ANISOU 57 CG LEU A 216 8060 8180 6395 911 119 388 C
ATOM 58 CD1 LEU A 216 -44.170 45.525 12.935 1.00 59.10 C
ANISOU 58 CD1 LEU A 216 8009 8016 6430 899 -2 342 C
ATOM 59 CD2 LEU A 216 -46.007 44.293 14.085 1.00 61.37 C
ANISOU 59 CD2 LEU A 216 8372 8403 6542 977 377 598 C
ATOM 60 N ARG A 217 -47.808 48.444 12.975 1.00 55.27 N
ANISOU 60 N ARG A 217 7258 7807 5937 786 -71 130 N
ATOM 61 CA ARG A 217 -48.960 48.688 12.100 1.00 53.80 C
ANISOU 61 CA ARG A 217 6998 7623 5820 602 7 138 C
ATOM 62 C ARG A 217 -48.791 49.948 11.263 1.00 57.61 C
ANISOU 62 C ARG A 217 7335 8087 6468 552 -127 56 C
ATOM 63 O ARG A 217 -49.042 49.906 10.060 1.00 59.48 O
ANISOU 63 O ARG A 217 7506 8313 6783 425 -73 94 O
ATOM 64 CB ARG A 217 -50.251 48.778 12.937 1.00 52.05 C
ANISOU 64 CB ARG A 217 6793 7520 5466 651 94 154 C
ATOM 65 CG ARG A 217 -50.858 47.425 13.291 1.00 47.56 C
ANISOU 65 CG ARG A 217 6304 6921 4847 635 336 310 C
ATOM 66 CD ARG A 217 -52.104 47.602 14.101 1.00 46.67 C
ANISOU 66 CD ARG A 217 6188 6917 4626 707 438 358 C
ATOM 67 NE ARG A 217 -53.216 48.181 13.342 1.00 41.56 N
ANISOU 67 NE ARG A 217 5445 6279 4067 530 439 271 N
ATOM 68 CZ ARG A 217 -53.959 49.195 13.760 1.00 62.60 C
ANISOU 68 CZ ARG A 217 8068 9067 6649 579 360 201 C
ATOM 69 NH1 ARG A 217 -53.681 49.800 14.902 1.00 58.64 N
ANISOU 69 NH1 ARG A 217 7592 8701 5987 807 248 166 N
ATOM 70 NH2 ARG A 217 -54.989 49.617 13.035 1.00 60.43 N
ANISOU 70 NH2 ARG A 217 7709 8804 6449 422 382 137 N
ATOM 71 N ASP A 218 -48.319 51.043 11.871 1.00 52.59 N
ANISOU 71 N ASP A 218 6617 7453 5912 684 -293 -58 N
ATOM 72 CA ASP A 218 -48.052 52.299 11.172 1.00 52.41 C
ANISOU 72 CA ASP A 218 6407 7356 6152 664 -388 -102 C
ATOM 73 C ASP A 218 -47.153 52.114 9.960 1.00 55.69 C
ANISOU 73 C ASP A 218 6771 7657 6732 599 -354 11 C
ATOM 74 O ASP A 218 -47.387 52.748 8.942 1.00 56.51 O
ANISOU 74 O ASP A 218 6740 7758 6973 552 -308 96 O
ATOM 75 CB ASP A 218 -47.390 53.322 12.115 1.00 55.62 C
ANISOU 75 CB ASP A 218 6689 7721 6723 838 -584 -299 C
ATOM 76 CG ASP A 218 -47.379 54.715 11.525 1.00 68.06 C
ANISOU 76 CG ASP A 218 8018 9182 8658 818 -639 -333 C
ATOM 77 OD1 ASP A 218 -48.440 55.378 11.557 1.00 69.68 O
ANISOU 77 OD1 ASP A 218 8156 9463 8857 788 -620 -354 O
ATOM 78 OD2 ASP A 218 -46.347 55.095 10.914 1.00 75.10 O
ANISOU 78 OD2 ASP A 218 8776 9898 9861 826 -663 -292 O
ATOM 79 N GLU A 219 -46.123 51.269 10.084 1.00 51.95 N
ANISOU 79 N GLU A 219 6395 7112 6230 628 -368 30 N
ATOM 80 CA GLU A 219 -45.115 51.009 9.070 1.00 51.50 C
ANISOU 80 CA GLU A 219 6302 6954 6312 596 -346 133 C
ATOM 81 C GLU A 219 -45.252 49.770 8.183 1.00 54.73 C
ANISOU 81 C GLU A 219 6809 7416 6570 491 -218 233 C
ATOM 82 O GLU A 219 -44.737 49.795 7.067 1.00 54.06 O
ANISOU 82 O GLU A 219 6647 7318 6574 485 -188 326 O
ATOM 83 CB GLU A 219 -43.765 50.968 9.737 1.00 53.62 C
ANISOU 83 CB GLU A 219 6584 7096 6692 706 -468 55 C
ATOM 84 CG GLU A 219 -43.057 52.290 9.691 1.00 60.97 C
ANISOU 84 CG GLU A 219 7288 7876 8002 792 -584 -20 C
ATOM 85 CD GLU A 219 -41.675 52.119 10.254 1.00 70.45 C
ANISOU 85 CD GLU A 219 8491 8953 9323 901 -711 -137 C
ATOM 86 OE1 GLU A 219 -40.782 51.691 9.486 1.00 51.69 O
ANISOU 86 OE1 GLU A 219 6130 6474 7036 865 -665 -11 O
ATOM 87 OE2 GLU A 219 -41.516 52.304 11.484 1.00 71.38 O
ANISOU 87 OE2 GLU A 219 8610 9119 9391 1046 -856 -364 O
ATOM 88 N TYR A 220 -45.868 48.688 8.680 1.00 51.65 N
ANISOU 88 N TYR A 220 6557 7076 5991 438 -135 211 N
ATOM 89 CA TYR A 220 -46.013 47.444 7.928 1.00 51.68 C
ANISOU 89 CA TYR A 220 6607 7092 5938 340 -21 241 C
ATOM 90 C TYR A 220 -47.454 46.940 7.902 1.00 59.31 C
ANISOU 90 C TYR A 220 7564 8138 6832 248 99 192 C
ATOM 91 O TYR A 220 -48.195 47.114 8.885 1.00 58.73 O
ANISOU 91 O TYR A 220 7533 8086 6695 270 130 186 O
ATOM 92 CB TYR A 220 -45.098 46.349 8.526 1.00 53.02 C
ANISOU 92 CB TYR A 220 6913 7154 6079 365 2 273 C
ATOM 93 CG TYR A 220 -43.642 46.765 8.638 1.00 54.86 C
ANISOU 93 CG TYR A 220 7153 7297 6397 459 -124 287 C
ATOM 94 CD1 TYR A 220 -42.760 46.576 7.582 1.00 55.75 C
ANISOU 94 CD1 TYR A 220 7223 7358 6602 434 -138 337 C
ATOM 95 CD2 TYR A 220 -43.156 47.385 9.790 1.00 56.25 C
ANISOU 95 CD2 TYR A 220 7348 7453 6573 600 -239 224 C
ATOM 96 CE1 TYR A 220 -41.442 47.021 7.649 1.00 56.02 C
ANISOU 96 CE1 TYR A 220 7236 7281 6770 518 -241 355 C
ATOM 97 CE2 TYR A 220 -41.840 47.839 9.868 1.00 57.02 C
ANISOU 97 CE2 TYR A 220 7402 7446 6817 691 -369 183 C
ATOM 98 CZ TYR A 220 -40.978 47.638 8.800 1.00 63.01 C
ANISOU 98 CZ TYR A 220 8124 8110 7706 635 -359 265 C
ATOM 99 OH TYR A 220 -39.658 48.039 8.867 1.00 61.74 O
ANISOU 99 OH TYR A 220 7908 7816 7735 720 -469 234 O
ATOM 100 N ILE A 221 -47.837 46.289 6.769 1.00 58.01 N
ANISOU 100 N ILE A 221 7320 8030 6691 170 161 134 N
ATOM 101 CA ILE A 221 -49.123 45.615 6.582 1.00 59.04 C
ANISOU 101 CA ILE A 221 7391 8202 6839 78 272 26 C
ATOM 102 C ILE A 221 -48.854 44.137 6.819 1.00 68.87 C
ANISOU 102 C ILE A 221 8681 9294 8194 19 382 13 C
ATOM 103 O ILE A 221 -48.359 43.460 5.921 1.00 69.40 O
ANISOU 103 O ILE A 221 8686 9356 8326 -3 369 -67 O
ATOM 104 CB ILE A 221 -49.802 45.834 5.207 1.00 61.60 C
ANISOU 104 CB ILE A 221 7541 8718 7145 74 253 -107 C
ATOM 105 CG1 ILE A 221 -49.770 47.291 4.753 1.00 60.49 C
ANISOU 105 CG1 ILE A 221 7331 8724 6929 172 173 -23 C
ATOM 106 CG2 ILE A 221 -51.238 45.288 5.247 1.00 63.53 C
ANISOU 106 CG2 ILE A 221 7702 8981 7456 -16 350 -268 C
ATOM 107 CD1 ILE A 221 -50.594 47.536 3.507 1.00 60.65 C
ANISOU 107 CD1 ILE A 221 7174 8998 6872 230 178 -126 C
ATOM 108 N MET A 222 -49.146 43.652 8.036 1.00 70.63 N
ANISOU 108 N MET A 222 8994 9399 8443 24 503 110 N
ATOM 109 CA MET A 222 -48.907 42.267 8.462 1.00 73.59 C
ANISOU 109 CA MET A 222 9398 9594 8968 -1 665 175 C
ATOM 110 C MET A 222 -49.726 41.221 7.693 1.00 80.16 C
ANISOU 110 C MET A 222 10050 10337 10069 -130 787 4 C
ATOM 111 O MET A 222 -50.939 41.394 7.495 1.00 79.83 O
ANISOU 111 O MET A 222 9889 10342 10100 -187 829 -116 O
ATOM 112 CB MET A 222 -49.108 42.123 9.968 1.00 77.77 C
ANISOU 112 CB MET A 222 10039 10073 9437 110 800 377 C
ATOM 113 CG MET A 222 -48.118 42.907 10.800 1.00 82.21 C
ANISOU 113 CG MET A 222 10745 10724 9767 283 662 473 C
ATOM 114 SD MET A 222 -46.427 42.263 10.728 1.00 88.13 S
ANISOU 114 SD MET A 222 11588 11380 10517 341 609 534 S
ATOM 115 CE MET A 222 -46.661 40.554 11.254 1.00 86.95 C
ANISOU 115 CE MET A 222 11438 11046 10553 340 919 712 C
ATOM 116 N SER A 223 -49.040 40.140 7.253 1.00 78.22 N
ANISOU 116 N SER A 223 9762 9959 9999 -170 830 -42 N
ATOM 117 CA SER A 223 -49.597 39.047 6.449 1.00 80.21 C
ANISOU 117 CA SER A 223 9791 10104 10581 -277 911 -281 C
ATOM 118 C SER A 223 -49.360 37.631 7.068 1.00 89.76 C
ANISOU 118 C SER A 223 10963 11004 12137 -315 1146 -170 C
ATOM 119 O SER A 223 -49.019 37.515 8.251 1.00 90.78 O
ANISOU 119 O SER A 223 11246 11036 12210 -233 1288 139 O
ATOM 120 CB SER A 223 -49.069 39.136 5.016 1.00 81.04 C
ANISOU 120 CB SER A 223 9797 10386 10607 -262 716 -519 C
ATOM 121 OG SER A 223 -49.829 38.345 4.119 1.00 87.18 O
ANISOU 121 OG SER A 223 10305 11164 11658 -320 728 -866 O
ATOM 122 N LYS A 224 -49.571 36.572 6.255 1.00 89.35 N
ANISOU 122 N LYS A 224 10674 10817 12457 -408 1190 -434 N
ATOM 123 CA LYS A 224 -49.478 35.144 6.578 1.00 91.85 C
ANISOU 123 CA LYS A 224 10857 10795 13248 -466 1427 -395 C
ATOM 124 C LYS A 224 -48.180 34.675 7.246 1.00 96.37 C
ANISOU 124 C LYS A 224 11621 11253 13743 -397 1500 -91 C
ATOM 125 O LYS A 224 -47.097 35.154 6.913 1.00 94.09 O
ANISOU 125 O LYS A 224 11493 11129 13128 -346 1297 -82 O
ATOM 126 CB LYS A 224 -49.756 34.309 5.315 1.00 95.89 C
ANISOU 126 CB LYS A 224 11041 11247 14144 -557 1360 -856 C
ATOM 127 N THR A 225 -48.304 33.690 8.156 1.00 95.62 N
ANISOU 127 N THR A 225 11480 10865 13986 -378 1815 166 N
ATOM 128 CA THR A 225 -47.195 33.053 8.880 1.00 95.75 C
ANISOU 128 CA THR A 225 11640 10753 13986 -282 1949 483 C
ATOM 129 C THR A 225 -46.237 32.274 7.943 1.00 98.60 C
ANISOU 129 C THR A 225 11919 11022 14523 -366 1842 268 C
ATOM 130 O THR A 225 -46.689 31.508 7.090 1.00 99.49 O
ANISOU 130 O THR A 225 11741 10983 15076 -493 1854 -64 O
ATOM 131 CB THR A 225 -47.732 32.195 10.054 1.00106.92 C
ANISOU 131 CB THR A 225 12973 11892 15759 -197 2371 854 C
ATOM 132 OG1 THR A 225 -46.658 31.450 10.632 1.00105.72 O
ANISOU 132 OG1 THR A 225 12924 11624 15622 -82 2519 1151 O
ATOM 133 CG2 THR A 225 -48.865 31.242 9.641 1.00108.81 C
ANISOU 133 CG2 THR A 225 12831 11796 16715 -348 2600 664 C
ATOM 134 N LEU A 226 -44.918 32.477 8.113 1.00 93.09 N
ANISOU 134 N LEU A 226 11454 10424 13491 -278 1725 426 N
ATOM 135 CA LEU A 226 -43.877 31.808 7.317 1.00 92.37 C
ANISOU 135 CA LEU A 226 11326 10269 13501 -335 1618 270 C
ATOM 136 C LEU A 226 -43.283 30.596 8.052 1.00 99.66 C
ANISOU 136 C LEU A 226 12243 10900 14724 -294 1896 550 C
ATOM 137 O LEU A 226 -42.957 29.588 7.414 1.00100.39 O
ANISOU 137 O LEU A 226 12157 10795 15192 -389 1930 377 O
ATOM 138 CB LEU A 226 -42.749 32.787 6.930 1.00 88.94 C
ANISOU 138 CB LEU A 226 11123 10114 12555 -268 1311 253 C
ATOM 139 CG LEU A 226 -43.130 34.054 6.160 1.00 90.75 C
ANISOU 139 CG LEU A 226 11356 10641 12485 -268 1056 46 C
ATOM 140 CD1 LEU A 226 -42.080 35.113 6.340 1.00 88.30 C
ANISOU 140 CD1 LEU A 226 11283 10519 11750 -160 862 189 C
ATOM 141 CD2 LEU A 226 -43.368 33.771 4.690 1.00 91.52 C
ANISOU 141 CD2 LEU A 226 11216 10828 12731 -340 914 -352 C
ATOM 142 N GLY A 227 -43.140 30.723 9.375 1.00 97.51 N
ANISOU 142 N GLY A 227 12150 10632 14270 -120 2090 972 N
ATOM 143 CA GLY A 227 -42.602 29.692 10.259 1.00129.87 C
ANISOU 143 CA GLY A 227 16262 14512 18570 0 2398 1339 C
ATOM 144 C GLY A 227 -42.248 30.217 11.636 1.00143.53 C
ANISOU 144 C GLY A 227 18250 16444 19843 287 2485 1752 C
ATOM 145 O GLY A 227 -43.015 30.063 12.587 1.00 99.84 O
ANISOU 145 O GLY A 227 12672 10874 14387 438 2774 2052 O
ATOM 146 N GLY A 232 -39.872 30.778 18.181 1.00112.70 N
ANISOU 146 N GLY A 232 15133 13761 13925 2286 3078 3543 N
ATOM 147 CA GLY A 232 -40.087 32.055 17.515 1.00108.90 C
ANISOU 147 CA GLY A 232 14708 13382 13286 2036 2643 3070 C
ATOM 148 C GLY A 232 -41.001 31.971 16.304 1.00110.86 C
ANISOU 148 C GLY A 232 14793 13316 14012 1591 2642 2839 C
ATOM 149 O GLY A 232 -40.796 31.114 15.435 1.00111.17 O
ANISOU 149 O GLY A 232 14711 13028 14502 1336 2747 2789 O
ATOM 150 N GLU A 233 -42.027 32.871 16.243 1.00104.09 N
ANISOU 150 N GLU A 233 13913 12581 13057 1519 2510 2665 N
ATOM 151 CA GLU A 233 -43.008 32.976 15.148 1.00100.82 C
ANISOU 151 CA GLU A 233 13337 11954 13014 1151 2471 2402 C
ATOM 152 C GLU A 233 -42.534 34.008 14.118 1.00 97.07 C
ANISOU 152 C GLU A 233 12933 11585 12363 932 2027 1971 C
ATOM 153 O GLU A 233 -42.142 35.113 14.502 1.00 95.21 O
ANISOU 153 O GLU A 233 12833 11622 11722 1074 1772 1876 O
ATOM 154 CB GLU A 233 -44.403 33.336 15.686 1.00103.26 C
ANISOU 154 CB GLU A 233 13564 12327 13345 1229 2645 2525 C
ATOM 155 N VAL A 234 -42.536 33.635 12.818 1.00 88.95 N
ANISOU 155 N VAL A 234 11784 10353 11662 624 1945 1712 N
ATOM 156 CA VAL A 234 -42.082 34.498 11.713 1.00 83.71 C
ANISOU 156 CA VAL A 234 11153 9793 10862 453 1580 1363 C
ATOM 157 C VAL A 234 -43.238 34.747 10.739 1.00 83.84 C
ANISOU 157 C VAL A 234 10990 9773 11093 234 1535 1103 C
ATOM 158 O VAL A 234 -43.806 33.803 10.195 1.00 84.98 O
ANISOU 158 O VAL A 234 10936 9700 11654 86 1694 1015 O
ATOM 159 CB VAL A 234 -40.792 33.937 11.024 1.00 85.73 C
ANISOU 159 CB VAL A 234 11445 9956 11173 379 1467 1280 C
ATOM 160 CG1 VAL A 234 -40.485 34.647 9.716 1.00 82.96 C
ANISOU 160 CG1 VAL A 234 11066 9694 10763 217 1164 964 C
ATOM 161 CG2 VAL A 234 -39.588 34.026 11.953 1.00 85.38 C
ANISOU 161 CG2 VAL A 234 11595 10023 10825 618 1424 1470 C
ATOM 162 N LYS A 235 -43.601 36.012 10.543 1.00 76.29 N
ANISOU 162 N LYS A 235 10076 9027 9883 232 1321 964 N
ATOM 163 CA LYS A 235 -44.693 36.351 9.637 1.00 74.70 C
ANISOU 163 CA LYS A 235 9714 8850 9821 67 1264 720 C
ATOM 164 C LYS A 235 -44.211 37.206 8.487 1.00 73.01 C
ANISOU 164 C LYS A 235 9498 8799 9443 1 971 484 C
ATOM 165 O LYS A 235 -43.252 37.959 8.630 1.00 70.97 O
ANISOU 165 O LYS A 235 9378 8651 8936 93 801 533 O
ATOM 166 CB LYS A 235 -45.852 37.060 10.380 1.00 77.68 C
ANISOU 166 CB LYS A 235 10093 9330 10090 134 1334 800 C
ATOM 167 CG LYS A 235 -46.619 36.155 11.338 1.00 94.52 C
ANISOU 167 CG LYS A 235 12157 11296 12459 205 1683 1051 C
ATOM 168 CD LYS A 235 -48.118 36.355 11.234 1.00102.95 C
ANISOU 168 CD LYS A 235 13072 12342 13701 117 1780 964 C
ATOM 169 N LEU A 236 -44.883 37.082 7.346 1.00 68.19 N
ANISOU 169 N LEU A 236 8701 8212 8994 -125 924 226 N
ATOM 170 CA LEU A 236 -44.670 37.895 6.153 1.00 66.00 C
ANISOU 170 CA LEU A 236 8375 8145 8557 -134 694 32 C
ATOM 171 C LEU A 236 -45.355 39.255 6.420 1.00 67.98 C
ANISOU 171 C LEU A 236 8665 8572 8594 -84 614 64 C
ATOM 172 O LEU A 236 -46.367 39.305 7.111 1.00 68.31 O
ANISOU 172 O LEU A 236 8692 8581 8683 -97 732 108 O
ATOM 173 CB LEU A 236 -45.330 37.191 4.942 1.00 67.06 C
ANISOU 173 CB LEU A 236 8255 8297 8926 -221 688 -287 C
ATOM 174 CG LEU A 236 -45.456 37.945 3.608 1.00 70.25 C
ANISOU 174 CG LEU A 236 8544 8998 9149 -165 491 -501 C
ATOM 175 CD1 LEU A 236 -44.124 38.017 2.887 1.00 69.80 C
ANISOU 175 CD1 LEU A 236 8541 9035 8944 -84 357 -470 C
ATOM 176 CD2 LEU A 236 -46.469 37.285 2.721 1.00 72.70 C
ANISOU 176 CD2 LEU A 236 8573 9365 9685 -205 497 -866 C
ATOM 177 N ALA A 237 -44.786 40.344 5.904 1.00 62.43 N
ANISOU 177 N ALA A 237 7996 8033 7691 -17 434 66 N
ATOM 178 CA ALA A 237 -45.333 41.688 6.045 1.00 61.32 C
ANISOU 178 CA ALA A 237 7858 8039 7403 32 356 92 C
ATOM 179 C ALA A 237 -44.864 42.510 4.857 1.00 64.35 C
ANISOU 179 C ALA A 237 8158 8591 7699 95 217 56 C
ATOM 180 O ALA A 237 -43.919 42.104 4.168 1.00 65.36 O
ANISOU 180 O ALA A 237 8274 8719 7841 124 173 52 O
ATOM 181 CB ALA A 237 -44.857 42.321 7.354 1.00 61.58 C
ANISOU 181 CB ALA A 237 8046 8025 7326 126 330 257 C
ATOM 182 N PHE A 238 -45.513 43.656 4.615 1.00 59.05 N
ANISOU 182 N PHE A 238 7420 8068 6949 140 171 60 N
ATOM 183 CA PHE A 238 -45.141 44.562 3.541 1.00 58.54 C
ANISOU 183 CA PHE A 238 7247 8173 6821 250 93 105 C
ATOM 184 C PHE A 238 -44.831 45.961 4.066 1.00 62.07 C
ANISOU 184 C PHE A 238 7714 8584 7287 319 39 257 C
ATOM 185 O PHE A 238 -45.699 46.613 4.652 1.00 61.50 O
ANISOU 185 O PHE A 238 7636 8530 7200 299 46 242 O
ATOM 186 CB PHE A 238 -46.231 44.641 2.472 1.00 61.53 C
ANISOU 186 CB PHE A 238 7449 8802 7127 288 107 -43 C
ATOM 187 CG PHE A 238 -46.705 43.308 1.960 1.00 65.06 C
ANISOU 187 CG PHE A 238 7806 9282 7633 229 139 -293 C
ATOM 188 CD1 PHE A 238 -46.061 42.684 0.899 1.00 68.89 C
ANISOU 188 CD1 PHE A 238 8193 9889 8091 317 92 -394 C
ATOM 189 CD2 PHE A 238 -47.809 42.680 2.528 1.00 68.57 C
ANISOU 189 CD2 PHE A 238 8225 9625 8202 102 220 -443 C
ATOM 190 CE1 PHE A 238 -46.515 41.454 0.415 1.00 71.55 C
ANISOU 190 CE1 PHE A 238 8392 10247 8548 273 100 -699 C
ATOM 191 CE2 PHE A 238 -48.243 41.440 2.059 1.00 73.12 C
ANISOU 191 CE2 PHE A 238 8656 10174 8953 44 257 -713 C
ATOM 192 CZ PHE A 238 -47.592 40.835 1.006 1.00 71.62 C
ANISOU 192 CZ PHE A 238 8352 10104 8756 127 184 -867 C
ATOM 193 N GLU A 239 -43.596 46.434 3.838 1.00 57.77 N
ANISOU 193 N GLU A 239 7160 7971 6818 404 -14 387 N
ATOM 194 CA GLU A 239 -43.221 47.779 4.227 1.00 56.59 C
ANISOU 194 CA GLU A 239 6955 7742 6805 480 -64 494 C
ATOM 195 C GLU A 239 -44.102 48.704 3.392 1.00 58.50 C
ANISOU 195 C GLU A 239 7027 8167 7034 549 -15 555 C
ATOM 196 O GLU A 239 -44.127 48.568 2.168 1.00 59.17 O
ANISOU 196 O GLU A 239 7004 8440 7039 643 36 614 O
ATOM 197 CB GLU A 239 -41.726 48.011 3.962 1.00 58.01 C
ANISOU 197 CB GLU A 239 7108 7787 7148 562 -104 616 C
ATOM 198 CG GLU A 239 -41.152 49.205 4.712 1.00 69.47 C
ANISOU 198 CG GLU A 239 8487 9056 8854 623 -177 644 C
ATOM 199 CD GLU A 239 -39.748 49.616 4.314 1.00 96.21 C
ANISOU 199 CD GLU A 239 11772 12280 12503 716 -193 773 C
ATOM 200 OE1 GLU A 239 -39.010 48.779 3.741 1.00 98.14 O
ANISOU 200 OE1 GLU A 239 12077 12535 12675 722 -172 830 O
ATOM 201 OE2 GLU A 239 -39.383 50.782 4.588 1.00 90.88 O
ANISOU 201 OE2 GLU A 239 10932 11448 12150 788 -224 805 O
ATOM 202 N ARG A 240 -44.898 49.564 4.058 1.00 53.42 N
ANISOU 202 N ARG A 240 6354 7509 6432 529 -28 528 N
ATOM 203 CA ARG A 240 -45.854 50.503 3.427 1.00 52.87 C
ANISOU 203 CA ARG A 240 6129 7607 6353 592 27 589 C
ATOM 204 C ARG A 240 -45.173 51.514 2.492 1.00 59.91 C
ANISOU 204 C ARG A 240 6823 8516 7424 764 88 831 C
ATOM 205 O ARG A 240 -45.779 51.917 1.493 1.00 62.98 O
ANISOU 205 O ARG A 240 7071 9139 7721 886 177 937 O
ATOM 206 CB ARG A 240 -46.659 51.277 4.489 1.00 48.87 C
ANISOU 206 CB ARG A 240 5632 7036 5902 537 -11 513 C
ATOM 207 CG ARG A 240 -47.540 50.440 5.394 1.00 49.52 C
ANISOU 207 CG ARG A 240 5870 7135 5809 414 -18 343 C
ATOM 208 CD ARG A 240 -48.368 51.319 6.314 1.00 50.51 C
ANISOU 208 CD ARG A 240 5981 7251 5961 403 -52 287 C
ATOM 209 NE ARG A 240 -49.110 50.527 7.304 1.00 55.11 N
ANISOU 209 NE ARG A 240 6709 7840 6390 328 -29 179 N
ATOM 210 CZ ARG A 240 -50.323 50.018 7.108 1.00 61.18 C
ANISOU 210 CZ ARG A 240 7484 8716 7047 248 58 119 C
ATOM 211 NH1 ARG A 240 -50.952 50.211 5.961 1.00 47.72 N
ANISOU 211 NH1 ARG A 240 5655 7163 5313 244 97 107 N
ATOM 212 NH2 ARG A 240 -50.910 49.303 8.055 1.00 45.91 N
ANISOU 212 NH2 ARG A 240 5657 6747 5041 201 118 75 N
ATOM 213 N LYS A 241 -43.939 51.958 2.850 1.00 53.87 N
ANISOU 213 N LYS A 241 6022 7505 6941 802 54 925 N
ATOM 214 CA LYS A 241 -43.154 52.944 2.121 1.00 53.67 C
ANISOU 214 CA LYS A 241 5776 7400 7216 968 145 1191 C
ATOM 215 C LYS A 241 -42.724 52.418 0.747 1.00 58.03 C
ANISOU 215 C LYS A 241 6273 8168 7609 1123 250 1380 C
ATOM 216 O LYS A 241 -42.780 53.137 -0.254 1.00 57.98 O
ANISOU 216 O LYS A 241 6061 8306 7661 1330 398 1648 O
ATOM 217 CB LYS A 241 -41.917 53.300 2.967 1.00 56.44 C
ANISOU 217 CB LYS A 241 6102 7403 7937 948 56 1155 C
ATOM 218 CG LYS A 241 -41.126 54.521 2.485 1.00 69.87 C
ANISOU 218 CG LYS A 241 7511 8899 10136 1101 161 1410 C
ATOM 219 N THR A 242 -42.288 51.157 0.719 1.00 54.89 N
ANISOU 219 N THR A 242 6042 7805 7008 1053 184 1247 N
ATOM 220 CA THR A 242 -41.690 50.504 -0.428 1.00 55.08 C
ANISOU 220 CA THR A 242 6027 8017 6883 1200 242 1360 C
ATOM 221 C THR A 242 -42.573 49.495 -1.131 1.00 61.18 C
ANISOU 221 C THR A 242 6835 9135 7276 1218 227 1168 C
ATOM 222 O THR A 242 -42.294 49.170 -2.288 1.00 62.42 O
ANISOU 222 O THR A 242 6891 9559 7267 1422 276 1249 O
ATOM 223 CB THR A 242 -40.374 49.852 0.026 1.00 61.55 C
ANISOU 223 CB THR A 242 6970 8589 7827 1122 169 1332 C
ATOM 224 OG1 THR A 242 -40.647 48.748 0.904 1.00 62.02 O
ANISOU 224 OG1 THR A 242 7252 8582 7732 915 58 1050 O
ATOM 225 CG2 THR A 242 -39.442 50.834 0.701 1.00 55.10 C
ANISOU 225 CG2 THR A 242 6070 7426 7441 1128 161 1453 C
ATOM 226 N CYS A 243 -43.611 48.969 -0.432 1.00 58.52 N
ANISOU 226 N CYS A 243 6616 8794 6826 1028 158 895 N
ATOM 227 CA CYS A 243 -44.541 47.933 -0.912 1.00 58.99 C
ANISOU 227 CA CYS A 243 6676 9098 6637 1001 131 625 C
ATOM 228 C CYS A 243 -43.795 46.621 -1.101 1.00 68.82 C
ANISOU 228 C CYS A 243 7999 10306 7844 955 81 488 C
ATOM 229 O CYS A 243 -44.246 45.735 -1.835 1.00 72.74 O
ANISOU 229 O CYS A 243 8418 11029 8191 1004 55 260 O
ATOM 230 CB CYS A 243 -45.266 48.364 -2.181 1.00 59.55 C
ANISOU 230 CB CYS A 243 6539 9585 6502 1253 189 658 C
ATOM 231 SG CYS A 243 -46.553 49.587 -1.894 1.00 63.30 S
ANISOU 231 SG CYS A 243 6935 10126 6991 1257 243 720 S
ATOM 232 N LYS A 244 -42.638 46.516 -0.447 1.00 63.91 N
ANISOU 232 N LYS A 244 7502 9399 7381 876 58 600 N
ATOM 233 CA LYS A 244 -41.764 45.370 -0.544 1.00 63.40 C
ANISOU 233 CA LYS A 244 7520 9258 7311 831 20 516 C
ATOM 234 C LYS A 244 -41.984 44.433 0.611 1.00 64.16 C
ANISOU 234 C LYS A 244 7786 9116 7474 602 -4 340 C
ATOM 235 O LYS A 244 -42.333 44.865 1.714 1.00 62.47 O
ANISOU 235 O LYS A 244 7664 8742 7331 504 -2 361 O
ATOM 236 CB LYS A 244 -40.291 45.812 -0.653 1.00 66.68 C
ANISOU 236 CB LYS A 244 7947 9529 7859 923 25 766 C
ATOM 237 CG LYS A 244 -39.984 46.626 -1.918 1.00 79.80 C
ANISOU 237 CG LYS A 244 9405 11432 9482 1205 108 1017 C
ATOM 238 CD LYS A 244 -39.448 45.794 -3.089 1.00 81.72 C
ANISOU 238 CD LYS A 244 9575 11936 9538 1383 107 996 C
ATOM 239 CE LYS A 244 -38.553 46.607 -4.004 1.00 81.55 C
ANISOU 239 CE LYS A 244 9397 12020 9567 1671 219 1370 C
ATOM 240 NZ LYS A 244 -37.490 47.361 -3.259 1.00 77.22 N
ANISOU 240 NZ LYS A 244 8893 11058 9387 1589 250 1603 N
ATOM 241 N LYS A 245 -41.799 43.138 0.334 1.00 60.37 N
ANISOU 241 N LYS A 245 7322 8633 6984 548 -14 171 N
ATOM 242 CA LYS A 245 -41.978 42.046 1.274 1.00 59.89 C
ANISOU 242 CA LYS A 245 7379 8346 7030 365 16 43 C
ATOM 243 C LYS A 245 -40.854 42.031 2.297 1.00 65.48 C
ANISOU 243 C LYS A 245 8271 8796 7812 320 6 207 C
ATOM 244 O LYS A 245 -39.674 42.237 1.947 1.00 65.46 O
ANISOU 244 O LYS A 245 8287 8765 7818 398 -40 328 O
ATOM 245 CB LYS A 245 -42.049 40.710 0.511 1.00 62.16 C
ANISOU 245 CB LYS A 245 7562 8696 7360 346 16 -199 C
ATOM 246 CG LYS A 245 -43.450 40.358 0.006 1.00 66.63 C
ANISOU 246 CG LYS A 245 7940 9433 7945 338 29 -487 C
ATOM 247 CD LYS A 245 -43.478 39.277 -1.057 1.00 69.42 C
ANISOU 247 CD LYS A 245 8097 9931 8348 398 -21 -804 C
ATOM 248 N VAL A 246 -41.227 41.802 3.577 1.00 61.42 N
ANISOU 248 N VAL A 246 7876 8115 7345 227 56 215 N
ATOM 249 CA VAL A 246 -40.283 41.665 4.710 1.00 59.98 C
ANISOU 249 CA VAL A 246 7861 7739 7190 231 46 329 C
ATOM 250 C VAL A 246 -40.701 40.462 5.553 1.00 62.25 C
ANISOU 250 C VAL A 246 8222 7897 7533 152 174 305 C
ATOM 251 O VAL A 246 -41.806 39.948 5.384 1.00 63.42 O
ANISOU 251 O VAL A 246 8279 8064 7753 76 269 201 O
ATOM 252 CB VAL A 246 -40.122 42.964 5.577 1.00 63.69 C
ANISOU 252 CB VAL A 246 8371 8185 7642 312 -30 412 C
ATOM 253 CG1 VAL A 246 -39.510 44.116 4.775 1.00 62.76 C
ANISOU 253 CG1 VAL A 246 8139 8113 7593 400 -112 486 C
ATOM 254 CG2 VAL A 246 -41.438 43.388 6.251 1.00 63.81 C
ANISOU 254 CG2 VAL A 246 8375 8261 7607 292 14 372 C
ATOM 255 N ALA A 247 -39.831 40.001 6.437 1.00 58.42 N
ANISOU 255 N ALA A 247 7874 7280 7045 191 195 409 N
ATOM 256 CA ALA A 247 -40.161 38.920 7.377 1.00 59.35 C
ANISOU 256 CA ALA A 247 8053 7273 7223 176 367 478 C
ATOM 257 C ALA A 247 -40.091 39.529 8.779 1.00 64.06 C
ANISOU 257 C ALA A 247 8769 7904 7666 326 359 597 C
ATOM 258 O ALA A 247 -39.115 40.233 9.090 1.00 63.28 O
ANISOU 258 O ALA A 247 8734 7835 7474 434 209 602 O
ATOM 259 CB ALA A 247 -39.178 37.772 7.246 1.00 60.04 C
ANISOU 259 CB ALA A 247 8184 7223 7404 156 416 517 C
ATOM 260 N ILE A 248 -41.150 39.352 9.586 1.00 61.05 N
ANISOU 260 N ILE A 248 8386 7538 7271 356 507 663 N
ATOM 261 CA ILE A 248 -41.154 39.891 10.939 1.00 62.11 C
ANISOU 261 CA ILE A 248 8613 7774 7212 559 498 758 C
ATOM 262 C ILE A 248 -41.174 38.767 11.949 1.00 69.96 C
ANISOU 262 C ILE A 248 9672 8714 8195 686 731 970 C
ATOM 263 O ILE A 248 -42.155 38.011 11.999 1.00 72.49 O
ANISOU 263 O ILE A 248 9920 8944 8681 619 963 1065 O
ATOM 264 CB ILE A 248 -42.239 40.981 11.198 1.00 65.24 C
ANISOU 264 CB ILE A 248 8955 8304 7527 579 449 692 C
ATOM 265 CG1 ILE A 248 -42.082 42.152 10.196 1.00 63.29 C
ANISOU 265 CG1 ILE A 248 8623 8103 7320 491 245 535 C
ATOM 266 CG2 ILE A 248 -42.191 41.476 12.685 1.00 66.71 C
ANISOU 266 CG2 ILE A 248 9218 8643 7485 848 421 754 C
ATOM 267 CD1 ILE A 248 -43.046 43.215 10.342 1.00 66.62 C
ANISOU 267 CD1 ILE A 248 8981 8638 7694 504 191 470 C
ATOM 268 N LYS A 249 -40.072 38.643 12.732 1.00 66.30 N
ANISOU 268 N LYS A 249 9319 8301 7570 890 684 1052 N
ATOM 269 CA LYS A 249 -39.897 37.640 13.789 1.00 67.50 C
ANISOU 269 CA LYS A 249 9537 8456 7655 1098 915 1306 C
ATOM 270 C LYS A 249 -40.412 38.217 15.106 1.00 73.40 C
ANISOU 270 C LYS A 249 10316 9449 8122 1404 945 1397 C
ATOM 271 O LYS A 249 -39.933 39.250 15.578 1.00 72.08 O
ANISOU 271 O LYS A 249 10180 9479 7728 1581 701 1233 O
ATOM 272 CB LYS A 249 -38.423 37.188 13.909 1.00 69.17 C
ANISOU 272 CB LYS A 249 9841 8640 7799 1200 844 1335 C
ATOM 273 CG LYS A 249 -38.167 36.019 14.881 1.00 79.21 C
ANISOU 273 CG LYS A 249 11167 9912 9017 1432 1121 1644 C
ATOM 274 N ILE A 250 -41.425 37.554 15.663 1.00 73.26 N
ANISOU 274 N ILE A 250 10257 9415 8164 1475 1252 1642 N
ATOM 275 CA ILE A 250 -42.074 37.870 16.937 1.00 75.22 C
ANISOU 275 CA ILE A 250 10519 9915 8147 1805 1361 1804 C
ATOM 276 C ILE A 250 -41.437 36.972 18.035 1.00 83.63 C
ANISOU 276 C ILE A 250 11647 11098 9032 2182 1586 2128 C
ATOM 277 O ILE A 250 -41.303 35.760 17.843 1.00 83.80 O
ANISOU 277 O ILE A 250 11641 10893 9308 2113 1862 2369 O
ATOM 278 CB ILE A 250 -43.629 37.679 16.845 1.00 78.06 C
ANISOU 278 CB ILE A 250 10769 10179 8711 1674 1597 1916 C
ATOM 279 CG1 ILE A 250 -44.224 38.442 15.641 1.00 75.47 C
ANISOU 279 CG1 ILE A 250 10368 9750 8556 1316 1387 1599 C
ATOM 280 CG2 ILE A 250 -44.338 38.071 18.151 1.00 79.02 C
ANISOU 280 CG2 ILE A 250 10901 10593 8529 2041 1708 2096 C
ATOM 281 CD1 ILE A 250 -44.557 37.602 14.454 1.00 79.21 C
ANISOU 281 CD1 ILE A 250 10726 9923 9447 978 1504 1541 C
ATOM 282 N ILE A 251 -41.014 37.591 19.154 1.00 82.69 N
ANISOU 282 N ILE A 251 11586 11349 8484 2602 1455 2106 N
ATOM 283 CA ILE A 251 -40.435 36.934 20.333 1.00 85.76 C
ANISOU 283 CA ILE A 251 12025 11985 8573 3083 1635 2395 C
ATOM 284 C ILE A 251 -41.268 37.404 21.513 1.00 91.90 C
ANISOU 284 C ILE A 251 12771 13136 9010 3494 1722 2522 C
ATOM 285 O ILE A 251 -41.316 38.606 21.777 1.00 90.80 O
ANISOU 285 O ILE A 251 12620 13244 8634 3601 1397 2185 O
ATOM 286 CB ILE A 251 -38.910 37.253 20.543 1.00 88.17 C
ANISOU 286 CB ILE A 251 12407 12466 8626 3280 1321 2152 C
ATOM 287 CG1 ILE A 251 -38.046 36.798 19.365 1.00 85.83 C
ANISOU 287 CG1 ILE A 251 12143 11816 8651 2882 1219 2025 C
ATOM 288 CG2 ILE A 251 -38.384 36.657 21.832 1.00 91.62 C
ANISOU 288 CG2 ILE A 251 12884 13240 8688 3845 1497 2436 C
ATOM 289 CD1 ILE A 251 -37.548 37.914 18.573 1.00 89.18 C
ANISOU 289 CD1 ILE A 251 12550 12178 9158 2636 820 1590 C
ATOM 290 N SER A 252 -41.936 36.469 22.206 1.00 91.80 N
ANISOU 290 N SER A 252 12718 13154 9007 3738 2173 3011 N
ATOM 291 CA SER A 252 -42.756 36.789 23.379 1.00 94.07 C
ANISOU 291 CA SER A 252 12967 13831 8945 4198 2319 3216 C
ATOM 292 C SER A 252 -41.866 37.130 24.571 1.00 98.41 C
ANISOU 292 C SER A 252 13564 14931 8897 4830 2153 3162 C
ATOM 293 O SER A 252 -40.780 36.557 24.723 1.00 98.14 O
ANISOU 293 O SER A 252 13583 14935 8771 4991 2157 3226 O
ATOM 294 CB SER A 252 -43.686 35.631 23.724 1.00100.96 C
ANISOU 294 CB SER A 252 13749 14540 10071 4296 2902 3812 C
ATOM 295 N LYS A 253 -42.323 38.075 25.400 1.00 95.85 N
ANISOU 295 N LYS A 253 13203 15047 8168 5198 1985 3000 N
ATOM 296 CA LYS A 253 -41.591 38.523 26.586 1.00110.48 C
ANISOU 296 CA LYS A 253 15051 17507 9421 5868 1775 2848 C
ATOM 297 C LYS A 253 -41.877 37.651 27.809 1.00138.55 C
ANISOU 297 C LYS A 253 18579 21461 12601 6538 2230 3445 C
ATOM 298 O LYS A 253 -41.255 36.600 27.978 1.00102.56 O
ANISOU 298 O LYS A 253 14054 16874 8040 6724 2512 3820 O
ATOM 299 CB LYS A 253 -41.879 39.999 26.872 1.00111.56 C
ANISOU 299 CB LYS A 253 15115 17944 9327 5971 1334 2310 C
ATOM 300 CG LYS A 253 -41.354 40.928 25.786 1.00111.96 C
ANISOU 300 CG LYS A 253 15156 17654 9729 5424 887 1739 C
ATOM 301 CD LYS A 253 -41.708 42.352 26.097 1.00119.31 C
ANISOU 301 CD LYS A 253 15973 18846 10515 5543 503 1247 C
ATOM 302 CE LYS A 253 -40.648 43.304 25.631 1.00125.03 C
ANISOU 302 CE LYS A 253 16624 19475 11406 5386 16 644 C
ATOM 303 NZ LYS A 253 -40.993 44.706 25.982 1.00131.69 N
ANISOU 303 NZ LYS A 253 17304 20539 12194 5513 -348 144 N
ATOM 304 N ASN A 269 -31.211 39.534 26.284 1.00110.13 N
ANISOU 304 N ASN A 269 15018 17836 8989 6559 -517 254 N
ATOM 305 CA ASN A 269 -30.808 38.538 25.288 1.00107.23 C
ANISOU 305 CA ASN A 269 14811 16971 8963 6073 -272 614 C
ATOM 306 C ASN A 269 -31.285 38.894 23.859 1.00108.13 C
ANISOU 306 C ASN A 269 14941 16480 9661 5306 -294 572 C
ATOM 307 O ASN A 269 -30.620 38.535 22.875 1.00105.64 O
ANISOU 307 O ASN A 269 14690 15759 9688 4892 -306 586 O
ATOM 308 CB ASN A 269 -31.305 37.148 25.693 1.00108.70 C
ANISOU 308 CB ASN A 269 15121 17240 8941 6266 266 1324 C
ATOM 309 CG ASN A 269 -30.515 36.008 25.094 1.00131.13 C
ANISOU 309 CG ASN A 269 18084 19749 11990 6029 475 1626 C
ATOM 310 OD1 ASN A 269 -29.359 35.750 25.462 1.00123.63 O
ANISOU 310 OD1 ASN A 269 17152 18985 10837 6327 355 1513 O
ATOM 311 ND2 ASN A 269 -31.139 35.275 24.183 1.00123.99 N
ANISOU 311 ND2 ASN A 269 17247 18362 11500 5512 793 1996 N
ATOM 312 N VAL A 270 -32.452 39.571 23.749 1.00103.57 N
ANISOU 312 N VAL A 270 14302 15879 9169 5154 -287 538 N
ATOM 313 CA VAL A 270 -33.008 39.999 22.460 1.00 98.82 C
ANISOU 313 CA VAL A 270 13694 14795 9057 4511 -310 490 C
ATOM 314 C VAL A 270 -32.282 41.286 22.074 1.00102.55 C
ANISOU 314 C VAL A 270 14015 15162 9789 4393 -759 -87 C
ATOM 315 O VAL A 270 -31.925 41.453 20.906 1.00 99.60 O
ANISOU 315 O VAL A 270 13641 14372 9829 3932 -824 -147 O
ATOM 316 CB VAL A 270 -34.559 40.117 22.452 1.00101.52 C
ANISOU 316 CB VAL A 270 14029 15132 9411 4387 -90 717 C
ATOM 317 CG1 VAL A 270 -35.082 40.550 21.088 1.00 97.40 C
ANISOU 317 CG1 VAL A 270 13487 14163 9359 3771 -130 642 C
ATOM 318 CG2 VAL A 270 -35.206 38.797 22.854 1.00102.96 C
ANISOU 318 CG2 VAL A 270 14312 15356 9452 4515 394 1309 C
ATOM 319 N GLU A 271 -31.973 42.141 23.076 1.00101.71 N
ANISOU 319 N GLU A 271 13750 15440 9455 4858 -1062 -514 N
ATOM 320 CA GLU A 271 -31.216 43.381 22.883 1.00101.19 C
ANISOU 320 CA GLU A 271 13467 15272 9709 4823 -1491 -1112 C
ATOM 321 C GLU A 271 -29.797 43.055 22.365 1.00102.35 C
ANISOU 321 C GLU A 271 13631 15176 10081 4704 -1601 -1216 C
ATOM 322 O GLU A 271 -29.346 43.688 21.400 1.00100.30 O
ANISOU 322 O GLU A 271 13273 14512 10324 4323 -1750 -1408 O
ATOM 323 CB GLU A 271 -31.161 44.196 24.186 1.00106.69 C
ANISOU 323 CB GLU A 271 13957 16480 10101 5423 -1789 -1587 C
ATOM 324 N THR A 272 -29.133 42.028 22.968 1.00 97.43 N
ANISOU 324 N THR A 272 13132 14795 9092 5036 -1489 -1035 N
ATOM 325 CA THR A 272 -27.803 41.542 22.571 1.00 94.88 C
ANISOU 325 CA THR A 272 12855 14281 8914 4959 -1557 -1082 C
ATOM 326 C THR A 272 -27.822 40.989 21.140 1.00 90.63 C
ANISOU 326 C THR A 272 12460 13208 8768 4331 -1344 -734 C
ATOM 327 O THR A 272 -26.856 41.178 20.394 1.00 89.05 O
ANISOU 327 O THR A 272 12213 12695 8926 4086 -1495 -903 O
ATOM 328 CB THR A 272 -27.287 40.487 23.565 1.00104.82 C
ANISOU 328 CB THR A 272 14233 15947 9648 5467 -1414 -869 C
ATOM 329 N GLU A 273 -28.925 40.308 20.764 1.00 81.88 N
ANISOU 329 N GLU A 273 11495 12007 7609 4098 -996 -270 N
ATOM 330 CA GLU A 273 -29.120 39.746 19.432 1.00 76.21 C
ANISOU 330 CA GLU A 273 10880 10848 7230 3551 -797 19 C
ATOM 331 C GLU A 273 -29.214 40.883 18.405 1.00 75.17 C
ANISOU 331 C GLU A 273 10609 10413 7538 3178 -998 -239 C
ATOM 332 O GLU A 273 -28.626 40.763 17.335 1.00 72.44 O
ANISOU 332 O GLU A 273 10277 9746 7501 2853 -1010 -209 O
ATOM 333 CB GLU A 273 -30.368 38.843 19.405 1.00 77.36 C
ANISOU 333 CB GLU A 273 11138 10988 7268 3446 -407 482 C
ATOM 334 CG GLU A 273 -30.574 38.119 18.085 1.00 85.05 C
ANISOU 334 CG GLU A 273 12185 11553 8579 2942 -212 725 C
ATOM 335 CD GLU A 273 -31.841 37.306 17.888 1.00112.50 C
ANISOU 335 CD GLU A 273 15707 14938 12099 2781 155 1104 C
ATOM 336 OE1 GLU A 273 -32.457 36.890 18.899 1.00108.51 O
ANISOU 336 OE1 GLU A 273 15219 14676 11333 3100 367 1335 O
ATOM 337 OE2 GLU A 273 -32.195 37.053 16.710 1.00100.64 O
ANISOU 337 OE2 GLU A 273 14200 13128 10911 2363 237 1165 O
ATOM 338 N ILE A 274 -29.938 41.987 18.737 1.00 71.20 N
ANISOU 338 N ILE A 274 9959 10028 7064 3257 -1142 -475 N
ATOM 339 CA ILE A 274 -30.113 43.171 17.882 1.00 68.58 C
ANISOU 339 CA ILE A 274 9458 9433 7167 2963 -1306 -694 C
ATOM 340 C ILE A 274 -28.798 43.899 17.714 1.00 71.42 C
ANISOU 340 C ILE A 274 9643 9632 7861 3005 -1593 -1061 C
ATOM 341 O ILE A 274 -28.444 44.268 16.604 1.00 67.52 O
ANISOU 341 O ILE A 274 9079 8795 7781 2686 -1607 -1039 O
ATOM 342 CB ILE A 274 -31.286 44.077 18.386 1.00 73.03 C
ANISOU 342 CB ILE A 274 9904 10174 7671 3061 -1360 -831 C
ATOM 343 CG1 ILE A 274 -32.620 43.556 17.864 1.00 72.43 C
ANISOU 343 CG1 ILE A 274 9957 10038 7524 2791 -1061 -449 C
ATOM 344 CG2 ILE A 274 -31.148 45.545 17.981 1.00 72.78 C
ANISOU 344 CG2 ILE A 274 9610 9951 8093 2951 -1616 -1198 C
ATOM 345 CD1 ILE A 274 -33.291 42.761 18.772 1.00 83.76 C
ANISOU 345 CD1 ILE A 274 11512 11758 8555 3042 -856 -215 C
ATOM 346 N GLU A 275 -28.064 44.062 18.818 1.00 74.05 N
ANISOU 346 N GLU A 275 9888 10231 8015 3433 -1806 -1388 N
ATOM 347 CA GLU A 275 -26.746 44.692 18.894 1.00 75.82 C
ANISOU 347 CA GLU A 275 9908 10339 8561 3556 -2103 -1815 C
ATOM 348 C GLU A 275 -25.741 43.962 17.994 1.00 79.11 C
ANISOU 348 C GLU A 275 10443 10453 9162 3302 -2012 -1603 C
ATOM 349 O GLU A 275 -25.012 44.629 17.256 1.00 78.27 O
ANISOU 349 O GLU A 275 10163 10012 9565 3119 -2138 -1770 O
ATOM 350 CB GLU A 275 -26.261 44.766 20.355 1.00 80.87 C
ANISOU 350 CB GLU A 275 10454 11430 8845 4139 -2330 -2200 C
ATOM 351 N ILE A 276 -25.746 42.602 18.001 1.00 75.90 N
ANISOU 351 N ILE A 276 10311 10138 8390 3284 -1766 -1210 N
ATOM 352 CA ILE A 276 -24.873 41.811 17.130 1.00 74.42 C
ANISOU 352 CA ILE A 276 10247 9680 8348 3038 -1665 -994 C
ATOM 353 C ILE A 276 -25.288 42.017 15.658 1.00 77.99 C
ANISOU 353 C ILE A 276 10693 9769 9170 2561 -1536 -772 C
ATOM 354 O ILE A 276 -24.498 42.533 14.872 1.00 77.70 O
ANISOU 354 O ILE A 276 10532 9449 9540 2399 -1637 -869 O
ATOM 355 CB ILE A 276 -24.810 40.317 17.542 1.00 77.58 C
ANISOU 355 CB ILE A 276 10901 10258 8317 3157 -1426 -645 C
ATOM 356 N LEU A 277 -26.548 41.720 15.325 1.00 74.88 N
ANISOU 356 N LEU A 277 10394 9406 8650 2382 -1320 -499 N
ATOM 357 CA LEU A 277 -27.114 41.832 13.985 1.00 73.83 C
ANISOU 357 CA LEU A 277 10253 9030 8769 1998 -1188 -294 C
ATOM 358 C LEU A 277 -27.043 43.210 13.329 1.00 77.39 C
ANISOU 358 C LEU A 277 10466 9281 9659 1883 -1333 -473 C
ATOM 359 O LEU A 277 -26.964 43.282 12.096 1.00 75.74 O
ANISOU 359 O LEU A 277 10225 8857 9696 1631 -1249 -305 O
ATOM 360 CB LEU A 277 -28.539 41.258 13.942 1.00 74.42 C
ANISOU 360 CB LEU A 277 10443 9216 8618 1889 -950 -37 C
ATOM 361 CG LEU A 277 -28.658 39.712 13.873 1.00 80.79 C
ANISOU 361 CG LEU A 277 11445 10031 9220 1823 -696 273 C
ATOM 362 CD1 LEU A 277 -29.954 39.211 14.500 1.00 82.33 C
ANISOU 362 CD1 LEU A 277 11704 10397 9180 1895 -481 458 C
ATOM 363 CD2 LEU A 277 -28.510 39.192 12.446 1.00 81.60 C
ANISOU 363 CD2 LEU A 277 11570 9893 9542 1488 -596 425 C
ATOM 364 N LYS A 278 -27.063 44.294 14.138 1.00 75.05 N
ANISOU 364 N LYS A 278 9973 9063 9481 2098 -1539 -808 N
ATOM 365 CA LYS A 278 -26.953 45.678 13.656 1.00 74.74 C
ANISOU 365 CA LYS A 278 9644 8796 9958 2027 -1667 -999 C
ATOM 366 C LYS A 278 -25.536 45.957 13.136 1.00 80.80 C
ANISOU 366 C LYS A 278 10263 9274 11164 2004 -1770 -1101 C
ATOM 367 O LYS A 278 -25.377 46.668 12.139 1.00 81.42 O
ANISOU 367 O LYS A 278 10160 9073 11702 1836 -1726 -1011 O
ATOM 368 CB LYS A 278 -27.303 46.688 14.770 1.00 78.18 C
ANISOU 368 CB LYS A 278 9875 9394 10437 2293 -1879 -1396 C
ATOM 369 CG LYS A 278 -28.782 47.060 14.836 1.00 83.13 C
ANISOU 369 CG LYS A 278 10521 10164 10901 2229 -1780 -1296 C
ATOM 370 N LYS A 279 -24.515 45.387 13.809 1.00 77.45 N
ANISOU 370 N LYS A 279 9904 8925 10599 2197 -1888 -1264 N
ATOM 371 CA LYS A 279 -23.107 45.590 13.498 1.00 77.59 C
ANISOU 371 CA LYS A 279 9779 8685 11016 2214 -2006 -1407 C
ATOM 372 C LYS A 279 -22.542 44.649 12.430 1.00 80.79 C
ANISOU 372 C LYS A 279 10374 8933 11389 1985 -1824 -1036 C
ATOM 373 O LYS A 279 -21.483 44.948 11.859 1.00 81.83 O
ANISOU 373 O LYS A 279 10363 8789 11938 1936 -1869 -1064 O
ATOM 374 CB LYS A 279 -22.270 45.523 14.786 1.00 82.40 C
ANISOU 374 CB LYS A 279 10329 9485 11493 2579 -2256 -1833 C
ATOM 375 N LEU A 280 -23.193 43.499 12.189 1.00 74.71 N
ANISOU 375 N LEU A 280 9894 8326 10165 1862 -1622 -710 N
ATOM 376 CA LEU A 280 -22.690 42.560 11.185 1.00 72.37 C
ANISOU 376 CA LEU A 280 9755 7907 9836 1663 -1469 -409 C
ATOM 377 C LEU A 280 -23.092 43.026 9.789 1.00 74.09 C
ANISOU 377 C LEU A 280 9872 7951 10327 1427 -1334 -171 C
ATOM 378 O LEU A 280 -24.118 43.692 9.618 1.00 74.19 O
ANISOU 378 O LEU A 280 9796 8009 10384 1376 -1285 -140 O
ATOM 379 CB LEU A 280 -23.148 41.114 11.440 1.00 71.77 C
ANISOU 379 CB LEU A 280 9967 8031 9271 1636 -1302 -190 C
ATOM 380 CG LEU A 280 -22.800 40.463 12.788 1.00 78.20 C
ANISOU 380 CG LEU A 280 10903 9074 9735 1920 -1360 -310 C
ATOM 381 CD1 LEU A 280 -23.577 39.187 12.964 1.00 78.19 C
ANISOU 381 CD1 LEU A 280 11125 9224 9361 1878 -1118 -17 C
ATOM 382 CD2 LEU A 280 -21.310 40.159 12.917 1.00 81.11 C
ANISOU 382 CD2 LEU A 280 11279 9352 10188 2028 -1483 -430 C
ATOM 383 N ASN A 281 -22.253 42.723 8.799 1.00 67.79 N
ANISOU 383 N ASN A 281 9073 6980 9703 1320 -1273 0 N
ATOM 384 CA ASN A 281 -22.491 43.131 7.425 1.00 65.45 C
ANISOU 384 CA ASN A 281 8663 6576 9630 1178 -1133 254 C
ATOM 385 C ASN A 281 -21.828 42.160 6.445 1.00 64.68 C
ANISOU 385 C ASN A 281 8689 6448 9437 1079 -1030 482 C
ATOM 386 O ASN A 281 -20.664 42.329 6.057 1.00 63.50 O
ANISOU 386 O ASN A 281 8451 6108 9568 1111 -1060 512 O
ATOM 387 CB ASN A 281 -22.053 44.588 7.204 1.00 66.23 C
ANISOU 387 CB ASN A 281 8430 6424 10309 1249 -1191 180 C
ATOM 388 CG ASN A 281 -22.419 45.128 5.850 1.00 89.95 C
ANISOU 388 CG ASN A 281 11286 9366 13527 1174 -1007 497 C
ATOM 389 OD1 ASN A 281 -23.412 44.729 5.241 1.00 86.80 O
ANISOU 389 OD1 ASN A 281 10994 9169 12815 1087 -878 681 O
ATOM 390 ND2 ASN A 281 -21.624 46.059 5.348 1.00 83.70 N
ANISOU 390 ND2 ASN A 281 10211 8296 13294 1237 -977 570 N
ATOM 391 N HIS A 282 -22.580 41.120 6.066 1.00 58.36 N
ANISOU 391 N HIS A 282 8073 5829 8271 967 -909 618 N
ATOM 392 CA HIS A 282 -22.109 40.109 5.137 1.00 56.78 C
ANISOU 392 CA HIS A 282 7976 5640 7959 880 -822 785 C
ATOM 393 C HIS A 282 -23.271 39.593 4.313 1.00 60.46 C
ANISOU 393 C HIS A 282 8472 6291 8209 774 -688 903 C
ATOM 394 O HIS A 282 -24.387 39.507 4.825 1.00 58.13 O
ANISOU 394 O HIS A 282 8220 6114 7753 742 -655 840 O
ATOM 395 CB HIS A 282 -21.439 38.987 5.899 1.00 57.76 C
ANISOU 395 CB HIS A 282 8298 5758 7891 893 -863 709 C
ATOM 396 CG HIS A 282 -20.607 38.083 5.059 1.00 60.99 C
ANISOU 396 CG HIS A 282 8779 6117 8277 825 -816 834 C
ATOM 397 ND1 HIS A 282 -21.141 36.944 4.487 1.00 62.50 N
ANISOU 397 ND1 HIS A 282 9072 6422 8254 711 -703 917 N
ATOM 398 CD2 HIS A 282 -19.282 38.124 4.798 1.00 63.14 C
ANISOU 398 CD2 HIS A 282 9023 6233 8734 867 -877 855 C
ATOM 399 CE1 HIS A 282 -20.130 36.334 3.886 1.00 61.58 C
ANISOU 399 CE1 HIS A 282 8993 6235 8172 692 -706 982 C
ATOM 400 NE2 HIS A 282 -18.991 37.003 4.043 1.00 62.10 N
ANISOU 400 NE2 HIS A 282 8996 6141 8457 780 -802 969 N
ATOM 401 N PRO A 283 -23.056 39.272 3.016 1.00 59.95 N
ANISOU 401 N PRO A 283 8359 6278 8142 749 -613 1054 N
ATOM 402 CA PRO A 283 -24.177 38.784 2.187 1.00 60.03 C
ANISOU 402 CA PRO A 283 8351 6505 7951 689 -517 1087 C
ATOM 403 C PRO A 283 -24.756 37.424 2.606 1.00 64.31 C
ANISOU 403 C PRO A 283 9046 7109 8280 574 -477 974 C
ATOM 404 O PRO A 283 -25.840 37.060 2.136 1.00 65.48 O
ANISOU 404 O PRO A 283 9148 7408 8323 521 -411 927 O
ATOM 405 CB PRO A 283 -23.569 38.738 0.783 1.00 61.71 C
ANISOU 405 CB PRO A 283 8458 6793 8197 763 -472 1243 C
ATOM 406 CG PRO A 283 -22.115 38.518 1.017 1.00 65.91 C
ANISOU 406 CG PRO A 283 9050 7123 8870 784 -530 1278 C
ATOM 407 CD PRO A 283 -21.808 39.350 2.226 1.00 61.55 C
ANISOU 407 CD PRO A 283 8493 6372 8522 808 -615 1185 C
ATOM 408 N CYS A 284 -24.033 36.665 3.463 1.00 58.83 N
ANISOU 408 N CYS A 284 8505 6291 7559 555 -503 934 N
ATOM 409 CA CYS A 284 -24.479 35.356 3.948 1.00 57.52 C
ANISOU 409 CA CYS A 284 8454 6130 7269 470 -416 887 C
ATOM 410 C CYS A 284 -24.893 35.389 5.414 1.00 56.81 C
ANISOU 410 C CYS A 284 8460 6023 7101 523 -393 862 C
ATOM 411 O CYS A 284 -24.993 34.358 6.061 1.00 56.07 O
ANISOU 411 O CYS A 284 8464 5900 6938 511 -292 890 O
ATOM 412 CB CYS A 284 -23.453 34.264 3.651 1.00 57.95 C
ANISOU 412 CB CYS A 284 8589 6098 7332 435 -409 910 C
ATOM 413 SG CYS A 284 -22.976 34.162 1.906 1.00 61.86 S
ANISOU 413 SG CYS A 284 8955 6683 7866 433 -437 935 S
ATOM 414 N ILE A 285 -25.177 36.582 5.914 1.00 52.63 N
ANISOU 414 N ILE A 285 7875 5527 6595 610 -471 819 N
ATOM 415 CA ILE A 285 -25.686 36.819 7.262 1.00 53.84 C
ANISOU 415 CA ILE A 285 8083 5735 6639 716 -472 768 C
ATOM 416 C ILE A 285 -26.917 37.712 7.146 1.00 58.97 C
ANISOU 416 C ILE A 285 8624 6479 7303 693 -462 734 C
ATOM 417 O ILE A 285 -26.800 38.792 6.578 1.00 60.36 O
ANISOU 417 O ILE A 285 8669 6635 7628 704 -544 712 O
ATOM 418 CB ILE A 285 -24.605 37.388 8.239 1.00 57.06 C
ANISOU 418 CB ILE A 285 8516 6106 7060 905 -626 666 C
ATOM 419 CG1 ILE A 285 -23.534 36.319 8.541 1.00 56.78 C
ANISOU 419 CG1 ILE A 285 8615 6013 6947 948 -609 711 C
ATOM 420 CG2 ILE A 285 -25.259 37.871 9.556 1.00 58.85 C
ANISOU 420 CG2 ILE A 285 8748 6473 7142 1078 -656 570 C
ATOM 421 CD1 ILE A 285 -22.284 36.841 8.898 1.00 61.74 C
ANISOU 421 CD1 ILE A 285 9219 6570 7668 1083 -778 592 C
ATOM 422 N ILE A 286 -28.085 37.278 7.673 1.00 55.37 N
ANISOU 422 N ILE A 286 8202 6110 6725 672 -340 753 N
ATOM 423 CA ILE A 286 -29.344 38.064 7.668 1.00 55.41 C
ANISOU 423 CA ILE A 286 8118 6214 6721 652 -323 716 C
ATOM 424 C ILE A 286 -29.185 39.504 8.268 1.00 61.53 C
ANISOU 424 C ILE A 286 8815 7013 7549 789 -479 610 C
ATOM 425 O ILE A 286 -28.401 39.702 9.206 1.00 62.94 O
ANISOU 425 O ILE A 286 9031 7183 7702 950 -584 526 O
ATOM 426 CB ILE A 286 -30.503 37.249 8.335 1.00 58.49 C
ANISOU 426 CB ILE A 286 8561 6663 7000 634 -145 772 C
ATOM 427 CG1 ILE A 286 -31.876 37.621 7.787 1.00 58.26 C
ANISOU 427 CG1 ILE A 286 8424 6709 7005 528 -87 737 C
ATOM 428 CG2 ILE A 286 -30.458 37.255 9.865 1.00 59.27 C
ANISOU 428 CG2 ILE A 286 8753 6837 6931 844 -130 800 C
ATOM 429 CD1 ILE A 286 -32.147 37.041 6.446 1.00 64.04 C
ANISOU 429 CD1 ILE A 286 9065 7429 7840 374 -36 705 C
ATOM 430 N LYS A 287 -29.894 40.493 7.712 1.00 57.96 N
ANISOU 430 N LYS A 287 8229 6598 7197 744 -499 590 N
ATOM 431 CA LYS A 287 -29.822 41.887 8.182 1.00 58.20 C
ANISOU 431 CA LYS A 287 8131 6611 7372 856 -633 474 C
ATOM 432 C LYS A 287 -31.103 42.354 8.842 1.00 61.78 C
ANISOU 432 C LYS A 287 8562 7195 7715 884 -611 417 C
ATOM 433 O LYS A 287 -32.190 42.079 8.334 1.00 60.52 O
ANISOU 433 O LYS A 287 8404 7113 7478 767 -490 493 O
ATOM 434 CB LYS A 287 -29.475 42.833 7.023 1.00 60.35 C
ANISOU 434 CB LYS A 287 8220 6786 7925 818 -655 538 C
ATOM 435 CG LYS A 287 -27.984 42.965 6.746 1.00 75.72 C
ANISOU 435 CG LYS A 287 10120 8560 10092 868 -728 552 C
ATOM 436 CD LYS A 287 -27.736 43.483 5.336 1.00 78.13 C
ANISOU 436 CD LYS A 287 10265 8809 10613 841 -655 736 C
ATOM 437 CE LYS A 287 -26.275 43.542 4.975 1.00 83.63 C
ANISOU 437 CE LYS A 287 10902 9318 11557 895 -696 790 C
ATOM 438 NZ LYS A 287 -25.749 42.227 4.520 1.00 91.77 N
ANISOU 438 NZ LYS A 287 12103 10393 12373 833 -655 862 N
ATOM 439 N ILE A 288 -30.972 43.076 9.963 1.00 60.71 N
ANISOU 439 N ILE A 288 8386 7100 7582 1059 -740 249 N
ATOM 440 CA ILE A 288 -32.107 43.666 10.688 1.00 61.89 C
ANISOU 440 CA ILE A 288 8495 7390 7630 1126 -747 168 C
ATOM 441 C ILE A 288 -32.477 44.896 9.881 1.00 64.53 C
ANISOU 441 C ILE A 288 8631 7643 8244 1043 -783 150 C
ATOM 442 O ILE A 288 -31.591 45.646 9.463 1.00 63.89 O
ANISOU 442 O ILE A 288 8398 7399 8477 1066 -873 106 O
ATOM 443 CB ILE A 288 -31.769 44.065 12.173 1.00 67.21 C
ANISOU 443 CB ILE A 288 9151 8184 8201 1406 -907 -59 C
ATOM 444 CG1 ILE A 288 -31.025 42.952 12.905 1.00 70.70 C
ANISOU 444 CG1 ILE A 288 9757 8705 8401 1556 -881 -21 C
ATOM 445 CG2 ILE A 288 -33.014 44.497 12.983 1.00 66.63 C
ANISOU 445 CG2 ILE A 288 9058 8307 7951 1507 -896 -123 C
ATOM 446 CD1 ILE A 288 -31.912 41.869 13.657 1.00 87.34 C
ANISOU 446 CD1 ILE A 288 12029 11006 10150 1642 -676 166 C
ATOM 447 N LYS A 289 -33.773 45.086 9.645 1.00 60.51 N
ANISOU 447 N LYS A 289 8106 7235 7651 959 -691 207 N
ATOM 448 CA LYS A 289 -34.296 46.232 8.910 1.00 59.70 C
ANISOU 448 CA LYS A 289 7814 7092 7776 905 -692 227 C
ATOM 449 C LYS A 289 -34.966 47.184 9.892 1.00 64.17 C
ANISOU 449 C LYS A 289 8288 7727 8366 1012 -789 48 C
ATOM 450 O LYS A 289 -34.933 48.392 9.678 1.00 64.76 O
ANISOU 450 O LYS A 289 8151 7701 8755 1038 -855 -17 O
ATOM 451 CB LYS A 289 -35.285 45.785 7.813 1.00 60.46 C
ANISOU 451 CB LYS A 289 7934 7285 7752 752 -530 394 C
ATOM 452 CG LYS A 289 -34.640 45.188 6.577 1.00 58.93 C
ANISOU 452 CG LYS A 289 7742 7054 7595 686 -460 537 C
ATOM 453 CD LYS A 289 -35.691 44.841 5.543 1.00 73.42 C
ANISOU 453 CD LYS A 289 9548 9045 9303 597 -339 614 C
ATOM 454 CE LYS A 289 -35.419 45.487 4.205 1.00 90.56 C
ANISOU 454 CE LYS A 289 11547 11250 11610 649 -298 761 C
ATOM 455 NZ LYS A 289 -35.828 46.920 4.168 1.00105.26 N
ANISOU 455 NZ LYS A 289 13228 13098 13669 718 -297 812 N
ATOM 456 N ASN A 290 -35.571 46.632 10.971 1.00 61.19 N
ANISOU 456 N ASN A 290 8051 7521 7678 1095 -780 -14 N
ATOM 457 CA ASN A 290 -36.279 47.370 12.029 1.00 61.80 C
ANISOU 457 CA ASN A 290 8064 7733 7682 1241 -871 -192 C
ATOM 458 C ASN A 290 -36.477 46.533 13.294 1.00 65.69 C
ANISOU 458 C ASN A 290 8722 8436 7802 1430 -848 -213 C
ATOM 459 O ASN A 290 -36.309 45.313 13.277 1.00 65.36 O
ANISOU 459 O ASN A 290 8846 8409 7578 1404 -710 -41 O
ATOM 460 CB ASN A 290 -37.642 47.889 11.516 1.00 61.93 C
ANISOU 460 CB ASN A 290 8022 7801 7709 1107 -776 -113 C
ATOM 461 CG ASN A 290 -38.010 49.276 11.960 1.00 81.12 C
ANISOU 461 CG ASN A 290 10251 10234 10338 1199 -912 -310 C
ATOM 462 OD1 ASN A 290 -37.472 49.820 12.931 1.00 88.15 O
ANISOU 462 OD1 ASN A 290 11044 11148 11303 1402 -1095 -568 O
ATOM 463 ND2 ASN A 290 -38.961 49.868 11.269 1.00 65.21 N
ANISOU 463 ND2 ASN A 290 8148 8214 8417 1071 -831 -220 N
ATOM 464 N PHE A 291 -36.845 47.197 14.396 1.00 63.42 N
ANISOU 464 N PHE A 291 8365 8323 7410 1653 -968 -413 N
ATOM 465 CA PHE A 291 -37.086 46.550 15.686 1.00 63.65 C
ANISOU 465 CA PHE A 291 8514 8623 7048 1927 -935 -411 C
ATOM 466 C PHE A 291 -38.147 47.307 16.496 1.00 64.99 C
ANISOU 466 C PHE A 291 8604 9006 7082 2085 -987 -541 C
ATOM 467 O PHE A 291 -38.120 48.540 16.565 1.00 62.86 O
ANISOU 467 O PHE A 291 8133 8707 7044 2126 -1187 -816 O
ATOM 468 CB PHE A 291 -35.767 46.379 16.474 1.00 67.29 C
ANISOU 468 CB PHE A 291 8966 9164 7436 2213 -1101 -599 C
ATOM 469 CG PHE A 291 -35.951 45.912 17.903 1.00 72.56 C
ANISOU 469 CG PHE A 291 9710 10193 7665 2610 -1088 -618 C
ATOM 470 CD1 PHE A 291 -36.217 44.573 18.188 1.00 76.55 C
ANISOU 470 CD1 PHE A 291 10417 10801 7869 2665 -817 -268 C
ATOM 471 CD2 PHE A 291 -35.900 46.820 18.965 1.00 77.59 C
ANISOU 471 CD2 PHE A 291 10187 11086 8207 2964 -1330 -980 C
ATOM 472 CE1 PHE A 291 -36.431 44.151 19.511 1.00 80.26 C
ANISOU 472 CE1 PHE A 291 10939 11638 7919 3091 -751 -207 C
ATOM 473 CE2 PHE A 291 -36.113 46.396 20.285 1.00 83.00 C
ANISOU 473 CE2 PHE A 291 10930 12187 8420 3405 -1305 -976 C
ATOM 474 CZ PHE A 291 -36.369 45.065 20.549 1.00 81.61 C
ANISOU 474 CZ PHE A 291 10966 12122 7919 3479 -999 -555 C
ATOM 475 N PHE A 292 -39.062 46.545 17.122 1.00 62.54 N
ANISOU 475 N PHE A 292 8432 8898 6433 2187 -792 -333 N
ATOM 476 CA PHE A 292 -40.139 47.050 17.976 1.00 63.63 C
ANISOU 476 CA PHE A 292 8526 9282 6367 2371 -795 -393 C
ATOM 477 C PHE A 292 -40.150 46.336 19.329 1.00 74.32 C
ANISOU 477 C PHE A 292 9972 10985 7283 2796 -713 -302 C
ATOM 478 O PHE A 292 -40.291 45.107 19.412 1.00 73.54 O
ANISOU 478 O PHE A 292 10025 10894 7022 2808 -439 43 O
ATOM 479 CB PHE A 292 -41.498 46.929 17.284 1.00 63.13 C
ANISOU 479 CB PHE A 292 8500 9122 6364 2078 -586 -174 C
ATOM 480 CG PHE A 292 -41.580 47.709 15.984 1.00 62.28 C
ANISOU 480 CG PHE A 292 8281 8759 6624 1744 -656 -246 C
ATOM 481 CD1 PHE A 292 -41.921 49.062 15.982 1.00 63.68 C
ANISOU 481 CD1 PHE A 292 8278 8939 6980 1747 -827 -472 C
ATOM 482 CD2 PHE A 292 -41.312 47.093 14.762 1.00 61.03 C
ANISOU 482 CD2 PHE A 292 8173 8380 6634 1464 -537 -77 C
ATOM 483 CE1 PHE A 292 -41.970 49.784 14.786 1.00 61.98 C
ANISOU 483 CE1 PHE A 292 7940 8504 7107 1491 -845 -472 C
ATOM 484 CE2 PHE A 292 -41.368 47.822 13.568 1.00 61.51 C
ANISOU 484 CE2 PHE A 292 8114 8273 6983 1236 -578 -102 C
ATOM 485 CZ PHE A 292 -41.685 49.165 13.591 1.00 59.07 C
ANISOU 485 CZ PHE A 292 7631 7963 6851 1259 -716 -272 C
ATOM 486 N ASP A 293 -39.953 47.125 20.387 1.00 76.63 N
ANISOU 486 N ASP A 293 10136 11571 7407 3181 -952 -625 N
ATOM 487 CA ASP A 293 -39.961 46.674 21.774 1.00 81.31 C
ANISOU 487 CA ASP A 293 10768 12605 7523 3702 -917 -591 C
ATOM 488 C ASP A 293 -41.348 47.029 22.332 1.00 89.33 C
ANISOU 488 C ASP A 293 11760 13848 8336 3823 -824 -518 C
ATOM 489 O ASP A 293 -41.538 48.131 22.867 1.00 91.86 O
ANISOU 489 O ASP A 293 11908 14367 8627 4028 -1083 -892 O
ATOM 490 CB ASP A 293 -38.834 47.387 22.551 1.00 85.80 C
ANISOU 490 CB ASP A 293 11166 13401 8032 4099 -1285 -1081 C
ATOM 491 CG ASP A 293 -38.603 46.955 23.991 1.00101.00 C
ANISOU 491 CG ASP A 293 13101 15868 9406 4742 -1297 -1105 C
ATOM 492 OD1 ASP A 293 -39.329 46.053 24.472 1.00101.87 O
ANISOU 492 OD1 ASP A 293 13362 16180 9164 4910 -968 -659 O
ATOM 493 OD2 ASP A 293 -37.695 47.524 24.640 1.00108.86 O
ANISOU 493 OD2 ASP A 293 13927 17094 10342 5108 -1626 -1572 O
ATOM 494 N ALA A 294 -42.332 46.113 22.129 1.00 84.84 N
ANISOU 494 N ALA A 294 11334 13206 7695 3666 -452 -55 N
ATOM 495 CA ALA A 294 -43.741 46.242 22.542 1.00 84.86 C
ANISOU 495 CA ALA A 294 11336 13363 7544 3726 -280 115 C
ATOM 496 C ALA A 294 -44.072 45.220 23.659 1.00 90.95 C
ANISOU 496 C ALA A 294 12195 14464 7897 4175 33 514 C
ATOM 497 O ALA A 294 -43.171 44.883 24.428 1.00 92.79 O
ANISOU 497 O ALA A 294 12439 14967 7851 4589 -18 492 O
ATOM 498 CB ALA A 294 -44.628 46.008 21.338 1.00 82.65 C
ANISOU 498 CB ALA A 294 11102 12695 7606 3189 -80 323 C
ATOM 499 N GLU A 295 -45.333 44.700 23.740 1.00 86.85 N
ANISOU 499 N GLU A 295 11720 13921 7358 4117 379 899 N
ATOM 500 CA GLU A 295 -45.711 43.669 24.727 1.00 89.73 C
ANISOU 500 CA GLU A 295 12137 14540 7415 4538 764 1381 C
ATOM 501 C GLU A 295 -44.950 42.364 24.394 1.00 93.84 C
ANISOU 501 C GLU A 295 12750 14829 8077 4457 1017 1705 C
ATOM 502 O GLU A 295 -44.858 41.440 25.213 1.00 96.98 O
ANISOU 502 O GLU A 295 13176 15430 8240 4860 1326 2110 O
ATOM 503 CB GLU A 295 -47.235 43.452 24.770 1.00 91.37 C
ANISOU 503 CB GLU A 295 12332 14682 7701 4436 1089 1710 C
ATOM 504 N ASP A 296 -44.379 42.339 23.175 1.00 86.25 N
ANISOU 504 N ASP A 296 11816 13453 7501 3956 882 1526 N
ATOM 505 CA ASP A 296 -43.528 41.312 22.583 1.00 83.92 C
ANISOU 505 CA ASP A 296 11592 12878 7415 3772 1013 1693 C
ATOM 506 C ASP A 296 -42.477 42.047 21.769 1.00 81.36 C
ANISOU 506 C ASP A 296 11260 12395 7260 3513 616 1252 C
ATOM 507 O ASP A 296 -42.674 43.214 21.419 1.00 78.46 O
ANISOU 507 O ASP A 296 10815 12012 6986 3357 332 902 O
ATOM 508 CB ASP A 296 -44.341 40.396 21.641 1.00 84.63 C
ANISOU 508 CB ASP A 296 11683 12531 7943 3324 1351 1988 C
ATOM 509 CG ASP A 296 -45.448 39.587 22.296 1.00100.94 C
ANISOU 509 CG ASP A 296 13711 14630 10012 3511 1807 2462 C
ATOM 510 OD1 ASP A 296 -45.214 39.040 23.408 1.00106.86 O
ANISOU 510 OD1 ASP A 296 14475 15665 10461 4010 2026 2785 O
ATOM 511 OD2 ASP A 296 -46.531 39.455 21.677 1.00104.19 O
ANISOU 511 OD2 ASP A 296 14057 14780 10749 3181 1966 2528 O
ATOM 512 N TYR A 297 -41.369 41.378 21.466 1.00 77.33 N
ANISOU 512 N TYR A 297 10810 11752 6820 3475 617 1293 N
ATOM 513 CA TYR A 297 -40.332 41.938 20.612 1.00 75.10 C
ANISOU 513 CA TYR A 297 10510 11269 6754 3216 298 944 C
ATOM 514 C TYR A 297 -40.715 41.649 19.160 1.00 75.30 C
ANISOU 514 C TYR A 297 10543 10868 7198 2661 395 1008 C
ATOM 515 O TYR A 297 -41.269 40.582 18.886 1.00 74.50 O
ANISOU 515 O TYR A 297 10477 10598 7232 2519 717 1325 O
ATOM 516 CB TYR A 297 -38.968 41.311 20.925 1.00 77.77 C
ANISOU 516 CB TYR A 297 10911 11666 6973 3433 260 962 C
ATOM 517 CG TYR A 297 -38.407 41.709 22.269 1.00 83.68 C
ANISOU 517 CG TYR A 297 11618 12885 7293 4024 86 789 C
ATOM 518 CD1 TYR A 297 -37.951 43.003 22.499 1.00 85.79 C
ANISOU 518 CD1 TYR A 297 11751 13302 7542 4154 -328 276 C
ATOM 519 CD2 TYR A 297 -38.299 40.785 23.303 1.00 88.38 C
ANISOU 519 CD2 TYR A 297 12272 13785 7522 4491 339 1124 C
ATOM 520 CE1 TYR A 297 -37.423 43.377 23.732 1.00 90.25 C
ANISOU 520 CE1 TYR A 297 12233 14337 7719 4740 -529 25 C
ATOM 521 CE2 TYR A 297 -37.785 41.150 24.548 1.00 93.00 C
ANISOU 521 CE2 TYR A 297 12798 14889 7647 5114 165 937 C
ATOM 522 CZ TYR A 297 -37.332 42.445 24.754 1.00101.23 C
ANISOU 522 CZ TYR A 297 13700 16100 8664 5238 -294 347 C
ATOM 523 OH TYR A 297 -36.801 42.813 25.970 1.00105.32 O
ANISOU 523 OH TYR A 297 14117 17161 8740 5886 -508 71 O
ATOM 524 N TYR A 298 -40.464 42.607 18.244 1.00 69.67 N
ANISOU 524 N TYR A 298 9762 9996 6715 2382 129 705 N
ATOM 525 CA TYR A 298 -40.732 42.450 16.812 1.00 67.01 C
ANISOU 525 CA TYR A 298 9408 9337 6716 1929 181 726 C
ATOM 526 C TYR A 298 -39.481 42.803 16.055 1.00 70.51 C
ANISOU 526 C TYR A 298 9830 9630 7332 1805 -43 533 C
ATOM 527 O TYR A 298 -39.006 43.940 16.134 1.00 70.10 O
ANISOU 527 O TYR A 298 9683 9621 7332 1874 -307 264 O
ATOM 528 CB TYR A 298 -41.930 43.297 16.341 1.00 66.69 C
ANISOU 528 CB TYR A 298 9279 9274 6785 1734 153 635 C
ATOM 529 CG TYR A 298 -43.255 42.847 16.925 1.00 69.02 C
ANISOU 529 CG TYR A 298 9585 9663 6976 1803 409 850 C
ATOM 530 CD1 TYR A 298 -43.658 43.261 18.194 1.00 71.90 C
ANISOU 530 CD1 TYR A 298 9945 10326 7047 2159 400 860 C
ATOM 531 CD2 TYR A 298 -44.124 42.038 16.195 1.00 69.29 C
ANISOU 531 CD2 TYR A 298 9600 9495 7231 1533 654 1016 C
ATOM 532 CE1 TYR A 298 -44.867 42.839 18.744 1.00 73.58 C
ANISOU 532 CE1 TYR A 298 10157 10622 7178 2246 667 1102 C
ATOM 533 CE2 TYR A 298 -45.360 41.646 16.717 1.00 71.74 C
ANISOU 533 CE2 TYR A 298 9886 9848 7526 1588 907 1212 C
ATOM 534 CZ TYR A 298 -45.719 42.032 18.003 1.00 80.46 C
ANISOU 534 CZ TYR A 298 11006 11237 8327 1945 931 1290 C
ATOM 535 OH TYR A 298 -46.914 41.616 18.559 1.00 80.47 O
ANISOU 535 OH TYR A 298 10975 11281 8319 2032 1214 1535 O
ATOM 536 N ILE A 299 -38.909 41.809 15.372 1.00 67.04 N
ANISOU 536 N ILE A 299 9455 9003 7016 1643 71 670 N
ATOM 537 CA ILE A 299 -37.688 41.988 14.590 1.00 65.36 C
ANISOU 537 CA ILE A 299 9227 8636 6969 1527 -103 540 C
ATOM 538 C ILE A 299 -37.959 41.868 13.096 1.00 65.14 C
ANISOU 538 C ILE A 299 9154 8401 7195 1179 -55 565 C
ATOM 539 O ILE A 299 -38.305 40.791 12.608 1.00 63.90 O
ANISOU 539 O ILE A 299 9032 8143 7106 1032 143 715 O
ATOM 540 CB ILE A 299 -36.521 41.086 15.064 1.00 69.57 C
ANISOU 540 CB ILE A 299 9860 9177 7397 1698 -77 619 C
ATOM 541 CG1 ILE A 299 -36.210 41.305 16.570 1.00 72.86 C
ANISOU 541 CG1 ILE A 299 10291 9889 7504 2132 -162 546 C
ATOM 542 CG2 ILE A 299 -35.285 41.357 14.214 1.00 67.82 C
ANISOU 542 CG2 ILE A 299 9611 8781 7376 1566 -257 482 C
ATOM 543 CD1 ILE A 299 -35.259 40.228 17.197 1.00 85.23 C
ANISOU 543 CD1 ILE A 299 11965 11534 8884 2370 -48 714 C
ATOM 544 N VAL A 300 -37.776 42.989 12.381 1.00 59.87 N
ANISOU 544 N VAL A 300 8375 7684 6688 1083 -232 409 N
ATOM 545 CA VAL A 300 -37.980 43.115 10.933 1.00 57.15 C
ANISOU 545 CA VAL A 300 7953 7226 6535 839 -213 425 C
ATOM 546 C VAL A 300 -36.682 42.726 10.229 1.00 61.41 C
ANISOU 546 C VAL A 300 8509 7635 7188 795 -266 442 C
ATOM 547 O VAL A 300 -35.638 43.362 10.416 1.00 60.68 O
ANISOU 547 O VAL A 300 8376 7492 7186 897 -424 353 O
ATOM 548 CB VAL A 300 -38.531 44.508 10.532 1.00 58.42 C
ANISOU 548 CB VAL A 300 7967 7417 6814 806 -318 325 C
ATOM 549 CG1 VAL A 300 -38.871 44.579 9.042 1.00 56.62 C
ANISOU 549 CG1 VAL A 300 7649 7153 6713 626 -263 381 C
ATOM 550 CG2 VAL A 300 -39.745 44.870 11.386 1.00 58.33 C
ANISOU 550 CG2 VAL A 300 7952 7545 6665 874 -280 294 C
ATOM 551 N LEU A 301 -36.754 41.620 9.483 1.00 57.86 N
ANISOU 551 N LEU A 301 8100 7125 6759 655 -131 536 N
ATOM 552 CA LEU A 301 -35.621 41.025 8.787 1.00 57.46 C
ANISOU 552 CA LEU A 301 8077 6968 6788 607 -153 567 C
ATOM 553 C LEU A 301 -35.875 40.930 7.288 1.00 62.41 C
ANISOU 553 C LEU A 301 8601 7598 7515 460 -126 565 C
ATOM 554 O LEU A 301 -37.019 41.069 6.834 1.00 63.83 O
ANISOU 554 O LEU A 301 8700 7862 7690 388 -66 532 O
ATOM 555 CB LEU A 301 -35.333 39.615 9.369 1.00 57.94 C
ANISOU 555 CB LEU A 301 8261 6975 6779 628 -13 664 C
ATOM 556 CG LEU A 301 -35.065 39.541 10.880 1.00 62.03 C
ANISOU 556 CG LEU A 301 8877 7566 7125 855 -5 707 C
ATOM 557 CD1 LEU A 301 -35.733 38.338 11.488 1.00 63.05 C
ANISOU 557 CD1 LEU A 301 9063 7687 7205 879 249 881 C
ATOM 558 CD2 LEU A 301 -33.560 39.676 11.215 1.00 59.25 C
ANISOU 558 CD2 LEU A 301 8577 7186 6747 997 -159 651 C
ATOM 559 N GLU A 302 -34.814 40.693 6.515 1.00 71.12 N
ANISOU 559 N GLU A 302 9681 8614 8727 2144 -1496 -816 N
ATOM 560 CA GLU A 302 -35.001 40.555 5.083 1.00 71.26 C
ANISOU 560 CA GLU A 302 9796 8671 8607 2177 -1649 -718 C
ATOM 561 C GLU A 302 -35.628 39.201 4.788 1.00 70.24 C
ANISOU 561 C GLU A 302 9400 8830 8459 2061 -1647 -832 C
ATOM 562 O GLU A 302 -35.301 38.225 5.464 1.00 68.42 O
ANISOU 562 O GLU A 302 9025 8683 8290 1848 -1468 -897 O
ATOM 563 CB GLU A 302 -33.705 40.835 4.291 1.00 72.57 C
ANISOU 563 CB GLU A 302 10300 8624 8648 2042 -1605 -502 C
ATOM 564 CG GLU A 302 -32.485 39.982 4.622 1.00 80.55 C
ANISOU 564 CG GLU A 302 11339 9617 9649 1738 -1376 -463 C
ATOM 565 CD GLU A 302 -31.133 40.632 4.369 1.00100.32 C
ANISOU 565 CD GLU A 302 14137 11874 12108 1623 -1292 -270 C
ATOM 566 OE1 GLU A 302 -31.077 41.682 3.685 1.00 96.22 O
ANISOU 566 OE1 GLU A 302 13849 11180 11530 1746 -1412 -124 O
ATOM 567 OE2 GLU A 302 -30.124 40.087 4.871 1.00 91.35 O
ANISOU 567 OE2 GLU A 302 12990 10719 11001 1405 -1106 -256 O
ATOM 568 N LEU A 303 -36.592 39.168 3.855 1.00 65.37 N
ANISOU 568 N LEU A 303 8703 8363 7772 2212 -1859 -866 N
ATOM 569 CA LEU A 303 -37.328 37.973 3.473 1.00 63.89 C
ANISOU 569 CA LEU A 303 8255 8442 7578 2112 -1909 -998 C
ATOM 570 C LEU A 303 -36.536 37.087 2.537 1.00 67.05 C
ANISOU 570 C LEU A 303 8806 8839 7831 1897 -1867 -938 C
ATOM 571 O LEU A 303 -36.045 37.538 1.497 1.00 67.58 O
ANISOU 571 O LEU A 303 9142 8818 7718 1953 -1956 -801 O
ATOM 572 CB LEU A 303 -38.693 38.323 2.860 1.00 66.77 C
ANISOU 572 CB LEU A 303 8448 8992 7928 2369 -2178 -1082 C
ATOM 573 CG LEU A 303 -39.522 37.126 2.395 1.00 72.01 C
ANISOU 573 CG LEU A 303 8822 9939 8600 2252 -2265 -1239 C
ATOM 574 CD1 LEU A 303 -40.128 36.388 3.570 1.00 72.28 C
ANISOU 574 CD1 LEU A 303 8486 10136 8842 2131 -2120 -1395 C
ATOM 575 CD2 LEU A 303 -40.586 37.538 1.436 1.00 75.82 C
ANISOU 575 CD2 LEU A 303 9223 10587 9000 2500 -2574 -1279 C
ATOM 576 N MET A 304 -36.476 35.798 2.892 1.00 62.61 N
ANISOU 576 N MET A 304 8064 8383 7341 1660 -1732 -1045 N
ATOM 577 CA MET A 304 -35.757 34.745 2.178 1.00 60.47 C
ANISOU 577 CA MET A 304 7894 8115 6969 1446 -1664 -1041 C
ATOM 578 C MET A 304 -36.759 33.762 1.594 1.00 69.29 C
ANISOU 578 C MET A 304 8785 9451 8093 1393 -1809 -1217 C
ATOM 579 O MET A 304 -37.183 32.824 2.278 1.00 69.59 O
ANISOU 579 O MET A 304 8572 9574 8295 1230 -1721 -1340 O
ATOM 580 CB MET A 304 -34.759 34.058 3.129 1.00 58.48 C
ANISOU 580 CB MET A 304 7643 7758 6820 1219 -1392 -1018 C
ATOM 581 CG MET A 304 -33.699 34.984 3.637 1.00 59.14 C
ANISOU 581 CG MET A 304 7941 7637 6892 1245 -1269 -861 C
ATOM 582 SD MET A 304 -32.577 35.560 2.333 1.00 62.70 S
ANISOU 582 SD MET A 304 8765 7948 7109 1263 -1297 -671 S
ATOM 583 CE MET A 304 -31.516 34.133 2.188 1.00 56.99 C
ANISOU 583 CE MET A 304 8063 7234 6356 1002 -1095 -691 C
ATOM 584 N GLU A 305 -37.154 33.992 0.332 1.00 68.69 N
ANISOU 584 N GLU A 305 8798 9466 7836 1526 -2041 -1224 N
ATOM 585 CA GLU A 305 -38.166 33.194 -0.362 1.00 71.36 C
ANISOU 585 CA GLU A 305 8928 10027 8159 1498 -2238 -1410 C
ATOM 586 C GLU A 305 -37.949 31.677 -0.513 1.00 75.98 C
ANISOU 586 C GLU A 305 9436 10644 8788 1217 -2152 -1556 C
ATOM 587 O GLU A 305 -38.915 30.933 -0.656 1.00 77.36 O
ANISOU 587 O GLU A 305 9350 10985 9058 1138 -2278 -1740 O
ATOM 588 CB GLU A 305 -38.616 33.881 -1.653 1.00 76.01 C
ANISOU 588 CB GLU A 305 9651 10717 8514 1728 -2523 -1375 C
ATOM 589 CG GLU A 305 -39.621 34.992 -1.386 1.00 91.02 C
ANISOU 589 CG GLU A 305 11418 12687 10479 2015 -2700 -1351 C
ATOM 590 CD GLU A 305 -39.601 36.121 -2.393 1.00117.87 C
ANISOU 590 CD GLU A 305 15092 16048 13643 2287 -2905 -1185 C
ATOM 591 OE1 GLU A 305 -40.274 35.993 -3.441 1.00119.07 O
ANISOU 591 OE1 GLU A 305 15219 16393 13630 2393 -3165 -1249 O
ATOM 592 OE2 GLU A 305 -38.922 37.140 -2.127 1.00109.77 O
ANISOU 592 OE2 GLU A 305 14312 14797 12598 2390 -2813 -986 O
ATOM 593 N GLY A 306 -36.704 31.229 -0.429 1.00 72.17 N
ANISOU 593 N GLY A 306 9163 9994 8265 1066 -1938 -1479 N
ATOM 594 CA GLY A 306 -36.374 29.809 -0.514 1.00 71.84 C
ANISOU 594 CA GLY A 306 9085 9930 8281 822 -1839 -1608 C
ATOM 595 C GLY A 306 -36.694 29.028 0.749 1.00 73.87 C
ANISOU 595 C GLY A 306 9075 10165 8825 636 -1683 -1672 C
ATOM 596 O GLY A 306 -36.754 27.792 0.714 1.00 74.27 O
ANISOU 596 O GLY A 306 9039 10204 8978 431 -1647 -1803 O
ATOM 597 N GLY A 307 -36.897 29.750 1.856 1.00 66.80 N
ANISOU 597 N GLY A 307 8067 9260 8055 709 -1589 -1579 N
ATOM 598 CA GLY A 307 -37.235 29.166 3.145 1.00 64.80 C
ANISOU 598 CA GLY A 307 7562 9020 8041 560 -1426 -1606 C
ATOM 599 C GLY A 307 -36.031 28.618 3.858 1.00 65.71 C
ANISOU 599 C GLY A 307 7812 8951 8204 405 -1168 -1504 C
ATOM 600 O GLY A 307 -34.913 29.074 3.623 1.00 65.14 O
ANISOU 600 O GLY A 307 8004 8747 7999 460 -1094 -1385 O
ATOM 601 N GLU A 308 -36.247 27.642 4.737 1.00 61.45 N
ANISOU 601 N GLU A 308 7085 8408 7857 209 -1030 -1537 N
ATOM 602 CA GLU A 308 -35.176 27.024 5.519 1.00 58.69 C
ANISOU 602 CA GLU A 308 6836 7894 7568 69 -794 -1433 C
ATOM 603 C GLU A 308 -34.540 25.898 4.721 1.00 65.37 C
ANISOU 603 C GLU A 308 7828 8616 8395 -72 -784 -1497 C
ATOM 604 O GLU A 308 -35.223 25.228 3.933 1.00 68.14 O
ANISOU 604 O GLU A 308 8100 9017 8774 -151 -928 -1657 O
ATOM 605 CB GLU A 308 -35.725 26.427 6.826 1.00 59.88 C
ANISOU 605 CB GLU A 308 6731 8097 7925 -73 -647 -1415 C
ATOM 606 CG GLU A 308 -36.396 27.391 7.788 1.00 65.31 C
ANISOU 606 CG GLU A 308 7240 8933 8641 61 -618 -1377 C
ATOM 607 CD GLU A 308 -37.143 26.727 8.936 1.00 90.17 C
ANISOU 607 CD GLU A 308 10101 12192 11968 -88 -477 -1370 C
ATOM 608 OE1 GLU A 308 -37.102 25.479 9.048 1.00 68.86 O
ANISOU 608 OE1 GLU A 308 7353 9419 9393 -319 -395 -1367 O
ATOM 609 OE2 GLU A 308 -37.761 27.464 9.739 1.00 95.18 O
ANISOU 609 OE2 GLU A 308 10565 12983 12617 30 -439 -1361 O
ATOM 610 N LEU A 309 -33.242 25.642 4.973 1.00 59.95 N
ANISOU 610 N LEU A 309 7336 7769 7673 -106 -614 -1389 N
ATOM 611 CA LEU A 309 -32.498 24.553 4.351 1.00 59.52 C
ANISOU 611 CA LEU A 309 7427 7578 7610 -211 -567 -1447 C
ATOM 612 C LEU A 309 -33.044 23.212 4.881 1.00 67.87 C
ANISOU 612 C LEU A 309 8313 8572 8901 -424 -518 -1522 C
ATOM 613 O LEU A 309 -33.013 22.198 4.172 1.00 69.42 O
ANISOU 613 O LEU A 309 8562 8679 9134 -526 -570 -1660 O
ATOM 614 CB LEU A 309 -31.017 24.704 4.681 1.00 56.70 C
ANISOU 614 CB LEU A 309 7261 7094 7188 -177 -385 -1296 C
ATOM 615 CG LEU A 309 -30.078 23.640 4.158 1.00 60.30 C
ANISOU 615 CG LEU A 309 7870 7409 7633 -242 -305 -1342 C
ATOM 616 CD1 LEU A 309 -30.052 23.614 2.622 1.00 61.87 C
ANISOU 616 CD1 LEU A 309 8219 7653 7637 -171 -445 -1479 C
ATOM 617 CD2 LEU A 309 -28.715 23.819 4.745 1.00 58.25 C
ANISOU 617 CD2 LEU A 309 7724 7059 7351 -209 -118 -1178 C
ATOM 618 N PHE A 310 -33.575 23.229 6.120 1.00 64.61 N
ANISOU 618 N PHE A 310 7699 8207 8641 -492 -418 -1433 N
ATOM 619 CA PHE A 310 -34.185 22.076 6.780 1.00 65.15 C
ANISOU 619 CA PHE A 310 7584 8229 8943 -710 -348 -1452 C
ATOM 620 C PHE A 310 -35.223 21.388 5.896 1.00 72.61 C
ANISOU 620 C PHE A 310 8400 9210 9976 -835 -533 -1662 C
ATOM 621 O PHE A 310 -35.230 20.161 5.817 1.00 73.81 O
ANISOU 621 O PHE A 310 8557 9204 10285 -1026 -509 -1729 O
ATOM 622 CB PHE A 310 -34.805 22.512 8.109 1.00 65.65 C
ANISOU 622 CB PHE A 310 7422 8429 9091 -720 -238 -1332 C
ATOM 623 CG PHE A 310 -35.570 21.444 8.842 1.00 67.83 C
ANISOU 623 CG PHE A 310 7478 8697 9599 -956 -150 -1316 C
ATOM 624 CD1 PHE A 310 -34.906 20.468 9.569 1.00 69.31 C
ANISOU 624 CD1 PHE A 310 7741 8697 9897 -1096 26 -1187 C
ATOM 625 CD2 PHE A 310 -36.960 21.440 8.846 1.00 72.38 C
ANISOU 625 CD2 PHE A 310 7756 9458 10285 -1037 -241 -1413 C
ATOM 626 CE1 PHE A 310 -35.617 19.503 10.288 1.00 72.06 C
ANISOU 626 CE1 PHE A 310 7897 9021 10462 -1329 120 -1134 C
ATOM 627 CE2 PHE A 310 -37.672 20.480 9.572 1.00 76.36 C
ANISOU 627 CE2 PHE A 310 8038 9963 11013 -1284 -138 -1372 C
ATOM 628 CZ PHE A 310 -36.994 19.511 10.280 1.00 73.50 C
ANISOU 628 CZ PHE A 310 7780 9390 10757 -1437 46 -1223 C
ATOM 629 N ASP A 311 -36.066 22.182 5.201 1.00 70.61 N
ANISOU 629 N ASP A 311 8048 9154 9625 -720 -734 -1772 N
ATOM 630 CA ASP A 311 -37.129 21.700 4.306 1.00 73.12 C
ANISOU 630 CA ASP A 311 8218 9561 10001 -815 -956 -1991 C
ATOM 631 C ASP A 311 -36.593 21.002 3.036 1.00 76.22 C
ANISOU 631 C ASP A 311 8843 9820 10295 -842 -1071 -2158 C
ATOM 632 O ASP A 311 -37.366 20.344 2.344 1.00 79.26 O
ANISOU 632 O ASP A 311 9124 10235 10756 -968 -1247 -2365 O
ATOM 633 CB ASP A 311 -38.125 22.831 3.958 1.00 76.66 C
ANISOU 633 CB ASP A 311 8497 10278 10353 -639 -1150 -2046 C
ATOM 634 CG ASP A 311 -38.703 23.577 5.159 1.00 92.40 C
ANISOU 634 CG ASP A 311 10255 12422 12429 -576 -1042 -1919 C
ATOM 635 OD1 ASP A 311 -39.531 22.984 5.886 1.00 95.10 O
ANISOU 635 OD1 ASP A 311 10313 12837 12985 -758 -975 -1931 O
ATOM 636 OD2 ASP A 311 -38.355 24.771 5.346 1.00 99.99 O
ANISOU 636 OD2 ASP A 311 11317 13432 13241 -345 -1024 -1814 O
ATOM 637 N LYS A 312 -35.276 21.134 2.748 1.00 69.03 N
ANISOU 637 N LYS A 312 8233 8776 9219 -727 -968 -2081 N
ATOM 638 CA LYS A 312 -34.581 20.511 1.617 1.00 68.31 C
ANISOU 638 CA LYS A 312 8386 8569 9000 -713 -1026 -2227 C
ATOM 639 C LYS A 312 -33.851 19.208 2.049 1.00 74.24 C
ANISOU 639 C LYS A 312 9231 9048 9931 -871 -856 -2228 C
ATOM 640 O LYS A 312 -33.459 18.405 1.204 1.00 74.83 O
ANISOU 640 O LYS A 312 9467 8998 9966 -896 -907 -2400 O
ATOM 641 CB LYS A 312 -33.598 21.505 0.949 1.00 66.53 C
ANISOU 641 CB LYS A 312 8412 8398 8469 -477 -1009 -2135 C
ATOM 642 CG LYS A 312 -34.214 22.850 0.512 1.00 71.74 C
ANISOU 642 CG LYS A 312 9029 9283 8945 -295 -1176 -2098 C
ATOM 643 CD LYS A 312 -34.968 22.854 -0.837 1.00 73.08 C
ANISOU 643 CD LYS A 312 9214 9607 8944 -237 -1454 -2307 C
ATOM 644 N VAL A 313 -33.695 18.992 3.362 1.00 71.91 N
ANISOU 644 N VAL A 313 8839 8661 9824 -963 -663 -2041 N
ATOM 645 CA VAL A 313 -32.979 17.834 3.918 1.00 72.47 C
ANISOU 645 CA VAL A 313 9000 8462 10071 -1086 -496 -1988 C
ATOM 646 C VAL A 313 -33.834 16.811 4.702 1.00 81.03 C
ANISOU 646 C VAL A 313 9884 9432 11471 -1352 -461 -1983 C
ATOM 647 O VAL A 313 -33.349 15.701 4.943 1.00 81.18 O
ANISOU 647 O VAL A 313 10004 9188 11655 -1465 -365 -1971 O
ATOM 648 CB VAL A 313 -31.678 18.234 4.672 1.00 72.71 C
ANISOU 648 CB VAL A 313 9168 8433 10026 -955 -281 -1753 C
ATOM 649 CG1 VAL A 313 -30.666 18.863 3.727 1.00 71.31 C
ANISOU 649 CG1 VAL A 313 9217 8298 9580 -749 -294 -1780 C
ATOM 650 CG2 VAL A 313 -31.963 19.161 5.846 1.00 70.54 C
ANISOU 650 CG2 VAL A 313 8732 8312 9759 -922 -191 -1547 C
ATOM 651 N VAL A 314 -35.090 17.173 5.086 1.00 80.59 N
ANISOU 651 N VAL A 314 9545 9571 11506 -1448 -535 -1986 N
ATOM 652 CA VAL A 314 -36.021 16.287 5.811 1.00 83.82 C
ANISOU 652 CA VAL A 314 9718 9916 12212 -1727 -494 -1966 C
ATOM 653 C VAL A 314 -36.405 15.038 5.034 1.00 94.64 C
ANISOU 653 C VAL A 314 11112 11079 13767 -1944 -628 -2199 C
ATOM 654 O VAL A 314 -36.464 15.071 3.802 1.00 95.43 O
ANISOU 654 O VAL A 314 11311 11209 13741 -1878 -830 -2444 O
ATOM 655 CB VAL A 314 -37.294 16.978 6.365 1.00 88.19 C
ANISOU 655 CB VAL A 314 9925 10764 12818 -1772 -529 -1926 C
ATOM 656 CG1 VAL A 314 -36.939 18.002 7.404 1.00 85.12 C
ANISOU 656 CG1 VAL A 314 9509 10523 12308 -1601 -358 -1690 C
ATOM 657 CG2 VAL A 314 -38.153 17.592 5.261 1.00 89.47 C
ANISOU 657 CG2 VAL A 314 9973 11157 12866 -1690 -800 -2153 C
ATOM 658 N GLY A 315 -36.722 13.977 5.775 1.00 95.26 N
ANISOU 658 N GLY A 315 11096 10960 14139 -2208 -522 -2120 N
ATOM 659 CA GLY A 315 -37.170 12.703 5.224 1.00 99.46 C
ANISOU 659 CA GLY A 315 11632 11243 14915 -2469 -637 -2326 C
ATOM 660 C GLY A 315 -36.191 12.035 4.282 1.00105.20 C
ANISOU 660 C GLY A 315 12699 11695 15578 -2377 -696 -2510 C
ATOM 661 O GLY A 315 -36.597 11.528 3.226 1.00108.26 O
ANISOU 661 O GLY A 315 13122 12022 15991 -2457 -910 -2817 O
ATOM 662 N ASN A 316 -34.889 12.035 4.667 1.00 98.57 N
ANISOU 662 N ASN A 316 12100 10708 14643 -2196 -511 -2337 N
ATOM 663 CA ASN A 316 -33.788 11.428 3.910 1.00 98.13 C
ANISOU 663 CA ASN A 316 12364 10404 14517 -2062 -513 -2475 C
ATOM 664 C ASN A 316 -33.568 12.042 2.510 1.00100.99 C
ANISOU 664 C ASN A 316 12858 10947 14567 -1851 -690 -2733 C
ATOM 665 O ASN A 316 -33.016 11.386 1.615 1.00101.92 O
ANISOU 665 O ASN A 316 13201 10886 14638 -1787 -749 -2954 O
ATOM 666 CB ASN A 316 -33.883 9.884 3.898 1.00101.75 C
ANISOU 666 CB ASN A 316 12914 10447 15300 -2293 -523 -2588 C
ATOM 667 CG ASN A 316 -34.025 9.261 5.273 1.00130.44 C
ANISOU 667 CG ASN A 316 16451 13889 19222 -2494 -333 -2287 C
ATOM 668 OD1 ASN A 316 -33.288 9.591 6.222 1.00119.56 O
ANISOU 668 OD1 ASN A 316 15112 12536 17781 -2365 -132 -1989 O
ATOM 669 ND2 ASN A 316 -34.974 8.330 5.404 1.00128.06 N
ANISOU 669 ND2 ASN A 316 16023 13395 19238 -2823 -396 -2357 N
ATOM 670 N LYS A 317 -33.984 13.320 2.340 1.00 94.60 N
ANISOU 670 N LYS A 317 11917 10494 13532 -1727 -767 -2694 N
ATOM 671 CA LYS A 317 -33.797 14.060 1.097 1.00 93.44 C
ANISOU 671 CA LYS A 317 11892 10555 13058 -1515 -923 -2870 C
ATOM 672 C LYS A 317 -32.321 14.437 0.985 1.00 94.83 C
ANISOU 672 C LYS A 317 12323 10697 13013 -1265 -758 -2751 C
ATOM 673 O LYS A 317 -31.728 15.022 1.900 1.00 90.67 O
ANISOU 673 O LYS A 317 11781 10204 12465 -1180 -574 -2478 O
ATOM 674 CB LYS A 317 -34.696 15.297 1.023 1.00 94.54 C
ANISOU 674 CB LYS A 317 11822 11049 13051 -1448 -1051 -2828 C
ATOM 675 CG LYS A 317 -36.142 15.010 0.645 1.00 95.38 C
ANISOU 675 CG LYS A 317 11678 11265 13297 -1643 -1286 -3035 C
ATOM 676 CD LYS A 317 -36.794 16.184 -0.106 1.00 97.63 C
ANISOU 676 CD LYS A 317 11865 11904 13326 -1474 -1499 -3107 C
ATOM 677 CE LYS A 317 -37.054 17.431 0.714 1.00 94.46 C
ANISOU 677 CE LYS A 317 11300 11726 12866 -1345 -1414 -2852 C
ATOM 678 NZ LYS A 317 -38.090 17.212 1.752 1.00 98.54 N
ANISOU 678 NZ LYS A 317 11475 12294 13670 -1552 -1368 -2773 N
ATOM 679 N ARG A 318 -31.727 14.020 -0.124 1.00 94.21 N
ANISOU 679 N ARG A 318 12467 10550 12778 -1159 -821 -2975 N
ATOM 680 CA ARG A 318 -30.316 14.189 -0.413 1.00 92.90 C
ANISOU 680 CA ARG A 318 12533 10354 12410 -934 -667 -2913 C
ATOM 681 C ARG A 318 -30.093 15.300 -1.428 1.00 95.02 C
ANISOU 681 C ARG A 318 12891 10918 12295 -727 -748 -2950 C
ATOM 682 O ARG A 318 -30.563 15.206 -2.574 1.00 97.63 O
ANISOU 682 O ARG A 318 13280 11353 12464 -706 -946 -3207 O
ATOM 683 CB ARG A 318 -29.727 12.854 -0.928 1.00 96.25 C
ANISOU 683 CB ARG A 318 13155 10482 12931 -940 -647 -3138 C
ATOM 684 CG ARG A 318 -28.212 12.828 -0.942 1.00102.76 C
ANISOU 684 CG ARG A 318 14172 11243 13630 -721 -438 -3040 C
ATOM 685 CD ARG A 318 -27.682 11.979 -2.071 1.00110.13 C
ANISOU 685 CD ARG A 318 15329 12054 14464 -614 -478 -3355 C
ATOM 686 NE ARG A 318 -27.743 10.554 -1.757 1.00124.47 N
ANISOU 686 NE ARG A 318 17202 13478 16611 -743 -473 -3488 N
ATOM 687 CZ ARG A 318 -26.779 9.881 -1.137 1.00143.47 C
ANISOU 687 CZ ARG A 318 19700 15631 19183 -668 -288 -3370 C
ATOM 688 NH1 ARG A 318 -25.675 10.501 -0.739 1.00133.03 N
ANISOU 688 NH1 ARG A 318 18392 14430 17723 -475 -93 -3127 N
ATOM 689 NH2 ARG A 318 -26.913 8.583 -0.905 1.00132.93 N
ANISOU 689 NH2 ARG A 318 18437 13909 18160 -786 -305 -3492 N
ATOM 690 N LEU A 319 -29.345 16.340 -1.000 1.00 85.45 N
ANISOU 690 N LEU A 319 11698 9834 10934 -579 -597 -2686 N
ATOM 691 CA LEU A 319 -28.935 17.472 -1.824 1.00 82.23 C
ANISOU 691 CA LEU A 319 11399 9672 10174 -384 -620 -2638 C
ATOM 692 C LEU A 319 -27.828 16.982 -2.784 1.00 84.10 C
ANISOU 692 C LEU A 319 11872 9868 10213 -242 -537 -2776 C
ATOM 693 O LEU A 319 -27.017 16.118 -2.408 1.00 83.57 O
ANISOU 693 O LEU A 319 11871 9589 10294 -240 -380 -2780 O
ATOM 694 CB LEU A 319 -28.355 18.544 -0.894 1.00 78.81 C
ANISOU 694 CB LEU A 319 10913 9310 9722 -313 -456 -2313 C
ATOM 695 CG LEU A 319 -29.142 19.832 -0.612 1.00 81.80 C
ANISOU 695 CG LEU A 319 11156 9886 10037 -291 -553 -2172 C
ATOM 696 CD1 LEU A 319 -30.424 19.557 0.145 1.00 82.27 C
ANISOU 696 CD1 LEU A 319 10978 9928 10355 -458 -647 -2199 C
ATOM 697 CD2 LEU A 319 -28.304 20.775 0.239 1.00 79.68 C
ANISOU 697 CD2 LEU A 319 10893 9640 9741 -212 -375 -1890 C
ATOM 698 N LYS A 320 -27.820 17.515 -4.031 1.00 78.58 N
ANISOU 698 N LYS A 320 11300 9384 9174 -109 -644 -2890 N
ATOM 699 CA LYS A 320 -26.825 17.261 -5.092 1.00 77.68 C
ANISOU 699 CA LYS A 320 11407 9321 8788 55 -562 -3018 C
ATOM 700 C LYS A 320 -25.456 17.676 -4.521 1.00 75.59 C
ANISOU 700 C LYS A 320 11175 9038 8508 154 -285 -2753 C
ATOM 701 O LYS A 320 -25.386 18.732 -3.872 1.00 73.14 O
ANISOU 701 O LYS A 320 10777 8814 8199 151 -229 -2479 O
ATOM 702 CB LYS A 320 -27.146 18.199 -6.266 1.00 80.83 C
ANISOU 702 CB LYS A 320 11899 10020 8792 178 -706 -3050 C
ATOM 703 CG LYS A 320 -27.226 17.573 -7.638 1.00 77.37 C
ANISOU 703 CG LYS A 320 11622 9666 8109 248 -850 -3392 C
ATOM 704 CD LYS A 320 -27.849 18.563 -8.618 1.00 82.44 C
ANISOU 704 CD LYS A 320 12315 10617 8391 345 -1044 -3377 C
ATOM 705 CE LYS A 320 -29.310 18.267 -8.879 1.00 99.71 C
ANISOU 705 CE LYS A 320 14385 12847 10652 234 -1368 -3608 C
ATOM 706 NZ LYS A 320 -29.889 19.182 -9.900 1.00114.18 N
ANISOU 706 NZ LYS A 320 16283 14994 12105 364 -1581 -3608 N
ATOM 707 N GLU A 321 -24.382 16.879 -4.734 1.00 69.15 N
ANISOU 707 N GLU A 321 10474 8113 7686 246 -119 -2842 N
ATOM 708 CA GLU A 321 -23.058 17.231 -4.190 1.00 65.84 C
ANISOU 708 CA GLU A 321 10051 7700 7265 339 135 -2601 C
ATOM 709 C GLU A 321 -22.632 18.683 -4.479 1.00 70.62 C
ANISOU 709 C GLU A 321 10670 8567 7595 416 197 -2360 C
ATOM 710 O GLU A 321 -22.107 19.357 -3.586 1.00 69.45 O
ANISOU 710 O GLU A 321 10428 8417 7540 394 320 -2093 O
ATOM 711 CB GLU A 321 -21.958 16.216 -4.548 1.00 67.94 C
ANISOU 711 CB GLU A 321 10429 7858 7526 470 297 -2752 C
ATOM 712 CG GLU A 321 -20.608 16.591 -3.949 1.00 69.64 C
ANISOU 712 CG GLU A 321 10594 8104 7763 561 546 -2500 C
ATOM 713 CD GLU A 321 -19.517 15.553 -3.794 1.00 83.42 C
ANISOU 713 CD GLU A 321 12375 9692 9630 687 718 -2584 C
ATOM 714 OE1 GLU A 321 -19.817 14.338 -3.793 1.00 83.68 O
ANISOU 714 OE1 GLU A 321 12465 9475 9854 674 654 -2808 O
ATOM 715 OE2 GLU A 321 -18.355 15.972 -3.596 1.00 80.21 O
ANISOU 715 OE2 GLU A 321 11924 9399 9155 792 915 -2410 O
ATOM 716 N ALA A 322 -22.928 19.170 -5.694 1.00 69.24 N
ANISOU 716 N ALA A 322 10614 8606 7089 493 93 -2452 N
ATOM 717 CA ALA A 322 -22.606 20.522 -6.142 1.00 68.60 C
ANISOU 717 CA ALA A 322 10582 8756 6725 562 135 -2223 C
ATOM 718 C ALA A 322 -23.371 21.585 -5.349 1.00 70.76 C
ANISOU 718 C ALA A 322 10736 9032 7116 473 28 -2000 C
ATOM 719 O ALA A 322 -22.763 22.580 -4.929 1.00 68.83 O
ANISOU 719 O ALA A 322 10473 8836 6846 481 147 -1731 O
ATOM 720 CB ALA A 322 -22.854 20.659 -7.634 1.00 72.10 C
ANISOU 720 CB ALA A 322 11197 9420 6777 672 28 -2380 C
ATOM 721 N THR A 323 -24.681 21.337 -5.087 1.00 67.66 N
ANISOU 721 N THR A 323 10248 8581 6878 382 -191 -2122 N
ATOM 722 CA THR A 323 -25.568 22.214 -4.301 1.00 65.42 C
ANISOU 722 CA THR A 323 9824 8304 6730 314 -305 -1962 C
ATOM 723 C THR A 323 -25.035 22.308 -2.864 1.00 66.15 C
ANISOU 723 C THR A 323 9790 8247 7097 239 -136 -1764 C
ATOM 724 O THR A 323 -25.030 23.400 -2.311 1.00 65.13 O
ANISOU 724 O THR A 323 9614 8158 6976 244 -120 -1550 O
ATOM 725 CB THR A 323 -27.020 21.697 -4.378 1.00 76.49 C
ANISOU 725 CB THR A 323 11118 9693 8251 229 -553 -2176 C
ATOM 726 OG1 THR A 323 -27.457 21.634 -5.741 1.00 80.64 O
ANISOU 726 OG1 THR A 323 11766 10382 8493 309 -732 -2370 O
ATOM 727 CG2 THR A 323 -27.994 22.510 -3.545 1.00 70.51 C
ANISOU 727 CG2 THR A 323 10182 8959 7650 176 -661 -2039 C
ATOM 728 N CYS A 324 -24.561 21.171 -2.287 1.00 62.59 N
ANISOU 728 N CYS A 324 9299 7621 6859 184 -18 -1840 N
ATOM 729 CA CYS A 324 -23.957 21.054 -0.950 1.00 60.88 C
ANISOU 729 CA CYS A 324 8976 7270 6884 128 143 -1667 C
ATOM 730 C CYS A 324 -22.802 22.007 -0.852 1.00 63.20 C
ANISOU 730 C CYS A 324 9312 7654 7048 203 301 -1446 C
ATOM 731 O CYS A 324 -22.725 22.770 0.122 1.00 62.38 O
ANISOU 731 O CYS A 324 9116 7542 7043 164 339 -1253 O
ATOM 732 CB CYS A 324 -23.483 19.631 -0.680 1.00 62.72 C
ANISOU 732 CB CYS A 324 9218 7309 7303 105 237 -1790 C
ATOM 733 SG CYS A 324 -24.807 18.457 -0.325 1.00 68.65 S
ANISOU 733 SG CYS A 324 9879 7875 8328 -57 80 -1988 S
ATOM 734 N LYS A 325 -21.894 21.949 -1.862 1.00 57.12 N
ANISOU 734 N LYS A 325 8673 6976 6052 306 399 -1486 N
ATOM 735 CA LYS A 325 -20.709 22.782 -1.952 1.00 54.86 C
ANISOU 735 CA LYS A 325 8420 6795 5629 360 567 -1286 C
ATOM 736 C LYS A 325 -21.056 24.255 -2.012 1.00 59.39 C
ANISOU 736 C LYS A 325 9013 7471 6081 344 492 -1097 C
ATOM 737 O LYS A 325 -20.490 25.040 -1.259 1.00 57.78 O
ANISOU 737 O LYS A 325 8749 7251 5953 305 578 -893 O
ATOM 738 CB LYS A 325 -19.843 22.371 -3.150 1.00 58.44 C
ANISOU 738 CB LYS A 325 9001 7365 5840 475 684 -1391 C
ATOM 739 CG LYS A 325 -18.394 22.846 -3.023 1.00 56.42 C
ANISOU 739 CG LYS A 325 8716 7192 5529 510 914 -1198 C
ATOM 740 CD LYS A 325 -17.563 22.514 -4.233 1.00 54.67 C
ANISOU 740 CD LYS A 325 8602 7130 5040 633 1054 -1290 C
ATOM 741 CE LYS A 325 -17.261 21.045 -4.369 1.00 61.22 C
ANISOU 741 CE LYS A 325 9439 7864 5958 725 1115 -1538 C
ATOM 742 NZ LYS A 325 -16.133 20.806 -5.324 1.00 72.37 N
ANISOU 742 NZ LYS A 325 10909 9456 7133 867 1320 -1590 N
ATOM 743 N LEU A 326 -21.984 24.642 -2.900 1.00 58.39 N
ANISOU 743 N LEU A 326 8974 7440 5771 380 319 -1167 N
ATOM 744 CA LEU A 326 -22.363 26.047 -3.050 1.00 57.46 C
ANISOU 744 CA LEU A 326 8901 7396 5534 395 230 -982 C
ATOM 745 C LEU A 326 -22.904 26.641 -1.740 1.00 57.82 C
ANISOU 745 C LEU A 326 8808 7333 5827 326 169 -874 C
ATOM 746 O LEU A 326 -22.589 27.776 -1.392 1.00 56.03 O
ANISOU 746 O LEU A 326 8599 7099 5592 321 196 -674 O
ATOM 747 CB LEU A 326 -23.355 26.232 -4.223 1.00 59.24 C
ANISOU 747 CB LEU A 326 9239 7752 5518 473 25 -1091 C
ATOM 748 CG LEU A 326 -23.821 27.676 -4.498 1.00 64.17 C
ANISOU 748 CG LEU A 326 9937 8440 6005 523 -95 -896 C
ATOM 749 CD1 LEU A 326 -22.655 28.587 -4.896 1.00 64.46 C
ANISOU 749 CD1 LEU A 326 10103 8528 5863 538 80 -646 C
ATOM 750 CD2 LEU A 326 -24.915 27.712 -5.535 1.00 69.62 C
ANISOU 750 CD2 LEU A 326 10704 9262 6485 614 -335 -1024 C
ATOM 751 N TYR A 327 -23.705 25.865 -1.025 1.00 54.26 N
ANISOU 751 N TYR A 327 8225 6798 5595 269 94 -1009 N
ATOM 752 CA TYR A 327 -24.312 26.277 0.238 1.00 52.70 C
ANISOU 752 CA TYR A 327 7879 6527 5616 213 48 -936 C
ATOM 753 C TYR A 327 -23.258 26.291 1.348 1.00 56.98 C
ANISOU 753 C TYR A 327 8357 6985 6305 161 231 -798 C
ATOM 754 O TYR A 327 -23.162 27.277 2.074 1.00 55.86 O
ANISOU 754 O TYR A 327 8183 6829 6214 152 237 -656 O
ATOM 755 CB TYR A 327 -25.460 25.315 0.612 1.00 52.81 C
ANISOU 755 CB TYR A 327 7759 6499 5808 148 -63 -1116 C
ATOM 756 CG TYR A 327 -26.664 25.340 -0.303 1.00 54.95 C
ANISOU 756 CG TYR A 327 8037 6870 5972 185 -282 -1266 C
ATOM 757 CD1 TYR A 327 -26.778 26.288 -1.320 1.00 57.85 C
ANISOU 757 CD1 TYR A 327 8537 7359 6083 297 -385 -1216 C
ATOM 758 CD2 TYR A 327 -27.720 24.454 -0.117 1.00 56.41 C
ANISOU 758 CD2 TYR A 327 8084 7033 6316 102 -396 -1444 C
ATOM 759 CE1 TYR A 327 -27.900 26.335 -2.144 1.00 59.98 C
ANISOU 759 CE1 TYR A 327 8803 7743 6242 350 -613 -1351 C
ATOM 760 CE2 TYR A 327 -28.863 24.514 -0.914 1.00 58.77 C
ANISOU 760 CE2 TYR A 327 8353 7448 6529 130 -622 -1592 C
ATOM 761 CZ TYR A 327 -28.938 25.442 -1.937 1.00 63.97 C
ANISOU 761 CZ TYR A 327 9148 8244 6916 267 -737 -1551 C
ATOM 762 OH TYR A 327 -30.040 25.470 -2.743 1.00 65.42 O
ANISOU 762 OH TYR A 327 9299 8561 6996 313 -980 -1697 O
ATOM 763 N PHE A 328 -22.460 25.207 1.458 1.00 53.98 N
ANISOU 763 N PHE A 328 7966 6551 5993 141 365 -852 N
ATOM 764 CA PHE A 328 -21.442 25.068 2.483 1.00 52.71 C
ANISOU 764 CA PHE A 328 7730 6329 5969 108 521 -734 C
ATOM 765 C PHE A 328 -20.382 26.135 2.410 1.00 57.21 C
ANISOU 765 C PHE A 328 8343 6960 6435 121 617 -558 C
ATOM 766 O PHE A 328 -20.022 26.707 3.449 1.00 57.65 O
ANISOU 766 O PHE A 328 8320 6985 6599 77 654 -434 O
ATOM 767 CB PHE A 328 -20.837 23.663 2.494 1.00 54.94 C
ANISOU 767 CB PHE A 328 8001 6533 6342 119 627 -831 C
ATOM 768 CG PHE A 328 -20.129 23.349 3.787 1.00 53.98 C
ANISOU 768 CG PHE A 328 7770 6338 6402 90 737 -717 C
ATOM 769 CD1 PHE A 328 -20.844 23.187 4.966 1.00 55.03 C
ANISOU 769 CD1 PHE A 328 7795 6404 6709 21 689 -680 C
ATOM 770 CD2 PHE A 328 -18.745 23.217 3.824 1.00 54.86 C
ANISOU 770 CD2 PHE A 328 7873 6472 6497 139 889 -642 C
ATOM 771 CE1 PHE A 328 -20.185 22.941 6.172 1.00 55.10 C
ANISOU 771 CE1 PHE A 328 7716 6371 6849 6 780 -560 C
ATOM 772 CE2 PHE A 328 -18.086 22.952 5.026 1.00 56.71 C
ANISOU 772 CE2 PHE A 328 8000 6661 6886 128 965 -532 C
ATOM 773 CZ PHE A 328 -18.810 22.834 6.198 1.00 53.97 C
ANISOU 773 CZ PHE A 328 7571 6247 6687 63 904 -488 C
ATOM 774 N TYR A 329 -19.921 26.442 1.195 1.00 53.84 N
ANISOU 774 N TYR A 329 8040 6626 5792 171 653 -545 N
ATOM 775 CA TYR A 329 -18.931 27.494 0.937 1.00 53.86 C
ANISOU 775 CA TYR A 329 8090 6692 5681 157 753 -361 C
ATOM 776 C TYR A 329 -19.408 28.813 1.531 1.00 58.66 C
ANISOU 776 C TYR A 329 8701 7251 6335 114 651 -230 C
ATOM 777 O TYR A 329 -18.644 29.465 2.244 1.00 59.10 O
ANISOU 777 O TYR A 329 8708 7276 6472 51 722 -95 O
ATOM 778 CB TYR A 329 -18.652 27.605 -0.576 1.00 56.72 C
ANISOU 778 CB TYR A 329 8601 7183 5766 220 794 -369 C
ATOM 779 CG TYR A 329 -17.752 28.743 -0.993 1.00 58.94 C
ANISOU 779 CG TYR A 329 8947 7536 5912 184 899 -153 C
ATOM 780 CD1 TYR A 329 -16.410 28.767 -0.629 1.00 60.16 C
ANISOU 780 CD1 TYR A 329 9009 7725 6123 131 1090 -47 C
ATOM 781 CD2 TYR A 329 -18.227 29.773 -1.800 1.00 61.52 C
ANISOU 781 CD2 TYR A 329 9422 7900 6052 200 806 -45 C
ATOM 782 CE1 TYR A 329 -15.582 29.826 -0.993 1.00 61.86 C
ANISOU 782 CE1 TYR A 329 9263 8003 6237 61 1193 162 C
ATOM 783 CE2 TYR A 329 -17.398 30.822 -2.199 1.00 63.67 C
ANISOU 783 CE2 TYR A 329 9767 8214 6210 143 912 181 C
ATOM 784 CZ TYR A 329 -16.080 30.855 -1.776 1.00 69.85 C
ANISOU 784 CZ TYR A 329 10442 9023 7074 57 1110 284 C
ATOM 785 OH TYR A 329 -15.257 31.888 -2.165 1.00 73.29 O
ANISOU 785 OH TYR A 329 10930 9499 7417 -34 1222 515 O
ATOM 786 N GLN A 330 -20.695 29.149 1.320 1.00 55.11 N
ANISOU 786 N GLN A 330 8293 6789 5856 155 472 -290 N
ATOM 787 CA GLN A 330 -21.328 30.355 1.856 1.00 54.80 C
ANISOU 787 CA GLN A 330 8261 6691 5870 156 354 -201 C
ATOM 788 C GLN A 330 -21.427 30.332 3.395 1.00 58.53 C
ANISOU 788 C GLN A 330 8583 7087 6569 106 362 -207 C
ATOM 789 O GLN A 330 -21.170 31.362 4.038 1.00 59.75 O
ANISOU 789 O GLN A 330 8742 7181 6778 80 353 -103 O
ATOM 790 CB GLN A 330 -22.706 30.551 1.234 1.00 57.13 C
ANISOU 790 CB GLN A 330 8605 7021 6081 242 158 -287 C
ATOM 791 CG GLN A 330 -22.674 30.807 -0.268 1.00 60.30 C
ANISOU 791 CG GLN A 330 9180 7516 6216 309 121 -255 C
ATOM 792 CD GLN A 330 -24.049 30.836 -0.868 1.00 71.34 C
ANISOU 792 CD GLN A 330 10600 8974 7531 405 -97 -365 C
ATOM 793 OE1 GLN A 330 -24.818 31.770 -0.657 1.00 69.78 O
ANISOU 793 OE1 GLN A 330 10410 8741 7361 468 -239 -308 O
ATOM 794 NE2 GLN A 330 -24.384 29.821 -1.643 1.00 62.36 N
ANISOU 794 NE2 GLN A 330 9471 7931 6294 428 -141 -538 N
ATOM 795 N MET A 331 -21.768 29.156 3.982 1.00 52.40 N
ANISOU 795 N MET A 331 7686 6308 5916 88 381 -327 N
ATOM 796 CA MET A 331 -21.870 28.931 5.437 1.00 48.95 C
ANISOU 796 CA MET A 331 7108 5828 5661 45 406 -327 C
ATOM 797 C MET A 331 -20.476 29.137 6.050 1.00 53.77 C
ANISOU 797 C MET A 331 7694 6424 6311 -5 538 -210 C
ATOM 798 O MET A 331 -20.361 29.751 7.116 1.00 53.56 O
ANISOU 798 O MET A 331 7609 6374 6365 -31 529 -158 O
ATOM 799 CB MET A 331 -22.398 27.511 5.772 1.00 49.93 C
ANISOU 799 CB MET A 331 7134 5940 5898 21 420 -445 C
ATOM 800 CG MET A 331 -23.825 27.237 5.314 1.00 52.90 C
ANISOU 800 CG MET A 331 7481 6342 6276 38 279 -575 C
ATOM 801 SD MET A 331 -24.412 25.580 5.772 1.00 57.01 S
ANISOU 801 SD MET A 331 7884 6810 6969 -41 302 -696 S
ATOM 802 CE MET A 331 -25.228 25.136 4.340 1.00 55.13 C
ANISOU 802 CE MET A 331 7707 6607 6635 -21 164 -871 C
ATOM 803 N LEU A 332 -19.405 28.673 5.350 1.00 49.30 N
ANISOU 803 N LEU A 332 7165 5890 5676 -10 657 -181 N
ATOM 804 CA LEU A 332 -18.026 28.844 5.825 1.00 46.45 C
ANISOU 804 CA LEU A 332 6749 5548 5354 -57 780 -73 C
ATOM 805 C LEU A 332 -17.620 30.274 5.772 1.00 50.36 C
ANISOU 805 C LEU A 332 7300 6030 5804 -110 761 49 C
ATOM 806 O LEU A 332 -16.945 30.738 6.681 1.00 50.32 O
ANISOU 806 O LEU A 332 7220 6012 5886 -172 786 116 O
ATOM 807 CB LEU A 332 -17.049 28.017 5.018 1.00 46.89 C
ANISOU 807 CB LEU A 332 6808 5663 5345 -28 918 -84 C
ATOM 808 CG LEU A 332 -17.037 26.535 5.272 1.00 49.38 C
ANISOU 808 CG LEU A 332 7061 5949 5752 22 964 -188 C
ATOM 809 CD1 LEU A 332 -16.240 25.841 4.181 1.00 50.68 C
ANISOU 809 CD1 LEU A 332 7269 6173 5814 89 1084 -241 C
ATOM 810 CD2 LEU A 332 -16.477 26.224 6.638 1.00 45.84 C
ANISOU 810 CD2 LEU A 332 6479 5479 5460 2 1004 -125 C
ATOM 811 N LEU A 333 -18.025 30.993 4.709 1.00 48.18 N
ANISOU 811 N LEU A 333 7164 5751 5391 -89 706 83 N
ATOM 812 CA LEU A 333 -17.720 32.415 4.563 1.00 47.61 C
ANISOU 812 CA LEU A 333 7181 5623 5284 -145 677 220 C
ATOM 813 C LEU A 333 -18.425 33.216 5.670 1.00 51.95 C
ANISOU 813 C LEU A 333 7711 6070 5959 -144 546 197 C
ATOM 814 O LEU A 333 -17.824 34.123 6.244 1.00 53.10 O
ANISOU 814 O LEU A 333 7856 6145 6175 -223 547 274 O
ATOM 815 CB LEU A 333 -18.142 32.924 3.173 1.00 48.55 C
ANISOU 815 CB LEU A 333 7475 5758 5214 -96 631 274 C
ATOM 816 CG LEU A 333 -17.404 32.392 1.929 1.00 53.36 C
ANISOU 816 CG LEU A 333 8139 6493 5642 -89 769 310 C
ATOM 817 CD1 LEU A 333 -18.002 33.006 0.673 1.00 55.25 C
ANISOU 817 CD1 LEU A 333 8567 6757 5667 -28 691 374 C
ATOM 818 CD2 LEU A 333 -15.900 32.694 1.970 1.00 51.58 C
ANISOU 818 CD2 LEU A 333 7855 6312 5433 -203 946 451 C
ATOM 819 N ALA A 334 -19.697 32.872 5.967 1.00 47.31 N
ANISOU 819 N ALA A 334 7095 5479 5401 -57 437 76 N
ATOM 820 CA ALA A 334 -20.494 33.537 6.998 1.00 45.99 C
ANISOU 820 CA ALA A 334 6893 5249 5332 -21 326 26 C
ATOM 821 C ALA A 334 -19.909 33.290 8.391 1.00 48.09 C
ANISOU 821 C ALA A 334 7028 5528 5717 -80 386 9 C
ATOM 822 O ALA A 334 -19.642 34.236 9.111 1.00 48.40 O
ANISOU 822 O ALA A 334 7079 5500 5809 -110 346 30 O
ATOM 823 CB ALA A 334 -21.939 33.072 6.922 1.00 46.39 C
ANISOU 823 CB ALA A 334 6901 5343 5382 78 225 -97 C
ATOM 824 N VAL A 335 -19.653 32.029 8.740 1.00 44.41 N
ANISOU 824 N VAL A 335 6449 5138 5286 -94 473 -27 N
ATOM 825 CA VAL A 335 -19.038 31.647 10.012 1.00 43.56 C
ANISOU 825 CA VAL A 335 6219 5066 5264 -134 528 -21 C
ATOM 826 C VAL A 335 -17.583 32.200 10.134 1.00 47.09 C
ANISOU 826 C VAL A 335 6658 5510 5724 -224 587 74 C
ATOM 827 O VAL A 335 -17.181 32.603 11.225 1.00 46.73 O
ANISOU 827 O VAL A 335 6548 5472 5734 -260 563 74 O
ATOM 828 CB VAL A 335 -19.193 30.131 10.274 1.00 47.17 C
ANISOU 828 CB VAL A 335 6580 5578 5764 -114 598 -60 C
ATOM 829 CG1 VAL A 335 -18.510 29.713 11.562 1.00 46.21 C
ANISOU 829 CG1 VAL A 335 6345 5502 5709 -136 647 -24 C
ATOM 830 CG2 VAL A 335 -20.678 29.753 10.321 1.00 47.20 C
ANISOU 830 CG2 VAL A 335 6563 5586 5785 -65 529 -153 C
ATOM 831 N GLN A 336 -16.850 32.331 9.022 1.00 44.12 N
ANISOU 831 N GLN A 336 6343 5136 5286 -264 655 151 N
ATOM 832 CA GLN A 336 -15.513 32.915 9.096 1.00 45.55 C
ANISOU 832 CA GLN A 336 6487 5329 5492 -373 717 248 C
ATOM 833 C GLN A 336 -15.607 34.399 9.501 1.00 51.65 C
ANISOU 833 C GLN A 336 7335 5983 6305 -441 611 272 C
ATOM 834 O GLN A 336 -14.930 34.799 10.448 1.00 53.36 O
ANISOU 834 O GLN A 336 7472 6200 6602 -517 590 269 O
ATOM 835 CB GLN A 336 -14.726 32.678 7.807 1.00 47.78 C
ANISOU 835 CB GLN A 336 6801 5669 5684 -400 841 331 C
ATOM 836 CG GLN A 336 -13.415 33.447 7.694 1.00 59.48 C
ANISOU 836 CG GLN A 336 8234 7174 7193 -539 917 453 C
ATOM 837 CD GLN A 336 -12.775 33.239 6.342 1.00 74.18 C
ANISOU 837 CD GLN A 336 10128 9122 8934 -554 1061 541 C
ATOM 838 OE1 GLN A 336 -11.678 32.673 6.240 1.00 70.24 O
ANISOU 838 OE1 GLN A 336 9490 8750 8447 -578 1197 575 O
ATOM 839 NE2 GLN A 336 -13.468 33.646 5.266 1.00 60.19 N
ANISOU 839 NE2 GLN A 336 8535 7307 7029 -519 1037 576 N
ATOM 840 N TYR A 337 -16.541 35.154 8.880 1.00 48.21 N
ANISOU 840 N TYR A 337 7055 5442 5821 -393 523 274 N
ATOM 841 CA TYR A 337 -16.853 36.564 9.166 1.00 48.87 C
ANISOU 841 CA TYR A 337 7253 5364 5951 -416 403 282 C
ATOM 842 C TYR A 337 -17.187 36.742 10.666 1.00 53.76 C
ANISOU 842 C TYR A 337 7793 5975 6659 -385 319 153 C
ATOM 843 O TYR A 337 -16.613 37.614 11.330 1.00 54.03 O
ANISOU 843 O TYR A 337 7836 5925 6768 -473 269 146 O
ATOM 844 CB TYR A 337 -18.030 37.040 8.285 1.00 50.31 C
ANISOU 844 CB TYR A 337 7594 5464 6058 -301 309 286 C
ATOM 845 CG TYR A 337 -18.434 38.483 8.522 1.00 53.93 C
ANISOU 845 CG TYR A 337 8192 5722 6575 -286 175 294 C
ATOM 846 CD1 TYR A 337 -17.698 39.535 7.973 1.00 56.91 C
ANISOU 846 CD1 TYR A 337 8705 5949 6971 -406 178 443 C
ATOM 847 CD2 TYR A 337 -19.536 38.803 9.316 1.00 53.64 C
ANISOU 847 CD2 TYR A 337 8153 5642 6588 -150 52 152 C
ATOM 848 CE1 TYR A 337 -18.039 40.865 8.223 1.00 56.06 C
ANISOU 848 CE1 TYR A 337 8746 5608 6944 -393 46 447 C
ATOM 849 CE2 TYR A 337 -19.894 40.132 9.559 1.00 55.09 C
ANISOU 849 CE2 TYR A 337 8474 5620 6836 -107 -76 136 C
ATOM 850 CZ TYR A 337 -19.146 41.157 9.003 1.00 61.77 C
ANISOU 850 CZ TYR A 337 9477 6277 7716 -228 -87 283 C
ATOM 851 OH TYR A 337 -19.494 42.469 9.219 1.00 66.65 O
ANISOU 851 OH TYR A 337 10256 6647 8421 -183 -222 269 O
ATOM 852 N LEU A 338 -18.086 35.874 11.192 1.00 48.51 N
ANISOU 852 N LEU A 338 7047 5408 5978 -270 310 50 N
ATOM 853 CA LEU A 338 -18.519 35.856 12.584 1.00 46.59 C
ANISOU 853 CA LEU A 338 6719 5209 5775 -219 259 -65 C
ATOM 854 C LEU A 338 -17.319 35.767 13.520 1.00 53.56 C
ANISOU 854 C LEU A 338 7499 6155 6698 -321 293 -53 C
ATOM 855 O LEU A 338 -17.183 36.590 14.426 1.00 55.30 O
ANISOU 855 O LEU A 338 7727 6333 6950 -340 211 -126 O
ATOM 856 CB LEU A 338 -19.451 34.654 12.830 1.00 44.15 C
ANISOU 856 CB LEU A 338 6311 5024 5439 -124 296 -124 C
ATOM 857 CG LEU A 338 -20.882 34.704 12.246 1.00 46.58 C
ANISOU 857 CG LEU A 338 6663 5316 5720 -10 231 -184 C
ATOM 858 CD1 LEU A 338 -21.763 33.520 12.807 1.00 42.97 C
ANISOU 858 CD1 LEU A 338 6065 4991 5271 41 273 -249 C
ATOM 859 CD2 LEU A 338 -21.555 36.061 12.515 1.00 48.04 C
ANISOU 859 CD2 LEU A 338 6936 5395 5921 73 106 -252 C
ATOM 860 N HIS A 339 -16.429 34.784 13.269 1.00 48.82 N
ANISOU 860 N HIS A 339 6800 5655 6092 -373 403 27 N
ATOM 861 CA HIS A 339 -15.250 34.502 14.086 1.00 46.93 C
ANISOU 861 CA HIS A 339 6430 5513 5887 -446 432 50 C
ATOM 862 C HIS A 339 -14.251 35.643 14.027 1.00 53.58 C
ANISOU 862 C HIS A 339 7293 6279 6787 -592 391 85 C
ATOM 863 O HIS A 339 -13.808 36.134 15.074 1.00 54.50 O
ANISOU 863 O HIS A 339 7355 6413 6938 -644 313 22 O
ATOM 864 CB HIS A 339 -14.652 33.136 13.717 1.00 45.35 C
ANISOU 864 CB HIS A 339 6124 5427 5678 -426 557 122 C
ATOM 865 CG HIS A 339 -15.552 31.960 14.036 1.00 46.09 C
ANISOU 865 CG HIS A 339 6188 5573 5749 -312 586 86 C
ATOM 866 ND1 HIS A 339 -15.173 30.662 13.732 1.00 46.18 N
ANISOU 866 ND1 HIS A 339 6134 5642 5772 -272 685 133 N
ATOM 867 CD2 HIS A 339 -16.764 31.924 14.653 1.00 46.36 C
ANISOU 867 CD2 HIS A 339 6243 5607 5766 -241 533 11 C
ATOM 868 CE1 HIS A 339 -16.163 29.886 14.155 1.00 44.85 C
ANISOU 868 CE1 HIS A 339 5960 5479 5602 -202 683 97 C
ATOM 869 NE2 HIS A 339 -17.142 30.596 14.710 1.00 45.27 N
ANISOU 869 NE2 HIS A 339 6050 5518 5633 -186 602 29 N
ATOM 870 N GLU A 340 -14.010 36.157 12.814 1.00 51.15 N
ANISOU 870 N GLU A 340 7080 5874 6480 -663 431 177 N
ATOM 871 CA GLU A 340 -13.171 37.332 12.580 1.00 51.96 C
ANISOU 871 CA GLU A 340 7226 5863 6653 -831 400 239 C
ATOM 872 C GLU A 340 -13.637 38.542 13.395 1.00 57.21 C
ANISOU 872 C GLU A 340 7994 6365 7378 -845 240 128 C
ATOM 873 O GLU A 340 -12.802 39.269 13.922 1.00 58.95 O
ANISOU 873 O GLU A 340 8179 6534 7685 -992 182 111 O
ATOM 874 CB GLU A 340 -13.180 37.684 11.104 1.00 53.57 C
ANISOU 874 CB GLU A 340 7558 5981 6815 -874 471 375 C
ATOM 875 CG GLU A 340 -12.356 36.703 10.311 1.00 62.05 C
ANISOU 875 CG GLU A 340 8519 7222 7836 -897 639 475 C
ATOM 876 CD GLU A 340 -12.115 37.041 8.859 1.00 78.40 C
ANISOU 876 CD GLU A 340 10698 9260 9831 -956 737 624 C
ATOM 877 OE1 GLU A 340 -12.954 37.750 8.251 1.00 61.49 O
ANISOU 877 OE1 GLU A 340 8753 6971 7641 -917 668 656 O
ATOM 878 OE2 GLU A 340 -11.096 36.550 8.318 1.00 75.89 O
ANISOU 878 OE2 GLU A 340 10264 9083 9488 -1021 887 711 O
ATOM 879 N ASN A 341 -14.968 38.701 13.545 1.00 52.62 N
ANISOU 879 N ASN A 341 7521 5716 6756 -686 166 34 N
ATOM 880 CA ASN A 341 -15.639 39.769 14.273 1.00 52.60 C
ANISOU 880 CA ASN A 341 7629 5562 6796 -634 21 -101 C
ATOM 881 C ASN A 341 -15.937 39.498 15.729 1.00 56.86 C
ANISOU 881 C ASN A 341 8072 6225 7306 -548 -36 -269 C
ATOM 882 O ASN A 341 -16.611 40.313 16.358 1.00 57.92 O
ANISOU 882 O ASN A 341 8296 6258 7453 -466 -147 -412 O
ATOM 883 CB ASN A 341 -16.900 40.168 13.543 1.00 51.82 C
ANISOU 883 CB ASN A 341 7689 5332 6666 -490 -27 -103 C
ATOM 884 CG ASN A 341 -16.575 40.957 12.312 1.00 63.28 C
ANISOU 884 CG ASN A 341 9297 6597 8148 -586 -24 56 C
ATOM 885 OD1 ASN A 341 -16.274 42.153 12.375 1.00 60.65 O
ANISOU 885 OD1 ASN A 341 9090 6044 7911 -676 -110 64 O
ATOM 886 ND2 ASN A 341 -16.515 40.277 11.187 1.00 49.56 N
ANISOU 886 ND2 ASN A 341 7556 4946 6327 -584 82 191 N
ATOM 887 N GLY A 342 -15.437 38.381 16.257 1.00 52.40 N
ANISOU 887 N GLY A 342 7337 5878 6695 -552 40 -250 N
ATOM 888 CA GLY A 342 -15.594 38.001 17.660 1.00 51.52 C
ANISOU 888 CA GLY A 342 7129 5925 6523 -478 2 -370 C
ATOM 889 C GLY A 342 -16.944 37.451 18.074 1.00 54.46 C
ANISOU 889 C GLY A 342 7494 6389 6810 -296 25 -439 C
ATOM 890 O GLY A 342 -17.277 37.496 19.258 1.00 55.19 O
ANISOU 890 O GLY A 342 7547 6589 6834 -221 -17 -556 O
ATOM 891 N ILE A 343 -17.706 36.885 17.122 1.00 49.53 N
ANISOU 891 N ILE A 343 6894 5747 6179 -232 96 -369 N
ATOM 892 CA ILE A 343 -19.039 36.297 17.348 1.00 48.37 C
ANISOU 892 CA ILE A 343 6714 5689 5976 -88 126 -421 C
ATOM 893 C ILE A 343 -19.023 34.796 17.102 1.00 51.88 C
ANISOU 893 C ILE A 343 7051 6261 6401 -92 246 -317 C
ATOM 894 O ILE A 343 -18.562 34.359 16.049 1.00 51.78 O
ANISOU 894 O ILE A 343 7054 6201 6417 -148 300 -220 O
ATOM 895 CB ILE A 343 -20.121 36.984 16.430 1.00 50.62 C
ANISOU 895 CB ILE A 343 7115 5833 6285 1 70 -455 C
ATOM 896 CG1 ILE A 343 -20.049 38.532 16.447 1.00 50.80 C
ANISOU 896 CG1 ILE A 343 7287 5654 6360 5 -56 -531 C
ATOM 897 CG2 ILE A 343 -21.560 36.404 16.614 1.00 48.97 C
ANISOU 897 CG2 ILE A 343 6832 5738 6037 142 94 -519 C
ATOM 898 CD1 ILE A 343 -20.627 39.207 17.688 1.00 58.90 C
ANISOU 898 CD1 ILE A 343 8317 6700 7361 122 -136 -721 C
ATOM 899 N ILE A 344 -19.553 34.023 18.063 1.00 50.17 N
ANISOU 899 N ILE A 344 6736 6197 6130 -29 291 -339 N
ATOM 900 CA ILE A 344 -19.766 32.564 17.990 1.00 50.24 C
ANISOU 900 CA ILE A 344 6656 6296 6139 -26 398 -246 C
ATOM 901 C ILE A 344 -21.299 32.405 17.924 1.00 51.31 C
ANISOU 901 C ILE A 344 6767 6461 6267 55 409 -308 C
ATOM 902 O ILE A 344 -21.971 32.831 18.855 1.00 50.97 O
ANISOU 902 O ILE A 344 6690 6506 6170 128 389 -395 O
ATOM 903 CB ILE A 344 -19.234 31.773 19.223 1.00 54.55 C
ANISOU 903 CB ILE A 344 7104 6993 6630 -26 446 -188 C
ATOM 904 CG1 ILE A 344 -17.798 32.101 19.592 1.00 55.68 C
ANISOU 904 CG1 ILE A 344 7232 7155 6768 -87 401 -161 C
ATOM 905 CG2 ILE A 344 -19.406 30.259 19.023 1.00 56.66 C
ANISOU 905 CG2 ILE A 344 7310 7288 6930 -30 554 -72 C
ATOM 906 CD1 ILE A 344 -17.582 31.758 21.073 1.00 58.55 C
ANISOU 906 CD1 ILE A 344 7520 7697 7028 -45 393 -153 C
ATOM 907 N HIS A 345 -21.830 31.803 16.849 1.00 45.70 N
ANISOU 907 N HIS A 345 6062 5697 5605 46 437 -279 N
ATOM 908 CA HIS A 345 -23.266 31.594 16.645 1.00 45.22 C
ANISOU 908 CA HIS A 345 5947 5675 5558 104 434 -340 C
ATOM 909 C HIS A 345 -23.899 30.677 17.731 1.00 50.88 C
ANISOU 909 C HIS A 345 6528 6544 6259 106 524 -317 C
ATOM 910 O HIS A 345 -24.953 30.997 18.287 1.00 51.19 O
ANISOU 910 O HIS A 345 6491 6685 6272 174 521 -395 O
ATOM 911 CB HIS A 345 -23.530 31.080 15.229 1.00 45.28 C
ANISOU 911 CB HIS A 345 5992 5600 5612 76 426 -322 C
ATOM 912 CG HIS A 345 -24.978 31.075 14.868 1.00 49.75 C
ANISOU 912 CG HIS A 345 6497 6207 6198 133 380 -404 C
ATOM 913 ND1 HIS A 345 -25.816 30.023 15.238 1.00 52.10 N
ANISOU 913 ND1 HIS A 345 6657 6597 6540 99 445 -404 N
ATOM 914 CD2 HIS A 345 -25.706 31.996 14.203 1.00 51.96 C
ANISOU 914 CD2 HIS A 345 6824 6451 6468 221 271 -479 C
ATOM 915 CE1 HIS A 345 -27.010 30.335 14.781 1.00 51.93 C
ANISOU 915 CE1 HIS A 345 6579 6615 6537 159 373 -493 C
ATOM 916 NE2 HIS A 345 -26.998 31.511 14.154 1.00 52.71 N
ANISOU 916 NE2 HIS A 345 6786 6641 6598 250 262 -542 N
ATOM 917 N ARG A 346 -23.258 29.530 17.998 1.00 47.88 N
ANISOU 917 N ARG A 346 6115 6179 5897 37 610 -201 N
ATOM 918 CA ARG A 346 -23.645 28.561 19.016 1.00 47.27 C
ANISOU 918 CA ARG A 346 5936 6221 5805 17 708 -123 C
ATOM 919 C ARG A 346 -24.927 27.740 18.724 1.00 52.32 C
ANISOU 919 C ARG A 346 6479 6879 6520 -24 761 -123 C
ATOM 920 O ARG A 346 -25.262 26.859 19.511 1.00 55.00 O
ANISOU 920 O ARG A 346 6735 7300 6862 -68 858 -30 O
ATOM 921 CB ARG A 346 -23.674 29.234 20.408 1.00 44.20 C
ANISOU 921 CB ARG A 346 5513 5993 5290 84 709 -155 C
ATOM 922 CG ARG A 346 -22.303 29.525 21.027 1.00 38.86 C
ANISOU 922 CG ARG A 346 4889 5332 4543 86 675 -115 C
ATOM 923 CD ARG A 346 -22.397 30.100 22.428 1.00 48.46 C
ANISOU 923 CD ARG A 346 6076 6728 5608 155 665 -168 C
ATOM 924 NE ARG A 346 -23.349 29.357 23.257 1.00 75.05 N
ANISOU 924 NE ARG A 346 9344 10261 8910 172 780 -104 N
ATOM 925 CZ ARG A 346 -24.254 29.915 24.055 1.00108.68 C
ANISOU 925 CZ ARG A 346 13548 14685 13059 254 804 -205 C
ATOM 926 NH1 ARG A 346 -24.300 31.238 24.198 1.00101.90 N
ANISOU 926 NH1 ARG A 346 12743 13827 12148 345 704 -393 N
ATOM 927 NH2 ARG A 346 -25.120 29.157 24.717 1.00105.65 N
ANISOU 927 NH2 ARG A 346 13056 14466 12622 248 934 -119 N
ATOM 928 N ASP A 347 -25.636 28.001 17.626 1.00 47.49 N
ANISOU 928 N ASP A 347 5874 6200 5969 -20 694 -217 N
ATOM 929 CA ASP A 347 -26.855 27.255 17.300 1.00 48.24 C
ANISOU 929 CA ASP A 347 5854 6324 6150 -76 719 -240 C
ATOM 930 C ASP A 347 -27.039 27.046 15.778 1.00 55.03 C
ANISOU 930 C ASP A 347 6771 7056 7082 -105 635 -309 C
ATOM 931 O ASP A 347 -28.130 27.257 15.230 1.00 56.10 O
ANISOU 931 O ASP A 347 6831 7235 7251 -89 567 -406 O
ATOM 932 CB ASP A 347 -28.089 27.893 17.976 1.00 50.69 C
ANISOU 932 CB ASP A 347 6024 6811 6423 -7 722 -322 C
ATOM 933 CG ASP A 347 -29.362 27.060 17.961 1.00 58.93 C
ANISOU 933 CG ASP A 347 6889 7940 7561 -91 778 -323 C
ATOM 934 OD1 ASP A 347 -29.262 25.808 17.981 1.00 60.20 O
ANISOU 934 OD1 ASP A 347 7029 8037 7809 -227 855 -218 O
ATOM 935 OD2 ASP A 347 -30.451 27.654 17.917 1.00 64.49 O
ANISOU 935 OD2 ASP A 347 7469 8769 8267 -22 740 -431 O
ATOM 936 N LEU A 348 -25.950 26.627 15.087 1.00 50.29 N
ANISOU 936 N LEU A 348 6296 6321 6492 -134 636 -264 N
ATOM 937 CA LEU A 348 -25.986 26.374 13.640 1.00 48.38 C
ANISOU 937 CA LEU A 348 6129 5976 6277 -151 569 -333 C
ATOM 938 C LEU A 348 -26.635 25.020 13.365 1.00 52.80 C
ANISOU 938 C LEU A 348 6620 6487 6956 -257 599 -349 C
ATOM 939 O LEU A 348 -26.212 24.002 13.913 1.00 52.88 O
ANISOU 939 O LEU A 348 6623 6434 7034 -323 695 -256 O
ATOM 940 CB LEU A 348 -24.570 26.422 13.029 1.00 46.67 C
ANISOU 940 CB LEU A 348 6056 5662 6016 -135 584 -287 C
ATOM 941 CG LEU A 348 -23.872 27.773 12.997 1.00 49.50 C
ANISOU 941 CG LEU A 348 6496 6031 6281 -70 540 -275 C
ATOM 942 CD1 LEU A 348 -22.442 27.622 12.596 1.00 48.06 C
ANISOU 942 CD1 LEU A 348 6398 5785 6075 -84 590 -208 C
ATOM 943 CD2 LEU A 348 -24.576 28.753 12.068 1.00 51.94 C
ANISOU 943 CD2 LEU A 348 6860 6336 6539 -9 422 -357 C
ATOM 944 N LYS A 349 -27.721 25.033 12.582 1.00 49.55 N
ANISOU 944 N LYS A 349 6150 6101 6576 -273 507 -466 N
ATOM 945 CA LYS A 349 -28.484 23.855 12.150 1.00 49.07 C
ANISOU 945 CA LYS A 349 6016 5987 6643 -395 498 -524 C
ATOM 946 C LYS A 349 -29.207 24.181 10.843 1.00 56.51 C
ANISOU 946 C LYS A 349 6964 6952 7555 -366 341 -680 C
ATOM 947 O LYS A 349 -29.273 25.366 10.493 1.00 56.17 O
ANISOU 947 O LYS A 349 6964 6981 7399 -242 255 -711 O
ATOM 948 CB LYS A 349 -29.427 23.316 13.255 1.00 49.86 C
ANISOU 948 CB LYS A 349 5924 6171 6849 -497 581 -466 C
ATOM 949 CG LYS A 349 -30.253 24.339 13.987 1.00 56.06 C
ANISOU 949 CG LYS A 349 6563 7159 7577 -422 572 -485 C
ATOM 950 CD LYS A 349 -30.664 23.802 15.336 1.00 67.49 C
ANISOU 950 CD LYS A 349 7866 8704 9073 -504 719 -366 C
ATOM 951 CE LYS A 349 -31.978 24.413 15.782 1.00 80.04 C
ANISOU 951 CE LYS A 349 9236 10515 10659 -471 712 -434 C
ATOM 952 NZ LYS A 349 -32.167 24.316 17.255 1.00 93.27 N
ANISOU 952 NZ LYS A 349 10798 12344 12295 -490 875 -310 N
ATOM 953 N PRO A 350 -29.729 23.185 10.071 1.00 55.66 N
ANISOU 953 N PRO A 350 6831 6776 7540 -470 285 -784 N
ATOM 954 CA PRO A 350 -30.432 23.518 8.824 1.00 56.52 C
ANISOU 954 CA PRO A 350 6943 6940 7591 -430 111 -943 C
ATOM 955 C PRO A 350 -31.599 24.483 8.992 1.00 61.80 C
ANISOU 955 C PRO A 350 7448 7794 8240 -357 10 -990 C
ATOM 956 O PRO A 350 -31.887 25.246 8.063 1.00 62.95 O
ANISOU 956 O PRO A 350 7644 8000 8274 -244 -140 -1070 O
ATOM 957 CB PRO A 350 -30.908 22.152 8.325 1.00 59.88 C
ANISOU 957 CB PRO A 350 7327 7265 8158 -590 78 -1053 C
ATOM 958 CG PRO A 350 -29.944 21.191 8.914 1.00 63.04 C
ANISOU 958 CG PRO A 350 7815 7490 8647 -660 235 -945 C
ATOM 959 CD PRO A 350 -29.717 21.723 10.277 1.00 57.38 C
ANISOU 959 CD PRO A 350 7028 6852 7920 -627 360 -769 C
ATOM 960 N GLU A 351 -32.250 24.486 10.173 1.00 58.16 N
ANISOU 960 N GLU A 351 6794 7433 7871 -401 95 -933 N
ATOM 961 CA GLU A 351 -33.390 25.401 10.417 1.00 58.34 C
ANISOU 961 CA GLU A 351 6633 7653 7883 -304 15 -991 C
ATOM 962 C GLU A 351 -33.016 26.885 10.574 1.00 59.74 C
ANISOU 962 C GLU A 351 6913 7869 7915 -93 -20 -958 C
ATOM 963 O GLU A 351 -33.899 27.746 10.555 1.00 60.41 O
ANISOU 963 O GLU A 351 6884 8088 7980 36 -117 -1025 O
ATOM 964 CB GLU A 351 -34.405 24.883 11.473 1.00 60.39 C
ANISOU 964 CB GLU A 351 6615 8046 8283 -422 116 -968 C
ATOM 965 CG GLU A 351 -33.803 24.050 12.584 1.00 68.13 C
ANISOU 965 CG GLU A 351 7611 8950 9324 -551 320 -812 C
ATOM 966 CD GLU A 351 -33.777 22.547 12.372 1.00 87.73 C
ANISOU 966 CD GLU A 351 10092 11274 11966 -773 364 -794 C
ATOM 967 OE1 GLU A 351 -34.865 21.932 12.439 1.00109.82 O
ANISOU 967 OE1 GLU A 351 12674 14141 14910 -926 356 -841 O
ATOM 968 OE2 GLU A 351 -32.671 21.970 12.253 1.00 62.32 O
ANISOU 968 OE2 GLU A 351 7075 7863 8742 -798 419 -726 O
ATOM 969 N ASN A 352 -31.697 27.179 10.688 1.00 53.22 N
ANISOU 969 N ASN A 352 6301 6917 7002 -57 49 -861 N
ATOM 970 CA ASN A 352 -31.162 28.543 10.821 1.00 51.14 C
ANISOU 970 CA ASN A 352 6168 6640 6623 104 19 -823 C
ATOM 971 C ASN A 352 -30.363 28.991 9.591 1.00 52.68 C
ANISOU 971 C ASN A 352 6592 6719 6704 159 -68 -809 C
ATOM 972 O ASN A 352 -29.694 30.028 9.619 1.00 50.26 O
ANISOU 972 O ASN A 352 6427 6353 6318 248 -76 -748 O
ATOM 973 CB ASN A 352 -30.348 28.693 12.108 1.00 50.51 C
ANISOU 973 CB ASN A 352 6112 6544 6533 92 166 -721 C
ATOM 974 CG ASN A 352 -31.171 28.598 13.358 1.00 76.78 C
ANISOU 974 CG ASN A 352 9233 10025 9913 85 252 -725 C
ATOM 975 OD1 ASN A 352 -32.346 28.992 13.408 1.00 85.65 O
ANISOU 975 OD1 ASN A 352 10193 11286 11065 155 193 -813 O
ATOM 976 ND2 ASN A 352 -30.568 28.064 14.397 1.00 62.43 N
ANISOU 976 ND2 ASN A 352 7411 8210 8101 10 398 -624 N
ATOM 977 N VAL A 353 -30.430 28.190 8.515 1.00 50.39 N
ANISOU 977 N VAL A 353 6340 6401 6407 94 -126 -868 N
ATOM 978 CA VAL A 353 -29.772 28.484 7.240 1.00 50.08 C
ANISOU 978 CA VAL A 353 6506 6294 6228 145 -198 -862 C
ATOM 979 C VAL A 353 -30.918 28.701 6.233 1.00 58.37 C
ANISOU 979 C VAL A 353 7508 7440 7229 219 -395 -977 C
ATOM 980 O VAL A 353 -31.654 27.751 5.946 1.00 60.22 O
ANISOU 980 O VAL A 353 7617 7726 7538 130 -446 -1092 O
ATOM 981 CB VAL A 353 -28.754 27.393 6.797 1.00 50.95 C
ANISOU 981 CB VAL A 353 6722 6305 6330 39 -96 -850 C
ATOM 982 CG1 VAL A 353 -28.088 27.770 5.483 1.00 50.30 C
ANISOU 982 CG1 VAL A 353 6844 6197 6073 104 -147 -840 C
ATOM 983 CG2 VAL A 353 -27.710 27.130 7.887 1.00 48.17 C
ANISOU 983 CG2 VAL A 353 6377 5883 6044 -19 79 -734 C
ATOM 984 N LEU A 354 -31.113 29.974 5.776 1.00 54.16 N
ANISOU 984 N LEU A 354 7067 6928 6586 382 -517 -945 N
ATOM 985 CA LEU A 354 -32.184 30.347 4.847 1.00 54.91 C
ANISOU 985 CA LEU A 354 7120 7129 6615 495 -729 -1034 C
ATOM 986 C LEU A 354 -31.708 30.459 3.408 1.00 59.02 C
ANISOU 986 C LEU A 354 7860 7629 6937 542 -822 -1016 C
ATOM 987 O LEU A 354 -30.598 30.944 3.163 1.00 56.92 O
ANISOU 987 O LEU A 354 7801 7261 6564 555 -739 -887 O
ATOM 988 CB LEU A 354 -32.858 31.662 5.255 1.00 55.05 C
ANISOU 988 CB LEU A 354 7088 7188 6642 682 -826 -1011 C
ATOM 989 CG LEU A 354 -33.334 31.814 6.689 1.00 57.54 C
ANISOU 989 CG LEU A 354 7202 7554 7107 686 -731 -1033 C
ATOM 990 CD1 LEU A 354 -33.486 33.266 7.040 1.00 57.12 C
ANISOU 990 CD1 LEU A 354 7211 7463 7031 890 -794 -993 C
ATOM 991 CD2 LEU A 354 -34.617 31.087 6.906 1.00 60.37 C
ANISOU 991 CD2 LEU A 354 7266 8088 7584 639 -780 -1163 C
ATOM 992 N LEU A 355 -32.576 30.048 2.461 1.00 56.93 N
ANISOU 992 N LEU A 355 7537 7480 6613 564 -997 -1146 N
ATOM 993 CA LEU A 355 -32.310 30.099 1.019 1.00 58.52 C
ANISOU 993 CA LEU A 355 7938 7713 6586 626 -1111 -1153 C
ATOM 994 C LEU A 355 -32.998 31.335 0.394 1.00 64.13 C
ANISOU 994 C LEU A 355 8706 8497 7163 842 -1322 -1099 C
ATOM 995 O LEU A 355 -34.138 31.653 0.742 1.00 63.44 O
ANISOU 995 O LEU A 355 8422 8506 7175 931 -1457 -1168 O
ATOM 996 CB LEU A 355 -32.750 28.786 0.302 1.00 59.88 C
ANISOU 996 CB LEU A 355 8039 7962 6750 515 -1191 -1354 C
ATOM 997 CG LEU A 355 -32.466 27.409 0.968 1.00 61.74 C
ANISOU 997 CG LEU A 355 8168 8110 7179 305 -1030 -1442 C
ATOM 998 CD1 LEU A 355 -32.752 26.279 0.020 1.00 62.89 C
ANISOU 998 CD1 LEU A 355 8318 8291 7285 218 -1134 -1646 C
ATOM 999 CD2 LEU A 355 -31.055 27.285 1.435 1.00 59.56 C
ANISOU 999 CD2 LEU A 355 8041 7686 6903 253 -795 -1309 C
ATOM 1000 N SER A 356 -32.294 32.041 -0.503 1.00 62.68 N
ANISOU 1000 N SER A 356 8788 8270 6758 932 -1341 -959 N
ATOM 1001 CA SER A 356 -32.799 33.278 -1.098 1.00 65.39 C
ANISOU 1001 CA SER A 356 9237 8640 6967 1147 -1531 -857 C
ATOM 1002 C SER A 356 -33.935 33.125 -2.106 1.00 73.84 C
ANISOU 1002 C SER A 356 10241 9906 7909 1267 -1804 -983 C
ATOM 1003 O SER A 356 -34.764 34.033 -2.243 1.00 75.05 O
ANISOU 1003 O SER A 356 10361 10109 8045 1466 -1995 -947 O
ATOM 1004 CB SER A 356 -31.659 34.129 -1.646 1.00 69.23 C
ANISOU 1004 CB SER A 356 10032 9002 7271 1185 -1446 -627 C
ATOM 1005 OG SER A 356 -31.037 33.470 -2.735 1.00 84.12 O
ANISOU 1005 OG SER A 356 12068 10959 8936 1120 -1405 -634 O
ATOM 1006 N SER A 357 -33.975 31.990 -2.806 1.00 72.27 N
ANISOU 1006 N SER A 357 10020 9815 7625 1157 -1837 -1143 N
ATOM 1007 CA SER A 357 -35.010 31.698 -3.800 1.00 75.39 C
ANISOU 1007 CA SER A 357 10343 10415 7885 1242 -2111 -1301 C
ATOM 1008 C SER A 357 -35.335 30.205 -3.880 1.00 81.25 C
ANISOU 1008 C SER A 357 10915 11234 8722 1047 -2122 -1563 C
ATOM 1009 O SER A 357 -34.643 29.363 -3.299 1.00 79.69 O
ANISOU 1009 O SER A 357 10709 10914 8656 860 -1905 -1599 O
ATOM 1010 CB SER A 357 -34.639 32.263 -5.175 1.00 80.00 C
ANISOU 1010 CB SER A 357 11225 11064 8109 1388 -2223 -1183 C
ATOM 1011 OG SER A 357 -33.581 31.567 -5.815 1.00 86.18 O
ANISOU 1011 OG SER A 357 12200 11828 8716 1272 -2069 -1194 O
ATOM 1012 N GLN A 358 -36.387 29.882 -4.613 1.00 81.34 N
ANISOU 1012 N GLN A 358 10797 11439 8671 1093 -2389 -1745 N
ATOM 1013 CA GLN A 358 -36.834 28.507 -4.791 1.00 82.71 C
ANISOU 1013 CA GLN A 358 10807 11677 8942 902 -2451 -2019 C
ATOM 1014 C GLN A 358 -35.915 27.740 -5.784 1.00 86.23 C
ANISOU 1014 C GLN A 358 11514 12096 9155 835 -2395 -2103 C
ATOM 1015 O GLN A 358 -36.120 26.548 -6.029 1.00 85.66 O
ANISOU 1015 O GLN A 358 11365 12032 9150 675 -2436 -2345 O
ATOM 1016 CB GLN A 358 -38.322 28.490 -5.203 1.00 87.57 C
ANISOU 1016 CB GLN A 358 11168 12528 9578 970 -2779 -2199 C
ATOM 1017 CG GLN A 358 -39.283 29.062 -4.144 1.00103.89 C
ANISOU 1017 CG GLN A 358 12916 14647 11912 1022 -2808 -2163 C
ATOM 1018 CD GLN A 358 -39.460 30.573 -4.182 1.00127.13 C
ANISOU 1018 CD GLN A 358 15942 17618 14745 1318 -2896 -1956 C
ATOM 1019 OE1 GLN A 358 -38.684 31.325 -4.802 1.00119.59 O
ANISOU 1019 OE1 GLN A 358 15310 16585 13542 1461 -2876 -1770 O
ATOM 1020 NE2 GLN A 358 -40.488 31.057 -3.490 1.00123.25 N
ANISOU 1020 NE2 GLN A 358 15153 17228 14446 1416 -2983 -1978 N
ATOM 1021 N GLU A 359 -34.881 28.431 -6.313 1.00 82.62 N
ANISOU 1021 N GLU A 359 11360 11596 8437 953 -2285 -1901 N
ATOM 1022 CA GLU A 359 -33.881 27.893 -7.237 1.00 83.03 C
ANISOU 1022 CA GLU A 359 11671 11647 8230 931 -2187 -1941 C
ATOM 1023 C GLU A 359 -32.817 27.210 -6.413 1.00 82.65 C
ANISOU 1023 C GLU A 359 11639 11389 8375 764 -1872 -1913 C
ATOM 1024 O GLU A 359 -32.486 27.709 -5.335 1.00 80.50 O
ANISOU 1024 O GLU A 359 11304 10983 8301 735 -1706 -1733 O
ATOM 1025 CB GLU A 359 -33.245 29.020 -8.069 1.00 85.59 C
ANISOU 1025 CB GLU A 359 12284 12033 8204 1121 -2180 -1692 C
ATOM 1026 CG GLU A 359 -34.224 29.767 -8.965 1.00100.02 C
ANISOU 1026 CG GLU A 359 14138 14068 9796 1325 -2504 -1679 C
ATOM 1027 CD GLU A 359 -34.532 29.127 -10.305 1.00124.03 C
ANISOU 1027 CD GLU A 359 17284 17330 12512 1373 -2707 -1893 C
ATOM 1028 OE1 GLU A 359 -34.034 28.008 -10.573 1.00113.93 O
ANISOU 1028 OE1 GLU A 359 16049 16034 11205 1240 -2604 -2099 O
ATOM 1029 OE2 GLU A 359 -35.264 29.762 -11.098 1.00121.14 O
ANISOU 1029 OE2 GLU A 359 16966 17155 11907 1561 -2980 -1859 O
ATOM 1030 N GLU A 360 -32.298 26.062 -6.888 1.00 78.30 N
ANISOU 1030 N GLU A 360 11167 10810 7774 666 -1800 -2105 N
ATOM 1031 CA GLU A 360 -31.286 25.307 -6.144 1.00 75.33 C
ANISOU 1031 CA GLU A 360 10801 10234 7587 530 -1517 -2092 C
ATOM 1032 C GLU A 360 -29.937 26.010 -6.097 1.00 74.58 C
ANISOU 1032 C GLU A 360 10898 10084 7355 597 -1273 -1832 C
ATOM 1033 O GLU A 360 -29.187 25.829 -5.150 1.00 69.69 O
ANISOU 1033 O GLU A 360 10235 9308 6936 512 -1052 -1730 O
ATOM 1034 CB GLU A 360 -31.211 23.815 -6.552 1.00 78.31 C
ANISOU 1034 CB GLU A 360 11190 10557 8008 414 -1522 -2392 C
ATOM 1035 CG GLU A 360 -30.603 23.531 -7.913 1.00 94.10 C
ANISOU 1035 CG GLU A 360 13438 12671 9642 518 -1536 -2513 C
ATOM 1036 CD GLU A 360 -30.512 22.064 -8.299 1.00124.14 C
ANISOU 1036 CD GLU A 360 17274 16394 13499 423 -1546 -2842 C
ATOM 1037 OE1 GLU A 360 -29.960 21.268 -7.504 1.00126.26 O
ANISOU 1037 OE1 GLU A 360 17497 16442 14036 308 -1355 -2862 O
ATOM 1038 OE2 GLU A 360 -30.943 21.723 -9.425 1.00116.23 O
ANISOU 1038 OE2 GLU A 360 16363 15544 12256 478 -1748 -3079 O
ATOM 1039 N ASP A 361 -29.647 26.828 -7.106 1.00 73.19 N
ANISOU 1039 N ASP A 361 10925 10047 6837 743 -1318 -1713 N
ATOM 1040 CA ASP A 361 -28.433 27.625 -7.152 1.00 71.87 C
ANISOU 1040 CA ASP A 361 10929 9847 6529 791 -1100 -1441 C
ATOM 1041 C ASP A 361 -28.897 28.979 -6.641 1.00 74.76 C
ANISOU 1041 C ASP A 361 11263 10181 6960 861 -1182 -1206 C
ATOM 1042 O ASP A 361 -29.571 29.729 -7.359 1.00 76.84 O
ANISOU 1042 O ASP A 361 11603 10567 7025 998 -1387 -1148 O
ATOM 1043 CB ASP A 361 -27.890 27.696 -8.594 1.00 76.78 C
ANISOU 1043 CB ASP A 361 11798 10648 6728 901 -1094 -1438 C
ATOM 1044 CG ASP A 361 -27.101 26.485 -9.092 1.00 88.95 C
ANISOU 1044 CG ASP A 361 13411 12209 8177 864 -945 -1645 C
ATOM 1045 OD1 ASP A 361 -26.825 25.557 -8.270 1.00 87.14 O
ANISOU 1045 OD1 ASP A 361 13053 11817 8240 747 -827 -1772 O
ATOM 1046 OD2 ASP A 361 -26.692 26.492 -10.283 1.00 95.23 O
ANISOU 1046 OD2 ASP A 361 14402 13182 8601 965 -928 -1664 O
ATOM 1047 N CYS A 362 -28.680 29.223 -5.348 1.00 68.46 N
ANISOU 1047 N CYS A 362 10336 9219 6455 779 -1053 -1101 N
ATOM 1048 CA CYS A 362 -29.126 30.455 -4.704 1.00 67.74 C
ANISOU 1048 CA CYS A 362 10203 9066 6468 848 -1122 -919 C
ATOM 1049 C CYS A 362 -28.201 30.898 -3.588 1.00 71.67 C
ANISOU 1049 C CYS A 362 10684 9391 7156 765 -897 -745 C
ATOM 1050 O CYS A 362 -27.294 30.156 -3.177 1.00 70.66 O
ANISOU 1050 O CYS A 362 10533 9201 7116 649 -695 -772 O
ATOM 1051 CB CYS A 362 -30.567 30.321 -4.215 1.00 68.04 C
ANISOU 1051 CB CYS A 362 10009 9149 6693 870 -1334 -1074 C
ATOM 1052 SG CYS A 362 -30.772 29.202 -2.805 1.00 69.50 S
ANISOU 1052 SG CYS A 362 9919 9230 7257 679 -1209 -1231 S
ATOM 1053 N LEU A 363 -28.438 32.122 -3.089 1.00 68.68 N
ANISOU 1053 N LEU A 363 10319 8933 6845 837 -947 -577 N
ATOM 1054 CA LEU A 363 -27.673 32.650 -1.968 1.00 66.37 C
ANISOU 1054 CA LEU A 363 10003 8477 6738 761 -774 -437 C
ATOM 1055 C LEU A 363 -28.296 32.170 -0.679 1.00 66.88 C
ANISOU 1055 C LEU A 363 9824 8502 7084 703 -771 -570 C
ATOM 1056 O LEU A 363 -29.521 32.082 -0.571 1.00 66.49 O
ANISOU 1056 O LEU A 363 9632 8527 7102 768 -941 -693 O
ATOM 1057 CB LEU A 363 -27.623 34.183 -1.988 1.00 67.45 C
ANISOU 1057 CB LEU A 363 10284 8513 6832 860 -832 -217 C
ATOM 1058 CG LEU A 363 -26.731 34.831 -3.045 1.00 73.29 C
ANISOU 1058 CG LEU A 363 11280 9247 7318 875 -769 -1 C
ATOM 1059 CD1 LEU A 363 -26.975 36.325 -3.088 1.00 74.62 C
ANISOU 1059 CD1 LEU A 363 11595 9285 7473 987 -881 205 C
ATOM 1060 CD2 LEU A 363 -25.245 34.546 -2.778 1.00 72.95 C
ANISOU 1060 CD2 LEU A 363 11267 9151 7301 711 -497 89 C
ATOM 1061 N ILE A 364 -27.456 31.809 0.280 1.00 61.80 N
ANISOU 1061 N ILE A 364 9120 7768 6595 581 -577 -543 N
ATOM 1062 CA ILE A 364 -27.926 31.369 1.596 1.00 60.07 C
ANISOU 1062 CA ILE A 364 8683 7519 6620 519 -542 -632 C
ATOM 1063 C ILE A 364 -27.567 32.448 2.622 1.00 63.46 C
ANISOU 1063 C ILE A 364 9119 7840 7153 537 -486 -503 C
ATOM 1064 O ILE A 364 -26.633 33.227 2.394 1.00 65.25 O
ANISOU 1064 O ILE A 364 9507 7982 7302 534 -421 -349 O
ATOM 1065 CB ILE A 364 -27.512 29.898 2.027 1.00 61.06 C
ANISOU 1065 CB ILE A 364 8705 7634 6860 376 -398 -736 C
ATOM 1066 CG1 ILE A 364 -26.009 29.736 2.333 1.00 60.32 C
ANISOU 1066 CG1 ILE A 364 8691 7460 6767 300 -188 -622 C
ATOM 1067 CG2 ILE A 364 -27.957 28.870 1.020 1.00 60.16 C
ANISOU 1067 CG2 ILE A 364 8596 7599 6663 360 -478 -902 C
ATOM 1068 CD1 ILE A 364 -25.534 30.230 3.720 1.00 66.25 C
ANISOU 1068 CD1 ILE A 364 9368 8131 7672 257 -86 -521 C
ATOM 1069 N LYS A 365 -28.302 32.499 3.730 1.00 56.70 N
ANISOU 1069 N LYS A 365 8088 6991 6466 551 -509 -571 N
ATOM 1070 CA LYS A 365 -28.037 33.442 4.814 1.00 54.08 C
ANISOU 1070 CA LYS A 365 7753 6564 6230 576 -463 -497 C
ATOM 1071 C LYS A 365 -28.254 32.735 6.133 1.00 55.41 C
ANISOU 1071 C LYS A 365 7718 6773 6562 500 -364 -575 C
ATOM 1072 O LYS A 365 -29.176 31.911 6.260 1.00 53.66 O
ANISOU 1072 O LYS A 365 7325 6655 6407 480 -396 -690 O
ATOM 1073 CB LYS A 365 -28.893 34.728 4.712 1.00 57.30 C
ANISOU 1073 CB LYS A 365 8204 6943 6625 756 -633 -481 C
ATOM 1074 CG LYS A 365 -28.586 35.581 3.476 1.00 62.92 C
ANISOU 1074 CG LYS A 365 9156 7583 7167 835 -723 -345 C
ATOM 1075 CD LYS A 365 -29.118 36.986 3.601 1.00 71.43 C
ANISOU 1075 CD LYS A 365 10321 8553 8266 1009 -863 -288 C
ATOM 1076 CE LYS A 365 -29.258 37.597 2.228 1.00 77.00 C
ANISOU 1076 CE LYS A 365 11229 9241 8786 1120 -1002 -167 C
ATOM 1077 NZ LYS A 365 -28.519 38.881 2.088 1.00 78.69 N
ANISOU 1077 NZ LYS A 365 11685 9236 8977 1141 -997 32 N
ATOM 1078 N ILE A 366 -27.351 33.005 7.092 1.00 51.61 N
ANISOU 1078 N ILE A 366 7257 6216 6138 440 -240 -505 N
ATOM 1079 CA ILE A 366 -27.369 32.473 8.448 1.00 50.40 C
ANISOU 1079 CA ILE A 366 6944 6104 6102 377 -135 -542 C
ATOM 1080 C ILE A 366 -28.279 33.391 9.232 1.00 56.32 C
ANISOU 1080 C ILE A 366 7616 6884 6901 502 -211 -601 C
ATOM 1081 O ILE A 366 -28.151 34.614 9.153 1.00 56.94 O
ANISOU 1081 O ILE A 366 7818 6867 6949 600 -287 -568 O
ATOM 1082 CB ILE A 366 -25.922 32.387 9.053 1.00 52.97 C
ANISOU 1082 CB ILE A 366 7328 6358 6439 275 7 -446 C
ATOM 1083 CG1 ILE A 366 -24.995 31.448 8.249 1.00 52.93 C
ANISOU 1083 CG1 ILE A 366 7385 6338 6387 183 95 -401 C
ATOM 1084 CG2 ILE A 366 -25.901 32.039 10.548 1.00 54.71 C
ANISOU 1084 CG2 ILE A 366 7408 6632 6746 237 97 -465 C
ATOM 1085 CD1 ILE A 366 -25.395 30.014 8.155 1.00 57.63 C
ANISOU 1085 CD1 ILE A 366 7877 6985 7033 127 132 -476 C
ATOM 1086 N THR A 367 -29.212 32.795 9.976 1.00 54.54 N
ANISOU 1086 N THR A 367 7184 6786 6754 500 -186 -688 N
ATOM 1087 CA THR A 367 -30.175 33.491 10.821 1.00 54.83 C
ANISOU 1087 CA THR A 367 7097 6902 6834 631 -229 -768 C
ATOM 1088 C THR A 367 -30.117 32.968 12.277 1.00 57.47 C
ANISOU 1088 C THR A 367 7285 7332 7221 563 -79 -779 C
ATOM 1089 O THR A 367 -29.385 32.020 12.562 1.00 53.77 O
ANISOU 1089 O THR A 367 6812 6853 6765 417 39 -711 O
ATOM 1090 CB THR A 367 -31.563 33.407 10.169 1.00 62.83 C
ANISOU 1090 CB THR A 367 7973 8033 7865 725 -362 -864 C
ATOM 1091 OG1 THR A 367 -32.400 34.444 10.681 1.00 70.60 O
ANISOU 1091 OG1 THR A 367 8885 9068 8872 918 -438 -939 O
ATOM 1092 CG2 THR A 367 -32.227 32.050 10.349 1.00 58.64 C
ANISOU 1092 CG2 THR A 367 7221 7645 7415 592 -298 -917 C
ATOM 1093 N ASP A 368 -30.898 33.600 13.183 1.00 57.97 N
ANISOU 1093 N ASP A 368 7230 7496 7301 689 -86 -863 N
ATOM 1094 CA ASP A 368 -31.081 33.238 14.602 1.00 58.66 C
ANISOU 1094 CA ASP A 368 7162 7726 7399 663 51 -883 C
ATOM 1095 C ASP A 368 -29.811 33.339 15.464 1.00 58.13 C
ANISOU 1095 C ASP A 368 7214 7590 7281 598 143 -815 C
ATOM 1096 O ASP A 368 -29.145 32.334 15.750 1.00 56.29 O
ANISOU 1096 O ASP A 368 6971 7364 7053 450 250 -721 O
ATOM 1097 CB ASP A 368 -31.860 31.898 14.749 1.00 62.14 C
ANISOU 1097 CB ASP A 368 7380 8322 7908 536 141 -874 C
ATOM 1098 CG ASP A 368 -32.180 31.427 16.155 1.00 85.15 C
ANISOU 1098 CG ASP A 368 10124 11410 10819 496 301 -859 C
ATOM 1099 OD1 ASP A 368 -32.348 32.299 17.061 1.00 88.07 O
ANISOU 1099 OD1 ASP A 368 10471 11865 11125 637 320 -927 O
ATOM 1100 OD2 ASP A 368 -32.313 30.191 16.349 1.00 94.81 O
ANISOU 1100 OD2 ASP A 368 11242 12684 12099 330 408 -782 O
ATOM 1101 N PHE A 369 -29.500 34.586 15.881 1.00 51.77 N
ANISOU 1101 N PHE A 369 6523 6711 6436 718 83 -873 N
ATOM 1102 CA PHE A 369 -28.343 34.903 16.702 1.00 49.29 C
ANISOU 1102 CA PHE A 369 6314 6339 6074 668 130 -844 C
ATOM 1103 C PHE A 369 -28.725 35.028 18.166 1.00 56.08 C
ANISOU 1103 C PHE A 369 7060 7374 6873 739 207 -928 C
ATOM 1104 O PHE A 369 -28.002 35.645 18.935 1.00 58.38 O
ANISOU 1104 O PHE A 369 7442 7631 7108 755 199 -965 O
ATOM 1105 CB PHE A 369 -27.624 36.142 16.159 1.00 50.32 C
ANISOU 1105 CB PHE A 369 6663 6248 6210 708 11 -849 C
ATOM 1106 CG PHE A 369 -26.961 35.886 14.820 1.00 50.29 C
ANISOU 1106 CG PHE A 369 6778 6106 6224 604 -20 -727 C
ATOM 1107 CD1 PHE A 369 -27.694 35.953 13.634 1.00 54.16 C
ANISOU 1107 CD1 PHE A 369 7289 6565 6726 668 -108 -723 C
ATOM 1108 CD2 PHE A 369 -25.607 35.595 14.743 1.00 49.82 C
ANISOU 1108 CD2 PHE A 369 6801 5972 6154 457 36 -622 C
ATOM 1109 CE1 PHE A 369 -27.093 35.699 12.399 1.00 54.39 C
ANISOU 1109 CE1 PHE A 369 7435 6498 6732 584 -126 -617 C
ATOM 1110 CE2 PHE A 369 -24.999 35.355 13.505 1.00 53.09 C
ANISOU 1110 CE2 PHE A 369 7316 6291 6566 376 31 -517 C
ATOM 1111 CZ PHE A 369 -25.745 35.394 12.344 1.00 52.29 C
ANISOU 1111 CZ PHE A 369 7250 6167 6452 439 -44 -516 C
ATOM 1112 N GLY A 370 -29.839 34.395 18.541 1.00 52.74 N
ANISOU 1112 N GLY A 370 6431 7153 6454 768 285 -956 N
ATOM 1113 CA GLY A 370 -30.393 34.365 19.885 1.00 53.89 C
ANISOU 1113 CA GLY A 370 6432 7525 6519 836 394 -1020 C
ATOM 1114 C GLY A 370 -29.511 33.722 20.930 1.00 61.32 C
ANISOU 1114 C GLY A 370 7387 8545 7368 725 510 -924 C
ATOM 1115 O GLY A 370 -29.521 34.156 22.084 1.00 64.77 O
ANISOU 1115 O GLY A 370 7807 9117 7686 813 553 -1001 O
ATOM 1116 N HIS A 371 -28.766 32.676 20.551 1.00 58.11 N
ANISOU 1116 N HIS A 371 7011 8064 7003 552 556 -762 N
ATOM 1117 CA HIS A 371 -27.835 31.942 21.427 1.00 58.13 C
ANISOU 1117 CA HIS A 371 7033 8124 6930 454 650 -637 C
ATOM 1118 C HIS A 371 -26.375 32.323 21.160 1.00 57.17 C
ANISOU 1118 C HIS A 371 7086 7830 6805 408 567 -605 C
ATOM 1119 O HIS A 371 -25.476 31.697 21.711 1.00 54.02 O
ANISOU 1119 O HIS A 371 6703 7462 6362 332 618 -494 O
ATOM 1120 CB HIS A 371 -28.007 30.417 21.259 1.00 60.08 C
ANISOU 1120 CB HIS A 371 7183 8399 7246 305 764 -471 C
ATOM 1121 CG HIS A 371 -29.396 29.945 21.537 1.00 66.68 C
ANISOU 1121 CG HIS A 371 7819 9411 8107 302 859 -480 C
ATOM 1122 ND1 HIS A 371 -30.207 29.460 20.527 1.00 69.91 N
ANISOU 1122 ND1 HIS A 371 8139 9768 8654 239 835 -491 N
ATOM 1123 CD2 HIS A 371 -30.098 29.957 22.692 1.00 70.99 C
ANISOU 1123 CD2 HIS A 371 8228 10199 8547 356 973 -492 C
ATOM 1124 CE1 HIS A 371 -31.358 29.150 21.108 1.00 71.16 C
ANISOU 1124 CE1 HIS A 371 8090 10133 8813 235 937 -498 C
ATOM 1125 NE2 HIS A 371 -31.338 29.434 22.410 1.00 72.28 N
ANISOU 1125 NE2 HIS A 371 8196 10463 8804 308 1036 -492 N
ATOM 1126 N SER A 372 -26.136 33.322 20.294 1.00 54.31 N
ANISOU 1126 N SER A 372 6848 7292 6497 450 440 -687 N
ATOM 1127 CA SER A 372 -24.778 33.717 19.947 1.00 53.41 C
ANISOU 1127 CA SER A 372 6878 7017 6399 379 371 -647 C
ATOM 1128 C SER A 372 -24.037 34.406 21.087 1.00 58.61 C
ANISOU 1128 C SER A 372 7583 7723 6965 404 334 -717 C
ATOM 1129 O SER A 372 -24.686 34.909 22.000 1.00 60.23 O
ANISOU 1129 O SER A 372 7754 8046 7085 518 331 -845 O
ATOM 1130 CB SER A 372 -24.724 34.447 18.610 1.00 55.61 C
ANISOU 1130 CB SER A 372 7277 7091 6760 387 268 -667 C
ATOM 1131 OG SER A 372 -25.365 35.705 18.666 1.00 67.33 O
ANISOU 1131 OG SER A 372 8824 8514 8243 521 167 -809 O
ATOM 1132 N LYS A 373 -22.698 34.307 21.115 1.00 55.27 N
ANISOU 1132 N LYS A 373 7213 7242 6544 300 314 -640 N
ATOM 1133 CA LYS A 373 -21.866 34.877 22.188 1.00 56.25 C
ANISOU 1133 CA LYS A 373 7367 7424 6582 298 256 -709 C
ATOM 1134 C LYS A 373 -20.788 35.799 21.618 1.00 63.31 C
ANISOU 1134 C LYS A 373 8375 8120 7558 210 144 -732 C
ATOM 1135 O LYS A 373 -20.383 35.608 20.474 1.00 62.43 O
ANISOU 1135 O LYS A 373 8299 7877 7546 127 155 -627 O
ATOM 1136 CB LYS A 373 -21.231 33.760 23.045 1.00 56.58 C
ANISOU 1136 CB LYS A 373 7318 7644 6536 252 335 -581 C
ATOM 1137 N ILE A 374 -20.343 36.807 22.402 1.00 63.74 N
ANISOU 1137 N ILE A 374 8489 8157 7570 222 38 -876 N
ATOM 1138 CA ILE A 374 -19.264 37.740 22.029 1.00 64.88 C
ANISOU 1138 CA ILE A 374 8730 8114 7807 104 -75 -905 C
ATOM 1139 C ILE A 374 -17.994 37.363 22.801 1.00 73.15 C
ANISOU 1139 C ILE A 374 9698 9294 8802 4 -97 -868 C
ATOM 1140 O ILE A 374 -18.042 37.229 24.021 1.00 73.31 O
ANISOU 1140 O ILE A 374 9671 9502 8681 71 -116 -952 O
ATOM 1141 CB ILE A 374 -19.625 39.234 22.228 1.00 68.53 C
ANISOU 1141 CB ILE A 374 9332 8404 8302 169 -208 -1109 C
ATOM 1142 CG1 ILE A 374 -20.810 39.632 21.358 1.00 68.60 C
ANISOU 1142 CG1 ILE A 374 9414 8278 8374 290 -205 -1128 C
ATOM 1143 CG2 ILE A 374 -18.417 40.125 21.923 1.00 68.99 C
ANISOU 1143 CG2 ILE A 374 9480 8256 8475 0 -321 -1119 C
ATOM 1144 CD1 ILE A 374 -21.616 40.788 21.924 1.00 75.06 C
ANISOU 1144 CD1 ILE A 374 10328 9012 9179 456 -304 -1359 C
ATOM 1145 N LEU A 375 -16.864 37.238 22.088 1.00 72.97 N
ANISOU 1145 N LEU A 375 9653 9191 8879 -146 -99 -746 N
ATOM 1146 CA LEU A 375 -15.550 36.855 22.625 1.00 74.58 C
ANISOU 1146 CA LEU A 375 9751 9522 9064 -244 -128 -692 C
ATOM 1147 C LEU A 375 -14.880 37.849 23.574 1.00 87.09 C
ANISOU 1147 C LEU A 375 11353 11118 10621 -301 -289 -865 C
ATOM 1148 O LEU A 375 -14.155 37.420 24.486 1.00 88.69 O
ANISOU 1148 O LEU A 375 11449 11519 10729 -310 -332 -866 O
ATOM 1149 CB LEU A 375 -14.628 36.418 21.496 1.00 73.12 C
ANISOU 1149 CB LEU A 375 9515 9266 9001 -370 -64 -521 C
ATOM 1150 CG LEU A 375 -15.174 35.239 20.712 1.00 75.12 C
ANISOU 1150 CG LEU A 375 9742 9540 9259 -305 84 -376 C
ATOM 1151 CD1 LEU A 375 -14.353 34.955 19.491 1.00 73.96 C
ANISOU 1151 CD1 LEU A 375 9572 9316 9215 -406 152 -243 C
ATOM 1152 CD2 LEU A 375 -15.257 34.037 21.585 1.00 78.64 C
ANISOU 1152 CD2 LEU A 375 10085 10189 9605 -218 144 -310 C
ATOM 1153 N GLY A 376 -15.163 39.140 23.369 1.00 94.85 N
ANISOU 1153 N GLY A 376 13306 10986 11748 -580 -480 636 N
ATOM 1154 CA GLY A 376 -14.716 40.285 24.171 1.00 97.53 C
ANISOU 1154 CA GLY A 376 13836 11203 12017 -599 -699 643 C
ATOM 1155 C GLY A 376 -13.352 40.257 24.848 1.00105.33 C
ANISOU 1155 C GLY A 376 14690 12240 13089 -737 -713 653 C
ATOM 1156 O GLY A 376 -12.323 40.094 24.179 1.00106.36 O
ANISOU 1156 O GLY A 376 14707 12440 13267 -1000 -621 686 O
ATOM 1157 N GLU A 377 -13.337 40.480 26.188 1.00102.78 N
ANISOU 1157 N GLU A 377 14386 11897 12768 -548 -843 625 N
ATOM 1158 CA GLU A 377 -12.119 40.494 27.010 1.00103.43 C
ANISOU 1158 CA GLU A 377 14342 12035 12920 -632 -886 618 C
ATOM 1159 C GLU A 377 -12.298 39.528 28.175 1.00105.16 C
ANISOU 1159 C GLU A 377 14353 12384 13218 -337 -803 588 C
ATOM 1160 O GLU A 377 -13.061 39.797 29.107 1.00105.26 O
ANISOU 1160 O GLU A 377 14473 12348 13173 -59 -924 566 O
ATOM 1161 CB GLU A 377 -11.770 41.916 27.489 1.00106.79 C
ANISOU 1161 CB GLU A 377 15048 12276 13253 -725 -1174 608 C
ATOM 1162 N THR A 378 -11.625 38.376 28.077 1.00 99.03 N
ANISOU 1162 N THR A 378 13284 11782 12560 -378 -589 595 N
ATOM 1163 CA THR A 378 -11.691 37.273 29.028 1.00 96.27 C
ANISOU 1163 CA THR A 378 12716 11566 12296 -124 -463 581 C
ATOM 1164 C THR A 378 -11.220 37.657 30.424 1.00 97.77 C
ANISOU 1164 C THR A 378 12908 11765 12476 28 -611 550 C
ATOM 1165 O THR A 378 -10.250 38.410 30.585 1.00 98.84 O
ANISOU 1165 O THR A 378 13087 11877 12593 -153 -748 531 O
ATOM 1166 CB THR A 378 -10.989 36.029 28.456 1.00103.26 C
ANISOU 1166 CB THR A 378 13334 12614 13286 -219 -214 591 C
ATOM 1167 OG1 THR A 378 -11.260 35.941 27.052 1.00105.81 O
ANISOU 1167 OG1 THR A 378 13698 12912 13594 -399 -125 611 O
ATOM 1168 CG2 THR A 378 -11.449 34.748 29.119 1.00100.42 C
ANISOU 1168 CG2 THR A 378 12801 12346 13009 50 -54 593 C
ATOM 1169 N SER A 379 -11.944 37.145 31.438 1.00 90.12 N
ANISOU 1169 N SER A 379 11890 10837 11515 363 -589 548 N
ATOM 1170 CA SER A 379 -11.607 37.334 32.837 1.00 88.62 C
ANISOU 1170 CA SER A 379 11682 10681 11310 582 -707 516 C
ATOM 1171 C SER A 379 -10.360 36.490 33.149 1.00 88.13 C
ANISOU 1171 C SER A 379 11353 10787 11347 528 -567 500 C
ATOM 1172 O SER A 379 -9.638 36.810 34.092 1.00 89.82 O
ANISOU 1172 O SER A 379 11540 11040 11549 600 -684 457 O
ATOM 1173 CB SER A 379 -12.780 36.948 33.736 1.00 91.59 C
ANISOU 1173 CB SER A 379 12063 11084 11655 965 -691 542 C
ATOM 1174 OG SER A 379 -13.143 35.584 33.591 1.00101.90 O
ANISOU 1174 OG SER A 379 13151 12507 13061 1055 -436 591 O
ATOM 1175 N LEU A 380 -10.093 35.443 32.331 1.00 78.82 N
ANISOU 1175 N LEU A 380 9988 9708 10250 412 -330 527 N
ATOM 1176 CA LEU A 380 -8.926 34.583 32.467 1.00 76.91 C
ANISOU 1176 CA LEU A 380 9501 9644 10078 373 -181 512 C
ATOM 1177 C LEU A 380 -7.647 35.367 32.169 1.00 84.05 C
ANISOU 1177 C LEU A 380 10388 10590 10956 79 -294 486 C
ATOM 1178 O LEU A 380 -6.678 35.241 32.922 1.00 83.87 O
ANISOU 1178 O LEU A 380 10225 10697 10945 118 -317 450 O
ATOM 1179 CB LEU A 380 -9.043 33.318 31.597 1.00 74.57 C
ANISOU 1179 CB LEU A 380 9057 9423 9852 340 76 542 C
ATOM 1180 CG LEU A 380 -7.909 32.289 31.684 1.00 77.14 C
ANISOU 1180 CG LEU A 380 9141 9942 10226 349 248 525 C
ATOM 1181 CD1 LEU A 380 -7.782 31.695 33.069 1.00 76.14 C
ANISOU 1181 CD1 LEU A 380 8909 9895 10124 661 282 513 C
ATOM 1182 CD2 LEU A 380 -8.115 31.196 30.706 1.00 76.87 C
ANISOU 1182 CD2 LEU A 380 9029 9940 10239 308 459 545 C
ATOM 1183 N MET A 381 -7.663 36.210 31.119 1.00 83.09 N
ANISOU 1183 N MET A 381 10413 10365 10792 -211 -374 509 N
ATOM 1184 CA MET A 381 -6.521 37.055 30.760 1.00 86.26 C
ANISOU 1184 CA MET A 381 10815 10794 11167 -537 -491 512 C
ATOM 1185 C MET A 381 -6.204 38.015 31.917 1.00 90.24 C
ANISOU 1185 C MET A 381 11432 11221 11634 -486 -754 462 C
ATOM 1186 O MET A 381 -5.037 38.159 32.284 1.00 91.46 O
ANISOU 1186 O MET A 381 11447 11502 11803 -619 -807 439 O
ATOM 1187 CB MET A 381 -6.775 37.823 29.454 1.00 90.39 C
ANISOU 1187 CB MET A 381 11517 11187 11641 -828 -534 563 C
ATOM 1188 CG MET A 381 -7.081 36.925 28.254 1.00 94.95 C
ANISOU 1188 CG MET A 381 11998 11837 12242 -872 -295 600 C
ATOM 1189 SD MET A 381 -7.744 37.856 26.824 1.00101.41 S
ANISOU 1189 SD MET A 381 13079 12473 12981 -1117 -359 654 S
ATOM 1190 CE MET A 381 -8.269 36.495 25.758 1.00 96.67 C
ANISOU 1190 CE MET A 381 12330 11979 12420 -1044 -76 662 C
ATOM 1191 N ARG A 382 -7.253 38.605 32.538 1.00 85.36 N
ANISOU 1191 N ARG A 382 11054 10420 10961 -266 -917 440 N
ATOM 1192 CA ARG A 382 -7.147 39.495 33.706 1.00 85.47 C
ANISOU 1192 CA ARG A 382 11219 10337 10920 -140 -1187 379 C
ATOM 1193 C ARG A 382 -6.556 38.747 34.932 1.00 86.19 C
ANISOU 1193 C ARG A 382 11079 10615 11055 110 -1136 327 C
ATOM 1194 O ARG A 382 -5.651 39.275 35.574 1.00 86.46 O
ANISOU 1194 O ARG A 382 11090 10681 11080 37 -1302 272 O
ATOM 1195 CB ARG A 382 -8.515 40.122 34.038 1.00 85.45 C
ANISOU 1195 CB ARG A 382 11508 10135 10822 112 -1338 372 C
ATOM 1196 N THR A 383 -7.045 37.507 35.218 1.00 79.82 N
ANISOU 1196 N THR A 383 10102 9931 10294 391 -905 348 N
ATOM 1197 CA THR A 383 -6.591 36.604 36.299 1.00 78.31 C
ANISOU 1197 CA THR A 383 9691 9924 10141 666 -803 317 C
ATOM 1198 C THR A 383 -5.112 36.221 36.089 1.00 81.98 C
ANISOU 1198 C THR A 383 9904 10595 10649 457 -717 293 C
ATOM 1199 O THR A 383 -4.351 36.176 37.052 1.00 82.14 O
ANISOU 1199 O THR A 383 9807 10739 10662 578 -781 233 O
ATOM 1200 CB THR A 383 -7.527 35.362 36.379 1.00 84.23 C
ANISOU 1200 CB THR A 383 10348 10722 10933 945 -561 374 C
ATOM 1201 OG1 THR A 383 -8.829 35.757 36.812 1.00 87.48 O
ANISOU 1201 OG1 THR A 383 10956 10998 11285 1177 -661 397 O
ATOM 1202 CG2 THR A 383 -7.030 34.293 37.318 1.00 80.07 C
ANISOU 1202 CG2 THR A 383 9598 10379 10445 1210 -415 361 C
ATOM 1203 N LEU A 384 -4.708 35.970 34.827 1.00 78.34 N
ANISOU 1203 N LEU A 384 9357 10192 10217 157 -577 338 N
ATOM 1204 CA LEU A 384 -3.335 35.604 34.482 1.00 78.68 C
ANISOU 1204 CA LEU A 384 9149 10469 10277 -44 -482 330 C
ATOM 1205 C LEU A 384 -2.367 36.750 34.662 1.00 86.96 C
ANISOU 1205 C LEU A 384 10216 11529 11294 -316 -720 298 C
ATOM 1206 O LEU A 384 -1.161 36.509 34.723 1.00 89.69 O
ANISOU 1206 O LEU A 384 10324 12113 11643 -430 -679 279 O
ATOM 1207 CB LEU A 384 -3.213 35.044 33.047 1.00 77.53 C
ANISOU 1207 CB LEU A 384 8915 10396 10148 -265 -273 394 C
ATOM 1208 CG LEU A 384 -3.826 33.681 32.720 1.00 77.98 C
ANISOU 1208 CG LEU A 384 8893 10492 10245 -50 -11 419 C
ATOM 1209 CD1 LEU A 384 -3.425 33.254 31.343 1.00 76.98 C
ANISOU 1209 CD1 LEU A 384 8668 10469 10113 -277 155 461 C
ATOM 1210 CD2 LEU A 384 -3.471 32.614 33.760 1.00 77.65 C
ANISOU 1210 CD2 LEU A 384 8672 10606 10224 280 111 381 C
ATOM 1211 N CYS A 385 -2.864 37.993 34.730 1.00 84.25 N
ANISOU 1211 N CYS A 385 10156 10939 10915 -424 -975 292 N
ATOM 1212 CA CYS A 385 -1.976 39.137 34.925 1.00 87.17 C
ANISOU 1212 CA CYS A 385 10584 11274 11262 -709 -1235 262 C
ATOM 1213 C CYS A 385 -1.432 39.198 36.350 1.00 91.65 C
ANISOU 1213 C CYS A 385 11073 11930 11821 -491 -1386 161 C
ATOM 1214 O CYS A 385 -0.367 39.779 36.578 1.00 93.20 O
ANISOU 1214 O CYS A 385 11190 12207 12016 -727 -1547 126 O
ATOM 1215 CB CYS A 385 -2.640 40.441 34.503 1.00 88.78 C
ANISOU 1215 CB CYS A 385 11151 11162 11418 -894 -1470 287 C
ATOM 1216 SG CYS A 385 -2.786 40.640 32.710 1.00 93.21 S
ANISOU 1216 SG CYS A 385 11776 11664 11976 -1279 -1338 407 S
ATOM 1217 N GLY A 386 -2.135 38.542 37.274 1.00 86.75 N
ANISOU 1217 N GLY A 386 10454 11313 11193 -49 -1322 122 N
ATOM 1218 CA GLY A 386 -1.730 38.459 38.669 1.00 87.61 C
ANISOU 1218 CA GLY A 386 10484 11522 11283 233 -1436 26 C
ATOM 1219 C GLY A 386 -0.807 37.300 39.011 1.00 91.83 C
ANISOU 1219 C GLY A 386 10666 12381 11845 362 -1217 5 C
ATOM 1220 O GLY A 386 -0.397 36.516 38.144 1.00 90.55 O
ANISOU 1220 O GLY A 386 10309 12382 11713 226 -975 62 O
ATOM 1221 N THR A 387 -0.467 37.202 40.302 1.00 89.36 N
ANISOU 1221 N THR A 387 10283 12167 11504 653 -1313 -85 N
ATOM 1222 CA THR A 387 0.347 36.121 40.842 1.00 88.98 C
ANISOU 1222 CA THR A 387 9929 12422 11456 863 -1129 -121 C
ATOM 1223 C THR A 387 -0.611 34.980 41.175 1.00 88.87 C
ANISOU 1223 C THR A 387 9916 12397 11452 1274 -887 -71 C
ATOM 1224 O THR A 387 -1.714 35.230 41.686 1.00 88.80 O
ANISOU 1224 O THR A 387 10118 12197 11426 1514 -964 -57 O
ATOM 1225 CB THR A 387 1.215 36.587 42.033 1.00103.04 C
ANISOU 1225 CB THR A 387 11632 14324 13195 969 -1354 -244 C
ATOM 1226 OG1 THR A 387 2.165 35.564 42.355 1.00101.68 O
ANISOU 1226 OG1 THR A 387 11139 14485 13010 1113 -1166 -276 O
ATOM 1227 CG2 THR A 387 0.386 36.993 43.282 1.00103.52 C
ANISOU 1227 CG2 THR A 387 11913 14213 13206 1367 -1545 -306 C
ATOM 1228 N PRO A 388 -0.239 33.725 40.871 1.00 81.57 N
ANISOU 1228 N PRO A 388 8770 11675 10549 1362 -598 -36 N
ATOM 1229 CA PRO A 388 -1.167 32.621 41.132 1.00 77.88 C
ANISOU 1229 CA PRO A 388 8322 11168 10101 1712 -373 26 C
ATOM 1230 C PRO A 388 -1.056 32.001 42.519 1.00 75.88 C
ANISOU 1230 C PRO A 388 7984 11038 9811 2162 -337 -17 C
ATOM 1231 O PRO A 388 -1.617 30.934 42.725 1.00 73.79 O
ANISOU 1231 O PRO A 388 7693 10781 9564 2432 -118 47 O
ATOM 1232 CB PRO A 388 -0.855 31.638 40.007 1.00 79.60 C
ANISOU 1232 CB PRO A 388 8393 11498 10353 1560 -105 83 C
ATOM 1233 CG PRO A 388 0.596 31.893 39.672 1.00 86.48 C
ANISOU 1233 CG PRO A 388 9057 12612 11190 1303 -146 28 C
ATOM 1234 CD PRO A 388 0.996 33.241 40.225 1.00 83.79 C
ANISOU 1234 CD PRO A 388 8787 12225 10825 1147 -464 -43 C
ATOM 1235 N THR A 389 -0.402 32.683 43.482 1.00 71.02 N
ANISOU 1235 N THR A 389 7345 10500 9141 2247 -559 -119 N
ATOM 1236 CA THR A 389 -0.257 32.190 44.862 1.00 70.51 C
ANISOU 1236 CA THR A 389 7206 10562 9022 2698 -548 -170 C
ATOM 1237 C THR A 389 -1.563 31.571 45.379 1.00 71.87 C
ANISOU 1237 C THR A 389 7500 10607 9199 3072 -412 -74 C
ATOM 1238 O THR A 389 -1.558 30.433 45.858 1.00 70.73 O
ANISOU 1238 O THR A 389 7241 10582 9051 3367 -189 -34 O
ATOM 1239 CB THR A 389 0.262 33.282 45.823 1.00 75.14 C
ANISOU 1239 CB THR A 389 7841 11161 9547 2744 -877 -297 C
ATOM 1240 OG1 THR A 389 1.075 34.208 45.111 1.00 77.52 O
ANISOU 1240 OG1 THR A 389 8118 11471 9865 2281 -1056 -348 O
ATOM 1241 CG2 THR A 389 1.056 32.701 46.980 1.00 72.09 C
ANISOU 1241 CG2 THR A 389 7268 11025 9096 3101 -849 -383 C
ATOM 1242 N TYR A 390 -2.689 32.297 45.181 1.00 66.61 N
ANISOU 1242 N TYR A 390 7064 9705 8538 3035 -536 -25 N
ATOM 1243 CA TYR A 390 -4.030 31.895 45.599 1.00 62.99 C
ANISOU 1243 CA TYR A 390 6722 9135 8075 3345 -438 81 C
ATOM 1244 C TYR A 390 -4.897 31.293 44.472 1.00 63.66 C
ANISOU 1244 C TYR A 390 6843 9106 8241 3168 -227 204 C
ATOM 1245 O TYR A 390 -6.036 30.924 44.730 1.00 63.51 O
ANISOU 1245 O TYR A 390 6897 9009 8225 3383 -137 306 O
ATOM 1246 CB TYR A 390 -4.732 33.073 46.279 1.00 62.92 C
ANISOU 1246 CB TYR A 390 6936 8983 7986 3492 -723 49 C
ATOM 1247 CG TYR A 390 -3.863 33.792 47.282 1.00 64.08 C
ANISOU 1247 CG TYR A 390 7079 9211 8056 3617 -979 -93 C
ATOM 1248 CD1 TYR A 390 -3.805 33.376 48.608 1.00 65.91 C
ANISOU 1248 CD1 TYR A 390 7247 9577 8218 4079 -969 -118 C
ATOM 1249 CD2 TYR A 390 -3.100 34.894 46.909 1.00 65.85 C
ANISOU 1249 CD2 TYR A 390 7366 9377 8276 3269 -1237 -201 C
ATOM 1250 CE1 TYR A 390 -2.969 34.004 49.528 1.00 67.56 C
ANISOU 1250 CE1 TYR A 390 7443 9872 8353 4203 -1213 -265 C
ATOM 1251 CE2 TYR A 390 -2.289 35.554 47.827 1.00 68.80 C
ANISOU 1251 CE2 TYR A 390 7735 9821 8587 3361 -1493 -341 C
ATOM 1252 CZ TYR A 390 -2.217 35.099 49.135 1.00 76.65 C
ANISOU 1252 CZ TYR A 390 8656 10958 9510 3836 -1483 -382 C
ATOM 1253 OH TYR A 390 -1.432 35.765 50.046 1.00 79.61 O
ANISOU 1253 OH TYR A 390 9031 11402 9817 3938 -1754 -534 O
ATOM 1254 N LEU A 391 -4.358 31.147 43.259 1.00 58.42 N
ANISOU 1254 N LEU A 391 6113 8450 7633 2794 -146 199 N
ATOM 1255 CA LEU A 391 -5.106 30.618 42.126 1.00 57.71 C
ANISOU 1255 CA LEU A 391 6062 8252 7613 2613 30 294 C
ATOM 1256 C LEU A 391 -5.298 29.082 42.092 1.00 62.34 C
ANISOU 1256 C LEU A 391 6531 8904 8253 2791 333 374 C
ATOM 1257 O LEU A 391 -4.313 28.341 42.057 1.00 62.36 O
ANISOU 1257 O LEU A 391 6373 9067 8253 2810 462 338 O
ATOM 1258 CB LEU A 391 -4.468 31.114 40.831 1.00 58.63 C
ANISOU 1258 CB LEU A 391 6169 8356 7753 2165 -11 260 C
ATOM 1259 CG LEU A 391 -5.308 31.061 39.575 1.00 62.92 C
ANISOU 1259 CG LEU A 391 6815 8745 8345 1930 71 334 C
ATOM 1260 CD1 LEU A 391 -6.648 31.779 39.751 1.00 60.91 C
ANISOU 1260 CD1 LEU A 391 6780 8295 8066 2012 -65 377 C
ATOM 1261 CD2 LEU A 391 -4.542 31.648 38.424 1.00 69.30 C
ANISOU 1261 CD2 LEU A 391 7605 9570 9154 1515 15 302 C
ATOM 1262 N ALA A 392 -6.592 28.624 42.055 1.00 57.40 N
ANISOU 1262 N ALA A 392 5992 8151 7666 2909 438 487 N
ATOM 1263 CA ALA A 392 -7.044 27.225 42.002 1.00 54.31 C
ANISOU 1263 CA ALA A 392 5540 7758 7337 3052 701 586 C
ATOM 1264 C ALA A 392 -6.438 26.551 40.801 1.00 57.40 C
ANISOU 1264 C ALA A 392 5861 8169 7778 2794 849 565 C
ATOM 1265 O ALA A 392 -6.268 27.226 39.775 1.00 56.64 O
ANISOU 1265 O ALA A 392 5804 8029 7687 2471 763 523 O
ATOM 1266 CB ALA A 392 -8.555 27.158 41.925 1.00 53.58 C
ANISOU 1266 CB ALA A 392 5557 7521 7280 3109 733 706 C
ATOM 1267 N PRO A 393 -6.071 25.241 40.923 1.00 53.45 N
ANISOU 1267 N PRO A 393 5269 7740 7300 2948 1064 592 N
ATOM 1268 CA PRO A 393 -5.438 24.543 39.798 1.00 53.94 C
ANISOU 1268 CA PRO A 393 5273 7837 7383 2750 1200 562 C
ATOM 1269 C PRO A 393 -6.290 24.424 38.541 1.00 58.67 C
ANISOU 1269 C PRO A 393 5970 8267 8055 2493 1247 611 C
ATOM 1270 O PRO A 393 -5.767 24.607 37.448 1.00 60.33 O
ANISOU 1270 O PRO A 393 6159 8507 8256 2234 1246 560 O
ATOM 1271 CB PRO A 393 -5.097 23.165 40.375 1.00 55.93 C
ANISOU 1271 CB PRO A 393 5461 8159 7629 3040 1403 592 C
ATOM 1272 CG PRO A 393 -5.325 23.246 41.814 1.00 58.98 C
ANISOU 1272 CG PRO A 393 5843 8583 7985 3372 1368 628 C
ATOM 1273 CD PRO A 393 -6.253 24.331 42.072 1.00 53.82 C
ANISOU 1273 CD PRO A 393 5281 7828 7340 3327 1192 659 C
ATOM 1274 N GLU A 394 -7.588 24.148 38.676 1.00 53.23 N
ANISOU 1274 N GLU A 394 5376 7421 7429 2563 1284 711 N
ATOM 1275 CA GLU A 394 -8.450 24.019 37.495 1.00 52.18 C
ANISOU 1275 CA GLU A 394 5328 7136 7362 2328 1320 749 C
ATOM 1276 C GLU A 394 -8.444 25.254 36.563 1.00 58.08 C
ANISOU 1276 C GLU A 394 6137 7851 8081 2022 1156 691 C
ATOM 1277 O GLU A 394 -8.698 25.118 35.357 1.00 59.54 O
ANISOU 1277 O GLU A 394 6364 7962 8297 1796 1196 685 O
ATOM 1278 CB GLU A 394 -9.874 23.603 37.882 1.00 51.84 C
ANISOU 1278 CB GLU A 394 5351 6963 7385 2449 1372 874 C
ATOM 1279 CG GLU A 394 -10.578 24.617 38.754 1.00 54.00 C
ANISOU 1279 CG GLU A 394 5666 7240 7610 2580 1217 913 C
ATOM 1280 CD GLU A 394 -10.525 24.469 40.260 1.00 53.92 C
ANISOU 1280 CD GLU A 394 5607 7322 7557 2936 1223 961 C
ATOM 1281 OE1 GLU A 394 -9.622 23.797 40.812 1.00 56.38 O
ANISOU 1281 OE1 GLU A 394 5838 7730 7853 3099 1317 934 O
ATOM 1282 OE2 GLU A 394 -11.402 25.086 40.898 1.00 42.55 O
ANISOU 1282 OE2 GLU A 394 4214 5873 6080 3073 1125 1023 O
ATOM 1283 N VAL A 395 -8.139 26.447 37.128 1.00 52.07 N
ANISOU 1283 N VAL A 395 5392 7138 7253 2023 967 647 N
ATOM 1284 CA VAL A 395 -8.082 27.693 36.375 1.00 50.11 C
ANISOU 1284 CA VAL A 395 5229 6844 6968 1745 793 600 C
ATOM 1285 C VAL A 395 -6.848 27.656 35.484 1.00 52.80 C
ANISOU 1285 C VAL A 395 5475 7299 7287 1511 830 535 C
ATOM 1286 O VAL A 395 -6.929 28.002 34.304 1.00 53.32 O
ANISOU 1286 O VAL A 395 5594 7312 7354 1244 815 530 O
ATOM 1287 CB VAL A 395 -8.141 28.923 37.307 1.00 52.98 C
ANISOU 1287 CB VAL A 395 5669 7199 7264 1835 564 572 C
ATOM 1288 CG1 VAL A 395 -7.961 30.219 36.529 1.00 52.77 C
ANISOU 1288 CG1 VAL A 395 5755 7104 7193 1532 374 525 C
ATOM 1289 CG2 VAL A 395 -9.454 28.946 38.079 1.00 51.42 C
ANISOU 1289 CG2 VAL A 395 5560 6916 7062 2087 538 651 C
ATOM 1290 N LEU A 396 -5.743 27.162 36.020 1.00 47.22 N
ANISOU 1290 N LEU A 396 4621 6770 6552 1630 893 492 N
ATOM 1291 CA LEU A 396 -4.494 27.028 35.283 1.00 47.77 C
ANISOU 1291 CA LEU A 396 4561 7011 6578 1452 944 438 C
ATOM 1292 C LEU A 396 -4.598 25.936 34.200 1.00 55.56 C
ANISOU 1292 C LEU A 396 5535 7982 7592 1400 1138 459 C
ATOM 1293 O LEU A 396 -3.973 26.047 33.148 1.00 56.66 O
ANISOU 1293 O LEU A 396 5627 8208 7695 1179 1162 436 O
ATOM 1294 CB LEU A 396 -3.334 26.745 36.262 1.00 48.28 C
ANISOU 1294 CB LEU A 396 4460 7298 6587 1647 959 384 C
ATOM 1295 CG LEU A 396 -2.984 27.878 37.271 1.00 53.02 C
ANISOU 1295 CG LEU A 396 5060 7938 7149 1684 739 338 C
ATOM 1296 CD1 LEU A 396 -2.114 27.369 38.409 1.00 52.61 C
ANISOU 1296 CD1 LEU A 396 4855 8089 7046 1966 775 286 C
ATOM 1297 CD2 LEU A 396 -2.322 29.081 36.586 1.00 56.51 C
ANISOU 1297 CD2 LEU A 396 5502 8411 7558 1323 561 302 C
ATOM 1298 N VAL A 397 -5.429 24.914 34.443 1.00 53.99 N
ANISOU 1298 N VAL A 397 5392 7668 7454 1599 1267 507 N
ATOM 1299 CA VAL A 397 -5.683 23.781 33.544 1.00 53.87 C
ANISOU 1299 CA VAL A 397 5405 7589 7475 1585 1434 523 C
ATOM 1300 C VAL A 397 -6.555 24.203 32.369 1.00 58.66 C
ANISOU 1300 C VAL A 397 6127 8040 8119 1334 1389 541 C
ATOM 1301 O VAL A 397 -6.383 23.671 31.275 1.00 61.96 O
ANISOU 1301 O VAL A 397 6550 8461 8529 1222 1475 519 O
ATOM 1302 CB VAL A 397 -6.251 22.562 34.328 1.00 57.05 C
ANISOU 1302 CB VAL A 397 5838 7902 7936 1871 1568 580 C
ATOM 1303 CG1 VAL A 397 -6.903 21.539 33.413 1.00 56.45 C
ANISOU 1303 CG1 VAL A 397 5850 7674 7924 1820 1691 607 C
ATOM 1304 CG2 VAL A 397 -5.164 21.909 35.170 1.00 57.22 C
ANISOU 1304 CG2 VAL A 397 5746 8103 7894 2124 1653 547 C
ATOM 1305 N SER A 398 -7.458 25.168 32.575 1.00 52.74 N
ANISOU 1305 N SER A 398 5475 7171 7393 1265 1250 574 N
ATOM 1306 CA SER A 398 -8.328 25.687 31.520 1.00 51.65 C
ANISOU 1306 CA SER A 398 5455 6897 7273 1047 1192 588 C
ATOM 1307 C SER A 398 -7.589 26.575 30.513 1.00 58.89 C
ANISOU 1307 C SER A 398 6369 7886 8121 770 1115 545 C
ATOM 1308 O SER A 398 -8.110 26.824 29.426 1.00 60.50 O
ANISOU 1308 O SER A 398 6660 8002 8324 591 1100 548 O
ATOM 1309 CB SER A 398 -9.492 26.452 32.126 1.00 53.28 C
ANISOU 1309 CB SER A 398 5770 6979 7495 1103 1064 636 C
ATOM 1310 OG SER A 398 -9.062 27.510 32.965 1.00 63.30 O
ANISOU 1310 OG SER A 398 7042 8304 8705 1147 908 617 O
ATOM 1311 N VAL A 399 -6.379 27.043 30.864 1.00 56.25 N
ANISOU 1311 N VAL A 399 5927 7722 7725 732 1066 511 N
ATOM 1312 CA VAL A 399 -5.531 27.908 30.034 1.00 56.97 C
ANISOU 1312 CA VAL A 399 5986 7914 7747 454 993 493 C
ATOM 1313 C VAL A 399 -5.206 27.228 28.681 1.00 63.32 C
ANISOU 1313 C VAL A 399 6748 8786 8525 336 1134 486 C
ATOM 1314 O VAL A 399 -5.210 27.900 27.659 1.00 64.35 O
ANISOU 1314 O VAL A 399 6933 8899 8619 98 1087 499 O
ATOM 1315 CB VAL A 399 -4.277 28.420 30.818 1.00 61.59 C
ANISOU 1315 CB VAL A 399 6431 8692 8277 447 913 462 C
ATOM 1316 CG1 VAL A 399 -3.343 29.249 29.941 1.00 63.04 C
ANISOU 1316 CG1 VAL A 399 6556 9004 8394 129 848 466 C
ATOM 1317 CG2 VAL A 399 -4.687 29.230 32.039 1.00 61.00 C
ANISOU 1317 CG2 VAL A 399 6439 8522 8217 557 740 458 C
ATOM 1318 N GLY A 400 -5.020 25.911 28.682 1.00 60.59 N
ANISOU 1318 N GLY A 400 6333 8497 8191 524 1299 467 N
ATOM 1319 CA GLY A 400 -4.703 25.138 27.485 1.00 61.61 C
ANISOU 1319 CA GLY A 400 6437 8692 8279 478 1428 448 C
ATOM 1320 C GLY A 400 -5.775 25.110 26.415 1.00 67.98 C
ANISOU 1320 C GLY A 400 7395 9311 9125 361 1428 456 C
ATOM 1321 O GLY A 400 -5.458 25.149 25.219 1.00 69.25 O
ANISOU 1321 O GLY A 400 7551 9538 9222 216 1461 446 O
ATOM 1322 N THR A 401 -7.057 25.053 26.836 1.00 63.99 N
ANISOU 1322 N THR A 401 7012 8589 8712 432 1389 479 N
ATOM 1323 CA THR A 401 -8.217 25.012 25.928 1.00 62.61 C
ANISOU 1323 CA THR A 401 6973 8239 8578 337 1376 483 C
ATOM 1324 C THR A 401 -8.775 26.404 25.618 1.00 63.73 C
ANISOU 1324 C THR A 401 7217 8304 8693 148 1224 506 C
ATOM 1325 O THR A 401 -9.320 26.596 24.534 1.00 64.70 O
ANISOU 1325 O THR A 401 7429 8355 8799 17 1211 497 O
ATOM 1326 CB THR A 401 -9.305 24.136 26.508 1.00 72.05 C
ANISOU 1326 CB THR A 401 8225 9270 9878 505 1422 505 C
ATOM 1327 OG1 THR A 401 -9.916 24.852 27.580 1.00 78.95 O
ANISOU 1327 OG1 THR A 401 9126 10088 10783 568 1320 554 O
ATOM 1328 CG2 THR A 401 -8.761 22.801 27.028 1.00 73.07 C
ANISOU 1328 CG2 THR A 401 8287 9444 10033 717 1560 494 C
ATOM 1329 N ALA A 402 -8.664 27.362 26.576 1.00 56.13 N
ANISOU 1329 N ALA A 402 6262 7348 7718 153 1099 531 N
ATOM 1330 CA ALA A 402 -9.187 28.735 26.477 1.00 53.59 C
ANISOU 1330 CA ALA A 402 6074 6931 7357 11 929 551 C
ATOM 1331 C ALA A 402 -9.053 29.370 25.099 1.00 58.00 C
ANISOU 1331 C ALA A 402 6702 7488 7847 -237 903 550 C
ATOM 1332 O ALA A 402 -7.979 29.324 24.503 1.00 61.66 O
ANISOU 1332 O ALA A 402 7068 8100 8259 -358 960 547 O
ATOM 1333 CB ALA A 402 -8.552 29.613 27.530 1.00 54.00 C
ANISOU 1333 CB ALA A 402 6104 7035 7378 24 800 557 C
ATOM 1334 N GLY A 403 -10.137 29.924 24.584 1.00 51.33 N
ANISOU 1334 N GLY A 403 6017 6497 6989 -295 824 559 N
ATOM 1335 CA GLY A 403 -10.126 30.563 23.269 1.00 50.94 C
ANISOU 1335 CA GLY A 403 6061 6430 6866 -509 797 563 C
ATOM 1336 C GLY A 403 -10.414 29.675 22.062 1.00 54.24 C
ANISOU 1336 C GLY A 403 6465 6857 7288 -521 924 532 C
ATOM 1337 O GLY A 403 -10.137 30.087 20.935 1.00 56.86 O
ANISOU 1337 O GLY A 403 6838 7223 7544 -683 929 538 O
ATOM 1338 N TYR A 404 -10.962 28.456 22.277 1.00 46.83 N
ANISOU 1338 N TYR A 404 5476 5883 6434 -352 1023 502 N
ATOM 1339 CA TYR A 404 -11.352 27.521 21.229 1.00 44.83 C
ANISOU 1339 CA TYR A 404 5233 5605 6197 -341 1119 457 C
ATOM 1340 C TYR A 404 -12.867 27.300 21.254 1.00 48.72 C
ANISOU 1340 C TYR A 404 5818 5941 6753 -277 1078 447 C
ATOM 1341 O TYR A 404 -13.330 26.270 20.779 1.00 49.89 O
ANISOU 1341 O TYR A 404 5960 6040 6955 -228 1151 407 O
ATOM 1342 CB TYR A 404 -10.578 26.191 21.337 1.00 45.63 C
ANISOU 1342 CB TYR A 404 5208 5798 6332 -218 1263 425 C
ATOM 1343 CG TYR A 404 -9.264 26.249 20.582 1.00 50.26 C
ANISOU 1343 CG TYR A 404 5708 6575 6813 -303 1326 418 C
ATOM 1344 CD1 TYR A 404 -8.155 26.912 21.117 1.00 53.06 C
ANISOU 1344 CD1 TYR A 404 5962 7085 7114 -370 1302 459 C
ATOM 1345 CD2 TYR A 404 -9.163 25.760 19.284 1.00 51.04 C
ANISOU 1345 CD2 TYR A 404 5827 6714 6853 -331 1395 376 C
ATOM 1346 CE1 TYR A 404 -6.967 27.036 20.398 1.00 52.21 C
ANISOU 1346 CE1 TYR A 404 5749 7189 6899 -471 1359 473 C
ATOM 1347 CE2 TYR A 404 -7.988 25.906 18.545 1.00 52.81 C
ANISOU 1347 CE2 TYR A 404 5960 7148 6957 -405 1453 388 C
ATOM 1348 CZ TYR A 404 -6.888 26.529 19.114 1.00 57.64 C
ANISOU 1348 CZ TYR A 404 6447 7933 7518 -480 1442 444 C
ATOM 1349 OH TYR A 404 -5.716 26.623 18.410 1.00 61.49 O
ANISOU 1349 OH TYR A 404 6813 8667 7882 -557 1509 471 O
ATOM 1350 N ASN A 405 -13.644 28.263 21.796 1.00 43.76 N
ANISOU 1350 N ASN A 405 5278 5240 6109 -273 952 482 N
ATOM 1351 CA ASN A 405 -15.104 28.111 21.903 1.00 43.38 C
ANISOU 1351 CA ASN A 405 5290 5089 6103 -199 910 485 C
ATOM 1352 C ASN A 405 -15.754 28.177 20.537 1.00 46.70 C
ANISOU 1352 C ASN A 405 5799 5467 6478 -300 896 437 C
ATOM 1353 O ASN A 405 -16.772 27.519 20.306 1.00 45.36 O
ANISOU 1353 O ASN A 405 5628 5240 6367 -256 911 415 O
ATOM 1354 CB ASN A 405 -15.766 29.133 22.864 1.00 43.90 C
ANISOU 1354 CB ASN A 405 5428 5120 6131 -122 775 534 C
ATOM 1355 CG ASN A 405 -15.101 29.407 24.191 1.00 78.39 C
ANISOU 1355 CG ASN A 405 9742 9533 10510 -21 746 574 C
ATOM 1356 OD1 ASN A 405 -13.895 29.686 24.297 1.00 78.48 O
ANISOU 1356 OD1 ASN A 405 9715 9609 10495 -90 750 568 O
ATOM 1357 ND2 ASN A 405 -15.926 29.532 25.208 1.00 76.11 N
ANISOU 1357 ND2 ASN A 405 9458 9223 10237 144 691 617 N
ATOM 1358 N ARG A 406 -15.135 28.952 19.629 1.00 43.49 N
ANISOU 1358 N ARG A 406 5461 5097 5967 -440 870 425 N
ATOM 1359 CA ARG A 406 -15.556 29.143 18.247 1.00 43.29 C
ANISOU 1359 CA ARG A 406 5528 5051 5869 -531 859 380 C
ATOM 1360 C ARG A 406 -15.581 27.822 17.539 1.00 46.54 C
ANISOU 1360 C ARG A 406 5872 5468 6341 -499 967 315 C
ATOM 1361 O ARG A 406 -16.374 27.676 16.637 1.00 48.64 O
ANISOU 1361 O ARG A 406 6204 5692 6586 -517 947 262 O
ATOM 1362 CB ARG A 406 -14.626 30.135 17.504 1.00 43.74 C
ANISOU 1362 CB ARG A 406 5649 5167 5802 -688 835 406 C
ATOM 1363 CG ARG A 406 -13.222 29.589 17.167 1.00 46.30 C
ANISOU 1363 CG ARG A 406 5846 5629 6118 -739 953 410 C
ATOM 1364 CD ARG A 406 -12.341 30.636 16.580 1.00 41.40 C
ANISOU 1364 CD ARG A 406 5266 5085 5379 -914 926 467 C
ATOM 1365 NE ARG A 406 -12.128 31.698 17.553 1.00 49.92 N
ANISOU 1365 NE ARG A 406 6394 6124 6449 -973 810 528 N
ATOM 1366 CZ ARG A 406 -11.358 32.754 17.346 1.00 62.56 C
ANISOU 1366 CZ ARG A 406 8044 7761 7965 -1153 752 595 C
ATOM 1367 NH1 ARG A 406 -10.712 32.898 16.197 1.00 53.51 N
ANISOU 1367 NH1 ARG A 406 6883 6717 6731 -1291 817 626 N
ATOM 1368 NH2 ARG A 406 -11.230 33.678 18.281 1.00 53.40 N
ANISOU 1368 NH2 ARG A 406 6951 6535 6803 -1197 622 635 N
ATOM 1369 N ALA A 407 -14.703 26.865 17.929 1.00 41.87 N
ANISOU 1369 N ALA A 407 5165 4931 5813 -438 1073 310 N
ATOM 1370 CA ALA A 407 -14.654 25.518 17.357 1.00 41.32 C
ANISOU 1370 CA ALA A 407 5058 4846 5795 -378 1166 242 C
ATOM 1371 C ALA A 407 -16.007 24.791 17.446 1.00 46.13 C
ANISOU 1371 C ALA A 407 5693 5321 6511 -327 1139 211 C
ATOM 1372 O ALA A 407 -16.229 23.900 16.644 1.00 47.62 O
ANISOU 1372 O ALA A 407 5905 5462 6726 -317 1170 137 O
ATOM 1373 CB ALA A 407 -13.551 24.696 18.000 1.00 41.39 C
ANISOU 1373 CB ALA A 407 4957 4930 5839 -286 1268 251 C
ATOM 1374 N VAL A 408 -16.933 25.202 18.357 1.00 42.14 N
ANISOU 1374 N VAL A 408 5187 4767 6057 -298 1072 269 N
ATOM 1375 CA VAL A 408 -18.280 24.603 18.446 1.00 42.22 C
ANISOU 1375 CA VAL A 408 5194 4687 6159 -273 1042 262 C
ATOM 1376 C VAL A 408 -19.076 24.832 17.166 1.00 46.92 C
ANISOU 1376 C VAL A 408 5871 5259 6695 -352 978 184 C
ATOM 1377 O VAL A 408 -19.866 23.977 16.789 1.00 49.33 O
ANISOU 1377 O VAL A 408 6168 5495 7078 -362 975 135 O
ATOM 1378 CB VAL A 408 -19.107 24.955 19.724 1.00 45.74 C
ANISOU 1378 CB VAL A 408 5596 5132 6650 -198 992 355 C
ATOM 1379 CG1 VAL A 408 -18.324 24.646 20.992 1.00 46.01 C
ANISOU 1379 CG1 VAL A 408 5550 5191 6742 -94 1059 424 C
ATOM 1380 CG2 VAL A 408 -19.627 26.396 19.730 1.00 44.36 C
ANISOU 1380 CG2 VAL A 408 5502 5001 6353 -209 873 378 C
ATOM 1381 N ASP A 409 -18.855 25.982 16.505 1.00 41.96 N
ANISOU 1381 N ASP A 409 5329 4685 5929 -411 922 174 N
ATOM 1382 CA ASP A 409 -19.468 26.369 15.241 1.00 41.94 C
ANISOU 1382 CA ASP A 409 5421 4680 5834 -467 863 102 C
ATOM 1383 C ASP A 409 -18.975 25.498 14.083 1.00 48.57 C
ANISOU 1383 C ASP A 409 6271 5515 6667 -486 925 8 C
ATOM 1384 O ASP A 409 -19.713 25.281 13.125 1.00 48.06 O
ANISOU 1384 O ASP A 409 6258 5422 6581 -501 881 -76 O
ATOM 1385 CB ASP A 409 -19.196 27.847 14.934 1.00 42.58 C
ANISOU 1385 CB ASP A 409 5610 4809 5759 -518 798 137 C
ATOM 1386 CG ASP A 409 -20.090 28.844 15.625 1.00 45.18 C
ANISOU 1386 CG ASP A 409 6000 5127 6040 -477 687 190 C
ATOM 1387 OD1 ASP A 409 -21.173 28.422 16.157 1.00 42.40 O
ANISOU 1387 OD1 ASP A 409 5591 4762 5759 -407 656 194 O
ATOM 1388 OD2 ASP A 409 -19.770 30.067 15.563 1.00 47.23 O
ANISOU 1388 OD2 ASP A 409 6375 5395 6175 -514 623 228 O
ATOM 1389 N CYS A 410 -17.735 25.003 14.169 1.00 48.30 N
ANISOU 1389 N CYS A 410 6190 5525 6637 -466 1019 15 N
ATOM 1390 CA CYS A 410 -17.185 24.124 13.142 1.00 50.20 C
ANISOU 1390 CA CYS A 410 6446 5780 6849 -439 1078 -74 C
ATOM 1391 C CYS A 410 -17.667 22.704 13.288 1.00 53.07 C
ANISOU 1391 C CYS A 410 6792 6024 7347 -379 1092 -137 C
ATOM 1392 O CYS A 410 -17.830 22.022 12.288 1.00 54.87 O
ANISOU 1392 O CYS A 410 7079 6210 7559 -361 1077 -241 O
ATOM 1393 CB CYS A 410 -15.675 24.214 13.112 1.00 52.23 C
ANISOU 1393 CB CYS A 410 6652 6167 7026 -423 1169 -39 C
ATOM 1394 SG CYS A 410 -15.093 25.864 12.725 1.00 57.13 S
ANISOU 1394 SG CYS A 410 7308 6913 7487 -543 1143 43 S
ATOM 1395 N TRP A 411 -17.959 22.277 14.512 1.00 47.67 N
ANISOU 1395 N TRP A 411 6044 5277 6793 -350 1108 -72 N
ATOM 1396 CA TRP A 411 -18.544 20.980 14.744 1.00 47.78 C
ANISOU 1396 CA TRP A 411 6054 5152 6948 -322 1112 -106 C
ATOM 1397 C TRP A 411 -19.911 20.985 14.028 1.00 55.44 C
ANISOU 1397 C TRP A 411 7066 6057 7944 -400 1008 -170 C
ATOM 1398 O TRP A 411 -20.104 20.193 13.106 1.00 57.31 O
ANISOU 1398 O TRP A 411 7366 6216 8193 -404 980 -280 O
ATOM 1399 CB TRP A 411 -18.699 20.713 16.252 1.00 45.02 C
ANISOU 1399 CB TRP A 411 5621 4765 6720 -282 1148 6 C
ATOM 1400 CG TRP A 411 -19.374 19.403 16.545 1.00 46.66 C
ANISOU 1400 CG TRP A 411 5831 4815 7081 -281 1151 -2 C
ATOM 1401 CD1 TRP A 411 -20.716 19.190 16.692 1.00 49.63 C
ANISOU 1401 CD1 TRP A 411 6182 5119 7557 -359 1083 22 C
ATOM 1402 CD2 TRP A 411 -18.756 18.105 16.578 1.00 47.38 C
ANISOU 1402 CD2 TRP A 411 5970 4802 7232 -208 1215 -41 C
ATOM 1403 NE1 TRP A 411 -20.966 17.850 16.868 1.00 50.14 N
ANISOU 1403 NE1 TRP A 411 6270 5025 7757 -369 1101 13 N
ATOM 1404 CE2 TRP A 411 -19.781 17.159 16.801 1.00 51.74 C
ANISOU 1404 CE2 TRP A 411 6537 5188 7935 -267 1177 -30 C
ATOM 1405 CE3 TRP A 411 -17.430 17.652 16.463 1.00 49.51 C
ANISOU 1405 CE3 TRP A 411 6271 5110 7430 -91 1297 -79 C
ATOM 1406 CZ2 TRP A 411 -19.519 15.791 16.963 1.00 52.38 C
ANISOU 1406 CZ2 TRP A 411 6693 5104 8106 -218 1214 -52 C
ATOM 1407 CZ3 TRP A 411 -17.169 16.289 16.614 1.00 52.31 C
ANISOU 1407 CZ3 TRP A 411 6698 5323 7856 -7 1337 -111 C
ATOM 1408 CH2 TRP A 411 -18.206 15.376 16.860 1.00 53.66 C
ANISOU 1408 CH2 TRP A 411 6913 5291 8184 -74 1292 -99 C
ATOM 1409 N SER A 412 -20.811 21.938 14.399 1.00 51.35 N
ANISOU 1409 N SER A 412 6517 5585 7408 -444 940 -110 N
ATOM 1410 CA SER A 412 -22.173 22.135 13.864 1.00 50.64 C
ANISOU 1410 CA SER A 412 6439 5483 7318 -504 837 -157 C
ATOM 1411 C SER A 412 -22.220 22.135 12.334 1.00 54.41 C
ANISOU 1411 C SER A 412 7012 5965 7696 -524 790 -294 C
ATOM 1412 O SER A 412 -23.051 21.446 11.743 1.00 55.11 O
ANISOU 1412 O SER A 412 7114 5986 7841 -564 723 -383 O
ATOM 1413 CB SER A 412 -22.773 23.417 14.421 1.00 53.00 C
ANISOU 1413 CB SER A 412 6716 5879 7543 -497 781 -73 C
ATOM 1414 OG SER A 412 -22.815 23.403 15.842 1.00 62.45 O
ANISOU 1414 OG SER A 412 7823 7083 8823 -452 814 50 O
ATOM 1415 N LEU A 413 -21.292 22.860 11.698 1.00 50.05 N
ANISOU 1415 N LEU A 413 6524 5497 6998 -498 824 -308 N
ATOM 1416 CA LEU A 413 -21.141 22.920 10.239 1.00 50.18 C
ANISOU 1416 CA LEU A 413 6632 5542 6891 -487 800 -422 C
ATOM 1417 C LEU A 413 -20.838 21.528 9.658 1.00 55.74 C
ANISOU 1417 C LEU A 413 7366 6156 7657 -443 816 -533 C
ATOM 1418 O LEU A 413 -21.322 21.184 8.572 1.00 56.99 O
ANISOU 1418 O LEU A 413 7592 6283 7778 -433 748 -659 O
ATOM 1419 CB LEU A 413 -20.009 23.908 9.835 1.00 49.03 C
ANISOU 1419 CB LEU A 413 6527 5519 6581 -476 858 -374 C
ATOM 1420 CG LEU A 413 -20.294 25.408 9.909 1.00 50.74 C
ANISOU 1420 CG LEU A 413 6792 5803 6684 -520 808 -301 C
ATOM 1421 CD1 LEU A 413 -19.110 26.192 9.418 1.00 50.35 C
ANISOU 1421 CD1 LEU A 413 6786 5855 6490 -542 867 -248 C
ATOM 1422 CD2 LEU A 413 -21.533 25.804 9.105 1.00 52.30 C
ANISOU 1422 CD2 LEU A 413 7062 5997 6815 -519 705 -381 C
ATOM 1423 N GLY A 414 -20.046 20.752 10.398 1.00 51.29 N
ANISOU 1423 N GLY A 414 6765 5545 7177 -399 897 -492 N
ATOM 1424 CA GLY A 414 -19.667 19.396 10.026 1.00 52.15 C
ANISOU 1424 CA GLY A 414 6929 5547 7337 -331 910 -588 C
ATOM 1425 C GLY A 414 -20.846 18.453 10.092 1.00 56.82 C
ANISOU 1425 C GLY A 414 7539 5963 8085 -396 817 -648 C
ATOM 1426 O GLY A 414 -20.959 17.562 9.253 1.00 60.24 O
ANISOU 1426 O GLY A 414 8068 6294 8527 -366 760 -780 O
ATOM 1427 N VAL A 415 -21.726 18.637 11.095 1.00 50.63 N
ANISOU 1427 N VAL A 415 6664 5150 7423 -486 796 -549 N
ATOM 1428 CA VAL A 415 -22.962 17.861 11.280 1.00 49.80 C
ANISOU 1428 CA VAL A 415 6536 4912 7475 -588 708 -568 C
ATOM 1429 C VAL A 415 -23.928 18.300 10.155 1.00 55.26 C
ANISOU 1429 C VAL A 415 7253 5649 8096 -644 586 -681 C
ATOM 1430 O VAL A 415 -24.620 17.447 9.598 1.00 57.84 O
ANISOU 1430 O VAL A 415 7619 5857 8502 -706 491 -786 O
ATOM 1431 CB VAL A 415 -23.580 18.015 12.707 1.00 50.85 C
ANISOU 1431 CB VAL A 415 6536 5055 7728 -647 736 -403 C
ATOM 1432 CG1 VAL A 415 -24.873 17.228 12.851 1.00 51.36 C
ANISOU 1432 CG1 VAL A 415 6553 5013 7951 -777 650 -402 C
ATOM 1433 CG2 VAL A 415 -22.601 17.580 13.781 1.00 49.98 C
ANISOU 1433 CG2 VAL A 415 6409 4907 7673 -567 855 -302 C
ATOM 1434 N ILE A 416 -23.939 19.611 9.793 1.00 49.85 N
ANISOU 1434 N ILE A 416 6561 5128 7254 -618 582 -666 N
ATOM 1435 CA ILE A 416 -24.774 20.137 8.711 1.00 49.95 C
ANISOU 1435 CA ILE A 416 6608 5205 7165 -636 477 -772 C
ATOM 1436 C ILE A 416 -24.344 19.528 7.366 1.00 57.14 C
ANISOU 1436 C ILE A 416 7643 6064 8004 -572 441 -940 C
ATOM 1437 O ILE A 416 -25.191 18.992 6.646 1.00 59.39 O
ANISOU 1437 O ILE A 416 7956 6286 8322 -612 325 -1068 O
ATOM 1438 CB ILE A 416 -24.817 21.687 8.678 1.00 51.08 C
ANISOU 1438 CB ILE A 416 6752 5514 7144 -603 484 -706 C
ATOM 1439 CG1 ILE A 416 -25.566 22.233 9.893 1.00 50.13 C
ANISOU 1439 CG1 ILE A 416 6521 5447 7080 -641 475 -570 C
ATOM 1440 CG2 ILE A 416 -25.466 22.208 7.363 1.00 51.74 C
ANISOU 1440 CG2 ILE A 416 6906 5668 7083 -581 387 -832 C
ATOM 1441 CD1 ILE A 416 -25.337 23.769 10.127 1.00 55.32 C
ANISOU 1441 CD1 ILE A 416 7215 6231 7573 -586 489 -482 C
ATOM 1442 N LEU A 417 -23.032 19.582 7.048 1.00 52.90 N
ANISOU 1442 N LEU A 417 7172 5568 7361 -467 535 -941 N
ATOM 1443 CA LEU A 417 -22.466 19.045 5.804 1.00 53.65 C
ANISOU 1443 CA LEU A 417 7383 5650 7351 -359 517 -1086 C
ATOM 1444 C LEU A 417 -22.772 17.549 5.619 1.00 59.41 C
ANISOU 1444 C LEU A 417 8180 6180 8213 -360 437 -1207 C
ATOM 1445 O LEU A 417 -23.107 17.119 4.511 1.00 63.53 O
ANISOU 1445 O LEU A 417 8798 6658 8684 -314 335 -1369 O
ATOM 1446 CB LEU A 417 -20.946 19.349 5.715 1.00 53.09 C
ANISOU 1446 CB LEU A 417 7330 5698 7144 -247 650 -1026 C
ATOM 1447 CG LEU A 417 -20.202 18.929 4.434 1.00 58.39 C
ANISOU 1447 CG LEU A 417 8107 6417 7660 -94 654 -1151 C
ATOM 1448 CD1 LEU A 417 -20.824 19.572 3.183 1.00 59.19 C
ANISOU 1448 CD1 LEU A 417 8270 6597 7621 -70 573 -1247 C
ATOM 1449 CD2 LEU A 417 -18.738 19.257 4.521 1.00 57.09 C
ANISOU 1449 CD2 LEU A 417 7912 6411 7369 -2 796 -1058 C
ATOM 1450 N PHE A 418 -22.687 16.777 6.697 1.00 53.17 N
ANISOU 1450 N PHE A 418 7354 5260 7587 -409 473 -1131 N
ATOM 1451 CA PHE A 418 -22.989 15.352 6.732 1.00 54.35 C
ANISOU 1451 CA PHE A 418 7585 5182 7883 -436 396 -1215 C
ATOM 1452 C PHE A 418 -24.463 15.119 6.333 1.00 58.29 C
ANISOU 1452 C PHE A 418 8067 5599 8482 -587 234 -1301 C
ATOM 1453 O PHE A 418 -24.737 14.346 5.425 1.00 58.57 O
ANISOU 1453 O PHE A 418 8220 5512 8522 -572 112 -1467 O
ATOM 1454 CB PHE A 418 -22.711 14.814 8.153 1.00 55.60 C
ANISOU 1454 CB PHE A 418 7688 5242 8195 -475 485 -1069 C
ATOM 1455 CG PHE A 418 -22.734 13.310 8.301 1.00 58.59 C
ANISOU 1455 CG PHE A 418 8189 5363 8711 -483 430 -1130 C
ATOM 1456 CD1 PHE A 418 -23.936 12.607 8.256 1.00 62.77 C
ANISOU 1456 CD1 PHE A 418 8731 5717 9403 -653 293 -1176 C
ATOM 1457 CD2 PHE A 418 -21.562 12.601 8.528 1.00 60.20 C
ANISOU 1457 CD2 PHE A 418 8494 5501 8878 -325 512 -1132 C
ATOM 1458 CE1 PHE A 418 -23.964 11.223 8.417 1.00 64.73 C
ANISOU 1458 CE1 PHE A 418 9116 5693 9784 -682 230 -1222 C
ATOM 1459 CE2 PHE A 418 -21.593 11.218 8.699 1.00 65.23 C
ANISOU 1459 CE2 PHE A 418 9278 5874 9633 -320 454 -1185 C
ATOM 1460 CZ PHE A 418 -22.799 10.541 8.656 1.00 64.55 C
ANISOU 1460 CZ PHE A 418 9226 5582 9719 -510 311 -1225 C
ATOM 1461 N ILE A 419 -25.395 15.817 6.994 1.00 55.38 N
ANISOU 1461 N ILE A 419 7548 5318 8177 -718 226 -1191 N
ATOM 1462 CA ILE A 419 -26.839 15.734 6.727 1.00 56.84 C
ANISOU 1462 CA ILE A 419 7665 5491 8442 -867 82 -1246 C
ATOM 1463 C ILE A 419 -27.158 16.098 5.262 1.00 63.62 C
ANISOU 1463 C ILE A 419 8600 6424 9147 -803 -28 -1431 C
ATOM 1464 O ILE A 419 -27.948 15.411 4.619 1.00 65.25 O
ANISOU 1464 O ILE A 419 8844 6530 9419 -878 -178 -1571 O
ATOM 1465 CB ILE A 419 -27.636 16.578 7.768 1.00 57.91 C
ANISOU 1465 CB ILE A 419 7613 5769 8621 -964 117 -1074 C
ATOM 1466 CG1 ILE A 419 -27.624 15.883 9.134 1.00 57.76 C
ANISOU 1466 CG1 ILE A 419 7517 5640 8790 -1049 186 -915 C
ATOM 1467 CG2 ILE A 419 -29.080 16.862 7.310 1.00 59.22 C
ANISOU 1467 CG2 ILE A 419 7685 6029 8787 -1071 -23 -1135 C
ATOM 1468 CD1 ILE A 419 -27.710 16.809 10.325 1.00 63.16 C
ANISOU 1468 CD1 ILE A 419 8057 6482 9461 -1037 284 -721 C
ATOM 1469 N CYS A 420 -26.539 17.167 4.746 1.00 59.67 N
ANISOU 1469 N CYS A 420 8129 6099 8445 -668 41 -1428 N
ATOM 1470 CA CYS A 420 -26.736 17.603 3.373 1.00 60.35 C
ANISOU 1470 CA CYS A 420 8297 6275 8360 -576 -40 -1584 C
ATOM 1471 C CYS A 420 -26.297 16.565 2.352 1.00 66.05 C
ANISOU 1471 C CYS A 420 9178 6865 9054 -474 -115 -1770 C
ATOM 1472 O CYS A 420 -27.052 16.273 1.424 1.00 67.33 O
ANISOU 1472 O CYS A 420 9388 6997 9197 -478 -266 -1937 O
ATOM 1473 CB CYS A 420 -26.033 18.928 3.140 1.00 59.39 C
ANISOU 1473 CB CYS A 420 8186 6347 8032 -462 69 -1508 C
ATOM 1474 SG CYS A 420 -26.791 20.302 4.004 1.00 62.08 S
ANISOU 1474 SG CYS A 420 8394 6841 8353 -543 98 -1341 S
ATOM 1475 N LEU A 421 -25.065 16.031 2.521 1.00 62.23 N
ANISOU 1475 N LEU A 421 8777 6317 8549 -361 -17 -1745 N
ATOM 1476 CA LEU A 421 -24.439 15.060 1.624 1.00 63.25 C
ANISOU 1476 CA LEU A 421 9078 6338 8615 -207 -72 -1909 C
ATOM 1477 C LEU A 421 -25.106 13.703 1.635 1.00 70.66 C
ANISOU 1477 C LEU A 421 10101 7011 9735 -301 -230 -2029 C
ATOM 1478 O LEU A 421 -25.266 13.116 0.571 1.00 74.37 O
ANISOU 1478 O LEU A 421 10712 7399 10147 -212 -369 -2225 O
ATOM 1479 CB LEU A 421 -22.938 14.892 1.947 1.00 61.94 C
ANISOU 1479 CB LEU A 421 8956 6212 8366 -50 86 -1829 C
ATOM 1480 CG LEU A 421 -22.010 16.092 1.730 1.00 63.28 C
ANISOU 1480 CG LEU A 421 9071 6641 8332 58 237 -1724 C
ATOM 1481 CD1 LEU A 421 -20.670 15.810 2.315 1.00 63.16 C
ANISOU 1481 CD1 LEU A 421 9050 6662 8284 161 383 -1626 C
ATOM 1482 CD2 LEU A 421 -21.829 16.431 0.241 1.00 62.73 C
ANISOU 1482 CD2 LEU A 421 9094 6702 8039 226 196 -1856 C
ATOM 1483 N SER A 422 -25.473 13.198 2.825 1.00 66.38 N
ANISOU 1483 N SER A 422 9486 6330 9407 -477 -216 -1910 N
ATOM 1484 CA SER A 422 -26.033 11.860 3.036 1.00 68.16 C
ANISOU 1484 CA SER A 422 9797 6271 9829 -604 -352 -1980 C
ATOM 1485 C SER A 422 -27.573 11.704 3.149 1.00 73.57 C
ANISOU 1485 C SER A 422 10373 6898 10684 -863 -505 -1998 C
ATOM 1486 O SER A 422 -28.098 10.629 2.866 1.00 75.81 O
ANISOU 1486 O SER A 422 10761 6953 11092 -966 -670 -2118 O
ATOM 1487 CB SER A 422 -25.345 11.208 4.230 1.00 70.74 C
ANISOU 1487 CB SER A 422 10143 6459 10275 -614 -236 -1836 C
ATOM 1488 OG SER A 422 -25.718 11.810 5.459 1.00 78.60 O
ANISOU 1488 OG SER A 422 10941 7541 11384 -764 -131 -1624 O
ATOM 1489 N GLY A 423 -28.262 12.746 3.599 1.00 69.17 N
ANISOU 1489 N GLY A 423 9610 6548 10124 -965 -455 -1876 N
ATOM 1490 CA GLY A 423 -29.704 12.730 3.825 1.00 69.83 C
ANISOU 1490 CA GLY A 423 9540 6650 10344 -1197 -575 -1859 C
ATOM 1491 C GLY A 423 -30.041 12.278 5.234 1.00 74.21 C
ANISOU 1491 C GLY A 423 9971 7115 11111 -1386 -514 -1656 C
ATOM 1492 O GLY A 423 -31.192 12.379 5.654 1.00 74.49 O
ANISOU 1492 O GLY A 423 9829 7222 11252 -1581 -574 -1583 O
ATOM 1493 N TYR A 424 -29.035 11.783 5.980 1.00 70.66 N
ANISOU 1493 N TYR A 424 9606 6533 10710 -1316 -388 -1557 N
ATOM 1494 CA TYR A 424 -29.211 11.289 7.346 1.00 70.51 C
ANISOU 1494 CA TYR A 424 9496 6415 10881 -1461 -312 -1356 C
ATOM 1495 C TYR A 424 -28.261 11.953 8.368 1.00 72.12 C
ANISOU 1495 C TYR A 424 9638 6740 11023 -1324 -99 -1174 C
ATOM 1496 O TYR A 424 -27.145 12.335 7.998 1.00 69.21 O
ANISOU 1496 O TYR A 424 9367 6434 10497 -1119 -15 -1222 O
ATOM 1497 CB TYR A 424 -29.138 9.729 7.397 1.00 73.43 C
ANISOU 1497 CB TYR A 424 10045 6434 11419 -1555 -406 -1411 C
ATOM 1498 CG TYR A 424 -27.745 9.132 7.326 1.00 73.50 C
ANISOU 1498 CG TYR A 424 10283 6287 11356 -1334 -331 -1464 C
ATOM 1499 CD1 TYR A 424 -27.017 8.869 8.483 1.00 73.41 C
ANISOU 1499 CD1 TYR A 424 10276 6216 11401 -1281 -174 -1292 C
ATOM 1500 CD2 TYR A 424 -27.194 8.739 6.108 1.00 75.65 C
ANISOU 1500 CD2 TYR A 424 10773 6474 11498 -1165 -429 -1688 C
ATOM 1501 CE1 TYR A 424 -25.748 8.293 8.427 1.00 73.04 C
ANISOU 1501 CE1 TYR A 424 10431 6050 11271 -1061 -108 -1344 C
ATOM 1502 CE2 TYR A 424 -25.929 8.151 6.040 1.00 76.88 C
ANISOU 1502 CE2 TYR A 424 11133 6513 11565 -937 -366 -1735 C
ATOM 1503 CZ TYR A 424 -25.195 7.959 7.200 1.00 82.94 C
ANISOU 1503 CZ TYR A 424 11888 7247 12379 -884 -201 -1563 C
ATOM 1504 OH TYR A 424 -23.929 7.416 7.126 1.00 83.65 O
ANISOU 1504 OH TYR A 424 12166 7261 12355 -634 -136 -1613 O
ATOM 1505 N PRO A 425 -28.668 12.044 9.664 1.00 69.26 N
ANISOU 1505 N PRO A 425 9115 6417 10786 -1434 -15 -962 N
ATOM 1506 CA PRO A 425 -27.766 12.631 10.683 1.00 67.17 C
ANISOU 1506 CA PRO A 425 8797 6258 10468 -1297 171 -798 C
ATOM 1507 C PRO A 425 -26.613 11.707 11.112 1.00 72.17 C
ANISOU 1507 C PRO A 425 9588 6696 11140 -1187 258 -781 C
ATOM 1508 O PRO A 425 -26.784 10.477 11.167 1.00 74.08 O
ANISOU 1508 O PRO A 425 9944 6682 11521 -1274 192 -808 O
ATOM 1509 CB PRO A 425 -28.704 12.921 11.860 1.00 68.50 C
ANISOU 1509 CB PRO A 425 8747 6529 10749 -1435 207 -592 C
ATOM 1510 CG PRO A 425 -29.766 11.874 11.747 1.00 75.20 C
ANISOU 1510 CG PRO A 425 9580 7210 11781 -1668 75 -609 C
ATOM 1511 CD PRO A 425 -29.959 11.631 10.262 1.00 71.74 C
ANISOU 1511 CD PRO A 425 9273 6702 11282 -1680 -87 -855 C
ATOM 1512 N PRO A 426 -25.437 12.273 11.462 1.00 67.10 N
ANISOU 1512 N PRO A 426 8953 6167 10372 -998 401 -729 N
ATOM 1513 CA PRO A 426 -24.314 11.405 11.876 1.00 67.61 C
ANISOU 1513 CA PRO A 426 9158 6082 10450 -863 488 -717 C
ATOM 1514 C PRO A 426 -24.489 10.746 13.242 1.00 71.74 C
ANISOU 1514 C PRO A 426 9634 6482 11141 -931 561 -536 C
ATOM 1515 O PRO A 426 -23.962 9.658 13.457 1.00 73.05 O
ANISOU 1515 O PRO A 426 9956 6436 11362 -872 577 -549 O
ATOM 1516 CB PRO A 426 -23.095 12.349 11.849 1.00 67.29 C
ANISOU 1516 CB PRO A 426 9094 6257 10218 -665 613 -706 C
ATOM 1517 CG PRO A 426 -23.638 13.723 11.911 1.00 69.00 C
ANISOU 1517 CG PRO A 426 9146 6703 10369 -721 618 -643 C
ATOM 1518 CD PRO A 426 -25.066 13.708 11.466 1.00 65.59 C
ANISOU 1518 CD PRO A 426 8659 6245 10018 -900 480 -685 C
ATOM 1519 N PHE A 427 -25.188 11.429 14.170 1.00 66.85 N
ANISOU 1519 N PHE A 427 8811 6006 10583 -1024 609 -365 N
ATOM 1520 CA PHE A 427 -25.418 10.979 15.543 1.00 67.20 C
ANISOU 1520 CA PHE A 427 8777 5986 10770 -1073 693 -165 C
ATOM 1521 C PHE A 427 -26.933 10.943 15.790 1.00 75.84 C
ANISOU 1521 C PHE A 427 9714 7101 12001 -1309 611 -70 C
ATOM 1522 O PHE A 427 -27.603 11.964 15.676 1.00 75.09 O
ANISOU 1522 O PHE A 427 9461 7229 11839 -1345 581 -53 O
ATOM 1523 CB PHE A 427 -24.670 11.882 16.548 1.00 65.91 C
ANISOU 1523 CB PHE A 427 8503 6021 10518 -908 846 -32 C
ATOM 1524 CG PHE A 427 -23.225 12.151 16.179 1.00 65.54 C
ANISOU 1524 CG PHE A 427 8561 6032 10310 -698 916 -129 C
ATOM 1525 CD1 PHE A 427 -22.227 11.240 16.498 1.00 68.44 C
ANISOU 1525 CD1 PHE A 427 9065 6259 10680 -561 988 -138 C
ATOM 1526 CD2 PHE A 427 -22.870 13.300 15.477 1.00 64.24 C
ANISOU 1526 CD2 PHE A 427 8359 6070 9979 -636 908 -207 C
ATOM 1527 CE1 PHE A 427 -20.897 11.481 16.127 1.00 67.71 C
ANISOU 1527 CE1 PHE A 427 9040 6264 10422 -364 1053 -223 C
ATOM 1528 CE2 PHE A 427 -21.547 13.526 15.095 1.00 65.30 C
ANISOU 1528 CE2 PHE A 427 8567 6282 9963 -466 974 -279 C
ATOM 1529 CZ PHE A 427 -20.571 12.617 15.422 1.00 64.05 C
ANISOU 1529 CZ PHE A 427 8514 6016 9805 -330 1047 -288 C
ATOM 1530 N SER A 428 -27.479 9.748 16.051 1.00 77.04 N
ANISOU 1530 N SER A 428 9918 7020 12333 -1473 563 -16 N
ATOM 1531 CA SER A 428 -28.915 9.535 16.216 1.00 79.45 C
ANISOU 1531 CA SER A 428 10068 7340 12781 -1732 474 76 C
ATOM 1532 C SER A 428 -29.218 8.357 17.129 1.00 88.24 C
ANISOU 1532 C SER A 428 11205 8231 14092 -1875 504 246 C
ATOM 1533 O SER A 428 -28.421 7.421 17.245 1.00 89.54 O
ANISOU 1533 O SER A 428 11587 8138 14298 -1804 534 221 O
ATOM 1534 CB SER A 428 -29.554 9.284 14.849 1.00 85.46 C
ANISOU 1534 CB SER A 428 10899 8026 13547 -1874 283 -131 C
ATOM 1535 OG SER A 428 -30.958 9.089 14.915 1.00 99.10 O
ANISOU 1535 OG SER A 428 12454 9796 15402 -2139 181 -58 O
ATOM 1536 N GLU A 429 -30.406 8.371 17.727 1.00 87.49 N
ANISOU 1536 N GLU A 429 10893 8238 14111 -2079 488 420 N
ATOM 1537 CA GLU A 429 -30.833 7.260 18.564 1.00 90.33 C
ANISOU 1537 CA GLU A 429 11258 8396 14668 -2258 513 609 C
ATOM 1538 C GLU A 429 -31.520 6.168 17.727 1.00 99.89 C
ANISOU 1538 C GLU A 429 12595 9326 16033 -2542 324 504 C
ATOM 1539 O GLU A 429 -31.707 5.061 18.236 1.00102.49 O
ANISOU 1539 O GLU A 429 13014 9395 16531 -2702 321 627 O
ATOM 1540 CB GLU A 429 -31.653 7.741 19.771 1.00 91.28 C
ANISOU 1540 CB GLU A 429 11079 8774 14829 -2314 614 887 C
ATOM 1541 CG GLU A 429 -30.792 8.509 20.769 1.00 99.38 C
ANISOU 1541 CG GLU A 429 12055 9976 15730 -2017 796 996 C
ATOM 1542 CD GLU A 429 -31.471 9.201 21.938 1.00115.34 C
ANISOU 1542 CD GLU A 429 13792 12297 17734 -1986 896 1247 C
ATOM 1543 OE1 GLU A 429 -32.715 9.357 21.912 1.00107.82 O
ANISOU 1543 OE1 GLU A 429 12625 11514 16827 -2175 828 1335 O
ATOM 1544 OE2 GLU A 429 -30.749 9.595 22.885 1.00 97.33 O
ANISOU 1544 OE2 GLU A 429 11500 10100 15382 -1753 1039 1353 O
ATOM 1545 N HIS A 430 -31.812 6.453 16.418 1.00 98.22 N
ANISOU 1545 N HIS A 430 12419 9144 15755 -2590 162 268 N
ATOM 1546 CA HIS A 430 -32.425 5.511 15.464 1.00102.29 C
ANISOU 1546 CA HIS A 430 13069 9402 16393 -2838 -50 119 C
ATOM 1547 C HIS A 430 -31.491 4.344 15.114 1.00109.03 C
ANISOU 1547 C HIS A 430 14298 9844 17284 -2763 -98 -10 C
ATOM 1548 O HIS A 430 -30.347 4.567 14.695 1.00107.16 O
ANISOU 1548 O HIS A 430 14238 9591 16888 -2476 -49 -159 O
ATOM 1549 CB HIS A 430 -32.940 6.208 14.182 1.00103.01 C
ANISOU 1549 CB HIS A 430 13099 9666 16375 -2857 -204 -108 C
ATOM 1550 CG HIS A 430 -33.637 5.272 13.222 1.00110.09 C
ANISOU 1550 CG HIS A 430 14116 10316 17396 -3113 -442 -269 C
ATOM 1551 ND1 HIS A 430 -34.987 4.979 13.346 1.00114.35 N
ANISOU 1551 ND1 HIS A 430 14447 10907 18093 -3456 -554 -169 N
ATOM 1552 CD2 HIS A 430 -33.138 4.576 12.170 1.00113.06 C
ANISOU 1552 CD2 HIS A 430 14797 10404 17755 -3065 -590 -519 C
ATOM 1553 CE1 HIS A 430 -35.264 4.139 12.359 1.00116.42 C
ANISOU 1553 CE1 HIS A 430 14897 10899 18438 -3620 -775 -369 C
ATOM 1554 NE2 HIS A 430 -34.184 3.871 11.624 1.00116.13 N
ANISOU 1554 NE2 HIS A 430 15182 10645 18295 -3381 -807 -588 N
ATOM 1555 N ARG A 431 -32.020 3.104 15.269 1.00109.56 N
ANISOU 1555 N ARG A 431 14485 9588 17555 -3029 -204 52 N
ATOM 1556 CA ARG A 431 -31.355 1.814 15.044 1.00112.09 C
ANISOU 1556 CA ARG A 431 15187 9462 17938 -3004 -281 -45 C
ATOM 1557 C ARG A 431 -29.915 1.759 15.620 1.00113.76 C
ANISOU 1557 C ARG A 431 15581 9619 18025 -2647 -95 -18 C
ATOM 1558 O ARG A 431 -28.942 1.512 14.896 1.00113.95 O
ANISOU 1558 O ARG A 431 15874 9504 17918 -2409 -136 -229 O
ATOM 1559 CB ARG A 431 -31.464 1.360 13.572 1.00114.87 C
ANISOU 1559 CB ARG A 431 15763 9620 18263 -3046 -529 -357 C
ATOM 1560 N THR A 432 -29.800 2.049 16.935 1.00106.95 N
ANISOU 1560 N THR A 432 14547 8904 17187 -2594 110 243 N
ATOM 1561 CA THR A 432 -28.540 2.111 17.682 1.00103.56 C
ANISOU 1561 CA THR A 432 14221 8484 16642 -2267 302 304 C
ATOM 1562 C THR A 432 -28.772 1.777 19.154 1.00104.71 C
ANISOU 1562 C THR A 432 14261 8612 16911 -2332 458 616 C
ATOM 1563 O THR A 432 -29.835 2.089 19.693 1.00104.57 O
ANISOU 1563 O THR A 432 13967 8766 17001 -2556 477 809 O
ATOM 1564 CB THR A 432 -27.919 3.518 17.544 1.00104.62 C
ANISOU 1564 CB THR A 432 14182 9005 16563 -2001 412 233 C
ATOM 1565 N GLN A 433 -27.773 1.162 19.803 1.00 99.10 N
ANISOU 1565 N GLN A 433 13764 7722 16167 -2114 573 668 N
ATOM 1566 CA GLN A 433 -27.801 0.816 21.230 1.00 98.20 C
ANISOU 1566 CA GLN A 433 13589 7584 16140 -2106 742 958 C
ATOM 1567 C GLN A 433 -27.075 1.909 22.035 1.00 96.27 C
ANISOU 1567 C GLN A 433 13141 7701 15734 -1800 945 1037 C
ATOM 1568 O GLN A 433 -27.486 2.260 23.145 1.00 94.79 O
ANISOU 1568 O GLN A 433 12727 7698 15593 -1820 1075 1282 O
ATOM 1569 CB GLN A 433 -27.133 -0.554 21.467 1.00101.74 C
ANISOU 1569 CB GLN A 433 14419 7604 16632 -2028 740 963 C
ATOM 1570 N VAL A 434 -26.004 2.452 21.442 1.00 89.52 N
ANISOU 1570 N VAL A 434 12370 6957 14687 -1521 960 827 N
ATOM 1571 CA VAL A 434 -25.125 3.470 22.008 1.00 85.88 C
ANISOU 1571 CA VAL A 434 11765 6809 14057 -1225 1120 849 C
ATOM 1572 C VAL A 434 -25.846 4.813 22.179 1.00 86.08 C
ANISOU 1572 C VAL A 434 11447 7209 14052 -1298 1141 922 C
ATOM 1573 O VAL A 434 -26.466 5.302 21.226 1.00 86.61 O
ANISOU 1573 O VAL A 434 11438 7364 14107 -1441 1014 796 O
ATOM 1574 CB VAL A 434 -23.799 3.549 21.188 1.00 89.34 C
ANISOU 1574 CB VAL A 434 12401 7242 14303 -946 1110 602 C
ATOM 1575 CG1 VAL A 434 -24.057 3.577 19.679 1.00 89.95 C
ANISOU 1575 CG1 VAL A 434 12574 7256 14345 -1050 927 359 C
ATOM 1576 CG2 VAL A 434 -22.910 4.714 21.626 1.00 86.12 C
ANISOU 1576 CG2 VAL A 434 11823 7179 13719 -684 1250 607 C
ATOM 1577 N SER A 435 -25.785 5.401 23.397 1.00 78.22 N
ANISOU 1577 N SER A 435 10256 6430 13032 -1180 1292 1123 N
ATOM 1578 CA SER A 435 -26.447 6.685 23.652 1.00 74.45 C
ANISOU 1578 CA SER A 435 9478 6306 12503 -1205 1308 1199 C
ATOM 1579 C SER A 435 -25.877 7.780 22.772 1.00 76.41 C
ANISOU 1579 C SER A 435 9708 6750 12576 -1075 1263 989 C
ATOM 1580 O SER A 435 -24.677 7.769 22.468 1.00 75.95 O
ANISOU 1580 O SER A 435 9801 6655 12402 -872 1298 853 O
ATOM 1581 CB SER A 435 -26.390 7.076 25.130 1.00 74.58 C
ANISOU 1581 CB SER A 435 9327 6508 12503 -1050 1469 1435 C
ATOM 1582 OG SER A 435 -25.158 7.647 25.544 1.00 76.79 O
ANISOU 1582 OG SER A 435 9635 6914 12627 -744 1569 1380 O
ATOM 1583 N LEU A 436 -26.755 8.714 22.339 1.00 71.31 N
ANISOU 1583 N LEU A 436 8876 6321 11899 -1193 1185 970 N
ATOM 1584 CA LEU A 436 -26.423 9.868 21.501 1.00 67.12 C
ANISOU 1584 CA LEU A 436 8312 5988 11202 -1102 1135 798 C
ATOM 1585 C LEU A 436 -25.229 10.640 22.108 1.00 67.22 C
ANISOU 1585 C LEU A 436 8314 6159 11067 -826 1256 808 C
ATOM 1586 O LEU A 436 -24.315 10.965 21.370 1.00 67.08 O
ANISOU 1586 O LEU A 436 8401 6161 10927 -713 1244 641 O
ATOM 1587 CB LEU A 436 -27.691 10.729 21.270 1.00 66.21 C
ANISOU 1587 CB LEU A 436 7982 6097 11078 -1250 1051 835 C
ATOM 1588 CG LEU A 436 -27.622 12.034 20.449 1.00 68.04 C
ANISOU 1588 CG LEU A 436 8169 6547 11136 -1179 989 687 C
ATOM 1589 CD1 LEU A 436 -26.962 11.841 19.115 1.00 68.30 C
ANISOU 1589 CD1 LEU A 436 8397 6451 11105 -1166 912 448 C
ATOM 1590 CD2 LEU A 436 -28.984 12.546 20.172 1.00 69.05 C
ANISOU 1590 CD2 LEU A 436 8122 6843 11273 -1336 891 717 C
ATOM 1591 N LYS A 437 -25.162 10.781 23.446 1.00 61.49 N
ANISOU 1591 N LYS A 437 7479 5525 10358 -716 1373 1001 N
ATOM 1592 CA LYS A 437 -24.045 11.432 24.151 1.00 58.98 C
ANISOU 1592 CA LYS A 437 7147 5348 9913 -460 1478 1016 C
ATOM 1593 C LYS A 437 -22.726 10.709 23.898 1.00 65.52 C
ANISOU 1593 C LYS A 437 8177 6019 10700 -316 1528 900 C
ATOM 1594 O LYS A 437 -21.722 11.364 23.610 1.00 64.45 O
ANISOU 1594 O LYS A 437 8061 6006 10422 -168 1548 791 O
ATOM 1595 CB LYS A 437 -24.305 11.460 25.673 1.00 59.89 C
ANISOU 1595 CB LYS A 437 7126 5559 10070 -360 1586 1250 C
ATOM 1596 CG LYS A 437 -23.348 12.353 26.434 1.00 58.22 C
ANISOU 1596 CG LYS A 437 6865 5534 9720 -106 1663 1261 C
ATOM 1597 CD LYS A 437 -22.879 11.746 27.728 1.00 61.00 C
ANISOU 1597 CD LYS A 437 7220 5851 10108 66 1794 1414 C
ATOM 1598 CE LYS A 437 -22.179 12.799 28.565 1.00 71.64 C
ANISOU 1598 CE LYS A 437 8476 7425 11319 300 1842 1434 C
ATOM 1599 NZ LYS A 437 -21.422 12.190 29.696 1.00 84.96 N
ANISOU 1599 NZ LYS A 437 10195 9078 13010 514 1970 1534 N
ATOM 1600 N ASP A 438 -22.723 9.363 24.057 1.00 65.30 N
ANISOU 1600 N ASP A 438 8298 5727 10786 -352 1548 936 N
ATOM 1601 CA ASP A 438 -21.546 8.504 23.879 1.00 65.73 C
ANISOU 1601 CA ASP A 438 8569 5615 10790 -188 1593 835 C
ATOM 1602 C ASP A 438 -21.047 8.586 22.452 1.00 68.99 C
ANISOU 1602 C ASP A 438 9107 6004 11102 -189 1498 599 C
ATOM 1603 O ASP A 438 -19.838 8.683 22.249 1.00 68.49 O
ANISOU 1603 O ASP A 438 9116 6008 10898 13 1547 497 O
ATOM 1604 CB ASP A 438 -21.864 7.041 24.241 1.00 70.39 C
ANISOU 1604 CB ASP A 438 9326 5892 11528 -255 1605 924 C
ATOM 1605 CG ASP A 438 -22.181 6.753 25.702 1.00 81.45 C
ANISOU 1605 CG ASP A 438 10637 7293 13018 -217 1723 1175 C
ATOM 1606 OD1 ASP A 438 -21.948 7.653 26.560 1.00 79.22 O
ANISOU 1606 OD1 ASP A 438 10174 7266 12661 -71 1810 1268 O
ATOM 1607 OD2 ASP A 438 -22.678 5.632 25.990 1.00 88.99 O
ANISOU 1607 OD2 ASP A 438 11709 7991 14114 -335 1723 1282 O
ATOM 1608 N GLN A 439 -21.978 8.573 21.463 1.00 64.89 N
ANISOU 1608 N GLN A 439 8599 5415 10643 -406 1364 515 N
ATOM 1609 CA GLN A 439 -21.660 8.706 20.037 1.00 63.32 C
ANISOU 1609 CA GLN A 439 8509 5207 10344 -411 1262 294 C
ATOM 1610 C GLN A 439 -20.878 9.990 19.840 1.00 63.44 C
ANISOU 1610 C GLN A 439 8413 5510 10179 -272 1308 236 C
ATOM 1611 O GLN A 439 -19.766 9.940 19.321 1.00 64.50 O
ANISOU 1611 O GLN A 439 8648 5680 10180 -110 1332 113 O
ATOM 1612 CB GLN A 439 -22.932 8.765 19.171 1.00 64.96 C
ANISOU 1612 CB GLN A 439 8681 5365 10636 -666 1112 237 C
ATOM 1613 CG GLN A 439 -23.784 7.514 19.201 1.00 80.46 C
ANISOU 1613 CG GLN A 439 10754 7032 12787 -861 1032 279 C
ATOM 1614 CD GLN A 439 -25.021 7.672 18.353 1.00 96.72 C
ANISOU 1614 CD GLN A 439 12742 9090 14917 -1113 878 215 C
ATOM 1615 OE1 GLN A 439 -24.958 7.998 17.159 1.00 89.41 O
ANISOU 1615 OE1 GLN A 439 11873 8199 13898 -1110 777 24 O
ATOM 1616 NE2 GLN A 439 -26.175 7.417 18.946 1.00 89.80 N
ANISOU 1616 NE2 GLN A 439 11734 8186 14200 -1330 856 379 N
ATOM 1617 N ILE A 440 -21.435 11.130 20.295 1.00 55.27 N
ANISOU 1617 N ILE A 440 7177 4688 9135 -329 1318 333 N
ATOM 1618 CA ILE A 440 -20.809 12.443 20.146 1.00 52.01 C
ANISOU 1618 CA ILE A 440 6668 4529 8563 -235 1342 294 C
ATOM 1619 C ILE A 440 -19.447 12.560 20.847 1.00 56.87 C
ANISOU 1619 C ILE A 440 7283 5243 9081 -16 1461 320 C
ATOM 1620 O ILE A 440 -18.517 13.038 20.223 1.00 56.93 O
ANISOU 1620 O ILE A 440 7311 5371 8947 69 1470 217 O
ATOM 1621 CB ILE A 440 -21.773 13.624 20.460 1.00 52.22 C
ANISOU 1621 CB ILE A 440 6517 4735 8588 -330 1302 384 C
ATOM 1622 CG1 ILE A 440 -23.096 13.493 19.676 1.00 52.23 C
ANISOU 1622 CG1 ILE A 440 6504 4675 8666 -537 1180 344 C
ATOM 1623 CG2 ILE A 440 -21.093 14.962 20.165 1.00 49.98 C
ANISOU 1623 CG2 ILE A 440 6186 4669 8136 -251 1304 329 C
ATOM 1624 CD1 ILE A 440 -24.245 14.270 20.265 1.00 50.43 C
ANISOU 1624 CD1 ILE A 440 6097 4599 8466 -616 1152 475 C
ATOM 1625 N THR A 441 -19.316 12.134 22.113 1.00 54.92 N
ANISOU 1625 N THR A 441 7002 4963 8901 77 1553 460 N
ATOM 1626 CA THR A 441 -18.028 12.266 22.815 1.00 54.70 C
ANISOU 1626 CA THR A 441 6957 5052 8772 296 1659 477 C
ATOM 1627 C THR A 441 -16.945 11.421 22.210 1.00 61.42 C
ANISOU 1627 C THR A 441 7967 5828 9540 432 1688 351 C
ATOM 1628 O THR A 441 -15.811 11.887 22.091 1.00 62.56 O
ANISOU 1628 O THR A 441 8081 6151 9540 569 1734 290 O
ATOM 1629 CB THR A 441 -18.144 12.158 24.331 1.00 58.04 C
ANISOU 1629 CB THR A 441 7295 5496 9263 392 1748 655 C
ATOM 1630 OG1 THR A 441 -18.579 10.842 24.682 1.00 65.71 O
ANISOU 1630 OG1 THR A 441 8376 6226 10364 372 1777 726 O
ATOM 1631 CG2 THR A 441 -19.059 13.219 24.911 1.00 44.47 C
ANISOU 1631 CG2 THR A 441 5405 3921 7571 312 1715 770 C
ATOM 1632 N SER A 442 -17.299 10.218 21.754 1.00 58.76 N
ANISOU 1632 N SER A 442 7804 5237 9284 389 1649 304 N
ATOM 1633 CA SER A 442 -16.369 9.326 21.069 1.00 59.71 C
ANISOU 1633 CA SER A 442 8115 5263 9310 540 1652 167 C
ATOM 1634 C SER A 442 -16.144 9.774 19.613 1.00 67.69 C
ANISOU 1634 C SER A 442 9157 6363 10201 503 1569 -2 C
ATOM 1635 O SER A 442 -15.235 9.258 18.952 1.00 68.79 O
ANISOU 1635 O SER A 442 9422 6506 10209 665 1576 -124 O
ATOM 1636 CB SER A 442 -16.904 7.899 21.087 1.00 61.46 C
ANISOU 1636 CB SER A 442 8544 5147 9660 500 1612 175 C
ATOM 1637 OG SER A 442 -18.066 7.780 20.287 1.00 63.29 O
ANISOU 1637 OG SER A 442 8812 5231 10003 256 1481 131 O
ATOM 1638 N GLY A 443 -17.007 10.680 19.120 1.00 65.31 N
ANISOU 1638 N GLY A 443 8748 6135 9932 309 1492 -5 N
ATOM 1639 CA GLY A 443 -17.019 11.171 17.741 1.00 64.95 C
ANISOU 1639 CA GLY A 443 8727 6165 9785 251 1407 -149 C
ATOM 1640 C GLY A 443 -17.178 10.056 16.722 1.00 70.44 C
ANISOU 1640 C GLY A 443 9638 6638 10489 258 1314 -294 C
ATOM 1641 O GLY A 443 -16.596 10.123 15.636 1.00 70.49 O
ANISOU 1641 O GLY A 443 9716 6720 10348 349 1283 -433 O
ATOM 1642 N LYS A 444 -17.958 9.016 17.078 1.00 68.88 N
ANISOU 1642 N LYS A 444 9550 6164 10458 167 1265 -258 N
ATOM 1643 CA LYS A 444 -18.190 7.848 16.228 1.00 72.11 C
ANISOU 1643 CA LYS A 444 10197 6305 10896 160 1152 -393 C
ATOM 1644 C LYS A 444 -19.531 7.953 15.499 1.00 77.26 C
ANISOU 1644 C LYS A 444 10837 6857 11662 -96 1003 -443 C
ATOM 1645 O LYS A 444 -20.559 7.467 15.976 1.00 79.57 O
ANISOU 1645 O LYS A 444 11118 6974 12139 -288 954 -352 O
ATOM 1646 CB LYS A 444 -18.012 6.519 17.010 1.00 76.08 C
ANISOU 1646 CB LYS A 444 10881 6538 11488 240 1182 -336 C
ATOM 1647 N TYR A 445 -19.507 8.633 14.351 1.00 71.74 N
ANISOU 1647 N TYR A 445 10120 6297 10842 -95 936 -578 N
ATOM 1648 CA TYR A 445 -20.674 8.855 13.505 1.00 71.21 C
ANISOU 1648 CA TYR A 445 10034 6184 10838 -298 790 -656 C
ATOM 1649 C TYR A 445 -21.104 7.572 12.819 1.00 78.41 C
ANISOU 1649 C TYR A 445 11181 6783 11829 -349 639 -790 C
ATOM 1650 O TYR A 445 -20.290 6.676 12.552 1.00 79.60 O
ANISOU 1650 O TYR A 445 11547 6792 11906 -164 632 -884 O
ATOM 1651 CB TYR A 445 -20.406 9.956 12.455 1.00 69.84 C
ANISOU 1651 CB TYR A 445 9791 6259 10485 -245 774 -760 C
ATOM 1652 CG TYR A 445 -19.096 9.780 11.725 1.00 70.83 C
ANISOU 1652 CG TYR A 445 10040 6464 10409 5 813 -880 C
ATOM 1653 CD1 TYR A 445 -18.993 8.927 10.633 1.00 75.00 C
ANISOU 1653 CD1 TYR A 445 10781 6838 10875 96 699 -1063 C
ATOM 1654 CD2 TYR A 445 -17.954 10.468 12.126 1.00 70.20 C
ANISOU 1654 CD2 TYR A 445 9857 6626 10190 159 959 -809 C
ATOM 1655 CE1 TYR A 445 -17.776 8.725 9.979 1.00 77.30 C
ANISOU 1655 CE1 TYR A 445 11181 7231 10959 361 740 -1164 C
ATOM 1656 CE2 TYR A 445 -16.740 10.308 11.454 1.00 71.95 C
ANISOU 1656 CE2 TYR A 445 10161 6966 10211 392 1003 -904 C
ATOM 1657 CZ TYR A 445 -16.650 9.419 10.393 1.00 83.44 C
ANISOU 1657 CZ TYR A 445 11828 8282 11595 506 899 -1078 C
ATOM 1658 OH TYR A 445 -15.456 9.231 9.735 1.00 87.21 O
ANISOU 1658 OH TYR A 445 12381 8905 11851 768 944 -1165 O
ATOM 1659 N ASN A 446 -22.391 7.504 12.514 1.00 66.16 N
ANISOU 1659 N ASN A 446 9603 5144 10390 34 558 -348 N
ATOM 1660 CA ASN A 446 -22.972 6.389 11.816 1.00 68.26 C
ANISOU 1660 CA ASN A 446 9934 4958 11042 45 523 -553 C
ATOM 1661 C ASN A 446 -22.577 6.507 10.342 1.00 71.71 C
ANISOU 1661 C ASN A 446 10535 5361 11352 144 493 -989 C
ATOM 1662 O ASN A 446 -23.066 7.392 9.629 1.00 67.13 O
ANISOU 1662 O ASN A 446 10065 4939 10503 50 408 -1241 O
ATOM 1663 CB ASN A 446 -24.487 6.410 12.009 1.00 70.18 C
ANISOU 1663 CB ASN A 446 10170 5065 11431 -171 428 -580 C
ATOM 1664 CG ASN A 446 -25.167 5.160 11.542 1.00 91.81 C
ANISOU 1664 CG ASN A 446 12924 7303 14655 -183 385 -727 C
ATOM 1665 OD1 ASN A 446 -24.915 4.060 12.043 1.00 90.19 O
ANISOU 1665 OD1 ASN A 446 12624 6818 14827 -110 454 -501 O
ATOM 1666 ND2 ASN A 446 -26.060 5.309 10.584 1.00 82.46 N
ANISOU 1666 ND2 ASN A 446 11851 5990 13490 -279 257 -1104 N
ATOM 1667 N PHE A 447 -21.637 5.656 9.901 1.00 72.67 N
ANISOU 1667 N PHE A 447 10665 5304 11641 347 572 -1065 N
ATOM 1668 CA PHE A 447 -21.226 5.682 8.500 1.00 73.74 C
ANISOU 1668 CA PHE A 447 10949 5425 11644 465 567 -1482 C
ATOM 1669 C PHE A 447 -21.905 4.562 7.709 1.00 81.07 C
ANISOU 1669 C PHE A 447 11954 5897 12951 488 491 -1805 C
ATOM 1670 O PHE A 447 -21.664 3.394 8.003 1.00 84.48 O
ANISOU 1670 O PHE A 447 12308 5990 13800 590 538 -1718 O
ATOM 1671 CB PHE A 447 -19.690 5.665 8.341 1.00 76.21 C
ANISOU 1671 CB PHE A 447 11225 5900 11833 687 708 -1432 C
ATOM 1672 CG PHE A 447 -19.263 5.782 6.894 1.00 78.74 C
ANISOU 1672 CG PHE A 447 11694 6262 11960 812 728 -1852 C
ATOM 1673 CD1 PHE A 447 -19.270 7.012 6.248 1.00 78.95 C
ANISOU 1673 CD1 PHE A 447 11821 6637 11539 746 704 -1997 C
ATOM 1674 CD2 PHE A 447 -18.927 4.649 6.157 1.00 84.86 C
ANISOU 1674 CD2 PHE A 447 12509 6720 13013 992 765 -2113 C
ATOM 1675 CE1 PHE A 447 -18.916 7.116 4.907 1.00 81.00 C
ANISOU 1675 CE1 PHE A 447 12221 6965 11592 863 731 -2360 C
ATOM 1676 CE2 PHE A 447 -18.592 4.749 4.804 1.00 88.81 C
ANISOU 1676 CE2 PHE A 447 13152 7292 13301 1114 787 -2525 C
ATOM 1677 CZ PHE A 447 -18.584 5.985 4.189 1.00 84.55 C
ANISOU 1677 CZ PHE A 447 12714 7135 12277 1050 775 -2631 C
ATOM 1678 N ILE A 448 -22.750 4.914 6.710 1.00 77.13 N
ANISOU 1678 N ILE A 448 11598 5384 12324 396 362 -2178 N
ATOM 1679 CA ILE A 448 -23.458 3.945 5.851 1.00 79.61 C
ANISOU 1679 CA ILE A 448 11990 5290 12969 409 253 -2559 C
ATOM 1680 C ILE A 448 -22.809 3.924 4.447 1.00 87.73 C
ANISOU 1680 C ILE A 448 13172 6387 13772 597 266 -2998 C
ATOM 1681 O ILE A 448 -23.056 4.826 3.642 1.00 85.06 O
ANISOU 1681 O ILE A 448 12967 6322 13032 556 198 -3222 O
ATOM 1682 CB ILE A 448 -24.997 4.165 5.823 1.00 80.93 C
ANISOU 1682 CB ILE A 448 12177 5346 13224 174 77 -2664 C
ATOM 1683 CG1 ILE A 448 -25.587 4.149 7.247 1.00 78.59 C
ANISOU 1683 CG1 ILE A 448 11711 5006 13144 6 101 -2212 C
ATOM 1684 CG2 ILE A 448 -25.667 3.110 4.940 1.00 85.49 C
ANISOU 1684 CG2 ILE A 448 12816 5489 14178 195 -52 -3080 C
ATOM 1685 CD1 ILE A 448 -26.959 4.707 7.365 1.00 80.68 C
ANISOU 1685 CD1 ILE A 448 11969 5289 13398 -228 -39 -2250 C
ATOM 1686 N PRO A 449 -21.956 2.911 4.161 1.00 91.81 N
ANISOU 1686 N PRO A 449 13669 6676 14540 813 362 -3110 N
ATOM 1687 CA PRO A 449 -21.226 2.881 2.871 1.00 94.44 C
ANISOU 1687 CA PRO A 449 14133 7119 14631 1018 409 -3519 C
ATOM 1688 C PRO A 449 -22.026 3.078 1.589 1.00101.76 C
ANISOU 1688 C PRO A 449 15242 8063 15361 985 251 -4015 C
ATOM 1689 O PRO A 449 -21.572 3.824 0.719 1.00100.62 O
ANISOU 1689 O PRO A 449 15217 8265 14747 1069 290 -4201 O
ATOM 1690 CB PRO A 449 -20.511 1.527 2.893 1.00 99.90 C
ANISOU 1690 CB PRO A 449 14745 7435 15778 1229 501 -3583 C
ATOM 1691 CG PRO A 449 -20.352 1.205 4.336 1.00103.41 C
ANISOU 1691 CG PRO A 449 15002 7753 16535 1173 565 -3059 C
ATOM 1692 CD PRO A 449 -21.558 1.777 5.027 1.00 96.31 C
ANISOU 1692 CD PRO A 449 14082 6897 15616 897 444 -2846 C
ATOM 1693 N GLU A 450 -23.199 2.416 1.473 1.00102.13 N
ANISOU 1693 N GLU A 450 15295 7744 15764 865 72 -4214 N
ATOM 1694 CA GLU A 450 -24.081 2.480 0.294 1.00103.97 C
ANISOU 1694 CA GLU A 450 15685 7952 15869 830 -122 -4708 C
ATOM 1695 C GLU A 450 -24.524 3.915 0.017 1.00103.91 C
ANISOU 1695 C GLU A 450 15776 8387 15318 692 -197 -4665 C
ATOM 1696 O GLU A 450 -24.526 4.354 -1.134 1.00104.04 O
ANISOU 1696 O GLU A 450 15952 8626 14953 764 -262 -5007 O
ATOM 1697 CB GLU A 450 -25.315 1.559 0.451 1.00107.93 C
ANISOU 1697 CB GLU A 450 16125 7960 16922 691 -309 -4863 C
ATOM 1698 CG GLU A 450 -25.005 0.110 0.813 1.00124.22 C
ANISOU 1698 CG GLU A 450 18066 9514 19617 798 -252 -4862 C
ATOM 1699 CD GLU A 450 -25.064 -0.264 2.287 1.00143.29 C
ANISOU 1699 CD GLU A 450 20282 11716 22444 683 -165 -4309 C
ATOM 1700 OE1 GLU A 450 -25.802 0.396 3.056 1.00127.16 O
ANISOU 1700 OE1 GLU A 450 18181 9792 20341 461 -213 -4009 O
ATOM 1701 OE2 GLU A 450 -24.415 -1.269 2.659 1.00138.06 O
ANISOU 1701 OE2 GLU A 450 19517 10756 22183 822 -55 -4186 O
ATOM 1702 N VAL A 451 -24.866 4.645 1.079 1.00 97.28 N
ANISOU 1702 N VAL A 451 14836 7683 14441 507 -183 -4238 N
ATOM 1703 CA VAL A 451 -25.314 6.034 1.002 1.00 94.43 C
ANISOU 1703 CA VAL A 451 14537 7705 13638 362 -253 -4144 C
ATOM 1704 C VAL A 451 -24.170 6.941 0.510 1.00 97.70 C
ANISOU 1704 C VAL A 451 15029 8558 13535 496 -107 -4096 C
ATOM 1705 O VAL A 451 -24.355 7.703 -0.445 1.00 96.32 O
ANISOU 1705 O VAL A 451 14993 8645 12958 499 -180 -4297 O
ATOM 1706 CB VAL A 451 -25.896 6.488 2.375 1.00 95.37 C
ANISOU 1706 CB VAL A 451 14502 7832 13902 148 -257 -3707 C
ATOM 1707 CG1 VAL A 451 -26.141 7.991 2.417 1.00 91.42 C
ANISOU 1707 CG1 VAL A 451 14039 7740 12957 24 -297 -3571 C
ATOM 1708 CG2 VAL A 451 -27.173 5.723 2.715 1.00 96.61 C
ANISOU 1708 CG2 VAL A 451 14584 7591 14532 -7 -408 -3770 C
ATOM 1709 N TRP A 452 -22.986 6.806 1.146 1.00 94.55 N
ANISOU 1709 N TRP A 452 14527 8226 13171 611 99 -3821 N
ATOM 1710 CA TRP A 452 -21.777 7.598 0.911 1.00 93.07 C
ANISOU 1710 CA TRP A 452 14353 8424 12585 729 270 -3699 C
ATOM 1711 C TRP A 452 -20.953 7.285 -0.327 1.00 99.52 C
ANISOU 1711 C TRP A 452 15285 9336 13193 963 367 -4033 C
ATOM 1712 O TRP A 452 -20.121 8.110 -0.704 1.00 97.79 O
ANISOU 1712 O TRP A 452 15093 9478 12585 1034 493 -3957 O
ATOM 1713 CB TRP A 452 -20.903 7.621 2.161 1.00 90.19 C
ANISOU 1713 CB TRP A 452 13806 8106 12355 745 427 -3264 C
ATOM 1714 CG TRP A 452 -21.458 8.492 3.247 1.00 87.54 C
ANISOU 1714 CG TRP A 452 13377 7908 11978 530 370 -2915 C
ATOM 1715 CD1 TRP A 452 -22.320 8.122 4.238 1.00 89.81 C
ANISOU 1715 CD1 TRP A 452 13565 7975 12584 382 290 -2729 C
ATOM 1716 CD2 TRP A 452 -21.170 9.883 3.458 1.00 84.33 C
ANISOU 1716 CD2 TRP A 452 12953 7893 11197 446 398 -2718 C
ATOM 1717 NE1 TRP A 452 -22.601 9.199 5.047 1.00 86.00 N
ANISOU 1717 NE1 TRP A 452 13011 7746 11920 220 267 -2453 N
ATOM 1718 CE2 TRP A 452 -21.903 10.294 4.596 1.00 86.02 C
ANISOU 1718 CE2 TRP A 452 13061 8110 11515 255 323 -2449 C
ATOM 1719 CE3 TRP A 452 -20.375 10.833 2.782 1.00 84.47 C
ANISOU 1719 CE3 TRP A 452 13025 8255 10814 512 483 -2741 C
ATOM 1720 CZ2 TRP A 452 -21.867 11.618 5.074 1.00 82.14 C
ANISOU 1720 CZ2 TRP A 452 12519 7941 10750 136 315 -2244 C
ATOM 1721 CZ3 TRP A 452 -20.344 12.140 3.254 1.00 82.69 C
ANISOU 1721 CZ3 TRP A 452 12745 8324 10348 380 473 -2509 C
ATOM 1722 CH2 TRP A 452 -21.083 12.523 4.383 1.00 81.08 C
ANISOU 1722 CH2 TRP A 452 12438 8103 10264 198 382 -2283 C
ATOM 1723 N ALA A 453 -21.188 6.122 -0.974 1.00100.22 N
ANISOU 1723 N ALA A 453 15432 9108 13540 1084 311 -4409 N
ATOM 1724 CA ALA A 453 -20.499 5.711 -2.207 1.00102.91 C
ANISOU 1724 CA ALA A 453 15885 9525 13692 1325 395 -4799 C
ATOM 1725 C ALA A 453 -20.818 6.687 -3.357 1.00107.26 C
ANISOU 1725 C ALA A 453 16616 10444 13694 1311 319 -5019 C
ATOM 1726 O ALA A 453 -20.020 6.841 -4.286 1.00108.93 O
ANISOU 1726 O ALA A 453 16913 10912 13562 1497 447 -5204 O
ATOM 1727 CB ALA A 453 -20.912 4.305 -2.582 1.00107.31 C
ANISOU 1727 CB ALA A 453 16460 9632 14682 1421 298 -5186 C
ATOM 1728 N GLU A 454 -21.979 7.363 -3.255 1.00101.79 N
ANISOU 1728 N GLU A 454 15968 9786 12920 1092 118 -4969 N
ATOM 1729 CA GLU A 454 -22.497 8.375 -4.180 1.00100.75 C
ANISOU 1729 CA GLU A 454 15992 9978 12311 1037 1 -5101 C
ATOM 1730 C GLU A 454 -21.711 9.680 -4.022 1.00 98.22 C
ANISOU 1730 C GLU A 454 15646 10081 11592 1018 163 -4743 C
ATOM 1731 O GLU A 454 -21.568 10.437 -4.984 1.00 99.71 O
ANISOU 1731 O GLU A 454 15960 10603 11324 1081 185 -4837 O
ATOM 1732 CB GLU A 454 -23.995 8.650 -3.886 1.00100.90 C
ANISOU 1732 CB GLU A 454 16015 9847 12475 798 -265 -5101 C
ATOM 1733 CG GLU A 454 -24.906 7.441 -4.054 1.00113.35 C
ANISOU 1733 CG GLU A 454 17605 11000 14464 788 -455 -5468 C
ATOM 1734 N VAL A 455 -21.233 9.946 -2.798 1.00 87.59 N
ANISOU 1734 N VAL A 455 14131 8721 10427 931 272 -4330 N
ATOM 1735 CA VAL A 455 -20.485 11.160 -2.399 1.00 82.09 C
ANISOU 1735 CA VAL A 455 13363 8372 9455 884 412 -3963 C
ATOM 1736 C VAL A 455 -18.981 10.970 -2.701 1.00 84.15 C
ANISOU 1736 C VAL A 455 13578 8802 9594 1102 677 -3929 C
ATOM 1737 O VAL A 455 -18.477 9.844 -2.637 1.00 85.56 O
ANISOU 1737 O VAL A 455 13709 8761 10039 1259 765 -4056 O
ATOM 1738 CB VAL A 455 -20.775 11.516 -0.896 1.00 80.43 C
ANISOU 1738 CB VAL A 455 12983 8076 9500 688 377 -3576 C
ATOM 1739 CG1 VAL A 455 -19.982 12.726 -0.417 1.00 77.15 C
ANISOU 1739 CG1 VAL A 455 12471 7989 8854 638 501 -3227 C
ATOM 1740 CG2 VAL A 455 -22.269 11.728 -0.653 1.00 78.24 C
ANISOU 1740 CG2 VAL A 455 12740 7657 9331 481 134 -3624 C
ATOM 1741 N SER A 456 -18.286 12.065 -3.064 1.00 77.38 N
ANISOU 1741 N SER A 456 12725 8321 8355 1115 802 -3763 N
ATOM 1742 CA SER A 456 -16.850 12.050 -3.347 1.00 77.84 C
ANISOU 1742 CA SER A 456 12713 8581 8281 1304 1067 -3696 C
ATOM 1743 C SER A 456 -16.019 11.830 -2.067 1.00 82.57 C
ANISOU 1743 C SER A 456 13089 9089 9194 1303 1187 -3374 C
ATOM 1744 O SER A 456 -16.480 12.136 -0.957 1.00 80.67 O
ANISOU 1744 O SER A 456 12751 8760 9140 1126 1083 -3122 O
ATOM 1745 CB SER A 456 -16.424 13.342 -4.045 1.00 78.41 C
ANISOU 1745 CB SER A 456 12830 9067 7896 1287 1160 -3562 C
ATOM 1746 OG SER A 456 -16.056 14.377 -3.144 1.00 80.94 O
ANISOU 1746 OG SER A 456 12993 9525 8236 1141 1206 -3160 O
ATOM 1747 N GLU A 457 -14.784 11.324 -2.237 1.00 81.38 N
ANISOU 1747 N GLU A 457 12851 8989 9082 1511 1407 -3384 N
ATOM 1748 CA GLU A 457 -13.822 11.085 -1.156 1.00 80.38 C
ANISOU 1748 CA GLU A 457 12503 8814 9224 1553 1532 -3092 C
ATOM 1749 C GLU A 457 -13.382 12.408 -0.502 1.00 81.08 C
ANISOU 1749 C GLU A 457 12460 9187 9158 1405 1571 -2715 C
ATOM 1750 O GLU A 457 -13.153 12.439 0.715 1.00 79.50 O
ANISOU 1750 O GLU A 457 12092 8926 9188 1334 1551 -2440 O
ATOM 1751 CB GLU A 457 -12.610 10.299 -1.685 1.00 85.17 C
ANISOU 1751 CB GLU A 457 13049 9433 9878 1827 1759 -3232 C
ATOM 1752 N LYS A 458 -13.305 13.501 -1.313 1.00 75.75 N
ANISOU 1752 N LYS A 458 11861 8821 8101 1359 1615 -2706 N
ATOM 1753 CA LYS A 458 -12.947 14.851 -0.869 1.00 72.72 C
ANISOU 1753 CA LYS A 458 11362 8695 7574 1211 1642 -2386 C
ATOM 1754 C LYS A 458 -14.017 15.442 0.060 1.00 73.48 C
ANISOU 1754 C LYS A 458 11447 8699 7774 968 1415 -2235 C
ATOM 1755 O LYS A 458 -13.671 15.997 1.101 1.00 71.21 O
ANISOU 1755 O LYS A 458 10986 8474 7597 869 1410 -1963 O
ATOM 1756 CB LYS A 458 -12.725 15.783 -2.066 1.00 75.38 C
ANISOU 1756 CB LYS A 458 11798 9341 7504 1224 1735 -2418 C
ATOM 1757 CG LYS A 458 -11.410 15.568 -2.781 1.00 80.08 C
ANISOU 1757 CG LYS A 458 12325 10130 7971 1437 2015 -2443 C
ATOM 1758 CD LYS A 458 -11.327 16.399 -4.048 1.00 83.86 C
ANISOU 1758 CD LYS A 458 12924 10920 8020 1458 2113 -2474 C
ATOM 1759 CE LYS A 458 -9.919 16.469 -4.577 1.00 88.39 C
ANISOU 1759 CE LYS A 458 13372 11737 8473 1634 2422 -2404 C
ATOM 1760 NZ LYS A 458 -9.746 17.644 -5.459 1.00103.71 N
ANISOU 1760 NZ LYS A 458 15358 14013 10036 1588 2529 -2263 N
ATOM 1761 N ALA A 459 -15.307 15.326 -0.315 1.00 69.72 N
ANISOU 1761 N ALA A 459 11143 8084 7262 879 1225 -2428 N
ATOM 1762 CA ALA A 459 -16.424 15.826 0.482 1.00 66.76 C
ANISOU 1762 CA ALA A 459 10761 7615 6989 659 1015 -2324 C
ATOM 1763 C ALA A 459 -16.375 15.190 1.873 1.00 70.10 C
ANISOU 1763 C ALA A 459 11026 7845 7765 628 990 -2158 C
ATOM 1764 O ALA A 459 -16.295 15.915 2.867 1.00 67.15 O
ANISOU 1764 O ALA A 459 10516 7564 7436 500 953 -1909 O
ATOM 1765 CB ALA A 459 -17.744 15.502 -0.208 1.00 68.16 C
ANISOU 1765 CB ALA A 459 11134 7640 7124 610 828 -2601 C
ATOM 1766 N LEU A 460 -16.308 13.840 1.926 1.00 68.68 N
ANISOU 1766 N LEU A 460 10853 7412 7831 763 1023 -2289 N
ATOM 1767 CA LEU A 460 -16.231 13.052 3.162 1.00 68.09 C
ANISOU 1767 CA LEU A 460 10634 7131 8104 765 1013 -2116 C
ATOM 1768 C LEU A 460 -14.960 13.329 3.996 1.00 71.36 C
ANISOU 1768 C LEU A 460 10840 7720 8554 824 1147 -1823 C
ATOM 1769 O LEU A 460 -15.022 13.243 5.225 1.00 70.57 O
ANISOU 1769 O LEU A 460 10605 7578 8630 754 1096 -1590 O
ATOM 1770 CB LEU A 460 -16.385 11.552 2.842 1.00 71.04 C
ANISOU 1770 CB LEU A 460 11066 7177 8750 916 1026 -2338 C
ATOM 1771 CG LEU A 460 -16.256 10.535 3.986 1.00 75.80 C
ANISOU 1771 CG LEU A 460 11529 7521 9752 952 1030 -2153 C
ATOM 1772 CD1 LEU A 460 -17.393 10.667 5.007 1.00 73.65 C
ANISOU 1772 CD1 LEU A 460 11223 7137 9623 742 869 -1991 C
ATOM 1773 CD2 LEU A 460 -16.173 9.136 3.439 1.00 80.18 C
ANISOU 1773 CD2 LEU A 460 12136 7754 10576 1130 1067 -2401 C
ATOM 1774 N ASP A 461 -13.821 13.661 3.337 1.00 67.73 N
ANISOU 1774 N ASP A 461 10343 7467 7923 955 1318 -1835 N
ATOM 1775 CA ASP A 461 -12.565 13.992 4.021 1.00 66.40 C
ANISOU 1775 CA ASP A 461 9960 7481 7788 1013 1442 -1581 C
ATOM 1776 C ASP A 461 -12.771 15.234 4.873 1.00 67.38 C
ANISOU 1776 C ASP A 461 9981 7798 7822 811 1343 -1349 C
ATOM 1777 O ASP A 461 -12.397 15.215 6.044 1.00 67.91 O
ANISOU 1777 O ASP A 461 9873 7893 8036 793 1321 -1127 O
ATOM 1778 CB ASP A 461 -11.407 14.187 3.022 1.00 69.79 C
ANISOU 1778 CB ASP A 461 10370 8106 8041 1174 1651 -1656 C
ATOM 1779 CG ASP A 461 -10.043 14.387 3.663 1.00 77.98 C
ANISOU 1779 CG ASP A 461 11161 9308 9161 1254 1785 -1418 C
ATOM 1780 OD1 ASP A 461 -9.557 13.450 4.337 1.00 79.78 O
ANISOU 1780 OD1 ASP A 461 11270 9393 9652 1380 1816 -1343 O
ATOM 1781 OD2 ASP A 461 -9.434 15.451 3.438 1.00 82.29 O
ANISOU 1781 OD2 ASP A 461 11624 10115 9525 1199 1860 -1308 O
ATOM 1782 N LEU A 462 -13.433 16.281 4.316 1.00 60.70 N
ANISOU 1782 N LEU A 462 9244 7074 6746 664 1266 -1411 N
ATOM 1783 CA LEU A 462 -13.740 17.533 5.029 1.00 57.09 C
ANISOU 1783 CA LEU A 462 8700 6774 6217 467 1156 -1239 C
ATOM 1784 C LEU A 462 -14.638 17.285 6.237 1.00 61.41 C
ANISOU 1784 C LEU A 462 9207 7187 6938 350 997 -1155 C
ATOM 1785 O LEU A 462 -14.365 17.826 7.302 1.00 60.64 O
ANISOU 1785 O LEU A 462 8945 7213 6882 275 956 -963 O
ATOM 1786 CB LEU A 462 -14.374 18.543 4.073 1.00 55.56 C
ANISOU 1786 CB LEU A 462 8650 6683 5777 356 1100 -1339 C
ATOM 1787 CG LEU A 462 -14.716 19.941 4.588 1.00 56.57 C
ANISOU 1787 CG LEU A 462 8703 6953 5840 158 985 -1200 C
ATOM 1788 CD1 LEU A 462 -13.531 20.644 5.258 1.00 54.35 C
ANISOU 1788 CD1 LEU A 462 8187 6865 5597 150 1066 -986 C
ATOM 1789 CD2 LEU A 462 -15.187 20.780 3.444 1.00 61.71 C
ANISOU 1789 CD2 LEU A 462 9501 7686 6259 96 955 -1288 C
ATOM 1790 N VAL A 463 -15.681 16.439 6.074 1.00 59.15 N
ANISOU 1790 N VAL A 463 9060 6655 6760 342 912 -1304 N
ATOM 1791 CA VAL A 463 -16.626 16.026 7.119 1.00 57.83 C
ANISOU 1791 CA VAL A 463 8861 6334 6778 239 786 -1226 C
ATOM 1792 C VAL A 463 -15.786 15.478 8.271 1.00 62.80 C
ANISOU 1792 C VAL A 463 9302 6979 7581 327 852 -989 C
ATOM 1793 O VAL A 463 -15.796 16.059 9.359 1.00 61.43 O
ANISOU 1793 O VAL A 463 8993 6951 7398 234 793 -799 O
ATOM 1794 CB VAL A 463 -17.670 14.983 6.587 1.00 62.34 C
ANISOU 1794 CB VAL A 463 9592 6599 7493 248 716 -1438 C
ATOM 1795 CG1 VAL A 463 -18.502 14.377 7.720 1.00 61.53 C
ANISOU 1795 CG1 VAL A 463 9422 6321 7635 162 628 -1309 C
ATOM 1796 CG2 VAL A 463 -18.573 15.591 5.517 1.00 61.20 C
ANISOU 1796 CG2 VAL A 463 9623 6470 7160 155 613 -1664 C
ATOM 1797 N LYS A 464 -14.978 14.428 7.986 1.00 61.27 N
ANISOU 1797 N LYS A 464 9092 6664 7525 521 974 -1011 N
ATOM 1798 CA LYS A 464 -14.054 13.769 8.917 1.00 61.40 C
ANISOU 1798 CA LYS A 464 8930 6677 7721 648 1044 -788 C
ATOM 1799 C LYS A 464 -13.184 14.785 9.657 1.00 64.89 C
ANISOU 1799 C LYS A 464 9182 7435 8037 615 1055 -583 C
ATOM 1800 O LYS A 464 -13.031 14.657 10.858 1.00 66.70 O
ANISOU 1800 O LYS A 464 9266 7723 8356 612 1011 -362 O
ATOM 1801 CB LYS A 464 -13.167 12.751 8.178 1.00 65.55 C
ANISOU 1801 CB LYS A 464 9469 7059 8377 875 1189 -896 C
ATOM 1802 CG LYS A 464 -13.864 11.466 7.757 1.00 66.58 C
ANISOU 1802 CG LYS A 464 9729 6825 8742 941 1169 -1071 C
ATOM 1803 CD LYS A 464 -12.929 10.594 6.940 1.00 75.11 C
ANISOU 1803 CD LYS A 464 10820 7790 9927 1177 1317 -1230 C
ATOM 1804 CE LYS A 464 -13.330 9.145 6.965 1.00 94.71 C
ANISOU 1804 CE LYS A 464 13338 9879 12769 1278 1300 -1308 C
ATOM 1805 NZ LYS A 464 -12.298 8.286 6.332 1.00109.69 N
ANISOU 1805 NZ LYS A 464 15205 11669 14804 1531 1450 -1445 N
ATOM 1806 N LYS A 465 -12.678 15.824 8.963 1.00 59.87 N
ANISOU 1806 N LYS A 465 8545 7007 7197 581 1102 -652 N
ATOM 1807 CA LYS A 465 -11.834 16.879 9.543 1.00 57.43 C
ANISOU 1807 CA LYS A 465 8044 6981 6797 535 1104 -494 C
ATOM 1808 C LYS A 465 -12.561 17.857 10.464 1.00 59.38 C
ANISOU 1808 C LYS A 465 8235 7358 6968 339 944 -412 C
ATOM 1809 O LYS A 465 -11.929 18.475 11.319 1.00 58.48 O
ANISOU 1809 O LYS A 465 7931 7447 6842 314 911 -268 O
ATOM 1810 CB LYS A 465 -11.025 17.589 8.458 1.00 58.05 C
ANISOU 1810 CB LYS A 465 8122 7205 6729 570 1229 -575 C
ATOM 1811 CG LYS A 465 -9.770 16.806 8.121 1.00 59.83 C
ANISOU 1811 CG LYS A 465 8257 7423 7052 789 1405 -558 C
ATOM 1812 CD LYS A 465 -9.309 17.002 6.694 1.00 67.61 C
ANISOU 1812 CD LYS A 465 9335 8462 7892 865 1564 -716 C
ATOM 1813 CE LYS A 465 -8.114 16.122 6.387 1.00 73.92 C
ANISOU 1813 CE LYS A 465 10032 9243 8812 1100 1748 -719 C
ATOM 1814 NZ LYS A 465 -7.484 16.459 5.070 1.00 81.13 N
ANISOU 1814 NZ LYS A 465 10985 10288 9551 1181 1938 -837 N
ATOM 1815 N LEU A 466 -13.881 17.998 10.294 1.00 55.55 N
ANISOU 1815 N LEU A 466 7904 6761 6440 205 841 -525 N
ATOM 1816 CA LEU A 466 -14.721 18.886 11.119 1.00 53.24 C
ANISOU 1816 CA LEU A 466 7571 6573 6087 24 693 -485 C
ATOM 1817 C LEU A 466 -15.345 18.102 12.249 1.00 57.94 C
ANISOU 1817 C LEU A 466 8125 7084 6805 19 632 -363 C
ATOM 1818 O LEU A 466 -15.581 18.655 13.305 1.00 56.80 O
ANISOU 1818 O LEU A 466 7863 7099 6619 -66 546 -260 O
ATOM 1819 CB LEU A 466 -15.817 19.598 10.295 1.00 51.39 C
ANISOU 1819 CB LEU A 466 7504 6278 5744 -117 612 -664 C
ATOM 1820 CG LEU A 466 -15.356 20.617 9.228 1.00 54.21 C
ANISOU 1820 CG LEU A 466 7900 6747 5949 -141 658 -743 C
ATOM 1821 CD1 LEU A 466 -16.413 20.768 8.132 1.00 53.00 C
ANISOU 1821 CD1 LEU A 466 7964 6471 5704 -207 599 -928 C
ATOM 1822 CD2 LEU A 466 -15.062 21.967 9.849 1.00 52.64 C
ANISOU 1822 CD2 LEU A 466 7539 6761 5702 -257 593 -656 C
ATOM 1823 N LEU A 467 -15.611 16.808 12.037 1.00 56.63 N
ANISOU 1823 N LEU A 467 8048 6670 6800 113 680 -374 N
ATOM 1824 CA LEU A 467 -16.175 15.969 13.083 1.00 55.93 C
ANISOU 1824 CA LEU A 467 7911 6480 6859 112 642 -213 C
ATOM 1825 C LEU A 467 -15.102 15.343 13.996 1.00 61.15 C
ANISOU 1825 C LEU A 467 8399 7225 7612 264 699 35 C
ATOM 1826 O LEU A 467 -15.268 14.219 14.471 1.00 64.83 O
ANISOU 1826 O LEU A 467 8851 7516 8266 341 722 176 O
ATOM 1827 CB LEU A 467 -17.210 14.977 12.532 1.00 56.07 C
ANISOU 1827 CB LEU A 467 8090 6167 7050 99 633 -331 C
ATOM 1828 CG LEU A 467 -18.510 15.620 11.971 1.00 58.23 C
ANISOU 1828 CG LEU A 467 8500 6386 7239 -74 530 -534 C
ATOM 1829 CD1 LEU A 467 -19.504 14.552 11.545 1.00 58.93 C
ANISOU 1829 CD1 LEU A 467 8714 6139 7539 -85 506 -650 C
ATOM 1830 CD2 LEU A 467 -19.181 16.584 12.992 1.00 55.94 C
ANISOU 1830 CD2 LEU A 467 8116 6299 6841 -236 431 -441 C
ATOM 1831 N VAL A 468 -14.014 16.118 14.264 1.00 54.20 N
ANISOU 1831 N VAL A 468 7370 6613 6610 299 710 97 N
ATOM 1832 CA VAL A 468 -12.869 15.806 15.149 1.00 54.10 C
ANISOU 1832 CA VAL A 468 7159 6756 6641 436 733 320 C
ATOM 1833 C VAL A 468 -13.296 16.181 16.585 1.00 58.25 C
ANISOU 1833 C VAL A 468 7562 7497 7072 353 618 494 C
ATOM 1834 O VAL A 468 -13.821 17.269 16.803 1.00 57.54 O
ANISOU 1834 O VAL A 468 7462 7575 6824 201 530 402 O
ATOM 1835 CB VAL A 468 -11.573 16.566 14.693 1.00 56.39 C
ANISOU 1835 CB VAL A 468 7335 7236 6855 494 788 271 C
ATOM 1836 CG1 VAL A 468 -10.499 16.622 15.781 1.00 56.86 C
ANISOU 1836 CG1 VAL A 468 7151 7533 6919 588 756 481 C
ATOM 1837 CG2 VAL A 468 -11.009 15.988 13.399 1.00 56.87 C
ANISOU 1837 CG2 VAL A 468 7489 7114 7004 624 935 139 C
ATOM 1838 N VAL A 469 -13.110 15.271 17.535 1.00 55.83 N
ANISOU 1838 N VAL A 469 7167 7185 6862 458 619 741 N
ATOM 1839 CA VAL A 469 -13.463 15.442 18.954 1.00 54.91 C
ANISOU 1839 CA VAL A 469 6930 7300 6633 416 528 943 C
ATOM 1840 C VAL A 469 -12.649 16.528 19.682 1.00 59.49 C
ANISOU 1840 C VAL A 469 7321 8266 7017 407 437 958 C
ATOM 1841 O VAL A 469 -13.247 17.322 20.405 1.00 59.42 O
ANISOU 1841 O VAL A 469 7269 8471 6836 287 341 927 O
ATOM 1842 CB VAL A 469 -13.447 14.079 19.675 1.00 59.86 C
ANISOU 1842 CB VAL A 469 7517 7800 7429 549 567 1241 C
ATOM 1843 CG1 VAL A 469 -13.477 14.229 21.189 1.00 60.05 C
ANISOU 1843 CG1 VAL A 469 7385 8141 7292 557 485 1498 C
ATOM 1844 CG2 VAL A 469 -14.599 13.203 19.187 1.00 59.82 C
ANISOU 1844 CG2 VAL A 469 7681 7428 7621 494 619 1210 C
ATOM 1845 N ASP A 470 -11.308 16.568 19.491 1.00 56.48 N
ANISOU 1845 N ASP A 470 6814 7969 6675 536 465 986 N
ATOM 1846 CA ASP A 470 -10.406 17.571 20.088 1.00 54.69 C
ANISOU 1846 CA ASP A 470 6382 8083 6313 534 372 978 C
ATOM 1847 C ASP A 470 -10.718 18.952 19.477 1.00 56.17 C
ANISOU 1847 C ASP A 470 6609 8330 6402 355 332 711 C
ATOM 1848 O ASP A 470 -10.486 19.134 18.277 1.00 55.60 O
ANISOU 1848 O ASP A 470 6626 8098 6402 342 423 569 O
ATOM 1849 CB ASP A 470 -8.930 17.182 19.844 1.00 56.57 C
ANISOU 1849 CB ASP A 470 6478 8339 6679 714 432 1060 C
ATOM 1850 CG ASP A 470 -7.905 18.005 20.601 1.00 60.26 C
ANISOU 1850 CG ASP A 470 6694 9150 7054 739 321 1091 C
ATOM 1851 OD1 ASP A 470 -8.303 18.963 21.290 1.00 60.84 O
ANISOU 1851 OD1 ASP A 470 6704 9457 6956 613 190 1016 O
ATOM 1852 OD2 ASP A 470 -6.695 17.701 20.488 1.00 64.76 O
ANISOU 1852 OD2 ASP A 470 7115 9751 7737 887 360 1170 O
ATOM 1853 N PRO A 471 -11.278 19.928 20.250 1.00 50.77 N
ANISOU 1853 N PRO A 471 5866 7869 5556 222 202 639 N
ATOM 1854 CA PRO A 471 -11.617 21.243 19.634 1.00 47.35 C
ANISOU 1854 CA PRO A 471 5467 7449 5073 53 159 393 C
ATOM 1855 C PRO A 471 -10.404 22.017 19.134 1.00 51.51 C
ANISOU 1855 C PRO A 471 5853 8064 5654 64 167 319 C
ATOM 1856 O PRO A 471 -10.572 22.821 18.227 1.00 50.48 O
ANISOU 1856 O PRO A 471 5788 7849 5543 -47 188 160 O
ATOM 1857 CB PRO A 471 -12.406 21.985 20.721 1.00 47.36 C
ANISOU 1857 CB PRO A 471 5406 7673 4917 -58 17 339 C
ATOM 1858 CG PRO A 471 -12.034 21.303 21.991 1.00 53.88 C
ANISOU 1858 CG PRO A 471 6097 8712 5662 68 -28 559 C
ATOM 1859 CD PRO A 471 -11.642 19.888 21.683 1.00 51.43 C
ANISOU 1859 CD PRO A 471 5846 8203 5492 228 94 772 C
ATOM 1860 N LYS A 472 -9.176 21.685 19.643 1.00 48.74 N
ANISOU 1860 N LYS A 472 5310 7863 5347 207 162 456 N
ATOM 1861 CA LYS A 472 -7.890 22.286 19.255 1.00 47.38 C
ANISOU 1861 CA LYS A 472 4958 7782 5264 235 180 419 C
ATOM 1862 C LYS A 472 -7.372 21.763 17.925 1.00 52.85 C
ANISOU 1862 C LYS A 472 5742 8251 6088 314 371 419 C
ATOM 1863 O LYS A 472 -6.746 22.518 17.173 1.00 53.01 O
ANISOU 1863 O LYS A 472 5695 8280 6166 266 427 334 O
ATOM 1864 CB LYS A 472 -6.839 22.116 20.345 1.00 49.06 C
ANISOU 1864 CB LYS A 472 4913 8252 5475 360 83 556 C
ATOM 1865 CG LYS A 472 -7.190 22.849 21.637 1.00 43.63 C
ANISOU 1865 CG LYS A 472 4100 7852 4626 284 -120 506 C
ATOM 1866 CD LYS A 472 -5.980 23.095 22.536 1.00 43.82 C
ANISOU 1866 CD LYS A 472 3829 8169 4651 377 -250 562 C
ATOM 1867 CE LYS A 472 -5.159 24.285 22.095 1.00 49.50 C
ANISOU 1867 CE LYS A 472 4368 8944 5496 282 -291 391 C
ATOM 1868 NZ LYS A 472 -3.982 24.464 22.977 1.00 55.39 N
ANISOU 1868 NZ LYS A 472 4809 9970 6266 375 -436 432 N
ATOM 1869 N ALA A 473 -7.652 20.485 17.629 1.00 50.47 N
ANISOU 1869 N ALA A 473 5589 7748 5840 435 475 509 N
ATOM 1870 CA ALA A 473 -7.266 19.800 16.389 1.00 51.40 C
ANISOU 1870 CA ALA A 473 5814 7644 6069 539 660 480 C
ATOM 1871 C ALA A 473 -8.317 19.982 15.291 1.00 56.89 C
ANISOU 1871 C ALA A 473 6768 8136 6712 426 721 309 C
ATOM 1872 O ALA A 473 -7.950 19.973 14.112 1.00 58.09 O
ANISOU 1872 O ALA A 473 6991 8188 6892 464 859 222 O
ATOM 1873 CB ALA A 473 -7.062 18.321 16.653 1.00 53.97 C
ANISOU 1873 CB ALA A 473 6160 7833 6513 731 721 638 C
ATOM 1874 N ARG A 474 -9.626 20.142 15.664 1.00 51.10 N
ANISOU 1874 N ARG A 474 6167 7357 5893 296 618 259 N
ATOM 1875 CA ARG A 474 -10.736 20.374 14.725 1.00 48.56 C
ANISOU 1875 CA ARG A 474 6075 6855 5519 179 635 94 C
ATOM 1876 C ARG A 474 -10.403 21.443 13.668 1.00 51.91 C
ANISOU 1876 C ARG A 474 6514 7314 5894 97 684 -32 C
ATOM 1877 O ARG A 474 -9.701 22.404 13.979 1.00 52.39 O
ANISOU 1877 O ARG A 474 6392 7562 5953 45 642 -12 O
ATOM 1878 CB ARG A 474 -11.969 20.813 15.499 1.00 45.01 C
ANISOU 1878 CB ARG A 474 5670 6445 4986 30 491 65 C
ATOM 1879 CG ARG A 474 -13.268 20.868 14.700 1.00 38.47 C
ANISOU 1879 CG ARG A 474 5069 5418 4128 -82 481 -87 C
ATOM 1880 CD ARG A 474 -14.276 20.195 15.562 1.00 49.09 C
ANISOU 1880 CD ARG A 474 6458 6701 5493 -105 421 -17 C
ATOM 1881 NE ARG A 474 -14.802 21.057 16.612 1.00 55.91 N
ANISOU 1881 NE ARG A 474 7222 7765 6256 -227 291 -19 N
ATOM 1882 CZ ARG A 474 -15.065 20.657 17.848 1.00 64.36 C
ANISOU 1882 CZ ARG A 474 8200 8959 7296 -205 242 124 C
ATOM 1883 NH1 ARG A 474 -14.777 19.425 18.229 1.00 49.88 N
ANISOU 1883 NH1 ARG A 474 6346 7061 5544 -68 306 317 N
ATOM 1884 NH2 ARG A 474 -15.610 21.488 18.714 1.00 56.46 N
ANISOU 1884 NH2 ARG A 474 7118 8152 6181 -312 132 80 N
ATOM 1885 N PHE A 475 -10.899 21.265 12.426 1.00 47.30 N
ANISOU 1885 N PHE A 475 6140 6557 5277 88 768 -155 N
ATOM 1886 CA PHE A 475 -10.666 22.210 11.336 1.00 46.43 C
ANISOU 1886 CA PHE A 475 6067 6479 5096 20 829 -240 C
ATOM 1887 C PHE A 475 -11.347 23.561 11.616 1.00 50.40 C
ANISOU 1887 C PHE A 475 6546 7062 5542 -180 683 -292 C
ATOM 1888 O PHE A 475 -12.484 23.615 12.118 1.00 48.26 O
ANISOU 1888 O PHE A 475 6357 6739 5242 -274 557 -345 O
ATOM 1889 CB PHE A 475 -11.186 21.631 10.014 1.00 48.51 C
ANISOU 1889 CB PHE A 475 6576 6560 5297 69 928 -367 C
ATOM 1890 CG PHE A 475 -10.180 21.320 8.924 1.00 52.31 C
ANISOU 1890 CG PHE A 475 7062 7051 5761 211 1125 -382 C
ATOM 1891 CD1 PHE A 475 -8.919 20.823 9.234 1.00 56.70 C
ANISOU 1891 CD1 PHE A 475 7434 7683 6426 361 1233 -276 C
ATOM 1892 CD2 PHE A 475 -10.524 21.441 7.587 1.00 55.56 C
ANISOU 1892 CD2 PHE A 475 7664 7408 6040 214 1205 -508 C
ATOM 1893 CE1 PHE A 475 -8.004 20.517 8.230 1.00 58.47 C
ANISOU 1893 CE1 PHE A 475 7650 7927 6639 502 1433 -301 C
ATOM 1894 CE2 PHE A 475 -9.606 21.130 6.585 1.00 60.67 C
ANISOU 1894 CE2 PHE A 475 8314 8097 6642 359 1406 -530 C
ATOM 1895 CZ PHE A 475 -8.354 20.668 6.920 1.00 59.37 C
ANISOU 1895 CZ PHE A 475 7954 8004 6601 501 1527 -430 C
ATOM 1896 N THR A 476 -10.640 24.656 11.299 1.00 47.69 N
ANISOU 1896 N THR A 476 6076 6836 5209 -244 705 -274 N
ATOM 1897 CA THR A 476 -11.189 26.008 11.454 1.00 45.80 C
ANISOU 1897 CA THR A 476 5800 6642 4961 -428 572 -328 C
ATOM 1898 C THR A 476 -11.937 26.328 10.158 1.00 49.68 C
ANISOU 1898 C THR A 476 6510 7006 5359 -486 610 -404 C
ATOM 1899 O THR A 476 -11.893 25.513 9.234 1.00 50.60 O
ANISOU 1899 O THR A 476 6784 7036 5405 -378 738 -425 O
ATOM 1900 CB THR A 476 -10.055 26.986 11.734 1.00 48.26 C
ANISOU 1900 CB THR A 476 5850 7110 5377 -469 571 -263 C
ATOM 1901 OG1 THR A 476 -9.157 26.956 10.616 1.00 57.96 O
ANISOU 1901 OG1 THR A 476 7072 8336 6613 -400 760 -197 O
ATOM 1902 CG2 THR A 476 -9.301 26.655 13.014 1.00 37.10 C
ANISOU 1902 CG2 THR A 476 4213 5847 4035 -396 510 -199 C
ATOM 1903 N THR A 477 -12.614 27.488 10.070 1.00 45.98 N
ANISOU 1903 N THR A 477 6052 6528 4892 -644 494 -453 N
ATOM 1904 CA THR A 477 -13.294 27.902 8.830 1.00 46.45 C
ANISOU 1904 CA THR A 477 6307 6487 4855 -699 510 -499 C
ATOM 1905 C THR A 477 -12.250 28.155 7.714 1.00 53.12 C
ANISOU 1905 C THR A 477 7131 7391 5663 -639 695 -399 C
ATOM 1906 O THR A 477 -12.453 27.732 6.571 1.00 54.87 O
ANISOU 1906 O THR A 477 7544 7564 5742 -569 796 -425 O
ATOM 1907 CB THR A 477 -14.248 29.071 9.086 1.00 55.02 C
ANISOU 1907 CB THR A 477 7383 7539 5984 -870 332 -559 C
ATOM 1908 OG1 THR A 477 -13.579 30.060 9.862 1.00 56.49 O
ANISOU 1908 OG1 THR A 477 7318 7829 6315 -949 273 -515 O
ATOM 1909 CG2 THR A 477 -15.497 28.639 9.819 1.00 51.19 C
ANISOU 1909 CG2 THR A 477 6978 6984 5488 -909 190 -673 C
ATOM 1910 N GLU A 478 -11.086 28.731 8.080 1.00 48.21 N
ANISOU 1910 N GLU A 478 6263 6887 5168 -652 749 -291 N
ATOM 1911 CA GLU A 478 -9.961 28.968 7.159 1.00 49.01 C
ANISOU 1911 CA GLU A 478 6288 7067 5267 -596 949 -167 C
ATOM 1912 C GLU A 478 -9.389 27.653 6.572 1.00 53.25 C
ANISOU 1912 C GLU A 478 6912 7618 5703 -395 1144 -172 C
ATOM 1913 O GLU A 478 -9.132 27.554 5.353 1.00 55.45 O
ANISOU 1913 O GLU A 478 7296 7921 5851 -326 1315 -142 O
ATOM 1914 CB GLU A 478 -8.847 29.820 7.809 1.00 50.70 C
ANISOU 1914 CB GLU A 478 6183 7390 5690 -661 946 -64 C
ATOM 1915 CG GLU A 478 -9.342 31.097 8.487 1.00 68.60 C
ANISOU 1915 CG GLU A 478 8338 9629 8098 -849 739 -99 C
ATOM 1916 CD GLU A 478 -9.955 30.972 9.880 1.00 98.62 C
ANISOU 1916 CD GLU A 478 12089 13441 11942 -885 531 -229 C
ATOM 1917 OE1 GLU A 478 -9.426 30.181 10.698 1.00103.81 O
ANISOU 1917 OE1 GLU A 478 12658 14182 12604 -779 537 -231 O
ATOM 1918 OE2 GLU A 478 -10.938 31.696 10.168 1.00 90.01 O
ANISOU 1918 OE2 GLU A 478 11035 12285 10880 -1012 365 -319 O
ATOM 1919 N GLU A 479 -9.217 26.644 7.426 1.00 47.24 N
ANISOU 1919 N GLU A 479 6108 6843 4998 -293 1120 -210 N
ATOM 1920 CA GLU A 479 -8.700 25.344 6.986 1.00 47.87 C
ANISOU 1920 CA GLU A 479 6255 6899 5033 -92 1286 -231 C
ATOM 1921 C GLU A 479 -9.683 24.676 6.034 1.00 52.67 C
ANISOU 1921 C GLU A 479 7166 7376 5471 -44 1303 -371 C
ATOM 1922 O GLU A 479 -9.266 24.176 4.978 1.00 54.99 O
ANISOU 1922 O GLU A 479 7554 7683 5656 86 1480 -407 O
ATOM 1923 CB GLU A 479 -8.392 24.428 8.179 1.00 48.44 C
ANISOU 1923 CB GLU A 479 6209 6964 5232 3 1233 -212 C
ATOM 1924 CG GLU A 479 -7.207 24.888 9.006 1.00 50.08 C
ANISOU 1924 CG GLU A 479 6105 7328 5595 1 1228 -89 C
ATOM 1925 CD GLU A 479 -6.856 23.916 10.100 1.00 65.50 C
ANISOU 1925 CD GLU A 479 7950 9294 7645 123 1179 -46 C
ATOM 1926 OE1 GLU A 479 -7.714 23.679 10.977 1.00 55.91 O
ANISOU 1926 OE1 GLU A 479 6791 8035 6416 77 1020 -72 O
ATOM 1927 OE2 GLU A 479 -5.774 23.298 10.013 1.00 72.37 O
ANISOU 1927 OE2 GLU A 479 8692 10210 8597 279 1314 21 O
ATOM 1928 N ALA A 480 -10.995 24.713 6.398 1.00 46.18 N
ANISOU 1928 N ALA A 480 6482 6439 4625 -150 1116 -463 N
ATOM 1929 CA ALA A 480 -12.104 24.182 5.610 1.00 45.62 C
ANISOU 1929 CA ALA A 480 6681 6230 4421 -136 1077 -614 C
ATOM 1930 C ALA A 480 -12.132 24.859 4.228 1.00 52.67 C
ANISOU 1930 C ALA A 480 7697 7189 5128 -151 1159 -620 C
ATOM 1931 O ALA A 480 -12.050 24.161 3.231 1.00 54.42 O
ANISOU 1931 O ALA A 480 8067 7400 5210 -19 1280 -712 O
ATOM 1932 CB ALA A 480 -13.415 24.391 6.350 1.00 44.17 C
ANISOU 1932 CB ALA A 480 6557 5945 4279 -276 859 -678 C
ATOM 1933 N LEU A 481 -12.104 26.209 4.172 1.00 50.41 N
ANISOU 1933 N LEU A 481 7323 6985 4846 -295 1112 -508 N
ATOM 1934 CA LEU A 481 -12.086 26.997 2.932 1.00 51.56 C
ANISOU 1934 CA LEU A 481 7557 7207 4825 -322 1190 -446 C
ATOM 1935 C LEU A 481 -10.874 26.704 2.049 1.00 59.63 C
ANISOU 1935 C LEU A 481 8541 8368 5746 -173 1455 -372 C
ATOM 1936 O LEU A 481 -10.947 26.936 0.827 1.00 61.87 O
ANISOU 1936 O LEU A 481 8967 8730 5812 -134 1552 -357 O
ATOM 1937 CB LEU A 481 -12.185 28.504 3.238 1.00 50.54 C
ANISOU 1937 CB LEU A 481 7290 7107 4806 -509 1085 -308 C
ATOM 1938 CG LEU A 481 -13.565 29.041 3.632 1.00 51.22 C
ANISOU 1938 CG LEU A 481 7465 7072 4926 -653 839 -393 C
ATOM 1939 CD1 LEU A 481 -13.432 30.343 4.405 1.00 47.88 C
ANISOU 1939 CD1 LEU A 481 6824 6656 4711 -816 728 -296 C
ATOM 1940 CD2 LEU A 481 -14.435 29.235 2.409 1.00 52.42 C
ANISOU 1940 CD2 LEU A 481 7854 7197 4866 -658 804 -428 C
ATOM 1941 N ARG A 482 -9.770 26.166 2.659 1.00 57.34 N
ANISOU 1941 N ARG A 482 8056 8126 5603 -78 1574 -324 N
ATOM 1942 CA ARG A 482 -8.527 25.766 1.962 1.00 59.90 C
ANISOU 1942 CA ARG A 482 8303 8584 5875 84 1842 -265 C
ATOM 1943 C ARG A 482 -8.572 24.317 1.527 1.00 65.49 C
ANISOU 1943 C ARG A 482 9168 9229 6487 288 1932 -453 C
ATOM 1944 O ARG A 482 -7.722 23.905 0.743 1.00 69.78 O
ANISOU 1944 O ARG A 482 9693 9881 6939 444 2160 -455 O
ATOM 1945 CB ARG A 482 -7.273 25.961 2.828 1.00 59.48 C
ANISOU 1945 CB ARG A 482 7931 8611 6060 89 1913 -122 C
ATOM 1946 CG ARG A 482 -6.792 27.373 2.896 1.00 67.52 C
ANISOU 1946 CG ARG A 482 8748 9720 7186 -72 1912 68 C
ATOM 1947 CD ARG A 482 -5.449 27.434 3.582 1.00 84.08 C
ANISOU 1947 CD ARG A 482 10524 11910 9513 -38 2003 182 C
ATOM 1948 NE ARG A 482 -5.502 27.961 4.952 1.00100.39 N
ANISOU 1948 NE ARG A 482 12396 13941 11805 -171 1784 198 N
ATOM 1949 CZ ARG A 482 -5.753 29.231 5.281 1.00117.65 C
ANISOU 1949 CZ ARG A 482 14478 16117 14108 -366 1648 264 C
ATOM 1950 NH1 ARG A 482 -6.072 30.122 4.344 1.00104.95 N
ANISOU 1950 NH1 ARG A 482 12953 14502 12419 -463 1696 351 N
ATOM 1951 NH2 ARG A 482 -5.727 29.610 6.551 1.00102.90 N
ANISOU 1951 NH2 ARG A 482 12424 14242 12431 -458 1455 238 N
ATOM 1952 N HIS A 483 -9.523 23.535 2.052 1.00 59.15 N
ANISOU 1952 N HIS A 483 8498 8246 5729 291 1763 -610 N
ATOM 1953 CA HIS A 483 -9.673 22.127 1.706 1.00 60.61 C
ANISOU 1953 CA HIS A 483 8828 8317 5884 472 1819 -807 C
ATOM 1954 C HIS A 483 -9.868 21.909 0.201 1.00 68.01 C
ANISOU 1954 C HIS A 483 9982 9318 6539 579 1935 -954 C
ATOM 1955 O HIS A 483 -10.603 22.677 -0.431 1.00 68.28 O
ANISOU 1955 O HIS A 483 10154 9403 6388 474 1855 -953 O
ATOM 1956 CB HIS A 483 -10.839 21.504 2.492 1.00 59.77 C
ANISOU 1956 CB HIS A 483 8824 7990 5895 413 1599 -923 C
ATOM 1957 CG HIS A 483 -10.884 20.012 2.417 1.00 64.33 C
ANISOU 1957 CG HIS A 483 9490 8401 6553 588 1641 -1094 C
ATOM 1958 ND1 HIS A 483 -11.505 19.366 1.368 1.00 67.34 N
ANISOU 1958 ND1 HIS A 483 10102 8695 6787 674 1647 -1330 N
ATOM 1959 CD2 HIS A 483 -10.342 19.090 3.246 1.00 65.78 C
ANISOU 1959 CD2 HIS A 483 9546 8486 6962 694 1671 -1058 C
ATOM 1960 CE1 HIS A 483 -11.332 18.073 1.597 1.00 67.75 C
ANISOU 1960 CE1 HIS A 483 10157 8575 7010 823 1683 -1444 C
ATOM 1961 NE2 HIS A 483 -10.642 17.861 2.719 1.00 67.24 N
ANISOU 1961 NE2 HIS A 483 9882 8492 7175 840 1701 -1269 N
ATOM 1962 N PRO A 484 -9.239 20.856 -0.383 1.00 66.89 N
ANISOU 1962 N PRO A 484 9874 9183 6359 798 2115 -1093 N
ATOM 1963 CA PRO A 484 -9.424 20.577 -1.819 1.00 68.50 C
ANISOU 1963 CA PRO A 484 10289 9478 6261 923 2225 -1276 C
ATOM 1964 C PRO A 484 -10.870 20.529 -2.323 1.00 73.04 C
ANISOU 1964 C PRO A 484 11130 9949 6673 852 2016 -1465 C
ATOM 1965 O PRO A 484 -11.089 20.778 -3.504 1.00 75.44 O
ANISOU 1965 O PRO A 484 11594 10401 6669 896 2067 -1541 O
ATOM 1966 CB PRO A 484 -8.767 19.205 -1.985 1.00 71.66 C
ANISOU 1966 CB PRO A 484 10676 9803 6749 1165 2377 -1462 C
ATOM 1967 CG PRO A 484 -7.741 19.160 -0.959 1.00 75.05 C
ANISOU 1967 CG PRO A 484 10829 10230 7456 1180 2451 -1268 C
ATOM 1968 CD PRO A 484 -8.317 19.868 0.222 1.00 68.52 C
ANISOU 1968 CD PRO A 484 9919 9322 6793 956 2225 -1098 C
ATOM 1969 N TRP A 485 -11.848 20.212 -1.451 1.00 67.96 N
ANISOU 1969 N TRP A 485 10525 9071 6227 747 1785 -1532 N
ATOM 1970 CA TRP A 485 -13.252 20.124 -1.863 1.00 67.36 C
ANISOU 1970 CA TRP A 485 10671 8876 6046 672 1573 -1718 C
ATOM 1971 C TRP A 485 -13.812 21.469 -2.264 1.00 69.02 C
ANISOU 1971 C TRP A 485 10938 9224 6062 510 1474 -1585 C
ATOM 1972 O TRP A 485 -14.603 21.558 -3.192 1.00 69.81 O
ANISOU 1972 O TRP A 485 11237 9354 5932 515 1384 -1728 O
ATOM 1973 CB TRP A 485 -14.123 19.468 -0.781 1.00 64.18 C
ANISOU 1973 CB TRP A 485 10258 8195 5931 589 1373 -1785 C
ATOM 1974 CG TRP A 485 -15.508 19.089 -1.247 1.00 64.86 C
ANISOU 1974 CG TRP A 485 10557 8125 5960 545 1173 -2025 C
ATOM 1975 CD1 TRP A 485 -15.834 18.214 -2.247 1.00 70.01 C
ANISOU 1975 CD1 TRP A 485 11392 8718 6491 686 1173 -2323 C
ATOM 1976 CD2 TRP A 485 -16.750 19.524 -0.670 1.00 62.18 C
ANISOU 1976 CD2 TRP A 485 10250 7664 5713 353 934 -2009 C
ATOM 1977 NE1 TRP A 485 -17.200 18.119 -2.366 1.00 68.68 N
ANISOU 1977 NE1 TRP A 485 11364 8398 6333 584 938 -2487 N
ATOM 1978 CE2 TRP A 485 -17.791 18.915 -1.412 1.00 67.11 C
ANISOU 1978 CE2 TRP A 485 11074 8159 6268 379 795 -2290 C
ATOM 1979 CE3 TRP A 485 -17.085 20.422 0.372 1.00 60.36 C
ANISOU 1979 CE3 TRP A 485 9888 7435 5610 165 822 -1802 C
ATOM 1980 CZ2 TRP A 485 -19.147 19.148 -1.132 1.00 64.46 C
ANISOU 1980 CZ2 TRP A 485 10799 7687 6006 220 556 -2349 C
ATOM 1981 CZ3 TRP A 485 -18.421 20.664 0.639 1.00 60.38 C
ANISOU 1981 CZ3 TRP A 485 9959 7313 5668 17 600 -1868 C
ATOM 1982 CH2 TRP A 485 -19.436 20.017 -0.098 1.00 62.44 C
ANISOU 1982 CH2 TRP A 485 10408 7437 5878 43 471 -2129 C
ATOM 1983 N LEU A 486 -13.370 22.516 -1.592 1.00 63.14 N
ANISOU 1983 N LEU A 486 10008 8563 5418 376 1487 -1317 N
ATOM 1984 CA LEU A 486 -13.811 23.881 -1.874 1.00 61.09 C
ANISOU 1984 CA LEU A 486 9765 8406 5043 216 1396 -1156 C
ATOM 1985 C LEU A 486 -12.951 24.598 -2.944 1.00 63.37 C
ANISOU 1985 C LEU A 486 10038 8951 5088 275 1609 -995 C
ATOM 1986 O LEU A 486 -13.284 25.708 -3.361 1.00 60.78 O
ANISOU 1986 O LEU A 486 9734 8710 4650 161 1553 -838 O
ATOM 1987 CB LEU A 486 -13.929 24.671 -0.553 1.00 57.83 C
ANISOU 1987 CB LEU A 486 9159 7916 4898 27 1263 -985 C
ATOM 1988 CG LEU A 486 -15.018 24.123 0.319 1.00 58.72 C
ANISOU 1988 CG LEU A 486 9320 7814 5178 -44 1047 -1128 C
ATOM 1989 CD1 LEU A 486 -14.558 23.937 1.664 1.00 56.78 C
ANISOU 1989 CD1 LEU A 486 8869 7512 5191 -78 1041 -1039 C
ATOM 1990 CD2 LEU A 486 -16.275 24.901 0.198 1.00 58.03 C
ANISOU 1990 CD2 LEU A 486 9335 7672 5043 -196 830 -1152 C
ATOM 1991 N GLN A 487 -11.881 23.937 -3.417 1.00 62.60 N
ANISOU 1991 N GLN A 487 9902 8972 4912 460 1858 -1030 N
ATOM 1992 CA GLN A 487 -11.017 24.479 -4.476 1.00 65.85 C
ANISOU 1992 CA GLN A 487 10292 9652 5077 539 2102 -878 C
ATOM 1993 C GLN A 487 -11.685 24.183 -5.822 1.00 71.89 C
ANISOU 1993 C GLN A 487 11335 10528 5453 649 2091 -1063 C
ATOM 1994 O GLN A 487 -11.180 23.398 -6.604 1.00 72.79 O
ANISOU 1994 O GLN A 487 11521 10765 5370 851 2275 -1220 O
ATOM 1995 CB GLN A 487 -9.565 23.931 -4.383 1.00 68.72 C
ANISOU 1995 CB GLN A 487 10465 10115 5532 695 2384 -836 C
ATOM 1996 CG GLN A 487 -8.840 24.213 -3.048 1.00 75.07 C
ANISOU 1996 CG GLN A 487 10978 10837 6710 597 2378 -656 C
ATOM 1997 CD GLN A 487 -9.141 25.574 -2.461 1.00 85.59 C
ANISOU 1997 CD GLN A 487 12194 12152 8174 359 2231 -423 C
ATOM 1998 OE1 GLN A 487 -8.817 26.617 -3.040 1.00 75.83 O
ANISOU 1998 OE1 GLN A 487 10905 11066 6839 289 2327 -209 O
ATOM 1999 NE2 GLN A 487 -9.818 25.585 -1.315 1.00 79.32 N
ANISOU 1999 NE2 GLN A 487 11360 11169 7609 232 1994 -463 N
ATOM 2000 N ASP A 488 -12.876 24.790 -6.034 1.00 70.45 N
ANISOU 2000 N ASP A 488 11302 10294 5173 519 1853 -1066 N
ATOM 2001 CA ASP A 488 -13.791 24.611 -7.166 1.00 72.95 C
ANISOU 2001 CA ASP A 488 11886 10689 5140 588 1747 -1251 C
ATOM 2002 C ASP A 488 -14.119 25.970 -7.771 1.00 78.78 C
ANISOU 2002 C ASP A 488 12663 11583 5687 471 1696 -980 C
ATOM 2003 O ASP A 488 -14.977 26.696 -7.261 1.00 74.61 O
ANISOU 2003 O ASP A 488 12125 10911 5311 292 1462 -894 O
ATOM 2004 CB ASP A 488 -15.073 23.892 -6.671 1.00 73.09 C
ANISOU 2004 CB ASP A 488 12031 10434 5305 540 1455 -1539 C
ATOM 2005 CG ASP A 488 -16.068 23.471 -7.739 1.00 82.08 C
ANISOU 2005 CG ASP A 488 13436 11614 6137 624 1306 -1809 C
ATOM 2006 OD1 ASP A 488 -16.315 24.272 -8.669 1.00 85.99 O
ANISOU 2006 OD1 ASP A 488 14038 12316 6320 616 1286 -1690 O
ATOM 2007 OD2 ASP A 488 -16.680 22.379 -7.589 1.00 79.38 O
ANISOU 2007 OD2 ASP A 488 13187 11079 5894 683 1181 -2131 O
ATOM 2008 N GLU A 489 -13.432 26.299 -8.879 1.00 81.80 N
ANISOU 2008 N GLU A 489 13084 12263 5734 584 1923 -841 N
ATOM 2009 CA GLU A 489 -13.592 27.574 -9.569 1.00 83.28 C
ANISOU 2009 CA GLU A 489 13298 12624 5721 497 1919 -529 C
ATOM 2010 C GLU A 489 -14.954 27.830 -10.184 1.00 87.18 C
ANISOU 2010 C GLU A 489 14026 13111 5990 464 1640 -623 C
ATOM 2011 O GLU A 489 -15.388 28.989 -10.232 1.00 86.20 O
ANISOU 2011 O GLU A 489 13879 12982 5893 318 1522 -355 O
ATOM 2012 CB GLU A 489 -12.413 27.885 -10.490 1.00 88.50 C
ANISOU 2012 CB GLU A 489 13898 13613 6113 618 2269 -297 C
ATOM 2013 CG GLU A 489 -11.213 28.449 -9.727 1.00101.22 C
ANISOU 2013 CG GLU A 489 15196 15202 8063 527 2475 -8 C
ATOM 2014 CD GLU A 489 -11.480 29.564 -8.721 1.00118.83 C
ANISOU 2014 CD GLU A 489 17248 17216 10684 272 2296 233 C
ATOM 2015 OE1 GLU A 489 -12.191 30.536 -9.072 1.00101.79 O
ANISOU 2015 OE1 GLU A 489 15162 15058 8457 156 2145 413 O
ATOM 2016 OE2 GLU A 489 -10.984 29.457 -7.575 1.00112.28 O
ANISOU 2016 OE2 GLU A 489 16204 16222 10234 198 2297 230 O
ATOM 2017 N ASP A 490 -15.653 26.739 -10.577 1.00 83.54 N
ANISOU 2017 N ASP A 490 13769 12615 5358 592 1513 -1016 N
ATOM 2018 CA ASP A 490 -17.014 26.747 -11.111 1.00 82.79 C
ANISOU 2018 CA ASP A 490 13892 12489 5073 578 1213 -1192 C
ATOM 2019 C ASP A 490 -18.006 27.181 -10.019 1.00 81.84 C
ANISOU 2019 C ASP A 490 13700 12053 5343 359 918 -1173 C
ATOM 2020 O ASP A 490 -18.777 28.125 -10.230 1.00 81.28 O
ANISOU 2020 O ASP A 490 13670 11983 5229 248 733 -1009 O
ATOM 2021 CB ASP A 490 -17.387 25.345 -11.622 1.00 85.86 C
ANISOU 2021 CB ASP A 490 14466 12870 5288 763 1159 -1661 C
ATOM 2022 CG ASP A 490 -17.077 25.080 -13.081 1.00 95.59 C
ANISOU 2022 CG ASP A 490 15878 14463 5978 986 1302 -1765 C
ATOM 2023 OD1 ASP A 490 -16.138 25.718 -13.617 1.00 98.72 O
ANISOU 2023 OD1 ASP A 490 16214 15142 6154 1039 1572 -1464 O
ATOM 2024 OD2 ASP A 490 -17.748 24.206 -13.679 1.00 96.91 O
ANISOU 2024 OD2 ASP A 490 16237 14637 5947 1111 1152 -2158 O
ATOM 2025 N MET A 491 -17.967 26.496 -8.844 1.00 73.56 N
ANISOU 2025 N MET A 491 12534 10742 4673 306 884 -1330 N
ATOM 2026 CA MET A 491 -18.838 26.767 -7.706 1.00 68.15 C
ANISOU 2026 CA MET A 491 11763 9774 4358 117 640 -1340 C
ATOM 2027 C MET A 491 -18.659 28.220 -7.261 1.00 72.25 C
ANISOU 2027 C MET A 491 12117 10298 5037 -57 632 -971 C
ATOM 2028 O MET A 491 -19.654 28.917 -7.068 1.00 71.88 O
ANISOU 2028 O MET A 491 12085 10138 5088 -190 394 -928 O
ATOM 2029 CB MET A 491 -18.589 25.741 -6.581 1.00 67.51 C
ANISOU 2029 CB MET A 491 11570 9473 4609 120 672 -1517 C
ATOM 2030 CG MET A 491 -19.287 26.052 -5.233 1.00 66.03 C
ANISOU 2030 CG MET A 491 11246 9033 4810 -74 479 -1478 C
ATOM 2031 SD MET A 491 -18.522 27.392 -4.269 1.00 66.45 S
ANISOU 2031 SD MET A 491 11029 9106 5112 -237 563 -1103 S
ATOM 2032 CE MET A 491 -16.945 26.626 -3.775 1.00 62.76 C
ANISOU 2032 CE MET A 491 10397 8693 4757 -117 861 -1072 C
ATOM 2033 N LYS A 492 -17.395 28.681 -7.141 1.00 69.34 N
ANISOU 2033 N LYS A 492 11581 10051 4713 -51 889 -715 N
ATOM 2034 CA LYS A 492 -17.047 30.056 -6.761 1.00 67.80 C
ANISOU 2034 CA LYS A 492 11202 9854 4705 -210 908 -365 C
ATOM 2035 C LYS A 492 -17.629 31.086 -7.730 1.00 74.34 C
ANISOU 2035 C LYS A 492 12141 10794 5312 -248 809 -161 C
ATOM 2036 O LYS A 492 -18.215 32.068 -7.272 1.00 73.00 O
ANISOU 2036 O LYS A 492 11893 10483 5362 -410 628 -20 O
ATOM 2037 CB LYS A 492 -15.531 30.222 -6.562 1.00 69.34 C
ANISOU 2037 CB LYS A 492 11189 10166 4991 -181 1213 -156 C
ATOM 2038 CG LYS A 492 -15.064 29.667 -5.219 1.00 72.63 C
ANISOU 2038 CG LYS A 492 11417 10418 5761 -218 1231 -258 C
ATOM 2039 CD LYS A 492 -13.558 29.506 -5.178 1.00 89.83 C
ANISOU 2039 CD LYS A 492 13412 12734 7986 -140 1535 -117 C
ATOM 2040 CE LYS A 492 -13.027 29.010 -3.847 1.00 94.78 C
ANISOU 2040 CE LYS A 492 13838 13223 8950 -165 1544 -190 C
ATOM 2041 NZ LYS A 492 -11.567 28.703 -3.918 1.00 97.55 N
ANISOU 2041 NZ LYS A 492 14018 13719 9326 -56 1839 -86 N
ATOM 2042 N ARG A 493 -17.556 30.808 -9.058 1.00 74.73 N
ANISOU 2042 N ARG A 493 12382 11094 4919 -87 906 -172 N
ATOM 2043 CA ARG A 493 -18.097 31.651 -10.133 1.00 76.72 C
ANISOU 2043 CA ARG A 493 12768 11504 4878 -83 819 30 C
ATOM 2044 C ARG A 493 -19.607 31.835 -9.957 1.00 79.57 C
ANISOU 2044 C ARG A 493 13238 11679 5317 -173 448 -120 C
ATOM 2045 O ARG A 493 -20.062 32.973 -9.868 1.00 78.35 O
ANISOU 2045 O ARG A 493 13022 11447 5299 -304 308 123 O
ATOM 2046 CB ARG A 493 -17.778 31.048 -11.505 1.00 80.97 C
ANISOU 2046 CB ARG A 493 13506 12372 4887 137 982 -40 C
ATOM 2047 CG ARG A 493 -17.410 32.082 -12.562 1.00 95.72 C
ANISOU 2047 CG ARG A 493 15393 14515 6463 161 1122 371 C
ATOM 2048 CD ARG A 493 -17.013 31.455 -13.895 1.00108.51 C
ANISOU 2048 CD ARG A 493 17200 16512 7516 398 1317 295 C
ATOM 2049 NE ARG A 493 -15.759 30.686 -13.851 1.00113.58 N
ANISOU 2049 NE ARG A 493 17748 17275 8131 525 1655 207 N
ATOM 2050 CZ ARG A 493 -15.686 29.355 -13.887 1.00125.55 C
ANISOU 2050 CZ ARG A 493 19360 18795 9546 683 1688 -218 C
ATOM 2051 NH1 ARG A 493 -16.792 28.621 -13.957 1.00113.47 N
ANISOU 2051 NH1 ARG A 493 18018 17149 7944 723 1404 -600 N
ATOM 2052 NH2 ARG A 493 -14.506 28.748 -13.849 1.00107.74 N
ANISOU 2052 NH2 ARG A 493 16997 16645 7295 801 2002 -266 N
ATOM 2053 N LYS A 494 -20.366 30.716 -9.811 1.00 76.56 N
ANISOU 2053 N LYS A 494 12985 11192 4913 -112 289 -521 N
ATOM 2054 CA LYS A 494 -21.821 30.695 -9.590 1.00 75.55 C
ANISOU 2054 CA LYS A 494 12941 10874 4889 -191 -58 -717 C
ATOM 2055 C LYS A 494 -22.236 31.549 -8.388 1.00 79.76 C
ANISOU 2055 C LYS A 494 13279 11149 5876 -400 -200 -586 C
ATOM 2056 O LYS A 494 -23.242 32.246 -8.484 1.00 81.69 O
ANISOU 2056 O LYS A 494 13553 11312 6174 -484 -444 -536 O
ATOM 2057 CB LYS A 494 -22.335 29.258 -9.410 1.00 76.98 C
ANISOU 2057 CB LYS A 494 13226 10940 5082 -109 -148 -1158 C
ATOM 2058 CG LYS A 494 -23.834 29.098 -9.659 1.00 86.80 C
ANISOU 2058 CG LYS A 494 14606 12074 6300 -137 -490 -1390 C
ATOM 2059 N PHE A 495 -21.464 31.519 -7.285 1.00 73.01 N
ANISOU 2059 N PHE A 495 12221 10182 5338 -474 -56 -537 N
ATOM 2060 CA PHE A 495 -21.756 32.317 -6.097 1.00 70.87 C
ANISOU 2060 CA PHE A 495 11751 9696 5480 -659 -174 -443 C
ATOM 2061 C PHE A 495 -21.588 33.824 -6.387 1.00 75.61 C
ANISOU 2061 C PHE A 495 12258 10329 6142 -754 -183 -81 C
ATOM 2062 O PHE A 495 -22.458 34.625 -6.025 1.00 73.20 O
ANISOU 2062 O PHE A 495 11902 9867 6044 -874 -407 -42 O
ATOM 2063 CB PHE A 495 -20.872 31.858 -4.919 1.00 71.11 C
ANISOU 2063 CB PHE A 495 11592 9648 5780 -688 -12 -485 C
ATOM 2064 CG PHE A 495 -20.731 32.843 -3.785 1.00 70.62 C
ANISOU 2064 CG PHE A 495 11291 9446 6095 -857 -62 -337 C
ATOM 2065 CD1 PHE A 495 -21.764 33.031 -2.875 1.00 71.71 C
ANISOU 2065 CD1 PHE A 495 11374 9389 6484 -973 -294 -474 C
ATOM 2066 CD2 PHE A 495 -19.565 33.584 -3.629 1.00 73.31 C
ANISOU 2066 CD2 PHE A 495 11448 9855 6550 -897 124 -78 C
ATOM 2067 CE1 PHE A 495 -21.633 33.943 -1.821 1.00 71.21 C
ANISOU 2067 CE1 PHE A 495 11088 9214 6756 -1115 -344 -378 C
ATOM 2068 CE2 PHE A 495 -19.441 34.508 -2.591 1.00 74.83 C
ANISOU 2068 CE2 PHE A 495 11413 9915 7104 -1050 56 19 C
ATOM 2069 CZ PHE A 495 -20.474 34.677 -1.689 1.00 71.17 C
ANISOU 2069 CZ PHE A 495 10908 9271 6862 -1152 -179 -144 C
ATOM 2070 N GLN A 496 -20.469 34.194 -7.062 1.00 74.11 N
ANISOU 2070 N GLN A 496 12035 10335 5788 -697 66 189 N
ATOM 2071 CA GLN A 496 -20.144 35.565 -7.459 1.00 74.39 C
ANISOU 2071 CA GLN A 496 11974 10407 5882 -778 104 580 C
ATOM 2072 C GLN A 496 -21.210 36.123 -8.374 1.00 79.97 C
ANISOU 2072 C GLN A 496 12847 11146 6390 -765 -114 667 C
ATOM 2073 O GLN A 496 -21.492 37.322 -8.322 1.00 80.46 O
ANISOU 2073 O GLN A 496 12814 11102 6656 -879 -223 920 O
ATOM 2074 CB GLN A 496 -18.785 35.619 -8.164 1.00 77.87 C
ANISOU 2074 CB GLN A 496 12374 11090 6123 -690 439 834 C
ATOM 2075 CG GLN A 496 -17.596 35.565 -7.221 1.00 87.53 C
ANISOU 2075 CG GLN A 496 13348 12261 7647 -745 646 878 C
ATOM 2076 CD GLN A 496 -17.594 36.674 -6.191 1.00102.03 C
ANISOU 2076 CD GLN A 496 14940 13865 9960 -943 531 1012 C
ATOM 2077 OE1 GLN A 496 -17.849 37.845 -6.493 1.00103.59 O
ANISOU 2077 OE1 GLN A 496 15087 14000 10273 -1039 444 1273 O
ATOM 2078 NE2 GLN A 496 -17.304 36.324 -4.948 1.00 83.59 N
ANISOU 2078 NE2 GLN A 496 12445 11399 7918 -1001 520 830 N
ATOM 2079 N ASP A 497 -21.801 35.238 -9.201 1.00 77.50 N
ANISOU 2079 N ASP A 497 12777 10972 5698 -622 -190 443 N
ATOM 2080 CA ASP A 497 -22.858 35.529 -10.160 1.00 79.80 C
ANISOU 2080 CA ASP A 497 13257 11338 5727 -574 -421 463 C
ATOM 2081 C ASP A 497 -24.184 35.805 -9.461 1.00 84.03 C
ANISOU 2081 C ASP A 497 13760 11602 6565 -693 -758 297 C
ATOM 2082 O ASP A 497 -24.894 36.736 -9.852 1.00 85.78 O
ANISOU 2082 O ASP A 497 13998 11785 6808 -738 -951 482 O
ATOM 2083 CB ASP A 497 -23.004 34.368 -11.157 1.00 83.35 C
ANISOU 2083 CB ASP A 497 13953 12022 5693 -376 -398 204 C
ATOM 2084 CG ASP A 497 -21.884 34.235 -12.181 1.00 90.99 C
ANISOU 2084 CG ASP A 497 14992 13328 6252 -224 -88 389 C
ATOM 2085 OD1 ASP A 497 -20.960 35.106 -12.186 1.00 90.40 O
ANISOU 2085 OD1 ASP A 497 14768 13313 6269 -279 127 773 O
ATOM 2086 OD2 ASP A 497 -21.914 33.254 -12.966 1.00 96.04 O
ANISOU 2086 OD2 ASP A 497 15824 14172 6496 -48 -51 139 O
ATOM 2087 N LEU A 498 -24.514 35.004 -8.426 1.00 78.13 N
ANISOU 2087 N LEU A 498 12956 10670 6059 -739 -822 -33 N
ATOM 2088 CA LEU A 498 -25.734 35.153 -7.618 1.00 75.48 C
ANISOU 2088 CA LEU A 498 12561 10083 6034 -854 -1105 -218 C
ATOM 2089 C LEU A 498 -25.668 36.451 -6.807 1.00 79.13 C
ANISOU 2089 C LEU A 498 12798 10368 6898 -1014 -1147 14 C
ATOM 2090 O LEU A 498 -26.697 37.108 -6.592 1.00 78.58 O
ANISOU 2090 O LEU A 498 12691 10143 7022 -1093 -1395 6 O
ATOM 2091 CB LEU A 498 -25.909 33.958 -6.655 1.00 72.32 C
ANISOU 2091 CB LEU A 498 12130 9553 5795 -863 -1100 -573 C
ATOM 2092 CG LEU A 498 -26.082 32.580 -7.278 1.00 76.80 C
ANISOU 2092 CG LEU A 498 12894 10220 6068 -717 -1090 -868 C
ATOM 2093 CD1 LEU A 498 -25.762 31.489 -6.266 1.00 74.37 C
ANISOU 2093 CD1 LEU A 498 12509 9789 5961 -724 -981 -1103 C
ATOM 2094 CD2 LEU A 498 -27.457 32.413 -7.899 1.00 77.80 C
ANISOU 2094 CD2 LEU A 498 13170 10319 6072 -692 -1391 -1056 C
ATOM 2095 N LEU A 499 -24.444 36.798 -6.362 1.00 75.12 N
ANISOU 2095 N LEU A 499 12130 9881 6530 -1056 -907 201 N
ATOM 2096 CA LEU A 499 -24.121 37.977 -5.585 1.00 74.56 C
ANISOU 2096 CA LEU A 499 11823 9653 6855 -1202 -907 404 C
ATOM 2097 C LEU A 499 -24.404 39.230 -6.400 1.00 84.32 C
ANISOU 2097 C LEU A 499 13066 10884 8088 -1230 -1005 737 C
ATOM 2098 O LEU A 499 -25.205 40.060 -5.969 1.00 84.14 O
ANISOU 2098 O LEU A 499 12949 10660 8360 -1329 -1223 751 O
ATOM 2099 CB LEU A 499 -22.637 37.933 -5.195 1.00 74.47 C
ANISOU 2099 CB LEU A 499 11658 9715 6922 -1211 -614 533 C
ATOM 2100 CG LEU A 499 -22.295 37.798 -3.729 1.00 76.50 C
ANISOU 2100 CG LEU A 499 11706 9830 7529 -1304 -589 369 C
ATOM 2101 CD1 LEU A 499 -20.792 37.911 -3.532 1.00 76.79 C
ANISOU 2101 CD1 LEU A 499 11581 9958 7636 -1307 -317 548 C
ATOM 2102 CD2 LEU A 499 -23.012 38.853 -2.888 1.00 78.83 C
ANISOU 2102 CD2 LEU A 499 11836 9896 8219 -1451 -808 357 C
ATOM 2103 N SER A 500 -23.774 39.358 -7.589 1.00 85.39 N
ANISOU 2103 N SER A 500 13312 11246 7888 -1135 -844 1011 N
ATOM 2104 CA SER A 500 -23.966 40.513 -8.470 1.00 89.06 C
ANISOU 2104 CA SER A 500 13792 11733 8312 -1147 -913 1391 C
ATOM 2105 C SER A 500 -25.400 40.641 -8.974 1.00 94.99 C
ANISOU 2105 C SER A 500 14697 12442 8955 -1112 -1236 1305 C
ATOM 2106 O SER A 500 -25.842 41.759 -9.241 1.00 96.52 O
ANISOU 2106 O SER A 500 14837 12530 9306 -1166 -1383 1571 O
ATOM 2107 CB SER A 500 -22.954 40.532 -9.614 1.00 96.51 C
ANISOU 2107 CB SER A 500 14819 12970 8882 -1041 -641 1711 C
ATOM 2108 OG SER A 500 -22.800 39.262 -10.225 1.00108.87 O
ANISOU 2108 OG SER A 500 16594 14790 9981 -875 -537 1487 O
ATOM 2109 N GLU A 501 -26.135 39.508 -9.060 1.00 91.33 N
ANISOU 2109 N GLU A 501 14399 12034 8267 -1028 -1357 932 N
ATOM 2110 CA GLU A 501 -27.546 39.467 -9.440 1.00 92.09 C
ANISOU 2110 CA GLU A 501 14621 12082 8286 -997 -1682 780 C
ATOM 2111 C GLU A 501 -28.366 40.155 -8.330 1.00 96.67 C
ANISOU 2111 C GLU A 501 15008 12338 9383 -1148 -1898 690 C
ATOM 2112 O GLU A 501 -29.203 41.002 -8.647 1.00 98.14 O
ANISOU 2112 O GLU A 501 15183 12428 9677 -1171 -2127 829 O
ATOM 2113 CB GLU A 501 -28.013 38.020 -9.665 1.00 92.81 C
ANISOU 2113 CB GLU A 501 14895 12280 8089 -889 -1735 371 C
ATOM 2114 N GLU A 502 -28.077 39.832 -7.034 1.00 91.56 N
ANISOU 2114 N GLU A 502 14198 11539 9052 -1241 -1815 473 N
ATOM 2115 CA GLU A 502 -28.705 40.422 -5.837 1.00 89.94 C
ANISOU 2115 CA GLU A 502 13788 11060 9326 -1376 -1972 350 C
ATOM 2116 C GLU A 502 -28.324 41.917 -5.751 1.00 97.43 C
ANISOU 2116 C GLU A 502 14559 11875 10586 -1468 -1973 692 C
ATOM 2117 O GLU A 502 -29.196 42.776 -5.577 1.00 97.85 O
ANISOU 2117 O GLU A 502 14531 11743 10906 -1523 -2202 725 O
ATOM 2118 CB GLU A 502 -28.243 39.675 -4.553 1.00 88.19 C
ANISOU 2118 CB GLU A 502 13443 10781 9283 -1430 -1830 88 C
ATOM 2119 CG GLU A 502 -28.660 40.326 -3.232 1.00 99.11 C
ANISOU 2119 CG GLU A 502 14592 11933 11134 -1563 -1937 -30 C
ATOM 2120 CD GLU A 502 -27.790 40.088 -1.999 1.00123.13 C
ANISOU 2120 CD GLU A 502 17457 14951 14374 -1626 -1757 -133 C
ATOM 2121 OE1 GLU A 502 -26.563 40.330 -2.079 1.00128.54 O
ANISOU 2121 OE1 GLU A 502 18082 15717 15040 -1627 -1548 64 O
ATOM 2122 OE2 GLU A 502 -28.345 39.737 -0.929 1.00 93.61 O
ANISOU 2122 OE2 GLU A 502 13624 11119 10826 -1676 -1829 -396 O
ATOM 2123 N ASN A 503 -27.015 42.207 -5.900 1.00 95.38 N
ANISOU 2123 N ASN A 503 14229 11701 10309 -1480 -1715 946 N
ATOM 2124 CA ASN A 503 -26.429 43.540 -5.807 1.00 96.53 C
ANISOU 2124 CA ASN A 503 14184 11714 10780 -1575 -1669 1283 C
ATOM 2125 C ASN A 503 -26.756 44.505 -6.957 1.00103.92 C
ANISOU 2125 C ASN A 503 15188 12656 11639 -1544 -1774 1670 C
ATOM 2126 O ASN A 503 -26.565 45.710 -6.783 1.00104.69 O
ANISOU 2126 O ASN A 503 15105 12561 12110 -1639 -1805 1926 O
ATOM 2127 CB ASN A 503 -24.921 43.450 -5.530 1.00 97.27 C
ANISOU 2127 CB ASN A 503 14158 11896 10905 -1603 -1357 1411 C
ATOM 2128 CG ASN A 503 -24.562 42.825 -4.195 1.00117.39 C
ANISOU 2128 CG ASN A 503 16570 14384 13648 -1657 -1289 1083 C
ATOM 2129 OD1 ASN A 503 -25.237 43.015 -3.175 1.00106.01 O
ANISOU 2129 OD1 ASN A 503 15010 12757 12511 -1734 -1459 843 O
ATOM 2130 ND2 ASN A 503 -23.456 42.101 -4.157 1.00113.13 N
ANISOU 2130 ND2 ASN A 503 16033 14014 12938 -1611 -1033 1078 N
ATOM 2131 N GLU A 504 -27.273 43.993 -8.108 1.00102.43 N
ANISOU 2131 N GLU A 504 15251 12681 10986 -1410 -1844 1709 N
ATOM 2132 CA GLU A 504 -27.668 44.782 -9.292 1.00105.82 C
ANISOU 2132 CA GLU A 504 15780 13173 11254 -1351 -1963 2083 C
ATOM 2133 C GLU A 504 -28.698 45.876 -8.954 1.00110.60 C
ANISOU 2133 C GLU A 504 16255 13475 12292 -1430 -2265 2135 C
ATOM 2134 O GLU A 504 -28.684 46.942 -9.569 1.00112.93 O
ANISOU 2134 O GLU A 504 16511 13708 12690 -1439 -2319 2542 O
ATOM 2135 CB GLU A 504 -28.205 43.874 -10.412 1.00108.68 C
ANISOU 2135 CB GLU A 504 16434 13830 11029 -1182 -2036 1992 C
ATOM 2136 N SER A 505 -29.563 45.608 -7.956 1.00104.97 N
ANISOU 2136 N SER A 505 15462 12572 11850 -1486 -2448 1735 N
ATOM 2137 CA SER A 505 -30.599 46.508 -7.439 1.00104.21 C
ANISOU 2137 CA SER A 505 15217 12178 12199 -1556 -2729 1679 C
ATOM 2138 C SER A 505 -29.991 47.702 -6.656 1.00105.92 C
ANISOU 2138 C SER A 505 15155 12123 12967 -1693 -2669 1850 C
ATOM 2139 O SER A 505 -30.326 48.855 -6.948 1.00107.54 O
ANISOU 2139 O SER A 505 15267 12136 13458 -1721 -2820 2120 O
ATOM 2140 CB SER A 505 -31.570 45.726 -6.552 1.00105.13 C
ANISOU 2140 CB SER A 505 15319 12218 12408 -1572 -2878 1181 C
ATOM 2141 N THR A 506 -29.100 47.408 -5.670 1.00 98.25 N
ANISOU 2141 N THR A 506 14044 11130 12156 -1772 -2463 1684 N
ATOM 2142 CA THR A 506 -28.408 48.373 -4.804 1.00 96.65 C
ANISOU 2142 CA THR A 506 13563 10692 12467 -1904 -2395 1758 C
ATOM 2143 C THR A 506 -27.415 49.280 -5.555 1.00101.38 C
ANISOU 2143 C THR A 506 14097 11277 13146 -1934 -2241 2267 C
ATOM 2144 O THR A 506 -27.093 50.364 -5.062 1.00102.23 O
ANISOU 2144 O THR A 506 13966 11119 13757 -2044 -2268 2395 O
ATOM 2145 CB THR A 506 -27.680 47.620 -3.681 1.00 99.15 C
ANISOU 2145 CB THR A 506 13781 11066 12824 -1953 -2217 1439 C
ATOM 2146 N ALA A 507 -26.936 48.824 -6.733 1.00 97.36 N
ANISOU 2146 N ALA A 507 13789 11055 12148 -1836 -2075 2545 N
ATOM 2147 CA ALA A 507 -25.939 49.448 -7.608 1.00 99.31 C
ANISOU 2147 CA ALA A 507 14012 11381 12340 -1841 -1869 3058 C
ATOM 2148 C ALA A 507 -26.054 50.950 -7.893 1.00103.75 C
ANISOU 2148 C ALA A 507 14411 11664 13345 -1918 -1985 3470 C
ATOM 2149 O ALA A 507 -26.945 51.393 -8.622 1.00105.44 O
ANISOU 2149 O ALA A 507 14726 11841 13496 -1856 -2194 3657 O
ATOM 2150 CB ALA A 507 -25.816 48.664 -8.906 1.00102.11 C
ANISOU 2150 CB ALA A 507 14654 12117 12026 -1685 -1752 3234 C
ATOM 2151 N LEU A 508 -25.113 51.721 -7.326 1.00 99.04 N
ANISOU 2151 N LEU A 508 13550 10865 13217 -2052 -1852 3612 N
ATOM 2152 CA LEU A 508 -24.973 53.172 -7.517 1.00101.10 C
ANISOU 2152 CA LEU A 508 13607 10818 13990 -2148 -1917 4023 C
ATOM 2153 CB LEU A 508 -24.638 53.881 -6.185 1.00109.20 C
ANISOU 2153 CB LEU A 508 14302 11484 15704 -2308 -1966 3788 C
ATOM 2154 CG LEU A 508 -25.829 53.966 -5.240 1.00104.52 C
ANISOU 2154 CG LEU A 508 13658 10674 15382 -2317 -2270 3320 C
ATOM 2155 C LEU A 508 -23.884 53.397 -8.588 1.00105.30 C
ANISOU 2155 C LEU A 508 14165 11541 14305 -2134 -1628 4588 C
ATOM 2156 O LEU A 508 -22.966 52.572 -8.666 1.00103.95 O
ANISOU 2156 O LEU A 508 14047 11646 13804 -2105 -1354 4546 O
ATOM 2157 N PRO A 509 -23.969 54.458 -9.438 1.00104.27 N
ANISOU 2157 N PRO A 509 13998 11285 14336 -2144 -1672 5130 N
ATOM 2158 CA PRO A 509 -22.947 54.654 -10.490 1.00107.10 C
ANISOU 2158 CA PRO A 509 14378 11859 14457 -2126 -1371 5703 C
ATOM 2159 C PRO A 509 -21.521 54.770 -9.984 1.00109.55 C
ANISOU 2159 C PRO A 509 14444 12129 15052 -2254 -1069 5771 C
ATOM 2160 O PRO A 509 -21.278 55.284 -8.889 1.00107.14 O
ANISOU 2160 O PRO A 509 13868 11491 15350 -2399 -1136 5547 O
ATOM 2161 CB PRO A 509 -23.409 55.907 -11.226 1.00113.13 C
ANISOU 2161 CB PRO A 509 15087 12397 15501 -2141 -1521 6243 C
ATOM 2162 CG PRO A 509 -24.333 56.574 -10.297 1.00116.23 C
ANISOU 2162 CG PRO A 509 15319 12354 16489 -2219 -1858 5939 C
ATOM 2163 CD PRO A 509 -25.004 55.508 -9.513 1.00107.28 C
ANISOU 2163 CD PRO A 509 14311 11333 15116 -2162 -1989 5271 C
ATOM 2164 N GLN A 510 -20.588 54.214 -10.760 1.00106.91 N
ANISOU 2164 N GLN A 510 14205 12160 14254 -2187 -739 6033 N
ATOM 2165 CA GLN A 510 -19.184 54.173 -10.383 1.00106.33 C
ANISOU 2165 CA GLN A 510 13912 12115 14372 -2286 -424 6103 C
ATOM 2166 C GLN A 510 -18.410 55.389 -10.828 1.00112.98 C
ANISOU 2166 C GLN A 510 14511 12767 15648 -2409 -268 6722 C
ATOM 2167 O GLN A 510 -18.779 56.029 -11.810 1.00115.90 O
ANISOU 2167 O GLN A 510 14963 13147 15928 -2366 -300 7220 O
ATOM 2168 CB GLN A 510 -18.518 52.861 -10.830 1.00106.85 C
ANISOU 2168 CB GLN A 510 14174 12663 13762 -2150 -133 5991 C
ATOM 2169 CG GLN A 510 -18.864 51.660 -9.941 1.00112.99 C
ANISOU 2169 CG GLN A 510 15064 13532 14334 -2091 -227 5319 C
ATOM 2170 CD GLN A 510 -18.340 51.767 -8.523 1.00119.67 C
ANISOU 2170 CD GLN A 510 15629 14121 15721 -2238 -245 4965 C
ATOM 2171 OE1 GLN A 510 -17.309 52.402 -8.247 1.00113.55 O
ANISOU 2171 OE1 GLN A 510 14574 13209 15360 -2366 -79 5175 O
ATOM 2172 NE2 GLN A 510 -19.044 51.132 -7.594 1.00104.70 N
ANISOU 2172 NE2 GLN A 510 13793 12166 13821 -2219 -449 4419 N
ATOM 2173 N VAL A 511 -17.331 55.698 -10.096 1.00108.79 N
ANISOU 2173 N VAL A 511 13670 12065 15600 -2562 -104 6698 N
ATOM 2174 CA VAL A 511 -16.478 56.859 -10.318 1.00112.90 C
ANISOU 2174 CA VAL A 511 13888 12342 16666 -2717 50 7232 C
ATOM 2175 C VAL A 511 -15.612 56.742 -11.578 1.00122.49 C
ANISOU 2175 C VAL A 511 15171 13921 17450 -2650 431 7828 C
ATOM 2176 O VAL A 511 -15.652 57.653 -12.419 1.00127.31 O
ANISOU 2176 O VAL A 511 15740 14441 18190 -2676 468 8434 O
ATOM 2177 CB VAL A 511 -15.668 57.229 -9.055 1.00114.71 C
ANISOU 2177 CB VAL A 511 13745 12258 17583 -2905 62 6952 C
ATOM 2178 CG1 VAL A 511 -15.410 58.729 -8.997 1.00117.72 C
ANISOU 2178 CG1 VAL A 511 13793 12170 18763 -3091 8 7364 C
ATOM 2179 CG2 VAL A 511 -16.387 56.756 -7.789 1.00109.57 C
ANISOU 2179 CG2 VAL A 511 13111 11471 17050 -2904 -229 6227 C
ATOM 2180 N LEU A 512 -14.849 55.625 -11.716 1.00117.36 N
ANISOU 2180 N LEU A 512 14621 13685 16286 -2555 715 7664 N
ATOM 2181 CA LEU A 512 -13.950 55.333 -12.848 1.00146.03 C
ANISOU 2181 CA LEU A 512 18317 17729 19440 -2468 1116 8141 C
ATOM 2182 C LEU A 512 -12.911 56.430 -13.094 1.00164.05 C
ANISOU 2182 C LEU A 512 20252 19816 22261 -2639 1358 8744 C
ATOM 2183 O LEU A 512 -11.844 56.162 -13.641 1.00131.12 O
ANISOU 2183 O LEU A 512 16014 15938 17868 -2616 1742 9039 O
ATOM 2184 CB LEU A 512 -14.734 55.034 -14.136 1.00148.34 C
ANISOU 2184 CB LEU A 512 18979 18376 19008 -2266 1094 8405 C
TER 2185 LEU A 512
HETATM 2186 C1 H3R A1513 -36.572 34.999 7.740 1.00 79.83 C
HETATM 2187 C2 H3R A1513 -35.850 35.671 8.863 1.00 78.20 C
HETATM 2188 C3 H3R A1513 -37.411 33.914 7.721 1.00 81.36 C
HETATM 2189 C7 H3R A1513 -39.219 32.808 4.570 1.00 86.46 C
HETATM 2190 C8 H3R A1513 -38.694 31.398 6.441 1.00 83.15 C
HETATM 2191 C9 H3R A1513 -40.010 31.801 4.038 1.00 85.61 C
HETATM 2192 C10 H3R A1513 -39.493 30.399 5.907 1.00 83.63 C
HETATM 2193 C11 H3R A1513 -40.154 30.601 4.709 1.00 85.21 C
HETATM 2194 C12 H3R A1513 -37.737 33.699 6.370 1.00 80.74 C
HETATM 2195 N13 H3R A1513 -37.145 34.619 5.596 1.00 78.20 N
HETATM 2196 C4 H3R A1513 -38.552 32.619 5.781 1.00 84.44 C
HETATM 2197 N3 H3R A1513 -36.437 35.400 6.466 1.00 78.97 N
HETATM 2198 N NO3 A1514 -12.647 31.763 20.980 1.00 71.37 N
HETATM 2199 O1 NO3 A1514 -13.096 31.585 22.197 1.00 68.84 O
HETATM 2200 O2 NO3 A1514 -12.881 30.915 20.148 1.00 72.11 O
HETATM 2201 O3 NO3 A1514 -12.018 32.762 20.750 1.00 72.60 O
HETATM 2202 C1 EDO A1515 -39.267 52.291 14.546 1.00 91.36 C
HETATM 2203 O1 EDO A1515 -38.542 51.504 15.486 1.00 91.59 O
HETATM 2204 C2 EDO A1515 -38.299 53.068 13.607 1.00 90.42 C
HETATM 2205 O2 EDO A1515 -39.026 53.679 12.544 1.00 88.40 O
HETATM 2206 C1 EDO A1516 -6.359 20.031 4.141 1.00 85.43 C
HETATM 2207 O1 EDO A1516 -6.929 19.013 3.338 1.00 85.07 O
HETATM 2208 C2 EDO A1516 -6.538 21.432 3.473 1.00 85.31 C
HETATM 2209 O2 EDO A1516 -6.788 22.468 4.443 1.00 83.46 O
HETATM 2210 O HOH A2001 -53.993 43.296 14.598 1.00 47.61 O
HETATM 2211 O HOH A2002 -50.049 50.081 20.825 1.00 57.07 O
HETATM 2212 O HOH A2003 -47.029 50.839 19.140 1.00 70.00 O
HETATM 2213 O HOH A2004 -50.265 54.456 13.180 1.00 46.57 O
HETATM 2214 O HOH A2005 -47.049 57.237 8.525 1.00 65.44 O
HETATM 2215 O HOH A2006 -43.248 51.770 5.920 1.00 53.69 O
HETATM 2216 O HOH A2007 -40.560 52.061 6.820 1.00 65.52 O
HETATM 2217 O HOH A2008 -38.122 47.954 6.715 1.00 57.35 O
HETATM 2218 O HOH A2009 -36.575 41.707 2.402 1.00 65.28 O
HETATM 2219 O HOH A2010 -31.944 36.603 14.202 1.00 65.17 O
HETATM 2220 O HOH A2011 -25.938 41.557 9.648 1.00 64.91 O
HETATM 2221 O HOH A2012 -27.969 44.427 9.931 1.00 68.65 O
HETATM 2222 O HOH A2013 -25.836 45.556 8.752 1.00 66.74 O
HETATM 2223 O HOH A2014 -25.239 41.007 6.935 1.00 60.45 O
HETATM 2224 O HOH A2015 -27.328 39.969 4.129 1.00 60.66 O
HETATM 2225 O HOH A2016 -37.755 45.666 1.372 1.00 82.83 O
HETATM 2226 O HOH A2017 -39.147 49.980 20.046 1.00 80.80 O
HETATM 2227 O HOH A2018 -47.613 42.570 20.889 1.00 81.81 O
HETATM 2228 O HOH A2019 -31.347 44.291 3.087 1.00 74.42 O
HETATM 2229 O HOH A2020 -35.523 36.534 -0.996 1.00 59.32 O
HETATM 2230 O HOH A2021 -37.497 25.608 1.969 1.00 74.17 O
HETATM 2231 O HOH A2022 -44.546 54.479 6.633 1.00 52.18 O
HETATM 2232 O HOH A2023 -34.441 43.342 2.072 1.00 76.16 O
HETATM 2233 O HOH A2024 -42.364 50.407 19.537 1.00 71.86 O
HETATM 2234 O HOH A2025 -13.088 29.403 12.496 1.00 60.82 O
HETATM 2235 O HOH A2026 -10.901 36.879 16.535 1.00 70.91 O
HETATM 2236 O HOH A2027 -23.048 26.253 16.250 1.00 51.63 O
HETATM 2237 O HOH A2028 -26.232 23.648 16.772 1.00 69.51 O
HETATM 2238 O HOH A2029 -34.584 29.160 14.298 1.00 68.57 O
HETATM 2239 O HOH A2030 -37.010 31.936 -8.204 1.00 76.86 O
HETATM 2240 O HOH A2031 -31.870 25.571 -10.171 1.00 68.81 O
HETATM 2241 O HOH A2032 -34.886 33.754 11.465 1.00 69.38 O
HETATM 2242 O HOH A2033 -10.635 22.862 31.165 1.00 68.32 O
HETATM 2243 O HOH A2034 -9.052 36.778 39.947 1.00 58.55 O
HETATM 2244 O HOH A2035 -2.773 28.481 44.298 1.00 51.16 O
HETATM 2245 O HOH A2036 -10.086 23.084 34.234 1.00 56.76 O
HETATM 2246 O HOH A2037 -13.844 25.327 40.331 1.00 39.88 O
HETATM 2247 O HOH A2038 -1.635 24.123 26.090 1.00 63.05 O
HETATM 2248 O HOH A2039 -27.573 8.031 12.487 1.00 67.08 O
HETATM 2249 O HOH A2040 -27.751 10.154 24.487 1.00 63.00 O
HETATM 2250 O HOH A2041 -20.163 14.292 30.808 1.00 53.48 O
HETATM 2251 O HOH A2042 -16.737 8.898 24.895 1.00 57.42 O
HETATM 2252 O HOH A2043 -17.204 6.215 12.913 1.00 56.88 O
HETATM 2253 O HOH A2044 -17.790 8.716 0.475 1.00 69.69 O
HETATM 2254 O HOH A2045 -14.922 6.033 7.493 1.00 69.17 O
HETATM 2255 O HOH A2046 -11.767 12.992 16.923 1.00 52.68 O
HETATM 2256 O HOH A2047 -5.851 15.486 18.902 1.00 62.67 O
HETATM 2257 O HOH A2048 -10.020 24.176 16.068 1.00 39.51 O
HETATM 2258 O HOH A2049 -19.360 37.631 -11.283 1.00 71.04 O
HETATM 2259 O HOH A2050 -29.299 50.553 -9.565 1.00 67.66 O
CONECT 2186 2187 2188 2197
CONECT 2187 2186
CONECT 2188 2186 2194
CONECT 2189 2191 2196
CONECT 2190 2192 2196
CONECT 2191 2189 2193
CONECT 2192 2190 2193
CONECT 2193 2191 2192
CONECT 2194 2188 2195 2196
CONECT 2195 2194 2197
CONECT 2196 2189 2190 2194
CONECT 2197 2186 2195
CONECT 2198 2199 2200 2201
CONECT 2199 2198
CONECT 2200 2198
CONECT 2201 2198
CONECT 2202 2203 2204
CONECT 2203 2202
CONECT 2204 2202 2205
CONECT 2205 2204
CONECT 2206 2207 2208
CONECT 2207 2206
CONECT 2208 2206 2209
CONECT 2209 2208
MASTER 523 0 4 14 10 0 5 6 2258 1 24 26
END
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