HEADER MEMBRANE PROTEIN 05-JAN-18 6C1Q
TITLE CRYSTAL STRUCTURE OF HUMAN C5A RECEPTOR IN COMPLEX WITH AN ORTHOSTERIC
TITLE 2 ANTAGONIST PMX53 AND AN ALLOSTERIC ANTAGONIST NDT9513727
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOLUBLE CYTOCHROME B562, C5A ANAPHYLATOXIN CHEMOTACTIC
COMPND 3 RECEPTOR 1 CHIMERA;
COMPND 4 CHAIN: B;
COMPND 5 FRAGMENT: CYTOCHROME (UNP RESIDUES 23-127) + C5A RECEPTOR (UNP
COMPND 6 RESIDUES 30-331);
COMPND 7 SYNONYM: CYTOCHROME B-562,C5A ANAPHYLATOXIN CHEMOTACTIC RECEPTOR,
COMPND 8 C5AR;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: PMX53;
COMPND 13 CHAIN: L;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 562, 9606;
SOURCE 5 GENE: CYBC, C5AR1, C5AR, C5R1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 15 ORGANISM_TAXID: 32630
KEYWDS GPCR, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LIU,L.WANG,Z.WEI,C.ZHANG
REVDAT 3 08-JAN-20 6C1Q 1 REMARK
REVDAT 2 20-JUN-18 6C1Q 1 JRNL
REVDAT 1 30-MAY-18 6C1Q 0
JRNL AUTH H.LIU,H.R.KIM,R.N.V.K.DEEPAK,L.WANG,K.Y.CHUNG,H.FAN,Z.WEI,
JRNL AUTH 2 C.ZHANG
JRNL TITL ORTHOSTERIC AND ALLOSTERIC ACTION OF THE C5A RECEPTOR
JRNL TITL 2 ANTAGONISTS.
JRNL REF NAT. STRUCT. MOL. BIOL. V. 25 472 2018
JRNL REFN ESSN 1545-9985
JRNL PMID 29867214
JRNL DOI 10.1038/S41594-018-0067-Z
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 10108
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 516
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.4141 - 4.5994 0.93 2685 138 0.2281 0.2453
REMARK 3 2 4.5994 - 3.6529 0.93 2576 142 0.2225 0.2993
REMARK 3 3 3.6529 - 3.1918 0.85 2362 128 0.2796 0.3492
REMARK 3 4 3.1918 - 2.9002 0.72 1969 108 0.3479 0.4124
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.550
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 83.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 116.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 2991
REMARK 3 ANGLE : 0.779 4096
REMARK 3 CHIRALITY : 0.025 500
REMARK 3 PLANARITY : 0.003 497
REMARK 3 DIHEDRAL : 11.472 1006
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3217 26.3479 37.5163
REMARK 3 T TENSOR
REMARK 3 T11: 0.8608 T22: 0.9776
REMARK 3 T33: 0.7026 T12: 0.0704
REMARK 3 T13: 0.0854 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 5.3588 L22: 4.8208
REMARK 3 L33: 5.8976 L12: 1.5032
REMARK 3 L13: -0.9467 L23: -0.2333
REMARK 3 S TENSOR
REMARK 3 S11: -0.5116 S12: 0.2782 S13: -0.2805
REMARK 3 S21: -0.4098 S22: 0.2003 S23: -0.8618
REMARK 3 S31: 0.3709 S32: 1.5042 S33: 0.3780
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 115 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4744 24.0512 44.1528
REMARK 3 T TENSOR
REMARK 3 T11: 0.6770 T22: 0.5542
REMARK 3 T33: 0.5579 T12: -0.0055
REMARK 3 T13: -0.1737 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 3.9991 L22: 5.9997
REMARK 3 L33: 4.3122 L12: -1.2820
REMARK 3 L13: -3.1853 L23: 2.3720
REMARK 3 S TENSOR
REMARK 3 S11: -0.2838 S12: -0.4085 S13: -0.0314
REMARK 3 S21: 0.8059 S22: 0.0952 S23: 0.0845
REMARK 3 S31: 1.3320 S32: 0.4367 S33: 0.1886
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 197 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3840 27.1863 14.8736
REMARK 3 T TENSOR
REMARK 3 T11: 1.4298 T22: 1.0928
REMARK 3 T33: 0.5354 T12: 0.0540
REMARK 3 T13: -0.0663 T23: -0.0985
REMARK 3 L TENSOR
REMARK 3 L11: 8.5953 L22: 3.6009
REMARK 3 L33: 5.5648 L12: -0.9781
REMARK 3 L13: -6.5044 L23: 1.2420
REMARK 3 S TENSOR
REMARK 3 S11: 0.9371 S12: 2.2353 S13: -0.8803
REMARK 3 S21: -0.0155 S22: -0.9109 S23: 0.2988
REMARK 3 S31: -0.7594 S32: -0.5804 S33: -0.1597
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 237 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6586 36.9496 43.3363
REMARK 3 T TENSOR
REMARK 3 T11: 0.4314 T22: 0.4038
REMARK 3 T33: 0.4437 T12: 0.0148
REMARK 3 T13: -0.0085 T23: 0.0403
REMARK 3 L TENSOR
REMARK 3 L11: 6.6248 L22: 8.8324
REMARK 3 L33: 2.3427 L12: 0.4280
REMARK 3 L13: -1.3087 L23: 3.2759
REMARK 3 S TENSOR
REMARK 3 S11: -0.1223 S12: -0.1952 S13: 0.0226
REMARK 3 S21: 0.6283 S22: -0.3554 S23: 0.4162
REMARK 3 S31: -0.5666 S32: -0.4400 S33: 0.5560
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 238 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4828 36.4777 39.5650
REMARK 3 T TENSOR
REMARK 3 T11: 0.8564 T22: 0.6401
REMARK 3 T33: 0.5621 T12: -0.1994
REMARK 3 T13: 0.0459 T23: -0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 4.0767 L22: 5.4415
REMARK 3 L33: 2.0593 L12: -0.1704
REMARK 3 L13: -0.2068 L23: -0.9435
REMARK 3 S TENSOR
REMARK 3 S11: -0.2690 S12: -0.0693 S13: 0.0338
REMARK 3 S21: -0.2897 S22: 0.2175 S23: -0.4947
REMARK 3 S31: -0.9182 S32: 0.9637 S33: 0.2315
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 11 THROUGH 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0813 44.3812 3.8554
REMARK 3 T TENSOR
REMARK 3 T11: 1.7612 T22: 1.8277
REMARK 3 T33: 0.9312 T12: -0.4492
REMARK 3 T13: 0.3370 T23: 0.1181
REMARK 3 L TENSOR
REMARK 3 L11: 2.1607 L22: 8.2343
REMARK 3 L33: 6.6036 L12: -1.6356
REMARK 3 L13: -0.2980 L23: -2.9238
REMARK 3 S TENSOR
REMARK 3 S11: 1.1818 S12: -1.8120 S13: 0.3293
REMARK 3 S21: 0.8392 S22: -0.3378 S23: -0.2971
REMARK 3 S31: -1.5545 S32: 1.3491 S33: -0.9864
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 69 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8566 39.3837 -4.2344
REMARK 3 T TENSOR
REMARK 3 T11: 1.9287 T22: 1.8199
REMARK 3 T33: 0.9902 T12: 0.1248
REMARK 3 T13: 0.3762 T23: 0.3204
REMARK 3 L TENSOR
REMARK 3 L11: 4.8158 L22: 7.5771
REMARK 3 L33: 6.3380 L12: -0.8805
REMARK 3 L13: 2.9827 L23: 1.2733
REMARK 3 S TENSOR
REMARK 3 S11: 0.4082 S12: -0.9856 S13: -1.7115
REMARK 3 S21: -0.0877 S22: -0.0098 S23: -0.1948
REMARK 3 S31: 0.7865 S32: 2.4974 S33: -0.4066
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6C1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000231950.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10290
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.5
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-35% PEG300, 100 MM MES, PH 6.5, 80
REMARK 280 -150 MM SODIUM MALONATE, 0.5% P400, 5 UM NDT, 5 UM PMX53,
REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 26.27900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, L
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE PMX53 IS CYCLIC PEPTIDE, A MEMBER OF CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: PMX53
REMARK 400 CHAIN: L
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP B 1
REMARK 465 TYR B 2
REMARK 465 LYS B 3
REMARK 465 ASP B 4
REMARK 465 ASP B 5
REMARK 465 ASP B 6
REMARK 465 ASP B 7
REMARK 465 VAL B 8
REMARK 465 ASP B 9
REMARK 465 ALA B 10
REMARK 465 GLN B 50
REMARK 465 LYS B 51
REMARK 465 ALA B 52
REMARK 465 THR B 53
REMARK 465 PRO B 54
REMARK 465 PRO B 55
REMARK 465 LYS B 56
REMARK 465 LEU B 57
REMARK 465 GLU B 58
REMARK 465 ASP B 59
REMARK 465 LYS B 60
REMARK 465 SER B 61
REMARK 465 PRO B 62
REMARK 465 ASP B 63
REMARK 465 LEU B 115
REMARK 465 SER B 116
REMARK 465 ASN B 117
REMARK 465 ARG B 319
REMARK 465 ALA B 320
REMARK 465 THR B 321
REMARK 465 ARG B 322
REMARK 465 GLY B 395
REMARK 465 ARG B 396
REMARK 465 LEU B 397
REMARK 465 ARG B 398
REMARK 465 LYS B 399
REMARK 465 GLU B 411
REMARK 465 GLU B 412
REMARK 465 SER B 413
REMARK 465 VAL B 414
REMARK 465 VAL B 415
REMARK 465 ARG B 416
REMARK 465 GLU B 417
REMARK 465 ASN B 418
REMARK 465 LEU B 419
REMARK 465 TYR B 420
REMARK 465 PHE B 421
REMARK 465 GLN B 422
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 GLU B 27 CG CD OE1 OE2
REMARK 470 LYS B 28 CG CD CE NZ
REMARK 470 GLN B 34 CG CD OE1 NE2
REMARK 470 ARG B 43 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 47 CG CD1 CD2
REMARK 470 SER B 64 OG
REMARK 470 GLU B 66 CG CD OE1 OE2
REMARK 470 MET B 67 CG SD CE
REMARK 470 LYS B 68 CG CD CE NZ
REMARK 470 PHE B 70 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 82 CG OD1 OD2
REMARK 470 LYS B 92 CG CD CE NZ
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 GLU B 95 CG CD OE1 OE2
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 ARG B 107 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 108 CG OD1 ND2
REMARK 470 TYR B 110 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B 111 CG1 CG2 CD1
REMARK 470 GLN B 112 CG CD OE1 NE2
REMARK 470 LYS B 113 CG CD CE NZ
REMARK 470 TYR B 114 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 266 CG CD OE1 OE2
REMARK 470 TYR B 267 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE B 268 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 271 CG CD CE NZ
REMARK 470 HIS B 280 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 318 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 328 CG CD CE NZ
REMARK 470 LYS B 366 CG CD CE NZ
REMARK 470 GLN B 391 CG CD OE1 NE2
REMARK 470 PHE B 393 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 394 CG CD OE1 NE2
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 LYS B 28 51.46 -113.71
REMARK 500 GLN B 184 31.64 -93.36
REMARK 500 ASP B 281 60.07 -153.68
REMARK 500 PHE B 297 -61.98 -140.78
REMARK 500 CYS B 380 -11.52 -141.99
REMARK 500 LEU B 409 33.72 -92.66
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 9P2 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for PMX53 chain L
DBREF 6C1Q B 10 115 UNP P0ABE7 C562_ECOLX 23 128
DBREF 6C1Q B 116 417 UNP P21730 C5AR1_HUMAN 30 331
DBREF 6C1Q L 0 6 PDB 6C1Q 6C1Q 0 6
SEQADV 6C1Q ASP B 1 UNP P0ABE7 EXPRESSION TAG
SEQADV 6C1Q TYR B 2 UNP P0ABE7 EXPRESSION TAG
SEQADV 6C1Q LYS B 3 UNP P0ABE7 EXPRESSION TAG
SEQADV 6C1Q ASP B 4 UNP P0ABE7 EXPRESSION TAG
SEQADV 6C1Q ASP B 5 UNP P0ABE7 EXPRESSION TAG
SEQADV 6C1Q ASP B 6 UNP P0ABE7 EXPRESSION TAG
SEQADV 6C1Q ASP B 7 UNP P0ABE7 EXPRESSION TAG
SEQADV 6C1Q VAL B 8 UNP P0ABE7 EXPRESSION TAG
SEQADV 6C1Q ASP B 9 UNP P0ABE7 EXPRESSION TAG
SEQADV 6C1Q TRP B 16 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 6C1Q ILE B 111 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 6C1Q LEU B 115 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 6C1Q ASN B 418 UNP P21730 EXPRESSION TAG
SEQADV 6C1Q LEU B 419 UNP P21730 EXPRESSION TAG
SEQADV 6C1Q TYR B 420 UNP P21730 EXPRESSION TAG
SEQADV 6C1Q PHE B 421 UNP P21730 EXPRESSION TAG
SEQADV 6C1Q GLN B 422 UNP P21730 EXPRESSION TAG
SEQRES 1 B 422 ASP TYR LYS ASP ASP ASP ASP VAL ASP ALA ASP LEU GLU
SEQRES 2 B 422 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE
SEQRES 3 B 422 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU
SEQRES 4 B 422 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA
SEQRES 5 B 422 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO
SEQRES 6 B 422 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL
SEQRES 7 B 422 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY
SEQRES 8 B 422 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS
SEQRES 9 B 422 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SER ASN
SEQRES 10 B 422 THR LEU ARG VAL PRO ASP ILE LEU ALA LEU VAL ILE PHE
SEQRES 11 B 422 ALA VAL VAL PHE LEU VAL GLY VAL LEU GLY ASN ALA LEU
SEQRES 12 B 422 VAL VAL TRP VAL THR ALA PHE GLU ALA LYS ARG THR ILE
SEQRES 13 B 422 ASN ALA ILE TRP PHE LEU ASN LEU ALA VAL ALA ASP PHE
SEQRES 14 B 422 LEU SER CYS LEU ALA LEU PRO ILE LEU PHE THR SER ILE
SEQRES 15 B 422 VAL GLN HIS HIS HIS TRP PRO PHE GLY GLY ALA ALA CYS
SEQRES 16 B 422 SER ILE LEU PRO SER LEU ILE LEU LEU ASN MET TYR ALA
SEQRES 17 B 422 SER ILE LEU LEU LEU ALA THR ILE SER ALA ASP ARG PHE
SEQRES 18 B 422 LEU LEU VAL PHE LYS PRO ILE TRP YCM GLN ASN PHE ARG
SEQRES 19 B 422 GLY ALA GLY LEU ALA TRP ILE ALA CYS ALA VAL ALA TRP
SEQRES 20 B 422 GLY LEU ALA LEU LEU LEU THR ILE PRO SER PHE LEU TYR
SEQRES 21 B 422 ARG VAL VAL ARG GLU GLU TYR PHE PRO PRO LYS VAL LEU
SEQRES 22 B 422 CYS GLY VAL ASP TYR SER HIS ASP LYS ARG ARG GLU ARG
SEQRES 23 B 422 ALA VAL ALA ILE VAL ARG LEU VAL LEU GLY PHE LEU TRP
SEQRES 24 B 422 PRO LEU LEU THR LEU THR ILE CYS TYR THR PHE ILE LEU
SEQRES 25 B 422 LEU ARG THR TRP SER ARG ARG ALA THR ARG SER THR LYS
SEQRES 26 B 422 THR LEU LYS VAL VAL VAL ALA VAL VAL ALA SER PHE PHE
SEQRES 27 B 422 ILE PHE TRP LEU PRO TYR GLN VAL THR GLY ILE MET MET
SEQRES 28 B 422 SER PHE LEU GLU PRO SER SER PRO THR PHE LEU LEU LEU
SEQRES 29 B 422 LYS LYS LEU ASP SER LEU CYS VAL SER PHE ALA TYR ILE
SEQRES 30 B 422 ASN CYS CYS ILE ASN PRO ILE ILE TYR VAL VAL ALA GLY
SEQRES 31 B 422 GLN GLY PHE GLN GLY ARG LEU ARG LYS SER LEU PRO SER
SEQRES 32 B 422 LEU LEU ARG ASN VAL LEU THR GLU GLU SER VAL VAL ARG
SEQRES 33 B 422 GLU ASN LEU TYR PHE GLN
SEQRES 1 L 7 ACE PHE ORN PRO ZAL TRP ARG
MODRES 6C1Q YCM B 230 CYS MODIFIED RESIDUE
HET YCM B 230 10
HET ACE L 0 3
HET ORN L 2 8
HET ZAL L 4 11
HET 9P2 B 501 43
HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE
HETNAM ACE ACETYL GROUP
HETNAM ORN L-ORNITHINE
HETNAM ZAL 3-CYCLOHEXYL-D-ALANINE
HETNAM 9P2 1-(1,3-BENZODIOXOL-5-YL)-~{N}-(1,3-BENZODIOXOL-5-
HETNAM 2 9P2 YLMETHYL)-~{N}-[(3-BUTYL-2,5-DIPHENYL-IMIDAZOL-4-YL)
HETNAM 3 9P2 METHYL]METHANAMINE
HETSYN YCM CYSTEINE-S-ACETAMIDE
FORMUL 1 YCM C5 H10 N2 O3 S
FORMUL 2 ACE C2 H4 O
FORMUL 2 ORN C5 H12 N2 O2
FORMUL 2 ZAL C9 H17 N O2
FORMUL 3 9P2 C36 H35 N3 O4
HELIX 1 AA1 ASP B 11 LYS B 28 1 18
HELIX 2 AA2 ASN B 31 ALA B 49 1 19
HELIX 3 AA3 PRO B 65 GLY B 91 1 27
HELIX 4 AA4 LYS B 92 TYR B 114 1 23
HELIX 5 AA5 ARG B 120 GLU B 151 1 32
HELIX 6 AA6 THR B 155 LEU B 173 1 19
HELIX 7 AA7 ALA B 174 GLN B 184 1 11
HELIX 8 AA8 GLY B 191 LEU B 198 1 8
HELIX 9 AA9 SER B 200 LYS B 226 1 27
HELIX 10 AB1 LYS B 226 PHE B 233 1 8
HELIX 11 AB2 GLY B 235 TYR B 260 1 26
HELIX 12 AB3 ASP B 281 PHE B 297 1 17
HELIX 13 AB4 PHE B 297 SER B 317 1 21
HELIX 14 AB5 THR B 324 PHE B 353 1 30
HELIX 15 AB6 SER B 358 ILE B 377 1 20
HELIX 16 AB7 ILE B 377 GLY B 392 1 16
HELIX 17 AB8 LEU B 401 LEU B 409 1 9
SHEET 1 AA1 3 ARG B 261 GLU B 266 0
SHEET 2 AA1 3 LYS B 271 VAL B 276 -1 O LEU B 273 N ARG B 264
SHEET 3 AA1 3 ORN L 2 PRO L 3 -1 O ORN L 2 N VAL B 276
SSBOND 1 CYS B 195 CYS B 274 1555 1555 2.03
LINK C TRP B 229 N YCM B 230 1555 1555 1.33
LINK C YCM B 230 N GLN B 231 1555 1555 1.33
LINK C ACE L 0 N PHE L 1 1555 1555 1.33
LINK C PHE L 1 N ORN L 2 1555 1555 1.33
LINK NE ORN L 2 C ARG L 6 1555 1555 1.33
LINK C ORN L 2 N PRO L 3 1555 1555 1.34
LINK C PRO L 3 N ZAL L 4 1555 1555 1.33
LINK C ZAL L 4 N TRP L 5 1555 1555 1.33
CISPEP 1 PHE B 268 PRO B 269 0 -1.43
SITE 1 AC1 10 ILE B 210 LEU B 211 ALA B 214 THR B 215
SITE 2 AC1 10 ALA B 242 VAL B 245 LEU B 295 TRP B 299
SITE 3 AC1 10 PRO B 300 THR B 303
SITE 1 AC2 15 LEU B 178 SER B 181 PRO B 199 ARG B 261
SITE 2 AC2 15 VAL B 262 ARG B 264 CYS B 274 GLY B 275
SITE 3 AC2 15 VAL B 276 SER B 279 TYR B 344 THR B 347
SITE 4 AC2 15 GLY B 348 ASP B 368 VAL B 372
CRYST1 62.369 52.558 84.503 90.00 107.75 90.00 P 1 21 1 2
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 0.016034 0.000000 0.005131 0.00000
SCALE2 0.000000 0.019027 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012425 0.00000
ATOM 1 N ASP B 11 17.922 50.902 11.678 1.00223.87 N
ANISOU 1 N ASP B 11 31254 34862 18943 -12490 1111 -2116 N
ATOM 2 CA ASP B 11 16.815 50.041 11.281 1.00213.58 C
ANISOU 2 CA ASP B 11 29945 33411 17795 -11499 1460 -1773 C
ATOM 3 C ASP B 11 17.293 48.924 10.354 1.00204.54 C
ANISOU 3 C ASP B 11 27795 32634 17286 -10976 1287 -1218 C
ATOM 4 O ASP B 11 16.839 48.807 9.213 1.00197.75 O
ANISOU 4 O ASP B 11 26866 31354 16915 -10408 1752 -1043 O
ATOM 5 CB ASP B 11 15.715 50.863 10.607 1.00211.94 C
ANISOU 5 CB ASP B 11 30497 32329 17701 -11147 2281 -2003 C
ATOM 6 CG ASP B 11 15.223 52.003 11.482 1.00222.74 C
ANISOU 6 CG ASP B 11 32939 33265 18427 -11590 2536 -2548 C
ATOM 7 OD1 ASP B 11 15.275 51.869 12.724 1.00225.83 O
ANISOU 7 OD1 ASP B 11 33616 34008 18182 -11879 2144 -2676 O
ATOM 8 OD2 ASP B 11 14.786 53.035 10.929 1.00221.20 O
ANISOU 8 OD2 ASP B 11 33360 32356 18329 -11621 3138 -2847 O
ATOM 9 N LEU B 12 18.220 48.110 10.856 1.00208.89 N
ANISOU 9 N LEU B 12 27617 33955 17795 -11150 606 -941 N
ATOM 10 CA LEU B 12 18.702 46.933 10.138 1.00207.45 C
ANISOU 10 CA LEU B 12 26520 34178 18125 -10598 402 -384 C
ATOM 11 C LEU B 12 17.706 45.797 10.305 1.00204.61 C
ANISOU 11 C LEU B 12 26230 33852 17659 -9775 405 -45 C
ATOM 12 O LEU B 12 17.208 45.233 9.329 1.00190.11 O
ANISOU 12 O LEU B 12 24253 31727 16254 -9077 706 245 O
ATOM 13 CB LEU B 12 20.085 46.509 10.654 1.00212.07 C
ANISOU 13 CB LEU B 12 26276 35590 18709 -11077 -331 -186 C
ATOM 14 CG LEU B 12 20.981 45.570 9.832 1.00206.77 C
ANISOU 14 CG LEU B 12 24568 35363 18632 -10681 -513 358 C
ATOM 15 CD1 LEU B 12 22.387 45.543 10.423 1.00213.48 C
ANISOU 15 CD1 LEU B 12 24653 36981 19478 -11352 -1197 461 C
ATOM 16 CD2 LEU B 12 20.432 44.146 9.717 1.00202.33 C
ANISOU 16 CD2 LEU B 12 23789 34976 18113 -9757 -609 836 C
ATOM 17 N GLU B 13 17.444 45.460 11.562 1.00207.28 N
ANISOU 17 N GLU B 13 26810 34539 17407 -9888 41 -74 N
ATOM 18 CA GLU B 13 16.533 44.385 11.915 1.00197.06 C
ANISOU 18 CA GLU B 13 25586 33324 15962 -9207 7 266 C
ATOM 19 C GLU B 13 15.096 44.808 11.649 1.00191.28 C
ANISOU 19 C GLU B 13 25584 31870 15225 -8810 675 119 C
ATOM 20 O GLU B 13 14.226 43.976 11.380 1.00187.94 O
ANISOU 20 O GLU B 13 25123 31303 14983 -8137 814 462 O
ATOM 21 CB GLU B 13 16.713 44.002 13.388 1.00205.70 C
ANISOU 21 CB GLU B 13 26791 34991 16375 -9484 -539 270 C
ATOM 22 CG GLU B 13 16.121 42.659 13.768 1.00203.80 C
ANISOU 22 CG GLU B 13 26388 35011 16037 -8823 -718 749 C
ATOM 23 CD GLU B 13 16.733 41.509 12.988 1.00201.57 C
ANISOU 23 CD GLU B 13 25246 35052 16290 -8350 -1008 1268 C
ATOM 24 OE1 GLU B 13 17.974 41.470 12.850 1.00203.68 O
ANISOU 24 OE1 GLU B 13 24892 35779 16719 -8663 -1412 1337 O
ATOM 25 OE2 GLU B 13 15.972 40.647 12.502 1.00197.17 O
ANISOU 25 OE2 GLU B 13 24641 34272 16003 -7660 -830 1621 O
ATOM 26 N ASP B 14 14.863 46.115 11.715 1.00192.37 N
ANISOU 26 N ASP B 14 26377 31539 15174 -9241 1076 -375 N
ATOM 27 CA ASP B 14 13.516 46.671 11.645 1.00185.63 C
ANISOU 27 CA ASP B 14 26275 30026 14231 -8913 1723 -548 C
ATOM 28 C ASP B 14 12.913 46.597 10.247 1.00178.69 C
ANISOU 28 C ASP B 14 25279 28606 14009 -8320 2179 -363 C
ATOM 29 O ASP B 14 11.718 46.346 10.094 1.00174.11 O
ANISOU 29 O ASP B 14 24956 27677 13522 -7759 2518 -203 O
ATOM 30 CB ASP B 14 13.526 48.121 12.129 1.00191.79 C
ANISOU 30 CB ASP B 14 27850 30439 14582 -9542 2013 -1141 C
ATOM 31 CG ASP B 14 13.906 48.240 13.588 1.00196.15 C
ANISOU 31 CG ASP B 14 28738 31421 14369 -10082 1581 -1362 C
ATOM 32 OD1 ASP B 14 13.000 48.147 14.443 1.00195.04 O
ANISOU 32 OD1 ASP B 14 29162 31207 13737 -9836 1775 -1377 O
ATOM 33 OD2 ASP B 14 15.108 48.419 13.879 1.00202.93 O
ANISOU 33 OD2 ASP B 14 29294 32693 15118 -10742 1043 -1497 O
ATOM 34 N ASN B 15 13.737 46.829 9.231 1.00174.18 N
ANISOU 34 N ASN B 15 24327 27962 13892 -8446 2183 -368 N
ATOM 35 CA ASN B 15 13.284 46.701 7.854 1.00164.65 C
ANISOU 35 CA ASN B 15 23033 26260 13269 -7867 2550 -177 C
ATOM 36 C ASN B 15 12.862 45.266 7.566 1.00167.50 C
ANISOU 36 C ASN B 15 22951 26810 13883 -7159 2292 355 C
ATOM 37 O ASN B 15 11.826 45.024 6.943 1.00172.64 O
ANISOU 37 O ASN B 15 23793 27004 14797 -6584 2568 521 O
ATOM 38 CB ASN B 15 14.374 47.155 6.881 1.00162.68 C
ANISOU 38 CB ASN B 15 22446 25954 13410 -8138 2604 -240 C
ATOM 39 CG ASN B 15 14.489 48.665 6.806 1.00166.13 C
ANISOU 39 CG ASN B 15 23459 25924 13739 -8710 3028 -746 C
ATOM 40 OD1 ASN B 15 13.528 49.383 7.082 1.00167.90 O
ANISOU 40 OD1 ASN B 15 24410 25666 13719 -8671 3432 -1022 O
ATOM 41 ND2 ASN B 15 15.664 49.154 6.428 1.00180.20 N
ANISOU 41 ND2 ASN B 15 24918 27830 15720 -9236 2962 -845 N
ATOM 42 N TRP B 16 13.661 44.320 8.048 1.00163.33 N
ANISOU 42 N TRP B 16 21848 26945 13266 -7217 1731 629 N
ATOM 43 CA TRP B 16 13.347 42.905 7.916 1.00159.70 C
ANISOU 43 CA TRP B 16 21010 26689 12980 -6597 1431 1136 C
ATOM 44 C TRP B 16 12.058 42.554 8.655 1.00151.26 C
ANISOU 44 C TRP B 16 20317 25492 11662 -6315 1525 1241 C
ATOM 45 O TRP B 16 11.243 41.765 8.168 1.00150.95 O
ANISOU 45 O TRP B 16 20225 25208 11919 -5730 1552 1584 O
ATOM 46 CB TRP B 16 14.499 42.052 8.444 1.00169.93 C
ANISOU 46 CB TRP B 16 21664 28747 14154 -6749 821 1390 C
ATOM 47 CG TRP B 16 14.317 40.608 8.150 1.00168.70 C
ANISOU 47 CG TRP B 16 21141 28740 14218 -6093 532 1917 C
ATOM 48 CD1 TRP B 16 14.001 39.620 9.036 1.00171.35 C
ANISOU 48 CD1 TRP B 16 21391 29434 14281 -5901 176 2213 C
ATOM 49 CD2 TRP B 16 14.413 39.983 6.868 1.00157.17 C
ANISOU 49 CD2 TRP B 16 19438 27014 13267 -5526 584 2213 C
ATOM 50 NE1 TRP B 16 13.905 38.414 8.385 1.00166.24 N
ANISOU 50 NE1 TRP B 16 20448 28747 13966 -5278 -13 2673 N
ATOM 51 CE2 TRP B 16 14.155 38.611 7.050 1.00154.54 C
ANISOU 51 CE2 TRP B 16 18890 26878 12949 -5029 222 2670 C
ATOM 52 CE3 TRP B 16 14.700 40.451 5.581 1.00161.12 C
ANISOU 52 CE3 TRP B 16 19941 27099 14179 -5378 914 2141 C
ATOM 53 CZ2 TRP B 16 14.172 37.701 5.995 1.00154.13 C
ANISOU 53 CZ2 TRP B 16 18671 26598 13294 -4401 152 3029 C
ATOM 54 CZ3 TRP B 16 14.718 39.547 4.535 1.00159.86 C
ANISOU 54 CZ3 TRP B 16 19617 26735 14389 -4725 864 2504 C
ATOM 55 CH2 TRP B 16 14.457 38.189 4.748 1.00170.71 C
ANISOU 55 CH2 TRP B 16 20819 28290 15753 -4248 472 2930 C
ATOM 56 N GLU B 17 11.884 43.146 9.833 1.00153.58 N
ANISOU 56 N GLU B 17 21008 25935 11409 -6742 1576 960 N
ATOM 57 CA GLU B 17 10.683 42.930 10.635 1.00154.77 C
ANISOU 57 CA GLU B 17 21548 25978 11278 -6498 1766 1061 C
ATOM 58 C GLU B 17 9.432 43.441 9.920 1.00143.87 C
ANISOU 58 C GLU B 17 20558 23883 10223 -6105 2360 1024 C
ATOM 59 O GLU B 17 8.386 42.791 9.937 1.00135.76 O
ANISOU 59 O GLU B 17 19522 22701 9360 -5627 2456 1363 O
ATOM 60 CB GLU B 17 10.824 43.610 11.996 1.00160.14 C
ANISOU 60 CB GLU B 17 22701 26906 11240 -7034 1764 713 C
ATOM 61 CG GLU B 17 9.657 43.356 12.932 1.00155.98 C
ANISOU 61 CG GLU B 17 22584 26325 10358 -6762 2009 857 C
ATOM 62 CD GLU B 17 9.781 44.117 14.235 1.00165.20 C
ANISOU 62 CD GLU B 17 24376 27654 10739 -7253 2065 474 C
ATOM 63 OE1 GLU B 17 10.256 45.272 14.208 1.00166.49 O
ANISOU 63 OE1 GLU B 17 24926 27620 10712 -7752 2203 -21 O
ATOM 64 OE2 GLU B 17 9.407 43.558 15.287 1.00182.86 O
ANISOU 64 OE2 GLU B 17 26769 30186 12524 -7143 1969 670 O
ATOM 65 N THR B 18 9.549 44.612 9.300 1.00154.33 N
ANISOU 65 N THR B 18 22208 24774 11658 -6320 2745 636 N
ATOM 66 CA THR B 18 8.465 45.173 8.503 1.00143.02 C
ANISOU 66 CA THR B 18 21129 22652 10559 -5933 3288 597 C
ATOM 67 C THR B 18 8.168 44.256 7.324 1.00132.80 C
ANISOU 67 C THR B 18 19423 21160 9875 -5348 3128 1015 C
ATOM 68 O THR B 18 7.007 44.061 6.949 1.00126.74 O
ANISOU 68 O THR B 18 18763 20002 9391 -4875 3339 1232 O
ATOM 69 CB THR B 18 8.805 46.586 7.984 1.00142.29 C
ANISOU 69 CB THR B 18 21472 22124 10469 -6285 3700 111 C
ATOM 70 OG1 THR B 18 10.128 46.592 7.438 1.00158.17 O
ANISOU 70 OG1 THR B 18 23098 24365 12636 -6618 3407 39 O
ATOM 71 CG2 THR B 18 8.730 47.607 9.106 1.00154.60 C
ANISOU 71 CG2 THR B 18 23665 23662 11412 -6771 3964 -325 C
ATOM 72 N LEU B 19 9.227 43.689 6.751 1.00134.75 N
ANISOU 72 N LEU B 19 19207 21674 10318 -5378 2742 1141 N
ATOM 73 CA LEU B 19 9.092 42.772 5.625 1.00130.73 C
ANISOU 73 CA LEU B 19 18390 20970 10311 -4822 2548 1519 C
ATOM 74 C LEU B 19 8.296 41.529 6.000 1.00127.05 C
ANISOU 74 C LEU B 19 17725 20629 9917 -4411 2251 1979 C
ATOM 75 O LEU B 19 7.332 41.187 5.326 1.00120.00 O
ANISOU 75 O LEU B 19 16906 19298 9393 -3950 2313 2212 O
ATOM 76 CB LEU B 19 10.466 42.362 5.090 1.00127.61 C
ANISOU 76 CB LEU B 19 17544 20901 10039 -4911 2228 1594 C
ATOM 77 CG LEU B 19 11.283 43.427 4.356 1.00128.13 C
ANISOU 77 CG LEU B 19 17707 20761 10217 -5220 2528 1260 C
ATOM 78 CD1 LEU B 19 12.604 42.850 3.872 1.00138.53 C
ANISOU 78 CD1 LEU B 19 18469 22465 11700 -5225 2228 1452 C
ATOM 79 CD2 LEU B 19 10.495 44.021 3.201 1.00138.85 C
ANISOU 79 CD2 LEU B 19 19488 21363 11905 -4855 2970 1178 C
ATOM 80 N ASN B 20 8.700 40.853 7.072 1.00144.76 N
ANISOU 80 N ASN B 20 19724 23459 11817 -4594 1903 2127 N
ATOM 81 CA ASN B 20 8.000 39.646 7.506 1.00141.29 C
ANISOU 81 CA ASN B 20 19105 23151 11426 -4247 1629 2590 C
ATOM 82 C ASN B 20 6.580 39.936 7.998 1.00129.18 C
ANISOU 82 C ASN B 20 17891 21315 9876 -4114 2010 2647 C
ATOM 83 O ASN B 20 5.655 39.163 7.732 1.00123.36 O
ANISOU 83 O ASN B 20 17044 20350 9477 -3711 1928 3043 O
ATOM 84 CB ASN B 20 8.795 38.926 8.599 1.00140.10 C
ANISOU 84 CB ASN B 20 18671 23706 10856 -4476 1197 2731 C
ATOM 85 CG ASN B 20 9.726 37.862 8.039 1.00155.12 C
ANISOU 85 CG ASN B 20 20101 25872 12966 -4247 705 3036 C
ATOM 86 OD1 ASN B 20 10.100 37.902 6.866 1.00153.29 O
ANISOU 86 OD1 ASN B 20 19780 25362 13102 -4041 727 3025 O
ATOM 87 ND2 ASN B 20 10.099 36.901 8.878 1.00144.63 N
ANISOU 87 ND2 ASN B 20 18510 25066 11377 -4237 287 3326 N
ATOM 88 N ASP B 21 6.412 41.045 8.713 1.00132.45 N
ANISOU 88 N ASP B 21 18705 21713 9906 -4450 2428 2271 N
ATOM 89 CA ASP B 21 5.090 41.453 9.180 1.00142.77 C
ANISOU 89 CA ASP B 21 20340 22725 11184 -4283 2904 2319 C
ATOM 90 C ASP B 21 4.137 41.657 8.009 1.00131.87 C
ANISOU 90 C ASP B 21 18996 20708 10401 -3856 3148 2437 C
ATOM 91 O ASP B 21 3.043 41.088 7.984 1.00124.42 O
ANISOU 91 O ASP B 21 17921 19584 9768 -3496 3181 2834 O
ATOM 92 CB ASP B 21 5.176 42.734 10.014 1.00156.20 C
ANISOU 92 CB ASP B 21 22585 24429 12336 -4688 3353 1831 C
ATOM 93 CG ASP B 21 5.555 42.468 11.457 1.00152.78 C
ANISOU 93 CG ASP B 21 22249 24553 11246 -4997 3184 1816 C
ATOM 94 OD1 ASP B 21 6.192 41.428 11.726 1.00150.02 O
ANISOU 94 OD1 ASP B 21 21489 24676 10838 -5022 2642 2083 O
ATOM 95 OD2 ASP B 21 5.215 43.300 12.325 1.00158.55 O
ANISOU 95 OD2 ASP B 21 23521 25233 11490 -5187 3596 1541 O
ATOM 96 N ASN B 22 4.558 42.460 7.036 1.00156.14 N
ANISOU 96 N ASN B 22 22237 23442 13645 -3908 3297 2117 N
ATOM 97 CA ASN B 22 3.731 42.715 5.863 1.00133.91 C
ANISOU 97 CA ASN B 22 19515 20011 11356 -3497 3488 2204 C
ATOM 98 C ASN B 22 3.574 41.477 4.989 1.00120.29 C
ANISOU 98 C ASN B 22 17414 18182 10108 -3095 2980 2648 C
ATOM 99 O ASN B 22 2.602 41.352 4.253 1.00120.21 O
ANISOU 99 O ASN B 22 17418 17716 10541 -2710 3002 2871 O
ATOM 100 CB ASN B 22 4.308 43.860 5.036 1.00122.90 C
ANISOU 100 CB ASN B 22 18444 18274 9979 -3652 3775 1762 C
ATOM 101 CG ASN B 22 4.174 45.198 5.724 1.00126.18 C
ANISOU 101 CG ASN B 22 19371 18576 9996 -3975 4339 1325 C
ATOM 102 OD1 ASN B 22 3.141 45.860 5.622 1.00127.74 O
ANISOU 102 OD1 ASN B 22 19884 18346 10306 -3731 4798 1298 O
ATOM 103 ND2 ASN B 22 5.219 45.606 6.433 1.00128.04 N
ANISOU 103 ND2 ASN B 22 19709 19179 9760 -4521 4291 990 N
ATOM 104 N LEU B 23 4.539 40.568 5.077 1.00123.24 N
ANISOU 104 N LEU B 23 17477 18965 10381 -3179 2502 2781 N
ATOM 105 CA LEU B 23 4.472 39.298 4.367 1.00124.76 C
ANISOU 105 CA LEU B 23 17392 19070 10941 -2801 1994 3203 C
ATOM 106 C LEU B 23 3.333 38.461 4.934 1.00130.26 C
ANISOU 106 C LEU B 23 17924 19763 11804 -2604 1858 3653 C
ATOM 107 O LEU B 23 2.565 37.840 4.192 1.00126.44 O
ANISOU 107 O LEU B 23 17373 18889 11780 -2251 1623 3980 O
ATOM 108 CB LEU B 23 5.805 38.553 4.477 1.00133.93 C
ANISOU 108 CB LEU B 23 18271 20714 11903 -2916 1577 3254 C
ATOM 109 CG LEU B 23 5.963 37.212 3.760 1.00142.61 C
ANISOU 109 CG LEU B 23 19162 21731 13292 -2512 1054 3661 C
ATOM 110 CD1 LEU B 23 5.646 37.349 2.279 1.00125.97 C
ANISOU 110 CD1 LEU B 23 17289 18976 11596 -2134 1063 3656 C
ATOM 111 CD2 LEU B 23 7.374 36.683 3.967 1.00145.12 C
ANISOU 111 CD2 LEU B 23 19197 22577 13363 -2625 757 3677 C
ATOM 112 N LYS B 24 3.221 38.463 6.259 1.00145.68 N
ANISOU 112 N LYS B 24 19839 22139 13376 -2850 2004 3680 N
ATOM 113 CA LYS B 24 2.136 37.760 6.930 1.00133.92 C
ANISOU 113 CA LYS B 24 18191 20676 12016 -2699 1990 4127 C
ATOM 114 C LYS B 24 0.812 38.473 6.676 1.00132.77 C
ANISOU 114 C LYS B 24 18182 20060 12206 -2503 2446 4173 C
ATOM 115 O LYS B 24 -0.242 37.839 6.610 1.00130.84 O
ANISOU 115 O LYS B 24 17718 19620 12377 -2261 2352 4627 O
ATOM 116 CB LYS B 24 2.412 37.646 8.432 1.00157.63 C
ANISOU 116 CB LYS B 24 21197 24249 14445 -2987 2087 4132 C
ATOM 117 CG LYS B 24 3.163 36.378 8.831 1.00161.18 C
ANISOU 117 CG LYS B 24 21360 25146 14735 -3008 1523 4424 C
ATOM 118 CD LYS B 24 4.457 36.221 8.043 1.00154.61 C
ANISOU 118 CD LYS B 24 20425 24414 13904 -3040 1147 4231 C
ATOM 119 CE LYS B 24 5.088 34.856 8.246 1.00157.67 C
ANISOU 119 CE LYS B 24 20518 25153 14237 -2924 580 4600 C
ATOM 120 NZ LYS B 24 6.271 34.674 7.358 1.00146.48 N
ANISOU 120 NZ LYS B 24 18977 23784 12895 -2849 279 4478 N
ATOM 121 N VAL B 25 0.877 39.793 6.528 1.00136.16 N
ANISOU 121 N VAL B 25 18959 20300 12476 -2613 2933 3723 N
ATOM 122 CA VAL B 25 -0.295 40.585 6.164 1.00147.65 C
ANISOU 122 CA VAL B 25 20570 21278 14252 -2371 3393 3739 C
ATOM 123 C VAL B 25 -0.815 40.171 4.787 1.00143.40 C
ANISOU 123 C VAL B 25 19888 20239 14359 -2006 3046 3982 C
ATOM 124 O VAL B 25 -2.022 40.036 4.585 1.00144.51 O
ANISOU 124 O VAL B 25 19869 20088 14951 -1733 3103 4332 O
ATOM 125 CB VAL B 25 0.017 42.100 6.164 1.00146.43 C
ANISOU 125 CB VAL B 25 20905 20959 13772 -2552 3959 3172 C
ATOM 126 CG1 VAL B 25 -1.102 42.885 5.494 1.00147.98 C
ANISOU 126 CG1 VAL B 25 21265 20592 14371 -2210 4371 3201 C
ATOM 127 CG2 VAL B 25 0.243 42.598 7.584 1.00141.50 C
ANISOU 127 CG2 VAL B 25 20537 20725 12502 -2880 4339 2947 C
ATOM 128 N ILE B 26 0.103 39.965 3.846 1.00131.43 N
ANISOU 128 N ILE B 26 18435 18623 12882 -1995 2680 3817 N
ATOM 129 CA ILE B 26 -0.262 39.514 2.506 1.00135.17 C
ANISOU 129 CA ILE B 26 18889 18601 13868 -1639 2286 4019 C
ATOM 130 C ILE B 26 -0.814 38.097 2.563 1.00124.03 C
ANISOU 130 C ILE B 26 17124 17213 12788 -1482 1727 4572 C
ATOM 131 O ILE B 26 -1.794 37.774 1.889 1.00128.55 O
ANISOU 131 O ILE B 26 17613 17361 13868 -1214 1489 4883 O
ATOM 132 CB ILE B 26 0.936 39.555 1.536 1.00141.08 C
ANISOU 132 CB ILE B 26 19836 19257 14513 -1627 2073 3739 C
ATOM 133 CG1 ILE B 26 1.447 40.986 1.377 1.00129.82 C
ANISOU 133 CG1 ILE B 26 18769 17730 12827 -1812 2626 3217 C
ATOM 134 CG2 ILE B 26 0.541 39.013 0.172 1.00135.96 C
ANISOU 134 CG2 ILE B 26 19277 18065 14317 -1218 1638 3958 C
ATOM 135 CD1 ILE B 26 2.753 41.087 0.620 1.00124.77 C
ANISOU 135 CD1 ILE B 26 18256 17102 12048 -1877 2522 2960 C
ATOM 136 N GLU B 27 -0.182 37.254 3.375 1.00123.31 N
ANISOU 136 N GLU B 27 16835 17606 12412 -1667 1491 4705 N
ATOM 137 CA GLU B 27 -0.678 35.901 3.595 1.00125.39 C
ANISOU 137 CA GLU B 27 16795 17908 12939 -1566 1004 5241 C
ATOM 138 C GLU B 27 -2.106 35.928 4.141 1.00133.62 C
ANISOU 138 C GLU B 27 17608 18845 14317 -1517 1241 5614 C
ATOM 139 O GLU B 27 -2.917 35.059 3.822 1.00126.00 O
ANISOU 139 O GLU B 27 16410 17623 13840 -1371 842 6083 O
ATOM 140 CB GLU B 27 0.242 35.141 4.551 1.00118.15 C
ANISOU 140 CB GLU B 27 15736 17574 11581 -1775 816 5307 C
ATOM 141 N LYS B 28 -2.411 36.933 4.956 1.00145.82 N
ANISOU 141 N LYS B 28 19229 20569 15608 -1639 1901 5421 N
ATOM 142 CA LYS B 28 -3.754 37.087 5.506 1.00145.20 C
ANISOU 142 CA LYS B 28 18925 20410 15833 -1540 2268 5784 C
ATOM 143 C LYS B 28 -4.428 38.346 4.966 1.00156.35 C
ANISOU 143 C LYS B 28 20521 21433 17452 -1354 2754 5569 C
ATOM 144 O LYS B 28 -4.935 39.168 5.730 1.00151.67 O
ANISOU 144 O LYS B 28 20008 20935 16682 -1352 3417 5505 O
ATOM 145 CB LYS B 28 -3.703 37.128 7.034 1.00155.60 C
ANISOU 145 CB LYS B 28 20224 22246 16653 -1745 2708 5831 C
ATOM 146 N ALA B 29 -4.429 38.491 3.644 1.00164.17 N
ANISOU 146 N ALA B 29 21633 21963 18783 -1162 2434 5467 N
ATOM 147 CA ALA B 29 -4.949 39.693 3.000 1.00144.79 C
ANISOU 147 CA ALA B 29 19413 19103 16497 -954 2842 5238 C
ATOM 148 C ALA B 29 -6.427 39.564 2.639 1.00146.59 C
ANISOU 148 C ALA B 29 19288 18989 17420 -660 2782 5741 C
ATOM 149 O ALA B 29 -6.895 38.491 2.265 1.00142.69 O
ANISOU 149 O ALA B 29 18456 18368 17392 -603 2165 6195 O
ATOM 150 CB ALA B 29 -4.132 40.014 1.761 1.00143.54 C
ANISOU 150 CB ALA B 29 19630 18621 16286 -882 2579 4854 C
ATOM 151 N ASP B 30 -7.150 40.675 2.743 1.00163.41 N
ANISOU 151 N ASP B 30 21505 20955 19627 -476 3413 5666 N
ATOM 152 CA ASP B 30 -8.595 40.691 2.529 1.00175.35 C
ANISOU 152 CA ASP B 30 22604 22208 21814 -178 3462 6176 C
ATOM 153 C ASP B 30 -8.943 41.007 1.072 1.00168.55 C
ANISOU 153 C ASP B 30 21871 20781 21390 112 3079 6143 C
ATOM 154 O ASP B 30 -9.874 40.435 0.504 1.00172.22 O
ANISOU 154 O ASP B 30 21938 20988 22510 280 2586 6628 O
ATOM 155 CB ASP B 30 -9.243 41.713 3.465 1.00182.24 C
ANISOU 155 CB ASP B 30 23502 23209 22531 -50 4405 6168 C
ATOM 156 CG ASP B 30 -10.729 41.478 3.664 1.00181.93 C
ANISOU 156 CG ASP B 30 22840 23102 23181 215 4537 6852 C
ATOM 157 OD1 ASP B 30 -11.201 41.676 4.803 1.00183.25 O
ANISOU 157 OD1 ASP B 30 22858 23560 23207 245 5203 7058 O
ATOM 158 OD2 ASP B 30 -11.427 41.109 2.697 1.00178.35 O
ANISOU 158 OD2 ASP B 30 22055 22304 23406 396 3986 7200 O
ATOM 159 N ASN B 31 -8.187 41.925 0.477 1.00163.72 N
ANISOU 159 N ASN B 31 21833 19966 20407 152 3289 5582 N
ATOM 160 CA ASN B 31 -8.402 42.329 -0.907 1.00162.44 C
ANISOU 160 CA ASN B 31 21926 19254 20541 451 2991 5494 C
ATOM 161 C ASN B 31 -7.090 42.664 -1.603 1.00162.91 C
ANISOU 161 C ASN B 31 22586 19187 20124 354 2915 4930 C
ATOM 162 O ASN B 31 -6.021 42.598 -0.996 1.00156.42 O
ANISOU 162 O ASN B 31 21915 18730 18788 35 3077 4620 O
ATOM 163 CB ASN B 31 -9.346 43.531 -0.976 1.00173.15 C
ANISOU 163 CB ASN B 31 23334 20355 22102 782 3609 5512 C
ATOM 164 CG ASN B 31 -10.808 43.129 -0.934 1.00176.21 C
ANISOU 164 CG ASN B 31 23062 20664 23224 1025 3434 6187 C
ATOM 165 OD1 ASN B 31 -11.202 42.122 -1.523 1.00172.33 O
ANISOU 165 OD1 ASN B 31 22229 20027 23221 1031 2629 6584 O
ATOM 166 ND2 ASN B 31 -11.621 43.915 -0.237 1.00180.69 N
ANISOU 166 ND2 ASN B 31 23457 21314 23883 1227 4190 6339 N
ATOM 167 N ALA B 32 -7.181 43.030 -2.878 1.00164.45 N
ANISOU 167 N ALA B 32 23111 18870 20502 640 2672 4827 N
ATOM 168 CA ALA B 32 -6.006 43.394 -3.660 1.00140.04 C
ANISOU 168 CA ALA B 32 20596 15599 17013 607 2659 4348 C
ATOM 169 C ALA B 32 -5.360 44.674 -3.136 1.00136.83 C
ANISOU 169 C ALA B 32 20573 15311 16104 427 3493 3836 C
ATOM 170 O ALA B 32 -4.144 44.849 -3.230 1.00129.30 O
ANISOU 170 O ALA B 32 19931 14469 14727 190 3589 3447 O
ATOM 171 CB ALA B 32 -6.378 43.552 -5.127 1.00138.82 C
ANISOU 171 CB ALA B 32 20767 14825 17152 1006 2259 4392 C
ATOM 172 N ALA B 33 -6.180 45.563 -2.583 1.00142.14 N
ANISOU 172 N ALA B 33 21225 15945 16837 541 4097 3856 N
ATOM 173 CA ALA B 33 -5.695 46.848 -2.087 1.00141.79 C
ANISOU 173 CA ALA B 33 21642 15915 16314 384 4896 3369 C
ATOM 174 C ALA B 33 -4.721 46.669 -0.926 1.00153.46 C
ANISOU 174 C ALA B 33 23100 17946 17264 -122 5087 3116 C
ATOM 175 O ALA B 33 -3.663 47.302 -0.890 1.00142.27 O
ANISOU 175 O ALA B 33 22092 16565 15399 -417 5354 2640 O
ATOM 176 CB ALA B 33 -6.863 47.729 -1.669 1.00143.94 C
ANISOU 176 CB ALA B 33 21907 16024 16759 679 5506 3505 C
ATOM 177 N GLN B 34 -5.080 45.803 0.018 1.00153.40 N
ANISOU 177 N GLN B 34 22608 18361 17317 -234 4928 3459 N
ATOM 178 CA GLN B 34 -4.223 45.522 1.165 1.00143.76 C
ANISOU 178 CA GLN B 34 21349 17687 15586 -683 5027 3278 C
ATOM 179 C GLN B 34 -2.912 44.885 0.715 1.00144.62 C
ANISOU 179 C GLN B 34 21483 17965 15500 -941 4513 3093 C
ATOM 180 O GLN B 34 -1.848 45.168 1.272 1.00149.00 O
ANISOU 180 O GLN B 34 22217 18832 15563 -1335 4674 2728 O
ATOM 181 CB GLN B 34 -4.940 44.612 2.165 1.00150.48 C
ANISOU 181 CB GLN B 34 21679 18916 16582 -686 4923 3761 C
ATOM 182 N VAL B 35 -2.998 44.027 -0.297 1.00138.11 N
ANISOU 182 N VAL B 35 20488 16922 15064 -706 3887 3361 N
ATOM 183 CA VAL B 35 -1.816 43.407 -0.883 1.00132.59 C
ANISOU 183 CA VAL B 35 19847 16310 14220 -825 3437 3235 C
ATOM 184 C VAL B 35 -0.894 44.475 -1.457 1.00127.34 C
ANISOU 184 C VAL B 35 19669 15447 13268 -937 3807 2734 C
ATOM 185 O VAL B 35 0.312 44.459 -1.217 1.00120.82 O
ANISOU 185 O VAL B 35 18877 14935 12093 -1268 3818 2479 O
ATOM 186 CB VAL B 35 -2.186 42.404 -1.994 1.00133.11 C
ANISOU 186 CB VAL B 35 19808 16036 14731 -473 2737 3594 C
ATOM 187 CG1 VAL B 35 -0.929 41.843 -2.646 1.00135.28 C
ANISOU 187 CG1 VAL B 35 20232 16358 14811 -512 2380 3455 C
ATOM 188 CG2 VAL B 35 -3.049 41.285 -1.437 1.00137.42 C
ANISOU 188 CG2 VAL B 35 19854 16757 15601 -433 2323 4118 C
ATOM 189 N LYS B 36 -1.475 45.405 -2.209 1.00128.32 N
ANISOU 189 N LYS B 36 20147 15048 13561 -663 4112 2624 N
ATOM 190 CA LYS B 36 -0.714 46.493 -2.815 1.00135.26 C
ANISOU 190 CA LYS B 36 21536 15649 14205 -748 4519 2180 C
ATOM 191 C LYS B 36 -0.041 47.375 -1.768 1.00149.53 C
ANISOU 191 C LYS B 36 23514 17765 15537 -1247 5073 1768 C
ATOM 192 O LYS B 36 1.124 47.746 -1.913 1.00139.33 O
ANISOU 192 O LYS B 36 22406 16559 13974 -1570 5187 1443 O
ATOM 193 CB LYS B 36 -1.618 47.349 -3.704 1.00134.33 C
ANISOU 193 CB LYS B 36 21789 14900 14349 -324 4769 2180 C
ATOM 194 CG LYS B 36 -0.957 48.629 -4.185 1.00124.31 C
ANISOU 194 CG LYS B 36 21108 13307 12819 -430 5319 1723 C
ATOM 195 CD LYS B 36 -1.875 49.436 -5.081 1.00124.04 C
ANISOU 195 CD LYS B 36 21466 12634 13030 48 5544 1758 C
ATOM 196 CE LYS B 36 -1.224 50.753 -5.471 1.00123.63 C
ANISOU 196 CE LYS B 36 22044 12234 12694 -88 6154 1308 C
ATOM 197 NZ LYS B 36 -2.022 51.488 -6.489 1.00124.95 N
ANISOU 197 NZ LYS B 36 22650 11746 13080 432 6329 1358 N
ATOM 198 N ASP B 37 -0.783 47.711 -0.717 1.00147.76 N
ANISOU 198 N ASP B 37 23242 17689 15211 -1308 5415 1799 N
ATOM 199 CA ASP B 37 -0.259 48.555 0.352 1.00137.60 C
ANISOU 199 CA ASP B 37 22225 16643 13415 -1769 5915 1401 C
ATOM 200 C ASP B 37 0.895 47.870 1.080 1.00126.20 C
ANISOU 200 C ASP B 37 20503 15808 11639 -2254 5583 1319 C
ATOM 201 O ASP B 37 1.952 48.472 1.311 1.00126.03 O
ANISOU 201 O ASP B 37 20709 15917 11258 -2710 5745 923 O
ATOM 202 CB ASP B 37 -1.371 48.911 1.340 1.00141.81 C
ANISOU 202 CB ASP B 37 22789 17204 13889 -1636 6347 1519 C
ATOM 203 CG ASP B 37 -0.866 49.711 2.523 1.00168.25 C
ANISOU 203 CG ASP B 37 26518 20778 16631 -2098 6822 1106 C
ATOM 204 OD1 ASP B 37 0.009 50.579 2.327 1.00170.32 O
ANISOU 204 OD1 ASP B 37 27220 20887 16606 -2440 7042 648 O
ATOM 205 OD2 ASP B 37 -1.345 49.470 3.652 1.00165.78 O
ANISOU 205 OD2 ASP B 37 26094 20777 16118 -2130 6969 1248 O
ATOM 206 N ALA B 38 0.683 46.607 1.435 1.00125.54 N
ANISOU 206 N ALA B 38 19915 16088 11696 -2161 5095 1718 N
ATOM 207 CA ALA B 38 1.701 45.821 2.121 1.00124.00 C
ANISOU 207 CA ALA B 38 19412 16488 11213 -2537 4723 1721 C
ATOM 208 C ALA B 38 2.956 45.692 1.264 1.00121.13 C
ANISOU 208 C ALA B 38 19027 16142 10855 -2670 4464 1564 C
ATOM 209 O ALA B 38 4.069 45.836 1.761 1.00121.04 O
ANISOU 209 O ALA B 38 18970 16515 10506 -3124 4439 1322 O
ATOM 210 CB ALA B 38 1.160 44.449 2.483 1.00131.87 C
ANISOU 210 CB ALA B 38 19916 17766 12423 -2332 4246 2230 C
ATOM 211 N LEU B 39 2.765 45.428 -0.026 1.00135.18 N
ANISOU 211 N LEU B 39 20846 17499 13018 -2260 4273 1723 N
ATOM 212 CA LEU B 39 3.871 45.339 -0.975 1.00123.18 C
ANISOU 212 CA LEU B 39 19365 15914 11523 -2274 4126 1618 C
ATOM 213 C LEU B 39 4.589 46.675 -1.130 1.00117.90 C
ANISOU 213 C LEU B 39 19082 15080 10635 -2622 4648 1155 C
ATOM 214 O LEU B 39 5.781 46.716 -1.430 1.00117.23 O
ANISOU 214 O LEU B 39 18922 15163 10457 -2866 4616 1022 O
ATOM 215 CB LEU B 39 3.372 44.862 -2.340 1.00120.35 C
ANISOU 215 CB LEU B 39 19122 15042 11563 -1705 3855 1875 C
ATOM 216 CG LEU B 39 3.072 43.372 -2.494 1.00114.76 C
ANISOU 216 CG LEU B 39 18070 14450 11083 -1401 3203 2326 C
ATOM 217 CD1 LEU B 39 2.403 43.102 -3.830 1.00113.70 C
ANISOU 217 CD1 LEU B 39 18196 13698 11308 -861 2941 2527 C
ATOM 218 CD2 LEU B 39 4.349 42.562 -2.360 1.00113.42 C
ANISOU 218 CD2 LEU B 39 17618 14742 10732 -1564 2900 2371 C
ATOM 219 N THR B 40 3.853 47.765 -0.940 1.00119.95 N
ANISOU 219 N THR B 40 19751 14990 10833 -2634 5145 938 N
ATOM 220 CA THR B 40 4.434 49.099 -1.013 1.00121.57 C
ANISOU 220 CA THR B 40 20410 14967 10816 -2996 5668 487 C
ATOM 221 C THR B 40 5.351 49.330 0.181 1.00134.13 C
ANISOU 221 C THR B 40 21895 17091 11977 -3676 5692 216 C
ATOM 222 O THR B 40 6.488 49.788 0.028 1.00133.60 O
ANISOU 222 O THR B 40 21860 17113 11788 -4107 5767 -32 O
ATOM 223 CB THR B 40 3.347 50.189 -1.051 1.00125.26 C
ANISOU 223 CB THR B 40 21400 14894 11298 -2782 6207 341 C
ATOM 224 OG1 THR B 40 2.460 49.944 -2.150 1.00122.37 O
ANISOU 224 OG1 THR B 40 21095 14057 11345 -2146 6098 625 O
ATOM 225 CG2 THR B 40 3.973 51.566 -1.206 1.00144.99 C
ANISOU 225 CG2 THR B 40 24449 17074 13568 -3158 6744 -125 C
ATOM 226 N LYS B 41 4.853 49.001 1.371 1.00139.47 N
ANISOU 226 N LYS B 41 22441 18121 12432 -3776 5614 290 N
ATOM 227 CA LYS B 41 5.658 49.105 2.585 1.00141.27 C
ANISOU 227 CA LYS B 41 22599 18880 12197 -4394 5536 61 C
ATOM 228 C LYS B 41 6.883 48.193 2.517 1.00135.17 C
ANISOU 228 C LYS B 41 21268 18644 11446 -4619 5002 200 C
ATOM 229 O LYS B 41 7.970 48.561 2.971 1.00146.64 O
ANISOU 229 O LYS B 41 22669 20414 12635 -5196 4946 -56 O
ATOM 230 CB LYS B 41 4.817 48.770 3.817 1.00143.88 C
ANISOU 230 CB LYS B 41 22914 19477 12277 -4342 5545 192 C
ATOM 231 CG LYS B 41 3.638 49.704 4.031 1.00139.00 C
ANISOU 231 CG LYS B 41 22831 18383 11601 -4105 6145 75 C
ATOM 232 CD LYS B 41 2.837 49.305 5.256 1.00134.07 C
ANISOU 232 CD LYS B 41 22158 18051 10731 -4012 6209 266 C
ATOM 233 CE LYS B 41 1.617 50.191 5.432 1.00137.32 C
ANISOU 233 CE LYS B 41 23055 17992 11129 -3674 6865 221 C
ATOM 234 NZ LYS B 41 0.816 49.786 6.619 1.00139.62 N
ANISOU 234 NZ LYS B 41 23288 18568 11193 -3534 7008 462 N
ATOM 235 N MET B 42 6.701 47.007 1.944 1.00133.58 N
ANISOU 235 N MET B 42 20659 18527 11569 -4157 4597 622 N
ATOM 236 CA MET B 42 7.797 46.059 1.768 1.00143.56 C
ANISOU 236 CA MET B 42 21410 20250 12887 -4227 4123 816 C
ATOM 237 C MET B 42 8.832 46.589 0.789 1.00125.05 C
ANISOU 237 C MET B 42 19099 17734 10680 -4362 4281 652 C
ATOM 238 O MET B 42 10.027 46.379 0.967 1.00123.23 O
ANISOU 238 O MET B 42 18501 17952 10368 -4706 4080 639 O
ATOM 239 CB MET B 42 7.280 44.704 1.279 1.00132.32 C
ANISOU 239 CB MET B 42 19679 18824 11773 -3647 3690 1298 C
ATOM 240 CG MET B 42 6.501 43.921 2.314 1.00118.77 C
ANISOU 240 CG MET B 42 17770 17410 9949 -3571 3448 1559 C
ATOM 241 SD MET B 42 6.139 42.239 1.781 1.00121.30 S
ANISOU 241 SD MET B 42 17712 17753 10622 -3013 2849 2130 S
ATOM 242 CE MET B 42 7.770 41.507 1.871 1.00116.21 C
ANISOU 242 CE MET B 42 16637 17703 9814 -3214 2458 2191 C
ATOM 243 N ARG B 43 8.363 47.265 -0.254 1.00120.83 N
ANISOU 243 N ARG B 43 18985 16553 10370 -4069 4650 564 N
ATOM 244 CA ARG B 43 9.254 47.859 -1.240 1.00127.19 C
ANISOU 244 CA ARG B 43 19904 17113 11307 -4161 4905 425 C
ATOM 245 C ARG B 43 10.081 48.958 -0.591 1.00133.94 C
ANISOU 245 C ARG B 43 20870 18123 11897 -4921 5188 18 C
ATOM 246 O ARG B 43 11.297 49.035 -0.783 1.00146.29 O
ANISOU 246 O ARG B 43 22136 19947 13499 -5272 5153 -14 O
ATOM 247 CB ARG B 43 8.461 48.416 -2.424 1.00130.97 C
ANISOU 247 CB ARG B 43 20911 16827 12026 -3670 5254 410 C
ATOM 248 N ALA B 44 9.409 49.802 0.186 1.00130.73 N
ANISOU 248 N ALA B 44 20900 17544 11229 -5172 5467 -276 N
ATOM 249 CA ALA B 44 10.072 50.892 0.891 1.00138.97 C
ANISOU 249 CA ALA B 44 22191 18651 11959 -5926 5702 -704 C
ATOM 250 C ALA B 44 11.118 50.365 1.868 1.00142.20 C
ANISOU 250 C ALA B 44 22062 19828 12140 -6479 5226 -692 C
ATOM 251 O ALA B 44 12.224 50.897 1.952 1.00151.86 O
ANISOU 251 O ALA B 44 23160 21225 13316 -7089 5224 -887 O
ATOM 252 CB ALA B 44 9.049 51.747 1.621 1.00143.83 C
ANISOU 252 CB ALA B 44 23443 18932 12276 -5981 6071 -985 C
ATOM 253 N ALA B 45 10.763 49.312 2.599 1.00140.76 N
ANISOU 253 N ALA B 45 21545 20101 11837 -6270 4806 -434 N
ATOM 254 CA ALA B 45 11.655 48.744 3.605 1.00150.16 C
ANISOU 254 CA ALA B 45 22251 22037 12765 -6727 4309 -389 C
ATOM 255 C ALA B 45 12.830 47.999 2.975 1.00137.22 C
ANISOU 255 C ALA B 45 19924 20788 11425 -6701 3979 -106 C
ATOM 256 O ALA B 45 13.932 47.986 3.522 1.00142.06 O
ANISOU 256 O ALA B 45 20136 21930 11910 -7246 3684 -154 O
ATOM 257 CB ALA B 45 10.881 47.818 4.527 1.00139.40 C
ANISOU 257 CB ALA B 45 20780 21001 11184 -6449 4007 -156 C
ATOM 258 N ALA B 46 12.590 47.377 1.826 1.00131.86 N
ANISOU 258 N ALA B 46 19124 19842 11134 -6047 4022 206 N
ATOM 259 CA ALA B 46 13.636 46.639 1.129 1.00142.54 C
ANISOU 259 CA ALA B 46 19901 21494 12764 -5883 3800 512 C
ATOM 260 C ALA B 46 14.619 47.601 0.476 1.00149.90 C
ANISOU 260 C ALA B 46 20824 22267 13864 -6288 4157 322 C
ATOM 261 O ALA B 46 15.824 47.350 0.449 1.00137.80 O
ANISOU 261 O ALA B 46 18712 21201 12445 -6549 3978 464 O
ATOM 262 CB ALA B 46 13.035 45.707 0.089 1.00145.94 C
ANISOU 262 CB ALA B 46 20354 21604 13494 -5040 3745 878 C
ATOM 263 N LEU B 47 14.097 48.705 -0.048 1.00151.78 N
ANISOU 263 N LEU B 47 21688 21842 14139 -6330 4679 33 N
ATOM 264 CA LEU B 47 14.936 49.719 -0.672 1.00164.56 C
ANISOU 264 CA LEU B 47 23391 23216 15919 -6744 5087 -154 C
ATOM 265 C LEU B 47 15.680 50.531 0.382 1.00172.89 C
ANISOU 265 C LEU B 47 24366 24603 16722 -7706 4998 -492 C
ATOM 266 O LEU B 47 16.762 51.059 0.122 1.00184.19 O
ANISOU 266 O LEU B 47 25527 26135 18324 -8215 5115 -539 O
ATOM 267 CB LEU B 47 14.097 50.644 -1.555 1.00168.44 C
ANISOU 267 CB LEU B 47 24648 22852 16500 -6456 5670 -347 C
ATOM 268 N ASP B 48 15.096 50.626 1.572 1.00183.38 N
ANISOU 268 N ASP B 48 25948 26086 17640 -7960 4787 -711 N
ATOM 269 CA ASP B 48 15.712 51.371 2.664 1.00200.25 C
ANISOU 269 CA ASP B 48 28145 28500 19439 -8870 4625 -1066 C
ATOM 270 C ASP B 48 16.983 50.674 3.137 1.00203.76 C
ANISOU 270 C ASP B 48 27715 29771 19935 -9262 4049 -838 C
ATOM 271 O ASP B 48 17.960 51.325 3.510 1.00216.52 O
ANISOU 271 O ASP B 48 29145 31603 21519 -10063 3927 -1029 O
ATOM 272 CB ASP B 48 14.730 51.535 3.825 1.00203.53 C
ANISOU 272 CB ASP B 48 29110 28877 19343 -8927 4556 -1315 C
ATOM 273 CG ASP B 48 15.081 52.703 4.724 1.00219.37 C
ANISOU 273 CG ASP B 48 31604 30805 20941 -9810 4598 -1814 C
ATOM 274 OD1 ASP B 48 14.661 53.838 4.414 1.00220.94 O
ANISOU 274 OD1 ASP B 48 32527 30327 21095 -9940 5130 -2148 O
ATOM 275 OD2 ASP B 48 15.776 52.488 5.739 1.00231.96 O
ANISOU 275 OD2 ASP B 48 32904 32991 22239 -10368 4076 -1873 O
ATOM 276 N ALA B 49 16.963 49.346 3.113 1.00187.87 N
ANISOU 276 N ALA B 49 25165 28201 18017 -8696 3676 -412 N
ATOM 277 CA ALA B 49 18.121 48.551 3.503 1.00176.73 C
ANISOU 277 CA ALA B 49 22882 27589 16677 -8913 3131 -118 C
ATOM 278 C ALA B 49 19.222 48.633 2.451 1.00182.67 C
ANISOU 278 C ALA B 49 23086 28387 17932 -8941 3331 112 C
ATOM 279 O ALA B 49 19.106 48.053 1.370 1.00166.66 O
ANISOU 279 O ALA B 49 20951 26144 16229 -8220 3567 430 O
ATOM 280 CB ALA B 49 17.716 47.103 3.734 1.00151.49 C
ANISOU 280 CB ALA B 49 19363 24769 13429 -8232 2732 286 C
ATOM 281 N SER B 64 32.750 47.464 -1.710 1.00224.23 N
ANISOU 281 N SER B 64 18317 38570 28309 -10573 3996 4493 N
ATOM 282 CA SER B 64 32.910 46.200 -1.002 1.00226.66 C
ANISOU 282 CA SER B 64 18070 39627 28424 -10077 3298 4799 C
ATOM 283 C SER B 64 32.275 45.049 -1.777 1.00221.22 C
ANISOU 283 C SER B 64 17863 38644 27545 -8669 3648 5058 C
ATOM 284 O SER B 64 31.181 45.193 -2.324 1.00210.87 O
ANISOU 284 O SER B 64 17674 36522 25926 -8223 4033 4718 O
ATOM 285 CB SER B 64 32.302 46.290 0.399 1.00222.02 C
ANISOU 285 CB SER B 64 17891 39225 27243 -10715 2401 4279 C
ATOM 286 N PRO B 65 32.966 43.900 -1.827 1.00229.14 N
ANISOU 286 N PRO B 65 18032 40297 28735 -7964 3490 5673 N
ATOM 287 CA PRO B 65 32.475 42.712 -2.535 1.00223.40 C
ANISOU 287 CA PRO B 65 17742 39316 27825 -6622 3760 5963 C
ATOM 288 C PRO B 65 31.311 42.041 -1.810 1.00223.99 C
ANISOU 288 C PRO B 65 18610 39237 27259 -6327 3158 5618 C
ATOM 289 O PRO B 65 30.494 41.375 -2.445 1.00221.91 O
ANISOU 289 O PRO B 65 19127 38434 26756 -5401 3407 5627 O
ATOM 290 CB PRO B 65 33.700 41.796 -2.567 1.00231.19 C
ANISOU 290 CB PRO B 65 17485 41146 29210 -6143 3677 6720 C
ATOM 291 CG PRO B 65 34.484 42.188 -1.366 1.00239.69 C
ANISOU 291 CG PRO B 65 17575 43058 30437 -7237 2919 6714 C
ATOM 292 CD PRO B 65 34.289 43.672 -1.220 1.00241.85 C
ANISOU 292 CD PRO B 65 18222 42915 30756 -8406 3028 6154 C
ATOM 293 N GLU B 66 31.245 42.215 -0.495 1.00224.93 N
ANISOU 293 N GLU B 66 18546 39816 27102 -7120 2368 5333 N
ATOM 294 CA GLU B 66 30.154 41.655 0.294 1.00213.91 C
ANISOU 294 CA GLU B 66 17873 38304 25101 -6930 1824 5019 C
ATOM 295 C GLU B 66 28.930 42.559 0.224 1.00215.65 C
ANISOU 295 C GLU B 66 19262 37678 24998 -7258 2068 4363 C
ATOM 296 O GLU B 66 27.797 42.082 0.149 1.00202.69 O
ANISOU 296 O GLU B 66 18452 35564 22996 -6694 2061 4190 O
ATOM 297 CB GLU B 66 30.585 41.459 1.749 1.00213.45 C
ANISOU 297 CB GLU B 66 17207 39077 24818 -7589 902 5003 C
ATOM 298 N MET B 67 29.169 43.866 0.246 1.00233.88 N
ANISOU 298 N MET B 67 21612 39790 27460 -8176 2283 4025 N
ATOM 299 CA MET B 67 28.094 44.847 0.173 1.00236.29 C
ANISOU 299 CA MET B 67 23004 39289 27486 -8517 2569 3414 C
ATOM 300 C MET B 67 27.395 44.790 -1.180 1.00234.23 C
ANISOU 300 C MET B 67 23480 38200 27317 -7658 3326 3447 C
ATOM 301 O MET B 67 26.191 45.013 -1.274 1.00231.56 O
ANISOU 301 O MET B 67 24113 37213 26656 -7463 3452 3070 O
ATOM 302 CB MET B 67 28.634 46.256 0.430 1.00242.51 C
ANISOU 302 CB MET B 67 23666 40025 28451 -9685 2658 3089 C
ATOM 303 N LYS B 68 28.158 44.485 -2.224 1.00238.91 N
ANISOU 303 N LYS B 68 23609 38822 28343 -7121 3827 3924 N
ATOM 304 CA LYS B 68 27.598 44.362 -3.563 1.00236.04 C
ANISOU 304 CA LYS B 68 23963 37688 28035 -6244 4524 4002 C
ATOM 305 C LYS B 68 26.711 43.124 -3.669 1.00234.16 C
ANISOU 305 C LYS B 68 24230 37274 27466 -5262 4266 4113 C
ATOM 306 O LYS B 68 25.770 43.091 -4.462 1.00229.93 O
ANISOU 306 O LYS B 68 24591 35984 26786 -4677 4596 3973 O
ATOM 307 CB LYS B 68 28.712 44.305 -4.609 1.00233.19 C
ANISOU 307 CB LYS B 68 22980 37436 28184 -5884 5152 4526 C
ATOM 308 N ASP B 69 27.012 42.113 -2.859 1.00251.87 N
ANISOU 308 N ASP B 69 25836 46090 23774 1539 3921 1148 N
ATOM 309 CA ASP B 69 26.261 40.861 -2.878 1.00250.52 C
ANISOU 309 CA ASP B 69 26238 45113 23837 2398 3730 1330 C
ATOM 310 C ASP B 69 24.979 40.955 -2.055 1.00244.19 C
ANISOU 310 C ASP B 69 26388 43488 22903 2192 3441 1750 C
ATOM 311 O ASP B 69 23.937 40.429 -2.449 1.00205.00 O
ANISOU 311 O ASP B 69 22176 37657 18057 2433 3526 1873 O
ATOM 312 CB ASP B 69 27.129 39.711 -2.367 1.00225.99 C
ANISOU 312 CB ASP B 69 22459 42365 21040 3371 3284 1333 C
ATOM 313 CG ASP B 69 28.215 39.322 -3.352 1.00223.35 C
ANISOU 313 CG ASP B 69 21254 42689 20919 3817 3626 873 C
ATOM 314 OD1 ASP B 69 28.597 40.174 -4.182 1.00225.69 O
ANISOU 314 OD1 ASP B 69 21231 43468 21051 3190 4187 582 O
ATOM 315 OD2 ASP B 69 28.687 38.166 -3.299 1.00227.09 O
ANISOU 315 OD2 ASP B 69 21372 43197 21715 4798 3341 802 O
ATOM 316 N PHE B 70 25.064 41.618 -0.907 1.00245.34 N
ANISOU 316 N PHE B 70 26482 43925 22811 1756 3095 1949 N
ATOM 317 CA PHE B 70 23.888 41.854 -0.080 1.00241.82 C
ANISOU 317 CA PHE B 70 26886 42825 22169 1490 2889 2313 C
ATOM 318 C PHE B 70 22.954 42.831 -0.783 1.00233.26 C
ANISOU 318 C PHE B 70 26448 41271 20911 734 3323 2203 C
ATOM 319 O PHE B 70 21.730 42.681 -0.737 1.00232.64 O
ANISOU 319 O PHE B 70 27161 40383 20847 728 3353 2405 O
ATOM 320 CB PHE B 70 24.288 42.389 1.295 1.00244.30 C
ANISOU 320 CB PHE B 70 26983 43641 22200 1221 2418 2489 C
ATOM 321 N ARG B 71 23.539 43.831 -1.440 1.00222.96 N
ANISOU 321 N ARG B 71 24791 40467 19458 91 3643 1888 N
ATOM 322 CA ARG B 71 22.754 44.770 -2.229 1.00196.86 C
ANISOU 322 CA ARG B 71 22099 36716 15982 -608 4030 1760 C
ATOM 323 C ARG B 71 22.163 44.059 -3.441 1.00188.61 C
ANISOU 323 C ARG B 71 21469 35039 15154 -196 4371 1657 C
ATOM 324 O ARG B 71 21.073 44.399 -3.892 1.00180.17 O
ANISOU 324 O ARG B 71 21169 33251 14038 -479 4525 1670 O
ATOM 325 CB ARG B 71 23.598 45.963 -2.681 1.00183.98 C
ANISOU 325 CB ARG B 71 20001 35762 14140 -1411 4283 1486 C
ATOM 326 CG ARG B 71 22.770 47.096 -3.258 1.00167.89 C
ANISOU 326 CG ARG B 71 18689 33234 11866 -2216 4547 1407 C
ATOM 327 CD ARG B 71 23.529 47.904 -4.293 1.00177.72 C
ANISOU 327 CD ARG B 71 19588 34956 12980 -2842 4985 1137 C
ATOM 328 NE ARG B 71 22.623 48.378 -5.334 1.00166.18 N
ANISOU 328 NE ARG B 71 18990 32575 11574 -3137 5223 1037 N
ATOM 329 CZ ARG B 71 22.979 49.162 -6.345 1.00167.42 C
ANISOU 329 CZ ARG B 71 19214 32594 11803 -3642 5480 838 C
ATOM 330 NH1 ARG B 71 24.234 49.575 -6.459 1.00171.96 N
ANISOU 330 NH1 ARG B 71 18968 34079 12290 -4031 5659 725 N
ATOM 331 NH2 ARG B 71 22.077 49.536 -7.243 1.00168.11 N
ANISOU 331 NH2 ARG B 71 20168 31665 12040 -3749 5550 776 N
ATOM 332 N HIS B 72 22.894 43.078 -3.967 1.00201.33 N
ANISOU 332 N HIS B 72 22567 36921 17009 500 4452 1519 N
ATOM 333 CA HIS B 72 22.397 42.252 -5.065 1.00207.06 C
ANISOU 333 CA HIS B 72 23681 37044 17948 1025 4698 1392 C
ATOM 334 C HIS B 72 21.152 41.490 -4.627 1.00195.54 C
ANISOU 334 C HIS B 72 22974 34615 16707 1425 4402 1704 C
ATOM 335 O HIS B 72 20.130 41.489 -5.322 1.00185.14 O
ANISOU 335 O HIS B 72 22363 32529 15451 1341 4560 1671 O
ATOM 336 CB HIS B 72 23.480 41.279 -5.543 1.00219.23 C
ANISOU 336 CB HIS B 72 24479 39102 19716 1802 4768 1162 C
ATOM 337 CG HIS B 72 23.035 40.365 -6.642 1.00219.18 C
ANISOU 337 CG HIS B 72 24874 38486 19917 2426 4964 986 C
ATOM 338 ND1 HIS B 72 22.558 40.827 -7.849 1.00213.34 N
ANISOU 338 ND1 HIS B 72 24634 37420 19007 2081 5409 755 N
ATOM 339 CD2 HIS B 72 23.002 39.012 -6.718 1.00221.58 C
ANISOU 339 CD2 HIS B 72 25196 38418 20576 3388 4726 994 C
ATOM 340 CE1 HIS B 72 22.247 39.800 -8.620 1.00209.67 C
ANISOU 340 CE1 HIS B 72 24468 36426 18770 2812 5437 606 C
ATOM 341 NE2 HIS B 72 22.507 38.689 -7.958 1.00216.23 N
ANISOU 341 NE2 HIS B 72 25011 37205 19942 3606 5027 741 N
ATOM 342 N GLY B 73 21.248 40.851 -3.464 1.00199.03 N
ANISOU 342 N GLY B 73 23257 35099 17267 1839 3957 2018 N
ATOM 343 CA GLY B 73 20.127 40.138 -2.882 1.00198.06 C
ANISOU 343 CA GLY B 73 23786 34130 17337 2149 3681 2391 C
ATOM 344 C GLY B 73 18.936 41.051 -2.672 1.00188.53 C
ANISOU 344 C GLY B 73 23268 32418 15945 1446 3782 2510 C
ATOM 345 O GLY B 73 17.806 40.701 -3.023 1.00177.50 O
ANISOU 345 O GLY B 73 22507 30176 14760 1530 3826 2601 O
ATOM 346 N PHE B 74 19.194 42.230 -2.110 1.00190.41 N
ANISOU 346 N PHE B 74 23362 33167 15819 765 3789 2477 N
ATOM 347 CA PHE B 74 18.152 43.235 -1.927 1.00185.26 C
ANISOU 347 CA PHE B 74 23321 32106 14965 91 3876 2510 C
ATOM 348 C PHE B 74 17.522 43.631 -3.259 1.00185.08 C
ANISOU 348 C PHE B 74 23756 31557 15009 -182 4223 2232 C
ATOM 349 O PHE B 74 16.329 43.904 -3.326 1.00187.14 O
ANISOU 349 O PHE B 74 24657 31125 15323 -403 4248 2286 O
ATOM 350 CB PHE B 74 18.712 44.477 -1.230 1.00192.40 C
ANISOU 350 CB PHE B 74 23955 33684 15462 -581 3797 2434 C
ATOM 351 CG PHE B 74 18.975 44.288 0.237 1.00196.59 C
ANISOU 351 CG PHE B 74 24289 34573 15834 -417 3395 2730 C
ATOM 352 CD1 PHE B 74 19.997 44.983 0.862 1.00200.79 C
ANISOU 352 CD1 PHE B 74 24281 35923 16088 -740 3198 2635 C
ATOM 353 CD2 PHE B 74 18.198 43.425 0.992 1.00193.06 C
ANISOU 353 CD2 PHE B 74 24217 33638 15499 33 3200 3114 C
ATOM 354 CE1 PHE B 74 20.245 44.817 2.210 1.00198.42 C
ANISOU 354 CE1 PHE B 74 23854 35947 15588 -565 2779 2891 C
ATOM 355 CE2 PHE B 74 18.441 43.255 2.345 1.00193.35 C
ANISOU 355 CE2 PHE B 74 24147 34011 15306 184 2836 3412 C
ATOM 356 CZ PHE B 74 19.466 43.953 2.953 1.00197.37 C
ANISOU 356 CZ PHE B 74 24154 35336 15501 -92 2607 3287 C
ATOM 357 N ASP B 75 18.329 43.655 -4.316 1.00174.02 N
ANISOU 357 N ASP B 75 22020 30504 13594 -150 4487 1928 N
ATOM 358 CA ASP B 75 17.848 44.023 -5.644 1.00157.80 C
ANISOU 358 CA ASP B 75 20427 28007 11522 -389 4811 1658 C
ATOM 359 C ASP B 75 16.904 42.968 -6.198 1.00147.23 C
ANISOU 359 C ASP B 75 19601 25781 10558 201 4761 1700 C
ATOM 360 O ASP B 75 15.852 43.294 -6.750 1.00136.48 O
ANISOU 360 O ASP B 75 18899 23712 9245 -34 4816 1632 O
ATOM 361 CB ASP B 75 19.018 44.233 -6.608 1.00171.94 C
ANISOU 361 CB ASP B 75 21705 30471 13152 -467 5157 1345 C
ATOM 362 CG ASP B 75 19.588 45.634 -6.537 1.00171.00 C
ANISOU 362 CG ASP B 75 21370 30945 12656 -1351 5306 1238 C
ATOM 363 OD1 ASP B 75 18.838 46.560 -6.166 1.00162.77 O
ANISOU 363 OD1 ASP B 75 20855 29378 11613 -1889 5125 1287 O
ATOM 364 OD2 ASP B 75 20.783 45.810 -6.856 1.00160.57 O
ANISOU 364 OD2 ASP B 75 19365 30424 11220 -1464 5527 1073 O
ATOM 365 N ILE B 76 17.291 41.705 -6.059 1.00152.42 N
ANISOU 365 N ILE B 76 19955 26451 11505 974 4607 1796 N
ATOM 366 CA ILE B 76 16.426 40.602 -6.459 1.00156.17 C
ANISOU 366 CA ILE B 76 20898 26046 12396 1558 4472 1869 C
ATOM 367 C ILE B 76 15.114 40.669 -5.678 1.00156.72 C
ANISOU 367 C ILE B 76 21504 25420 12622 1343 4264 2197 C
ATOM 368 O ILE B 76 14.025 40.468 -6.233 1.00155.58 O
ANISOU 368 O ILE B 76 21935 24445 12734 1364 4252 2165 O
ATOM 369 CB ILE B 76 17.111 39.240 -6.228 1.00165.76 C
ANISOU 369 CB ILE B 76 21690 27388 13904 2428 4250 1962 C
ATOM 370 CG1 ILE B 76 18.500 39.235 -6.870 1.00176.55 C
ANISOU 370 CG1 ILE B 76 22377 29596 15108 2650 4483 1610 C
ATOM 371 CG2 ILE B 76 16.257 38.108 -6.777 1.00167.16 C
ANISOU 371 CG2 ILE B 76 22381 26597 14537 3009 4087 1993 C
ATOM 372 CD1 ILE B 76 19.342 38.030 -6.508 1.00184.33 C
ANISOU 372 CD1 ILE B 76 22825 30857 16357 3512 4217 1661 C
ATOM 373 N LEU B 77 15.233 40.973 -4.387 1.00153.24 N
ANISOU 373 N LEU B 77 20853 25354 12016 1134 4103 2492 N
ATOM 374 CA LEU B 77 14.077 41.122 -3.509 1.00145.77 C
ANISOU 374 CA LEU B 77 20338 23914 11136 899 3974 2806 C
ATOM 375 C LEU B 77 13.117 42.196 -4.020 1.00138.31 C
ANISOU 375 C LEU B 77 19901 22552 10098 285 4147 2594 C
ATOM 376 O LEU B 77 11.925 41.941 -4.192 1.00125.25 O
ANISOU 376 O LEU B 77 18724 20114 8754 313 4111 2666 O
ATOM 377 CB LEU B 77 14.531 41.462 -2.088 1.00153.43 C
ANISOU 377 CB LEU B 77 20996 25511 11789 731 3808 3082 C
ATOM 378 CG LEU B 77 13.662 40.917 -0.955 1.00139.90 C
ANISOU 378 CG LEU B 77 19565 23401 10191 873 3625 3551 C
ATOM 379 CD1 LEU B 77 13.719 39.403 -0.964 1.00147.78 C
ANISOU 379 CD1 LEU B 77 20533 24013 11604 1608 3421 3823 C
ATOM 380 CD2 LEU B 77 14.105 41.467 0.393 1.00141.13 C
ANISOU 380 CD2 LEU B 77 19500 24224 9898 635 3479 3756 C
ATOM 381 N VAL B 78 13.651 43.392 -4.261 1.00150.98 N
ANISOU 381 N VAL B 78 21390 24670 11307 -272 4301 2333 N
ATOM 382 CA VAL B 78 12.874 44.519 -4.774 1.00144.38 C
ANISOU 382 CA VAL B 78 21049 23472 10338 -867 4415 2105 C
ATOM 383 C VAL B 78 12.231 44.181 -6.115 1.00128.67 C
ANISOU 383 C VAL B 78 19515 20756 8619 -690 4500 1882 C
ATOM 384 O VAL B 78 11.095 44.572 -6.384 1.00127.29 O
ANISOU 384 O VAL B 78 19870 19914 8581 -910 4456 1809 O
ATOM 385 CB VAL B 78 13.750 45.784 -4.933 1.00145.87 C
ANISOU 385 CB VAL B 78 21023 24271 10131 -1459 4521 1860 C
ATOM 386 CG1 VAL B 78 12.972 46.902 -5.618 1.00153.09 C
ANISOU 386 CG1 VAL B 78 22418 24467 11283 -1799 4436 1597 C
ATOM 387 CG2 VAL B 78 14.268 46.249 -3.581 1.00130.70 C
ANISOU 387 CG2 VAL B 78 18738 22837 8086 -1635 4308 2001 C
ATOM 388 N GLY B 79 12.961 43.450 -6.951 1.00124.92 N
ANISOU 388 N GLY B 79 18829 20419 8217 -257 4598 1744 N
ATOM 389 CA GLY B 79 12.448 43.029 -8.242 1.00127.72 C
ANISOU 389 CA GLY B 79 19630 20115 8783 -6 4646 1506 C
ATOM 390 C GLY B 79 11.225 42.145 -8.098 1.00121.48 C
ANISOU 390 C GLY B 79 19221 18414 8521 363 4399 1680 C
ATOM 391 O GLY B 79 10.191 42.383 -8.731 1.00118.14 O
ANISOU 391 O GLY B 79 19346 17269 8273 221 4335 1533 O
ATOM 392 N GLN B 80 11.342 41.123 -7.254 1.00132.53 N
ANISOU 392 N GLN B 80 20330 19832 10192 823 4233 2006 N
ATOM 393 CA GLN B 80 10.219 40.230 -6.989 1.00128.53 C
ANISOU 393 CA GLN B 80 20130 18484 10221 1119 4005 2250 C
ATOM 394 C GLN B 80 9.037 40.990 -6.384 1.00122.30 C
ANISOU 394 C GLN B 80 19644 17344 9483 605 3989 2373 C
ATOM 395 O GLN B 80 7.877 40.715 -6.710 1.00120.95 O
ANISOU 395 O GLN B 80 19859 16360 9736 633 3873 2366 O
ATOM 396 CB GLN B 80 10.651 39.090 -6.066 1.00136.18 C
ANISOU 396 CB GLN B 80 20748 19599 11396 1631 3826 2645 C
ATOM 397 CG GLN B 80 11.560 38.070 -6.734 1.00144.72 C
ANISOU 397 CG GLN B 80 21602 20775 12609 2310 3753 2499 C
ATOM 398 CD GLN B 80 12.024 36.989 -5.780 1.00153.14 C
ANISOU 398 CD GLN B 80 22352 21967 13868 2829 3506 2897 C
ATOM 399 OE1 GLN B 80 12.815 37.244 -4.872 1.00155.70 O
ANISOU 399 OE1 GLN B 80 22246 23033 13882 2761 3502 3074 O
ATOM 400 NE2 GLN B 80 11.532 35.772 -5.980 1.00159.37 N
ANISOU 400 NE2 GLN B 80 23384 21991 15177 3350 3247 3040 N
ATOM 401 N ILE B 81 9.339 41.953 -5.515 1.00120.78 N
ANISOU 401 N ILE B 81 19253 17767 8870 153 4088 2448 N
ATOM 402 CA ILE B 81 8.311 42.800 -4.913 1.00122.76 C
ANISOU 402 CA ILE B 81 19761 17790 9092 -318 4098 2492 C
ATOM 403 C ILE B 81 7.581 43.609 -5.980 1.00110.26 C
ANISOU 403 C ILE B 81 18652 15687 7553 -637 4110 2100 C
ATOM 404 O ILE B 81 6.370 43.801 -5.902 1.00107.62 O
ANISOU 404 O ILE B 81 18623 14756 7511 -774 4036 2088 O
ATOM 405 CB ILE B 81 8.904 43.767 -3.862 1.00141.47 C
ANISOU 405 CB ILE B 81 21866 20955 10932 -727 4165 2561 C
ATOM 406 CG1 ILE B 81 9.412 42.995 -2.645 1.00129.10 C
ANISOU 406 CG1 ILE B 81 19921 19821 9311 -416 4086 2990 C
ATOM 407 CG2 ILE B 81 7.865 44.787 -3.415 1.00138.87 C
ANISOU 407 CG2 ILE B 81 21849 20388 10528 -1197 4183 2480 C
ATOM 408 CD1 ILE B 81 9.959 43.878 -1.546 1.00119.30 C
ANISOU 408 CD1 ILE B 81 18453 19334 7543 -772 4085 3053 C
ATOM 409 N ASP B 82 8.322 44.072 -6.981 1.00123.57 N
ANISOU 409 N ASP B 82 20395 17609 8948 -748 4202 1784 N
ATOM 410 CA ASP B 82 7.751 44.878 -8.055 1.00119.88 C
ANISOU 410 CA ASP B 82 20447 16672 8429 -1055 4185 1424 C
ATOM 411 C ASP B 82 6.890 44.026 -8.977 1.00107.54 C
ANISOU 411 C ASP B 82 19263 14226 7373 -657 4017 1316 C
ATOM 412 O ASP B 82 5.864 44.483 -9.486 1.00104.91 O
ANISOU 412 O ASP B 82 19394 13243 7225 -835 3870 1119 O
ATOM 413 CB ASP B 82 8.858 45.567 -8.853 1.00110.18 C
ANISOU 413 CB ASP B 82 19129 15987 6746 -1298 4336 1170 C
ATOM 414 N ASP B 83 7.322 42.788 -9.191 1.00110.37 N
ANISOU 414 N ASP B 83 19425 14540 7968 -95 3988 1420 N
ATOM 415 CA ASP B 83 6.543 41.828 -9.963 1.00113.61 C
ANISOU 415 CA ASP B 83 20169 14085 8911 336 3764 1335 C
ATOM 416 C ASP B 83 5.201 41.575 -9.272 1.00127.11 C
ANISOU 416 C ASP B 83 21980 15148 11169 277 3576 1560 C
ATOM 417 O ASP B 83 4.124 41.714 -9.877 1.00119.33 O
ANISOU 417 O ASP B 83 21401 13413 10526 206 3382 1363 O
ATOM 418 CB ASP B 83 7.324 40.520 -10.131 1.00121.37 C
ANISOU 418 CB ASP B 83 20885 15176 10053 981 3734 1426 C
ATOM 419 CG ASP B 83 6.904 39.743 -11.360 1.00139.57 C
ANISOU 419 CG ASP B 83 23614 16718 12698 1420 3526 1151 C
ATOM 420 OD1 ASP B 83 5.729 39.863 -11.762 1.00123.72 O
ANISOU 420 OD1 ASP B 83 22043 13924 11039 1299 3305 1038 O
ATOM 421 OD2 ASP B 83 7.748 39.016 -11.926 1.00159.42 O
ANISOU 421 OD2 ASP B 83 26017 19421 15135 1912 3559 1017 O
ATOM 422 N ALA B 84 5.281 41.222 -7.992 1.00141.78 N
ANISOU 422 N ALA B 84 23452 17327 13091 297 3637 1973 N
ATOM 423 CA ALA B 84 4.094 40.997 -7.175 1.00122.80 C
ANISOU 423 CA ALA B 84 21058 14462 11139 193 3563 2250 C
ATOM 424 C ALA B 84 3.201 42.236 -7.143 1.00108.60 C
ANISOU 424 C ALA B 84 19490 12505 9267 -308 3589 2021 C
ATOM 425 O ALA B 84 1.975 42.131 -7.103 1.00109.11 O
ANISOU 425 O ALA B 84 19696 11930 9833 -366 3473 2026 O
ATOM 426 CB ALA B 84 4.494 40.595 -5.760 1.00128.47 C
ANISOU 426 CB ALA B 84 21367 15711 11735 241 3680 2738 C
ATOM 427 N LEU B 85 3.828 43.407 -7.168 1.00103.60 N
ANISOU 427 N LEU B 85 18878 12445 8039 -667 3718 1809 N
ATOM 428 CA LEU B 85 3.117 44.678 -7.123 1.00100.80 C
ANISOU 428 CA LEU B 85 18774 11976 7549 -1127 3701 1559 C
ATOM 429 C LEU B 85 2.351 44.907 -8.419 1.00 99.17 C
ANISOU 429 C LEU B 85 19071 10990 7618 -1126 3466 1172 C
ATOM 430 O LEU B 85 1.244 45.450 -8.410 1.00 97.41 O
ANISOU 430 O LEU B 85 19058 10289 7664 -1309 3327 1010 O
ATOM 431 CB LEU B 85 4.098 45.824 -6.865 1.00110.83 C
ANISOU 431 CB LEU B 85 19971 14021 8119 -1519 3845 1443 C
ATOM 432 CG LEU B 85 3.532 47.161 -6.389 1.00123.32 C
ANISOU 432 CG LEU B 85 21634 15646 9576 -1959 3764 1240 C
ATOM 433 CD1 LEU B 85 2.561 46.946 -5.244 1.00 98.67 C
ANISOU 433 CD1 LEU B 85 18427 12401 6661 -1949 3866 1480 C
ATOM 434 CD2 LEU B 85 4.664 48.082 -5.961 1.00161.94 C
ANISOU 434 CD2 LEU B 85 26018 21328 14185 -2169 3657 1155 C
ATOM 435 N LYS B 86 2.951 44.493 -9.532 1.00128.98 N
ANISOU 435 N LYS B 86 23042 14658 11309 -889 3410 1004 N
ATOM 436 CA LYS B 86 2.274 44.520 -10.821 1.00100.11 C
ANISOU 436 CA LYS B 86 19918 10228 7890 -797 3140 652 C
ATOM 437 C LYS B 86 1.047 43.621 -10.764 1.00104.91 C
ANISOU 437 C LYS B 86 20540 10023 9298 -526 2884 733 C
ATOM 438 O LYS B 86 -0.052 44.017 -11.175 1.00104.77 O
ANISOU 438 O LYS B 86 20830 9353 9623 -636 2624 495 O
ATOM 439 CB LYS B 86 3.216 44.072 -11.940 1.00114.50 C
ANISOU 439 CB LYS B 86 21917 12158 9430 -515 3178 485 C
ATOM 440 CG LYS B 86 2.611 44.133 -13.333 1.00113.81 C
ANISOU 440 CG LYS B 86 22472 11312 9460 -404 2885 101 C
ATOM 441 CD LYS B 86 3.582 43.611 -14.380 1.00104.84 C
ANISOU 441 CD LYS B 86 21494 10356 7983 -71 2987 -64 C
ATOM 442 CE LYS B 86 3.016 43.766 -15.784 1.00120.41 C
ANISOU 442 CE LYS B 86 24200 11608 9942 24 2688 -459 C
ATOM 443 NZ LYS B 86 3.928 43.198 -16.816 1.00108.97 N
ANISOU 443 NZ LYS B 86 22931 10347 8124 404 2823 -646 N
ATOM 444 N LEU B 87 1.237 42.415 -10.233 1.00122.09 N
ANISOU 444 N LEU B 87 22368 12225 11795 -183 2932 1078 N
ATOM 445 CA LEU B 87 0.129 41.472 -10.097 1.00114.33 C
ANISOU 445 CA LEU B 87 21347 10479 11614 24 2705 1228 C
ATOM 446 C LEU B 87 -1.018 42.020 -9.245 1.00112.28 C
ANISOU 446 C LEU B 87 20935 10059 11668 -317 2741 1320 C
ATOM 447 O LEU B 87 -2.189 41.857 -9.594 1.00113.70 O
ANISOU 447 O LEU B 87 21241 9490 12470 -311 2483 1182 O
ATOM 448 CB LEU B 87 0.626 40.153 -9.507 1.00131.25 C
ANISOU 448 CB LEU B 87 23151 12737 13982 393 2763 1656 C
ATOM 449 CG LEU B 87 1.402 39.267 -10.479 1.00123.13 C
ANISOU 449 CG LEU B 87 22289 11557 12937 890 2612 1511 C
ATOM 450 CD1 LEU B 87 1.897 38.009 -9.787 1.00127.99 C
ANISOU 450 CD1 LEU B 87 22574 12274 13783 1271 2620 1945 C
ATOM 451 CD2 LEU B 87 0.528 38.919 -11.675 1.00124.13 C
ANISOU 451 CD2 LEU B 87 22880 10720 13563 1078 2210 1159 C
ATOM 452 N ALA B 88 -0.679 42.662 -8.130 1.00109.19 N
ANISOU 452 N ALA B 88 20252 10384 10852 -593 3050 1523 N
ATOM 453 CA ALA B 88 -1.685 43.246 -7.249 1.00108.10 C
ANISOU 453 CA ALA B 88 19949 10217 10908 -886 3152 1578 C
ATOM 454 C ALA B 88 -2.397 44.407 -7.933 1.00118.23 C
ANISOU 454 C ALA B 88 21588 11141 12194 -1122 2943 1075 C
ATOM 455 O ALA B 88 -3.607 44.581 -7.787 1.00107.97 O
ANISOU 455 O ALA B 88 20244 9375 11406 -1204 2837 965 O
ATOM 456 CB ALA B 88 -1.048 43.705 -5.937 1.00105.19 C
ANISOU 456 CB ALA B 88 19262 10734 9971 -1086 3500 1860 C
ATOM 457 N ASN B 89 -1.634 45.197 -8.684 1.00120.49 N
ANISOU 457 N ASN B 89 22220 11644 11916 -1233 2879 777 N
ATOM 458 CA ASN B 89 -2.182 46.337 -9.407 1.00115.38 C
ANISOU 458 CA ASN B 89 22017 10634 11186 -1456 2628 317 C
ATOM 459 C ASN B 89 -3.141 45.900 -10.506 1.00108.75 C
ANISOU 459 C ASN B 89 21509 8843 10968 -1234 2208 47 C
ATOM 460 O ASN B 89 -4.072 46.626 -10.857 1.00106.02 O
ANISOU 460 O ASN B 89 21417 8010 10854 -1351 1925 -289 O
ATOM 461 CB ASN B 89 -1.054 47.187 -9.997 1.00100.29 C
ANISOU 461 CB ASN B 89 20432 9169 8504 -1663 2676 136 C
ATOM 462 CG ASN B 89 -0.575 48.260 -9.040 1.00100.26 C
ANISOU 462 CG ASN B 89 20271 9871 7950 -2046 2898 177 C
ATOM 463 OD1 ASN B 89 -1.374 48.875 -8.336 1.00127.04 O
ANISOU 463 OD1 ASN B 89 23590 13197 11483 -2204 2875 97 O
ATOM 464 ND2 ASN B 89 0.733 48.490 -9.007 1.00 93.92 N
ANISOU 464 ND2 ASN B 89 19397 9754 6534 -2187 3103 273 N
ATOM 465 N GLU B 90 -2.911 44.709 -11.050 1.00116.13 N
ANISOU 465 N GLU B 90 22452 9489 12184 -884 2115 167 N
ATOM 466 CA GLU B 90 -3.842 44.156 -12.028 1.00124.95 C
ANISOU 466 CA GLU B 90 23860 9665 13950 -643 1664 -79 C
ATOM 467 C GLU B 90 -5.184 43.820 -11.384 1.00125.93 C
ANISOU 467 C GLU B 90 23620 9318 14909 -675 1565 18 C
ATOM 468 O GLU B 90 -6.234 44.291 -11.827 1.00119.69 O
ANISOU 468 O GLU B 90 23008 7936 14534 -732 1220 -320 O
ATOM 469 CB GLU B 90 -3.268 42.908 -12.692 1.00136.54 C
ANISOU 469 CB GLU B 90 25419 10925 15533 -229 1571 12 C
ATOM 470 CG GLU B 90 -4.289 42.163 -13.538 1.00154.42 C
ANISOU 470 CG GLU B 90 27924 12177 18570 40 1063 -201 C
ATOM 471 CD GLU B 90 -3.680 41.051 -14.361 1.00171.62 C
ANISOU 471 CD GLU B 90 30325 14110 20774 490 902 -226 C
ATOM 472 OE1 GLU B 90 -2.436 40.973 -14.429 1.00174.32 O
ANISOU 472 OE1 GLU B 90 30676 15081 20478 606 1197 -143 O
ATOM 473 OE2 GLU B 90 -4.448 40.256 -14.942 1.00174.84 O
ANISOU 473 OE2 GLU B 90 30340 14232 21860 695 436 -331 O
ATOM 474 N GLY B 91 -5.145 42.996 -10.341 1.00146.79 N
ANISOU 474 N GLY B 91 25746 12229 17800 -640 1865 488 N
ATOM 475 CA GLY B 91 -6.354 42.577 -9.657 1.00147.83 C
ANISOU 475 CA GLY B 91 25467 11991 18711 -712 1872 663 C
ATOM 476 C GLY B 91 -6.340 41.105 -9.295 1.00150.69 C
ANISOU 476 C GLY B 91 25538 12143 19575 -511 1925 1132 C
ATOM 477 O GLY B 91 -7.332 40.572 -8.798 1.00159.50 O
ANISOU 477 O GLY B 91 26306 12886 21410 -592 1934 1339 O
ATOM 478 N LYS B 92 -5.216 40.443 -9.551 1.00148.41 N
ANISOU 478 N LYS B 92 25383 12082 18926 -252 1955 1297 N
ATOM 479 CA LYS B 92 -5.058 39.039 -9.197 1.00163.66 C
ANISOU 479 CA LYS B 92 27102 13813 21269 -18 1960 1753 C
ATOM 480 C LYS B 92 -4.484 38.906 -7.791 1.00161.37 C
ANISOU 480 C LYS B 92 26410 14303 20599 -138 2439 2299 C
ATOM 481 O LYS B 92 -3.268 38.841 -7.612 1.00160.17 O
ANISOU 481 O LYS B 92 26269 14759 19828 11 2597 2429 O
ATOM 482 CB LYS B 92 -4.158 38.324 -10.206 1.00181.90 C
ANISOU 482 CB LYS B 92 29764 15929 23420 412 1700 1609 C
ATOM 483 N VAL B 93 -5.368 38.871 -6.800 1.00156.37 N
ANISOU 483 N VAL B 93 25414 13668 20331 -401 2667 2606 N
ATOM 484 CA VAL B 93 -4.964 38.775 -5.401 1.00152.85 C
ANISOU 484 CA VAL B 93 24638 13939 19497 -533 3120 3138 C
ATOM 485 C VAL B 93 -4.178 37.490 -5.124 1.00142.04 C
ANISOU 485 C VAL B 93 23239 12577 18152 -236 3089 3635 C
ATOM 486 O VAL B 93 -3.050 37.534 -4.622 1.00137.52 O
ANISOU 486 O VAL B 93 22632 12704 16915 -124 3262 3828 O
ATOM 487 CB VAL B 93 -6.190 38.833 -4.466 1.00154.09 C
ANISOU 487 CB VAL B 93 24426 14010 20111 -853 3392 3387 C
ATOM 488 CG1 VAL B 93 -5.755 39.081 -3.030 1.00157.11 C
ANISOU 488 CG1 VAL B 93 24564 15265 19866 -1015 3892 3828 C
ATOM 489 CG2 VAL B 93 -7.156 39.916 -4.925 1.00143.17 C
ANISOU 489 CG2 VAL B 93 23061 12392 18944 -1051 3292 2829 C
ATOM 490 N LYS B 94 -4.775 36.351 -5.467 1.00144.51 N
ANISOU 490 N LYS B 94 23569 12076 19262 -98 2815 3819 N
ATOM 491 CA LYS B 94 -4.170 35.044 -5.215 1.00153.89 C
ANISOU 491 CA LYS B 94 24770 13107 20594 205 2706 4299 C
ATOM 492 C LYS B 94 -2.793 34.891 -5.868 1.00150.98 C
ANISOU 492 C LYS B 94 24637 13035 19693 645 2532 4079 C
ATOM 493 O LYS B 94 -1.853 34.380 -5.250 1.00147.28 O
ANISOU 493 O LYS B 94 24082 13012 18865 859 2625 4449 O
ATOM 494 CB LYS B 94 -5.100 33.932 -5.704 1.00157.11 C
ANISOU 494 CB LYS B 94 25229 12445 22018 268 2333 4414 C
ATOM 495 N GLU B 95 -2.679 35.338 -7.116 1.00160.68 N
ANISOU 495 N GLU B 95 26157 14033 20860 790 2282 3472 N
ATOM 496 CA GLU B 95 -1.427 35.226 -7.862 1.00149.17 C
ANISOU 496 CA GLU B 95 24903 12866 18907 1201 2167 3202 C
ATOM 497 C GLU B 95 -0.328 36.080 -7.234 1.00138.27 C
ANISOU 497 C GLU B 95 23334 12576 16625 1091 2543 3243 C
ATOM 498 O GLU B 95 0.832 35.655 -7.124 1.00137.04 O
ANISOU 498 O GLU B 95 23094 12877 16099 1417 2571 3356 O
ATOM 499 CB GLU B 95 -1.641 35.627 -9.323 1.00134.07 C
ANISOU 499 CB GLU B 95 23394 10492 17053 1314 1868 2552 C
ATOM 500 N ALA B 96 -0.704 37.287 -6.822 1.00133.62 N
ANISOU 500 N ALA B 96 22665 12384 15720 646 2794 3124 N
ATOM 501 CA ALA B 96 0.216 38.188 -6.141 1.00124.63 C
ANISOU 501 CA ALA B 96 21349 12235 13771 464 3113 3155 C
ATOM 502 C ALA B 96 0.701 37.562 -4.835 1.00137.95 C
ANISOU 502 C ALA B 96 22726 14391 15298 539 3291 3754 C
ATOM 503 O ALA B 96 1.885 37.649 -4.489 1.00144.55 O
ANISOU 503 O ALA B 96 23414 15940 15569 673 3383 3834 O
ATOM 504 CB ALA B 96 -0.450 39.533 -5.879 1.00119.70 C
ANISOU 504 CB ALA B 96 20738 11808 12934 -12 3285 2918 C
ATOM 505 N GLN B 97 -0.219 36.916 -4.122 1.00139.02 N
ANISOU 505 N GLN B 97 22763 14118 15940 445 3325 4185 N
ATOM 506 CA GLN B 97 0.137 36.229 -2.885 1.00145.68 C
ANISOU 506 CA GLN B 97 23404 15305 16642 513 3466 4819 C
ATOM 507 C GLN B 97 1.104 35.070 -3.154 1.00139.51 C
ANISOU 507 C GLN B 97 22663 14411 15931 1043 3192 5002 C
ATOM 508 O GLN B 97 2.018 34.826 -2.362 1.00142.29 O
ANISOU 508 O GLN B 97 22867 15352 15845 1207 3248 5330 O
ATOM 509 CB GLN B 97 -1.119 35.732 -2.161 1.00142.58 C
ANISOU 509 CB GLN B 97 22926 14432 16814 262 3590 5265 C
ATOM 510 CG GLN B 97 -2.051 36.859 -1.716 1.00135.10 C
ANISOU 510 CG GLN B 97 21862 13701 15769 -208 3907 5095 C
ATOM 511 CD GLN B 97 -3.229 36.376 -0.890 1.00137.96 C
ANISOU 511 CD GLN B 97 22049 13736 16634 -473 4133 5566 C
ATOM 512 OE1 GLN B 97 -4.335 36.202 -1.404 1.00135.23 O
ANISOU 512 OE1 GLN B 97 21671 12685 17024 -608 4035 5428 O
ATOM 513 NE2 GLN B 97 -3.001 36.174 0.403 1.00148.24 N
ANISOU 513 NE2 GLN B 97 23229 15569 17527 -562 4438 6125 N
ATOM 514 N ALA B 98 0.915 34.369 -4.271 1.00140.75 N
ANISOU 514 N ALA B 98 23034 13814 16630 1346 2858 4756 N
ATOM 515 CA ALA B 98 1.834 33.297 -4.664 1.00146.59 C
ANISOU 515 CA ALA B 98 23838 14408 17453 1926 2563 4813 C
ATOM 516 C ALA B 98 3.251 33.832 -4.888 1.00148.85 C
ANISOU 516 C ALA B 98 23986 15565 17004 2151 2655 4511 C
ATOM 517 O ALA B 98 4.251 33.324 -4.323 1.00153.10 O
ANISOU 517 O ALA B 98 24340 16562 17270 2477 2612 4778 O
ATOM 518 CB ALA B 98 1.322 32.607 -5.919 1.00144.77 C
ANISOU 518 CB ALA B 98 23910 13214 17883 2203 2180 4482 C
ATOM 519 N ALA B 99 3.324 34.871 -5.718 1.00141.99 N
ANISOU 519 N ALA B 99 23201 14912 15835 1961 2765 3958 N
ATOM 520 CA ALA B 99 4.579 35.577 -5.944 1.00143.76 C
ANISOU 520 CA ALA B 99 23259 16005 15359 2021 2924 3661 C
ATOM 521 C ALA B 99 5.216 35.976 -4.613 1.00148.65 C
ANISOU 521 C ALA B 99 23533 17491 15457 1837 3136 4028 C
ATOM 522 O ALA B 99 6.439 35.933 -4.464 1.00160.70 O
ANISOU 522 O ALA B 99 24799 19686 16573 2082 3149 4009 O
ATOM 523 CB ALA B 99 4.356 36.805 -6.819 1.00147.27 C
ANISOU 523 CB ALA B 99 23895 16528 15531 1665 3051 3124 C
ATOM 524 N ALA B 100 4.379 36.349 -3.646 1.00145.70 N
ANISOU 524 N ALA B 100 23144 17112 15102 1427 3291 4343 N
ATOM 525 CA ALA B 100 4.860 36.722 -2.318 1.00135.03 C
ANISOU 525 CA ALA B 100 21543 16535 13227 1252 3468 4697 C
ATOM 526 C ALA B 100 5.427 35.526 -1.563 1.00145.96 C
ANISOU 526 C ALA B 100 22808 17967 14681 1676 3292 5228 C
ATOM 527 O ALA B 100 6.368 35.673 -0.785 1.00143.53 O
ANISOU 527 O ALA B 100 22269 18402 13864 1753 3306 5400 O
ATOM 528 CB ALA B 100 3.748 37.367 -1.512 1.00130.34 C
ANISOU 528 CB ALA B 100 21000 15893 12630 757 3702 4870 C
ATOM 529 N GLU B 101 4.847 34.348 -1.768 1.00154.74 N
ANISOU 529 N GLU B 101 24099 18258 16436 1943 3079 5494 N
ATOM 530 CA GLU B 101 5.398 33.145 -1.151 1.00165.82 C
ANISOU 530 CA GLU B 101 25468 19589 17948 2390 2834 5995 C
ATOM 531 C GLU B 101 6.820 32.901 -1.671 1.00188.85 C
ANISOU 531 C GLU B 101 28187 22957 20611 2926 2635 5698 C
ATOM 532 O GLU B 101 7.781 32.699 -0.890 1.00194.52 O
ANISOU 532 O GLU B 101 28680 24279 20950 3165 2544 5949 O
ATOM 533 CB GLU B 101 4.501 31.935 -1.430 1.00166.77 C
ANISOU 533 CB GLU B 101 25857 18634 18875 2557 2590 6284 C
ATOM 534 CG GLU B 101 3.048 32.089 -0.994 1.00162.65 C
ANISOU 534 CG GLU B 101 25448 17634 18720 2025 2803 6566 C
ATOM 535 CD GLU B 101 2.847 31.893 0.496 1.00183.31 C
ANISOU 535 CD GLU B 101 28021 20543 21088 1801 2994 7276 C
ATOM 536 OE1 GLU B 101 2.214 30.886 0.877 1.00192.66 O
ANISOU 536 OE1 GLU B 101 29355 21074 22774 1800 2889 7816 O
ATOM 537 OE2 GLU B 101 3.306 32.747 1.284 1.00183.19 O
ANISOU 537 OE2 GLU B 101 27849 21391 20364 1608 3241 7301 O
ATOM 538 N GLN B 102 6.953 32.941 -2.997 1.00192.39 N
ANISOU 538 N GLN B 102 28710 23138 21252 3123 2569 5143 N
ATOM 539 CA GLN B 102 8.280 32.852 -3.610 1.00190.22 C
ANISOU 539 CA GLN B 102 28192 23379 20703 3594 2483 4767 C
ATOM 540 C GLN B 102 9.228 33.905 -3.019 1.00183.01 C
ANISOU 540 C GLN B 102 26887 23580 19069 3335 2716 4681 C
ATOM 541 O GLN B 102 10.415 33.635 -2.762 1.00191.51 O
ANISOU 541 O GLN B 102 27616 25258 19892 3717 2602 4686 O
ATOM 542 CB GLN B 102 8.188 33.020 -5.128 1.00187.97 C
ANISOU 542 CB GLN B 102 28091 22749 20579 3712 2495 4143 C
ATOM 543 CG GLN B 102 7.379 31.929 -5.817 1.00193.69 C
ANISOU 543 CG GLN B 102 29204 22362 22027 4045 2173 4142 C
ATOM 544 CD GLN B 102 7.362 32.059 -7.332 1.00192.38 C
ANISOU 544 CD GLN B 102 29276 21881 21940 4233 2142 3496 C
ATOM 545 OE1 GLN B 102 8.408 32.147 -7.977 1.00195.86 O
ANISOU 545 OE1 GLN B 102 29549 22833 22037 4578 2216 3104 O
ATOM 546 NE2 GLN B 102 6.166 32.057 -7.909 1.00191.25 N
ANISOU 546 NE2 GLN B 102 29519 20902 22245 4014 2031 3378 N
ATOM 547 N LEU B 103 8.682 35.099 -2.797 1.00171.60 N
ANISOU 547 N LEU B 103 25491 22379 17332 2695 3000 4585 N
ATOM 548 CA LEU B 103 9.416 36.205 -2.191 1.00167.56 C
ANISOU 548 CA LEU B 103 24671 22832 16164 2345 3190 4501 C
ATOM 549 C LEU B 103 9.953 35.811 -0.821 1.00168.40 C
ANISOU 549 C LEU B 103 24559 23409 16015 2497 3053 5007 C
ATOM 550 O LEU B 103 11.096 36.114 -0.479 1.00167.45 O
ANISOU 550 O LEU B 103 24061 24088 15475 2591 3006 4929 O
ATOM 551 CB LEU B 103 8.519 37.438 -2.078 1.00156.53 C
ANISOU 551 CB LEU B 103 23465 21428 14582 1667 3448 4359 C
ATOM 552 CG LEU B 103 9.192 38.713 -1.573 1.00146.94 C
ANISOU 552 CG LEU B 103 22008 21113 12709 1242 3610 4193 C
ATOM 553 CD1 LEU B 103 10.344 39.092 -2.486 1.00155.78 C
ANISOU 553 CD1 LEU B 103 22864 22735 13591 1324 3650 3746 C
ATOM 554 CD2 LEU B 103 8.185 39.849 -1.461 1.00134.06 C
ANISOU 554 CD2 LEU B 103 20636 19337 10965 642 3806 4041 C
ATOM 555 N LYS B 104 9.118 35.124 -0.047 1.00181.70 N
ANISOU 555 N LYS B 104 26490 24588 17961 2510 2975 5534 N
ATOM 556 CA LYS B 104 9.528 34.599 1.249 1.00196.52 C
ANISOU 556 CA LYS B 104 28284 26787 19597 2693 2807 6091 C
ATOM 557 C LYS B 104 10.708 33.652 1.110 1.00211.36 C
ANISOU 557 C LYS B 104 29925 28828 21554 3383 2446 6118 C
ATOM 558 O LYS B 104 11.658 33.716 1.902 1.00216.23 O
ANISOU 558 O LYS B 104 30263 30144 21751 3543 2290 6265 O
ATOM 559 CB LYS B 104 8.367 33.879 1.936 1.00192.43 C
ANISOU 559 CB LYS B 104 28122 25577 19416 2592 2815 6684 C
ATOM 560 N THR B 105 10.656 32.773 0.110 1.00223.34 N
ANISOU 560 N THR B 105 31550 29696 23613 3827 2275 5946 N
ATOM 561 CA THR B 105 11.764 31.826 -0.064 1.00235.73 C
ANISOU 561 CA THR B 105 32888 31382 25297 4569 1912 5917 C
ATOM 562 C THR B 105 13.095 32.532 -0.404 1.00241.52 C
ANISOU 562 C THR B 105 33068 33101 25597 4676 1989 5417 C
ATOM 563 O THR B 105 14.126 32.295 0.255 1.00247.36 O
ANISOU 563 O THR B 105 33451 34438 26097 5020 1746 5545 O
ATOM 564 CB THR B 105 11.445 30.757 -1.149 1.00240.56 C
ANISOU 564 CB THR B 105 33755 31076 26572 5068 1696 5745 C
ATOM 565 OG1 THR B 105 11.275 31.384 -2.425 1.00235.62 O
ANISOU 565 OG1 THR B 105 33142 30389 25994 4903 1951 5119 O
ATOM 566 CG2 THR B 105 10.174 29.987 -0.791 1.00240.62 C
ANISOU 566 CG2 THR B 105 34257 30083 27086 4935 1575 6272 C
ATOM 567 N THR B 106 13.078 33.403 -1.414 1.00236.13 N
ANISOU 567 N THR B 106 32310 32592 24818 4366 2310 4865 N
ATOM 568 CA THR B 106 14.310 34.098 -1.808 1.00230.86 C
ANISOU 568 CA THR B 106 31099 32850 23766 4381 2444 4404 C
ATOM 569 C THR B 106 14.841 34.995 -0.690 1.00232.07 C
ANISOU 569 C THR B 106 30933 33875 23370 3969 2474 4565 C
ATOM 570 O THR B 106 16.050 35.038 -0.437 1.00234.65 O
ANISOU 570 O THR B 106 30723 34963 23472 4214 2342 4452 O
ATOM 571 CB THR B 106 14.113 34.950 -3.080 1.00226.53 C
ANISOU 571 CB THR B 106 30624 32293 23152 4021 2813 3843 C
ATOM 572 OG1 THR B 106 13.031 35.871 -2.886 1.00220.15 O
ANISOU 572 OG1 THR B 106 30185 31232 22229 3310 3029 3913 O
ATOM 573 CG2 THR B 106 13.821 34.062 -4.280 1.00228.69 C
ANISOU 573 CG2 THR B 106 31172 31824 23894 4524 2740 3581 C
ATOM 574 N ARG B 107 13.932 35.703 -0.025 1.00227.74 N
ANISOU 574 N ARG B 107 30700 33210 22621 3367 2628 4799 N
ATOM 575 CA ARG B 107 14.268 36.487 1.160 1.00224.46 C
ANISOU 575 CA ARG B 107 30107 33507 21672 2997 2605 4988 C
ATOM 576 C ARG B 107 14.953 35.615 2.203 1.00234.24 C
ANISOU 576 C ARG B 107 31170 34997 22832 3509 2195 5422 C
ATOM 577 O ARG B 107 15.888 36.048 2.879 1.00238.95 O
ANISOU 577 O ARG B 107 31374 36392 23023 3485 2037 5403 O
ATOM 578 CB ARG B 107 13.013 37.127 1.759 1.00213.24 C
ANISOU 578 CB ARG B 107 29137 31771 20114 2412 2815 5213 C
ATOM 579 N ASN B 108 14.476 34.381 2.326 1.00239.89 N
ANISOU 579 N ASN B 108 32204 34989 23954 3965 1977 5819 N
ATOM 580 CA ASN B 108 15.058 33.434 3.267 1.00249.16 C
ANISOU 580 CA ASN B 108 33322 36255 25091 4502 1527 6279 C
ATOM 581 C ASN B 108 16.484 33.064 2.887 1.00255.87 C
ANISOU 581 C ASN B 108 33581 37648 25990 5111 1238 5952 C
ATOM 582 O ASN B 108 17.350 32.970 3.753 1.00263.73 O
ANISOU 582 O ASN B 108 34281 39225 26699 5354 898 6122 O
ATOM 583 CB ASN B 108 14.196 32.173 3.363 1.00248.43 C
ANISOU 583 CB ASN B 108 33747 35159 25487 4821 1347 6777 C
ATOM 584 N ALA B 109 16.733 32.858 1.597 1.00256.69 N
ANISOU 584 N ALA B 109 33503 37584 26445 5378 1366 5462 N
ATOM 585 CA ALA B 109 18.098 32.564 1.151 1.00264.61 C
ANISOU 585 CA ALA B 109 33860 39181 27500 5960 1179 5073 C
ATOM 586 C ALA B 109 19.034 33.758 1.379 1.00265.90 C
ANISOU 586 C ALA B 109 33405 40446 27181 5544 1328 4755 C
ATOM 587 O ALA B 109 20.198 33.592 1.764 1.00275.13 O
ANISOU 587 O ALA B 109 33991 42293 28255 5932 1026 4675 O
ATOM 588 CB ALA B 109 18.106 32.158 -0.317 1.00261.57 C
ANISOU 588 CB ALA B 109 33454 38411 27519 6304 1363 4581 C
ATOM 589 N TYR B 110 18.516 34.962 1.150 1.00255.50 N
ANISOU 589 N TYR B 110 32215 39273 25592 4752 1751 4571 N
ATOM 590 CA TYR B 110 19.319 36.180 1.271 1.00248.56 C
ANISOU 590 CA TYR B 110 30808 39344 24290 4249 1903 4254 C
ATOM 591 C TYR B 110 19.606 36.563 2.723 1.00250.38 C
ANISOU 591 C TYR B 110 30952 40086 24095 4053 1586 4594 C
ATOM 592 O TYR B 110 20.630 37.181 3.017 1.00252.30 O
ANISOU 592 O TYR B 110 30604 41181 24077 3914 1474 4378 O
ATOM 593 CB TYR B 110 18.624 37.346 0.561 1.00237.34 C
ANISOU 593 CB TYR B 110 29649 37813 22718 3470 2395 3963 C
ATOM 594 N ILE B 111 18.698 36.206 3.624 1.00251.47 N
ANISOU 594 N ILE B 111 31682 39712 24153 4023 1446 5120 N
ATOM 595 CA ILE B 111 18.894 36.480 5.044 1.00254.98 C
ANISOU 595 CA ILE B 111 32164 40591 24125 3895 1135 5477 C
ATOM 596 C ILE B 111 19.733 35.384 5.690 1.00267.10 C
ANISOU 596 C ILE B 111 33473 42273 25740 4669 559 5769 C
ATOM 597 O ILE B 111 20.521 35.645 6.600 1.00269.08 O
ANISOU 597 O ILE B 111 33424 43190 25626 4715 191 5841 O
ATOM 598 CB ILE B 111 17.557 36.601 5.793 1.00243.40 C
ANISOU 598 CB ILE B 111 31436 38584 22461 3515 1287 5933 C
ATOM 599 N GLN B 112 19.552 34.155 5.216 1.00276.16 N
ANISOU 599 N GLN B 112 34798 42755 27376 5293 426 5923 N
ATOM 600 CA GLN B 112 20.353 33.030 5.681 1.00289.33 C
ANISOU 600 CA GLN B 112 36278 44453 29203 6117 -167 6159 C
ATOM 601 C GLN B 112 21.790 33.196 5.214 1.00301.67 C
ANISOU 601 C GLN B 112 36931 46844 30844 6465 -327 5614 C
ATOM 602 O GLN B 112 22.720 32.700 5.851 1.00308.84 O
ANISOU 602 O GLN B 112 37481 48147 31718 7014 -878 5712 O
ATOM 603 CB GLN B 112 19.783 31.703 5.179 1.00288.96 C
ANISOU 603 CB GLN B 112 36668 43411 29712 6686 -281 6399 C
ATOM 604 N LYS B 113 21.962 33.887 4.090 1.00302.91 N
ANISOU 604 N LYS B 113 36713 47265 31113 6144 155 5043 N
ATOM 605 CA LYS B 113 23.291 34.240 3.613 1.00307.61 C
ANISOU 605 CA LYS B 113 36376 48756 31745 6303 144 4503 C
ATOM 606 C LYS B 113 24.015 35.057 4.677 1.00306.02 C
ANISOU 606 C LYS B 113 35764 49418 31091 5962 -150 4543 C
ATOM 607 O LYS B 113 25.128 34.723 5.082 1.00317.70 O
ANISOU 607 O LYS B 113 36613 51481 32618 6460 -617 4457 O
ATOM 608 CB LYS B 113 23.210 35.023 2.300 1.00304.27 C
ANISOU 608 CB LYS B 113 35751 48465 31391 5823 794 3964 C
ATOM 609 N TYR B 114 23.363 36.118 5.141 1.00285.93 N
ANISOU 609 N TYR B 114 33589 46930 28123 5141 82 4652 N
ATOM 610 CA TYR B 114 23.931 36.978 6.170 1.00267.41 C
ANISOU 610 CA TYR B 114 30966 45334 25305 4753 -211 4670 C
ATOM 611 C TYR B 114 23.232 36.780 7.511 1.00254.32 C
ANISOU 611 C TYR B 114 30029 43358 23244 4735 -539 5270 C
ATOM 612 O TYR B 114 22.586 37.693 8.026 1.00238.21 O
ANISOU 612 O TYR B 114 28392 41343 20775 4073 -354 5355 O
ATOM 613 CB TYR B 114 23.846 38.445 5.746 1.00255.39 C
ANISOU 613 CB TYR B 114 29296 44199 23542 3826 249 4283 C
ATOM 614 N THR B 118 20.046 38.339 15.936 1.00152.96 N
ANISOU 614 N THR B 118 19565 25743 12810 -7408 5287 2240 N
ATOM 615 CA THR B 118 19.485 39.279 16.899 1.00145.58 C
ANISOU 615 CA THR B 118 18733 24366 12213 -7558 4791 2551 C
ATOM 616 C THR B 118 18.174 38.754 17.478 1.00145.77 C
ANISOU 616 C THR B 118 19079 24051 12258 -7205 4401 2490 C
ATOM 617 O THR B 118 17.410 38.070 16.797 1.00141.10 O
ANISOU 617 O THR B 118 18852 23448 11311 -7006 4368 2383 O
ATOM 618 CB THR B 118 19.245 40.664 16.260 1.00180.47 C
ANISOU 618 CB THR B 118 23563 28493 16516 -8044 4540 3064 C
ATOM 619 OG1 THR B 118 20.411 41.069 15.530 1.00198.06 O
ANISOU 619 OG1 THR B 118 25558 31064 18633 -8387 4944 3117 O
ATOM 620 CG2 THR B 118 18.930 41.706 17.329 1.00159.49 C
ANISOU 620 CG2 THR B 118 20933 25356 14310 -8209 4110 3340 C
ATOM 621 N LEU B 119 17.923 39.068 18.744 1.00165.24 N
ANISOU 621 N LEU B 119 21397 26247 15140 -7145 4106 2544 N
ATOM 622 CA LEU B 119 16.696 38.656 19.413 1.00146.51 C
ANISOU 622 CA LEU B 119 19289 23431 12947 -6693 3649 2456 C
ATOM 623 C LEU B 119 15.988 39.877 19.992 1.00136.98 C
ANISOU 623 C LEU B 119 18351 21644 12049 -6853 3117 2833 C
ATOM 624 O LEU B 119 16.632 40.873 20.318 1.00147.73 O
ANISOU 624 O LEU B 119 19551 22934 13645 -7225 3112 3038 O
ATOM 625 CB LEU B 119 17.001 37.638 20.513 1.00137.07 C
ANISOU 625 CB LEU B 119 17631 22276 12174 -6110 3683 1991 C
ATOM 626 CG LEU B 119 15.830 36.905 21.167 1.00138.77 C
ANISOU 626 CG LEU B 119 18065 22096 12566 -5562 3307 1799 C
ATOM 627 CD1 LEU B 119 14.973 36.208 20.122 1.00131.60 C
ANISOU 627 CD1 LEU B 119 17616 21230 11157 -5502 3357 1747 C
ATOM 628 CD2 LEU B 119 16.336 35.906 22.197 1.00144.60 C
ANISOU 628 CD2 LEU B 119 18327 22929 13687 -5035 3410 1388 C
ATOM 629 N ARG B 120 14.666 39.802 20.116 1.00133.38 N
ANISOU 629 N ARG B 120 18298 20770 11611 -6581 2685 2912 N
ATOM 630 CA ARG B 120 13.888 40.924 20.632 1.00139.98 C
ANISOU 630 CA ARG B 120 19409 21018 12757 -6661 2197 3256 C
ATOM 631 C ARG B 120 14.196 41.210 22.097 1.00141.93 C
ANISOU 631 C ARG B 120 19312 20997 13618 -6474 2027 3065 C
ATOM 632 O ARG B 120 14.510 40.305 22.867 1.00129.77 O
ANISOU 632 O ARG B 120 17405 19620 12281 -6084 2114 2659 O
ATOM 633 CB ARG B 120 12.389 40.662 20.458 1.00127.69 C
ANISOU 633 CB ARG B 120 18277 19136 11103 -6354 1793 3344 C
ATOM 634 CG ARG B 120 11.975 40.353 19.031 1.00136.62 C
ANISOU 634 CG ARG B 120 19777 20551 11582 -6548 1886 3524 C
ATOM 635 CD ARG B 120 12.463 41.425 18.065 1.00136.21 C
ANISOU 635 CD ARG B 120 19922 20572 11261 -7097 1991 3975 C
ATOM 636 NE ARG B 120 12.180 41.084 16.672 1.00147.65 N
ANISOU 636 NE ARG B 120 21632 22286 12182 -7137 2049 4013 N
ATOM 637 CZ ARG B 120 12.632 41.776 15.631 1.00164.95 C
ANISOU 637 CZ ARG B 120 23955 24592 14126 -7470 2163 4277 C
ATOM 638 NH1 ARG B 120 13.392 42.845 15.826 1.00167.31 N
ANISOU 638 NH1 ARG B 120 24150 24745 14676 -7788 2239 4521 N
ATOM 639 NH2 ARG B 120 12.330 41.400 14.396 1.00154.42 N
ANISOU 639 NH2 ARG B 120 22865 23520 12287 -7509 2203 4288 N
ATOM 640 N VAL B 121 14.112 42.483 22.466 1.00150.74 N
ANISOU 640 N VAL B 121 20573 21691 15010 -6766 1785 3365 N
ATOM 641 CA VAL B 121 14.265 42.894 23.858 1.00137.04 C
ANISOU 641 CA VAL B 121 18605 19643 13822 -6640 1573 3190 C
ATOM 642 C VAL B 121 13.311 42.148 24.811 1.00123.13 C
ANISOU 642 C VAL B 121 16846 17630 12307 -6021 1281 2895 C
ATOM 643 O VAL B 121 13.754 41.651 25.856 1.00129.14 O
ANISOU 643 O VAL B 121 17231 18497 13338 -5765 1296 2551 O
ATOM 644 CB VAL B 121 14.061 44.423 24.013 1.00139.81 C
ANISOU 644 CB VAL B 121 19257 19446 14419 -7036 1331 3567 C
ATOM 645 CG1 VAL B 121 13.885 44.804 25.473 1.00122.97 C
ANISOU 645 CG1 VAL B 121 17005 16898 12818 -6839 1052 3342 C
ATOM 646 CG2 VAL B 121 15.222 45.180 23.389 1.00132.74 C
ANISOU 646 CG2 VAL B 121 18258 18793 13384 -7697 1645 3802 C
ATOM 647 N PRO B 122 12.007 42.049 24.462 1.00118.02 N
ANISOU 647 N PRO B 122 16600 16682 11559 -5788 1011 3043 N
ATOM 648 CA PRO B 122 11.115 41.363 25.406 1.00116.65 C
ANISOU 648 CA PRO B 122 16402 16282 11637 -5242 764 2763 C
ATOM 649 C PRO B 122 11.473 39.895 25.629 1.00127.08 C
ANISOU 649 C PRO B 122 17411 18017 12858 -4878 996 2347 C
ATOM 650 O PRO B 122 11.256 39.384 26.726 1.00154.89 O
ANISOU 650 O PRO B 122 20762 21424 16666 -4499 877 2071 O
ATOM 651 CB PRO B 122 9.740 41.484 24.741 1.00111.52 C
ANISOU 651 CB PRO B 122 16191 15351 10832 -5129 480 3030 C
ATOM 652 CG PRO B 122 9.854 42.657 23.841 1.00114.00 C
ANISOU 652 CG PRO B 122 16793 15533 10989 -5606 453 3514 C
ATOM 653 CD PRO B 122 11.249 42.599 23.320 1.00114.76 C
ANISOU 653 CD PRO B 122 16655 16111 10839 -6002 878 3483 C
ATOM 654 N ASP B 123 12.008 39.231 24.609 1.00135.09 N
ANISOU 654 N ASP B 123 18375 19487 13469 -4988 1339 2305 N
ATOM 655 CA ASP B 123 12.429 37.842 24.753 1.00136.70 C
ANISOU 655 CA ASP B 123 18295 20045 13600 -4634 1611 1909 C
ATOM 656 C ASP B 123 13.623 37.736 25.696 1.00142.28 C
ANISOU 656 C ASP B 123 18480 20969 14611 -4571 1773 1693 C
ATOM 657 O ASP B 123 13.754 36.762 26.437 1.00147.41 O
ANISOU 657 O ASP B 123 18880 21702 15425 -4143 1814 1387 O
ATOM 658 CB ASP B 123 12.772 37.231 23.392 1.00127.60 C
ANISOU 658 CB ASP B 123 17229 19320 11934 -4795 1988 1889 C
ATOM 659 CG ASP B 123 11.536 36.863 22.592 1.00128.18 C
ANISOU 659 CG ASP B 123 17761 19268 11673 -4729 1816 1968 C
ATOM 660 OD1 ASP B 123 10.892 35.846 22.926 1.00114.93 O
ANISOU 660 OD1 ASP B 123 16117 17507 10043 -4327 1748 1692 O
ATOM 661 OD2 ASP B 123 11.210 37.587 21.629 1.00144.61 O
ANISOU 661 OD2 ASP B 123 20167 21342 13434 -5099 1736 2322 O
ATOM 662 N ILE B 124 14.487 38.745 25.666 1.00135.91 N
ANISOU 662 N ILE B 124 17509 20255 13877 -5015 1849 1873 N
ATOM 663 CA ILE B 124 15.647 38.792 26.549 1.00134.90 C
ANISOU 663 CA ILE B 124 16848 20374 14034 -5038 1953 1700 C
ATOM 664 C ILE B 124 15.209 39.005 27.995 1.00143.76 C
ANISOU 664 C ILE B 124 17929 21132 15560 -4787 1569 1581 C
ATOM 665 O ILE B 124 15.680 38.314 28.908 1.00148.81 O
ANISOU 665 O ILE B 124 18192 21960 16390 -4465 1576 1322 O
ATOM 666 CB ILE B 124 16.626 39.906 26.135 1.00140.35 C
ANISOU 666 CB ILE B 124 17391 21236 14699 -5665 2115 1932 C
ATOM 667 CG1 ILE B 124 17.115 39.674 24.705 1.00156.15 C
ANISOU 667 CG1 ILE B 124 19420 23655 16253 -5936 2547 2043 C
ATOM 668 CG2 ILE B 124 17.806 39.965 27.090 1.00139.60 C
ANISOU 668 CG2 ILE B 124 16697 21437 14907 -5718 2174 1744 C
ATOM 669 CD1 ILE B 124 17.854 38.366 24.519 1.00159.28 C
ANISOU 669 CD1 ILE B 124 19400 24580 16540 -5600 2950 1709 C
ATOM 670 N LEU B 125 14.304 39.960 28.199 1.00146.89 N
ANISOU 670 N LEU B 125 18720 21011 16079 -4922 1243 1780 N
ATOM 671 CA LEU B 125 13.720 40.176 29.521 1.00137.62 C
ANISOU 671 CA LEU B 125 17583 19456 15249 -4676 903 1646 C
ATOM 672 C LEU B 125 13.058 38.894 30.019 1.00123.01 C
ANISOU 672 C LEU B 125 15716 17614 13408 -4087 848 1395 C
ATOM 673 O LEU B 125 13.161 38.542 31.196 1.00132.42 O
ANISOU 673 O LEU B 125 16697 18799 14818 -3818 726 1178 O
ATOM 674 CB LEU B 125 12.703 41.318 29.489 1.00131.10 C
ANISOU 674 CB LEU B 125 17226 18039 14548 -4843 611 1898 C
ATOM 675 CG LEU B 125 13.244 42.707 29.148 1.00145.19 C
ANISOU 675 CG LEU B 125 19111 19662 16394 -5432 625 2170 C
ATOM 676 CD1 LEU B 125 12.120 43.731 29.136 1.00149.56 C
ANISOU 676 CD1 LEU B 125 20155 19558 17114 -5478 332 2423 C
ATOM 677 CD2 LEU B 125 14.333 43.113 30.129 1.00152.60 C
ANISOU 677 CD2 LEU B 125 19661 20746 17572 -5666 643 1976 C
ATOM 678 N ALA B 126 12.392 38.195 29.104 1.00117.34 N
ANISOU 678 N ALA B 126 15236 16921 12427 -3924 939 1432 N
ATOM 679 CA ALA B 126 11.746 36.928 29.414 1.00111.15 C
ANISOU 679 CA ALA B 126 14477 16128 11626 -3423 927 1202 C
ATOM 680 C ALA B 126 12.775 35.883 29.827 1.00112.64 C
ANISOU 680 C ALA B 126 14229 16721 11848 -3163 1181 941 C
ATOM 681 O ALA B 126 12.504 35.046 30.684 1.00129.93 O
ANISOU 681 O ALA B 126 16338 18848 14181 -2746 1105 746 O
ATOM 682 CB ALA B 126 10.941 36.439 28.224 1.00108.41 C
ANISOU 682 CB ALA B 126 14469 15773 10950 -3402 991 1282 C
ATOM 683 N LEU B 127 13.954 35.936 29.214 1.00113.00 N
ANISOU 683 N LEU B 127 13983 17182 11768 -3401 1490 958 N
ATOM 684 CA LEU B 127 15.038 35.023 29.564 1.00113.59 C
ANISOU 684 CA LEU B 127 13570 17673 11916 -3141 1746 740 C
ATOM 685 C LEU B 127 15.543 35.297 30.976 1.00120.93 C
ANISOU 685 C LEU B 127 14154 18623 13173 -3053 1518 670 C
ATOM 686 O LEU B 127 15.712 34.372 31.777 1.00118.14 O
ANISOU 686 O LEU B 127 13574 18359 12954 -2615 1498 496 O
ATOM 687 CB LEU B 127 16.190 35.138 28.562 1.00115.53 C
ANISOU 687 CB LEU B 127 13539 18389 11968 -3452 2152 783 C
ATOM 688 CG LEU B 127 15.952 34.594 27.152 1.00119.94 C
ANISOU 688 CG LEU B 127 14364 19076 12132 -3498 2478 774 C
ATOM 689 CD1 LEU B 127 17.167 34.839 26.269 1.00117.31 C
ANISOU 689 CD1 LEU B 127 13722 19237 11613 -3852 2906 819 C
ATOM 690 CD2 LEU B 127 15.606 33.115 27.193 1.00114.93 C
ANISOU 690 CD2 LEU B 127 13772 18430 11468 -2953 2619 492 C
ATOM 691 N VAL B 128 15.784 36.571 31.275 1.00129.00 N
ANISOU 691 N VAL B 128 15158 19552 14306 -3489 1341 811 N
ATOM 692 CA VAL B 128 16.234 36.976 32.605 1.00124.45 C
ANISOU 692 CA VAL B 128 14299 18995 13993 -3504 1093 727 C
ATOM 693 C VAL B 128 15.239 36.540 33.682 1.00116.19 C
ANISOU 693 C VAL B 128 13471 17602 13074 -3087 801 606 C
ATOM 694 O VAL B 128 15.609 35.887 34.671 1.00123.69 O
ANISOU 694 O VAL B 128 14130 18729 14136 -2770 719 461 O
ATOM 695 CB VAL B 128 16.437 38.503 32.687 1.00119.78 C
ANISOU 695 CB VAL B 128 13791 18227 13493 -4093 944 878 C
ATOM 696 CG1 VAL B 128 16.707 38.936 34.120 1.00126.23 C
ANISOU 696 CG1 VAL B 128 14414 19002 14546 -4126 648 740 C
ATOM 697 CG2 VAL B 128 17.568 38.938 31.768 1.00115.48 C
ANISOU 697 CG2 VAL B 128 12958 18080 12837 -4556 1248 1002 C
ATOM 698 N ILE B 129 13.975 36.901 33.474 1.00111.16 N
ANISOU 698 N ILE B 129 13332 16492 12412 -3088 646 687 N
ATOM 699 CA ILE B 129 12.904 36.529 34.391 1.00107.86 C
ANISOU 699 CA ILE B 129 13145 15735 12102 -2725 409 582 C
ATOM 700 C ILE B 129 12.816 35.014 34.560 1.00111.20 C
ANISOU 700 C ILE B 129 13465 16316 12472 -2215 533 435 C
ATOM 701 O ILE B 129 12.733 34.520 35.679 1.00112.06 O
ANISOU 701 O ILE B 129 13475 16409 12693 -1917 396 316 O
ATOM 702 CB ILE B 129 11.542 37.071 33.919 1.00 99.51 C
ANISOU 702 CB ILE B 129 12586 14197 11027 -2784 269 714 C
ATOM 703 CG1 ILE B 129 11.546 38.601 33.935 1.00100.01 C
ANISOU 703 CG1 ILE B 129 12800 13988 11213 -3230 121 866 C
ATOM 704 CG2 ILE B 129 10.421 36.534 34.797 1.00 92.41 C
ANISOU 704 CG2 ILE B 129 11874 13006 10231 -2390 87 588 C
ATOM 705 CD1 ILE B 129 10.308 39.218 33.330 1.00 97.13 C
ANISOU 705 CD1 ILE B 129 12885 13168 10853 -3281 -12 1063 C
ATOM 706 N PHE B 130 12.846 34.281 33.450 1.00113.95 N
ANISOU 706 N PHE B 130 13860 16803 12634 -2130 802 442 N
ATOM 707 CA PHE B 130 12.807 32.820 33.494 1.00114.58 C
ANISOU 707 CA PHE B 130 13879 16980 12678 -1663 970 288 C
ATOM 708 C PHE B 130 13.945 32.255 34.335 1.00127.77 C
ANISOU 708 C PHE B 130 15064 18995 14489 -1415 1026 195 C
ATOM 709 O PHE B 130 13.757 31.300 35.091 1.00139.83 O
ANISOU 709 O PHE B 130 16561 20467 16102 -989 982 104 O
ATOM 710 CB PHE B 130 12.874 32.231 32.084 1.00115.25 C
ANISOU 710 CB PHE B 130 14070 17204 12516 -1690 1302 269 C
ATOM 711 CG PHE B 130 11.550 32.181 31.381 1.00105.76 C
ANISOU 711 CG PHE B 130 13356 15680 11148 -1738 1224 312 C
ATOM 712 CD1 PHE B 130 10.365 32.272 32.090 1.00101.51 C
ANISOU 712 CD1 PHE B 130 13075 14760 10734 -1607 926 323 C
ATOM 713 CD2 PHE B 130 11.492 32.035 30.005 1.00104.40 C
ANISOU 713 CD2 PHE B 130 13365 15627 10677 -1927 1450 340 C
ATOM 714 CE1 PHE B 130 9.147 32.220 31.438 1.00 99.95 C
ANISOU 714 CE1 PHE B 130 13259 14316 10403 -1652 833 373 C
ATOM 715 CE2 PHE B 130 10.279 31.984 29.350 1.00101.97 C
ANISOU 715 CE2 PHE B 130 13476 15078 10191 -1992 1333 392 C
ATOM 716 CZ PHE B 130 9.105 32.078 30.067 1.00102.66 C
ANISOU 716 CZ PHE B 130 13769 14796 10442 -1850 1012 416 C
ATOM 717 N ALA B 131 15.122 32.855 34.197 1.00132.01 N
ANISOU 717 N ALA B 131 15210 19896 15052 -1693 1112 244 N
ATOM 718 CA ALA B 131 16.300 32.406 34.928 1.00140.03 C
ANISOU 718 CA ALA B 131 15677 21320 16207 -1488 1141 187 C
ATOM 719 C ALA B 131 16.149 32.625 36.433 1.00147.45 C
ANISOU 719 C ALA B 131 16558 22173 17293 -1387 764 169 C
ATOM 720 O ALA B 131 16.296 31.683 37.225 1.00154.38 O
ANISOU 720 O ALA B 131 17275 23137 18247 -944 708 122 O
ATOM 721 CB ALA B 131 17.544 33.116 34.411 1.00150.18 C
ANISOU 721 CB ALA B 131 16532 23042 17490 -1891 1308 248 C
ATOM 722 N VAL B 132 15.848 33.861 36.830 1.00140.85 N
ANISOU 722 N VAL B 132 15881 21151 16486 -1796 515 209 N
ATOM 723 CA VAL B 132 15.737 34.166 38.257 1.00142.24 C
ANISOU 723 CA VAL B 132 16023 21268 16753 -1765 176 151 C
ATOM 724 C VAL B 132 14.577 33.400 38.907 1.00133.72 C
ANISOU 724 C VAL B 132 15302 19841 15665 -1342 62 97 C
ATOM 725 O VAL B 132 14.711 32.891 40.025 1.00141.17 O
ANISOU 725 O VAL B 132 16113 20891 16636 -1072 -103 57 O
ATOM 726 CB VAL B 132 15.575 35.688 38.514 1.00143.01 C
ANISOU 726 CB VAL B 132 16288 21155 16893 -2304 -30 158 C
ATOM 727 CG1 VAL B 132 16.881 36.417 38.223 1.00147.17 C
ANISOU 727 CG1 VAL B 132 16382 22083 17452 -2756 34 198 C
ATOM 728 CG2 VAL B 132 14.441 36.277 37.692 1.00137.20 C
ANISOU 728 CG2 VAL B 132 16075 19927 16127 -2468 10 236 C
ATOM 729 N VAL B 133 13.455 33.298 38.197 1.00123.81 N
ANISOU 729 N VAL B 133 14483 18202 14357 -1302 148 115 N
ATOM 730 CA VAL B 133 12.298 32.544 38.676 1.00116.38 C
ANISOU 730 CA VAL B 133 13869 16937 13412 -946 82 66 C
ATOM 731 C VAL B 133 12.649 31.065 38.793 1.00114.84 C
ANISOU 731 C VAL B 133 13510 16913 13211 -470 240 38 C
ATOM 732 O VAL B 133 12.155 30.367 39.680 1.00115.06 O
ANISOU 732 O VAL B 133 13647 16808 13261 -154 142 14 O
ATOM 733 CB VAL B 133 11.072 32.723 37.745 1.00110.56 C
ANISOU 733 CB VAL B 133 13568 15817 12621 -1033 139 101 C
ATOM 734 CG1 VAL B 133 9.977 31.710 38.067 1.00106.13 C
ANISOU 734 CG1 VAL B 133 13274 14996 12056 -666 136 42 C
ATOM 735 CG2 VAL B 133 10.527 34.140 37.849 1.00115.11 C
ANISOU 735 CG2 VAL B 133 14357 16117 13262 -1399 -55 150 C
ATOM 736 N PHE B 134 13.516 30.587 37.907 1.00121.38 N
ANISOU 736 N PHE B 134 14083 18022 14015 -414 509 47 N
ATOM 737 CA PHE B 134 13.950 29.200 37.983 1.00122.75 C
ANISOU 737 CA PHE B 134 14085 18325 14228 70 693 15 C
ATOM 738 C PHE B 134 14.790 28.958 39.230 1.00131.88 C
ANISOU 738 C PHE B 134 14849 19773 15488 297 504 65 C
ATOM 739 O PHE B 134 14.521 28.030 39.988 1.00139.49 O
ANISOU 739 O PHE B 134 15884 20627 16490 700 444 87 O
ATOM 740 CB PHE B 134 14.740 28.794 36.742 1.00113.85 C
ANISOU 740 CB PHE B 134 12751 17446 13060 84 1067 -21 C
ATOM 741 CG PHE B 134 15.363 27.432 36.848 1.00110.81 C
ANISOU 741 CG PHE B 134 12132 17196 12776 613 1285 -64 C
ATOM 742 CD1 PHE B 134 14.590 26.291 36.713 1.00106.97 C
ANISOU 742 CD1 PHE B 134 11997 16363 12285 966 1422 -141 C
ATOM 743 CD2 PHE B 134 16.718 27.292 37.094 1.00112.44 C
ANISOU 743 CD2 PHE B 134 11756 17861 13105 760 1352 -22 C
ATOM 744 CE1 PHE B 134 15.157 25.036 36.818 1.00108.42 C
ANISOU 744 CE1 PHE B 134 12005 16592 12596 1475 1639 -173 C
ATOM 745 CE2 PHE B 134 17.292 26.040 37.197 1.00113.11 C
ANISOU 745 CE2 PHE B 134 11612 18036 13327 1306 1555 -38 C
ATOM 746 CZ PHE B 134 16.510 24.910 37.059 1.00112.24 C
ANISOU 746 CZ PHE B 134 11907 17515 13224 1675 1708 -114 C
ATOM 747 N LEU B 135 15.808 29.788 39.440 1.00126.18 N
ANISOU 747 N LEU B 135 13712 19432 14796 14 399 100 N
ATOM 748 CA LEU B 135 16.673 29.625 40.608 1.00133.55 C
ANISOU 748 CA LEU B 135 14220 20726 15797 182 170 159 C
ATOM 749 C LEU B 135 15.884 29.739 41.917 1.00134.40 C
ANISOU 749 C LEU B 135 14611 20611 15844 233 -165 161 C
ATOM 750 O LEU B 135 15.889 28.814 42.744 1.00130.15 O
ANISOU 750 O LEU B 135 14036 20102 15311 654 -256 232 O
ATOM 751 CB LEU B 135 17.807 30.654 40.578 1.00135.76 C
ANISOU 751 CB LEU B 135 14024 21453 16105 -252 88 172 C
ATOM 752 CG LEU B 135 18.728 30.603 39.354 1.00151.92 C
ANISOU 752 CG LEU B 135 15711 23812 18199 -345 444 177 C
ATOM 753 CD1 LEU B 135 19.898 31.566 39.507 1.00157.63 C
ANISOU 753 CD1 LEU B 135 15901 25023 18970 -788 339 202 C
ATOM 754 CD2 LEU B 135 19.223 29.186 39.104 1.00150.83 C
ANISOU 754 CD2 LEU B 135 15319 23831 18158 257 708 193 C
ATOM 755 N VAL B 136 15.193 30.866 42.084 1.00136.35 N
ANISOU 755 N VAL B 136 15157 20616 16032 -185 -322 89 N
ATOM 756 CA VAL B 136 14.435 31.149 43.303 1.00134.11 C
ANISOU 756 CA VAL B 136 15148 20131 15675 -201 -599 44 C
ATOM 757 C VAL B 136 13.302 30.148 43.523 1.00124.79 C
ANISOU 757 C VAL B 136 14366 18582 14469 191 -527 59 C
ATOM 758 O VAL B 136 13.016 29.756 44.654 1.00135.28 O
ANISOU 758 O VAL B 136 15782 19896 15723 387 -697 82 O
ATOM 759 CB VAL B 136 13.849 32.578 43.274 1.00132.61 C
ANISOU 759 CB VAL B 136 15234 19676 15476 -703 -710 -62 C
ATOM 760 CG1 VAL B 136 13.004 32.846 44.516 1.00125.11 C
ANISOU 760 CG1 VAL B 136 14588 18502 14447 -697 -935 -155 C
ATOM 761 CG2 VAL B 136 14.966 33.603 43.158 1.00130.33 C
ANISOU 761 CG2 VAL B 136 14583 19719 15217 -1156 -791 -81 C
ATOM 762 N GLY B 137 12.666 29.733 42.435 1.00119.59 N
ANISOU 762 N GLY B 137 13949 17643 13847 269 -274 48 N
ATOM 763 CA GLY B 137 11.563 28.794 42.511 1.00117.09 C
ANISOU 763 CA GLY B 137 14004 16966 13518 572 -184 45 C
ATOM 764 C GLY B 137 12.026 27.405 42.895 1.00112.55 C
ANISOU 764 C GLY B 137 13292 16499 12974 1060 -100 137 C
ATOM 765 O GLY B 137 11.453 26.775 43.779 1.00109.65 O
ANISOU 765 O GLY B 137 13122 15969 12570 1295 -181 185 O
ATOM 766 N VAL B 138 13.071 26.926 42.231 1.00116.04 N
ANISOU 766 N VAL B 138 13396 17205 13491 1220 82 170 N
ATOM 767 CA VAL B 138 13.596 25.596 42.510 1.00125.16 C
ANISOU 767 CA VAL B 138 14397 18430 14728 1738 189 271 C
ATOM 768 C VAL B 138 14.172 25.516 43.919 1.00121.23 C
ANISOU 768 C VAL B 138 13648 18214 14202 1910 -119 423 C
ATOM 769 O VAL B 138 13.726 24.698 44.719 1.00123.90 O
ANISOU 769 O VAL B 138 14190 18373 14514 2222 -185 531 O
ATOM 770 CB VAL B 138 14.671 25.182 41.482 1.00134.53 C
ANISOU 770 CB VAL B 138 15218 19871 16027 1888 483 251 C
ATOM 771 CG1 VAL B 138 15.487 24.003 41.999 1.00138.41 C
ANISOU 771 CG1 VAL B 138 15416 20516 16659 2454 529 391 C
ATOM 772 CG2 VAL B 138 14.018 24.840 40.155 1.00142.34 C
ANISOU 772 CG2 VAL B 138 16543 20548 16993 1830 820 103 C
ATOM 773 N LEU B 139 15.144 26.370 44.231 1.00120.33 N
ANISOU 773 N LEU B 139 13103 18549 14069 1673 -317 442 N
ATOM 774 CA LEU B 139 15.779 26.326 45.548 1.00125.02 C
ANISOU 774 CA LEU B 139 13415 19495 14591 1797 -652 586 C
ATOM 775 C LEU B 139 14.789 26.669 46.662 1.00127.20 C
ANISOU 775 C LEU B 139 14100 19557 14672 1652 -899 565 C
ATOM 776 O LEU B 139 14.671 25.945 47.659 1.00115.16 O
ANISOU 776 O LEU B 139 12655 18045 13056 1958 -1045 721 O
ATOM 777 CB LEU B 139 16.978 27.275 45.595 1.00116.71 C
ANISOU 777 CB LEU B 139 11814 18985 13547 1468 -824 570 C
ATOM 778 CG LEU B 139 18.117 26.923 44.636 1.00117.23 C
ANISOU 778 CG LEU B 139 11363 19374 13803 1628 -575 606 C
ATOM 779 CD1 LEU B 139 19.301 27.855 44.837 1.00128.54 C
ANISOU 779 CD1 LEU B 139 12208 21389 15241 1265 -777 606 C
ATOM 780 CD2 LEU B 139 18.535 25.471 44.813 1.00111.78 C
ANISOU 780 CD2 LEU B 139 10498 18722 13251 2309 -468 788 C
ATOM 781 N GLY B 140 14.071 27.771 46.471 1.00115.63 N
ANISOU 781 N GLY B 140 12902 17887 13145 1195 -923 382 N
ATOM 782 CA GLY B 140 13.087 28.235 47.430 1.00108.96 C
ANISOU 782 CA GLY B 140 12438 16825 12135 1026 -1097 304 C
ATOM 783 C GLY B 140 11.999 27.224 47.724 1.00107.39 C
ANISOU 783 C GLY B 140 12654 16242 11906 1352 -976 370 C
ATOM 784 O GLY B 140 11.757 26.905 48.884 1.00123.51 O
ANISOU 784 O GLY B 140 14820 18325 13782 1474 -1140 453 O
ATOM 785 N ASN B 141 11.342 26.712 46.686 1.00106.27 N
ANISOU 785 N ASN B 141 12735 15743 11898 1458 -691 336 N
ATOM 786 CA ASN B 141 10.263 25.752 46.898 1.00108.85 C
ANISOU 786 CA ASN B 141 13456 15686 12215 1704 -559 381 C
ATOM 787 C ASN B 141 10.773 24.387 47.344 1.00112.40 C
ANISOU 787 C ASN B 141 13828 16193 12687 2188 -524 602 C
ATOM 788 O ASN B 141 10.046 23.647 47.998 1.00116.05 O
ANISOU 788 O ASN B 141 14593 16416 13084 2371 -502 698 O
ATOM 789 CB ASN B 141 9.409 25.589 45.640 1.00123.71 C
ANISOU 789 CB ASN B 141 15594 17195 14217 1635 -290 265 C
ATOM 790 CG ASN B 141 8.573 26.817 45.340 1.00128.72 C
ANISOU 790 CG ASN B 141 16403 17666 14838 1224 -340 105 C
ATOM 791 OD1 ASN B 141 7.666 27.165 46.096 1.00124.85 O
ANISOU 791 OD1 ASN B 141 16147 17012 14281 1126 -429 53 O
ATOM 792 ND2 ASN B 141 8.866 27.474 44.224 1.00132.14 N
ANISOU 792 ND2 ASN B 141 16728 18138 15339 996 -266 37 N
ATOM 793 N ALA B 142 12.008 24.043 46.989 1.00113.86 N
ANISOU 793 N ALA B 142 13603 16678 12979 2406 -502 699 N
ATOM 794 CA ALA B 142 12.596 22.812 47.509 1.00113.91 C
ANISOU 794 CA ALA B 142 13491 16751 13040 2915 -506 947 C
ATOM 795 C ALA B 142 12.764 22.943 49.015 1.00121.26 C
ANISOU 795 C ALA B 142 14379 17947 13747 2940 -860 1126 C
ATOM 796 O ALA B 142 12.476 22.012 49.772 1.00120.20 O
ANISOU 796 O ALA B 142 14455 17667 13549 3253 -889 1340 O
ATOM 797 CB ALA B 142 13.927 22.516 46.845 1.00114.68 C
ANISOU 797 CB ALA B 142 13086 17163 13325 3159 -410 1005 C
ATOM 798 N LEU B 143 13.218 24.117 49.443 1.00130.29 N
ANISOU 798 N LEU B 143 15280 19476 14750 2573 -1125 1033 N
ATOM 799 CA LEU B 143 13.402 24.388 50.863 1.00122.70 C
ANISOU 799 CA LEU B 143 14283 18827 13509 2506 -1484 1147 C
ATOM 800 C LEU B 143 12.065 24.443 51.603 1.00114.68 C
ANISOU 800 C LEU B 143 13811 17477 12286 2367 -1472 1085 C
ATOM 801 O LEU B 143 11.947 23.931 52.716 1.00121.32 O
ANISOU 801 O LEU B 143 14790 18402 12906 2531 -1631 1282 O
ATOM 802 CB LEU B 143 14.170 25.695 51.061 1.00121.25 C
ANISOU 802 CB LEU B 143 13742 19100 13228 2068 -1745 995 C
ATOM 803 CG LEU B 143 14.492 26.061 52.510 1.00131.87 C
ANISOU 803 CG LEU B 143 15016 20851 14236 1932 -2148 1068 C
ATOM 804 CD1 LEU B 143 15.242 24.933 53.191 1.00134.41 C
ANISOU 804 CD1 LEU B 143 15095 21472 14504 2430 -2330 1448 C
ATOM 805 CD2 LEU B 143 15.298 27.345 52.569 1.00131.23 C
ANISOU 805 CD2 LEU B 143 14574 21194 14095 1448 -2380 875 C
ATOM 806 N VAL B 144 11.064 25.060 50.981 1.00110.56 N
ANISOU 806 N VAL B 144 13579 16596 11832 2072 -1280 828 N
ATOM 807 CA VAL B 144 9.733 25.155 51.573 1.00108.18 C
ANISOU 807 CA VAL B 144 13742 15976 11384 1939 -1217 739 C
ATOM 808 C VAL B 144 9.111 23.772 51.722 1.00105.73 C
ANISOU 808 C VAL B 144 13723 15347 11102 2306 -1033 947 C
ATOM 809 O VAL B 144 8.552 23.449 52.767 1.00103.15 O
ANISOU 809 O VAL B 144 13656 14981 10555 2341 -1086 1052 O
ATOM 810 CB VAL B 144 8.792 26.050 50.737 1.00107.75 C
ANISOU 810 CB VAL B 144 13881 15595 11464 1604 -1045 453 C
ATOM 811 CG1 VAL B 144 7.365 25.964 51.264 1.00103.59 C
ANISOU 811 CG1 VAL B 144 13780 14732 10846 1542 -929 379 C
ATOM 812 CG2 VAL B 144 9.275 27.491 50.748 1.00126.36 C
ANISOU 812 CG2 VAL B 144 16045 18183 13784 1201 -1222 252 C
ATOM 813 N VAL B 145 9.214 22.960 50.674 1.00112.04 N
ANISOU 813 N VAL B 145 14500 15911 12160 2552 -797 997 N
ATOM 814 CA VAL B 145 8.713 21.591 50.714 1.00119.99 C
ANISOU 814 CA VAL B 145 15792 16560 13239 2891 -598 1182 C
ATOM 815 C VAL B 145 9.413 20.811 51.821 1.00109.87 C
ANISOU 815 C VAL B 145 14435 15496 11814 3241 -790 1532 C
ATOM 816 O VAL B 145 8.759 20.144 52.625 1.00106.47 O
ANISOU 816 O VAL B 145 14337 14874 11243 3342 -764 1708 O
ATOM 817 CB VAL B 145 8.908 20.874 49.360 1.00127.30 C
ANISOU 817 CB VAL B 145 16681 17226 14462 3094 -312 1134 C
ATOM 818 CG1 VAL B 145 8.776 19.367 49.521 1.00128.93 C
ANISOU 818 CG1 VAL B 145 17123 17099 14766 3511 -138 1364 C
ATOM 819 CG2 VAL B 145 7.908 21.393 48.338 1.00116.25 C
ANISOU 819 CG2 VAL B 145 15482 15539 13149 2761 -119 847 C
ATOM 820 N TRP B 146 10.740 20.915 51.860 1.00118.70 N
ANISOU 820 N TRP B 146 15097 17037 12964 3411 -987 1653 N
ATOM 821 CA TRP B 146 11.542 20.332 52.934 1.00122.86 C
ANISOU 821 CA TRP B 146 15461 17882 13340 3738 -1256 2017 C
ATOM 822 C TRP B 146 10.987 20.715 54.304 1.00126.17 C
ANISOU 822 C TRP B 146 16134 18456 13348 3507 -1489 2080 C
ATOM 823 O TRP B 146 10.810 19.864 55.172 1.00126.92 O
ANISOU 823 O TRP B 146 16456 18487 13280 3754 -1547 2396 O
ATOM 824 CB TRP B 146 13.003 20.785 52.810 1.00128.77 C
ANISOU 824 CB TRP B 146 15589 19189 14149 3806 -1497 2064 C
ATOM 825 CG TRP B 146 13.944 20.197 53.832 1.00138.35 C
ANISOU 825 CG TRP B 146 16536 20803 15230 4173 -1824 2469 C
ATOM 826 CD1 TRP B 146 13.696 19.159 54.682 1.00146.69 C
ANISOU 826 CD1 TRP B 146 17870 21700 16166 4526 -1880 2837 C
ATOM 827 CD2 TRP B 146 15.289 20.617 54.098 1.00144.02 C
ANISOU 827 CD2 TRP B 146 16636 22163 15921 4215 -2160 2576 C
ATOM 828 NE1 TRP B 146 14.799 18.912 55.465 1.00153.90 N
ANISOU 828 NE1 TRP B 146 18386 23122 16967 4813 -2253 3190 N
ATOM 829 CE2 TRP B 146 15.792 19.793 55.123 1.00148.92 C
ANISOU 829 CE2 TRP B 146 17176 23011 16397 4626 -2438 3026 C
ATOM 830 CE3 TRP B 146 16.117 21.610 53.566 1.00143.56 C
ANISOU 830 CE3 TRP B 146 16077 22523 15948 3923 -2256 2352 C
ATOM 831 CZ2 TRP B 146 17.083 19.932 55.629 1.00147.49 C
ANISOU 831 CZ2 TRP B 146 16392 23494 16155 4769 -2837 3252 C
ATOM 832 CZ3 TRP B 146 17.396 21.748 54.069 1.00146.48 C
ANISOU 832 CZ3 TRP B 146 15848 23541 16266 4028 -2622 2551 C
ATOM 833 CH2 TRP B 146 17.868 20.914 55.089 1.00144.28 C
ANISOU 833 CH2 TRP B 146 15463 23513 15846 4457 -2923 2993 C
ATOM 834 N VAL B 147 10.689 21.999 54.479 1.00132.60 N
ANISOU 834 N VAL B 147 16942 19449 13992 3028 -1595 1774 N
ATOM 835 CA VAL B 147 10.253 22.525 55.769 1.00130.30 C
ANISOU 835 CA VAL B 147 16865 19362 13282 2764 -1801 1753 C
ATOM 836 C VAL B 147 8.854 22.049 56.166 1.00133.85 C
ANISOU 836 C VAL B 147 17853 19382 13624 2728 -1555 1757 C
ATOM 837 O VAL B 147 8.650 21.570 57.281 1.00148.31 O
ANISOU 837 O VAL B 147 19906 21307 15137 2806 -1655 1993 O
ATOM 838 CB VAL B 147 10.289 24.070 55.771 1.00122.35 C
ANISOU 838 CB VAL B 147 15731 18582 12172 2254 -1929 1367 C
ATOM 839 CG1 VAL B 147 9.432 24.632 56.893 1.00124.71 C
ANISOU 839 CG1 VAL B 147 16389 18905 12089 1948 -1982 1219 C
ATOM 840 CG2 VAL B 147 11.727 24.564 55.883 1.00132.55 C
ANISOU 840 CG2 VAL B 147 16498 20443 13423 2206 -2267 1412 C
ATOM 841 N THR B 148 7.899 22.169 55.250 1.00117.64 N
ANISOU 841 N THR B 148 15992 16885 11822 2597 -1238 1515 N
ATOM 842 CA THR B 148 6.516 21.794 55.528 1.00114.48 C
ANISOU 842 CA THR B 148 16038 16097 11362 2513 -985 1481 C
ATOM 843 C THR B 148 6.324 20.279 55.613 1.00116.58 C
ANISOU 843 C THR B 148 16537 16056 11703 2881 -824 1830 C
ATOM 844 O THR B 148 5.347 19.808 56.194 1.00117.41 O
ANISOU 844 O THR B 148 17008 15933 11671 2825 -665 1909 O
ATOM 845 CB THR B 148 5.554 22.357 54.457 1.00108.97 C
ANISOU 845 CB THR B 148 15426 15045 10935 2269 -728 1140 C
ATOM 846 OG1 THR B 148 5.992 21.950 53.155 1.00118.28 O
ANISOU 846 OG1 THR B 148 16434 16053 12453 2439 -610 1136 O
ATOM 847 CG2 THR B 148 5.512 23.877 54.518 1.00103.78 C
ANISOU 847 CG2 THR B 148 14644 14584 10203 1893 -852 810 C
ATOM 848 N ALA B 149 7.255 19.521 55.037 1.00110.14 N
ANISOU 848 N ALA B 149 15511 15219 11118 3251 -841 2034 N
ATOM 849 CA ALA B 149 7.135 18.064 54.995 1.00110.46 C
ANISOU 849 CA ALA B 149 15790 14880 11301 3630 -659 2350 C
ATOM 850 C ALA B 149 7.198 17.442 56.390 1.00121.67 C
ANISOU 850 C ALA B 149 17415 16430 12385 3792 -824 2758 C
ATOM 851 O ALA B 149 6.523 16.448 56.657 1.00126.49 O
ANISOU 851 O ALA B 149 18411 16648 13003 3910 -622 2975 O
ATOM 852 CB ALA B 149 8.211 17.464 54.106 1.00121.15 C
ANISOU 852 CB ALA B 149 16844 16200 12988 4026 -629 2452 C
ATOM 853 N PHE B 150 8.009 18.022 57.270 1.00132.48 N
ANISOU 853 N PHE B 150 18538 18356 13440 3769 -1196 2872 N
ATOM 854 CA PHE B 150 8.111 17.536 58.639 1.00136.17 C
ANISOU 854 CA PHE B 150 19197 19038 13504 3884 -1405 3273 C
ATOM 855 C PHE B 150 6.768 17.607 59.366 1.00132.07 C
ANISOU 855 C PHE B 150 19159 18335 12686 3552 -1211 3197 C
ATOM 856 O PHE B 150 6.385 16.671 60.068 1.00135.19 O
ANISOU 856 O PHE B 150 19904 18547 12914 3694 -1136 3559 O
ATOM 857 CB PHE B 150 9.148 18.342 59.425 1.00139.18 C
ANISOU 857 CB PHE B 150 19214 20124 13545 3803 -1868 3321 C
ATOM 858 CG PHE B 150 10.560 18.156 58.956 1.00146.62 C
ANISOU 858 CG PHE B 150 19628 21349 14732 4164 -2100 3494 C
ATOM 859 CD1 PHE B 150 11.112 19.013 58.024 1.00143.22 C
ANISOU 859 CD1 PHE B 150 18779 21085 14555 4012 -2113 3145 C
ATOM 860 CD2 PHE B 150 11.341 17.135 59.464 1.00146.91 C
ANISOU 860 CD2 PHE B 150 19571 21497 14751 4661 -2299 4026 C
ATOM 861 CE1 PHE B 150 12.413 18.848 57.601 1.00140.02 C
ANISOU 861 CE1 PHE B 150 17842 20980 14378 4328 -2292 3295 C
ATOM 862 CE2 PHE B 150 12.645 16.963 59.044 1.00142.87 C
ANISOU 862 CE2 PHE B 150 18511 21274 14498 5028 -2499 4185 C
ATOM 863 CZ PHE B 150 13.182 17.819 58.110 1.00141.57 C
ANISOU 863 CZ PHE B 150 17903 21304 14582 4852 -2482 3805 C
ATOM 864 N GLU B 151 6.060 18.721 59.190 1.00121.79 N
ANISOU 864 N GLU B 151 17867 17074 11334 3117 -1113 2737 N
ATOM 865 CA GLU B 151 4.873 19.017 59.984 1.00125.34 C
ANISOU 865 CA GLU B 151 18681 17471 11469 2781 -946 2608 C
ATOM 866 C GLU B 151 3.572 18.831 59.215 1.00123.05 C
ANISOU 866 C GLU B 151 18616 16652 11487 2628 -525 2375 C
ATOM 867 O GLU B 151 2.511 19.268 59.667 1.00124.44 O
ANISOU 867 O GLU B 151 19002 16785 11493 2321 -341 2171 O
ATOM 868 CB GLU B 151 4.955 20.452 60.514 1.00127.32 C
ANISOU 868 CB GLU B 151 18796 18163 11418 2405 -1135 2247 C
ATOM 869 CG GLU B 151 6.257 20.782 61.219 1.00133.96 C
ANISOU 869 CG GLU B 151 19363 19592 11943 2465 -1592 2408 C
ATOM 870 CD GLU B 151 6.321 20.258 62.646 1.00160.86 C
ANISOU 870 CD GLU B 151 23027 23299 14794 2506 -1766 2782 C
ATOM 871 OE1 GLU B 151 5.882 19.116 62.906 1.00166.59 O
ANISOU 871 OE1 GLU B 151 24058 23737 15501 2728 -1598 3158 O
ATOM 872 OE2 GLU B 151 6.818 21.001 63.517 1.00163.93 O
ANISOU 872 OE2 GLU B 151 23330 24215 14739 2288 -2076 2701 O
ATOM 873 N ALA B 152 3.659 18.179 58.061 1.00118.14 N
ANISOU 873 N ALA B 152 17932 15649 11306 2838 -369 2395 N
ATOM 874 CA ALA B 152 2.546 18.136 57.119 1.00119.55 C
ANISOU 874 CA ALA B 152 18234 15388 11799 2657 -32 2120 C
ATOM 875 C ALA B 152 1.270 17.517 57.684 1.00127.57 C
ANISOU 875 C ALA B 152 19649 16119 12705 2496 256 2206 C
ATOM 876 O ALA B 152 0.178 18.002 57.423 1.00125.82 O
ANISOU 876 O ALA B 152 19478 15766 12561 2200 463 1909 O
ATOM 877 CB ALA B 152 2.968 17.398 55.862 1.00132.24 C
ANISOU 877 CB ALA B 152 19750 16665 13831 2916 76 2150 C
ATOM 878 N LYS B 153 1.398 16.449 58.457 1.00139.32 N
ANISOU 878 N LYS B 153 21403 17515 14019 2691 273 2632 N
ATOM 879 CA LYS B 153 0.216 15.774 58.983 1.00136.57 C
ANISOU 879 CA LYS B 153 21443 16879 13568 2512 577 2752 C
ATOM 880 C LYS B 153 -0.029 16.123 60.447 1.00141.55 C
ANISOU 880 C LYS B 153 22244 17883 13655 2335 513 2876 C
ATOM 881 O LYS B 153 -0.848 15.500 61.125 1.00133.85 O
ANISOU 881 O LYS B 153 21608 16753 12497 2202 747 3067 O
ATOM 882 CB LYS B 153 0.348 14.261 58.802 1.00136.15 C
ANISOU 882 CB LYS B 153 21663 16361 13707 2796 717 3150 C
ATOM 883 CG LYS B 153 0.415 13.845 57.339 1.00148.12 C
ANISOU 883 CG LYS B 153 23084 17462 15734 2913 860 2962 C
ATOM 884 CD LYS B 153 -0.059 12.418 57.137 1.00154.30 C
ANISOU 884 CD LYS B 153 24252 17645 16729 3001 1150 3206 C
ATOM 885 CE LYS B 153 -0.740 12.248 55.785 1.00148.59 C
ANISOU 885 CE LYS B 153 23524 16523 16411 2821 1403 2840 C
ATOM 886 NZ LYS B 153 -1.069 10.822 55.511 1.00140.04 N
ANISOU 886 NZ LYS B 153 22830 14817 15561 2901 1681 3040 N
ATOM 887 N ARG B 154 0.684 17.138 60.921 1.00144.23 N
ANISOU 887 N ARG B 154 22355 18725 13722 2299 208 2747 N
ATOM 888 CA ARG B 154 0.510 17.642 62.276 1.00130.77 C
ANISOU 888 CA ARG B 154 20799 17437 11451 2087 130 2771 C
ATOM 889 C ARG B 154 -0.222 18.987 62.256 1.00120.70 C
ANISOU 889 C ARG B 154 19409 16313 10139 1721 246 2222 C
ATOM 890 O ARG B 154 -0.984 19.304 63.171 1.00133.64 O
ANISOU 890 O ARG B 154 21251 18102 11422 1465 416 2119 O
ATOM 891 CB ARG B 154 1.868 17.777 62.971 1.00131.67 C
ANISOU 891 CB ARG B 154 20768 18039 11221 2284 -324 3032 C
ATOM 892 CG ARG B 154 1.838 18.509 64.302 1.00138.70 C
ANISOU 892 CG ARG B 154 21776 19451 11474 2015 -467 2965 C
ATOM 893 CD ARG B 154 3.225 18.990 64.696 1.00145.81 C
ANISOU 893 CD ARG B 154 22394 20891 12117 2124 -972 3057 C
ATOM 894 NE ARG B 154 3.182 19.941 65.802 1.00161.66 N
ANISOU 894 NE ARG B 154 24484 23405 13533 1779 -1109 2830 N
ATOM 895 CZ ARG B 154 4.247 20.567 66.290 1.00170.09 C
ANISOU 895 CZ ARG B 154 25326 25017 14284 1734 -1549 2809 C
ATOM 896 NH1 ARG B 154 5.446 20.343 65.769 1.00175.61 N
ANISOU 896 NH1 ARG B 154 25653 25846 15225 2034 -1892 3027 N
ATOM 897 NH2 ARG B 154 4.115 21.417 67.299 1.00161.17 N
ANISOU 897 NH2 ARG B 154 24330 24313 12593 1373 -1634 2549 N
ATOM 898 N THR B 155 0.005 19.772 61.205 1.00110.92 N
ANISOU 898 N THR B 155 17853 15017 9274 1707 177 1876 N
ATOM 899 CA THR B 155 -0.616 21.090 61.082 1.00105.27 C
ANISOU 899 CA THR B 155 17016 14382 8598 1411 267 1374 C
ATOM 900 C THR B 155 -1.202 21.338 59.689 1.00 99.16 C
ANISOU 900 C THR B 155 16066 13235 8373 1381 438 1109 C
ATOM 901 O THR B 155 -0.611 20.957 58.679 1.00110.23 O
ANISOU 901 O THR B 155 17312 14474 10096 1572 344 1196 O
ATOM 902 CB THR B 155 0.387 22.214 61.400 1.00104.73 C
ANISOU 902 CB THR B 155 16731 14742 8318 1339 -80 1179 C
ATOM 903 OG1 THR B 155 1.587 22.022 60.643 1.00103.45 O
ANISOU 903 OG1 THR B 155 16292 14628 8385 1578 -358 1331 O
ATOM 904 CG2 THR B 155 0.731 22.227 62.883 1.00124.67 C
ANISOU 904 CG2 THR B 155 19450 17706 10214 1255 -239 1333 C
ATOM 905 N ILE B 156 -2.357 21.996 59.651 1.00 95.54 N
ANISOU 905 N ILE B 156 15623 12672 8006 1146 687 784 N
ATOM 906 CA ILE B 156 -3.092 22.243 58.410 1.00 98.73 C
ANISOU 906 CA ILE B 156 15868 12754 8892 1092 841 557 C
ATOM 907 C ILE B 156 -2.388 23.258 57.502 1.00 92.28 C
ANISOU 907 C ILE B 156 14765 11988 8311 1106 609 330 C
ATOM 908 O ILE B 156 -2.318 23.082 56.276 1.00 91.62 O
ANISOU 908 O ILE B 156 14543 11685 8583 1176 598 320 O
ATOM 909 CB ILE B 156 -4.522 22.738 58.718 1.00 89.69 C
ANISOU 909 CB ILE B 156 14765 11532 7780 863 1155 291 C
ATOM 910 CG1 ILE B 156 -5.271 21.700 59.558 1.00 90.18 C
ANISOU 910 CG1 ILE B 156 15102 11543 7619 799 1430 525 C
ATOM 911 CG2 ILE B 156 -5.288 23.030 57.443 1.00 80.89 C
ANISOU 911 CG2 ILE B 156 13448 10134 7153 814 1257 88 C
ATOM 912 CD1 ILE B 156 -5.334 20.328 58.927 1.00 91.38 C
ANISOU 912 CD1 ILE B 156 15364 11373 7985 907 1509 836 C
ATOM 913 N ASN B 157 -1.871 24.322 58.110 1.00 95.18 N
ANISOU 913 N ASN B 157 15065 12642 8455 1005 436 141 N
ATOM 914 CA ASN B 157 -1.127 25.339 57.375 1.00104.03 C
ANISOU 914 CA ASN B 157 15938 13823 9765 970 215 -56 C
ATOM 915 C ASN B 157 0.031 24.728 56.591 1.00 94.48 C
ANISOU 915 C ASN B 157 14565 12643 8692 1177 10 185 C
ATOM 916 O ASN B 157 0.311 25.129 55.457 1.00 87.50 O
ANISOU 916 O ASN B 157 13485 11647 8115 1177 -44 86 O
ATOM 917 CB ASN B 157 -0.609 26.420 58.329 1.00103.65 C
ANISOU 917 CB ASN B 157 15891 14098 9393 800 45 -270 C
ATOM 918 CG ASN B 157 -1.716 27.318 58.850 1.00101.58 C
ANISOU 918 CG ASN B 157 15744 13753 9097 602 279 -622 C
ATOM 919 OD1 ASN B 157 -2.809 27.362 58.286 1.00 99.49 O
ANISOU 919 OD1 ASN B 157 15463 13197 9143 597 524 -728 O
ATOM 920 ND2 ASN B 157 -1.435 28.045 59.926 1.00116.45 N
ANISOU 920 ND2 ASN B 157 17732 15907 10606 437 205 -820 N
ATOM 921 N ALA B 158 0.692 23.749 57.203 1.00 99.55 N
ANISOU 921 N ALA B 158 15287 13437 9102 1365 -88 515 N
ATOM 922 CA ALA B 158 1.776 23.028 56.550 1.00110.00 C
ANISOU 922 CA ALA B 158 16446 14777 10571 1628 -239 765 C
ATOM 923 C ALA B 158 1.267 22.316 55.302 1.00101.27 C
ANISOU 923 C ALA B 158 15359 13261 9857 1728 -20 785 C
ATOM 924 O ALA B 158 1.951 22.285 54.285 1.00 97.47 O
ANISOU 924 O ALA B 158 14677 12744 9612 1836 -83 778 O
ATOM 925 CB ALA B 158 2.413 22.037 57.506 1.00116.02 C
ANISOU 925 CB ALA B 158 17320 15725 11036 1854 -362 1157 C
ATOM 926 N ILE B 159 0.065 21.749 55.384 1.00 95.72 N
ANISOU 926 N ILE B 159 14895 12274 9202 1660 248 793 N
ATOM 927 CA ILE B 159 -0.563 21.120 54.225 1.00 97.52 C
ANISOU 927 CA ILE B 159 15160 12122 9771 1675 452 761 C
ATOM 928 C ILE B 159 -0.764 22.143 53.111 1.00 85.32 C
ANISOU 928 C ILE B 159 13399 10539 8480 1518 421 463 C
ATOM 929 O ILE B 159 -0.356 21.916 51.963 1.00 93.98 O
ANISOU 929 O ILE B 159 14389 11522 9799 1594 411 451 O
ATOM 930 CB ILE B 159 -1.927 20.483 54.581 1.00 91.72 C
ANISOU 930 CB ILE B 159 14681 11135 9035 1542 737 786 C
ATOM 931 CG1 ILE B 159 -1.751 19.407 55.647 1.00 88.77 C
ANISOU 931 CG1 ILE B 159 14571 10756 8402 1682 787 1135 C
ATOM 932 CG2 ILE B 159 -2.590 19.896 53.344 1.00 83.95 C
ANISOU 932 CG2 ILE B 159 13716 9791 8389 1494 914 712 C
ATOM 933 CD1 ILE B 159 -3.045 18.784 56.126 1.00 82.29 C
ANISOU 933 CD1 ILE B 159 14008 9718 7539 1505 1090 1186 C
ATOM 934 N TRP B 160 -1.387 23.269 53.457 1.00 81.48 N
ANISOU 934 N TRP B 160 12867 10138 7952 1307 418 228 N
ATOM 935 CA TRP B 160 -1.627 24.332 52.478 1.00 92.43 C
ANISOU 935 CA TRP B 160 14072 11464 9581 1165 373 -15 C
ATOM 936 C TRP B 160 -0.342 24.754 51.759 1.00 98.95 C
ANISOU 936 C TRP B 160 14691 12436 10469 1224 163 -6 C
ATOM 937 O TRP B 160 -0.222 24.637 50.526 1.00 92.42 O
ANISOU 937 O TRP B 160 13774 11484 9858 1236 178 -20 O
ATOM 938 CB TRP B 160 -2.256 25.563 53.144 1.00 97.23 C
ANISOU 938 CB TRP B 160 14668 12144 10129 985 384 -258 C
ATOM 939 CG TRP B 160 -3.584 25.358 53.849 1.00 85.80 C
ANISOU 939 CG TRP B 160 13364 10598 8639 903 631 -319 C
ATOM 940 CD1 TRP B 160 -4.001 25.988 54.986 1.00 77.02 C
ANISOU 940 CD1 TRP B 160 12331 9613 7319 807 711 -472 C
ATOM 941 CD2 TRP B 160 -4.663 24.489 53.457 1.00 95.06 C
ANISOU 941 CD2 TRP B 160 14602 11543 9974 881 852 -255 C
ATOM 942 NE1 TRP B 160 -5.261 25.566 55.330 1.00 83.14 N
ANISOU 942 NE1 TRP B 160 13192 10272 8125 746 988 -494 N
ATOM 943 CE2 TRP B 160 -5.690 24.647 54.411 1.00103.16 C
ANISOU 943 CE2 TRP B 160 15709 12594 10895 775 1066 -353 C
ATOM 944 CE3 TRP B 160 -4.859 23.595 52.399 1.00 79.04 C
ANISOU 944 CE3 TRP B 160 12572 9302 8156 911 902 -148 C
ATOM 945 CZ2 TRP B 160 -6.890 23.942 54.339 1.00119.90 C
ANISOU 945 CZ2 TRP B 160 17869 14553 13136 690 1318 -322 C
ATOM 946 CZ3 TRP B 160 -6.051 22.896 52.331 1.00 79.52 C
ANISOU 946 CZ3 TRP B 160 12704 9185 8323 807 1128 -135 C
ATOM 947 CH2 TRP B 160 -7.051 23.074 53.295 1.00 88.49 C
ANISOU 947 CH2 TRP B 160 13880 10368 9373 694 1329 -209 C
ATOM 948 N PHE B 161 0.617 25.239 52.542 1.00100.88 N
ANISOU 948 N PHE B 161 14854 12977 10498 1232 -29 11 N
ATOM 949 CA PHE B 161 1.874 25.746 52.003 1.00 90.49 C
ANISOU 949 CA PHE B 161 13292 11862 9227 1240 -229 9 C
ATOM 950 C PHE B 161 2.645 24.674 51.233 1.00 88.50 C
ANISOU 950 C PHE B 161 12950 11589 9086 1485 -207 215 C
ATOM 951 O PHE B 161 3.314 24.975 50.240 1.00 89.96 O
ANISOU 951 O PHE B 161 12936 11820 9423 1472 -251 176 O
ATOM 952 CB PHE B 161 2.729 26.317 53.135 1.00 99.20 C
ANISOU 952 CB PHE B 161 14320 13327 10043 1180 -453 1 C
ATOM 953 CG PHE B 161 2.160 27.569 53.743 1.00103.02 C
ANISOU 953 CG PHE B 161 14881 13820 10441 913 -467 -280 C
ATOM 954 CD1 PHE B 161 1.750 28.618 52.937 1.00109.70 C
ANISOU 954 CD1 PHE B 161 15672 14471 11539 736 -432 -498 C
ATOM 955 CD2 PHE B 161 2.017 27.690 55.115 1.00115.20 C
ANISOU 955 CD2 PHE B 161 16575 15549 11645 847 -501 -324 C
ATOM 956 CE1 PHE B 161 1.221 29.771 53.487 1.00112.29 C
ANISOU 956 CE1 PHE B 161 16087 14742 11837 530 -416 -768 C
ATOM 957 CE2 PHE B 161 1.487 28.840 55.671 1.00129.00 C
ANISOU 957 CE2 PHE B 161 18418 17276 13321 611 -468 -633 C
ATOM 958 CZ PHE B 161 1.089 29.882 54.856 1.00110.14 C
ANISOU 958 CZ PHE B 161 15967 14643 11240 469 -418 -862 C
ATOM 959 N LEU B 162 2.542 23.427 51.688 1.00 87.83 N
ANISOU 959 N LEU B 162 13027 11415 8930 1705 -112 431 N
ATOM 960 CA LEU B 162 3.150 22.306 50.981 1.00 88.63 C
ANISOU 960 CA LEU B 162 13096 11405 9175 1976 -32 605 C
ATOM 961 C LEU B 162 2.574 22.193 49.581 1.00 90.62 C
ANISOU 961 C LEU B 162 13381 11370 9681 1889 149 454 C
ATOM 962 O LEU B 162 3.317 22.147 48.604 1.00 96.09 O
ANISOU 962 O LEU B 162 13906 12101 10502 1962 157 430 O
ATOM 963 CB LEU B 162 2.940 20.994 51.738 1.00 90.39 C
ANISOU 963 CB LEU B 162 13565 11475 9305 2208 69 869 C
ATOM 964 CG LEU B 162 3.396 19.708 51.049 1.00 87.06 C
ANISOU 964 CG LEU B 162 13191 10814 9075 2516 213 1035 C
ATOM 965 CD1 LEU B 162 4.890 19.748 50.766 1.00 89.25 C
ANISOU 965 CD1 LEU B 162 13134 11373 9402 2761 58 1129 C
ATOM 966 CD2 LEU B 162 3.041 18.492 51.892 1.00 87.92 C
ANISOU 966 CD2 LEU B 162 13607 10700 9097 2703 322 1315 C
ATOM 967 N ASN B 163 1.247 22.155 49.485 1.00 85.96 N
ANISOU 967 N ASN B 163 12988 10528 9144 1719 294 350 N
ATOM 968 CA ASN B 163 0.600 22.037 48.181 1.00 83.12 C
ANISOU 968 CA ASN B 163 12663 9932 8985 1599 427 213 C
ATOM 969 C ASN B 163 0.940 23.201 47.246 1.00 91.86 C
ANISOU 969 C ASN B 163 13555 11174 10172 1436 310 60 C
ATOM 970 O ASN B 163 1.231 22.990 46.058 1.00 84.36 O
ANISOU 970 O ASN B 163 12559 10172 9323 1433 369 17 O
ATOM 971 CB ASN B 163 -0.916 21.916 48.351 1.00 79.15 C
ANISOU 971 CB ASN B 163 12340 9208 8524 1416 561 135 C
ATOM 972 CG ASN B 163 -1.358 20.489 48.623 1.00 90.64 C
ANISOU 972 CG ASN B 163 14049 10405 9986 1514 759 271 C
ATOM 973 OD1 ASN B 163 -1.815 19.786 47.721 1.00 79.55 O
ANISOU 973 OD1 ASN B 163 12750 8755 8719 1458 899 214 O
ATOM 974 ND2 ASN B 163 -1.212 20.050 49.869 1.00 95.80 N
ANISOU 974 ND2 ASN B 163 14824 11105 10469 1637 768 455 N
ATOM 975 N LEU B 164 0.923 24.421 47.781 1.00104.60 N
ANISOU 975 N LEU B 164 15065 12950 11727 1287 160 -23 N
ATOM 976 CA LEU B 164 1.298 25.590 46.986 1.00 90.03 C
ANISOU 976 CA LEU B 164 13044 11202 9962 1115 44 -132 C
ATOM 977 C LEU B 164 2.729 25.466 46.449 1.00 85.51 C
ANISOU 977 C LEU B 164 12270 10843 9379 1214 -8 -61 C
ATOM 978 O LEU B 164 2.988 25.697 45.257 1.00 96.60 O
ANISOU 978 O LEU B 164 13591 12241 10869 1128 25 -102 O
ATOM 979 CB LEU B 164 1.151 26.872 47.811 1.00 96.34 C
ANISOU 979 CB LEU B 164 13802 12097 10707 953 -91 -244 C
ATOM 980 CG LEU B 164 -0.277 27.273 48.193 1.00 84.64 C
ANISOU 980 CG LEU B 164 12456 10417 9288 848 -13 -359 C
ATOM 981 CD1 LEU B 164 -0.291 28.554 49.019 1.00 82.91 C
ANISOU 981 CD1 LEU B 164 12216 10266 9022 712 -112 -511 C
ATOM 982 CD2 LEU B 164 -1.142 27.427 46.953 1.00 87.65 C
ANISOU 982 CD2 LEU B 164 12835 10590 9877 752 39 -398 C
ATOM 983 N ALA B 165 3.647 25.082 47.333 1.00 87.92 N
ANISOU 983 N ALA B 165 12481 11361 9564 1394 -87 58 N
ATOM 984 CA ALA B 165 5.055 24.926 46.973 1.00 93.60 C
ANISOU 984 CA ALA B 165 12935 12337 10292 1525 -137 140 C
ATOM 985 C ALA B 165 5.267 23.837 45.925 1.00114.50 C
ANISOU 985 C ALA B 165 15607 14839 13059 1724 74 181 C
ATOM 986 O ALA B 165 6.101 23.982 45.031 1.00104.83 O
ANISOU 986 O ALA B 165 14176 13757 11896 1723 117 154 O
ATOM 987 CB ALA B 165 5.883 24.625 48.210 1.00 92.29 C
ANISOU 987 CB ALA B 165 12651 12443 9972 1712 -294 296 C
ATOM 988 N VAL B 166 4.521 22.742 46.048 1.00123.80 N
ANISOU 988 N VAL B 166 17048 15729 14263 1874 230 229 N
ATOM 989 CA VAL B 166 4.615 21.642 45.095 1.00107.53 C
ANISOU 989 CA VAL B 166 15083 13458 12315 2044 461 221 C
ATOM 990 C VAL B 166 4.132 22.090 43.725 1.00 93.59 C
ANISOU 990 C VAL B 166 13354 11605 10600 1783 549 35 C
ATOM 991 O VAL B 166 4.794 21.828 42.718 1.00109.06 O
ANISOU 991 O VAL B 166 15225 13613 12599 1837 679 -22 O
ATOM 992 CB VAL B 166 3.803 20.412 45.546 1.00102.93 C
ANISOU 992 CB VAL B 166 14825 12528 11755 2188 614 299 C
ATOM 993 CG1 VAL B 166 3.753 19.370 44.433 1.00 95.50 C
ANISOU 993 CG1 VAL B 166 14041 11307 10939 2285 874 212 C
ATOM 994 CG2 VAL B 166 4.406 19.813 46.805 1.00100.12 C
ANISOU 994 CG2 VAL B 166 14457 12256 11329 2491 536 547 C
ATOM 995 N ALA B 167 2.986 22.765 43.687 1.00 90.79 N
ANISOU 995 N ALA B 167 13121 11141 10236 1511 481 -51 N
ATOM 996 CA ALA B 167 2.484 23.312 42.430 1.00 95.54 C
ANISOU 996 CA ALA B 167 13743 11696 10860 1253 498 -178 C
ATOM 997 C ALA B 167 3.538 24.193 41.759 1.00 89.61 C
ANISOU 997 C ALA B 167 12748 11214 10084 1160 434 -186 C
ATOM 998 O ALA B 167 3.949 23.951 40.612 1.00 81.26 O
ANISOU 998 O ALA B 167 11672 10197 9008 1128 566 -242 O
ATOM 999 CB ALA B 167 1.206 24.099 42.673 1.00 86.00 C
ANISOU 999 CB ALA B 167 12617 10381 9679 1023 383 -223 C
ATOM 1000 N ASP B 168 3.990 25.202 42.500 1.00 85.86 N
ANISOU 1000 N ASP B 168 12099 10931 9593 1091 251 -142 N
ATOM 1001 CA ASP B 168 4.966 26.148 41.969 1.00 88.28 C
ANISOU 1001 CA ASP B 168 12167 11489 9887 938 181 -141 C
ATOM 1002 C ASP B 168 6.251 25.475 41.492 1.00 92.19 C
ANISOU 1002 C ASP B 168 12455 12197 10376 1127 325 -109 C
ATOM 1003 O ASP B 168 6.762 25.810 40.427 1.00111.15 O
ANISOU 1003 O ASP B 168 14750 14724 12759 988 412 -142 O
ATOM 1004 CB ASP B 168 5.297 27.216 43.011 1.00 90.57 C
ANISOU 1004 CB ASP B 168 12319 11932 10159 825 -34 -126 C
ATOM 1005 CG ASP B 168 4.163 28.199 43.215 1.00104.38 C
ANISOU 1005 CG ASP B 168 14231 13478 11952 606 -142 -193 C
ATOM 1006 OD1 ASP B 168 3.237 28.226 42.376 1.00 95.29 O
ANISOU 1006 OD1 ASP B 168 13227 12124 10853 513 -88 -215 O
ATOM 1007 OD2 ASP B 168 4.202 28.950 44.212 1.00129.73 O
ANISOU 1007 OD2 ASP B 168 17412 16737 15143 530 -281 -231 O
ATOM 1008 N PHE B 169 6.765 24.530 42.273 1.00 92.44 N
ANISOU 1008 N PHE B 169 12425 12272 10426 1454 361 -29 N
ATOM 1009 CA PHE B 169 8.007 23.834 41.934 1.00 96.07 C
ANISOU 1009 CA PHE B 169 12642 12930 10932 1715 506 14 C
ATOM 1010 C PHE B 169 7.853 23.003 40.663 1.00102.80 C
ANISOU 1010 C PHE B 169 13650 13601 11809 1778 804 -100 C
ATOM 1011 O PHE B 169 8.668 23.103 39.729 1.00109.80 O
ANISOU 1011 O PHE B 169 14347 14682 12691 1750 957 -158 O
ATOM 1012 CB PHE B 169 8.452 22.942 43.100 1.00100.06 C
ANISOU 1012 CB PHE B 169 13084 13467 11467 2098 456 170 C
ATOM 1013 CG PHE B 169 9.767 22.249 42.873 1.00114.21 C
ANISOU 1013 CG PHE B 169 14563 15475 13355 2438 583 245 C
ATOM 1014 CD1 PHE B 169 10.956 22.857 43.238 1.00115.73 C
ANISOU 1014 CD1 PHE B 169 14311 16114 13549 2441 422 328 C
ATOM 1015 CD2 PHE B 169 9.813 20.986 42.304 1.00115.04 C
ANISOU 1015 CD2 PHE B 169 14806 15334 13569 2753 871 220 C
ATOM 1016 CE1 PHE B 169 12.169 22.222 43.032 1.00121.75 C
ANISOU 1016 CE1 PHE B 169 14716 17111 14434 2783 543 407 C
ATOM 1017 CE2 PHE B 169 11.021 20.345 42.095 1.00110.90 C
ANISOU 1017 CE2 PHE B 169 13972 14989 13176 3120 1019 280 C
ATOM 1018 CZ PHE B 169 12.200 20.964 42.460 1.00116.73 C
ANISOU 1018 CZ PHE B 169 14212 16210 13929 3152 853 385 C
ATOM 1019 N LEU B 170 6.809 22.179 40.638 1.00101.28 N
ANISOU 1019 N LEU B 170 13805 13049 11627 1834 901 -149 N
ATOM 1020 CA LEU B 170 6.507 21.370 39.466 1.00103.67 C
ANISOU 1020 CA LEU B 170 14323 13144 11922 1834 1171 -304 C
ATOM 1021 C LEU B 170 6.414 22.254 38.232 1.00112.32 C
ANISOU 1021 C LEU B 170 15396 14384 12898 1474 1183 -411 C
ATOM 1022 O LEU B 170 6.943 21.907 37.174 1.00116.44 O
ANISOU 1022 O LEU B 170 15900 14979 13364 1478 1417 -527 O
ATOM 1023 CB LEU B 170 5.206 20.586 39.656 1.00103.74 C
ANISOU 1023 CB LEU B 170 14714 12756 11946 1811 1217 -351 C
ATOM 1024 CG LEU B 170 4.740 19.805 38.423 1.00122.87 C
ANISOU 1024 CG LEU B 170 17403 14954 14326 1716 1465 -557 C
ATOM 1025 CD1 LEU B 170 5.680 18.640 38.128 1.00126.10 C
ANISOU 1025 CD1 LEU B 170 17818 15269 14826 2077 1771 -621 C
ATOM 1026 CD2 LEU B 170 3.301 19.327 38.579 1.00118.69 C
ANISOU 1026 CD2 LEU B 170 17204 14092 13800 1551 1443 -611 C
ATOM 1027 N SER B 171 5.755 23.402 38.369 1.00125.27 N
ANISOU 1027 N SER B 171 17046 16060 14490 1170 944 -366 N
ATOM 1028 CA SER B 171 5.686 24.341 37.256 1.00110.62 C
ANISOU 1028 CA SER B 171 15177 14334 12520 830 916 -398 C
ATOM 1029 C SER B 171 7.081 24.847 36.889 1.00101.79 C
ANISOU 1029 C SER B 171 13736 13562 11376 809 991 -363 C
ATOM 1030 O SER B 171 7.381 25.058 35.715 1.00 99.23 O
ANISOU 1030 O SER B 171 13410 13370 10925 624 1133 -416 O
ATOM 1031 CB SER B 171 4.771 25.523 37.583 1.00 96.17 C
ANISOU 1031 CB SER B 171 13402 12436 10704 568 640 -323 C
ATOM 1032 OG SER B 171 4.549 26.337 36.439 1.00 96.88 O
ANISOU 1032 OG SER B 171 13538 12590 10683 254 600 -308 O
ATOM 1033 N CYS B 172 7.934 25.023 37.895 1.00106.65 N
ANISOU 1033 N CYS B 172 14071 14358 12092 977 897 -272 N
ATOM 1034 CA CYS B 172 9.272 25.573 37.681 1.00105.29 C
ANISOU 1034 CA CYS B 172 13521 14561 11923 925 938 -230 C
ATOM 1035 C CYS B 172 10.193 24.614 36.940 1.00 98.81 C
ANISOU 1035 C CYS B 172 12552 13883 11109 1168 1273 -311 C
ATOM 1036 O CYS B 172 11.154 25.043 36.302 1.00 97.01 O
ANISOU 1036 O CYS B 172 12046 13969 10846 1048 1401 -315 O
ATOM 1037 CB CYS B 172 9.917 25.960 39.014 1.00122.96 C
ANISOU 1037 CB CYS B 172 15476 16990 14251 1026 711 -121 C
ATOM 1038 SG CYS B 172 9.343 27.516 39.718 1.00 99.63 S
ANISOU 1038 SG CYS B 172 12582 13994 11281 642 371 -78 S
ATOM 1039 N LEU B 173 9.912 23.318 37.035 1.00 98.46 N
ANISOU 1039 N LEU B 173 12692 13594 11125 1505 1442 -380 N
ATOM 1040 CA LEU B 173 10.728 22.325 36.333 1.00101.54 C
ANISOU 1040 CA LEU B 173 12981 14044 11554 1787 1807 -495 C
ATOM 1041 C LEU B 173 10.729 22.511 34.811 1.00118.62 C
ANISOU 1041 C LEU B 173 15257 16290 13523 1503 2062 -663 C
ATOM 1042 O LEU B 173 11.662 22.083 34.131 1.00115.48 O
ANISOU 1042 O LEU B 173 14668 16082 13125 1646 2385 -768 O
ATOM 1043 CB LEU B 173 10.253 20.910 36.666 1.00100.99 C
ANISOU 1043 CB LEU B 173 13194 13583 11593 2162 1951 -553 C
ATOM 1044 CG LEU B 173 10.420 20.461 38.117 1.00101.54 C
ANISOU 1044 CG LEU B 173 13164 13583 11833 2520 1766 -356 C
ATOM 1045 CD1 LEU B 173 10.019 19.002 38.276 1.00 97.83 C
ANISOU 1045 CD1 LEU B 173 13011 12680 11481 2878 1970 -399 C
ATOM 1046 CD2 LEU B 173 11.851 20.685 38.575 1.00114.68 C
ANISOU 1046 CD2 LEU B 173 14293 15670 13610 2754 1724 -219 C
ATOM 1047 N ALA B 174 9.690 23.149 34.281 1.00126.85 N
ANISOU 1047 N ALA B 174 16596 17210 14390 1110 1921 -679 N
ATOM 1048 CA ALA B 174 9.540 23.292 32.835 1.00106.72 C
ANISOU 1048 CA ALA B 174 14222 14737 11589 810 2120 -811 C
ATOM 1049 C ALA B 174 10.388 24.424 32.258 1.00108.77 C
ANISOU 1049 C ALA B 174 14200 15391 11736 510 2138 -716 C
ATOM 1050 O ALA B 174 10.659 24.456 31.058 1.00129.09 O
ANISOU 1050 O ALA B 174 16833 18132 14085 311 2387 -814 O
ATOM 1051 CB ALA B 174 8.076 23.511 32.484 1.00102.06 C
ANISOU 1051 CB ALA B 174 14034 13891 10853 518 1923 -823 C
ATOM 1052 N LEU B 175 10.807 25.343 33.122 1.00107.28 N
ANISOU 1052 N LEU B 175 13725 15351 11685 449 1885 -533 N
ATOM 1053 CA LEU B 175 11.484 26.572 32.704 1.00114.13 C
ANISOU 1053 CA LEU B 175 14358 16533 12472 83 1847 -412 C
ATOM 1054 C LEU B 175 12.770 26.419 31.869 1.00117.48 C
ANISOU 1054 C LEU B 175 14466 17349 12821 72 2223 -483 C
ATOM 1055 O LEU B 175 12.946 27.159 30.901 1.00117.44 O
ANISOU 1055 O LEU B 175 14488 17526 12606 -316 2319 -437 O
ATOM 1056 CB LEU B 175 11.790 27.426 33.938 1.00112.33 C
ANISOU 1056 CB LEU B 175 13871 16375 12435 47 1527 -257 C
ATOM 1057 CG LEU B 175 10.574 28.124 34.549 1.00112.43 C
ANISOU 1057 CG LEU B 175 14174 16066 12477 -112 1172 -172 C
ATOM 1058 CD1 LEU B 175 10.959 28.882 35.807 1.00120.67 C
ANISOU 1058 CD1 LEU B 175 14982 17187 13682 -141 901 -82 C
ATOM 1059 CD2 LEU B 175 9.942 29.058 33.529 1.00105.39 C
ANISOU 1059 CD2 LEU B 175 13533 15097 11414 -532 1115 -92 C
ATOM 1060 N PRO B 176 13.677 25.487 32.234 1.00108.25 N
ANISOU 1060 N PRO B 176 12985 16320 11826 499 2447 -573 N
ATOM 1061 CA PRO B 176 14.915 25.413 31.441 1.00123.31 C
ANISOU 1061 CA PRO B 176 14528 18636 13687 490 2833 -647 C
ATOM 1062 C PRO B 176 14.701 25.117 29.955 1.00117.81 C
ANISOU 1062 C PRO B 176 14130 17955 12677 296 3201 -826 C
ATOM 1063 O PRO B 176 15.421 25.656 29.112 1.00115.33 O
ANISOU 1063 O PRO B 176 13628 17995 12196 9 3437 -819 O
ATOM 1064 CB PRO B 176 15.683 24.263 32.101 1.00119.30 C
ANISOU 1064 CB PRO B 176 13700 18173 13454 1086 3002 -719 C
ATOM 1065 CG PRO B 176 15.189 24.237 33.490 1.00108.76 C
ANISOU 1065 CG PRO B 176 12404 16612 12307 1279 2589 -574 C
ATOM 1066 CD PRO B 176 13.733 24.587 33.402 1.00105.90 C
ANISOU 1066 CD PRO B 176 12589 15864 11784 995 2355 -568 C
ATOM 1067 N ILE B 177 13.726 24.271 29.645 1.00115.98 N
ANISOU 1067 N ILE B 177 14362 17362 12343 415 3254 -988 N
ATOM 1068 CA ILE B 177 13.450 23.906 28.260 1.00131.73 C
ANISOU 1068 CA ILE B 177 16689 19371 13991 213 3581 -1196 C
ATOM 1069 C ILE B 177 12.843 25.084 27.493 1.00133.00 C
ANISOU 1069 C ILE B 177 17090 19621 13822 -373 3379 -1032 C
ATOM 1070 O ILE B 177 13.200 25.333 26.337 1.00138.92 O
ANISOU 1070 O ILE B 177 17891 20642 14249 -671 3653 -1085 O
ATOM 1071 CB ILE B 177 12.520 22.674 28.186 1.00135.46 C
ANISOU 1071 CB ILE B 177 17608 19415 14447 452 3656 -1430 C
ATOM 1072 CG1 ILE B 177 13.321 21.404 28.492 1.00146.19 C
ANISOU 1072 CG1 ILE B 177 18776 20700 16067 1019 4026 -1631 C
ATOM 1073 CG2 ILE B 177 11.853 22.571 26.823 1.00127.03 C
ANISOU 1073 CG2 ILE B 177 16987 18337 12940 82 3816 -1610 C
ATOM 1074 CD1 ILE B 177 12.639 20.121 28.074 1.00145.92 C
ANISOU 1074 CD1 ILE B 177 19208 20262 15972 1196 4261 -1938 C
ATOM 1075 N LEU B 178 11.941 25.813 28.143 1.00119.33 N
ANISOU 1075 N LEU B 178 15506 17663 12170 -524 2913 -821 N
ATOM 1076 CA LEU B 178 11.375 27.027 27.562 1.00118.97 C
ANISOU 1076 CA LEU B 178 15655 17654 11892 -1022 2670 -600 C
ATOM 1077 C LEU B 178 12.477 28.042 27.273 1.00122.12 C
ANISOU 1077 C LEU B 178 15718 18430 12251 -1312 2776 -432 C
ATOM 1078 O LEU B 178 12.508 28.659 26.205 1.00130.06 O
ANISOU 1078 O LEU B 178 16868 19615 12932 -1719 2871 -333 O
ATOM 1079 CB LEU B 178 10.328 27.636 28.498 1.00103.42 C
ANISOU 1079 CB LEU B 178 13822 15357 10116 -1045 2181 -416 C
ATOM 1080 CG LEU B 178 9.116 26.765 28.833 1.00 95.27 C
ANISOU 1080 CG LEU B 178 13106 13959 9134 -832 2043 -543 C
ATOM 1081 CD1 LEU B 178 8.195 27.477 29.811 1.00104.04 C
ANISOU 1081 CD1 LEU B 178 14274 14803 10456 -852 1607 -359 C
ATOM 1082 CD2 LEU B 178 8.366 26.385 27.569 1.00110.06 C
ANISOU 1082 CD2 LEU B 178 15367 15815 10637 -1061 2135 -655 C
ATOM 1083 N PHE B 179 13.376 28.202 28.241 1.00112.64 N
ANISOU 1083 N PHE B 179 14069 17363 11367 -1125 2750 -388 N
ATOM 1084 CA PHE B 179 14.538 29.073 28.111 1.00116.82 C
ANISOU 1084 CA PHE B 179 14193 18275 11916 -1394 2864 -256 C
ATOM 1085 C PHE B 179 15.358 28.691 26.884 1.00139.47 C
ANISOU 1085 C PHE B 179 16957 21517 14517 -1496 3382 -393 C
ATOM 1086 O PHE B 179 15.664 29.537 26.039 1.00142.63 O
ANISOU 1086 O PHE B 179 17376 22148 14667 -1958 3492 -251 O
ATOM 1087 CB PHE B 179 15.399 28.993 29.376 1.00117.79 C
ANISOU 1087 CB PHE B 179 13809 18529 12416 -1103 2769 -249 C
ATOM 1088 CG PHE B 179 16.522 29.991 29.418 1.00118.65 C
ANISOU 1088 CG PHE B 179 13469 19024 12588 -1437 2804 -106 C
ATOM 1089 CD1 PHE B 179 16.368 31.198 30.078 1.00126.88 C
ANISOU 1089 CD1 PHE B 179 14500 19964 13744 -1763 2428 92 C
ATOM 1090 CD2 PHE B 179 17.738 29.716 28.812 1.00123.26 C
ANISOU 1090 CD2 PHE B 179 13632 20068 13135 -1436 3235 -189 C
ATOM 1091 CE1 PHE B 179 17.400 32.116 30.125 1.00127.90 C
ANISOU 1091 CE1 PHE B 179 14229 20428 13938 -2128 2459 208 C
ATOM 1092 CE2 PHE B 179 18.772 30.630 28.854 1.00137.38 C
ANISOU 1092 CE2 PHE B 179 14970 22237 14990 -1790 3274 -57 C
ATOM 1093 CZ PHE B 179 18.604 31.832 29.511 1.00132.05 C
ANISOU 1093 CZ PHE B 179 14310 21442 14420 -2158 2875 144 C
ATOM 1094 N THR B 180 15.702 27.409 26.797 1.00136.12 N
ANISOU 1094 N THR B 180 16445 21130 14146 -1059 3721 -669 N
ATOM 1095 CA THR B 180 16.463 26.880 25.669 1.00135.36 C
ANISOU 1095 CA THR B 180 16258 21363 13808 -1078 4282 -876 C
ATOM 1096 C THR B 180 15.776 27.177 24.338 1.00145.11 C
ANISOU 1096 C THR B 180 18001 22606 14529 -1532 4375 -878 C
ATOM 1097 O THR B 180 16.421 27.606 23.381 1.00145.34 O
ANISOU 1097 O THR B 180 17948 23009 14267 -1875 4697 -854 O
ATOM 1098 CB THR B 180 16.675 25.355 25.799 1.00125.62 C
ANISOU 1098 CB THR B 180 14984 20012 12733 -485 4611 -1206 C
ATOM 1099 OG1 THR B 180 17.476 25.078 26.953 1.00122.77 O
ANISOU 1099 OG1 THR B 180 14094 19728 12826 -49 4546 -1158 O
ATOM 1100 CG2 THR B 180 17.372 24.802 24.564 1.00145.87 C
ANISOU 1100 CG2 THR B 180 17515 22883 15024 -506 5238 -1477 C
ATOM 1101 N SER B 181 14.464 26.965 24.289 1.00136.60 N
ANISOU 1101 N SER B 181 17431 21146 13325 -1555 4083 -888 N
ATOM 1102 CA SER B 181 13.703 27.183 23.063 1.00127.87 C
ANISOU 1102 CA SER B 181 16818 20058 11710 -1970 4095 -873 C
ATOM 1103 C SER B 181 13.694 28.652 22.651 1.00129.45 C
ANISOU 1103 C SER B 181 17052 20416 11716 -2512 3877 -486 C
ATOM 1104 O SER B 181 13.811 28.970 21.467 1.00117.37 O
ANISOU 1104 O SER B 181 15717 19150 9727 -2906 4089 -436 O
ATOM 1105 CB SER B 181 12.268 26.681 23.226 1.00116.30 C
ANISOU 1105 CB SER B 181 15812 18167 10209 -1877 3762 -940 C
ATOM 1106 OG SER B 181 11.543 26.833 22.017 1.00112.85 O
ANISOU 1106 OG SER B 181 15823 17800 9254 -2278 3745 -928 O
ATOM 1107 N ILE B 182 13.556 29.545 23.627 1.00121.01 N
ANISOU 1107 N ILE B 182 15824 19171 10983 -2544 3466 -215 N
ATOM 1108 CA ILE B 182 13.551 30.977 23.342 1.00128.83 C
ANISOU 1108 CA ILE B 182 16866 20217 11866 -3038 3251 164 C
ATOM 1109 C ILE B 182 14.924 31.440 22.858 1.00138.02 C
ANISOU 1109 C ILE B 182 17663 21842 12939 -3314 3646 219 C
ATOM 1110 O ILE B 182 15.025 32.235 21.921 1.00132.02 O
ANISOU 1110 O ILE B 182 17071 21258 11833 -3799 3724 449 O
ATOM 1111 CB ILE B 182 13.127 31.799 24.575 1.00117.61 C
ANISOU 1111 CB ILE B 182 15364 18460 10863 -2989 2761 380 C
ATOM 1112 CG1 ILE B 182 11.658 31.531 24.901 1.00123.38 C
ANISOU 1112 CG1 ILE B 182 16477 18763 11639 -2810 2376 379 C
ATOM 1113 CG2 ILE B 182 13.331 33.285 24.331 1.00119.55 C
ANISOU 1113 CG2 ILE B 182 15628 18730 11065 -3490 2604 750 C
ATOM 1114 CD1 ILE B 182 11.111 32.404 26.003 1.00128.36 C
ANISOU 1114 CD1 ILE B 182 17090 19050 12631 -2786 1925 579 C
ATOM 1115 N VAL B 183 15.976 30.930 23.494 1.00141.36 N
ANISOU 1115 N VAL B 183 17568 22474 13668 -3007 3895 29 N
ATOM 1116 CA VAL B 183 17.341 31.229 23.071 1.00138.28 C
ANISOU 1116 CA VAL B 183 16729 22579 13231 -3226 4318 37 C
ATOM 1117 C VAL B 183 17.559 30.789 21.624 1.00139.73 C
ANISOU 1117 C VAL B 183 17114 23077 12898 -3420 4826 -109 C
ATOM 1118 O VAL B 183 18.245 31.464 20.853 1.00157.35 O
ANISOU 1118 O VAL B 183 19240 25670 14873 -3871 5099 40 O
ATOM 1119 CB VAL B 183 18.381 30.547 23.991 1.00138.39 C
ANISOU 1119 CB VAL B 183 16113 22793 13677 -2762 4496 -169 C
ATOM 1120 CG1 VAL B 183 19.784 30.665 23.412 1.00135.53 C
ANISOU 1120 CG1 VAL B 183 15239 23006 13252 -2946 5013 -214 C
ATOM 1121 CG2 VAL B 183 18.331 31.153 25.383 1.00133.06 C
ANISOU 1121 CG2 VAL B 183 15211 21912 13435 -2688 4007 -3 C
ATOM 1122 N GLN B 184 16.950 29.668 21.251 1.00134.05 N
ANISOU 1122 N GLN B 184 16715 22214 12003 -3117 4958 -407 N
ATOM 1123 CA GLN B 184 17.093 29.138 19.900 1.00134.52 C
ANISOU 1123 CA GLN B 184 17020 22556 11533 -3286 5451 -622 C
ATOM 1124 C GLN B 184 15.975 29.613 18.972 1.00132.87 C
ANISOU 1124 C GLN B 184 17456 22232 10797 -3729 5200 -430 C
ATOM 1125 O GLN B 184 15.580 28.896 18.054 1.00149.92 O
ANISOU 1125 O GLN B 184 19991 24458 12515 -3769 5432 -676 O
ATOM 1126 CB GLN B 184 17.133 27.608 19.929 1.00138.53 C
ANISOU 1126 CB GLN B 184 17536 22976 12122 -2738 5790 -1102 C
ATOM 1127 CG GLN B 184 18.266 27.034 20.766 1.00146.44 C
ANISOU 1127 CG GLN B 184 17889 24115 13638 -2233 6059 -1274 C
ATOM 1128 CD GLN B 184 18.370 25.526 20.650 1.00151.94 C
ANISOU 1128 CD GLN B 184 18631 24695 14405 -1690 6467 -1737 C
ATOM 1129 OE1 GLN B 184 17.804 24.923 19.738 1.00152.66 O
ANISOU 1129 OE1 GLN B 184 19215 24705 14084 -1777 6684 -1995 O
ATOM 1130 NE2 GLN B 184 19.092 24.907 21.577 1.00151.32 N
ANISOU 1130 NE2 GLN B 184 18052 24596 14848 -1131 6565 -1842 N
ATOM 1131 N HIS B 185 15.476 30.822 19.219 1.00135.50 N
ANISOU 1131 N HIS B 185 17915 22390 11180 -4057 4720 8 N
ATOM 1132 CA HIS B 185 14.476 31.460 18.359 1.00135.57 C
ANISOU 1132 CA HIS B 185 18476 22312 10722 -4486 4428 298 C
ATOM 1133 C HIS B 185 13.224 30.602 18.140 1.00138.91 C
ANISOU 1133 C HIS B 185 19352 22476 10953 -4293 4210 94 C
ATOM 1134 O HIS B 185 12.849 30.326 16.999 1.00140.14 O
ANISOU 1134 O HIS B 185 19898 22819 10531 -4554 4345 25 O
ATOM 1135 CB HIS B 185 15.093 31.820 17.000 1.00141.48 C
ANISOU 1135 CB HIS B 185 19343 23522 10890 -4979 4841 394 C
ATOM 1136 CG HIS B 185 16.143 32.887 17.070 1.00154.30 C
ANISOU 1136 CG HIS B 185 20599 25358 12669 -5299 4967 691 C
ATOM 1137 ND1 HIS B 185 15.837 34.229 17.133 1.00155.08 N
ANISOU 1137 ND1 HIS B 185 20848 25281 12795 -5702 4578 1198 N
ATOM 1138 CD2 HIS B 185 17.495 32.809 17.071 1.00157.26 C
ANISOU 1138 CD2 HIS B 185 20458 26084 13208 -5278 5434 551 C
ATOM 1139 CE1 HIS B 185 16.955 34.933 17.178 1.00156.56 C
ANISOU 1139 CE1 HIS B 185 20653 25687 13147 -5953 4803 1340 C
ATOM 1140 NE2 HIS B 185 17.975 34.095 17.142 1.00162.29 N
ANISOU 1140 NE2 HIS B 185 20947 26765 13952 -5709 5314 958 N
ATOM 1141 N HIS B 186 12.601 30.185 19.241 1.00127.89 N
ANISOU 1141 N HIS B 186 17896 20674 10022 -3872 3878 -5 N
ATOM 1142 CA HIS B 186 11.335 29.439 19.242 1.00129.39 C
ANISOU 1142 CA HIS B 186 18463 20566 10134 -3699 3607 -169 C
ATOM 1143 C HIS B 186 11.449 28.007 18.706 1.00148.37 C
ANISOU 1143 C HIS B 186 21005 23067 12303 -3496 4047 -681 C
ATOM 1144 O HIS B 186 10.450 27.292 18.636 1.00163.20 O
ANISOU 1144 O HIS B 186 23204 24714 14089 -3401 3871 -867 O
ATOM 1145 CB HIS B 186 10.260 30.191 18.445 1.00128.87 C
ANISOU 1145 CB HIS B 186 18841 20471 9653 -4120 3204 175 C
ATOM 1146 CG HIS B 186 9.951 31.556 18.975 1.00117.39 C
ANISOU 1146 CG HIS B 186 17329 18804 8469 -4272 2744 670 C
ATOM 1147 ND1 HIS B 186 9.059 32.410 18.359 1.00126.62 N
ANISOU 1147 ND1 HIS B 186 18838 19911 9360 -4605 2347 1073 N
ATOM 1148 CD2 HIS B 186 10.411 32.219 20.063 1.00112.16 C
ANISOU 1148 CD2 HIS B 186 16323 17960 8333 -4136 2618 818 C
ATOM 1149 CE1 HIS B 186 8.985 33.536 19.043 1.00113.48 C
ANISOU 1149 CE1 HIS B 186 17056 17988 8074 -4641 2027 1440 C
ATOM 1150 NE2 HIS B 186 9.795 33.447 20.082 1.00110.49 N
ANISOU 1150 NE2 HIS B 186 16276 17537 8169 -4385 2188 1272 N
ATOM 1151 N HIS B 187 12.655 27.586 18.337 1.00134.40 N
ANISOU 1151 N HIS B 187 18985 21624 10457 -3433 4631 -925 N
ATOM 1152 CA HIS B 187 12.865 26.231 17.825 1.00130.66 C
ANISOU 1152 CA HIS B 187 18642 21206 9797 -3207 5121 -1450 C
ATOM 1153 C HIS B 187 12.558 25.170 18.884 1.00132.74 C
ANISOU 1153 C HIS B 187 18824 21038 10572 -2633 5050 -1724 C
ATOM 1154 O HIS B 187 13.029 25.259 20.018 1.00118.16 O
ANISOU 1154 O HIS B 187 16563 19060 9273 -2282 4953 -1626 O
ATOM 1155 CB HIS B 187 14.300 26.067 17.320 1.00131.16 C
ANISOU 1155 CB HIS B 187 18359 21688 9789 -3179 5769 -1630 C
ATOM 1156 CG HIS B 187 14.614 24.694 16.820 1.00134.06 C
ANISOU 1156 CG HIS B 187 18802 21984 10153 -2815 6212 -2139 C
ATOM 1157 ND1 HIS B 187 13.875 24.066 15.837 1.00131.39 N
ANISOU 1157 ND1 HIS B 187 18959 21520 9442 -2931 6169 -2358 N
ATOM 1158 CD2 HIS B 187 15.595 23.822 17.157 1.00135.42 C
ANISOU 1158 CD2 HIS B 187 18607 22180 10666 -2326 6699 -2465 C
ATOM 1159 CE1 HIS B 187 14.381 22.874 15.597 1.00137.37 C
ANISOU 1159 CE1 HIS B 187 19688 22200 10305 -2552 6620 -2809 C
ATOM 1160 NE2 HIS B 187 15.430 22.700 16.387 1.00141.71 N
ANISOU 1160 NE2 HIS B 187 19720 22822 11300 -2151 6950 -2869 N
ATOM 1161 N TRP B 188 11.774 24.164 18.507 1.00123.25 N
ANISOU 1161 N TRP B 188 18037 19624 9169 -2570 5094 -2062 N
ATOM 1162 CA TRP B 188 11.341 23.135 19.451 1.00121.86 C
ANISOU 1162 CA TRP B 188 17873 18986 9441 -2085 5012 -2295 C
ATOM 1163 C TRP B 188 11.715 21.725 19.000 1.00128.02 C
ANISOU 1163 C TRP B 188 18808 19688 10146 -1814 5586 -2850 C
ATOM 1164 O TRP B 188 10.977 21.094 18.247 1.00136.87 O
ANISOU 1164 O TRP B 188 20380 20689 10934 -1989 5592 -3109 O
ATOM 1165 CB TRP B 188 9.828 23.219 19.666 1.00130.33 C
ANISOU 1165 CB TRP B 188 19310 19739 10472 -2244 4442 -2166 C
ATOM 1166 CG TRP B 188 9.334 22.325 20.762 1.00139.14 C
ANISOU 1166 CG TRP B 188 20418 20375 12073 -1799 4311 -2318 C
ATOM 1167 CD1 TRP B 188 8.883 21.043 20.636 1.00143.18 C
ANISOU 1167 CD1 TRP B 188 21239 20595 12567 -1639 4504 -2728 C
ATOM 1168 CD2 TRP B 188 9.247 22.646 22.156 1.00137.40 C
ANISOU 1168 CD2 TRP B 188 19894 19905 12405 -1487 3973 -2058 C
ATOM 1169 NE1 TRP B 188 8.519 20.547 21.866 1.00146.16 N
ANISOU 1169 NE1 TRP B 188 21521 20550 13462 -1245 4308 -2702 N
ATOM 1170 CE2 TRP B 188 8.732 21.512 22.815 1.00145.13 C
ANISOU 1170 CE2 TRP B 188 21015 20462 13667 -1143 3981 -2296 C
ATOM 1171 CE3 TRP B 188 9.553 23.783 22.910 1.00134.20 C
ANISOU 1171 CE3 TRP B 188 19139 19586 12266 -1494 3676 -1662 C
ATOM 1172 CZ2 TRP B 188 8.518 21.482 24.192 1.00124.03 C
ANISOU 1172 CZ2 TRP B 188 18141 17492 11494 -804 3704 -2126 C
ATOM 1173 CZ3 TRP B 188 9.338 23.752 24.277 1.00128.08 C
ANISOU 1173 CZ3 TRP B 188 18167 18516 11981 -1159 3399 -1537 C
ATOM 1174 CH2 TRP B 188 8.825 22.609 24.903 1.00121.06 C
ANISOU 1174 CH2 TRP B 188 17421 17249 11329 -816 3415 -1756 C
ATOM 1175 N PRO B 189 12.865 21.223 19.469 1.00128.81 N
ANISOU 1175 N PRO B 189 18494 19819 10629 -1350 6009 -3006 N
ATOM 1176 CA PRO B 189 13.322 19.882 19.098 1.00135.02 C
ANISOU 1176 CA PRO B 189 19375 20459 11468 -987 6553 -3504 C
ATOM 1177 C PRO B 189 12.946 18.793 20.106 1.00142.98 C
ANISOU 1177 C PRO B 189 20462 20912 12953 -471 6530 -3698 C
ATOM 1178 O PRO B 189 13.605 17.755 20.133 1.00144.88 O
ANISOU 1178 O PRO B 189 20599 20982 13468 0 6932 -3992 O
ATOM 1179 CB PRO B 189 14.837 20.053 19.044 1.00131.64 C
ANISOU 1179 CB PRO B 189 18383 20414 11220 -751 7013 -3497 C
ATOM 1180 CG PRO B 189 15.111 21.052 20.131 1.00127.86 C
ANISOU 1180 CG PRO B 189 17437 20043 11100 -718 6646 -3049 C
ATOM 1181 CD PRO B 189 13.908 21.976 20.189 1.00122.11 C
ANISOU 1181 CD PRO B 189 17032 19208 10158 -1180 5999 -2701 C
ATOM 1182 N PHE B 190 11.910 19.013 20.911 1.00133.28 N
ANISOU 1182 N PHE B 190 19363 19363 11915 -508 5947 -3446 N
ATOM 1183 CA PHE B 190 11.600 18.089 22.001 1.00128.51 C
ANISOU 1183 CA PHE B 190 18775 18234 11819 -16 5852 -3514 C
ATOM 1184 C PHE B 190 10.395 17.189 21.726 1.00127.71 C
ANISOU 1184 C PHE B 190 19263 17704 11559 -154 5781 -3808 C
ATOM 1185 O PHE B 190 10.044 16.346 22.553 1.00118.08 O
ANISOU 1185 O PHE B 190 18135 16005 10724 198 5730 -3877 O
ATOM 1186 CB PHE B 190 11.372 18.868 23.296 1.00115.28 C
ANISOU 1186 CB PHE B 190 16779 16486 10535 98 5301 -3044 C
ATOM 1187 CG PHE B 190 12.492 19.808 23.638 1.00121.34 C
ANISOU 1187 CG PHE B 190 16973 17667 11464 162 5307 -2753 C
ATOM 1188 CD1 PHE B 190 13.664 19.333 24.202 1.00126.88 C
ANISOU 1188 CD1 PHE B 190 17221 18429 12559 680 5614 -2798 C
ATOM 1189 CD2 PHE B 190 12.374 21.165 23.392 1.00120.02 C
ANISOU 1189 CD2 PHE B 190 16711 17822 11068 -302 4998 -2425 C
ATOM 1190 CE1 PHE B 190 14.697 20.194 24.515 1.00138.17 C
ANISOU 1190 CE1 PHE B 190 18084 20281 14135 692 5603 -2543 C
ATOM 1191 CE2 PHE B 190 13.403 22.032 23.703 1.00121.97 C
ANISOU 1191 CE2 PHE B 190 16445 18430 11468 -304 5010 -2177 C
ATOM 1192 CZ PHE B 190 14.567 21.546 24.266 1.00136.09 C
ANISOU 1192 CZ PHE B 190 17754 20323 13632 173 5308 -2246 C
ATOM 1193 N GLY B 191 9.766 17.365 20.568 1.00130.87 N
ANISOU 1193 N GLY B 191 20058 18286 11382 -690 5763 -3964 N
ATOM 1194 CA GLY B 191 8.651 16.519 20.179 1.00141.00 C
ANISOU 1194 CA GLY B 191 21802 19217 12553 -868 5583 -4199 C
ATOM 1195 C GLY B 191 7.291 17.102 20.514 1.00129.68 C
ANISOU 1195 C GLY B 191 20585 17709 10979 -1245 5023 -3969 C
ATOM 1196 O GLY B 191 7.184 18.055 21.285 1.00135.56 O
ANISOU 1196 O GLY B 191 21023 18537 11947 -1211 4626 -3527 O
ATOM 1197 N GLY B 192 6.248 16.515 19.935 1.00124.88 N
ANISOU 1197 N GLY B 192 20346 16924 10179 -1541 4823 -4154 N
ATOM 1198 CA GLY B 192 4.893 17.009 20.104 1.00129.24 C
ANISOU 1198 CA GLY B 192 21073 17452 10582 -1921 4278 -3953 C
ATOM 1199 C GLY B 192 4.326 16.808 21.496 1.00103.80 C
ANISOU 1199 C GLY B 192 17756 13809 7873 -1634 4029 -3794 C
ATOM 1200 O GLY B 192 3.573 17.647 21.994 1.00111.45 O
ANISOU 1200 O GLY B 192 18572 14834 8939 -1767 3518 -3412 O
ATOM 1201 N ALA B 193 4.683 15.691 22.121 1.00107.99 N
ANISOU 1201 N ALA B 193 18341 13900 8789 -1208 4363 -4041 N
ATOM 1202 CA ALA B 193 4.206 15.375 23.463 1.00123.75 C
ANISOU 1202 CA ALA B 193 20234 15477 11311 -901 4135 -3853 C
ATOM 1203 C ALA B 193 4.697 16.405 24.474 1.00109.10 C
ANISOU 1203 C ALA B 193 17884 13789 9781 -627 3873 -3370 C
ATOM 1204 O ALA B 193 3.907 16.959 25.240 1.00 99.31 O
ANISOU 1204 O ALA B 193 16532 12488 8713 -690 3431 -3066 O
ATOM 1205 CB ALA B 193 4.647 13.979 23.870 1.00138.43 C
ANISOU 1205 CB ALA B 193 22266 16829 13502 -470 4584 -4175 C
ATOM 1206 N ALA B 194 6.003 16.658 24.465 1.00123.57 N
ANISOU 1206 N ALA B 194 19413 15845 11693 -341 4162 -3326 N
ATOM 1207 CA ALA B 194 6.606 17.651 25.347 1.00121.15 C
ANISOU 1207 CA ALA B 194 18629 15743 11658 -131 3939 -2911 C
ATOM 1208 C ALA B 194 6.029 19.038 25.076 1.00127.41 C
ANISOU 1208 C ALA B 194 19341 16859 12209 -568 3491 -2588 C
ATOM 1209 O ALA B 194 5.789 19.818 26.002 1.00121.07 O
ANISOU 1209 O ALA B 194 18302 16045 11653 -508 3124 -2249 O
ATOM 1210 CB ALA B 194 8.118 17.659 25.181 1.00126.70 C
ANISOU 1210 CB ALA B 194 19003 16701 12436 171 4354 -2961 C
ATOM 1211 N CYS B 195 5.809 19.328 23.798 1.00125.17 N
ANISOU 1211 N CYS B 195 19279 16850 11431 -1001 3532 -2696 N
ATOM 1212 CA CYS B 195 5.195 20.580 23.375 1.00107.52 C
ANISOU 1212 CA CYS B 195 17031 14893 8929 -1425 3109 -2375 C
ATOM 1213 C CYS B 195 3.792 20.726 23.949 1.00102.35 C
ANISOU 1213 C CYS B 195 16476 13997 8414 -1538 2623 -2215 C
ATOM 1214 O CYS B 195 3.345 21.831 24.262 1.00114.28 O
ANISOU 1214 O CYS B 195 17830 15602 9991 -1662 2219 -1852 O
ATOM 1215 CB CYS B 195 5.148 20.656 21.851 1.00 96.68 C
ANISOU 1215 CB CYS B 195 15944 13848 6941 -1872 3253 -2538 C
ATOM 1216 SG CYS B 195 4.164 22.022 21.198 1.00110.98 S
ANISOU 1216 SG CYS B 195 17838 15952 8379 -2405 2686 -2123 S
ATOM 1217 N SER B 196 3.099 19.603 24.088 1.00 99.50 N
ANISOU 1217 N SER B 196 16374 13312 8120 -1497 2686 -2496 N
ATOM 1218 CA SER B 196 1.756 19.615 24.644 1.00101.28 C
ANISOU 1218 CA SER B 196 16664 13321 8496 -1610 2277 -2380 C
ATOM 1219 C SER B 196 1.789 19.785 26.160 1.00 96.04 C
ANISOU 1219 C SER B 196 15725 12411 8356 -1226 2140 -2149 C
ATOM 1220 O SER B 196 0.996 20.543 26.717 1.00 84.09 O
ANISOU 1220 O SER B 196 14078 10888 6983 -1299 1746 -1875 O
ATOM 1221 CB SER B 196 1.009 18.333 24.265 1.00 90.72 C
ANISOU 1221 CB SER B 196 15704 11722 7044 -1761 2410 -2773 C
ATOM 1222 OG SER B 196 0.706 18.313 22.881 1.00 95.72 O
ANISOU 1222 OG SER B 196 16612 12629 7129 -2216 2416 -2964 O
ATOM 1223 N ILE B 197 2.721 19.104 26.825 1.00 94.66 N
ANISOU 1223 N ILE B 197 15455 12053 8457 -806 2466 -2253 N
ATOM 1224 CA ILE B 197 2.690 19.040 28.285 1.00105.32 C
ANISOU 1224 CA ILE B 197 16612 13155 10251 -452 2347 -2066 C
ATOM 1225 C ILE B 197 3.431 20.181 28.999 1.00106.55 C
ANISOU 1225 C ILE B 197 16372 13532 10580 -288 2187 -1740 C
ATOM 1226 O ILE B 197 2.856 20.826 29.875 1.00 97.13 O
ANISOU 1226 O ILE B 197 15050 12281 9575 -280 1864 -1505 O
ATOM 1227 CB ILE B 197 3.240 17.676 28.799 1.00103.17 C
ANISOU 1227 CB ILE B 197 16443 12532 10225 -47 2722 -2284 C
ATOM 1228 CG1 ILE B 197 3.194 17.624 30.326 1.00122.60 C
ANISOU 1228 CG1 ILE B 197 18724 14773 13085 295 2571 -2045 C
ATOM 1229 CG2 ILE B 197 4.654 17.403 28.299 1.00103.63 C
ANISOU 1229 CG2 ILE B 197 16386 12747 10242 198 3138 -2431 C
ATOM 1230 CD1 ILE B 197 3.605 16.292 30.902 1.00138.02 C
ANISOU 1230 CD1 ILE B 197 20810 16337 15296 701 2884 -2180 C
ATOM 1231 N LEU B 198 4.681 20.445 28.627 1.00 98.39 N
ANISOU 1231 N LEU B 198 15145 12758 9483 -186 2422 -1744 N
ATOM 1232 CA LEU B 198 5.518 21.372 29.393 1.00 98.43 C
ANISOU 1232 CA LEU B 198 14758 12956 9685 -25 2307 -1477 C
ATOM 1233 C LEU B 198 5.044 22.838 29.377 1.00 94.18 C
ANISOU 1233 C LEU B 198 14119 12590 9074 -343 1920 -1190 C
ATOM 1234 O LEU B 198 5.032 23.484 30.426 1.00 90.87 O
ANISOU 1234 O LEU B 198 13498 12130 8899 -234 1686 -985 O
ATOM 1235 CB LEU B 198 6.971 21.285 28.912 1.00102.48 C
ANISOU 1235 CB LEU B 198 15045 13744 10148 120 2675 -1563 C
ATOM 1236 CG LEU B 198 7.637 19.921 29.108 1.00112.74 C
ANISOU 1236 CG LEU B 198 16358 14853 11624 554 3071 -1804 C
ATOM 1237 CD1 LEU B 198 9.077 19.957 28.631 1.00111.84 C
ANISOU 1237 CD1 LEU B 198 15936 15069 11488 707 3435 -1873 C
ATOM 1238 CD2 LEU B 198 7.559 19.478 30.566 1.00119.63 C
ANISOU 1238 CD2 LEU B 198 17124 15448 12881 945 2926 -1665 C
ATOM 1239 N PRO B 199 4.656 23.378 28.203 1.00109.98 N
ANISOU 1239 N PRO B 199 16280 14773 10735 -732 1851 -1169 N
ATOM 1240 CA PRO B 199 4.161 24.761 28.253 1.00102.99 C
ANISOU 1240 CA PRO B 199 15318 13975 9840 -981 1472 -858 C
ATOM 1241 C PRO B 199 2.796 24.907 28.938 1.00 80.59 C
ANISOU 1241 C PRO B 199 12562 10877 7183 -987 1118 -760 C
ATOM 1242 O PRO B 199 2.398 26.026 29.258 1.00 78.27 O
ANISOU 1242 O PRO B 199 12169 10578 6991 -1086 818 -509 O
ATOM 1243 CB PRO B 199 4.065 25.153 26.770 1.00 97.33 C
ANISOU 1243 CB PRO B 199 14787 13515 8681 -1376 1495 -837 C
ATOM 1244 CG PRO B 199 4.978 24.213 26.064 1.00 90.40 C
ANISOU 1244 CG PRO B 199 13969 12779 7599 -1312 1960 -1134 C
ATOM 1245 CD PRO B 199 4.849 22.927 26.814 1.00 92.65 C
ANISOU 1245 CD PRO B 199 14307 12753 8141 -956 2122 -1386 C
ATOM 1246 N SER B 200 2.097 23.797 29.157 1.00 79.87 N
ANISOU 1246 N SER B 200 12644 10559 7144 -888 1177 -962 N
ATOM 1247 CA SER B 200 0.780 23.821 29.799 1.00102.31 C
ANISOU 1247 CA SER B 200 15533 13181 10160 -908 891 -894 C
ATOM 1248 C SER B 200 0.874 23.832 31.331 1.00 86.17 C
ANISOU 1248 C SER B 200 13312 10946 8484 -590 848 -815 C
ATOM 1249 O SER B 200 -0.090 24.168 32.038 1.00 81.16 O
ANISOU 1249 O SER B 200 12642 10171 8025 -590 614 -713 O
ATOM 1250 CB SER B 200 -0.049 22.619 29.337 1.00 88.32 C
ANISOU 1250 CB SER B 200 14033 11259 8266 -1016 978 -1150 C
ATOM 1251 OG SER B 200 -0.422 22.742 27.976 1.00 90.82 O
ANISOU 1251 OG SER B 200 14526 11782 8200 -1378 914 -1202 O
ATOM 1252 N LEU B 201 2.049 23.465 31.831 1.00 72.27 N
ANISOU 1252 N LEU B 201 9013 8762 9684 1137 -1131 -304 N
ATOM 1253 CA LEU B 201 2.292 23.353 33.263 1.00 73.67 C
ANISOU 1253 CA LEU B 201 9025 9041 9924 1259 -1344 -353 C
ATOM 1254 C LEU B 201 2.090 24.674 34.001 1.00 82.87 C
ANISOU 1254 C LEU B 201 9853 10373 11261 1134 -1437 -409 C
ATOM 1255 O LEU B 201 1.732 24.679 35.178 1.00 88.87 O
ANISOU 1255 O LEU B 201 10578 11223 11965 1140 -1639 -424 O
ATOM 1256 CB LEU B 201 3.707 22.826 33.515 1.00 75.80 C
ANISOU 1256 CB LEU B 201 9131 9326 10343 1570 -1327 -456 C
ATOM 1257 CG LEU B 201 3.987 21.374 33.123 1.00 78.74 C
ANISOU 1257 CG LEU B 201 9845 9512 10560 1762 -1248 -403 C
ATOM 1258 CD1 LEU B 201 5.412 21.007 33.488 1.00 81.18 C
ANISOU 1258 CD1 LEU B 201 9906 9875 11063 2119 -1264 -512 C
ATOM 1259 CD2 LEU B 201 3.004 20.427 33.789 1.00 79.75 C
ANISOU 1259 CD2 LEU B 201 10361 9533 10408 1741 -1374 -288 C
ATOM 1260 N ILE B 202 2.315 25.792 33.318 1.00 81.01 N
ANISOU 1260 N ILE B 202 9403 10152 11224 1023 -1253 -440 N
ATOM 1261 CA ILE B 202 2.130 27.090 33.957 1.00 96.18 C
ANISOU 1261 CA ILE B 202 11014 12186 13344 888 -1278 -508 C
ATOM 1262 C ILE B 202 0.638 27.368 34.141 1.00 88.54 C
ANISOU 1262 C ILE B 202 10222 11214 12204 690 -1384 -377 C
ATOM 1263 O ILE B 202 0.225 27.985 35.127 1.00 78.60 O
ANISOU 1263 O ILE B 202 8804 10047 11013 601 -1500 -425 O
ATOM 1264 CB ILE B 202 2.798 28.234 33.152 1.00 93.41 C
ANISOU 1264 CB ILE B 202 10417 11786 13287 825 -964 -571 C
ATOM 1265 CG1 ILE B 202 2.646 29.567 33.889 1.00 85.71 C
ANISOU 1265 CG1 ILE B 202 9119 10892 12556 676 -949 -673 C
ATOM 1266 CG2 ILE B 202 2.246 28.309 31.735 1.00 83.80 C
ANISOU 1266 CG2 ILE B 202 9509 10422 11908 758 -751 -385 C
ATOM 1267 CD1 ILE B 202 3.205 29.549 35.288 1.00 79.47 C
ANISOU 1267 CD1 ILE B 202 8023 10289 11880 747 -1185 -899 C
ATOM 1268 N LEU B 203 -0.170 26.896 33.197 1.00 79.44 N
ANISOU 1268 N LEU B 203 9381 9968 10833 622 -1348 -241 N
ATOM 1269 CA LEU B 203 -1.615 27.044 33.294 1.00 75.72 C
ANISOU 1269 CA LEU B 203 9039 9512 10220 447 -1465 -154 C
ATOM 1270 C LEU B 203 -2.139 26.159 34.423 1.00 84.28 C
ANISOU 1270 C LEU B 203 10250 10599 11172 427 -1652 -181 C
ATOM 1271 O LEU B 203 -2.998 26.566 35.225 1.00101.87 O
ANISOU 1271 O LEU B 203 12418 12874 13414 296 -1745 -182 O
ATOM 1272 CB LEU B 203 -2.285 26.687 31.966 1.00 72.50 C
ANISOU 1272 CB LEU B 203 8902 9047 9597 400 -1417 -62 C
ATOM 1273 CG LEU B 203 -3.743 27.126 31.847 1.00 75.93 C
ANISOU 1273 CG LEU B 203 9366 9541 9942 240 -1535 0 C
ATOM 1274 CD1 LEU B 203 -3.832 28.642 31.900 1.00 70.82 C
ANISOU 1274 CD1 LEU B 203 8472 8936 9500 222 -1448 64 C
ATOM 1275 CD2 LEU B 203 -4.384 26.593 30.575 1.00 72.47 C
ANISOU 1275 CD2 LEU B 203 9191 9103 9243 220 -1560 31 C
ATOM 1276 N LEU B 204 -1.605 24.942 34.476 1.00 73.22 N
ANISOU 1276 N LEU B 204 9053 9120 9648 572 -1662 -196 N
ATOM 1277 CA LEU B 204 -1.905 24.033 35.572 1.00 72.68 C
ANISOU 1277 CA LEU B 204 9169 9005 9441 616 -1773 -196 C
ATOM 1278 C LEU B 204 -1.575 24.694 36.905 1.00 84.30 C
ANISOU 1278 C LEU B 204 10406 10616 11009 680 -1896 -256 C
ATOM 1279 O LEU B 204 -2.348 24.604 37.861 1.00 76.45 O
ANISOU 1279 O LEU B 204 9511 9617 9918 597 -1970 -242 O
ATOM 1280 CB LEU B 204 -1.125 22.729 35.425 1.00 68.62 C
ANISOU 1280 CB LEU B 204 8895 8364 8815 840 -1726 -187 C
ATOM 1281 CG LEU B 204 -1.352 21.722 36.554 1.00 68.57 C
ANISOU 1281 CG LEU B 204 9160 8258 8637 948 -1787 -145 C
ATOM 1282 CD1 LEU B 204 -2.814 21.317 36.583 1.00 68.70 C
ANISOU 1282 CD1 LEU B 204 9430 8143 8531 672 -1734 -121 C
ATOM 1283 CD2 LEU B 204 -0.449 20.505 36.404 1.00 67.80 C
ANISOU 1283 CD2 LEU B 204 9289 8016 8456 1238 -1717 -115 C
ATOM 1284 N ASN B 205 -0.431 25.372 36.952 1.00 75.11 N
ANISOU 1284 N ASN B 205 8923 9572 10042 812 -1895 -356 N
ATOM 1285 CA ASN B 205 -0.007 26.095 38.142 1.00 69.48 C
ANISOU 1285 CA ASN B 205 7931 9034 9435 863 -2025 -485 C
ATOM 1286 C ASN B 205 -0.994 27.194 38.500 1.00 65.03 C
ANISOU 1286 C ASN B 205 7245 8509 8956 603 -2009 -494 C
ATOM 1287 O ASN B 205 -1.299 27.409 39.664 1.00 64.84 O
ANISOU 1287 O ASN B 205 7197 8568 8872 580 -2124 -551 O
ATOM 1288 CB ASN B 205 1.388 26.684 37.934 1.00 72.78 C
ANISOU 1288 CB ASN B 205 7963 9571 10122 999 -1985 -659 C
ATOM 1289 CG ASN B 205 1.875 27.462 39.135 1.00 80.34 C
ANISOU 1289 CG ASN B 205 8581 10744 11202 1033 -2140 -870 C
ATOM 1290 OD1 ASN B 205 1.609 28.656 39.265 1.00 86.72 O
ANISOU 1290 OD1 ASN B 205 9148 11596 12207 824 -2059 -964 O
ATOM 1291 ND2 ASN B 205 2.579 26.785 40.029 1.00 82.52 N
ANISOU 1291 ND2 ASN B 205 8851 11157 11345 1317 -2365 -954 N
ATOM 1292 N MET B 206 -1.497 27.888 37.488 1.00 73.28 N
ANISOU 1292 N MET B 206 8235 9489 10121 434 -1856 -429 N
ATOM 1293 CA MET B 206 -2.508 28.916 37.708 1.00 84.66 C
ANISOU 1293 CA MET B 206 9570 10940 11658 221 -1820 -409 C
ATOM 1294 C MET B 206 -3.740 28.336 38.404 1.00 62.68 C
ANISOU 1294 C MET B 206 7018 8117 8682 109 -1918 -351 C
ATOM 1295 O MET B 206 -4.120 28.781 39.493 1.00 63.97 O
ANISOU 1295 O MET B 206 7106 8334 8867 34 -1964 -416 O
ATOM 1296 CB MET B 206 -2.917 29.562 36.383 1.00 74.24 C
ANISOU 1296 CB MET B 206 8239 9545 10425 136 -1657 -298 C
ATOM 1297 CG MET B 206 -3.784 30.804 36.552 1.00 69.39 C
ANISOU 1297 CG MET B 206 7463 8933 9969 -21 -1589 -271 C
ATOM 1298 SD MET B 206 -4.381 31.550 35.019 1.00124.87 S
ANISOU 1298 SD MET B 206 14542 15880 17021 -30 -1428 -86 S
ATOM 1299 CE MET B 206 -5.762 30.477 34.629 1.00 53.55 C
ANISOU 1299 CE MET B 206 5783 6867 7696 -91 -1631 -4 C
ATOM 1300 N TYR B 207 -4.357 27.337 37.777 1.00 61.01 N
ANISOU 1300 N TYR B 207 7089 7798 8293 82 -1917 -258 N
ATOM 1301 CA TYR B 207 -5.605 26.779 38.302 1.00 84.28 C
ANISOU 1301 CA TYR B 207 10237 10670 11115 -73 -1940 -236 C
ATOM 1302 C TYR B 207 -5.433 26.108 39.671 1.00 88.17 C
ANISOU 1302 C TYR B 207 10908 11135 11456 13 -1985 -263 C
ATOM 1303 O TYR B 207 -6.247 26.294 40.586 1.00 67.95 O
ANISOU 1303 O TYR B 207 8385 8557 8875 -117 -1967 -285 O
ATOM 1304 CB TYR B 207 -6.194 25.791 37.291 1.00 77.85 C
ANISOU 1304 CB TYR B 207 9667 9746 10169 -137 -1909 -197 C
ATOM 1305 CG TYR B 207 -6.794 26.482 36.087 1.00 79.99 C
ANISOU 1305 CG TYR B 207 9807 10074 10511 -232 -1906 -168 C
ATOM 1306 CD1 TYR B 207 -7.799 27.422 36.248 1.00 57.48 C
ANISOU 1306 CD1 TYR B 207 6763 7285 7791 -375 -1926 -167 C
ATOM 1307 CD2 TYR B 207 -6.362 26.196 34.795 1.00 80.42 C
ANISOU 1307 CD2 TYR B 207 9953 10120 10482 -148 -1878 -136 C
ATOM 1308 CE1 TYR B 207 -8.360 28.065 35.162 1.00 84.68 C
ANISOU 1308 CE1 TYR B 207 10110 10799 11268 -391 -1950 -115 C
ATOM 1309 CE2 TYR B 207 -6.921 26.837 33.695 1.00 84.32 C
ANISOU 1309 CE2 TYR B 207 10382 10686 10971 -182 -1893 -89 C
ATOM 1310 CZ TYR B 207 -7.917 27.770 33.887 1.00 95.35 C
ANISOU 1310 CZ TYR B 207 11586 12159 12484 -284 -1945 -69 C
ATOM 1311 OH TYR B 207 -8.470 28.406 32.799 1.00 68.57 O
ANISOU 1311 OH TYR B 207 8148 8851 9053 -247 -1984 2 O
ATOM 1312 N ALA B 208 -4.374 25.316 39.789 1.00 70.86 N
ANISOU 1312 N ALA B 208 8847 8932 9143 260 -2029 -254 N
ATOM 1313 CA ALA B 208 -4.025 24.662 41.041 1.00 68.80 C
ANISOU 1313 CA ALA B 208 8795 8664 8683 446 -2096 -248 C
ATOM 1314 C ALA B 208 -3.855 25.695 42.148 1.00 77.65 C
ANISOU 1314 C ALA B 208 9679 9969 9854 446 -2197 -356 C
ATOM 1315 O ALA B 208 -4.424 25.554 43.232 1.00 92.45 O
ANISOU 1315 O ALA B 208 11740 11817 11568 415 -2192 -349 O
ATOM 1316 CB ALA B 208 -2.756 23.842 40.876 1.00 70.99 C
ANISOU 1316 CB ALA B 208 9160 8945 8869 778 -2159 -228 C
ATOM 1317 N SER B 209 -3.073 26.735 41.859 1.00 67.47 N
ANISOU 1317 N SER B 209 7996 8848 8793 464 -2248 -475 N
ATOM 1318 CA SER B 209 -2.837 27.823 42.804 1.00 68.05 C
ANISOU 1318 CA SER B 209 7792 9101 8965 428 -2322 -642 C
ATOM 1319 C SER B 209 -4.138 28.464 43.246 1.00 58.20 C
ANISOU 1319 C SER B 209 6563 7790 7759 151 -2217 -631 C
ATOM 1320 O SER B 209 -4.388 28.595 44.437 1.00 54.28 O
ANISOU 1320 O SER B 209 6146 7350 7127 145 -2261 -699 O
ATOM 1321 CB SER B 209 -1.927 28.895 42.196 1.00 71.91 C
ANISOU 1321 CB SER B 209 7840 9706 9777 412 -2288 -793 C
ATOM 1322 OG SER B 209 -0.610 28.406 42.007 1.00 94.87 O
ANISOU 1322 OG SER B 209 10647 12708 12691 677 -2388 -872 O
ATOM 1323 N ILE B 210 -4.965 28.863 42.287 1.00 55.27 N
ANISOU 1323 N ILE B 210 6125 7312 7563 -53 -2082 -550 N
ATOM 1324 CA ILE B 210 -6.165 29.622 42.612 1.00 77.98 C
ANISOU 1324 CA ILE B 210 8931 10143 10554 -295 -1979 -558 C
ATOM 1325 C ILE B 210 -7.189 28.771 43.383 1.00 56.26 C
ANISOU 1325 C ILE B 210 6509 7273 7596 -381 -1934 -507 C
ATOM 1326 O ILE B 210 -7.893 29.280 44.256 1.00 49.41 O
ANISOU 1326 O ILE B 210 5622 6397 6755 -520 -1860 -568 O
ATOM 1327 CB ILE B 210 -6.804 30.229 41.334 1.00 48.64 C
ANISOU 1327 CB ILE B 210 5060 6365 7054 -424 -1880 -471 C
ATOM 1328 CG1 ILE B 210 -7.722 31.387 41.712 1.00 79.01 C
ANISOU 1328 CG1 ILE B 210 8709 10203 11110 -608 -1775 -510 C
ATOM 1329 CG2 ILE B 210 -7.557 29.181 40.525 1.00 47.86 C
ANISOU 1329 CG2 ILE B 210 5201 6159 6824 -465 -1883 -360 C
ATOM 1330 CD1 ILE B 210 -7.031 32.492 42.510 1.00 54.33 C
ANISOU 1330 CD1 ILE B 210 5338 7165 8142 -613 -1734 -672 C
ATOM 1331 N LEU B 211 -7.237 27.473 43.094 1.00 73.70 N
ANISOU 1331 N LEU B 211 9032 9361 9608 -303 -1930 -412 N
ATOM 1332 CA LEU B 211 -8.150 26.573 43.796 1.00 75.69 C
ANISOU 1332 CA LEU B 211 9636 9440 9683 -394 -1807 -372 C
ATOM 1333 C LEU B 211 -7.682 26.307 45.225 1.00 90.16 C
ANISOU 1333 C LEU B 211 11705 11303 11248 -219 -1837 -385 C
ATOM 1334 O LEU B 211 -8.474 26.368 46.176 1.00 66.10 O
ANISOU 1334 O LEU B 211 8814 8177 8123 -343 -1704 -407 O
ATOM 1335 CB LEU B 211 -8.287 25.258 43.032 1.00 53.80 C
ANISOU 1335 CB LEU B 211 7147 6491 6803 -372 -1743 -290 C
ATOM 1336 CG LEU B 211 -9.140 25.345 41.768 1.00 61.00 C
ANISOU 1336 CG LEU B 211 7905 7367 7905 -589 -1705 -312 C
ATOM 1337 CD1 LEU B 211 -9.003 24.082 40.932 1.00 71.97 C
ANISOU 1337 CD1 LEU B 211 9553 8614 9177 -548 -1662 -282 C
ATOM 1338 CD2 LEU B 211 -10.588 25.590 42.145 1.00 52.77 C
ANISOU 1338 CD2 LEU B 211 6809 6249 6992 -875 -1570 -384 C
ATOM 1339 N LEU B 212 -6.392 26.012 45.363 1.00 69.66 N
ANISOU 1339 N LEU B 212 9135 8831 8503 92 -2014 -381 N
ATOM 1340 CA LEU B 212 -5.766 25.830 46.671 1.00 65.20 C
ANISOU 1340 CA LEU B 212 8759 8375 7639 346 -2130 -410 C
ATOM 1341 C LEU B 212 -5.946 27.061 47.560 1.00 65.99 C
ANISOU 1341 C LEU B 212 8625 8647 7802 220 -2164 -580 C
ATOM 1342 O LEU B 212 -6.394 26.963 48.703 1.00 65.53 O
ANISOU 1342 O LEU B 212 8835 8559 7504 222 -2099 -587 O
ATOM 1343 CB LEU B 212 -4.276 25.524 46.497 1.00 66.31 C
ANISOU 1343 CB LEU B 212 8805 8692 7699 712 -2369 -433 C
ATOM 1344 CG LEU B 212 -3.894 24.118 46.032 1.00 77.01 C
ANISOU 1344 CG LEU B 212 10505 9872 8883 955 -2340 -261 C
ATOM 1345 CD1 LEU B 212 -2.403 24.037 45.743 1.00 73.63 C
ANISOU 1345 CD1 LEU B 212 9851 9647 8479 1300 -2574 -327 C
ATOM 1346 CD2 LEU B 212 -4.292 23.095 47.077 1.00 64.69 C
ANISOU 1346 CD2 LEU B 212 9514 8130 6936 1119 -2235 -112 C
ATOM 1347 N LEU B 213 -5.588 28.218 47.011 1.00 86.33 N
ANISOU 1347 N LEU B 213 10728 11374 10701 107 -2224 -721 N
ATOM 1348 CA LEU B 213 -5.741 29.504 47.680 1.00 83.20 C
ANISOU 1348 CA LEU B 213 10056 11108 10448 -52 -2209 -915 C
ATOM 1349 C LEU B 213 -7.192 29.758 48.063 1.00 72.44 C
ANISOU 1349 C LEU B 213 8818 9568 9135 -335 -1969 -876 C
ATOM 1350 O LEU B 213 -7.470 30.306 49.131 1.00 69.29 O
ANISOU 1350 O LEU B 213 8448 9223 8655 -407 -1922 -1001 O
ATOM 1351 CB LEU B 213 -5.233 30.640 46.784 1.00 65.29 C
ANISOU 1351 CB LEU B 213 7297 8928 8580 -154 -2205 -1035 C
ATOM 1352 CG LEU B 213 -3.722 30.774 46.582 1.00 87.15 C
ANISOU 1352 CG LEU B 213 9801 11902 11407 65 -2393 -1189 C
ATOM 1353 CD1 LEU B 213 -3.411 31.959 45.679 1.00 78.26 C
ANISOU 1353 CD1 LEU B 213 8243 10775 10717 -97 -2260 -1294 C
ATOM 1354 CD2 LEU B 213 -3.016 30.911 47.914 1.00 68.66 C
ANISOU 1354 CD2 LEU B 213 7437 9811 8842 232 -2604 -1419 C
ATOM 1355 N ALA B 214 -8.114 29.365 47.187 1.00 59.07 N
ANISOU 1355 N ALA B 214 7181 7678 7586 -498 -1819 -734 N
ATOM 1356 CA ALA B 214 -9.537 29.526 47.470 1.00 57.47 C
ANISOU 1356 CA ALA B 214 7041 7309 7485 -766 -1586 -724 C
ATOM 1357 C ALA B 214 -9.941 28.697 48.691 1.00 62.47 C
ANISOU 1357 C ALA B 214 8136 7820 7779 -736 -1458 -695 C
ATOM 1358 O ALA B 214 -10.633 29.193 49.589 1.00 67.39 O
ANISOU 1358 O ALA B 214 8801 8402 8402 -888 -1293 -779 O
ATOM 1359 CB ALA B 214 -10.371 29.139 46.254 1.00 52.18 C
ANISOU 1359 CB ALA B 214 6314 6498 7014 -914 -1504 -625 C
ATOM 1360 N THR B 215 -9.499 27.440 48.725 1.00 75.11 N
ANISOU 1360 N THR B 215 10113 9338 9086 -527 -1494 -568 N
ATOM 1361 CA THR B 215 -9.769 26.560 49.866 1.00 73.42 C
ANISOU 1361 CA THR B 215 10432 8968 8495 -432 -1334 -493 C
ATOM 1362 C THR B 215 -9.196 27.132 51.166 1.00 74.02 C
ANISOU 1362 C THR B 215 10586 9248 8288 -261 -1456 -598 C
ATOM 1363 O THR B 215 -9.864 27.148 52.208 1.00 79.87 O
ANISOU 1363 O THR B 215 11615 9886 8846 -344 -1244 -616 O
ATOM 1364 CB THR B 215 -9.189 25.142 49.647 1.00 84.65 C
ANISOU 1364 CB THR B 215 12261 10259 9643 -157 -1358 -318 C
ATOM 1365 OG1 THR B 215 -9.599 24.643 48.369 1.00 80.94 O
ANISOU 1365 OG1 THR B 215 11690 9637 9428 -318 -1277 -272 O
ATOM 1366 CG2 THR B 215 -9.671 24.189 50.732 1.00101.09 C
ANISOU 1366 CG2 THR B 215 14965 12085 11358 -81 -1084 -199 C
ATOM 1367 N ILE B 216 -7.946 27.583 51.094 1.00 70.64 N
ANISOU 1367 N ILE B 216 9899 9114 7825 -26 -1787 -695 N
ATOM 1368 CA ILE B 216 -7.263 28.209 52.222 1.00 74.74 C
ANISOU 1368 CA ILE B 216 10394 9906 8099 141 -1979 -875 C
ATOM 1369 C ILE B 216 -8.047 29.417 52.736 1.00 72.42 C
ANISOU 1369 C ILE B 216 9887 9623 8007 -183 -1805 -1062 C
ATOM 1370 O ILE B 216 -8.164 29.630 53.942 1.00 76.67 O
ANISOU 1370 O ILE B 216 10654 10228 8249 -147 -1771 -1163 O
ATOM 1371 CB ILE B 216 -5.842 28.657 51.825 1.00 72.81 C
ANISOU 1371 CB ILE B 216 9733 9982 7948 360 -2340 -1034 C
ATOM 1372 CG1 ILE B 216 -4.974 27.451 51.464 1.00 71.14 C
ANISOU 1372 CG1 ILE B 216 9739 9777 7513 739 -2519 -866 C
ATOM 1373 CG2 ILE B 216 -5.193 29.461 52.942 1.00 69.38 C
ANISOU 1373 CG2 ILE B 216 9164 9869 7328 468 -2554 -1318 C
ATOM 1374 CD1 ILE B 216 -3.715 27.822 50.704 1.00 68.20 C
ANISOU 1374 CD1 ILE B 216 8885 9647 7380 885 -2787 -1011 C
ATOM 1375 N SER B 217 -8.576 30.203 51.802 1.00 74.60 N
ANISOU 1375 N SER B 217 9746 9828 8772 -474 -1688 -1101 N
ATOM 1376 CA SER B 217 -9.360 31.397 52.111 1.00 95.12 C
ANISOU 1376 CA SER B 217 12095 12397 11648 -773 -1491 -1258 C
ATOM 1377 C SER B 217 -10.646 31.030 52.829 1.00 70.79 C
ANISOU 1377 C SER B 217 9367 9071 8460 -952 -1159 -1192 C
ATOM 1378 O SER B 217 -11.057 31.700 53.783 1.00 70.15 O
ANISOU 1378 O SER B 217 9322 8998 8333 -1075 -1009 -1343 O
ATOM 1379 CB SER B 217 -9.681 32.169 50.830 1.00108.43 C
ANISOU 1379 CB SER B 217 13319 14027 13854 -968 -1430 -1245 C
ATOM 1380 OG SER B 217 -8.498 32.635 50.207 1.00 87.08 O
ANISOU 1380 OG SER B 217 10291 11512 11285 -837 -1650 -1329 O
ATOM 1381 N ALA B 218 -11.284 29.964 52.354 1.00 70.22 N
ANISOU 1381 N ALA B 218 9545 8764 8371 -986 -1010 -996 N
ATOM 1382 CA ALA B 218 -12.461 29.424 53.025 1.00 94.72 C
ANISOU 1382 CA ALA B 218 13015 11592 11382 -1159 -639 -946 C
ATOM 1383 C ALA B 218 -12.113 29.046 54.466 1.00 78.96 C
ANISOU 1383 C ALA B 218 11541 9620 8841 -957 -597 -949 C
ATOM 1384 O ALA B 218 -12.865 29.344 55.408 1.00 76.88 O
ANISOU 1384 O ALA B 218 11468 9243 8499 -1114 -308 -1028 O
ATOM 1385 CB ALA B 218 -13.006 28.218 52.261 1.00 78.49 C
ANISOU 1385 CB ALA B 218 11153 9286 9385 -1214 -493 -779 C
ATOM 1386 N ASP B 219 -10.958 28.405 54.628 1.00 70.02 N
ANISOU 1386 N ASP B 219 10640 8645 7320 -582 -889 -866 N
ATOM 1387 CA ASP B 219 -10.473 28.009 55.946 1.00 73.08 C
ANISOU 1387 CA ASP B 219 11543 9116 7109 -283 -938 -849 C
ATOM 1388 C ASP B 219 -10.290 29.219 56.860 1.00 73.77 C
ANISOU 1388 C ASP B 219 11452 9459 7118 -337 -1028 -1124 C
ATOM 1389 O ASP B 219 -10.704 29.188 58.015 1.00 80.67 O
ANISOU 1389 O ASP B 219 12745 10270 7635 -326 -826 -1153 O
ATOM 1390 CB ASP B 219 -9.154 27.250 55.826 1.00 81.43 C
ANISOU 1390 CB ASP B 219 12750 10366 7826 182 -1320 -741 C
ATOM 1391 CG ASP B 219 -8.704 26.654 57.144 1.00102.78 C
ANISOU 1391 CG ASP B 219 16068 13142 9841 578 -1385 -666 C
ATOM 1392 OD1 ASP B 219 -9.565 26.138 57.887 1.00 95.26 O
ANISOU 1392 OD1 ASP B 219 15669 11895 8632 517 -989 -536 O
ATOM 1393 OD2 ASP B 219 -7.490 26.706 57.436 1.00112.35 O
ANISOU 1393 OD2 ASP B 219 17212 14711 10767 964 -1824 -748 O
ATOM 1394 N ARG B 220 -9.670 30.276 56.340 1.00 72.71 N
ANISOU 1394 N ARG B 220 10721 9588 7318 -403 -1292 -1337 N
ATOM 1395 CA ARG B 220 -9.458 31.506 57.103 1.00 77.75 C
ANISOU 1395 CA ARG B 220 11121 10457 7963 -501 -1357 -1656 C
ATOM 1396 C ARG B 220 -10.786 32.115 57.549 1.00 72.46 C
ANISOU 1396 C ARG B 220 10489 9543 7498 -870 -912 -1721 C
ATOM 1397 O ARG B 220 -10.975 32.471 58.725 1.00 75.13 O
ANISOU 1397 O ARG B 220 11081 9931 7534 -889 -796 -1878 O
ATOM 1398 CB ARG B 220 -8.677 32.529 56.271 1.00 67.74 C
ANISOU 1398 CB ARG B 220 9181 9413 7144 -574 -1600 -1866 C
ATOM 1399 CG ARG B 220 -7.327 32.063 55.760 1.00 66.62 C
ANISOU 1399 CG ARG B 220 8894 9517 6900 -243 -2010 -1859 C
ATOM 1400 CD ARG B 220 -6.454 31.548 56.884 1.00 76.59 C
ANISOU 1400 CD ARG B 220 10497 11064 7540 154 -2321 -1946 C
ATOM 1401 NE ARG B 220 -6.419 32.463 58.020 1.00 90.29 N
ANISOU 1401 NE ARG B 220 12205 13008 9094 75 -2347 -2281 N
ATOM 1402 CZ ARG B 220 -5.577 32.346 59.040 1.00105.77 C
ANISOU 1402 CZ ARG B 220 14341 15320 10529 404 -2686 -2475 C
ATOM 1403 NH1 ARG B 220 -5.609 33.220 60.038 1.00 88.09 N
ANISOU 1403 NH1 ARG B 220 12072 13271 8129 293 -2692 -2820 N
ATOM 1404 NH2 ARG B 220 -4.695 31.356 59.057 1.00101.18 N
ANISOU 1404 NH2 ARG B 220 13961 14909 9573 864 -3028 -2337 N
ATOM 1405 N PHE B 221 -11.697 32.240 56.589 1.00 70.40 N
ANISOU 1405 N PHE B 221 9962 9036 7751 -1147 -672 -1616 N
ATOM 1406 CA PHE B 221 -13.023 32.772 56.854 1.00 72.78 C
ANISOU 1406 CA PHE B 221 10219 9093 8342 -1488 -245 -1672 C
ATOM 1407 C PHE B 221 -13.700 32.022 57.984 1.00 76.61 C
ANISOU 1407 C PHE B 221 11330 9372 8407 -1488 86 -1602 C
ATOM 1408 O PHE B 221 -14.257 32.636 58.886 1.00 77.68 O
ANISOU 1408 O PHE B 221 11563 9451 8501 -1648 353 -1763 O
ATOM 1409 CB PHE B 221 -13.898 32.702 55.606 1.00 66.92 C
ANISOU 1409 CB PHE B 221 9150 8140 8137 -1700 -96 -1540 C
ATOM 1410 CG PHE B 221 -15.184 33.462 55.729 1.00 65.49 C
ANISOU 1410 CG PHE B 221 8754 7764 8366 -2024 283 -1640 C
ATOM 1411 CD1 PHE B 221 -15.251 34.791 55.348 1.00 75.83 C
ANISOU 1411 CD1 PHE B 221 9556 9146 10109 -2150 273 -1785 C
ATOM 1412 CD2 PHE B 221 -16.327 32.854 56.226 1.00 72.56 C
ANISOU 1412 CD2 PHE B 221 9951 8377 9242 -2195 687 -1596 C
ATOM 1413 CE1 PHE B 221 -16.430 35.500 55.456 1.00 93.80 C
ANISOU 1413 CE1 PHE B 221 11618 11239 12784 -2403 621 -1869 C
ATOM 1414 CE2 PHE B 221 -17.510 33.559 56.336 1.00 86.01 C
ANISOU 1414 CE2 PHE B 221 11404 9909 11368 -2481 1040 -1713 C
ATOM 1415 CZ PHE B 221 -17.561 34.884 55.950 1.00 73.70 C
ANISOU 1415 CZ PHE B 221 9328 8447 10230 -2566 987 -1842 C
ATOM 1416 N LEU B 222 -13.656 30.694 57.929 1.00 81.40 N
ANISOU 1416 N LEU B 222 12388 9831 8709 -1309 118 -1361 N
ATOM 1417 CA LEU B 222 -14.294 29.884 58.961 1.00 82.35 C
ANISOU 1417 CA LEU B 222 13181 9687 8420 -1294 511 -1256 C
ATOM 1418 C LEU B 222 -13.575 30.010 60.302 1.00 89.35 C
ANISOU 1418 C LEU B 222 14509 10793 8646 -1008 374 -1342 C
ATOM 1419 O LEU B 222 -14.201 29.975 61.361 1.00 85.16 O
ANISOU 1419 O LEU B 222 14429 10099 7828 -1077 744 -1370 O
ATOM 1420 CB LEU B 222 -14.352 28.423 58.527 1.00 80.33 C
ANISOU 1420 CB LEU B 222 13321 9184 8016 -1158 611 -977 C
ATOM 1421 CG LEU B 222 -15.258 28.170 57.324 1.00 78.35 C
ANISOU 1421 CG LEU B 222 12710 8693 8367 -1475 807 -938 C
ATOM 1422 CD1 LEU B 222 -15.308 26.691 56.989 1.00 80.48 C
ANISOU 1422 CD1 LEU B 222 13415 8689 8475 -1368 960 -711 C
ATOM 1423 CD2 LEU B 222 -16.652 28.714 57.595 1.00 78.51 C
ANISOU 1423 CD2 LEU B 222 12574 8481 8776 -1886 1279 -1086 C
ATOM 1424 N LEU B 223 -12.255 30.157 60.248 1.00 93.34 N
ANISOU 1424 N LEU B 223 14874 11682 8908 -681 -158 -1406 N
ATOM 1425 CA LEU B 223 -11.454 30.360 61.448 1.00 91.71 C
ANISOU 1425 CA LEU B 223 14984 11788 8075 -375 -406 -1554 C
ATOM 1426 C LEU B 223 -11.872 31.638 62.157 1.00 99.78 C
ANISOU 1426 C LEU B 223 15805 12897 9210 -657 -248 -1887 C
ATOM 1427 O LEU B 223 -11.811 31.723 63.383 1.00147.66 O
ANISOU 1427 O LEU B 223 22316 19061 14727 -528 -197 -1999 O
ATOM 1428 CB LEU B 223 -9.962 30.418 61.105 1.00 90.51 C
ANISOU 1428 CB LEU B 223 14529 12070 7791 -19 -1034 -1645 C
ATOM 1429 CG LEU B 223 -9.239 29.102 60.813 1.00103.44 C
ANISOU 1429 CG LEU B 223 16509 13709 9082 424 -1268 -1346 C
ATOM 1430 CD1 LEU B 223 -7.826 29.366 60.313 1.00 97.73 C
ANISOU 1430 CD1 LEU B 223 15299 13418 8414 697 -1859 -1506 C
ATOM 1431 CD2 LEU B 223 -9.216 28.223 62.052 1.00118.20 C
ANISOU 1431 CD2 LEU B 223 19229 15526 10154 803 -1178 -1170 C
ATOM 1432 N VAL B 224 -12.299 32.632 61.383 1.00101.61 N
ANISOU 1432 N VAL B 224 15393 13081 10134 -1022 -155 -2042 N
ATOM 1433 CA VAL B 224 -12.705 33.909 61.968 1.00 87.58 C
ANISOU 1433 CA VAL B 224 13381 11346 8550 -1304 36 -2366 C
ATOM 1434 C VAL B 224 -14.189 33.959 62.366 1.00 87.95 C
ANISOU 1434 C VAL B 224 13646 10990 8783 -1631 661 -2320 C
ATOM 1435 O VAL B 224 -14.527 34.410 63.461 1.00 95.73 O
ANISOU 1435 O VAL B 224 14906 11961 9507 -1716 906 -2506 O
ATOM 1436 CB VAL B 224 -12.406 35.080 61.002 1.00 98.16 C
ANISOU 1436 CB VAL B 224 13934 12809 10555 -1508 -124 -2564 C
ATOM 1437 CG1 VAL B 224 -13.016 36.376 61.514 1.00 92.34 C
ANISOU 1437 CG1 VAL B 224 12963 12009 10113 -1831 185 -2867 C
ATOM 1438 CG2 VAL B 224 -10.906 35.239 60.809 1.00 97.41 C
ANISOU 1438 CG2 VAL B 224 13582 13126 10304 -1237 -677 -2724 C
ATOM 1439 N PHE B 225 -15.071 33.487 61.490 1.00 90.47 N
ANISOU 1439 N PHE B 225 13831 10992 9550 -1816 923 -2104 N
ATOM 1440 CA PHE B 225 -16.506 33.699 61.669 1.00 94.53 C
ANISOU 1440 CA PHE B 225 14344 11146 10427 -2171 1501 -2126 C
ATOM 1441 C PHE B 225 -17.293 32.470 62.128 1.00104.51 C
ANISOU 1441 C PHE B 225 16230 12054 11424 -2186 1940 -1913 C
ATOM 1442 O PHE B 225 -18.380 32.609 62.685 1.00103.96 O
ANISOU 1442 O PHE B 225 16305 11700 11497 -2448 2475 -1985 O
ATOM 1443 CB PHE B 225 -17.117 34.222 60.366 1.00 91.25 C
ANISOU 1443 CB PHE B 225 13238 10630 10801 -2414 1528 -2115 C
ATOM 1444 CG PHE B 225 -16.532 35.525 59.905 1.00101.02 C
ANISOU 1444 CG PHE B 225 13890 12110 12382 -2443 1251 -2311 C
ATOM 1445 CD1 PHE B 225 -16.941 36.719 60.472 1.00 88.80 C
ANISOU 1445 CD1 PHE B 225 12145 10535 11061 -2648 1497 -2570 C
ATOM 1446 CD2 PHE B 225 -15.570 35.555 58.909 1.00 88.76 C
ANISOU 1446 CD2 PHE B 225 12005 10776 10942 -2274 802 -2245 C
ATOM 1447 CE1 PHE B 225 -16.405 37.921 60.056 1.00 83.65 C
ANISOU 1447 CE1 PHE B 225 10984 10049 10752 -2688 1316 -2757 C
ATOM 1448 CE2 PHE B 225 -15.029 36.755 58.487 1.00 79.41 C
ANISOU 1448 CE2 PHE B 225 10315 9761 10097 -2317 630 -2430 C
ATOM 1449 CZ PHE B 225 -15.449 37.940 59.062 1.00 96.28 C
ANISOU 1449 CZ PHE B 225 12269 11846 12466 -2526 895 -2684 C
ATOM 1450 N LYS B 226 -16.761 31.275 61.890 1.00121.21 N
ANISOU 1450 N LYS B 226 18713 14153 13190 -1915 1767 -1662 N
ATOM 1451 CA LYS B 226 -17.429 30.050 62.327 1.00129.42 C
ANISOU 1451 CA LYS B 226 20402 14805 13964 -1915 2235 -1451 C
ATOM 1452 C LYS B 226 -16.454 29.096 63.009 1.00123.45 C
ANISOU 1452 C LYS B 226 20365 14145 12396 -1442 2031 -1246 C
ATOM 1453 O LYS B 226 -16.233 27.990 62.521 1.00131.36 O
ANISOU 1453 O LYS B 226 21611 15003 13296 -1270 2000 -998 O
ATOM 1454 CB LYS B 226 -18.093 29.348 61.137 1.00126.09 C
ANISOU 1454 CB LYS B 226 19707 14122 14078 -2114 2381 -1321 C
ATOM 1455 CG LYS B 226 -19.183 30.155 60.454 1.00126.59 C
ANISOU 1455 CG LYS B 226 19092 14081 14924 -2532 2592 -1503 C
ATOM 1456 CD LYS B 226 -20.378 30.365 61.372 1.00134.63 C
ANISOU 1456 CD LYS B 226 20318 14786 16050 -2829 3245 -1638 C
ATOM 1457 CE LYS B 226 -21.456 31.191 60.688 1.00140.16 C
ANISOU 1457 CE LYS B 226 20290 15409 17554 -3192 3422 -1828 C
ATOM 1458 NZ LYS B 226 -22.642 31.411 61.562 1.00128.43 N
ANISOU 1458 NZ LYS B 226 18948 13607 16242 -3491 4091 -1988 N
ATOM 1459 N PRO B 227 -15.866 29.520 64.142 1.00114.71 N
ANISOU 1459 N PRO B 227 19602 13287 10696 -1210 1884 -1360 N
ATOM 1460 CA PRO B 227 -14.800 28.725 64.764 1.00118.14 C
ANISOU 1460 CA PRO B 227 20653 13913 10321 -667 1560 -1182 C
ATOM 1461 C PRO B 227 -15.274 27.361 65.267 1.00111.23 C
ANISOU 1461 C PRO B 227 20651 12597 9015 -511 2055 -847 C
ATOM 1462 O PRO B 227 -14.506 26.397 65.237 1.00113.79 O
ANISOU 1462 O PRO B 227 21385 12957 8894 -72 1820 -590 O
ATOM 1463 CB PRO B 227 -14.345 29.608 65.931 1.00130.77 C
ANISOU 1463 CB PRO B 227 22402 15859 11425 -536 1378 -1452 C
ATOM 1464 CG PRO B 227 -15.528 30.419 66.262 1.00116.57 C
ANISOU 1464 CG PRO B 227 20456 13814 10020 -1020 1924 -1657 C
ATOM 1465 CD PRO B 227 -16.210 30.700 64.955 1.00 93.95 C
ANISOU 1465 CD PRO B 227 16857 10761 8079 -1418 2040 -1668 C
ATOM 1466 N ILE B 228 -16.524 27.287 65.715 1.00114.88 N
ANISOU 1466 N ILE B 228 21390 12622 9637 -865 2770 -858 N
ATOM 1467 CA ILE B 228 -17.087 26.040 66.218 1.00119.87 C
ANISOU 1467 CA ILE B 228 22867 12751 9926 -787 3382 -568 C
ATOM 1468 C ILE B 228 -17.000 24.936 65.164 1.00128.75 C
ANISOU 1468 C ILE B 228 23952 13644 11324 -738 3371 -325 C
ATOM 1469 O ILE B 228 -16.607 23.808 65.474 1.00140.85 O
ANISOU 1469 O ILE B 228 26203 14983 12331 -359 3477 -18 O
ATOM 1470 CB ILE B 228 -18.553 26.219 66.660 1.00120.39 C
ANISOU 1470 CB ILE B 228 23053 12352 10339 -1288 4213 -689 C
ATOM 1471 CG1 ILE B 228 -18.649 27.275 67.762 1.00134.78 C
ANISOU 1471 CG1 ILE B 228 24989 14368 11852 -1331 4282 -935 C
ATOM 1472 CG2 ILE B 228 -19.132 24.893 67.127 1.00119.57 C
ANISOU 1472 CG2 ILE B 228 23826 11667 9937 -1242 4927 -403 C
ATOM 1473 CD1 ILE B 228 -20.041 27.426 68.336 1.00132.30 C
ANISOU 1473 CD1 ILE B 228 24870 13584 11813 -1780 5148 -1052 C
ATOM 1474 N TRP B 229 -17.353 25.276 63.923 1.00134.87 N
ANISOU 1474 N TRP B 229 23908 14441 12896 -1097 3245 -463 N
ATOM 1475 CA TRP B 229 -17.214 24.364 62.787 1.00125.22 C
ANISOU 1475 CA TRP B 229 22532 13071 11976 -1082 3155 -300 C
ATOM 1476 C TRP B 229 -15.803 23.790 62.746 1.00124.85 C
ANISOU 1476 C TRP B 229 22768 13298 11370 -491 2596 -76 C
ATOM 1477 O TRP B 229 -15.620 22.578 62.619 1.00142.00 O
ANISOU 1477 O TRP B 229 25451 15187 13314 -263 2765 194 O
ATOM 1478 CB TRP B 229 -17.523 25.070 61.459 1.00135.11 C
ANISOU 1478 CB TRP B 229 22804 14485 14048 -1447 2893 -510 C
ATOM 1479 CG TRP B 229 -18.927 25.575 61.306 1.00148.76 C
ANISOU 1479 CG TRP B 229 24144 15964 16415 -1993 3386 -734 C
ATOM 1480 CD1 TRP B 229 -19.858 25.741 62.291 1.00148.23 C
ANISOU 1480 CD1 TRP B 229 24402 15613 16308 -2223 3994 -827 C
ATOM 1481 CD2 TRP B 229 -19.559 25.983 60.087 1.00153.56 C
ANISOU 1481 CD2 TRP B 229 23951 16599 17798 -2349 3305 -902 C
ATOM 1482 NE1 TRP B 229 -21.028 26.229 61.760 1.00139.54 N
ANISOU 1482 NE1 TRP B 229 22701 14362 15956 -2705 4293 -1058 N
ATOM 1483 CE2 TRP B 229 -20.870 26.385 60.408 1.00147.56 C
ANISOU 1483 CE2 TRP B 229 23022 15581 17462 -2770 3852 -1103 C
ATOM 1484 CE3 TRP B 229 -19.141 26.046 58.754 1.00133.67 C
ANISOU 1484 CE3 TRP B 229 20855 14303 15632 -2328 2824 -902 C
ATOM 1485 CZ2 TRP B 229 -21.766 26.844 59.445 1.00145.66 C
ANISOU 1485 CZ2 TRP B 229 22029 15331 17983 -3135 3883 -1306 C
ATOM 1486 CZ3 TRP B 229 -20.031 26.502 57.800 1.00120.51 C
ANISOU 1486 CZ3 TRP B 229 18500 12619 14667 -2689 2865 -1086 C
ATOM 1487 CH2 TRP B 229 -21.329 26.895 58.150 1.00125.95 C
ANISOU 1487 CH2 TRP B 229 19008 13082 15766 -3071 3366 -1287 C
HETATM 1488 N YCM B 230 -14.815 24.672 62.880 1.00120.62 N
ANISOU 1488 N YCM B 230 21892 13301 10637 -246 1958 -214 N
HETATM 1489 CA YCM B 230 -13.427 24.275 62.921 1.00119.49 C
ANISOU 1489 CA YCM B 230 21919 13496 9986 331 1374 -71 C
HETATM 1490 CB YCM B 230 -12.478 25.473 62.876 1.00115.99 C
ANISOU 1490 CB YCM B 230 20851 13657 9563 440 702 -353 C
HETATM 1491 SG YCM B 230 -12.900 26.714 61.690 1.00142.52 S
ANISOU 1491 SG YCM B 230 23145 17143 13862 -109 586 -655 S
HETATM 1492 CD YCM B 230 -11.910 26.352 60.275 1.00112.68 C
ANISOU 1492 CD YCM B 230 18874 13557 10383 78 74 -566 C
HETATM 1493 CE YCM B 230 -12.598 25.476 59.251 1.00 96.61 C
ANISOU 1493 CE YCM B 230 16828 11126 8753 -137 385 -384 C
HETATM 1494 OZ1 YCM B 230 -13.708 24.954 59.496 1.00116.07 O
ANISOU 1494 OZ1 YCM B 230 19643 13166 11293 -390 953 -306 O
HETATM 1495 NZ2 YCM B 230 -11.983 25.267 58.047 1.00 91.09 N
ANISOU 1495 NZ2 YCM B 230 15720 10543 8348 -67 55 -341 N
HETATM 1496 C YCM B 230 -13.067 23.336 64.075 1.00146.73 C
ANISOU 1496 C YCM B 230 26375 16815 12561 848 1528 210 C
HETATM 1497 O YCM B 230 -12.226 22.441 63.968 1.00161.22 O
ANISOU 1497 O YCM B 230 28549 18681 14026 1336 1282 462 O
ATOM 1498 N GLN B 231 -13.719 23.542 65.216 1.00146.23 N
ANISOU 1498 N GLN B 231 26831 16590 12141 770 1965 179 N
ATOM 1499 CA GLN B 231 -13.537 22.639 66.352 1.00125.21 C
ANISOU 1499 CA GLN B 231 25231 13732 8610 1256 2223 480 C
ATOM 1500 C GLN B 231 -14.264 21.317 66.107 1.00123.98 C
ANISOU 1500 C GLN B 231 25660 12890 8556 1171 2933 802 C
ATOM 1501 O GLN B 231 -13.899 20.285 66.668 1.00147.60 O
ANISOU 1501 O GLN B 231 29297 15666 11117 1645 3028 1108 O
ATOM 1502 CB GLN B 231 -14.024 23.291 67.650 1.00127.96 C
ANISOU 1502 CB GLN B 231 25997 14105 8518 1187 2517 334 C
ATOM 1503 CG GLN B 231 -13.165 24.459 68.108 1.00129.35 C
ANISOU 1503 CG GLN B 231 25768 14961 8418 1368 1821 9 C
ATOM 1504 CD GLN B 231 -13.874 25.355 69.103 1.00144.75 C
ANISOU 1504 CD GLN B 231 27873 16908 10218 1080 2171 -251 C
ATOM 1505 OE1 GLN B 231 -15.053 25.672 68.942 1.00152.40 O
ANISOU 1505 OE1 GLN B 231 28656 17498 11752 513 2774 -357 O
ATOM 1506 NE2 GLN B 231 -13.157 25.770 70.139 1.00155.71 N
ANISOU 1506 NE2 GLN B 231 29378 18732 11054 1449 1746 -370 N
ATOM 1507 N ASN B 232 -15.281 21.353 65.250 1.00115.41 N
ANISOU 1507 N ASN B 232 24094 11469 8287 555 3350 670 N
ATOM 1508 CA ASN B 232 -16.073 20.163 64.943 1.00122.55 C
ANISOU 1508 CA ASN B 232 25438 11709 9417 359 4070 873 C
ATOM 1509 C ASN B 232 -15.560 19.376 63.734 1.00120.75 C
ANISOU 1509 C ASN B 232 24945 11434 9499 462 3811 1001 C
ATOM 1510 O ASN B 232 -15.610 18.144 63.713 1.00135.82 O
ANISOU 1510 O ASN B 232 27486 12880 11240 632 4228 1278 O
ATOM 1511 CB ASN B 232 -17.533 20.555 64.709 1.00115.76 C
ANISOU 1511 CB ASN B 232 24197 10501 9283 -375 4701 606 C
ATOM 1512 CG ASN B 232 -18.260 20.893 65.995 1.00134.57 C
ANISOU 1512 CG ASN B 232 27122 12673 11336 -493 5280 556 C
ATOM 1513 OD1 ASN B 232 -17.639 21.253 66.996 1.00176.43 O
ANISOU 1513 OD1 ASN B 232 32862 18259 15916 -87 5035 619 O
ATOM 1514 ND2 ASN B 232 -19.583 20.772 65.977 1.00124.30 N
ANISOU 1514 ND2 ASN B 232 25785 10879 10563 -1052 6058 413 N
ATOM 1515 N PHE B 233 -15.064 20.093 62.731 1.00118.55 N
ANISOU 1515 N PHE B 233 23762 11608 9673 359 3164 796 N
ATOM 1516 CA PHE B 233 -14.685 19.483 61.460 1.00123.27 C
ANISOU 1516 CA PHE B 233 24007 12174 10656 365 2939 856 C
ATOM 1517 C PHE B 233 -13.200 19.152 61.359 1.00156.34 C
ANISOU 1517 C PHE B 233 28303 16719 14382 1020 2291 1050 C
ATOM 1518 O PHE B 233 -12.833 18.014 61.072 1.00175.09 O
ANISOU 1518 O PHE B 233 31101 18822 16603 1308 2407 1310 O
ATOM 1519 CB PHE B 233 -15.050 20.405 60.292 1.00106.81 C
ANISOU 1519 CB PHE B 233 20885 10337 9363 -129 2660 534 C
ATOM 1520 CG PHE B 233 -16.499 20.373 59.908 1.00106.51 C
ANISOU 1520 CG PHE B 233 20618 9901 9951 -762 3264 350 C
ATOM 1521 CD1 PHE B 233 -17.068 19.211 59.421 1.00106.89 C
ANISOU 1521 CD1 PHE B 233 20936 9447 10229 -947 3765 426 C
ATOM 1522 CD2 PHE B 233 -17.281 21.515 59.992 1.00119.45 C
ANISOU 1522 CD2 PHE B 233 21720 11676 11991 -1173 3323 65 C
ATOM 1523 CE1 PHE B 233 -18.393 19.177 59.049 1.00110.43 C
ANISOU 1523 CE1 PHE B 233 21097 9568 11292 -1539 4292 190 C
ATOM 1524 CE2 PHE B 233 -18.608 21.485 59.621 1.00125.67 C
ANISOU 1524 CE2 PHE B 233 22230 12134 13386 -1724 3841 -133 C
ATOM 1525 CZ PHE B 233 -19.164 20.312 59.151 1.00128.84 C
ANISOU 1525 CZ PHE B 233 22871 12070 14012 -1913 4311 -88 C
ATOM 1526 N ARG B 234 -12.362 20.162 61.584 1.00164.45 N
ANISOU 1526 N ARG B 234 28910 18341 15232 1238 1634 892 N
ATOM 1527 CA ARG B 234 -10.938 20.133 61.243 1.00160.85 C
ANISOU 1527 CA ARG B 234 28226 18337 14554 1754 916 943 C
ATOM 1528 C ARG B 234 -10.176 18.859 61.590 1.00160.28 C
ANISOU 1528 C ARG B 234 28910 18104 13887 2408 905 1317 C
ATOM 1529 O ARG B 234 -10.033 18.489 62.757 1.00163.68 O
ANISOU 1529 O ARG B 234 30101 18473 13618 2829 1033 1514 O
ATOM 1530 CB ARG B 234 -10.236 21.312 61.911 1.00162.14 C
ANISOU 1530 CB ARG B 234 28064 19103 14440 1937 353 701 C
ATOM 1531 CG ARG B 234 -9.638 22.322 60.961 1.00143.70 C
ANISOU 1531 CG ARG B 234 24743 17225 12631 1759 -208 404 C
ATOM 1532 CD ARG B 234 -9.138 23.527 61.752 1.00131.01 C
ANISOU 1532 CD ARG B 234 22856 16133 10788 1839 -620 102 C
ATOM 1533 NE ARG B 234 -8.712 24.627 60.891 1.00121.30 N
ANISOU 1533 NE ARG B 234 20691 15266 10130 1581 -1025 -213 N
ATOM 1534 CZ ARG B 234 -7.444 24.955 60.656 1.00113.75 C
ANISOU 1534 CZ ARG B 234 19314 14777 9128 1897 -1632 -360 C
ATOM 1535 NH1 ARG B 234 -6.456 24.265 61.211 1.00127.12 N
ANISOU 1535 NH1 ARG B 234 21392 16682 10224 2518 -1976 -230 N
ATOM 1536 NH2 ARG B 234 -7.162 25.975 59.856 1.00107.27 N
ANISOU 1536 NH2 ARG B 234 17684 14201 8871 1608 -1876 -642 N
ATOM 1537 N GLY B 235 -9.686 18.206 60.544 1.00144.20 N
ANISOU 1537 N GLY B 235 26662 15995 12133 2508 759 1416 N
ATOM 1538 CA GLY B 235 -8.737 17.120 60.671 1.00133.57 C
ANISOU 1538 CA GLY B 235 25851 14585 10315 3183 613 1741 C
ATOM 1539 C GLY B 235 -7.823 17.190 59.466 1.00129.70 C
ANISOU 1539 C GLY B 235 24658 14395 10226 3265 85 1642 C
ATOM 1540 O GLY B 235 -8.071 17.969 58.544 1.00114.88 O
ANISOU 1540 O GLY B 235 22001 12683 8967 2770 -56 1362 O
ATOM 1541 N ALA B 236 -6.765 16.388 59.464 1.00134.10 N
ANISOU 1541 N ALA B 236 25372 15024 10555 3861 -178 1822 N
ATOM 1542 CA ALA B 236 -5.864 16.330 58.319 1.00115.19 C
ANISOU 1542 CA ALA B 236 22438 12856 8474 3991 -610 1771 C
ATOM 1543 C ALA B 236 -6.606 15.864 57.066 1.00117.21 C
ANISOU 1543 C ALA B 236 22557 12667 9310 3477 -187 1774 C
ATOM 1544 O ALA B 236 -6.354 16.350 55.959 1.00121.99 O
ANISOU 1544 O ALA B 236 22434 13489 10430 3209 -459 1560 O
ATOM 1545 CB ALA B 236 -4.692 15.409 58.616 1.00139.94 C
ANISOU 1545 CB ALA B 236 25659 16079 11431 4636 -820 1894 C
ATOM 1546 N GLY B 237 -7.534 14.932 57.260 1.00136.67 N
ANISOU 1546 N GLY B 237 25688 14511 11729 3311 508 1972 N
ATOM 1547 CA GLY B 237 -8.261 14.315 56.166 1.00109.04 C
ANISOU 1547 CA GLY B 237 22092 10560 8777 2829 958 1928 C
ATOM 1548 C GLY B 237 -9.009 15.279 55.267 1.00100.29 C
ANISOU 1548 C GLY B 237 20170 9615 8323 2120 902 1565 C
ATOM 1549 O GLY B 237 -8.885 15.206 54.049 1.00110.48 O
ANISOU 1549 O GLY B 237 20995 10933 10050 1913 783 1445 O
ATOM 1550 N LEU B 238 -9.787 16.180 55.862 1.00 96.33 N
ANISOU 1550 N LEU B 238 19517 9215 7869 1777 998 1398 N
ATOM 1551 CA LEU B 238 -10.565 17.149 55.091 1.00 92.96 C
ANISOU 1551 CA LEU B 238 18338 8936 8045 1152 957 1075 C
ATOM 1552 C LEU B 238 -9.664 18.060 54.261 1.00 89.54 C
ANISOU 1552 C LEU B 238 17127 9042 7851 1216 298 907 C
ATOM 1553 O LEU B 238 -9.970 18.372 53.108 1.00 99.98 O
ANISOU 1553 O LEU B 238 17900 10409 9678 849 237 735 O
ATOM 1554 CB LEU B 238 -11.446 17.993 56.016 1.00 94.04 C
ANISOU 1554 CB LEU B 238 18481 9100 8150 859 1168 942 C
ATOM 1555 CG LEU B 238 -12.721 17.351 56.568 1.00 97.76 C
ANISOU 1555 CG LEU B 238 19500 9001 8644 534 1941 985 C
ATOM 1556 CD1 LEU B 238 -13.456 18.319 57.485 1.00119.60 C
ANISOU 1556 CD1 LEU B 238 22208 11857 11378 282 2096 833 C
ATOM 1557 CD2 LEU B 238 -13.624 16.901 55.433 1.00 96.18 C
ANISOU 1557 CD2 LEU B 238 18998 8482 9064 7 2280 822 C
ATOM 1558 N ALA B 239 -8.553 18.482 54.857 1.00 82.51 N
ANISOU 1558 N ALA B 239 16202 8560 6586 1690 -180 940 N
ATOM 1559 CA ALA B 239 -7.574 19.316 54.168 1.00 79.42 C
ANISOU 1559 CA ALA B 239 15104 8659 6412 1784 -760 765 C
ATOM 1560 C ALA B 239 -6.981 18.574 52.974 1.00 85.80 C
ANISOU 1560 C ALA B 239 15781 9379 7441 1901 -844 841 C
ATOM 1561 O ALA B 239 -6.885 19.127 51.872 1.00 81.50 O
ANISOU 1561 O ALA B 239 14632 8995 7338 1641 -1020 672 O
ATOM 1562 CB ALA B 239 -6.476 19.747 55.124 1.00 80.36 C
ANISOU 1562 CB ALA B 239 15248 9215 6071 2295 -1228 748 C
ATOM 1563 N TRP B 240 -6.590 17.319 53.197 1.00110.06 N
ANISOU 1563 N TRP B 240 19458 12172 10189 2309 -685 1104 N
ATOM 1564 CA TRP B 240 -6.006 16.505 52.134 1.00 89.23 C
ANISOU 1564 CA TRP B 240 16772 9401 7730 2453 -710 1183 C
ATOM 1565 C TRP B 240 -7.000 16.238 51.004 1.00 90.38 C
ANISOU 1565 C TRP B 240 16756 9222 8362 1879 -344 1074 C
ATOM 1566 O TRP B 240 -6.623 16.241 49.831 1.00121.64 O
ANISOU 1566 O TRP B 240 20319 13266 12632 1793 -501 980 O
ATOM 1567 CB TRP B 240 -5.481 15.182 52.693 1.00 83.18 C
ANISOU 1567 CB TRP B 240 16758 8335 6510 3025 -540 1508 C
ATOM 1568 CG TRP B 240 -4.169 15.323 53.402 1.00 89.62 C
ANISOU 1568 CG TRP B 240 17584 9566 6902 3708 -1059 1590 C
ATOM 1569 CD1 TRP B 240 -3.914 15.063 54.717 1.00106.47 C
ANISOU 1569 CD1 TRP B 240 20286 11739 8430 4206 -1105 1783 C
ATOM 1570 CD2 TRP B 240 -2.931 15.771 52.836 1.00 89.23 C
ANISOU 1570 CD2 TRP B 240 16927 9975 7001 3978 -1612 1447 C
ATOM 1571 NE1 TRP B 240 -2.594 15.313 55.002 1.00104.05 N
ANISOU 1571 NE1 TRP B 240 19586 11938 8010 4688 -1654 1677 N
ATOM 1572 CE2 TRP B 240 -1.969 15.750 53.864 1.00 93.12 C
ANISOU 1572 CE2 TRP B 240 17562 10798 7023 4608 -1990 1511 C
ATOM 1573 CE3 TRP B 240 -2.544 16.185 51.557 1.00 95.49 C
ANISOU 1573 CE3 TRP B 240 17052 10930 8300 3733 -1792 1247 C
ATOM 1574 CZ2 TRP B 240 -0.642 16.128 53.654 1.00 99.10 C
ANISOU 1574 CZ2 TRP B 240 17675 12043 7937 4892 -2486 1303 C
ATOM 1575 CZ3 TRP B 240 -1.227 16.560 51.350 1.00 96.81 C
ANISOU 1575 CZ3 TRP B 240 16740 11537 8508 4110 -2297 1126 C
ATOM 1576 CH2 TRP B 240 -0.292 16.529 52.392 1.00106.56 C
ANISOU 1576 CH2 TRP B 240 18064 13097 9327 4702 -2661 1154 C
ATOM 1577 N ILE B 241 -8.261 16.002 51.357 1.00 85.49 N
ANISOU 1577 N ILE B 241 16438 8241 7802 1494 148 1061 N
ATOM 1578 CA ILE B 241 -9.312 15.778 50.366 1.00 82.04 C
ANISOU 1578 CA ILE B 241 15805 7534 7831 927 478 890 C
ATOM 1579 C ILE B 241 -9.532 17.038 49.541 1.00 82.52 C
ANISOU 1579 C ILE B 241 15066 7987 8302 568 142 626 C
ATOM 1580 O ILE B 241 -9.638 16.979 48.315 1.00 93.13 O
ANISOU 1580 O ILE B 241 16068 9343 9974 344 87 501 O
ATOM 1581 CB ILE B 241 -10.640 15.356 51.026 1.00 81.86 C
ANISOU 1581 CB ILE B 241 16209 7067 7829 572 1090 877 C
ATOM 1582 CG1 ILE B 241 -10.501 13.973 51.665 1.00106.76 C
ANISOU 1582 CG1 ILE B 241 20227 9717 10619 897 1547 1157 C
ATOM 1583 CG2 ILE B 241 -11.766 15.339 50.004 1.00 80.69 C
ANISOU 1583 CG2 ILE B 241 15688 6755 8216 -46 1336 604 C
ATOM 1584 CD1 ILE B 241 -11.673 13.577 52.538 1.00 88.97 C
ANISOU 1584 CD1 ILE B 241 18491 6999 8315 617 2210 1175 C
ATOM 1585 N ALA B 242 -9.590 18.178 50.224 1.00 75.58 N
ANISOU 1585 N ALA B 242 13923 7416 7377 537 -67 547 N
ATOM 1586 CA ALA B 242 -9.739 19.465 49.559 1.00 75.58 C
ANISOU 1586 CA ALA B 242 13207 7769 7742 256 -361 329 C
ATOM 1587 C ALA B 242 -8.596 19.701 48.574 1.00 73.28 C
ANISOU 1587 C ALA B 242 12524 7764 7555 471 -771 311 C
ATOM 1588 O ALA B 242 -8.815 20.175 47.455 1.00 70.18 O
ANISOU 1588 O ALA B 242 11678 7474 7512 214 -866 180 O
ATOM 1589 CB ALA B 242 -9.799 20.582 50.584 1.00 76.30 C
ANISOU 1589 CB ALA B 242 13156 8116 7720 259 -494 255 C
ATOM 1590 N CYS B 243 -7.381 19.358 48.992 1.00 76.82 N
ANISOU 1590 N CYS B 243 13158 8339 7691 966 -1001 439 N
ATOM 1591 CA CYS B 243 -6.218 19.471 48.117 1.00 74.50 C
ANISOU 1591 CA CYS B 243 12517 8284 7508 1198 -1336 412 C
ATOM 1592 C CYS B 243 -6.342 18.551 46.904 1.00 89.17 C
ANISOU 1592 C CYS B 243 14456 9877 9549 1091 -1152 447 C
ATOM 1593 O CYS B 243 -6.040 18.952 45.778 1.00 72.90 O
ANISOU 1593 O CYS B 243 11976 7965 7757 979 -1305 341 O
ATOM 1594 CB CYS B 243 -4.933 19.157 48.887 1.00 77.68 C
ANISOU 1594 CB CYS B 243 13108 8867 7541 1785 -1608 523 C
ATOM 1595 SG CYS B 243 -4.480 20.398 50.119 1.00 78.24 S
ANISOU 1595 SG CYS B 243 12928 9387 7411 1938 -1960 377 S
ATOM 1596 N ALA B 244 -6.789 17.321 47.140 1.00 94.10 N
ANISOU 1596 N ALA B 244 15649 10087 10017 1121 -787 583 N
ATOM 1597 CA ALA B 244 -6.949 16.338 46.072 1.00 84.13 C
ANISOU 1597 CA ALA B 244 14524 8529 8911 1001 -559 580 C
ATOM 1598 C ALA B 244 -7.949 16.819 45.022 1.00 83.89 C
ANISOU 1598 C ALA B 244 14091 8520 9262 460 -497 353 C
ATOM 1599 O ALA B 244 -7.693 16.737 43.818 1.00101.70 O
ANISOU 1599 O ALA B 244 16112 10831 11697 386 -588 268 O
ATOM 1600 CB ALA B 244 -7.386 14.999 46.648 1.00 81.63 C
ANISOU 1600 CB ALA B 244 14917 7711 8387 1076 -93 740 C
ATOM 1601 N VAL B 245 -9.083 17.329 45.492 1.00 79.86 N
ANISOU 1601 N VAL B 245 13505 7978 8858 109 -346 252 N
ATOM 1602 CA VAL B 245 -10.117 17.863 44.614 1.00 78.92 C
ANISOU 1602 CA VAL B 245 12971 7922 9092 -362 -325 29 C
ATOM 1603 C VAL B 245 -9.611 19.091 43.859 1.00 76.51 C
ANISOU 1603 C VAL B 245 12086 8036 8950 -341 -734 -41 C
ATOM 1604 O VAL B 245 -9.909 19.269 42.676 1.00 80.54 O
ANISOU 1604 O VAL B 245 12306 8624 9671 -541 -809 -165 O
ATOM 1605 CB VAL B 245 -11.391 18.228 45.407 1.00 81.46 C
ANISOU 1605 CB VAL B 245 13297 8136 9516 -696 -75 -68 C
ATOM 1606 CG1 VAL B 245 -12.405 18.932 44.514 1.00 68.35 C
ANISOU 1606 CG1 VAL B 245 11118 6621 8233 -1113 -140 -307 C
ATOM 1607 CG2 VAL B 245 -12.001 16.979 46.027 1.00 72.06 C
ANISOU 1607 CG2 VAL B 245 12695 6463 8220 -783 434 -26 C
ATOM 1608 N ALA B 246 -8.839 19.932 44.542 1.00 75.93 N
ANISOU 1608 N ALA B 246 11862 8223 8767 -94 -978 25 N
ATOM 1609 CA ALA B 246 -8.258 21.110 43.907 1.00 91.60 C
ANISOU 1609 CA ALA B 246 13327 10554 10923 -65 -1294 -43 C
ATOM 1610 C ALA B 246 -7.333 20.711 42.757 1.00 72.01 C
ANISOU 1610 C ALA B 246 10774 8113 8472 107 -1412 -21 C
ATOM 1611 O ALA B 246 -7.387 21.291 41.669 1.00 70.00 O
ANISOU 1611 O ALA B 246 10189 7992 8418 -29 -1509 -98 O
ATOM 1612 CB ALA B 246 -7.506 21.946 44.928 1.00 76.51 C
ANISOU 1612 CB ALA B 246 11292 8887 8890 167 -1497 -29 C
ATOM 1613 N TRP B 247 -6.492 19.711 43.006 1.00 74.18 N
ANISOU 1613 N TRP B 247 11389 8259 8535 433 -1381 95 N
ATOM 1614 CA TRP B 247 -5.563 19.219 41.994 1.00 76.63 C
ANISOU 1614 CA TRP B 247 11671 8570 8875 624 -1445 114 C
ATOM 1615 C TRP B 247 -6.294 18.598 40.808 1.00 87.88 C
ANISOU 1615 C TRP B 247 13173 9800 10418 337 -1260 33 C
ATOM 1616 O TRP B 247 -5.986 18.900 39.651 1.00100.42 O
ANISOU 1616 O TRP B 247 14518 11508 12130 293 -1354 -34 O
ATOM 1617 CB TRP B 247 -4.598 18.201 42.604 1.00 72.26 C
ANISOU 1617 CB TRP B 247 11495 7888 8072 1068 -1425 264 C
ATOM 1618 CG TRP B 247 -3.412 18.824 43.270 1.00 70.30 C
ANISOU 1618 CG TRP B 247 11017 7950 7743 1441 -1731 276 C
ATOM 1619 CD1 TRP B 247 -3.201 18.964 44.611 1.00 73.48 C
ANISOU 1619 CD1 TRP B 247 11558 8456 7904 1680 -1845 332 C
ATOM 1620 CD2 TRP B 247 -2.269 19.394 42.622 1.00 81.93 C
ANISOU 1620 CD2 TRP B 247 12065 9682 9382 1610 -1955 190 C
ATOM 1621 NE1 TRP B 247 -1.995 19.585 44.837 1.00 73.29 N
ANISOU 1621 NE1 TRP B 247 11180 8773 7892 1985 -2169 252 N
ATOM 1622 CE2 TRP B 247 -1.404 19.860 43.632 1.00 74.44 C
ANISOU 1622 CE2 TRP B 247 10962 9004 8319 1933 -2217 159 C
ATOM 1623 CE3 TRP B 247 -1.893 19.556 41.285 1.00 82.80 C
ANISOU 1623 CE3 TRP B 247 11920 9820 9720 1516 -1937 117 C
ATOM 1624 CZ2 TRP B 247 -0.187 20.476 43.347 1.00 78.11 C
ANISOU 1624 CZ2 TRP B 247 10971 9756 8952 2133 -2447 24 C
ATOM 1625 CZ3 TRP B 247 -0.686 20.168 41.004 1.00 71.31 C
ANISOU 1625 CZ3 TRP B 247 10066 8613 8415 1723 -2119 25 C
ATOM 1626 CH2 TRP B 247 0.153 20.620 42.030 1.00 72.49 C
ANISOU 1626 CH2 TRP B 247 10014 9020 8507 2013 -2366 -37 C
ATOM 1627 N GLY B 248 -7.254 17.726 41.101 1.00 90.89 N
ANISOU 1627 N GLY B 248 13904 9876 10754 139 -976 16 N
ATOM 1628 CA GLY B 248 -8.046 17.094 40.062 1.00107.65 C
ANISOU 1628 CA GLY B 248 16083 11823 12997 -174 -799 -135 C
ATOM 1629 C GLY B 248 -8.737 18.119 39.184 1.00 83.26 C
ANISOU 1629 C GLY B 248 12530 8996 10109 -467 -978 -295 C
ATOM 1630 O GLY B 248 -8.674 18.048 37.953 1.00 78.62 O
ANISOU 1630 O GLY B 248 11825 8477 9572 -538 -1044 -391 O
ATOM 1631 N LEU B 249 -9.380 19.090 39.825 1.00 80.38 N
ANISOU 1631 N LEU B 249 11924 8779 9838 -606 -1051 -315 N
ATOM 1632 CA LEU B 249 -10.101 20.137 39.113 1.00 90.85 C
ANISOU 1632 CA LEU B 249 12818 10345 11357 -832 -1215 -436 C
ATOM 1633 C LEU B 249 -9.151 20.987 38.274 1.00 67.59 C
ANISOU 1633 C LEU B 249 9595 7657 8427 -636 -1458 -372 C
ATOM 1634 O LEU B 249 -9.500 21.416 37.174 1.00 71.36 O
ANISOU 1634 O LEU B 249 9860 8272 8981 -743 -1562 -447 O
ATOM 1635 CB LEU B 249 -10.870 21.021 40.095 1.00117.47 C
ANISOU 1635 CB LEU B 249 16005 13788 14838 -972 -1206 -451 C
ATOM 1636 CG LEU B 249 -12.018 21.838 39.502 1.00119.98 C
ANISOU 1636 CG LEU B 249 15935 14264 15386 -1245 -1290 -599 C
ATOM 1637 CD1 LEU B 249 -13.072 20.909 38.919 1.00 98.31 C
ANISOU 1637 CD1 LEU B 249 13264 11369 12721 -1535 -1145 -810 C
ATOM 1638 CD2 LEU B 249 -12.625 22.759 40.550 1.00 92.33 C
ANISOU 1638 CD2 LEU B 249 12257 10817 12009 -1340 -1252 -600 C
ATOM 1639 N ALA B 250 -7.952 21.226 38.798 1.00 62.82 N
ANISOU 1639 N ALA B 250 9001 7121 7749 -339 -1535 -247 N
ATOM 1640 CA ALA B 250 -6.938 21.986 38.073 1.00 66.12 C
ANISOU 1640 CA ALA B 250 9160 7737 8224 -161 -1688 -211 C
ATOM 1641 C ALA B 250 -6.519 21.256 36.802 1.00 65.50 C
ANISOU 1641 C ALA B 250 9210 7588 8087 -110 -1645 -232 C
ATOM 1642 O ALA B 250 -6.425 21.854 35.725 1.00 62.76 O
ANISOU 1642 O ALA B 250 8679 7372 7796 -137 -1708 -252 O
ATOM 1643 CB ALA B 250 -5.734 22.239 38.959 1.00 70.21 C
ANISOU 1643 CB ALA B 250 9634 8342 8701 134 -1772 -144 C
ATOM 1644 N LEU B 251 -6.268 19.958 36.939 1.00 74.21 N
ANISOU 1644 N LEU B 251 10671 8464 9063 -21 -1505 -219 N
ATOM 1645 CA LEU B 251 -5.923 19.120 35.799 1.00 69.50 C
ANISOU 1645 CA LEU B 251 10249 7754 8404 9 -1415 -266 C
ATOM 1646 C LEU B 251 -7.029 19.151 34.746 1.00 72.24 C
ANISOU 1646 C LEU B 251 10539 8138 8769 -303 -1421 -423 C
ATOM 1647 O LEU B 251 -6.760 19.333 33.554 1.00 77.51 O
ANISOU 1647 O LEU B 251 11143 8906 9402 -287 -1470 -463 O
ATOM 1648 CB LEU B 251 -5.665 17.682 36.249 1.00 75.87 C
ANISOU 1648 CB LEU B 251 11487 8249 9091 132 -1208 -231 C
ATOM 1649 CG LEU B 251 -5.318 16.692 35.137 1.00 72.78 C
ANISOU 1649 CG LEU B 251 11322 7687 8645 153 -1059 -304 C
ATOM 1650 CD1 LEU B 251 -4.065 17.140 34.406 1.00 87.51 C
ANISOU 1650 CD1 LEU B 251 13004 9709 10537 407 -1153 -254 C
ATOM 1651 CD2 LEU B 251 -5.142 15.291 35.698 1.00 86.04 C
ANISOU 1651 CD2 LEU B 251 13459 9002 10231 282 -799 -253 C
ATOM 1652 N LEU B 252 -8.271 18.989 35.197 1.00 70.98 N
ANISOU 1652 N LEU B 252 10397 7912 8658 -575 -1369 -528 N
ATOM 1653 CA LEU B 252 -9.422 19.004 34.295 1.00 71.81 C
ANISOU 1653 CA LEU B 252 10388 8098 8800 -869 -1419 -732 C
ATOM 1654 C LEU B 252 -9.593 20.354 33.602 1.00 70.03 C
ANISOU 1654 C LEU B 252 9800 8191 8619 -849 -1661 -702 C
ATOM 1655 O LEU B 252 -10.071 20.423 32.470 1.00 72.98 O
ANISOU 1655 O LEU B 252 10102 8697 8929 -938 -1769 -825 O
ATOM 1656 CB LEU B 252 -10.700 18.652 35.055 1.00 70.23 C
ANISOU 1656 CB LEU B 252 10206 7766 8713 -1165 -1292 -877 C
ATOM 1657 CG LEU B 252 -10.734 17.254 35.667 1.00 75.90 C
ANISOU 1657 CG LEU B 252 11346 8102 9392 -1225 -966 -920 C
ATOM 1658 CD1 LEU B 252 -12.032 17.025 36.425 1.00104.37 C
ANISOU 1658 CD1 LEU B 252 14948 11558 13151 -1550 -776 -1078 C
ATOM 1659 CD2 LEU B 252 -10.537 16.201 34.592 1.00 71.84 C
ANISOU 1659 CD2 LEU B 252 11055 7445 8794 -1276 -857 -1075 C
ATOM 1660 N LEU B 253 -9.210 21.424 34.290 1.00 69.46 N
ANISOU 1660 N LEU B 253 9518 8234 8640 -718 -1736 -546 N
ATOM 1661 CA LEU B 253 -9.285 22.762 33.718 1.00 81.03 C
ANISOU 1661 CA LEU B 253 10678 9940 10171 -667 -1895 -481 C
ATOM 1662 C LEU B 253 -8.141 23.002 32.740 1.00 72.57 C
ANISOU 1662 C LEU B 253 9640 8924 9008 -446 -1895 -387 C
ATOM 1663 O LEU B 253 -8.231 23.866 31.868 1.00 89.96 O
ANISOU 1663 O LEU B 253 11706 11281 11195 -397 -1974 -339 O
ATOM 1664 CB LEU B 253 -9.263 23.824 34.822 1.00 68.56 C
ANISOU 1664 CB LEU B 253 8871 8424 8755 -636 -1914 -385 C
ATOM 1665 CG LEU B 253 -10.546 24.017 35.633 1.00 59.23 C
ANISOU 1665 CG LEU B 253 7570 7233 7701 -861 -1907 -472 C
ATOM 1666 CD1 LEU B 253 -10.301 24.950 36.809 1.00 58.91 C
ANISOU 1666 CD1 LEU B 253 7374 7224 7784 -808 -1886 -387 C
ATOM 1667 CD2 LEU B 253 -11.661 24.547 34.748 1.00 53.01 C
ANISOU 1667 CD2 LEU B 253 6555 6608 6977 -986 -2042 -561 C
ATOM 1668 N THR B 254 -7.068 22.231 32.887 1.00 68.95 N
ANISOU 1668 N THR B 254 9381 8324 8491 -293 -1780 -354 N
ATOM 1669 CA THR B 254 -5.882 22.421 32.057 1.00 70.81 C
ANISOU 1669 CA THR B 254 9632 8584 8690 -85 -1723 -285 C
ATOM 1670 C THR B 254 -5.897 21.574 30.779 1.00 76.10 C
ANISOU 1670 C THR B 254 10549 9196 9168 -108 -1664 -375 C
ATOM 1671 O THR B 254 -5.385 22.005 29.749 1.00 91.93 O
ANISOU 1671 O THR B 254 12555 11272 11101 -3 -1630 -333 O
ATOM 1672 CB THR B 254 -4.595 22.113 32.854 1.00 74.64 C
ANISOU 1672 CB THR B 254 10136 8979 9246 139 -1644 -225 C
ATOM 1673 OG1 THR B 254 -4.557 22.933 34.028 1.00 61.11 O
ANISOU 1673 OG1 THR B 254 8191 7353 7673 159 -1720 -183 O
ATOM 1674 CG2 THR B 254 -3.353 22.393 32.014 1.00 65.62 C
ANISOU 1674 CG2 THR B 254 8937 7859 8138 335 -1546 -190 C
ATOM 1675 N ILE B 255 -6.495 20.386 30.829 1.00 78.39 N
ANISOU 1675 N ILE B 255 11070 9342 9372 -257 -1617 -514 N
ATOM 1676 CA ILE B 255 -6.453 19.491 29.665 1.00 89.99 C
ANISOU 1676 CA ILE B 255 12794 10739 10659 -295 -1538 -650 C
ATOM 1677 C ILE B 255 -7.026 20.032 28.331 1.00 83.03 C
ANISOU 1677 C ILE B 255 11865 10077 9604 -358 -1677 -726 C
ATOM 1678 O ILE B 255 -6.473 19.710 27.271 1.00101.88 O
ANISOU 1678 O ILE B 255 14443 12450 11817 -271 -1595 -761 O
ATOM 1679 CB ILE B 255 -7.156 18.135 29.953 1.00 94.15 C
ANISOU 1679 CB ILE B 255 13568 11046 11158 -505 -1423 -842 C
ATOM 1680 CG1 ILE B 255 -8.359 18.298 30.875 1.00121.63 C
ANISOU 1680 CG1 ILE B 255 16905 14541 14767 -735 -1489 -911 C
ATOM 1681 CG2 ILE B 255 -6.172 17.145 30.559 1.00 81.52 C
ANISOU 1681 CG2 ILE B 255 12231 9159 9585 -324 -1196 -763 C
ATOM 1682 CD1 ILE B 255 -9.194 17.038 31.021 1.00108.03 C
ANISOU 1682 CD1 ILE B 255 15405 12587 13055 -1004 -1319 -1151 C
ATOM 1683 N PRO B 256 -8.114 20.839 28.356 1.00 73.41 N
ANISOU 1683 N PRO B 256 10415 9065 8414 -475 -1883 -751 N
ATOM 1684 CA PRO B 256 -8.628 21.264 27.045 1.00 74.56 C
ANISOU 1684 CA PRO B 256 10560 9437 8332 -461 -2046 -815 C
ATOM 1685 C PRO B 256 -7.630 22.072 26.213 1.00 77.05 C
ANISOU 1685 C PRO B 256 10937 9808 8529 -198 -1966 -609 C
ATOM 1686 O PRO B 256 -7.514 21.832 25.012 1.00 82.90 O
ANISOU 1686 O PRO B 256 11893 10612 8993 -138 -1962 -671 O
ATOM 1687 CB PRO B 256 -9.842 22.124 27.408 1.00 84.71 C
ANISOU 1687 CB PRO B 256 11535 10924 9725 -558 -2274 -828 C
ATOM 1688 CG PRO B 256 -10.268 21.628 28.733 1.00 77.13 C
ANISOU 1688 CG PRO B 256 10494 9804 9007 -751 -2199 -905 C
ATOM 1689 CD PRO B 256 -8.990 21.313 29.444 1.00 72.01 C
ANISOU 1689 CD PRO B 256 9994 8930 8437 -611 -1977 -747 C
ATOM 1690 N SER B 257 -6.924 23.009 26.837 1.00 91.48 N
ANISOU 1690 N SER B 257 12592 11603 10563 -58 -1874 -393 N
ATOM 1691 CA SER B 257 -5.907 23.782 26.133 1.00101.57 C
ANISOU 1691 CA SER B 257 13915 12874 11802 161 -1706 -219 C
ATOM 1692 C SER B 257 -4.735 22.886 25.753 1.00 89.97 C
ANISOU 1692 C SER B 257 12676 11225 10284 246 -1470 -263 C
ATOM 1693 O SER B 257 -4.108 23.066 24.708 1.00105.13 O
ANISOU 1693 O SER B 257 14767 13130 12046 378 -1309 -211 O
ATOM 1694 CB SER B 257 -5.417 24.946 26.992 1.00 71.68 C
ANISOU 1694 CB SER B 257 9848 9073 8316 240 -1627 -50 C
ATOM 1695 OG SER B 257 -4.693 24.474 28.114 1.00 63.38 O
ANISOU 1695 OG SER B 257 8705 7890 7486 231 -1548 -86 O
ATOM 1696 N PHE B 258 -4.451 21.922 26.624 1.00 82.27 N
ANISOU 1696 N PHE B 258 11722 10095 9442 190 -1425 -349 N
ATOM 1697 CA PHE B 258 -3.375 20.958 26.426 1.00 81.87 C
ANISOU 1697 CA PHE B 258 11870 9849 9388 298 -1205 -395 C
ATOM 1698 C PHE B 258 -3.562 20.170 25.135 1.00 81.54 C
ANISOU 1698 C PHE B 258 12158 9781 9042 251 -1140 -538 C
ATOM 1699 O PHE B 258 -2.601 19.898 24.414 1.00 80.10 O
ANISOU 1699 O PHE B 258 12143 9493 8798 386 -912 -533 O
ATOM 1700 CB PHE B 258 -3.305 20.014 27.633 1.00 79.26 C
ANISOU 1700 CB PHE B 258 11556 9356 9203 272 -1199 -443 C
ATOM 1701 CG PHE B 258 -2.612 18.708 27.358 1.00 80.27 C
ANISOU 1701 CG PHE B 258 11969 9255 9276 354 -997 -527 C
ATOM 1702 CD1 PHE B 258 -1.238 18.597 27.479 1.00 76.83 C
ANISOU 1702 CD1 PHE B 258 11494 8716 8983 607 -822 -456 C
ATOM 1703 CD2 PHE B 258 -3.341 17.581 27.007 1.00 83.48 C
ANISOU 1703 CD2 PHE B 258 12656 9539 9522 176 -963 -706 C
ATOM 1704 CE1 PHE B 258 -0.601 17.395 27.236 1.00 72.59 C
ANISOU 1704 CE1 PHE B 258 11214 7950 8417 717 -620 -524 C
ATOM 1705 CE2 PHE B 258 -2.711 16.377 26.761 1.00 76.59 C
ANISOU 1705 CE2 PHE B 258 12068 8413 8619 255 -731 -785 C
ATOM 1706 CZ PHE B 258 -1.339 16.284 26.876 1.00 74.00 C
ANISOU 1706 CZ PHE B 258 11719 7976 8422 544 -560 -674 C
ATOM 1707 N LEU B 259 -4.808 19.808 24.848 1.00 77.53 N
ANISOU 1707 N LEU B 259 11724 9378 8356 49 -1333 -701 N
ATOM 1708 CA LEU B 259 -5.117 19.030 23.654 1.00 77.00 C
ANISOU 1708 CA LEU B 259 11956 9327 7975 -31 -1317 -909 C
ATOM 1709 C LEU B 259 -5.015 19.844 22.366 1.00 91.01 C
ANISOU 1709 C LEU B 259 13837 11288 9454 109 -1339 -833 C
ATOM 1710 O LEU B 259 -4.902 19.280 21.278 1.00110.40 O
ANISOU 1710 O LEU B 259 16592 13745 11611 114 -1261 -974 O
ATOM 1711 CB LEU B 259 -6.516 18.425 23.770 1.00 77.59 C
ANISOU 1711 CB LEU B 259 12014 9485 7982 -312 -1531 -1173 C
ATOM 1712 CG LEU B 259 -6.664 17.299 24.793 1.00 76.35 C
ANISOU 1712 CG LEU B 259 11909 9060 8039 -478 -1401 -1297 C
ATOM 1713 CD1 LEU B 259 -8.110 16.842 24.885 1.00 71.41 C
ANISOU 1713 CD1 LEU B 259 11214 8515 7405 -797 -1566 -1592 C
ATOM 1714 CD2 LEU B 259 -5.753 16.142 24.426 1.00 73.59 C
ANISOU 1714 CD2 LEU B 259 11893 8427 7640 -417 -1098 -1376 C
ATOM 1715 N TYR B 260 -5.060 21.166 22.486 1.00101.59 N
ANISOU 1715 N TYR B 260 14971 12769 10861 234 -1416 -608 N
ATOM 1716 CA TYR B 260 -5.008 22.029 21.310 1.00 79.05 C
ANISOU 1716 CA TYR B 260 12265 10062 7708 410 -1401 -482 C
ATOM 1717 C TYR B 260 -3.596 22.535 21.029 1.00 84.74 C
ANISOU 1717 C TYR B 260 13062 10602 8534 610 -1017 -286 C
ATOM 1718 O TYR B 260 -3.401 23.432 20.209 1.00118.45 O
ANISOU 1718 O TYR B 260 17458 14925 12621 779 -902 -118 O
ATOM 1719 CB TYR B 260 -5.973 23.207 21.467 1.00 72.11 C
ANISOU 1719 CB TYR B 260 11159 9414 6824 452 -1668 -347 C
ATOM 1720 CG TYR B 260 -7.360 22.917 20.939 1.00 72.90 C
ANISOU 1720 CG TYR B 260 11280 9790 6630 354 -2045 -556 C
ATOM 1721 CD1 TYR B 260 -7.741 23.333 19.670 1.00 75.27 C
ANISOU 1721 CD1 TYR B 260 11801 10316 6480 533 -2183 -532 C
ATOM 1722 CD2 TYR B 260 -8.284 22.218 21.703 1.00 76.27 C
ANISOU 1722 CD2 TYR B 260 11503 10253 7222 92 -2253 -800 C
ATOM 1723 CE1 TYR B 260 -9.007 23.067 19.178 1.00 84.43 C
ANISOU 1723 CE1 TYR B 260 12925 11785 7368 466 -2584 -775 C
ATOM 1724 CE2 TYR B 260 -9.552 21.947 21.220 1.00 79.59 C
ANISOU 1724 CE2 TYR B 260 11869 10942 7429 -22 -2594 -1060 C
ATOM 1725 CZ TYR B 260 -9.908 22.374 19.958 1.00 88.60 C
ANISOU 1725 CZ TYR B 260 13178 12357 8128 171 -2791 -1062 C
ATOM 1726 OH TYR B 260 -11.169 22.105 19.474 1.00117.67 O
ANISOU 1726 OH TYR B 260 16753 16361 11594 79 -3186 -1369 O
ATOM 1727 N ARG B 261 -2.614 21.952 21.709 1.00 74.37 N
ANISOU 1727 N ARG B 261 11671 9067 7519 606 -800 -316 N
ATOM 1728 CA ARG B 261 -1.215 22.263 21.441 1.00 82.49 C
ANISOU 1728 CA ARG B 261 12718 9920 8704 775 -415 -212 C
ATOM 1729 C ARG B 261 -0.679 21.361 20.334 1.00101.03 C
ANISOU 1729 C ARG B 261 15449 12149 10788 819 -176 -335 C
ATOM 1730 O ARG B 261 -0.841 20.142 20.384 1.00 95.41 O
ANISOU 1730 O ARG B 261 14881 11360 10010 719 -218 -528 O
ATOM 1731 CB ARG B 261 -0.366 22.110 22.703 1.00 83.69 C
ANISOU 1731 CB ARG B 261 12553 9934 9310 799 -332 -209 C
ATOM 1732 CG ARG B 261 -0.787 23.011 23.847 1.00 86.35 C
ANISOU 1732 CG ARG B 261 12524 10378 9906 751 -532 -113 C
ATOM 1733 CD ARG B 261 0.367 23.253 24.802 1.00 86.83 C
ANISOU 1733 CD ARG B 261 12268 10344 10381 847 -386 -103 C
ATOM 1734 NE ARG B 261 1.492 23.902 24.136 1.00 84.24 N
ANISOU 1734 NE ARG B 261 11900 9920 10187 974 -22 -59 N
ATOM 1735 CZ ARG B 261 1.594 25.214 23.946 1.00 81.19 C
ANISOU 1735 CZ ARG B 261 11380 9556 9915 988 124 57 C
ATOM 1736 NH1 ARG B 261 0.633 26.024 24.369 1.00 79.07 N
ANISOU 1736 NH1 ARG B 261 10996 9415 9632 909 -95 152 N
ATOM 1737 NH2 ARG B 261 2.653 25.717 23.329 1.00 81.32 N
ANISOU 1737 NH2 ARG B 261 11381 9434 10082 1080 533 71 N
ATOM 1738 N VAL B 262 -0.061 21.971 19.326 1.00111.55 N
ANISOU 1738 N VAL B 262 16977 13439 11968 964 118 -227 N
ATOM 1739 CA VAL B 262 0.475 21.249 18.173 1.00 96.24 C
ANISOU 1739 CA VAL B 262 15441 11384 9742 1018 398 -336 C
ATOM 1740 C VAL B 262 1.844 21.829 17.793 1.00 95.54 C
ANISOU 1740 C VAL B 262 15352 11088 9860 1180 905 -217 C
ATOM 1741 O VAL B 262 2.143 22.994 18.094 1.00 97.26 O
ANISOU 1741 O VAL B 262 15341 11299 10315 1245 1023 -40 O
ATOM 1742 CB VAL B 262 -0.498 21.317 16.953 1.00109.47 C
ANISOU 1742 CB VAL B 262 17511 13272 10811 1023 218 -374 C
ATOM 1743 CG1 VAL B 262 0.005 20.472 15.786 1.00143.83 C
ANISOU 1743 CG1 VAL B 262 22316 17511 14821 1056 500 -534 C
ATOM 1744 CG2 VAL B 262 -1.904 20.867 17.347 1.00108.88 C
ANISOU 1744 CG2 VAL B 262 17340 13430 10600 842 -287 -540 C
ATOM 1745 N VAL B 263 2.686 21.004 17.174 1.00101.02 N
ANISOU 1745 N VAL B 263 16278 11590 10514 1226 1242 -344 N
ATOM 1746 CA VAL B 263 3.934 21.472 16.583 1.00122.89 C
ANISOU 1746 CA VAL B 263 19103 14153 13438 1363 1787 -277 C
ATOM 1747 C VAL B 263 3.740 21.756 15.091 1.00115.30 C
ANISOU 1747 C VAL B 263 18685 13205 11917 1439 2007 -214 C
ATOM 1748 O VAL B 263 2.896 21.141 14.439 1.00 99.32 O
ANISOU 1748 O VAL B 263 17016 11328 9392 1391 1764 -323 O
ATOM 1749 CB VAL B 263 5.077 20.444 16.769 1.00102.20 C
ANISOU 1749 CB VAL B 263 16400 11292 11140 1408 2086 -451 C
ATOM 1750 CG1 VAL B 263 5.316 20.175 18.243 1.00 94.55 C
ANISOU 1750 CG1 VAL B 263 14933 10326 10664 1404 1854 -490 C
ATOM 1751 CG2 VAL B 263 4.755 19.148 16.039 1.00106.85 C
ANISOU 1751 CG2 VAL B 263 17423 11831 11343 1355 2078 -643 C
ATOM 1752 N ARG B 264 4.509 22.699 14.559 1.00 97.05 N
ANISOU 1752 N ARG B 264 16448 10744 9683 1559 2478 -56 N
ATOM 1753 CA ARG B 264 4.497 22.970 13.126 1.00 98.65 C
ANISOU 1753 CA ARG B 264 17236 10911 9337 1678 2786 32 C
ATOM 1754 C ARG B 264 5.909 23.210 12.612 1.00 97.87 C
ANISOU 1754 C ARG B 264 17208 10476 9500 1760 3522 43 C
ATOM 1755 O ARG B 264 6.653 24.009 13.179 1.00 95.72 O
ANISOU 1755 O ARG B 264 16550 10055 9764 1764 3810 118 O
ATOM 1756 CB ARG B 264 3.613 24.174 12.800 1.00 98.55 C
ANISOU 1756 CB ARG B 264 17387 11077 8980 1786 2609 301 C
ATOM 1757 CG ARG B 264 2.127 23.877 12.820 1.00 98.96 C
ANISOU 1757 CG ARG B 264 17521 11490 8590 1747 1930 253 C
ATOM 1758 CD ARG B 264 1.369 24.854 11.944 1.00103.14 C
ANISOU 1758 CD ARG B 264 18436 12192 8560 1960 1842 501 C
ATOM 1759 NE ARG B 264 -0.058 24.553 11.903 1.00108.34 N
ANISOU 1759 NE ARG B 264 19122 13237 8804 1939 1167 404 N
ATOM 1760 CZ ARG B 264 -0.938 25.224 11.168 1.00111.01 C
ANISOU 1760 CZ ARG B 264 19766 13824 8589 2159 921 570 C
ATOM 1761 NH1 ARG B 264 -0.534 26.234 10.410 1.00118.33 N
ANISOU 1761 NH1 ARG B 264 21069 14616 9277 2430 1333 887 N
ATOM 1762 NH2 ARG B 264 -2.220 24.886 11.188 1.00107.52 N
ANISOU 1762 NH2 ARG B 264 19254 13760 7840 2124 280 412 N
ATOM 1763 N GLU B 265 6.277 22.521 11.537 1.00111.12 N
ANISOU 1763 N GLU B 265 19367 12035 10820 1807 3847 -67 N
ATOM 1764 CA GLU B 265 7.611 22.670 10.971 1.00109.57 C
ANISOU 1764 CA GLU B 265 19264 11499 10870 1874 4603 -86 C
ATOM 1765 C GLU B 265 7.670 23.835 9.986 1.00108.88 C
ANISOU 1765 C GLU B 265 19625 11307 10438 2014 5051 178 C
ATOM 1766 O GLU B 265 6.853 23.935 9.071 1.00105.71 O
ANISOU 1766 O GLU B 265 19797 11065 9303 2121 4898 293 O
ATOM 1767 CB GLU B 265 8.053 21.377 10.287 1.00114.23 C
ANISOU 1767 CB GLU B 265 20178 11958 11265 1865 4826 -333 C
ATOM 1768 CG GLU B 265 9.513 21.387 9.870 1.00123.94 C
ANISOU 1768 CG GLU B 265 21389 12820 12885 1920 5616 -408 C
ATOM 1769 CD GLU B 265 10.031 20.013 9.501 1.00160.32 C
ANISOU 1769 CD GLU B 265 26161 17275 17479 1907 5810 -683 C
ATOM 1770 OE1 GLU B 265 9.213 19.082 9.351 1.00162.34 O
ANISOU 1770 OE1 GLU B 265 26679 17693 17311 1846 5391 -813 O
ATOM 1771 OE2 GLU B 265 11.263 19.866 9.364 1.00169.52 O
ANISOU 1771 OE2 GLU B 265 27175 18143 19091 1953 6408 -793 O
ATOM 1772 N GLU B 266 8.636 24.721 10.199 1.00115.98 N
ANISOU 1772 N GLU B 266 20256 11938 11874 2022 5610 260 N
ATOM 1773 CA GLU B 266 8.867 25.857 9.315 1.00129.80 C
ANISOU 1773 CA GLU B 266 22436 13482 13400 2151 6197 518 C
ATOM 1774 C GLU B 266 10.019 25.542 8.372 1.00120.32 C
ANISOU 1774 C GLU B 266 21563 11928 12224 2184 7010 410 C
ATOM 1775 O GLU B 266 11.062 25.054 8.806 1.00118.94 O
ANISOU 1775 O GLU B 266 20943 11568 12681 2085 7309 162 O
ATOM 1776 CB GLU B 266 9.166 27.121 10.123 1.00144.18 C
ANISOU 1776 CB GLU B 266 23769 15182 15830 2102 6385 651 C
ATOM 1777 N TYR B 267 9.829 25.831 7.088 1.00119.81 N
ANISOU 1777 N TYR B 267 17922 18463 9140 1466 -445 -1293 N
ATOM 1778 CA TYR B 267 10.770 25.408 6.054 1.00124.57 C
ANISOU 1778 CA TYR B 267 18264 19398 9667 1611 -372 -1507 C
ATOM 1779 C TYR B 267 11.756 26.496 5.632 1.00115.31 C
ANISOU 1779 C TYR B 267 17363 18269 8180 1688 -39 -1024 C
ATOM 1780 O TYR B 267 12.741 26.209 4.956 1.00120.75 O
ANISOU 1780 O TYR B 267 17879 19110 8889 1727 60 -1127 O
ATOM 1781 CB TYR B 267 10.002 24.912 4.824 1.00110.19 C
ANISOU 1781 CB TYR B 267 16087 18317 7462 2028 -452 -2040 C
ATOM 1782 N PHE B 268 11.495 27.739 6.022 1.00105.43 N
ANISOU 1782 N PHE B 268 16534 16845 6680 1698 199 -518 N
ATOM 1783 CA PHE B 268 12.350 28.849 5.607 1.00108.27 C
ANISOU 1783 CA PHE B 268 17178 17183 6776 1765 642 -72 C
ATOM 1784 C PHE B 268 12.398 29.961 6.652 1.00116.16 C
ANISOU 1784 C PHE B 268 18626 17632 7877 1434 916 398 C
ATOM 1785 O PHE B 268 11.541 30.844 6.658 1.00130.24 O
ANISOU 1785 O PHE B 268 20708 19419 9358 1667 1150 698 O
ATOM 1786 CB PHE B 268 11.873 29.413 4.266 1.00115.73 C
ANISOU 1786 CB PHE B 268 18155 18774 7044 2412 889 43 C
ATOM 1787 N PRO B 269 13.401 29.922 7.546 1.00116.58 N
ANISOU 1787 N PRO B 269 18699 17246 8349 890 910 445 N
ATOM 1788 CA PRO B 269 14.450 28.900 7.646 1.00115.70 C
ANISOU 1788 CA PRO B 269 18214 17118 8628 644 655 171 C
ATOM 1789 C PRO B 269 13.943 27.626 8.316 1.00135.67 C
ANISOU 1789 C PRO B 269 20466 19544 11538 524 174 -155 C
ATOM 1790 O PRO B 269 12.942 27.683 9.029 1.00135.66 O
ANISOU 1790 O PRO B 269 20619 19363 11562 462 44 -127 O
ATOM 1791 CB PRO B 269 15.513 29.586 8.505 1.00119.41 C
ANISOU 1791 CB PRO B 269 18835 17218 9317 125 865 417 C
ATOM 1792 CG PRO B 269 14.720 30.466 9.405 1.00123.84 C
ANISOU 1792 CG PRO B 269 19793 17462 9800 -73 1004 658 C
ATOM 1793 CD PRO B 269 13.559 30.964 8.576 1.00111.84 C
ANISOU 1793 CD PRO B 269 18482 16162 7850 471 1197 780 C
ATOM 1794 N PRO B 270 14.616 26.487 8.085 1.00142.03 N
ANISOU 1794 N PRO B 270 20875 20419 12671 507 -21 -449 N
ATOM 1795 CA PRO B 270 14.135 25.243 8.691 1.00141.24 C
ANISOU 1795 CA PRO B 270 20526 20144 12997 428 -356 -737 C
ATOM 1796 C PRO B 270 14.250 25.250 10.212 1.00134.76 C
ANISOU 1796 C PRO B 270 19831 18884 12489 16 -504 -479 C
ATOM 1797 O PRO B 270 15.332 25.477 10.755 1.00130.14 O
ANISOU 1797 O PRO B 270 19219 18193 12035 -266 -478 -252 O
ATOM 1798 CB PRO B 270 15.043 24.172 8.076 1.00133.73 C
ANISOU 1798 CB PRO B 270 19152 19305 12353 506 -390 -1026 C
ATOM 1799 CG PRO B 270 16.259 24.903 7.645 1.00132.66 C
ANISOU 1799 CG PRO B 270 19060 19284 12060 452 -149 -785 C
ATOM 1800 CD PRO B 270 15.794 26.265 7.229 1.00132.80 C
ANISOU 1800 CD PRO B 270 19472 19456 11529 588 123 -532 C
ATOM 1801 N LYS B 271 13.125 25.014 10.880 1.00139.38 N
ANISOU 1801 N LYS B 271 20527 19274 13156 -13 -652 -536 N
ATOM 1802 CA LYS B 271 13.084 24.905 12.335 1.00131.36 C
ANISOU 1802 CA LYS B 271 19631 17877 12402 -361 -798 -313 C
ATOM 1803 C LYS B 271 11.744 24.317 12.758 1.00129.68 C
ANISOU 1803 C LYS B 271 19450 17474 12351 -289 -929 -506 C
ATOM 1804 O LYS B 271 10.868 24.106 11.923 1.00127.22 O
ANISOU 1804 O LYS B 271 19047 17370 11919 -4 -911 -834 O
ATOM 1805 CB LYS B 271 13.303 26.268 12.995 1.00126.51 C
ANISOU 1805 CB LYS B 271 19399 17164 11505 -669 -633 53 C
ATOM 1806 N VAL B 272 11.583 24.054 14.050 1.00134.98 N
ANISOU 1806 N VAL B 272 20222 17797 13268 -548 -1048 -323 N
ATOM 1807 CA VAL B 272 10.328 23.512 14.558 1.00118.20 C
ANISOU 1807 CA VAL B 272 18148 15419 11344 -518 -1116 -487 C
ATOM 1808 C VAL B 272 9.676 24.451 15.568 1.00113.83 C
ANISOU 1808 C VAL B 272 18013 14650 10585 -762 -1087 -201 C
ATOM 1809 O VAL B 272 10.308 24.887 16.526 1.00109.13 O
ANISOU 1809 O VAL B 272 17583 13937 9946 -1076 -1106 124 O
ATOM 1810 CB VAL B 272 10.534 22.135 15.213 1.00114.37 C
ANISOU 1810 CB VAL B 272 17410 14627 11420 -545 -1204 -542 C
ATOM 1811 CG1 VAL B 272 9.200 21.554 15.645 1.00114.35 C
ANISOU 1811 CG1 VAL B 272 17451 14323 11675 -518 -1188 -770 C
ATOM 1812 CG2 VAL B 272 11.238 21.194 14.253 1.00116.52 C
ANISOU 1812 CG2 VAL B 272 17268 15042 11960 -326 -1156 -831 C
ATOM 1813 N LEU B 273 8.405 24.760 15.346 1.00114.90 N
ANISOU 1813 N LEU B 273 18289 14784 10583 -622 -1029 -354 N
ATOM 1814 CA LEU B 273 7.666 25.624 16.254 1.00103.57 C
ANISOU 1814 CA LEU B 273 17253 13107 8992 -826 -947 -112 C
ATOM 1815 C LEU B 273 6.724 24.809 17.125 1.00109.44 C
ANISOU 1815 C LEU B 273 17993 13500 10090 -901 -1038 -233 C
ATOM 1816 O LEU B 273 6.121 23.843 16.665 1.00110.95 O
ANISOU 1816 O LEU B 273 17898 13701 10556 -697 -1085 -617 O
ATOM 1817 CB LEU B 273 6.873 26.677 15.477 1.00 98.31 C
ANISOU 1817 CB LEU B 273 16772 12664 7917 -581 -754 -101 C
ATOM 1818 CG LEU B 273 7.675 27.746 14.737 1.00 94.30 C
ANISOU 1818 CG LEU B 273 16395 12402 7031 -506 -519 127 C
ATOM 1819 CD1 LEU B 273 6.751 28.655 13.941 1.00106.93 C
ANISOU 1819 CD1 LEU B 273 18152 14236 8239 -129 -286 202 C
ATOM 1820 CD2 LEU B 273 8.494 28.549 15.727 1.00 93.62 C
ANISOU 1820 CD2 LEU B 273 16609 12043 6919 -971 -370 458 C
ATOM 1821 N CYS B 274 6.613 25.201 18.388 1.00137.16 N
ANISOU 1821 N CYS B 274 21814 16702 13597 -1218 -1018 60 N
ATOM 1822 CA CYS B 274 5.639 24.615 19.300 1.00116.51 C
ANISOU 1822 CA CYS B 274 19282 13715 11271 -1299 -1035 10 C
ATOM 1823 C CYS B 274 4.595 25.663 19.650 1.00105.00 C
ANISOU 1823 C CYS B 274 18193 12132 9570 -1384 -879 99 C
ATOM 1824 O CYS B 274 4.944 26.766 20.070 1.00105.36 O
ANISOU 1824 O CYS B 274 18557 12162 9313 -1618 -751 384 O
ATOM 1825 CB CYS B 274 6.324 24.094 20.565 1.00108.60 C
ANISOU 1825 CB CYS B 274 18327 12481 10454 -1557 -1124 307 C
ATOM 1826 SG CYS B 274 5.189 23.628 21.896 1.00112.51 S
ANISOU 1826 SG CYS B 274 19054 12481 11212 -1698 -1059 379 S
ATOM 1827 N GLY B 275 3.318 25.341 19.473 1.00101.56 N
ANISOU 1827 N GLY B 275 17694 11605 9289 -1209 -844 -172 N
ATOM 1828 CA GLY B 275 2.299 26.332 19.760 1.00 94.67 C
ANISOU 1828 CA GLY B 275 17137 10625 8207 -1236 -671 -65 C
ATOM 1829 C GLY B 275 0.890 25.813 19.922 1.00 94.19 C
ANISOU 1829 C GLY B 275 16983 10393 8412 -1129 -647 -358 C
ATOM 1830 O GLY B 275 0.673 24.628 20.162 1.00100.50 O
ANISOU 1830 O GLY B 275 17551 10999 9636 -1147 -716 -620 O
ATOM 1831 N VAL B 276 -0.071 26.722 19.804 1.00114.83 N
ANISOU 1831 N VAL B 276 19772 13053 10806 -1013 -490 -302 N
ATOM 1832 CA VAL B 276 -1.481 26.371 19.870 1.00102.76 C
ANISOU 1832 CA VAL B 276 18108 11446 9492 -889 -454 -604 C
ATOM 1833 C VAL B 276 -2.070 26.413 18.466 1.00 94.25 C
ANISOU 1833 C VAL B 276 16622 10989 8198 -425 -519 -941 C
ATOM 1834 O VAL B 276 -1.564 27.121 17.594 1.00 87.03 O
ANISOU 1834 O VAL B 276 15706 10492 6870 -175 -500 -767 O
ATOM 1835 CB VAL B 276 -2.262 27.319 20.803 1.00 82.39 C
ANISOU 1835 CB VAL B 276 15967 8507 6832 -1059 -218 -308 C
ATOM 1836 CG1 VAL B 276 -1.675 27.278 22.202 1.00 77.54 C
ANISOU 1836 CG1 VAL B 276 15729 7393 6340 -1530 -168 -16 C
ATOM 1837 CG2 VAL B 276 -2.242 28.742 20.262 1.00 78.80 C
ANISOU 1837 CG2 VAL B 276 15740 8284 5916 -862 -4 18 C
ATOM 1838 N ASP B 277 -3.131 25.648 18.243 1.00 92.44 N
ANISOU 1838 N ASP B 277 16026 10864 8233 -308 -574 -1441 N
ATOM 1839 CA ASP B 277 -3.736 25.587 16.921 1.00 97.92 C
ANISOU 1839 CA ASP B 277 16235 12296 8675 123 -679 -1855 C
ATOM 1840 C ASP B 277 -5.250 25.733 16.980 1.00101.69 C
ANISOU 1840 C ASP B 277 16536 12908 9192 274 -621 -2099 C
ATOM 1841 O ASP B 277 -5.976 24.750 17.127 1.00102.11 O
ANISOU 1841 O ASP B 277 16247 12876 9675 153 -647 -2660 O
ATOM 1842 CB ASP B 277 -3.368 24.277 16.224 1.00125.24 C
ANISOU 1842 CB ASP B 277 19188 15993 12405 126 -834 -2464 C
ATOM 1843 CG ASP B 277 -3.811 24.247 14.775 1.00108.69 C
ANISOU 1843 CG ASP B 277 16561 14809 9926 553 -967 -2928 C
ATOM 1844 OD1 ASP B 277 -3.924 25.332 14.168 1.00110.07 O
ANISOU 1844 OD1 ASP B 277 16823 15479 9518 923 -960 -2582 O
ATOM 1845 OD2 ASP B 277 -4.045 23.142 14.243 1.00112.20 O
ANISOU 1845 OD2 ASP B 277 16493 15493 10643 528 -1039 -3643 O
ATOM 1846 N TYR B 278 -5.720 26.969 16.865 1.00101.65 N
ANISOU 1846 N TYR B 278 16753 13096 8773 544 -487 -1676 N
ATOM 1847 CA TYR B 278 -7.148 27.236 16.786 1.00118.42 C
ANISOU 1847 CA TYR B 278 18655 15480 10859 791 -433 -1847 C
ATOM 1848 C TYR B 278 -7.497 27.695 15.376 1.00133.67 C
ANISOU 1848 C TYR B 278 20160 18424 12205 1416 -541 -1924 C
ATOM 1849 O TYR B 278 -8.358 28.554 15.182 1.00121.31 O
ANISOU 1849 O TYR B 278 18579 17177 10337 1804 -417 -1663 O
ATOM 1850 CB TYR B 278 -7.565 28.281 17.822 1.00103.68 C
ANISOU 1850 CB TYR B 278 17353 13035 9006 667 -128 -1274 C
ATOM 1851 CG TYR B 278 -7.304 27.854 19.249 1.00 99.96 C
ANISOU 1851 CG TYR B 278 17288 11670 9021 77 -27 -1197 C
ATOM 1852 CD1 TYR B 278 -8.204 27.041 19.927 1.00104.51 C
ANISOU 1852 CD1 TYR B 278 17715 11905 10089 -146 -5 -1590 C
ATOM 1853 CD2 TYR B 278 -6.157 28.261 19.918 1.00 90.94 C
ANISOU 1853 CD2 TYR B 278 16652 10078 7824 -250 67 -740 C
ATOM 1854 CE1 TYR B 278 -7.968 26.646 21.232 1.00104.78 C
ANISOU 1854 CE1 TYR B 278 18133 11165 10512 -623 117 -1455 C
ATOM 1855 CE2 TYR B 278 -5.913 27.871 21.223 1.00104.18 C
ANISOU 1855 CE2 TYR B 278 18663 11077 9845 -740 135 -646 C
ATOM 1856 CZ TYR B 278 -6.821 27.064 21.875 1.00108.27 C
ANISOU 1856 CZ TYR B 278 19064 11261 10814 -898 164 -967 C
ATOM 1857 OH TYR B 278 -6.580 26.676 23.173 1.00 99.83 O
ANISOU 1857 OH TYR B 278 18341 9555 10035 -1326 261 -810 O
ATOM 1858 N SER B 279 -6.813 27.108 14.398 1.00140.25 N
ANISOU 1858 N SER B 279 20639 19787 12862 1541 -750 -2258 N
ATOM 1859 CA SER B 279 -7.008 27.454 12.995 1.00132.02 C
ANISOU 1859 CA SER B 279 19169 19812 11181 2149 -875 -2347 C
ATOM 1860 C SER B 279 -8.418 27.112 12.543 1.00138.18 C
ANISOU 1860 C SER B 279 19307 21311 11884 2423 -1023 -2929 C
ATOM 1861 O SER B 279 -8.943 26.048 12.874 1.00137.43 O
ANISOU 1861 O SER B 279 18863 21054 12299 2071 -1114 -3639 O
ATOM 1862 CB SER B 279 -5.984 26.734 12.113 1.00142.75 C
ANISOU 1862 CB SER B 279 20259 21548 12429 2141 -1058 -2698 C
ATOM 1863 OG SER B 279 -6.216 25.335 12.099 1.00163.23 O
ANISOU 1863 OG SER B 279 22374 24141 15506 1820 -1219 -3559 O
ATOM 1864 N HIS B 280 -9.020 28.029 11.789 1.00147.33 N
ANISOU 1864 N HIS B 280 20295 23274 12410 3069 -1004 -2613 N
ATOM 1865 CA HIS B 280 -10.404 27.903 11.339 1.00163.50 C
ANISOU 1865 CA HIS B 280 21689 26166 14268 3424 -1152 -3072 C
ATOM 1866 C HIS B 280 -11.359 27.777 12.523 1.00164.47 C
ANISOU 1866 C HIS B 280 21926 25576 14990 3064 -1013 -3178 C
ATOM 1867 O HIS B 280 -12.440 27.200 12.406 1.00169.99 O
ANISOU 1867 O HIS B 280 22018 26734 15836 3070 -1149 -3855 O
ATOM 1868 CB HIS B 280 -10.566 26.707 10.397 1.00171.63 C
ANISOU 1868 CB HIS B 280 21903 28073 15236 3392 -1488 -4113 C
ATOM 1869 N ASP B 281 -10.950 28.323 13.663 1.00165.78 N
ANISOU 1869 N ASP B 281 22850 24648 15489 2730 -720 -2546 N
ATOM 1870 CA ASP B 281 -11.780 28.308 14.858 1.00159.01 C
ANISOU 1870 CA ASP B 281 22204 23045 15166 2387 -532 -2548 C
ATOM 1871 C ASP B 281 -11.424 29.484 15.763 1.00147.03 C
ANISOU 1871 C ASP B 281 21514 20698 13652 2304 -150 -1640 C
ATOM 1872 O ASP B 281 -11.015 29.301 16.909 1.00159.23 O
ANISOU 1872 O ASP B 281 23558 21283 15657 1733 -2 -1519 O
ATOM 1873 CB ASP B 281 -11.622 26.986 15.609 1.00155.15 C
ANISOU 1873 CB ASP B 281 21667 21877 15405 1707 -589 -3179 C
ATOM 1874 CG ASP B 281 -12.918 26.520 16.241 1.00143.01 C
ANISOU 1874 CG ASP B 281 19850 20135 14352 1510 -507 -3655 C
ATOM 1875 OD1 ASP B 281 -13.822 27.360 16.441 1.00140.84 O
ANISOU 1875 OD1 ASP B 281 19616 19974 13925 1795 -367 -3333 O
ATOM 1876 OD2 ASP B 281 -13.032 25.315 16.547 1.00145.48 O
ANISOU 1876 OD2 ASP B 281 19907 20132 15236 1076 -525 -4340 O
ATOM 1877 N LYS B 282 -11.582 30.690 15.228 1.00133.69 N
ANISOU 1877 N LYS B 282 19949 19416 11432 2891 49 -1010 N
ATOM 1878 CA LYS B 282 -11.291 31.923 15.952 1.00131.32 C
ANISOU 1878 CA LYS B 282 20401 18377 11119 2851 523 -181 C
ATOM 1879 C LYS B 282 -12.238 32.105 17.137 1.00120.68 C
ANISOU 1879 C LYS B 282 19291 16336 10226 2561 770 -137 C
ATOM 1880 O LYS B 282 -11.850 32.634 18.187 1.00104.16 O
ANISOU 1880 O LYS B 282 17867 13333 8378 2134 1109 260 O
ATOM 1881 CB LYS B 282 -11.389 33.117 14.997 1.00121.95 C
ANISOU 1881 CB LYS B 282 19219 17819 9298 3647 773 469 C
ATOM 1882 CG LYS B 282 -10.968 34.453 15.585 1.00113.08 C
ANISOU 1882 CG LYS B 282 18874 15923 8170 3624 1389 1312 C
ATOM 1883 CD LYS B 282 -9.488 34.478 15.916 1.00107.25 C
ANISOU 1883 CD LYS B 282 18643 14578 7530 3091 1476 1445 C
ATOM 1884 CE LYS B 282 -9.078 35.826 16.483 1.00106.49 C
ANISOU 1884 CE LYS B 282 19276 13737 7450 3001 2157 2170 C
ATOM 1885 NZ LYS B 282 -7.707 35.802 17.064 1.00106.16 N
ANISOU 1885 NZ LYS B 282 19659 13058 7620 2315 2219 2168 N
ATOM 1886 N ARG B 283 -13.479 31.657 16.962 1.00127.90 N
ANISOU 1886 N ARG B 283 19627 17728 11241 2772 608 -594 N
ATOM 1887 CA ARG B 283 -14.490 31.758 18.008 1.00131.90 C
ANISOU 1887 CA ARG B 283 20275 17647 12194 2533 843 -616 C
ATOM 1888 C ARG B 283 -14.107 30.898 19.211 1.00130.33 C
ANISOU 1888 C ARG B 283 20418 16492 12608 1712 835 -937 C
ATOM 1889 O ARG B 283 -14.423 31.233 20.352 1.00142.76 O
ANISOU 1889 O ARG B 283 22467 17264 14513 1366 1152 -704 O
ATOM 1890 CB ARG B 283 -15.869 31.350 17.468 1.00141.91 C
ANISOU 1890 CB ARG B 283 20730 19745 13445 2925 638 -1146 C
ATOM 1891 CG ARG B 283 -16.134 29.846 17.429 1.00154.55 C
ANISOU 1891 CG ARG B 283 21747 21524 15453 2516 277 -2153 C
ATOM 1892 CD ARG B 283 -17.168 29.444 18.475 1.00156.20 C
ANISOU 1892 CD ARG B 283 21930 21124 16294 2123 455 -2490 C
ATOM 1893 NE ARG B 283 -17.086 28.032 18.843 1.00160.11 N
ANISOU 1893 NE ARG B 283 22199 21267 17369 1528 319 -3290 N
ATOM 1894 CZ ARG B 283 -17.676 27.045 18.177 1.00168.96 C
ANISOU 1894 CZ ARG B 283 22496 23075 18626 1536 76 -4200 C
ATOM 1895 NH1 ARG B 283 -18.390 27.307 17.091 1.00178.48 N
ANISOU 1895 NH1 ARG B 283 22975 25494 19343 2119 -147 -4449 N
ATOM 1896 NH2 ARG B 283 -17.547 25.792 18.594 1.00165.81 N
ANISOU 1896 NH2 ARG B 283 21981 22176 18845 971 95 -4870 N
ATOM 1897 N ARG B 284 -13.412 29.796 18.946 1.00100.03 N
ANISOU 1897 N ARG B 284 12717 17293 7997 -369 -1509 -3059 N
ATOM 1898 CA ARG B 284 -12.984 28.885 19.998 1.00 97.46 C
ANISOU 1898 CA ARG B 284 11718 16659 8654 -619 -1011 -3242 C
ATOM 1899 C ARG B 284 -11.817 29.492 20.762 1.00 91.13 C
ANISOU 1899 C ARG B 284 11180 15381 8065 -799 -570 -2675 C
ATOM 1900 O ARG B 284 -11.698 29.329 21.979 1.00112.38 O
ANISOU 1900 O ARG B 284 13489 17728 11481 -802 -410 -2544 O
ATOM 1901 CB ARG B 284 -12.600 27.534 19.402 1.00126.02 C
ANISOU 1901 CB ARG B 284 14932 20480 12471 -992 -605 -3882 C
ATOM 1902 CG ARG B 284 -12.067 26.520 20.385 1.00116.55 C
ANISOU 1902 CG ARG B 284 13071 18926 12285 -1257 -79 -4048 C
ATOM 1903 CD ARG B 284 -12.164 25.121 19.803 1.00128.77 C
ANISOU 1903 CD ARG B 284 14074 20703 14149 -1509 160 -4804 C
ATOM 1904 NE ARG B 284 -13.510 24.565 19.922 1.00131.51 N
ANISOU 1904 NE ARG B 284 13881 21255 14830 -1269 -233 -5274 N
ATOM 1905 CZ ARG B 284 -13.941 23.883 20.979 1.00121.48 C
ANISOU 1905 CZ ARG B 284 11971 19705 14482 -1240 -104 -5396 C
ATOM 1906 NH1 ARG B 284 -15.179 23.409 21.010 1.00121.31 N
ANISOU 1906 NH1 ARG B 284 11524 19765 14802 -983 -346 -5726 N
ATOM 1907 NH2 ARG B 284 -13.131 23.676 22.009 1.00104.30 N
ANISOU 1907 NH2 ARG B 284 9659 17059 12912 -1406 339 -5047 N
ATOM 1908 N GLU B 285 -10.958 30.196 20.033 1.00 91.08 N
ANISOU 1908 N GLU B 285 11844 15356 7408 -956 -368 -2357 N
ATOM 1909 CA GLU B 285 -9.862 30.936 20.635 1.00 90.84 C
ANISOU 1909 CA GLU B 285 12106 14875 7534 -1114 11 -1839 C
ATOM 1910 C GLU B 285 -10.410 32.004 21.572 1.00 95.12 C
ANISOU 1910 C GLU B 285 12775 15158 8209 -744 -377 -1360 C
ATOM 1911 O GLU B 285 -9.953 32.142 22.712 1.00 78.10 O
ANISOU 1911 O GLU B 285 10401 12626 6647 -793 -181 -1148 O
ATOM 1912 CB GLU B 285 -8.986 31.565 19.551 1.00 90.85 C
ANISOU 1912 CB GLU B 285 12847 14910 6763 -1342 307 -1613 C
ATOM 1913 CG GLU B 285 -7.860 32.435 20.083 0.85101.33 C
ANISOU 1913 CG GLU B 285 14489 15751 8263 -1511 706 -1109 C
ATOM 1914 CD GLU B 285 -7.118 33.144 18.967 0.61112.70 C
ANISOU 1914 CD GLU B 285 16714 17198 8907 -1727 1029 -864 C
ATOM 1915 OE1 GLU B 285 -7.460 32.907 17.789 1.00141.21 O
ANISOU 1915 OE1 GLU B 285 20656 21224 11773 -1750 939 -1081 O
ATOM 1916 OE2 GLU B 285 -6.196 33.932 19.261 1.00 97.93 O
ANISOU 1916 OE2 GLU B 285 15144 14918 7146 -1884 1388 -475 O
ATOM 1917 N ARG B 286 -11.400 32.750 21.086 1.00 88.20 N
ANISOU 1917 N ARG B 286 12242 14485 6784 -362 -954 -1219 N
ATOM 1918 CA ARG B 286 -12.031 33.779 21.904 1.00 82.80 C
ANISOU 1918 CA ARG B 286 11647 13556 6256 15 -1343 -826 C
ATOM 1919 C ARG B 286 -12.681 33.143 23.132 1.00 85.06 C
ANISOU 1919 C ARG B 286 11196 13743 7380 118 -1400 -1088 C
ATOM 1920 O ARG B 286 -12.565 33.668 24.242 1.00 79.03 O
ANISOU 1920 O ARG B 286 10367 12633 7029 189 -1340 -804 O
ATOM 1921 CB ARG B 286 -13.072 34.567 21.109 1.00 85.87 C
ANISOU 1921 CB ARG B 286 12452 14183 5990 443 -2015 -695 C
ATOM 1922 CG ARG B 286 -13.337 35.959 21.669 1.00 88.04 C
ANISOU 1922 CG ARG B 286 13078 14106 6266 773 -2301 -143 C
ATOM 1923 CD ARG B 286 -14.617 36.559 21.109 1.00 94.24 C
ANISOU 1923 CD ARG B 286 14045 15098 6662 1284 -3080 -108 C
ATOM 1924 NE ARG B 286 -14.762 36.310 19.678 1.00139.09 N
ANISOU 1924 NE ARG B 286 20112 21200 11536 1281 -3315 -243 N
ATOM 1925 CZ ARG B 286 -15.812 35.707 19.130 1.00138.14 C
ANISOU 1925 CZ ARG B 286 19623 21389 11474 1413 -3739 -682 C
ATOM 1926 NH1 ARG B 286 -16.813 35.297 19.897 1.00128.28 N
ANISOU 1926 NH1 ARG B 286 17656 20142 10944 1643 -4006 -1056 N
ATOM 1927 NH2 ARG B 286 -15.867 35.517 17.817 1.00103.09 N
ANISOU 1927 NH2 ARG B 286 15541 17234 6393 1297 -3862 -757 N
ATOM 1928 N ALA B 287 -13.344 32.005 22.932 1.00 89.36 N
ANISOU 1928 N ALA B 287 11202 14582 8170 104 -1477 -1646 N
ATOM 1929 CA ALA B 287 -13.991 31.286 24.025 1.00 78.65 C
ANISOU 1929 CA ALA B 287 9155 13121 7607 163 -1448 -1923 C
ATOM 1930 C ALA B 287 -12.991 30.888 25.107 1.00 73.56 C
ANISOU 1930 C ALA B 287 8305 12103 7540 -133 -910 -1761 C
ATOM 1931 O ALA B 287 -13.245 31.084 26.294 1.00 63.38 O
ANISOU 1931 O ALA B 287 6823 10557 6701 -26 -902 -1605 O
ATOM 1932 CB ALA B 287 -14.714 30.061 23.492 1.00 79.24 C
ANISOU 1932 CB ALA B 287 8695 13543 7871 125 -1524 -2586 C
ATOM 1933 N VAL B 288 -11.857 30.332 24.690 1.00 72.15 N
ANISOU 1933 N VAL B 288 8171 11895 7346 -500 -475 -1818 N
ATOM 1934 CA VAL B 288 -10.807 29.936 25.623 1.00 63.35 C
ANISOU 1934 CA VAL B 288 6859 10421 6789 -766 -26 -1675 C
ATOM 1935 C VAL B 288 -10.264 31.139 26.390 1.00 61.47 C
ANISOU 1935 C VAL B 288 7008 9848 6501 -691 -42 -1135 C
ATOM 1936 O VAL B 288 -10.083 31.077 27.609 1.00 66.43 O
ANISOU 1936 O VAL B 288 7426 10202 7614 -691 47 -990 O
ATOM 1937 CB VAL B 288 -9.647 29.225 24.896 1.00 62.15 C
ANISOU 1937 CB VAL B 288 6686 10280 6649 -1164 430 -1871 C
ATOM 1938 CG1 VAL B 288 -8.476 28.998 25.841 1.00 55.24 C
ANISOU 1938 CG1 VAL B 288 5643 8991 6355 -1394 807 -1675 C
ATOM 1939 CG2 VAL B 288 -10.122 27.908 24.308 1.00 59.99 C
ANISOU 1939 CG2 VAL B 288 5932 10284 6579 -1275 510 -2470 C
ATOM 1940 N ALA B 289 -10.017 32.234 25.676 1.00 70.56 N
ANISOU 1940 N ALA B 289 8744 11013 7051 -630 -154 -843 N
ATOM 1941 CA ALA B 289 -9.529 33.455 26.314 1.00 72.80 C
ANISOU 1941 CA ALA B 289 9401 10957 7302 -562 -161 -365 C
ATOM 1942 C ALA B 289 -10.507 33.969 27.371 1.00 72.50 C
ANISOU 1942 C ALA B 289 9228 10814 7503 -226 -501 -249 C
ATOM 1943 O ALA B 289 -10.108 34.325 28.483 1.00 62.74 O
ANISOU 1943 O ALA B 289 7949 9279 6611 -246 -401 -49 O
ATOM 1944 CB ALA B 289 -9.272 34.526 25.273 1.00 77.28 C
ANISOU 1944 CB ALA B 289 10640 11543 7178 -528 -222 -70 C
ATOM 1945 N ILE B 290 -11.787 33.998 27.015 1.00 72.32 N
ANISOU 1945 N ILE B 290 9123 11044 7312 77 -902 -422 N
ATOM 1946 CA ILE B 290 -12.830 34.487 27.911 1.00 69.94 C
ANISOU 1946 CA ILE B 290 8658 10650 7267 400 -1202 -391 C
ATOM 1947 C ILE B 290 -12.992 33.601 29.145 1.00 72.07 C
ANISOU 1947 C ILE B 290 8397 10812 8174 305 -977 -591 C
ATOM 1948 O ILE B 290 -13.002 34.096 30.272 1.00 55.28 O
ANISOU 1948 O ILE B 290 6274 8435 6296 370 -941 -407 O
ATOM 1949 CB ILE B 290 -14.183 34.591 27.182 1.00 68.73 C
ANISOU 1949 CB ILE B 290 8436 10793 6884 746 -1700 -624 C
ATOM 1950 CG1 ILE B 290 -14.116 35.663 26.093 1.00 75.85 C
ANISOU 1950 CG1 ILE B 290 9973 11748 7097 918 -2006 -308 C
ATOM 1951 CG2 ILE B 290 -15.298 34.904 28.167 1.00 69.07 C
ANISOU 1951 CG2 ILE B 290 8166 10723 7352 1042 -1927 -713 C
ATOM 1952 CD1 ILE B 290 -15.350 35.728 25.223 1.00 79.08 C
ANISOU 1952 CD1 ILE B 290 10356 12482 7208 1275 -2587 -535 C
ATOM 1953 N VAL B 291 -13.120 32.295 28.927 1.00 93.63 N
ANISOU 1953 N VAL B 291 10701 13720 11155 145 -809 -969 N
ATOM 1954 CA VAL B 291 -13.275 31.340 30.021 1.00 71.56 C
ANISOU 1954 CA VAL B 291 7437 10796 8957 40 -553 -1130 C
ATOM 1955 C VAL B 291 -12.073 31.387 30.960 1.00 76.93 C
ANISOU 1955 C VAL B 291 8232 11156 9841 -174 -258 -813 C
ATOM 1956 O VAL B 291 -12.223 31.344 32.183 1.00 89.74 O
ANISOU 1956 O VAL B 291 9742 12587 11768 -144 -177 -714 O
ATOM 1957 CB VAL B 291 -13.465 29.902 29.491 1.00 76.13 C
ANISOU 1957 CB VAL B 291 7552 11567 9805 -131 -375 -1585 C
ATOM 1958 CG1 VAL B 291 -13.398 28.893 30.628 1.00 62.41 C
ANISOU 1958 CG1 VAL B 291 5411 9609 8694 -280 -36 -1649 C
ATOM 1959 CG2 VAL B 291 -14.786 29.783 28.750 1.00 90.79 C
ANISOU 1959 CG2 VAL B 291 9191 13741 11565 102 -713 -1988 C
ATOM 1960 N ARG B 292 -10.880 31.494 30.382 1.00 56.82 N
ANISOU 1960 N ARG B 292 5918 8554 7116 -392 -100 -676 N
ATOM 1961 CA ARG B 292 -9.664 31.607 31.176 1.00 58.17 C
ANISOU 1961 CA ARG B 292 6172 8418 7512 -583 118 -417 C
ATOM 1962 C ARG B 292 -9.663 32.895 31.995 1.00 85.38 C
ANISOU 1962 C ARG B 292 9944 11662 10834 -418 -49 -89 C
ATOM 1963 O ARG B 292 -9.254 32.902 33.156 1.00 83.92 O
ANISOU 1963 O ARG B 292 9711 11260 10915 -461 17 48 O
ATOM 1964 CB ARG B 292 -8.429 31.547 30.277 1.00 45.11 C
ANISOU 1964 CB ARG B 292 4669 6731 5739 -855 347 -406 C
ATOM 1965 CG ARG B 292 -7.114 31.471 31.031 1.00 47.53 C
ANISOU 1965 CG ARG B 292 4930 6715 6415 -1068 560 -242 C
ATOM 1966 CD ARG B 292 -6.009 30.983 30.118 1.00 55.90 C
ANISOU 1966 CD ARG B 292 5937 7749 7555 -1378 878 -394 C
ATOM 1967 NE ARG B 292 -6.339 29.688 29.533 1.00107.49 N
ANISOU 1967 NE ARG B 292 12090 14480 14271 -1479 1021 -769 N
ATOM 1968 CZ ARG B 292 -5.741 29.176 28.462 1.00101.20 C
ANISOU 1968 CZ ARG B 292 11236 13774 13443 -1728 1301 -1028 C
ATOM 1969 NH1 ARG B 292 -4.779 29.851 27.848 1.00 66.26 N
ANISOU 1969 NH1 ARG B 292 7129 9252 8796 -1913 1503 -930 N
ATOM 1970 NH2 ARG B 292 -6.111 27.990 28.003 1.00 83.88 N
ANISOU 1970 NH2 ARG B 292 8660 11751 11461 -1813 1423 -1418 N
ATOM 1971 N LEU B 293 -10.129 33.982 31.387 1.00 69.72 N
ANISOU 1971 N LEU B 293 8304 9742 8444 -223 -282 28 N
ATOM 1972 CA LEU B 293 -10.220 35.262 32.080 1.00 59.13 C
ANISOU 1972 CA LEU B 293 7254 8185 7026 -51 -436 298 C
ATOM 1973 C LEU B 293 -11.173 35.193 33.272 1.00 55.08 C
ANISOU 1973 C LEU B 293 6509 7640 6778 129 -527 211 C
ATOM 1974 O LEU B 293 -10.848 35.651 34.368 1.00 51.24 O
ANISOU 1974 O LEU B 293 6101 6939 6430 117 -482 353 O
ATOM 1975 CB LEU B 293 -10.673 36.363 31.118 1.00 57.05 C
ANISOU 1975 CB LEU B 293 7388 7972 6317 164 -690 446 C
ATOM 1976 CG LEU B 293 -11.004 37.706 31.776 1.00 57.16 C
ANISOU 1976 CG LEU B 293 7654 7742 6321 393 -876 678 C
ATOM 1977 CD1 LEU B 293 -9.751 38.341 32.362 1.00 57.20 C
ANISOU 1977 CD1 LEU B 293 7877 7422 6436 189 -659 910 C
ATOM 1978 CD2 LEU B 293 -11.693 38.647 30.799 1.00 65.41 C
ANISOU 1978 CD2 LEU B 293 9041 8831 6980 677 -1198 819 C
ATOM 1979 N VAL B 294 -12.349 34.615 33.051 1.00 47.79 N
ANISOU 1979 N VAL B 294 5295 6931 5930 281 -633 -64 N
ATOM 1980 CA VAL B 294 -13.380 34.556 34.081 1.00 52.28 C
ANISOU 1980 CA VAL B 294 5631 7466 6769 441 -654 -202 C
ATOM 1981 C VAL B 294 -13.030 33.586 35.207 1.00 54.34 C
ANISOU 1981 C VAL B 294 5665 7618 7363 239 -346 -225 C
ATOM 1982 O VAL B 294 -12.971 33.974 36.373 1.00 58.25 O
ANISOU 1982 O VAL B 294 6263 7940 7929 250 -280 -98 O
ATOM 1983 CB VAL B 294 -14.741 34.153 33.486 1.00 53.48 C
ANISOU 1983 CB VAL B 294 5463 7855 7000 644 -833 -557 C
ATOM 1984 CG1 VAL B 294 -15.782 34.015 34.589 1.00 51.70 C
ANISOU 1984 CG1 VAL B 294 4950 7555 7139 758 -743 -752 C
ATOM 1985 CG2 VAL B 294 -15.189 35.172 32.449 1.00 51.90 C
ANISOU 1985 CG2 VAL B 294 5525 7751 6443 911 -1236 -497 C
ATOM 1986 N LEU B 295 -12.800 32.324 34.856 1.00 71.30 N
ANISOU 1986 N LEU B 295 7529 9858 9704 60 -163 -385 N
ATOM 1987 CA LEU B 295 -12.549 31.294 35.857 1.00 51.54 C
ANISOU 1987 CA LEU B 295 4814 7223 7546 -105 116 -378 C
ATOM 1988 C LEU B 295 -11.170 31.431 36.494 1.00 51.40 C
ANISOU 1988 C LEU B 295 5017 6989 7522 -271 176 -69 C
ATOM 1989 O LEU B 295 -10.966 31.035 37.640 1.00 79.49 O
ANISOU 1989 O LEU B 295 8568 10393 11242 -330 294 54 O
ATOM 1990 CB LEU B 295 -12.694 29.903 35.237 1.00 49.93 C
ANISOU 1990 CB LEU B 295 4211 7131 7631 -243 298 -657 C
ATOM 1991 CG LEU B 295 -14.045 29.580 34.596 1.00 55.85 C
ANISOU 1991 CG LEU B 295 4643 8104 8475 -100 229 -1059 C
ATOM 1992 CD1 LEU B 295 -14.085 28.130 34.138 1.00 55.01 C
ANISOU 1992 CD1 LEU B 295 4238 8006 8656 -266 445 -1303 C
ATOM 1993 CD2 LEU B 295 -15.190 29.881 35.552 1.00 45.56 C
ANISOU 1993 CD2 LEU B 295 3250 6734 7326 69 258 -1138 C
ATOM 1994 N GLY B 296 -10.226 31.996 35.751 1.00 62.25 N
ANISOU 1994 N GLY B 296 6597 8344 8712 -348 94 45 N
ATOM 1995 CA GLY B 296 -8.857 32.078 36.221 1.00 53.82 C
ANISOU 1995 CA GLY B 296 5649 7062 7737 -519 141 254 C
ATOM 1996 C GLY B 296 -8.477 33.390 36.878 1.00 67.44 C
ANISOU 1996 C GLY B 296 7719 8631 9275 -447 -10 465 C
ATOM 1997 O GLY B 296 -7.427 33.480 37.513 1.00 73.91 O
ANISOU 1997 O GLY B 296 8603 9265 10215 -566 -18 599 O
ATOM 1998 N PHE B 297 -9.319 34.411 36.741 1.00 57.78 N
ANISOU 1998 N PHE B 297 6685 7461 7807 -245 -151 466 N
ATOM 1999 CA PHE B 297 -8.956 35.727 37.255 1.00 65.49 C
ANISOU 1999 CA PHE B 297 7976 8257 8650 -184 -270 630 C
ATOM 2000 C PHE B 297 -10.107 36.498 37.907 1.00 58.30 C
ANISOU 2000 C PHE B 297 7152 7347 7651 54 -378 583 C
ATOM 2001 O PHE B 297 -10.048 36.812 39.094 1.00 53.27 O
ANISOU 2001 O PHE B 297 6599 6598 7042 58 -373 612 O
ATOM 2002 CB PHE B 297 -8.351 36.574 36.131 1.00 54.97 C
ANISOU 2002 CB PHE B 297 6888 6860 7139 -222 -299 735 C
ATOM 2003 CG PHE B 297 -7.561 37.753 36.621 1.00 60.78 C
ANISOU 2003 CG PHE B 297 7894 7330 7872 -258 -337 890 C
ATOM 2004 CD1 PHE B 297 -6.207 37.631 36.889 1.00 58.12 C
ANISOU 2004 CD1 PHE B 297 7530 6819 7736 -490 -243 929 C
ATOM 2005 CD2 PHE B 297 -8.170 38.983 36.818 1.00 58.81 C
ANISOU 2005 CD2 PHE B 297 7878 6975 7492 -56 -472 954 C
ATOM 2006 CE1 PHE B 297 -5.475 38.712 37.343 1.00 74.75 C
ANISOU 2006 CE1 PHE B 297 9833 8668 9901 -537 -278 1005 C
ATOM 2007 CE2 PHE B 297 -7.443 40.067 37.272 1.00 53.22 C
ANISOU 2007 CE2 PHE B 297 7387 5993 6839 -104 -481 1052 C
ATOM 2008 CZ PHE B 297 -6.093 39.932 37.535 1.00 60.69 C
ANISOU 2008 CZ PHE B 297 8299 6784 7974 -353 -381 1065 C
ATOM 2009 N LEU B 298 -11.143 36.805 37.133 1.00 56.27 N
ANISOU 2009 N LEU B 298 6869 7216 7295 253 -490 482 N
ATOM 2010 CA LEU B 298 -12.182 37.735 37.580 1.00 66.88 C
ANISOU 2010 CA LEU B 298 8279 8507 8626 502 -616 416 C
ATOM 2011 C LEU B 298 -13.039 37.198 38.724 1.00 62.80 C
ANISOU 2011 C LEU B 298 7544 8026 8289 534 -470 225 C
ATOM 2012 O LEU B 298 -13.225 37.876 39.737 1.00 63.52 O
ANISOU 2012 O LEU B 298 7759 7988 8389 584 -438 213 O
ATOM 2013 CB LEU B 298 -13.077 38.125 36.401 1.00 68.56 C
ANISOU 2013 CB LEU B 298 8482 8837 8729 741 -842 348 C
ATOM 2014 CG LEU B 298 -12.396 38.976 35.325 1.00 62.00 C
ANISOU 2014 CG LEU B 298 8006 7920 7630 753 -977 594 C
ATOM 2015 CD1 LEU B 298 -13.408 39.466 34.302 1.00 63.21 C
ANISOU 2015 CD1 LEU B 298 8216 8178 7624 1055 -1286 564 C
ATOM 2016 CD2 LEU B 298 -11.646 40.145 35.950 1.00 59.09 C
ANISOU 2016 CD2 LEU B 298 7943 7239 7271 714 -944 801 C
ATOM 2017 N TRP B 299 -13.570 35.992 38.556 1.00 70.41 N
ANISOU 2017 N TRP B 299 8193 9153 9406 488 -340 52 N
ATOM 2018 CA TRP B 299 -14.346 35.342 39.611 1.00 75.73 C
ANISOU 2018 CA TRP B 299 8673 9830 10271 469 -100 -116 C
ATOM 2019 C TRP B 299 -13.528 35.158 40.905 1.00 59.99 C
ANISOU 2019 C TRP B 299 6884 7703 8207 291 61 71 C
ATOM 2020 O TRP B 299 -14.018 35.485 41.997 1.00 65.64 O
ANISOU 2020 O TRP B 299 7695 8351 8893 320 191 10 O
ATOM 2021 CB TRP B 299 -14.892 34.000 39.104 1.00 61.18 C
ANISOU 2021 CB TRP B 299 6445 8139 8663 409 49 -327 C
ATOM 2022 CG TRP B 299 -15.643 33.200 40.119 1.00 87.33 C
ANISOU 2022 CG TRP B 299 9559 11409 12212 345 387 -481 C
ATOM 2023 CD1 TRP B 299 -15.263 32.009 40.667 1.00 81.06 C
ANISOU 2023 CD1 TRP B 299 8689 10558 11552 141 667 -397 C
ATOM 2024 CD2 TRP B 299 -16.910 33.525 40.702 1.00 67.32 C
ANISOU 2024 CD2 TRP B 299 6887 8850 9842 476 524 -745 C
ATOM 2025 NE1 TRP B 299 -16.215 31.574 41.557 1.00 59.13 N
ANISOU 2025 NE1 TRP B 299 5787 7720 8961 122 1003 -557 N
ATOM 2026 CE2 TRP B 299 -17.235 32.486 41.597 1.00 54.42 C
ANISOU 2026 CE2 TRP B 299 5131 7149 8398 312 945 -803 C
ATOM 2027 CE3 TRP B 299 -17.799 34.593 40.556 1.00 57.55 C
ANISOU 2027 CE3 TRP B 299 5608 7606 8652 718 349 -943 C
ATOM 2028 CZ2 TRP B 299 -18.412 32.485 42.343 1.00 55.42 C
ANISOU 2028 CZ2 TRP B 299 5101 7215 8742 346 1257 -1080 C
ATOM 2029 CZ3 TRP B 299 -18.967 34.590 41.298 1.00 75.07 C
ANISOU 2029 CZ3 TRP B 299 7614 9764 11143 774 615 -1251 C
ATOM 2030 CH2 TRP B 299 -19.263 33.544 42.179 1.00 60.33 C
ANISOU 2030 CH2 TRP B 299 5635 7845 9445 571 1095 -1331 C
ATOM 2031 N PRO B 300 -12.279 34.654 40.795 1.00 59.76 N
ANISOU 2031 N PRO B 300 6924 7633 8149 110 40 275 N
ATOM 2032 CA PRO B 300 -11.456 34.579 42.006 1.00 60.27 C
ANISOU 2032 CA PRO B 300 7200 7573 8127 -14 74 456 C
ATOM 2033 C PRO B 300 -11.180 35.937 42.628 1.00 68.30 C
ANISOU 2033 C PRO B 300 8523 8484 8946 48 -73 494 C
ATOM 2034 O PRO B 300 -11.178 36.057 43.848 1.00101.81 O
ANISOU 2034 O PRO B 300 12945 12682 13057 18 -15 510 O
ATOM 2035 CB PRO B 300 -10.154 33.957 41.501 1.00 59.39 C
ANISOU 2035 CB PRO B 300 7034 7414 8117 -178 3 612 C
ATOM 2036 CG PRO B 300 -10.562 33.158 40.330 1.00 59.77 C
ANISOU 2036 CG PRO B 300 6781 7588 8339 -190 93 473 C
ATOM 2037 CD PRO B 300 -11.606 33.990 39.661 1.00 49.99 C
ANISOU 2037 CD PRO B 300 5541 6461 6993 3 5 306 C
ATOM 2038 N LEU B 301 -10.935 36.937 41.790 1.00 73.46 N
ANISOU 2038 N LEU B 301 9258 9087 9568 124 -245 507 N
ATOM 2039 CA LEU B 301 -10.692 38.291 42.266 1.00 82.87 C
ANISOU 2039 CA LEU B 301 10706 10127 10654 184 -363 515 C
ATOM 2040 C LEU B 301 -11.869 38.768 43.107 1.00 70.63 C
ANISOU 2040 C LEU B 301 9180 8580 9074 323 -261 321 C
ATOM 2041 O LEU B 301 -11.698 39.182 44.252 1.00102.67 O
ANISOU 2041 O LEU B 301 13425 12574 13012 277 -225 276 O
ATOM 2042 CB LEU B 301 -10.451 39.235 41.088 1.00 94.90 C
ANISOU 2042 CB LEU B 301 12316 11558 12184 263 -505 584 C
ATOM 2043 CG LEU B 301 -10.057 40.674 41.412 1.00 61.93 C
ANISOU 2043 CG LEU B 301 8391 7151 7988 304 -602 607 C
ATOM 2044 CD1 LEU B 301 -8.842 40.697 42.323 1.00 56.84 C
ANISOU 2044 CD1 LEU B 301 7851 6405 7341 108 -626 640 C
ATOM 2045 CD2 LEU B 301 -9.783 41.441 40.129 1.00 56.93 C
ANISOU 2045 CD2 LEU B 301 7883 6392 7355 362 -686 749 C
ATOM 2046 N LEU B 302 -13.062 38.678 42.529 1.00 62.08 N
ANISOU 2046 N LEU B 302 7890 7580 8119 486 -215 162 N
ATOM 2047 CA LEU B 302 -14.296 39.050 43.209 1.00 59.99 C
ANISOU 2047 CA LEU B 302 7552 7301 7940 619 -72 -94 C
ATOM 2048 C LEU B 302 -14.458 38.330 44.550 1.00 77.69 C
ANISOU 2048 C LEU B 302 9848 9584 10088 467 229 -157 C
ATOM 2049 O LEU B 302 -14.531 38.969 45.610 1.00 79.08 O
ANISOU 2049 O LEU B 302 10230 9687 10131 446 324 -253 O
ATOM 2050 CB LEU B 302 -15.494 38.747 42.307 1.00 53.93 C
ANISOU 2050 CB LEU B 302 6451 6634 7406 802 -92 -289 C
ATOM 2051 CG LEU B 302 -16.890 39.106 42.817 1.00 63.71 C
ANISOU 2051 CG LEU B 302 7495 7834 8879 964 57 -632 C
ATOM 2052 CD1 LEU B 302 -17.057 40.614 42.902 1.00 69.54 C
ANISOU 2052 CD1 LEU B 302 8384 8376 9664 1152 -117 -682 C
ATOM 2053 CD2 LEU B 302 -17.958 38.491 41.924 1.00 53.18 C
ANISOU 2053 CD2 LEU B 302 5747 6628 7829 1111 12 -862 C
ATOM 2054 N THR B 303 -14.498 37.000 44.498 1.00 62.97 N
ANISOU 2054 N THR B 303 7825 7823 8278 352 393 -102 N
ATOM 2055 CA THR B 303 -14.778 36.199 45.687 1.00 60.74 C
ANISOU 2055 CA THR B 303 7621 7552 7903 213 727 -115 C
ATOM 2056 C THR B 303 -13.731 36.358 46.791 1.00 68.01 C
ANISOU 2056 C THR B 303 8940 8427 8473 79 659 92 C
ATOM 2057 O THR B 303 -14.080 36.519 47.961 1.00100.49 O
ANISOU 2057 O THR B 303 13282 12532 12367 27 872 10 O
ATOM 2058 CB THR B 303 -14.888 34.713 45.332 1.00 55.76 C
ANISOU 2058 CB THR B 303 6748 6980 7458 111 908 -50 C
ATOM 2059 OG1 THR B 303 -13.683 34.291 44.687 1.00 76.42 O
ANISOU 2059 OG1 THR B 303 9370 9600 10064 35 664 200 O
ATOM 2060 CG2 THR B 303 -16.069 34.474 44.403 1.00 49.34 C
ANISOU 2060 CG2 THR B 303 5509 6236 7001 235 992 -349 C
ATOM 2061 N LEU B 304 -12.455 36.307 46.422 1.00 61.11 N
ANISOU 2061 N LEU B 304 8141 7527 7550 19 364 325 N
ATOM 2062 CA LEU B 304 -11.379 36.434 47.402 1.00 64.92 C
ANISOU 2062 CA LEU B 304 8945 7968 7753 -85 200 488 C
ATOM 2063 C LEU B 304 -11.322 37.843 47.984 1.00 97.05 C
ANISOU 2063 C LEU B 304 13246 11984 11645 -37 92 319 C
ATOM 2064 O LEU B 304 -11.024 38.020 49.169 1.00123.54 O
ANISOU 2064 O LEU B 304 16902 15355 14683 -107 77 308 O
ATOM 2065 CB LEU B 304 -10.029 36.064 46.782 1.00 60.39 C
ANISOU 2065 CB LEU B 304 8298 7344 7302 -158 -87 704 C
ATOM 2066 CG LEU B 304 -9.846 34.598 46.380 1.00 67.05 C
ANISOU 2066 CG LEU B 304 8928 8202 8346 -234 6 870 C
ATOM 2067 CD1 LEU B 304 -8.442 34.350 45.843 1.00 66.55 C
ANISOU 2067 CD1 LEU B 304 8771 8054 8460 -314 -265 1021 C
ATOM 2068 CD2 LEU B 304 -10.147 33.673 47.547 1.00 64.56 C
ANISOU 2068 CD2 LEU B 304 8788 7888 7852 -294 203 1001 C
ATOM 2069 N THR B 305 -11.614 38.845 47.157 1.00 75.51 N
ANISOU 2069 N THR B 305 10395 9183 9113 87 10 183 N
ATOM 2070 CA THR B 305 -11.646 40.219 47.646 1.00 89.00 C
ANISOU 2070 CA THR B 305 12278 10783 10754 142 -55 -8 C
ATOM 2071 C THR B 305 -12.772 40.389 48.661 1.00 72.28 C
ANISOU 2071 C THR B 305 10245 8707 8509 164 256 -272 C
ATOM 2072 O THR B 305 -12.582 41.035 49.688 1.00 63.31 O
ANISOU 2072 O THR B 305 9367 7551 7138 107 271 -421 O
ATOM 2073 CB THR B 305 -11.819 41.244 46.511 1.00 71.02 C
ANISOU 2073 CB THR B 305 9872 8361 8751 297 -188 -53 C
ATOM 2074 OG1 THR B 305 -10.779 41.061 45.542 1.00 71.36 O
ANISOU 2074 OG1 THR B 305 9870 8361 8883 238 -388 179 O
ATOM 2075 CG2 THR B 305 -11.744 42.662 47.056 1.00 61.40 C
ANISOU 2075 CG2 THR B 305 8825 6966 7539 341 -242 -246 C
ATOM 2076 N ILE B 306 -13.938 39.810 48.375 1.00 60.69 N
ANISOU 2076 N ILE B 306 8545 7296 7219 229 527 -378 N
ATOM 2077 CA ILE B 306 -15.028 39.797 49.350 1.00 72.92 C
ANISOU 2077 CA ILE B 306 10140 8869 8698 206 928 -655 C
ATOM 2078 C ILE B 306 -14.572 39.128 50.648 1.00 88.28 C
ANISOU 2078 C ILE B 306 12458 10909 10174 5 1087 -533 C
ATOM 2079 O ILE B 306 -14.706 39.693 51.745 1.00 92.82 O
ANISOU 2079 O ILE B 306 13323 11495 10452 -62 1239 -725 O
ATOM 2080 CB ILE B 306 -16.274 39.059 48.811 1.00 70.14 C
ANISOU 2080 CB ILE B 306 9414 8550 8687 276 1214 -802 C
ATOM 2081 CG1 ILE B 306 -16.884 39.814 47.627 1.00 73.70 C
ANISOU 2081 CG1 ILE B 306 9528 8919 9556 520 1003 -962 C
ATOM 2082 CG2 ILE B 306 -17.308 38.887 49.911 1.00 70.64 C
ANISOU 2082 CG2 ILE B 306 9532 8615 8693 188 1731 -1091 C
ATOM 2083 CD1 ILE B 306 -17.993 39.059 46.916 1.00 66.23 C
ANISOU 2083 CD1 ILE B 306 8150 8027 8986 613 1153 -1133 C
ATOM 2084 N CYS B 307 -14.020 37.927 50.500 1.00 73.41 N
ANISOU 2084 N CYS B 307 10584 9088 8221 -82 1037 -212 N
ATOM 2085 CA CYS B 307 -13.539 37.117 51.618 1.00 76.13 C
ANISOU 2085 CA CYS B 307 11301 9496 8128 -238 1124 9 C
ATOM 2086 C CYS B 307 -12.620 37.888 52.575 1.00 72.00 C
ANISOU 2086 C CYS B 307 11188 9007 7162 -289 838 2 C
ATOM 2087 O CYS B 307 -12.875 37.986 53.789 1.00 76.98 O
ANISOU 2087 O CYS B 307 12199 9707 7343 -381 1047 -96 O
ATOM 2088 CB CYS B 307 -12.821 35.873 51.066 1.00 86.83 C
ANISOU 2088 CB CYS B 307 12536 10845 9612 -278 965 378 C
ATOM 2089 SG CYS B 307 -12.409 34.624 52.314 1.00 68.88 S
ANISOU 2089 SG CYS B 307 10692 8587 6892 -423 1086 737 S
ATOM 2090 N TYR B 308 -11.558 38.451 52.014 1.00 64.93 N
ANISOU 2090 N TYR B 308 10213 8058 6397 -242 382 69 N
ATOM 2091 CA TYR B 308 -10.564 39.132 52.826 1.00 76.02 C
ANISOU 2091 CA TYR B 308 11928 9483 7474 -292 46 24 C
ATOM 2092 C TYR B 308 -10.997 40.545 53.199 1.00 73.31 C
ANISOU 2092 C TYR B 308 11658 9095 7103 -263 129 -384 C
ATOM 2093 O TYR B 308 -10.415 41.147 54.093 1.00 70.27 O
ANISOU 2093 O TYR B 308 11559 8751 6391 -325 -58 -532 O
ATOM 2094 CB TYR B 308 -9.209 39.141 52.114 1.00 64.64 C
ANISOU 2094 CB TYR B 308 10327 7960 6274 -284 -426 208 C
ATOM 2095 CG TYR B 308 -8.594 37.764 52.078 1.00 74.88 C
ANISOU 2095 CG TYR B 308 11610 9285 7557 -327 -555 574 C
ATOM 2096 CD1 TYR B 308 -8.670 36.979 50.936 1.00 88.98 C
ANISOU 2096 CD1 TYR B 308 13043 11015 9750 -305 -473 742 C
ATOM 2097 CD2 TYR B 308 -7.967 37.234 53.198 1.00 87.58 C
ANISOU 2097 CD2 TYR B 308 13568 10967 8742 -379 -768 742 C
ATOM 2098 CE1 TYR B 308 -8.123 35.714 50.904 1.00103.53 C
ANISOU 2098 CE1 TYR B 308 14837 12838 11661 -344 -563 1045 C
ATOM 2099 CE2 TYR B 308 -7.416 35.966 53.175 1.00 92.49 C
ANISOU 2099 CE2 TYR B 308 14168 11559 9415 -389 -906 1101 C
ATOM 2100 CZ TYR B 308 -7.498 35.212 52.025 1.00 93.80 C
ANISOU 2100 CZ TYR B 308 13937 11633 10071 -376 -780 1241 C
ATOM 2101 OH TYR B 308 -6.951 33.951 51.999 1.00 68.08 O
ANISOU 2101 OH TYR B 308 10622 8303 6944 -387 -894 1568 O
ATOM 2102 N THR B 309 -12.016 41.074 52.530 1.00 67.70 N
ANISOU 2102 N THR B 309 10674 8289 6761 -158 382 -591 N
ATOM 2103 CA THR B 309 -12.635 42.309 52.997 1.00 78.73 C
ANISOU 2103 CA THR B 309 12121 9607 8186 -122 546 -1006 C
ATOM 2104 C THR B 309 -13.280 42.010 54.341 1.00 89.88 C
ANISOU 2104 C THR B 309 13862 11162 9125 -250 936 -1189 C
ATOM 2105 O THR B 309 -13.012 42.692 55.339 1.00 82.47 O
ANISOU 2105 O THR B 309 13234 10271 7830 -335 915 -1437 O
ATOM 2106 CB THR B 309 -13.685 42.857 52.012 1.00 76.34 C
ANISOU 2106 CB THR B 309 11436 9148 8423 57 709 -1178 C
ATOM 2107 OG1 THR B 309 -13.042 43.251 50.794 1.00 72.14 O
ANISOU 2107 OG1 THR B 309 10703 8478 8229 165 359 -989 O
ATOM 2108 CG2 THR B 309 -14.402 44.062 52.609 1.00 73.72 C
ANISOU 2108 CG2 THR B 309 11131 8696 8184 99 922 -1637 C
ATOM 2109 N PHE B 310 -14.115 40.969 54.354 1.00 83.13 N
ANISOU 2109 N PHE B 310 12950 10370 8266 -283 1316 -1085 N
ATOM 2110 CA PHE B 310 -14.699 40.453 55.592 1.00 82.38 C
ANISOU 2110 CA PHE B 310 13221 10394 7684 -444 1773 -1172 C
ATOM 2111 C PHE B 310 -13.643 40.259 56.680 1.00 78.91 C
ANISOU 2111 C PHE B 310 13330 10110 6543 -570 1504 -990 C
ATOM 2112 O PHE B 310 -13.673 40.922 57.733 1.00 99.35 O
ANISOU 2112 O PHE B 310 16280 12784 8684 -664 1604 -1283 O
ATOM 2113 CB PHE B 310 -15.411 39.121 55.334 1.00 79.87 C
ANISOU 2113 CB PHE B 310 12765 10083 7498 -485 2154 -957 C
ATOM 2114 CG PHE B 310 -16.846 39.262 54.916 1.00 79.94 C
ANISOU 2114 CG PHE B 310 12367 9988 8017 -428 2636 -1315 C
ATOM 2115 CD1 PHE B 310 -17.181 39.780 53.676 1.00 85.21 C
ANISOU 2115 CD1 PHE B 310 12521 10541 9315 -223 2426 -1445 C
ATOM 2116 CD2 PHE B 310 -17.862 38.851 55.759 1.00 81.17 C
ANISOU 2116 CD2 PHE B 310 12659 10150 8030 -578 3300 -1527 C
ATOM 2117 CE1 PHE B 310 -18.506 39.901 53.294 1.00 86.81 C
ANISOU 2117 CE1 PHE B 310 12310 10645 10030 -136 2787 -1802 C
ATOM 2118 CE2 PHE B 310 -19.187 38.967 55.385 1.00 81.85 C
ANISOU 2118 CE2 PHE B 310 12296 10117 8684 -526 3742 -1922 C
ATOM 2119 CZ PHE B 310 -19.511 39.491 54.152 1.00 84.61 C
ANISOU 2119 CZ PHE B 310 12090 10362 9696 -287 3443 -2069 C
ATOM 2120 N ILE B 311 -12.706 39.356 56.405 1.00 75.80 N
ANISOU 2120 N ILE B 311 12978 9748 6074 -562 1135 -537 N
ATOM 2121 CA ILE B 311 -11.686 38.981 57.380 1.00 84.46 C
ANISOU 2121 CA ILE B 311 14567 10981 6545 -639 789 -302 C
ATOM 2122 C ILE B 311 -10.886 40.178 57.902 1.00 88.36 C
ANISOU 2122 C ILE B 311 15232 11528 6811 -643 376 -602 C
ATOM 2123 O ILE B 311 -10.715 40.329 59.114 1.00 93.26 O
ANISOU 2123 O ILE B 311 16353 12313 6768 -739 350 -716 O
ATOM 2124 CB ILE B 311 -10.713 37.940 56.785 1.00 88.01 C
ANISOU 2124 CB ILE B 311 14886 11386 7167 -585 373 189 C
ATOM 2125 CG1 ILE B 311 -11.462 36.647 56.462 1.00 81.42 C
ANISOU 2125 CG1 ILE B 311 13941 10493 6502 -611 804 473 C
ATOM 2126 CG2 ILE B 311 -9.568 37.660 57.745 1.00 86.98 C
ANISOU 2126 CG2 ILE B 311 15208 11369 6471 -612 -122 409 C
ATOM 2127 CD1 ILE B 311 -10.614 35.594 55.787 1.00 71.59 C
ANISOU 2127 CD1 ILE B 311 12495 9164 5542 -561 468 904 C
ATOM 2128 N LEU B 312 -10.412 41.031 56.999 1.00116.83 N
ANISOU 2128 N LEU B 312 18446 14992 10953 -550 75 -748 N
ATOM 2129 CA LEU B 312 -9.569 42.155 57.402 1.00112.65 C
ANISOU 2129 CA LEU B 312 18009 14459 10336 -565 -316 -1053 C
ATOM 2130 C LEU B 312 -10.336 43.230 58.166 1.00 92.69 C
ANISOU 2130 C LEU B 312 15648 11953 7616 -625 24 -1582 C
ATOM 2131 O LEU B 312 -9.787 43.852 59.073 1.00 84.50 O
ANISOU 2131 O LEU B 312 14905 11020 6181 -701 -202 -1862 O
ATOM 2132 CB LEU B 312 -8.886 42.782 56.187 1.00 84.25 C
ANISOU 2132 CB LEU B 312 13958 10642 7413 -475 -630 -1051 C
ATOM 2133 CG LEU B 312 -7.786 41.946 55.533 1.00 83.51 C
ANISOU 2133 CG LEU B 312 13695 10513 7524 -451 -1045 -647 C
ATOM 2134 CD1 LEU B 312 -7.167 42.702 54.372 1.00112.45 C
ANISOU 2134 CD1 LEU B 312 16964 13943 11819 -405 -1239 -704 C
ATOM 2135 CD2 LEU B 312 -6.728 41.557 56.550 1.00 83.30 C
ANISOU 2135 CD2 LEU B 312 13996 10637 7019 -506 -1510 -566 C
ATOM 2136 N LEU B 313 -11.593 43.463 57.802 1.00 81.00 N
ANISOU 2136 N LEU B 313 13951 10368 6458 -589 548 -1769 N
ATOM 2137 CA LEU B 313 -12.395 44.428 58.546 1.00 87.82 C
ANISOU 2137 CA LEU B 313 14933 11222 7212 -651 936 -2312 C
ATOM 2138 C LEU B 313 -12.636 43.918 59.966 1.00 93.55 C
ANISOU 2138 C LEU B 313 16245 12211 7089 -833 1215 -2385 C
ATOM 2139 O LEU B 313 -12.484 44.670 60.943 1.00107.66 O
ANISOU 2139 O LEU B 313 18350 14104 8451 -939 1219 -2793 O
ATOM 2140 CB LEU B 313 -13.719 44.710 57.831 1.00 89.84 C
ANISOU 2140 CB LEU B 313 14774 11284 8078 -548 1412 -2506 C
ATOM 2141 CG LEU B 313 -13.625 45.635 56.611 1.00 88.63 C
ANISOU 2141 CG LEU B 313 14146 10844 8686 -359 1169 -2563 C
ATOM 2142 CD1 LEU B 313 -14.989 45.823 55.964 1.00101.78 C
ANISOU 2142 CD1 LEU B 313 15417 12335 10918 -218 1565 -2743 C
ATOM 2143 CD2 LEU B 313 -13.024 46.979 56.994 1.00 87.41 C
ANISOU 2143 CD2 LEU B 313 14056 10567 8590 -380 952 -2944 C
ATOM 2144 N ARG B 314 -12.987 42.639 60.083 1.00 92.89 N
ANISOU 2144 N ARG B 314 16332 12223 6739 -879 1458 -1990 N
ATOM 2145 CA ARG B 314 -13.168 42.052 61.408 1.00 91.35 C
ANISOU 2145 CA ARG B 314 16784 12256 5668 -1057 1741 -1950 C
ATOM 2146 C ARG B 314 -11.887 42.153 62.231 1.00 93.99 C
ANISOU 2146 C ARG B 314 17588 12796 5327 -1091 1108 -1868 C
ATOM 2147 O ARG B 314 -11.921 42.543 63.397 1.00124.25 O
ANISOU 2147 O ARG B 314 21776 16821 8611 -1188 1184 -2129 O
ATOM 2148 CB ARG B 314 -13.612 40.591 61.310 1.00 90.43 C
ANISOU 2148 CB ARG B 314 16768 12141 5450 -1092 2066 -1453 C
ATOM 2149 CG ARG B 314 -13.775 39.904 62.665 1.00116.82 C
ANISOU 2149 CG ARG B 314 20721 15674 7991 -1245 2334 -1279 C
ATOM 2150 CD ARG B 314 -14.658 40.725 63.599 1.00111.15 C
ANISOU 2150 CD ARG B 314 20082 15026 7124 -1364 2841 -1816 C
ATOM 2151 NE ARG B 314 -14.730 40.160 64.944 1.00141.16 N
ANISOU 2151 NE ARG B 314 24368 19018 10247 -1474 2997 -1625 N
ATOM 2152 CZ ARG B 314 -15.374 40.727 65.961 1.00154.85 C
ANISOU 2152 CZ ARG B 314 26287 20857 11694 -1599 3408 -2022 C
ATOM 2153 NH1 ARG B 314 -15.385 40.137 67.149 1.00140.34 N
ANISOU 2153 NH1 ARG B 314 24947 19197 9180 -1696 3536 -1798 N
ATOM 2154 NH2 ARG B 314 -16.005 41.882 65.794 1.00166.09 N
ANISOU 2154 NH2 ARG B 314 27393 22188 13525 -1619 3691 -2641 N
ATOM 2155 N THR B 315 -10.760 41.812 61.614 1.00 91.52 N
ANISOU 2155 N THR B 315 17084 12441 5249 -968 447 -1502 N
ATOM 2156 CA THR B 315 -9.469 41.835 62.298 1.00107.95 C
ANISOU 2156 CA THR B 315 19510 14691 6816 -965 -253 -1426 C
ATOM 2157 C THR B 315 -9.085 43.238 62.765 1.00109.24 C
ANISOU 2157 C THR B 315 19688 14900 6917 -1010 -481 -2045 C
ATOM 2158 O THR B 315 -8.583 43.422 63.875 1.00100.62 O
ANISOU 2158 O THR B 315 18839 14054 5339 -1032 -745 -2166 O
ATOM 2159 CB THR B 315 -8.350 41.288 61.389 1.00109.33 C
ANISOU 2159 CB THR B 315 19321 14742 7478 -824 -877 -1004 C
ATOM 2160 OG1 THR B 315 -8.750 40.023 60.849 1.00133.98 O
ANISOU 2160 OG1 THR B 315 22348 17781 10775 -786 -627 -488 O
ATOM 2161 CG2 THR B 315 -7.053 41.115 62.167 1.00109.46 C
ANISOU 2161 CG2 THR B 315 19626 14926 7039 -792 -1615 -896 C
ATOM 2162 N TRP B 316 -9.327 44.224 61.908 1.00108.11 N
ANISOU 2162 N TRP B 316 19012 14515 7550 -957 -362 -2371 N
ATOM 2163 CA TRP B 316 -8.984 45.609 62.204 1.00117.52 C
ANISOU 2163 CA TRP B 316 20124 15658 8869 -996 -529 -2973 C
ATOM 2164 C TRP B 316 -9.943 46.218 63.216 1.00130.61 C
ANISOU 2164 C TRP B 316 22116 17437 10072 -1142 25 -3508 C
ATOM 2165 O TRP B 316 -9.648 47.252 63.817 1.00132.43 O
ANISOU 2165 O TRP B 316 22332 17712 10272 -1185 -104 -4020 O
ATOM 2166 CB TRP B 316 -8.981 46.438 60.922 1.00123.59 C
ANISOU 2166 CB TRP B 316 20253 16066 10639 -884 -531 -3079 C
ATOM 2167 CG TRP B 316 -7.887 46.054 59.968 1.00131.06 C
ANISOU 2167 CG TRP B 316 20881 16883 12033 -786 -1061 -2677 C
ATOM 2168 CD1 TRP B 316 -6.765 45.331 60.255 1.00125.01 C
ANISOU 2168 CD1 TRP B 316 20271 16263 10963 -786 -1623 -2394 C
ATOM 2169 CD2 TRP B 316 -7.815 46.366 58.571 1.00126.87 C
ANISOU 2169 CD2 TRP B 316 19827 16037 12340 -677 -1059 -2530 C
ATOM 2170 NE1 TRP B 316 -5.997 45.179 59.126 1.00114.76 N
ANISOU 2170 NE1 TRP B 316 18535 14750 10320 -706 -1921 -2128 N
ATOM 2171 CE2 TRP B 316 -6.620 45.804 58.078 1.00121.99 C
ANISOU 2171 CE2 TRP B 316 19066 15395 11890 -651 -1564 -2193 C
ATOM 2172 CE3 TRP B 316 -8.644 47.068 57.691 1.00122.02 C
ANISOU 2172 CE3 TRP B 316 18870 15152 12340 -591 -694 -2647 C
ATOM 2173 CZ2 TRP B 316 -6.234 45.923 56.744 1.00115.47 C
ANISOU 2173 CZ2 TRP B 316 17803 14300 11772 -581 -1638 -1988 C
ATOM 2174 CZ3 TRP B 316 -8.259 47.184 56.367 1.00119.56 C
ANISOU 2174 CZ3 TRP B 316 18168 14584 12675 -492 -836 -2391 C
ATOM 2175 CH2 TRP B 316 -7.065 46.614 55.907 1.00120.32 C
ANISOU 2175 CH2 TRP B 316 18165 14678 12872 -507 -1267 -2072 C
ATOM 2176 N SER B 317 -11.098 45.583 63.394 1.00126.72 N
ANISOU 2176 N SER B 317 21729 16990 9429 -1182 668 -3371 N
ATOM 2177 CA SER B 317 -12.030 46.015 64.429 1.00123.56 C
ANISOU 2177 CA SER B 317 21456 16719 8773 -1275 1223 -3768 C
ATOM 2178 C SER B 317 -11.685 45.378 65.777 1.00130.29 C
ANISOU 2178 C SER B 317 22801 17944 8760 -1332 1089 -3554 C
ATOM 2179 O SER B 317 -12.293 45.701 66.798 1.00126.34 O
ANISOU 2179 O SER B 317 22505 17597 7903 -1421 1478 -3866 O
ATOM 2180 CB SER B 317 -13.470 45.677 64.037 1.00119.60 C
ANISOU 2180 CB SER B 317 20755 16054 8632 -1297 2000 -3774 C
ATOM 2181 OG SER B 317 -13.842 46.311 62.824 1.00113.63 O
ANISOU 2181 OG SER B 317 19517 14959 8699 -1203 2107 -3999 O
ATOM 2182 N ARG B 318 -10.706 44.479 65.775 1.00145.55 N
ANISOU 2182 N ARG B 318 24912 20002 10388 -1266 528 -3021 N
ATOM 2183 CA ARG B 318 -10.285 43.803 66.998 1.00146.30 C
ANISOU 2183 CA ARG B 318 25466 20427 9695 -1278 319 -2751 C
ATOM 2184 C ARG B 318 -8.804 44.028 67.286 1.00146.39 C
ANISOU 2184 C ARG B 318 25491 20608 9524 -1187 -566 -2754 C
ATOM 2185 O ARG B 318 -8.057 43.078 67.521 1.00161.93 O
ANISOU 2185 O ARG B 318 27627 22693 11206 -1103 -1014 -2243 O
ATOM 2186 CB ARG B 318 -10.577 42.305 66.906 1.00147.97 C
ANISOU 2186 CB ARG B 318 25868 20614 9740 -1264 514 -2052 C
ATOM 2187 N SER B 323 -2.877 35.548 65.081 1.00164.54 N
ANISOU 2187 N SER B 323 27210 22233 13075 -136 -3864 1540 N
ATOM 2188 CA SER B 323 -2.734 34.704 63.900 1.00171.33 C
ANISOU 2188 CA SER B 323 27664 22778 14656 -73 -3831 1876 C
ATOM 2189 C SER B 323 -2.451 35.540 62.654 1.00149.09 C
ANISOU 2189 C SER B 323 24327 19791 12530 -120 -3938 1518 C
ATOM 2190 O SER B 323 -2.241 34.999 61.568 1.00135.74 O
ANISOU 2190 O SER B 323 22241 17853 11482 -85 -3948 1716 O
ATOM 2191 CB SER B 323 -3.994 33.861 63.694 1.00171.21 C
ANISOU 2191 CB SER B 323 27831 22658 14564 -159 -3072 2216 C
ATOM 2192 OG SER B 323 -4.356 33.181 64.884 1.00172.21 O
ANISOU 2192 OG SER B 323 28477 22928 14027 -152 -2886 2523 O
ATOM 2193 N THR B 324 -2.436 36.861 62.827 1.00124.10 N
ANISOU 2193 N THR B 324 20217 16898 10039 1321 77 -477 N
ATOM 2194 CA THR B 324 -2.239 37.802 61.725 1.00116.55 C
ANISOU 2194 CA THR B 324 19253 15641 9392 998 -29 -750 C
ATOM 2195 C THR B 324 -0.928 37.578 60.979 1.00121.75 C
ANISOU 2195 C THR B 324 19517 16470 10271 642 -414 -757 C
ATOM 2196 O THR B 324 -0.792 37.974 59.821 1.00122.59 O
ANISOU 2196 O THR B 324 19469 16353 10758 414 -440 -848 O
ATOM 2197 CB THR B 324 -2.264 39.258 62.218 1.00109.99 C
ANISOU 2197 CB THR B 324 18977 14628 8187 841 -100 -1180 C
ATOM 2198 OG1 THR B 324 -1.180 39.477 63.130 1.00111.20 O
ANISOU 2198 OG1 THR B 324 19304 15106 7842 650 -498 -1354 O
ATOM 2199 CG2 THR B 324 -3.580 39.563 62.925 1.00111.90 C
ANISOU 2199 CG2 THR B 324 19620 14666 8230 1204 333 -1201 C
ATOM 2200 N LYS B 325 0.034 36.948 61.647 1.00118.83 N
ANISOU 2200 N LYS B 325 18987 16498 9666 603 -704 -645 N
ATOM 2201 CA LYS B 325 1.333 36.663 61.046 1.00121.89 C
ANISOU 2201 CA LYS B 325 18956 17075 10281 292 -1056 -626 C
ATOM 2202 C LYS B 325 1.197 35.780 59.805 1.00100.98 C
ANISOU 2202 C LYS B 325 15810 14327 8229 339 -879 -378 C
ATOM 2203 O LYS B 325 1.759 36.083 58.755 1.00100.33 O
ANISOU 2203 O LYS B 325 15517 14140 8462 52 -979 -482 O
ATOM 2204 CB LYS B 325 2.251 36.006 62.076 1.00124.27 C
ANISOU 2204 CB LYS B 325 19145 17823 10248 318 -1379 -483 C
ATOM 2205 CG LYS B 325 2.548 36.916 63.262 1.00131.88 C
ANISOU 2205 CG LYS B 325 20617 18912 10580 214 -1640 -774 C
ATOM 2206 CD LYS B 325 2.643 36.153 64.567 1.00131.67 C
ANISOU 2206 CD LYS B 325 20683 19264 10082 476 -1736 -547 C
ATOM 2207 CE LYS B 325 2.756 37.113 65.741 1.00141.88 C
ANISOU 2207 CE LYS B 325 22577 20646 10683 401 -1951 -878 C
ATOM 2208 NZ LYS B 325 2.834 36.421 67.058 1.00156.28 N
ANISOU 2208 NZ LYS B 325 24561 22859 11959 659 -2054 -654 N
ATOM 2209 N THR B 326 0.438 34.696 59.928 1.00100.38 N
ANISOU 2209 N THR B 326 15563 14273 8304 697 -603 -55 N
ATOM 2210 CA THR B 326 0.195 33.797 58.805 1.00 99.13 C
ANISOU 2210 CA THR B 326 14968 13996 8702 770 -425 162 C
ATOM 2211 C THR B 326 -0.778 34.418 57.803 1.00 95.57 C
ANISOU 2211 C THR B 326 14647 13131 8533 749 -177 38 C
ATOM 2212 O THR B 326 -0.590 34.331 56.579 1.00 90.20 O
ANISOU 2212 O THR B 326 13722 12317 8235 586 -176 21 O
ATOM 2213 CB THR B 326 -0.368 32.446 59.287 1.00 99.10 C
ANISOU 2213 CB THR B 326 14745 14105 8805 1157 -212 550 C
ATOM 2214 OG1 THR B 326 0.558 31.831 60.191 1.00130.01 O
ANISOU 2214 OG1 THR B 326 18522 18406 12469 1187 -464 709 O
ATOM 2215 CG2 THR B 326 -0.608 31.512 58.111 1.00 93.65 C
ANISOU 2215 CG2 THR B 326 13617 13262 8703 1216 -52 734 C
ATOM 2216 N LEU B 327 -1.815 35.053 58.340 1.00 93.70 N
ANISOU 2216 N LEU B 327 14807 12698 8096 922 35 -43 N
ATOM 2217 CA LEU B 327 -2.872 35.650 57.532 1.00 99.56 C
ANISOU 2217 CA LEU B 327 15684 13035 9108 955 273 -124 C
ATOM 2218 C LEU B 327 -2.341 36.686 56.549 1.00101.23 C
ANISOU 2218 C LEU B 327 15967 13066 9428 575 96 -394 C
ATOM 2219 O LEU B 327 -2.742 36.708 55.386 1.00 98.38 O
ANISOU 2219 O LEU B 327 15474 12468 9440 521 187 -365 O
ATOM 2220 CB LEU B 327 -3.931 36.288 58.437 1.00 95.67 C
ANISOU 2220 CB LEU B 327 15627 12378 8345 1195 520 -196 C
ATOM 2221 CG LEU B 327 -5.048 37.073 57.745 1.00 92.71 C
ANISOU 2221 CG LEU B 327 15427 11563 8235 1243 752 -291 C
ATOM 2222 CD1 LEU B 327 -5.809 36.192 56.769 1.00108.95 C
ANISOU 2222 CD1 LEU B 327 17111 13455 10829 1396 930 -24 C
ATOM 2223 CD2 LEU B 327 -5.992 37.675 58.775 1.00 88.04 C
ANISOU 2223 CD2 LEU B 327 15255 10835 7362 1503 1021 -368 C
ATOM 2224 N LYS B 328 -1.437 37.540 57.020 1.00 98.59 N
ANISOU 2224 N LYS B 328 15849 12844 8767 307 -169 -648 N
ATOM 2225 CA LYS B 328 -0.838 38.567 56.175 1.00101.73 C
ANISOU 2225 CA LYS B 328 16316 13074 9264 -80 -341 -891 C
ATOM 2226 C LYS B 328 -0.037 37.946 55.032 1.00 91.29 C
ANISOU 2226 C LYS B 328 14542 11851 8294 -279 -440 -775 C
ATOM 2227 O LYS B 328 -0.032 38.459 53.910 1.00 93.21 O
ANISOU 2227 O LYS B 328 14766 11871 8777 -482 -418 -846 O
ATOM 2228 CB LYS B 328 0.058 39.488 57.006 1.00 91.71 C
ANISOU 2228 CB LYS B 328 15323 11925 7597 -339 -638 -1175 C
ATOM 2229 N VAL B 329 0.639 36.841 55.328 1.00 90.15 N
ANISOU 2229 N VAL B 329 14045 12039 8171 -208 -535 -587 N
ATOM 2230 CA VAL B 329 1.377 36.088 54.320 1.00 90.59 C
ANISOU 2230 CA VAL B 329 13647 12200 8571 -338 -577 -465 C
ATOM 2231 C VAL B 329 0.432 35.567 53.241 1.00 83.44 C
ANISOU 2231 C VAL B 329 12618 11051 8033 -177 -308 -328 C
ATOM 2232 O VAL B 329 0.681 35.742 52.042 1.00 76.38 O
ANISOU 2232 O VAL B 329 11610 10035 7376 -379 -295 -376 O
ATOM 2233 CB VAL B 329 2.144 34.905 54.952 1.00 87.39 C
ANISOU 2233 CB VAL B 329 12881 12169 8153 -219 -700 -256 C
ATOM 2234 CG1 VAL B 329 2.554 33.893 53.893 1.00 79.39 C
ANISOU 2234 CG1 VAL B 329 11398 11201 7565 -226 -623 -93 C
ATOM 2235 CG2 VAL B 329 3.354 35.406 55.725 1.00 90.15 C
ANISOU 2235 CG2 VAL B 329 13254 12782 8216 -469 -1054 -395 C
ATOM 2236 N VAL B 330 -0.656 34.935 53.676 1.00 84.79 N
ANISOU 2236 N VAL B 330 12819 11152 8245 181 -99 -152 N
ATOM 2237 CA VAL B 330 -1.660 34.414 52.748 1.00 85.44 C
ANISOU 2237 CA VAL B 330 12784 10987 8691 347 124 -20 C
ATOM 2238 C VAL B 330 -2.238 35.524 51.864 1.00 85.09 C
ANISOU 2238 C VAL B 330 13005 10600 8725 192 167 -185 C
ATOM 2239 O VAL B 330 -2.347 35.365 50.644 1.00 71.75 O
ANISOU 2239 O VAL B 330 11183 8772 7306 99 199 -165 O
ATOM 2240 CB VAL B 330 -2.805 33.708 53.499 1.00 81.66 C
ANISOU 2240 CB VAL B 330 12317 10458 8254 747 347 196 C
ATOM 2241 CG1 VAL B 330 -3.862 33.224 52.519 1.00 79.56 C
ANISOU 2241 CG1 VAL B 330 11914 9910 8405 890 533 318 C
ATOM 2242 CG2 VAL B 330 -2.260 32.547 54.321 1.00 84.57 C
ANISOU 2242 CG2 VAL B 330 12415 11150 8570 914 311 410 C
ATOM 2243 N VAL B 331 -2.592 36.646 52.487 1.00 89.70 N
ANISOU 2243 N VAL B 331 13977 11045 9059 167 165 -347 N
ATOM 2244 CA VAL B 331 -3.100 37.811 51.766 1.00104.92 C
ANISOU 2244 CA VAL B 331 16181 12628 11056 22 191 -496 C
ATOM 2245 C VAL B 331 -2.093 38.290 50.722 1.00107.57 C
ANISOU 2245 C VAL B 331 16443 12971 11458 -368 24 -612 C
ATOM 2246 O VAL B 331 -2.459 38.596 49.583 1.00 98.39 O
ANISOU 2246 O VAL B 331 15303 11578 10502 -461 68 -600 O
ATOM 2247 CB VAL B 331 -3.430 38.971 52.733 1.00 86.76 C
ANISOU 2247 CB VAL B 331 14319 10191 8456 38 203 -691 C
ATOM 2248 CG1 VAL B 331 -3.676 40.260 51.966 1.00 94.39 C
ANISOU 2248 CG1 VAL B 331 15553 10803 9507 -175 182 -857 C
ATOM 2249 CG2 VAL B 331 -4.632 38.619 53.597 1.00 87.43 C
ANISOU 2249 CG2 VAL B 331 14511 10198 8512 443 453 -566 C
ATOM 2250 N ALA B 332 -0.822 38.336 51.115 1.00 99.42 N
ANISOU 2250 N ALA B 332 15312 12210 10254 -592 -168 -704 N
ATOM 2251 CA ALA B 332 0.250 38.762 50.221 1.00 91.22 C
ANISOU 2251 CA ALA B 332 14161 11207 9292 -972 -302 -796 C
ATOM 2252 C ALA B 332 0.359 37.841 49.008 1.00101.51 C
ANISOU 2252 C ALA B 332 15132 12548 10888 -967 -205 -643 C
ATOM 2253 O ALA B 332 0.502 38.307 47.875 1.00 88.52 O
ANISOU 2253 O ALA B 332 13519 10754 9360 -1182 -184 -678 O
ATOM 2254 CB ALA B 332 1.575 38.814 50.969 1.00 72.24 C
ANISOU 2254 CB ALA B 332 11634 9111 6703 -1180 -535 -888 C
ATOM 2255 N VAL B 333 0.285 36.535 49.249 1.00 90.12 N
ANISOU 2255 N VAL B 333 13393 11296 9554 -719 -139 -473 N
ATOM 2256 CA VAL B 333 0.331 35.558 48.165 1.00 82.62 C
ANISOU 2256 CA VAL B 333 12142 10366 8884 -680 -36 -355 C
ATOM 2257 C VAL B 333 -0.853 35.734 47.209 1.00 81.09 C
ANISOU 2257 C VAL B 333 12112 9847 8850 -594 90 -323 C
ATOM 2258 O VAL B 333 -0.675 35.783 45.983 1.00 92.38 O
ANISOU 2258 O VAL B 333 13508 11198 10396 -758 116 -342 O
ATOM 2259 CB VAL B 333 0.348 34.114 48.709 1.00 90.88 C
ANISOU 2259 CB VAL B 333 12855 11623 10051 -396 17 -172 C
ATOM 2260 CG1 VAL B 333 0.119 33.113 47.586 1.00 92.12 C
ANISOU 2260 CG1 VAL B 333 12763 11717 10521 -313 147 -80 C
ATOM 2261 CG2 VAL B 333 1.663 33.833 49.427 1.00 90.15 C
ANISOU 2261 CG2 VAL B 333 12530 11870 9853 -504 -141 -171 C
ATOM 2262 N VAL B 334 -2.054 35.838 47.775 1.00 77.00 N
ANISOU 2262 N VAL B 334 11774 9149 8335 -335 168 -265 N
ATOM 2263 CA VAL B 334 -3.265 36.048 46.984 1.00 75.08 C
ANISOU 2263 CA VAL B 334 11670 8583 8275 -233 253 -214 C
ATOM 2264 C VAL B 334 -3.141 37.283 46.095 1.00 80.94 C
ANISOU 2264 C VAL B 334 12674 9120 8959 -521 185 -335 C
ATOM 2265 O VAL B 334 -3.440 37.231 44.902 1.00 74.98 O
ANISOU 2265 O VAL B 334 11918 8226 8345 -587 191 -296 O
ATOM 2266 CB VAL B 334 -4.513 36.199 47.881 1.00 78.38 C
ANISOU 2266 CB VAL B 334 12250 8825 8707 72 362 -142 C
ATOM 2267 CG1 VAL B 334 -5.710 36.660 47.061 1.00 84.27 C
ANISOU 2267 CG1 VAL B 334 13147 9211 9663 139 408 -98 C
ATOM 2268 CG2 VAL B 334 -4.821 34.890 48.588 1.00 73.95 C
ANISOU 2268 CG2 VAL B 334 11419 8418 8262 378 467 38 C
ATOM 2269 N ALA B 335 -2.687 38.386 46.681 1.00 98.88 N
ANISOU 2269 N ALA B 335 15183 11371 11016 -697 109 -479 N
ATOM 2270 CA ALA B 335 -2.491 39.625 45.934 1.00109.02 C
ANISOU 2270 CA ALA B 335 16721 12443 12258 -988 47 -580 C
ATOM 2271 C ALA B 335 -1.469 39.440 44.814 1.00107.29 C
ANISOU 2271 C ALA B 335 16331 12360 12077 -1276 15 -580 C
ATOM 2272 O ALA B 335 -1.676 39.898 43.684 1.00110.90 O
ANISOU 2272 O ALA B 335 16912 12632 12594 -1415 26 -550 O
ATOM 2273 CB ALA B 335 -2.056 40.745 46.870 1.00 85.24 C
ANISOU 2273 CB ALA B 335 13964 9394 9028 -1139 -40 -759 C
ATOM 2274 N SER B 336 -0.374 38.754 45.132 1.00103.00 N
ANISOU 2274 N SER B 336 15498 12139 11496 -1352 -15 -597 N
ATOM 2275 CA SER B 336 0.694 38.518 44.165 1.00 92.10 C
ANISOU 2275 CA SER B 336 13913 10912 10167 -1608 1 -598 C
ATOM 2276 C SER B 336 0.197 37.724 42.961 1.00 92.85 C
ANISOU 2276 C SER B 336 13915 10950 10414 -1505 116 -498 C
ATOM 2277 O SER B 336 0.638 37.961 41.833 1.00 80.07 O
ANISOU 2277 O SER B 336 12322 9309 8794 -1726 163 -503 O
ATOM 2278 CB SER B 336 1.864 37.785 44.825 1.00 88.95 C
ANISOU 2278 CB SER B 336 13166 10868 9763 -1644 -46 -608 C
ATOM 2279 OG SER B 336 1.514 36.448 45.141 1.00112.37 O
ANISOU 2279 OG SER B 336 15880 13970 12844 -1329 19 -494 O
ATOM 2280 N PHE B 337 -0.718 36.786 43.205 1.00 83.32 N
ANISOU 2280 N PHE B 337 12611 9716 9332 -1178 161 -408 N
ATOM 2281 CA PHE B 337 -1.332 36.020 42.120 1.00 81.83 C
ANISOU 2281 CA PHE B 337 12357 9435 9298 -1068 228 -336 C
ATOM 2282 C PHE B 337 -1.904 36.941 41.042 1.00 86.86 C
ANISOU 2282 C PHE B 337 13308 9804 9892 -1211 196 -333 C
ATOM 2283 O PHE B 337 -1.540 36.844 39.867 1.00 95.58 O
ANISOU 2283 O PHE B 337 14423 10925 10968 -1373 233 -340 O
ATOM 2284 CB PHE B 337 -2.433 35.104 42.663 1.00 77.40 C
ANISOU 2284 CB PHE B 337 11687 8804 8917 -703 256 -231 C
ATOM 2285 CG PHE B 337 -3.149 34.309 41.600 1.00 80.73 C
ANISOU 2285 CG PHE B 337 12045 9101 9529 -593 279 -176 C
ATOM 2286 CD1 PHE B 337 -2.675 33.067 41.208 1.00 89.29 C
ANISOU 2286 CD1 PHE B 337 12839 10345 10743 -535 347 -177 C
ATOM 2287 CD2 PHE B 337 -4.303 34.798 41.005 1.00 75.62 C
ANISOU 2287 CD2 PHE B 337 11625 8162 8946 -543 217 -129 C
ATOM 2288 CE1 PHE B 337 -3.332 32.332 40.236 1.00 82.29 C
ANISOU 2288 CE1 PHE B 337 11920 9327 10020 -446 346 -164 C
ATOM 2289 CE2 PHE B 337 -4.962 34.068 40.031 1.00 74.71 C
ANISOU 2289 CE2 PHE B 337 11458 7933 8996 -458 187 -91 C
ATOM 2290 CZ PHE B 337 -4.476 32.833 39.648 1.00 80.54 C
ANISOU 2290 CZ PHE B 337 11935 8831 9836 -416 248 -125 C
ATOM 2291 N PHE B 338 -2.793 37.839 41.452 1.00 68.44 N
ANISOU 2291 N PHE B 338 11237 7221 7546 -1143 138 -314 N
ATOM 2292 CA PHE B 338 -3.462 38.732 40.514 1.00 69.36 C
ANISOU 2292 CA PHE B 338 11649 7049 7655 -1241 84 -272 C
ATOM 2293 C PHE B 338 -2.506 39.769 39.935 1.00 69.65 C
ANISOU 2293 C PHE B 338 11856 7084 7526 -1609 74 -327 C
ATOM 2294 O PHE B 338 -2.599 40.116 38.752 1.00 71.51 O
ANISOU 2294 O PHE B 338 12248 7206 7719 -1754 63 -269 O
ATOM 2295 CB PHE B 338 -4.645 39.423 41.192 1.00 78.95 C
ANISOU 2295 CB PHE B 338 13067 7978 8951 -1046 48 -230 C
ATOM 2296 CG PHE B 338 -5.689 38.470 41.692 1.00 93.01 C
ANISOU 2296 CG PHE B 338 14678 9723 10939 -687 85 -139 C
ATOM 2297 CD1 PHE B 338 -6.533 37.825 40.804 1.00 75.85 C
ANISOU 2297 CD1 PHE B 338 12435 7431 8955 -563 41 -33 C
ATOM 2298 CD2 PHE B 338 -5.823 38.213 43.046 1.00 85.14 C
ANISOU 2298 CD2 PHE B 338 13594 8809 9945 -483 160 -151 C
ATOM 2299 CE1 PHE B 338 -7.493 36.942 41.255 1.00 86.21 C
ANISOU 2299 CE1 PHE B 338 13557 8687 10514 -251 75 64 C
ATOM 2300 CE2 PHE B 338 -6.783 37.331 43.505 1.00 62.23 C
ANISOU 2300 CE2 PHE B 338 10521 5865 7256 -158 229 -33 C
ATOM 2301 CZ PHE B 338 -7.618 36.694 42.608 1.00 59.47 C
ANISOU 2301 CZ PHE B 338 10067 5377 7153 -47 188 77 C
ATOM 2302 N ILE B 339 -1.591 40.258 40.767 1.00 70.08 N
ANISOU 2302 N ILE B 339 11880 7262 7485 -1766 69 -429 N
ATOM 2303 CA ILE B 339 -0.589 41.216 40.314 1.00 76.64 C
ANISOU 2303 CA ILE B 339 12820 8091 8209 -2139 66 -477 C
ATOM 2304 C ILE B 339 0.234 40.656 39.158 1.00 93.03 C
ANISOU 2304 C ILE B 339 14732 10355 10258 -2314 170 -439 C
ATOM 2305 O ILE B 339 0.437 41.327 38.144 1.00 89.01 O
ANISOU 2305 O ILE B 339 14405 9735 9678 -2543 205 -386 O
ATOM 2306 CB ILE B 339 0.359 41.622 41.461 1.00 73.09 C
ANISOU 2306 CB ILE B 339 12289 7787 7694 -2282 10 -608 C
ATOM 2307 CG1 ILE B 339 -0.380 42.487 42.482 1.00 71.47 C
ANISOU 2307 CG1 ILE B 339 12354 7346 7455 -2173 -73 -683 C
ATOM 2308 CG2 ILE B 339 1.571 42.370 40.921 1.00 73.61 C
ANISOU 2308 CG2 ILE B 339 12354 7898 7717 -2691 20 -643 C
ATOM 2309 CD1 ILE B 339 0.376 42.660 43.778 1.00 77.13 C
ANISOU 2309 CD1 ILE B 339 13005 8233 8067 -2239 -162 -834 C
ATOM 2310 N PHE B 340 0.692 39.418 39.302 1.00 84.51 N
ANISOU 2310 N PHE B 340 13321 9551 9239 -2192 239 -458 N
ATOM 2311 CA PHE B 340 1.567 38.832 38.294 1.00 86.96 C
ANISOU 2311 CA PHE B 340 13455 10052 9534 -2338 382 -452 C
ATOM 2312 C PHE B 340 0.808 38.119 37.175 1.00 76.48 C
ANISOU 2312 C PHE B 340 12200 8652 8207 -2194 434 -398 C
ATOM 2313 O PHE B 340 1.399 37.775 36.155 1.00 79.17 O
ANISOU 2313 O PHE B 340 12496 9104 8482 -2321 572 -404 O
ATOM 2314 CB PHE B 340 2.565 37.876 38.953 1.00 85.27 C
ANISOU 2314 CB PHE B 340 12826 10157 9415 -2294 439 -503 C
ATOM 2315 CG PHE B 340 3.575 38.571 39.825 1.00109.49 C
ANISOU 2315 CG PHE B 340 15796 13339 12467 -2514 365 -561 C
ATOM 2316 CD1 PHE B 340 4.469 39.477 39.279 1.00 97.51 C
ANISOU 2316 CD1 PHE B 340 14331 11811 10907 -2876 414 -571 C
ATOM 2317 CD2 PHE B 340 3.628 38.323 41.186 1.00 98.04 C
ANISOU 2317 CD2 PHE B 340 14207 12002 11041 -2369 237 -598 C
ATOM 2318 CE1 PHE B 340 5.397 40.124 40.075 1.00 97.69 C
ANISOU 2318 CE1 PHE B 340 14246 11919 10951 -3103 310 -635 C
ATOM 2319 CE2 PHE B 340 4.555 38.966 41.988 1.00 93.60 C
ANISOU 2319 CE2 PHE B 340 13571 11546 10445 -2586 118 -670 C
ATOM 2320 CZ PHE B 340 5.441 39.868 41.430 1.00107.48 C
ANISOU 2320 CZ PHE B 340 15359 13277 12201 -2961 141 -698 C
ATOM 2321 N TRP B 341 -0.495 37.911 37.345 1.00 75.91 N
ANISOU 2321 N TRP B 341 12243 8389 8211 -1934 325 -351 N
ATOM 2322 CA TRP B 341 -1.284 37.306 36.271 1.00 76.65 C
ANISOU 2322 CA TRP B 341 12424 8387 8314 -1818 311 -309 C
ATOM 2323 C TRP B 341 -2.018 38.331 35.413 1.00 80.20 C
ANISOU 2323 C TRP B 341 13256 8566 8650 -1925 206 -216 C
ATOM 2324 O TRP B 341 -2.471 38.006 34.315 1.00 73.93 O
ANISOU 2324 O TRP B 341 12587 7714 7789 -1911 172 -180 O
ATOM 2325 CB TRP B 341 -2.294 36.301 36.834 1.00 98.07 C
ANISOU 2325 CB TRP B 341 14976 11046 11240 -1470 244 -288 C
ATOM 2326 CG TRP B 341 -1.732 34.924 36.967 1.00 81.30 C
ANISOU 2326 CG TRP B 341 12504 9154 9231 -1349 356 -350 C
ATOM 2327 CD1 TRP B 341 -1.427 34.274 38.123 1.00 81.18 C
ANISOU 2327 CD1 TRP B 341 12198 9291 9354 -1190 392 -353 C
ATOM 2328 CD2 TRP B 341 -1.384 34.031 35.900 1.00 93.74 C
ANISOU 2328 CD2 TRP B 341 13998 10826 10792 -1373 453 -416 C
ATOM 2329 NE1 TRP B 341 -0.917 33.029 37.847 1.00 89.89 N
ANISOU 2329 NE1 TRP B 341 13019 10561 10574 -1107 502 -398 N
ATOM 2330 CE2 TRP B 341 -0.881 32.855 36.489 1.00 89.54 C
ANISOU 2330 CE2 TRP B 341 13100 10479 10443 -1215 553 -457 C
ATOM 2331 CE3 TRP B 341 -1.455 34.110 34.505 1.00111.42 C
ANISOU 2331 CE3 TRP B 341 16460 13009 12864 -1504 469 -445 C
ATOM 2332 CZ2 TRP B 341 -0.446 31.768 35.733 1.00111.62 C
ANISOU 2332 CZ2 TRP B 341 15734 13379 13298 -1180 684 -547 C
ATOM 2333 CZ3 TRP B 341 -1.026 33.027 33.756 1.00 88.76 C
ANISOU 2333 CZ3 TRP B 341 13457 10265 10002 -1474 600 -551 C
ATOM 2334 CH2 TRP B 341 -0.529 31.873 34.372 1.00 89.14 C
ANISOU 2334 CH2 TRP B 341 13127 10470 10271 -1311 714 -611 C
ATOM 2335 N LEU B 342 -2.130 39.562 35.908 1.00108.16 N
ANISOU 2335 N LEU B 342 16992 11935 12171 -2029 142 -178 N
ATOM 2336 CA LEU B 342 -2.887 40.604 35.210 1.00 77.04 C
ANISOU 2336 CA LEU B 342 13406 7696 8170 -2104 28 -58 C
ATOM 2337 C LEU B 342 -2.440 40.863 33.755 1.00 77.02 C
ANISOU 2337 C LEU B 342 13598 7719 7948 -2349 79 11 C
ATOM 2338 O LEU B 342 -3.281 40.845 32.847 1.00 82.15 O
ANISOU 2338 O LEU B 342 14447 8222 8544 -2287 -39 112 O
ATOM 2339 CB LEU B 342 -2.839 41.912 36.011 1.00 72.89 C
ANISOU 2339 CB LEU B 342 13046 6980 7670 -2211 -9 -58 C
ATOM 2340 CG LEU B 342 -3.605 43.101 35.426 1.00 72.70 C
ANISOU 2340 CG LEU B 342 13381 6604 7639 -2277 -122 83 C
ATOM 2341 CD1 LEU B 342 -5.086 42.780 35.307 1.00 67.14 C
ANISOU 2341 CD1 LEU B 342 12724 5691 7096 -1970 -267 182 C
ATOM 2342 CD2 LEU B 342 -3.384 44.341 36.276 1.00 64.98 C
ANISOU 2342 CD2 LEU B 342 12549 5436 6705 -2400 -129 36 C
ATOM 2343 N PRO B 343 -1.131 41.097 33.516 1.00 80.60 N
ANISOU 2343 N PRO B 343 13992 8359 8272 -2627 253 -29 N
ATOM 2344 CA PRO B 343 -0.738 41.395 32.131 1.00 75.53 C
ANISOU 2344 CA PRO B 343 13567 7737 7396 -2854 345 62 C
ATOM 2345 C PRO B 343 -1.034 40.257 31.153 1.00 83.09 C
ANISOU 2345 C PRO B 343 14516 8818 8237 -2725 369 32 C
ATOM 2346 O PRO B 343 -1.454 40.516 30.020 1.00 73.94 O
ANISOU 2346 O PRO B 343 13656 7564 6874 -2790 311 138 O
ATOM 2347 CB PRO B 343 0.773 41.632 32.240 1.00 92.93 C
ANISOU 2347 CB PRO B 343 15598 10152 9559 -3138 570 9 C
ATOM 2348 CG PRO B 343 0.986 42.035 33.657 1.00 84.13 C
ANISOU 2348 CG PRO B 343 14321 9008 8635 -3125 496 -72 C
ATOM 2349 CD PRO B 343 0.024 41.192 34.429 1.00 72.54 C
ANISOU 2349 CD PRO B 343 12726 7525 7310 -2764 364 -134 C
ATOM 2350 N TYR B 344 -0.817 39.021 31.596 1.00 89.86 N
ANISOU 2350 N TYR B 344 15048 9874 9220 -2547 440 -111 N
ATOM 2351 CA TYR B 344 -1.112 37.836 30.794 1.00 70.96 C
ANISOU 2351 CA TYR B 344 12622 7573 6766 -2404 457 -186 C
ATOM 2352 C TYR B 344 -2.570 37.838 30.343 1.00 71.40 C
ANISOU 2352 C TYR B 344 12912 7383 6834 -2235 178 -104 C
ATOM 2353 O TYR B 344 -2.866 37.676 29.159 1.00 67.75 O
ANISOU 2353 O TYR B 344 12689 6901 6154 -2278 123 -83 O
ATOM 2354 CB TYR B 344 -0.801 36.565 31.594 1.00 77.48 C
ANISOU 2354 CB TYR B 344 13036 8581 7822 -2199 543 -330 C
ATOM 2355 CG TYR B 344 -1.211 35.266 30.925 1.00 67.94 C
ANISOU 2355 CG TYR B 344 11769 7415 6631 -2020 539 -435 C
ATOM 2356 CD1 TYR B 344 -0.317 34.556 30.131 1.00 66.34 C
ANISOU 2356 CD1 TYR B 344 11500 7414 6292 -2098 778 -557 C
ATOM 2357 CD2 TYR B 344 -2.485 34.740 31.104 1.00 68.24 C
ANISOU 2357 CD2 TYR B 344 11805 7274 6850 -1771 308 -421 C
ATOM 2358 CE1 TYR B 344 -0.686 33.368 29.527 1.00 70.72 C
ANISOU 2358 CE1 TYR B 344 12026 7979 6867 -1936 773 -690 C
ATOM 2359 CE2 TYR B 344 -2.862 33.557 30.500 1.00 69.50 C
ANISOU 2359 CE2 TYR B 344 11910 7442 7057 -1627 278 -535 C
ATOM 2360 CZ TYR B 344 -1.959 32.875 29.714 1.00 74.17 C
ANISOU 2360 CZ TYR B 344 12470 8223 7487 -1711 504 -684 C
ATOM 2361 OH TYR B 344 -2.328 31.694 29.113 1.00100.54 O
ANISOU 2361 OH TYR B 344 15779 11545 10876 -1570 474 -833 O
ATOM 2362 N GLN B 345 -3.473 38.029 31.299 1.00 78.28 N
ANISOU 2362 N GLN B 345 13712 8072 7960 -2042 3 -53 N
ATOM 2363 CA GLN B 345 -4.903 38.029 31.022 1.00 86.22 C
ANISOU 2363 CA GLN B 345 14861 8824 9073 -1860 -269 44 C
ATOM 2364 C GLN B 345 -5.300 39.163 30.082 1.00 76.66 C
ANISOU 2364 C GLN B 345 14049 7420 7657 -2022 -412 217 C
ATOM 2365 O GLN B 345 -6.031 38.944 29.111 1.00 66.16 O
ANISOU 2365 O GLN B 345 12907 6002 6230 -1983 -605 277 O
ATOM 2366 CB GLN B 345 -5.696 38.128 32.329 1.00 66.75 C
ANISOU 2366 CB GLN B 345 12222 6200 6938 -1626 -357 81 C
ATOM 2367 CG GLN B 345 -5.590 36.900 33.224 1.00 63.31 C
ANISOU 2367 CG GLN B 345 11408 5920 6727 -1413 -263 -35 C
ATOM 2368 CD GLN B 345 -6.385 35.718 32.697 1.00 65.11 C
ANISOU 2368 CD GLN B 345 11531 6108 7099 -1224 -386 -65 C
ATOM 2369 OE1 GLN B 345 -7.023 35.804 31.649 1.00 80.47 O
ANISOU 2369 OE1 GLN B 345 13694 7925 8955 -1257 -569 -17 O
ATOM 2370 NE2 GLN B 345 -6.355 34.607 33.427 1.00 67.89 N
ANISOU 2370 NE2 GLN B 345 11552 6561 7683 -1032 -304 -139 N
ATOM 2371 N VAL B 346 -4.817 40.368 30.377 1.00 78.86 N
ANISOU 2371 N VAL B 346 14461 7622 7880 -2207 -337 301 N
ATOM 2372 CA VAL B 346 -5.128 41.538 29.560 1.00 83.85 C
ANISOU 2372 CA VAL B 346 15469 8043 8347 -2368 -455 501 C
ATOM 2373 C VAL B 346 -4.704 41.324 28.106 1.00 82.71 C
ANISOU 2373 C VAL B 346 15558 8041 7826 -2545 -408 537 C
ATOM 2374 O VAL B 346 -5.527 41.423 27.184 1.00 79.71 O
ANISOU 2374 O VAL B 346 15437 7531 7316 -2512 -637 666 O
ATOM 2375 CB VAL B 346 -4.448 42.810 30.116 1.00 84.36 C
ANISOU 2375 CB VAL B 346 15615 8011 8426 -2580 -333 557 C
ATOM 2376 CG1 VAL B 346 -4.623 43.976 29.160 1.00 69.95 C
ANISOU 2376 CG1 VAL B 346 14180 5975 6424 -2773 -418 788 C
ATOM 2377 CG2 VAL B 346 -5.012 43.157 31.485 1.00 96.05 C
ANISOU 2377 CG2 VAL B 346 16960 9310 10226 -2395 -400 518 C
ATOM 2378 N THR B 347 -3.426 41.008 27.910 1.00 87.54 N
ANISOU 2378 N THR B 347 16074 8926 8263 -2725 -112 425 N
ATOM 2379 CA THR B 347 -2.894 40.779 26.570 1.00 83.86 C
ANISOU 2379 CA THR B 347 15831 8624 7408 -2892 17 439 C
ATOM 2380 C THR B 347 -3.605 39.626 25.871 1.00 82.48 C
ANISOU 2380 C THR B 347 15696 8504 7140 -2706 -141 332 C
ATOM 2381 O THR B 347 -3.824 39.672 24.667 1.00 82.79 O
ANISOU 2381 O THR B 347 16069 8548 6840 -2784 -221 404 O
ATOM 2382 CB THR B 347 -1.378 40.487 26.596 1.00 85.43 C
ANISOU 2382 CB THR B 347 15832 9115 7514 -3078 410 315 C
ATOM 2383 OG1 THR B 347 -1.118 39.362 27.445 1.00106.87 O
ANISOU 2383 OG1 THR B 347 18135 11992 10476 -2893 491 99 O
ATOM 2384 CG2 THR B 347 -0.611 41.697 27.108 1.00 90.02 C
ANISOU 2384 CG2 THR B 347 16404 9632 8167 -3322 544 428 C
ATOM 2385 N GLY B 348 -3.968 38.598 26.633 1.00 88.29 N
ANISOU 2385 N GLY B 348 16103 9270 8173 -2465 -196 166 N
ATOM 2386 CA GLY B 348 -4.649 37.444 26.076 1.00 80.70 C
ANISOU 2386 CA GLY B 348 15136 8327 7200 -2289 -359 40 C
ATOM 2387 C GLY B 348 -6.016 37.794 25.519 1.00 86.91 C
ANISOU 2387 C GLY B 348 16184 8859 7979 -2205 -768 198 C
ATOM 2388 O GLY B 348 -6.313 37.505 24.358 1.00 83.33 O
ANISOU 2388 O GLY B 348 16008 8427 7227 -2246 -913 187 O
ATOM 2389 N ILE B 349 -6.847 38.425 26.345 1.00103.25 N
ANISOU 2389 N ILE B 349 18169 10686 10375 -2082 -957 345 N
ATOM 2390 CA ILE B 349 -8.187 38.830 25.924 1.00103.66 C
ANISOU 2390 CA ILE B 349 18408 10466 10512 -1982 -1355 530 C
ATOM 2391 C ILE B 349 -8.146 39.816 24.753 1.00 86.43 C
ANISOU 2391 C ILE B 349 16684 8228 7929 -2195 -1462 737 C
ATOM 2392 O ILE B 349 -8.813 39.614 23.721 1.00 81.61 O
ANISOU 2392 O ILE B 349 16319 7572 7119 -2187 -1753 799 O
ATOM 2393 CB ILE B 349 -8.969 39.452 27.101 1.00 84.62 C
ANISOU 2393 CB ILE B 349 15812 7795 8544 -1810 -1454 657 C
ATOM 2394 CG1 ILE B 349 -9.433 38.352 28.060 1.00 70.68 C
ANISOU 2394 CG1 ILE B 349 13638 6039 7178 -1548 -1450 512 C
ATOM 2395 CG2 ILE B 349 -10.162 40.249 26.592 1.00 80.33 C
ANISOU 2395 CG2 ILE B 349 15497 6948 8075 -1757 -1819 912 C
ATOM 2396 CD1 ILE B 349 -10.463 37.426 27.446 1.00 68.87 C
ANISOU 2396 CD1 ILE B 349 13368 5726 7074 -1398 -1761 489 C
ATOM 2397 N MET B 350 -7.351 40.872 24.913 1.00 89.87 N
ANISOU 2397 N MET B 350 17236 8664 8245 -2392 -1238 851 N
ATOM 2398 CA MET B 350 -7.177 41.851 23.843 1.00 94.31 C
ANISOU 2398 CA MET B 350 18228 9177 8428 -2614 -1279 1082 C
ATOM 2399 C MET B 350 -6.746 41.180 22.540 1.00 87.25 C
ANISOU 2399 C MET B 350 17587 8528 7036 -2730 -1225 998 C
ATOM 2400 O MET B 350 -7.266 41.498 21.474 1.00 87.20 O
ANISOU 2400 O MET B 350 17953 8456 6724 -2785 -1473 1172 O
ATOM 2401 CB MET B 350 -6.156 42.918 24.244 1.00111.27 C
ANISOU 2401 CB MET B 350 20409 11321 10547 -2841 -972 1172 C
ATOM 2402 CG MET B 350 -6.657 43.893 25.304 1.00103.35 C
ANISOU 2402 CG MET B 350 19309 10013 9946 -2765 -1063 1290 C
ATOM 2403 SD MET B 350 -5.402 45.054 25.889 1.00143.97 S
ANISOU 2403 SD MET B 350 24456 15139 15107 -3049 -725 1330 S
ATOM 2404 CE MET B 350 -5.092 46.014 24.412 1.00 90.51 C
ANISOU 2404 CE MET B 350 18172 8315 7904 -3337 -712 1641 C
ATOM 2405 N MET B 351 -5.807 40.241 22.636 1.00 87.49 N
ANISOU 2405 N MET B 351 17422 8837 6984 -2755 -904 733 N
ATOM 2406 CA MET B 351 -5.313 39.515 21.468 1.00 83.17 C
ANISOU 2406 CA MET B 351 17101 8530 5971 -2844 -779 598 C
ATOM 2407 C MET B 351 -6.418 38.685 20.829 1.00 83.65 C
ANISOU 2407 C MET B 351 17285 8527 5971 -2677 -1181 512 C
ATOM 2408 O MET B 351 -6.505 38.583 19.605 1.00100.06 O
ANISOU 2408 O MET B 351 19756 10684 7577 -2766 -1285 528 O
ATOM 2409 CB MET B 351 -4.144 38.611 21.853 1.00 81.84 C
ANISOU 2409 CB MET B 351 16620 8632 5842 -2857 -349 317 C
ATOM 2410 CG MET B 351 -3.184 38.315 20.726 1.00 84.17 C
ANISOU 2410 CG MET B 351 17165 9184 5630 -3030 -24 229 C
ATOM 2411 SD MET B 351 -1.832 37.252 21.255 1.00103.11 S
ANISOU 2411 SD MET B 351 19126 11869 8181 -3011 486 -83 S
ATOM 2412 CE MET B 351 -1.321 38.086 22.755 1.00 81.12 C
ANISOU 2412 CE MET B 351 15942 9013 5867 -3064 601 41 C
ATOM 2413 N SER B 352 -7.261 38.091 21.668 1.00 87.84 N
ANISOU 2413 N SER B 352 17482 8915 6979 -2441 -1408 422 N
ATOM 2414 CA SER B 352 -8.356 37.267 21.175 1.00 88.89 C
ANISOU 2414 CA SER B 352 17660 8954 7162 -2286 -1817 336 C
ATOM 2415 C SER B 352 -9.383 38.117 20.438 1.00 84.59 C
ANISOU 2415 C SER B 352 17464 8198 6478 -2313 -2270 628 C
ATOM 2416 O SER B 352 -10.039 37.632 19.516 1.00 86.81 O
ANISOU 2416 O SER B 352 17971 8467 6545 -2291 -2615 587 O
ATOM 2417 CB SER B 352 -9.024 36.496 22.318 1.00 82.67 C
ANISOU 2417 CB SER B 352 16393 8037 6979 -2032 -1924 219 C
ATOM 2418 OG SER B 352 -9.667 37.364 23.233 1.00 84.43 O
ANISOU 2418 OG SER B 352 16459 8024 7596 -1938 -2046 448 O
ATOM 2419 N PHE B 353 -9.529 39.381 20.830 1.00 92.31 N
ANISOU 2419 N PHE B 353 18492 8998 7585 -2360 -2290 922 N
ATOM 2420 CA PHE B 353 -10.492 40.237 20.130 1.00 94.55 C
ANISOU 2420 CA PHE B 353 19093 9060 7770 -2374 -2723 1239 C
ATOM 2421 C PHE B 353 -9.890 41.008 18.952 1.00 99.45 C
ANISOU 2421 C PHE B 353 20229 9792 7766 -2625 -2646 1431 C
ATOM 2422 O PHE B 353 -10.564 41.830 18.334 1.00 92.50 O
ANISOU 2422 O PHE B 353 19648 8736 6760 -2659 -2981 1742 O
ATOM 2423 CB PHE B 353 -11.152 41.208 21.109 1.00 86.99 C
ANISOU 2423 CB PHE B 353 17939 7789 7323 -2258 -2828 1478 C
ATOM 2424 CG PHE B 353 -12.265 40.587 21.904 0.71 85.99 C
ANISOU 2424 CG PHE B 353 17423 7475 7772 -1982 -3087 1414 C
ATOM 2425 CD1 PHE B 353 -13.572 40.615 21.439 0.44 87.81 C
ANISOU 2425 CD1 PHE B 353 17705 7485 8173 -1858 -3603 1588 C
ATOM 2426 CD2 PHE B 353 -12.002 39.959 23.108 1.00 83.45 C
ANISOU 2426 CD2 PHE B 353 16674 7203 7831 -1848 -2817 1200 C
ATOM 2427 CE1 PHE B 353 -14.596 40.034 22.171 0.54 87.14 C
ANISOU 2427 CE1 PHE B 353 17224 7219 8665 -1609 -3812 1548 C
ATOM 2428 CE2 PHE B 353 -13.018 39.379 23.840 1.00 82.83 C
ANISOU 2428 CE2 PHE B 353 16236 6954 8283 -1594 -3012 1169 C
ATOM 2429 CZ PHE B 353 -14.315 39.415 23.372 1.00 84.72 C
ANISOU 2429 CZ PHE B 353 16504 6962 8723 -1477 -3494 1341 C
ATOM 2430 N LEU B 354 -8.634 40.725 18.626 1.00103.24 N
ANISOU 2430 N LEU B 354 20803 10558 7866 -2794 -2198 1266 N
ATOM 2431 CA LEU B 354 -7.970 41.406 17.517 1.00111.78 C
ANISOU 2431 CA LEU B 354 22364 11769 8339 -3038 -2043 1452 C
ATOM 2432 C LEU B 354 -7.808 40.515 16.289 1.00127.29 C
ANISOU 2432 C LEU B 354 24574 13978 9812 -3064 -2047 1239 C
ATOM 2433 O LEU B 354 -7.711 39.293 16.402 1.00121.51 O
ANISOU 2433 O LEU B 354 23727 13384 9057 -2977 -2004 903 O
ATOM 2434 CB LEU B 354 -6.599 41.917 17.957 1.00117.65 C
ANISOU 2434 CB LEU B 354 22999 12643 9058 -3226 -1471 1453 C
ATOM 2435 CG LEU B 354 -6.553 43.131 18.885 1.00118.73 C
ANISOU 2435 CG LEU B 354 22980 12536 9597 -3272 -1410 1690 C
ATOM 2436 CD1 LEU B 354 -5.205 43.210 19.582 1.00114.01 C
ANISOU 2436 CD1 LEU B 354 22116 12097 9105 -3416 -881 1555 C
ATOM 2437 CD2 LEU B 354 -6.828 44.408 18.112 1.00115.98 C
ANISOU 2437 CD2 LEU B 354 22898 12031 9137 -3370 -1552 2023 C
ATOM 2438 N GLU B 355 -7.772 41.137 15.114 1.00133.49 N
ANISOU 2438 N GLU B 355 25657 14808 10255 -3165 -2079 1415 N
ATOM 2439 CA GLU B 355 -7.471 40.413 13.885 1.00121.85 C
ANISOU 2439 CA GLU B 355 24414 13580 8305 -3192 -1995 1220 C
ATOM 2440 C GLU B 355 -5.991 40.055 13.868 1.00113.76 C
ANISOU 2440 C GLU B 355 23309 12835 7079 -3308 -1340 1019 C
ATOM 2441 O GLU B 355 -5.151 40.872 14.243 1.00126.99 O
ANISOU 2441 O GLU B 355 24902 14526 8821 -3449 -975 1178 O
ATOM 2442 CB GLU B 355 -7.832 41.242 12.649 1.00150.05 C
ANISOU 2442 CB GLU B 355 28341 17133 11539 -3262 -2203 1499 C
ATOM 2443 CG GLU B 355 -9.298 41.633 12.547 1.00161.46 C
ANISOU 2443 CG GLU B 355 29844 18305 13198 -3147 -2861 1720 C
ATOM 2444 CD GLU B 355 -10.215 40.450 12.295 1.00163.76 C
ANISOU 2444 CD GLU B 355 30122 18585 13512 -2997 -3299 1471 C
ATOM 2445 OE1 GLU B 355 -9.723 39.382 11.873 1.00171.99 O
ANISOU 2445 OE1 GLU B 355 31207 19852 14287 -2991 -3102 1132 O
ATOM 2446 OE2 GLU B 355 -11.435 40.592 12.518 1.00164.88 O
ANISOU 2446 OE2 GLU B 355 30183 18479 13983 -2878 -3837 1612 O
ATOM 2447 N PRO B 356 -5.665 38.829 13.429 1.00112.05 N
ANISOU 2447 N PRO B 356 23091 12826 6657 -3244 -1190 662 N
ATOM 2448 CA PRO B 356 -4.275 38.355 13.405 1.00115.77 C
ANISOU 2448 CA PRO B 356 23438 13560 6988 -3318 -560 446 C
ATOM 2449 C PRO B 356 -3.362 39.184 12.500 1.00145.48 C
ANISOU 2449 C PRO B 356 27417 17475 10385 -3493 -177 649 C
ATOM 2450 O PRO B 356 -2.139 39.072 12.602 1.00146.50 O
ANISOU 2450 O PRO B 356 27394 17788 10480 -3581 373 558 O
ATOM 2451 CB PRO B 356 -4.401 36.921 12.875 1.00115.60 C
ANISOU 2451 CB PRO B 356 23441 13673 6808 -3179 -594 45 C
ATOM 2452 CG PRO B 356 -5.719 36.877 12.176 1.00119.27 C
ANISOU 2452 CG PRO B 356 24164 13996 7156 -3097 -1214 111 C
ATOM 2453 CD PRO B 356 -6.605 37.802 12.948 1.00118.05 C
ANISOU 2453 CD PRO B 356 23934 13562 7360 -3089 -1616 434 C
ATOM 2454 N SER B 357 -3.948 40.008 11.637 1.00148.07 N
ANISOU 2454 N SER B 357 28072 17723 10467 -3538 -466 933 N
ATOM 2455 CA SER B 357 -3.173 40.812 10.700 1.00140.54 C
ANISOU 2455 CA SER B 357 27348 16906 9143 -3690 -136 1153 C
ATOM 2456 C SER B 357 -2.976 42.246 11.189 1.00137.30 C
ANISOU 2456 C SER B 357 26876 16324 8968 -3835 -78 1536 C
ATOM 2457 O SER B 357 -2.357 43.059 10.504 1.00158.19 O
ANISOU 2457 O SER B 357 29685 19046 11375 -3971 183 1770 O
ATOM 2458 CB SER B 357 -3.848 40.818 9.327 1.00142.47 C
ANISOU 2458 CB SER B 357 28016 17203 8911 -3652 -455 1230 C
ATOM 2459 OG SER B 357 -5.153 41.368 9.400 1.00158.41 O
ANISOU 2459 OG SER B 357 30134 18966 11090 -3594 -1072 1458 O
ATOM 2460 N SER B 358 -3.500 42.554 12.372 1.00116.59 N
ANISOU 2460 N SER B 358 24015 13462 6823 -3798 -312 1598 N
ATOM 2461 CA SER B 358 -3.369 43.896 12.931 1.00114.53 C
ANISOU 2461 CA SER B 358 23672 12998 6844 -3919 -279 1923 C
ATOM 2462 C SER B 358 -2.024 44.058 13.637 1.00112.69 C
ANISOU 2462 C SER B 358 23149 12871 6796 -4072 280 1863 C
ATOM 2463 O SER B 358 -1.528 43.117 14.255 1.00144.51 O
ANISOU 2463 O SER B 358 26928 17036 10944 -4033 506 1570 O
ATOM 2464 CB SER B 358 -4.520 44.197 13.897 1.00130.79 C
ANISOU 2464 CB SER B 358 25601 14741 9351 -3798 -759 2014 C
ATOM 2465 OG SER B 358 -4.427 43.420 15.078 1.00104.81 O
ANISOU 2465 OG SER B 358 21994 11446 6382 -3720 -691 1761 O
ATOM 2466 N PRO B 359 -1.427 45.256 13.534 1.00115.09 N
ANISOU 2466 N PRO B 359 23470 13111 7148 -4246 495 2148 N
ATOM 2467 CA PRO B 359 -0.125 45.586 14.131 1.00114.30 C
ANISOU 2467 CA PRO B 359 23086 13089 7255 -4426 999 2139 C
ATOM 2468 C PRO B 359 -0.076 45.360 15.642 1.00120.22 C
ANISOU 2468 C PRO B 359 23464 13728 8486 -4407 986 1980 C
ATOM 2469 O PRO B 359 0.923 44.849 16.154 1.00131.59 O
ANISOU 2469 O PRO B 359 24618 15340 10039 -4479 1374 1792 O
ATOM 2470 CB PRO B 359 0.041 47.072 13.799 1.00127.43 C
ANISOU 2470 CB PRO B 359 24870 14587 8960 -4581 1027 2525 C
ATOM 2471 CG PRO B 359 -0.780 47.273 12.570 1.00142.55 C
ANISOU 2471 CG PRO B 359 27191 16495 10477 -4500 725 2708 C
ATOM 2472 CD PRO B 359 -1.967 46.377 12.745 1.00124.81 C
ANISOU 2472 CD PRO B 359 24996 14192 8236 -4284 256 2510 C
ATOM 2473 N THR B 360 -1.142 45.739 16.341 1.00122.42 N
ANISOU 2473 N THR B 360 23736 13725 9054 -4301 550 2063 N
ATOM 2474 CA THR B 360 -1.217 45.554 17.786 1.00120.59 C
ANISOU 2474 CA THR B 360 23187 13372 9260 -4257 506 1931 C
ATOM 2475 C THR B 360 -1.193 44.068 18.138 1.00111.60 C
ANISOU 2475 C THR B 360 21895 12434 8073 -4121 563 1595 C
ATOM 2476 O THR B 360 -0.567 43.660 19.120 1.00111.76 O
ANISOU 2476 O THR B 360 21603 12531 8330 -4153 794 1431 O
ATOM 2477 CB THR B 360 -2.487 46.204 18.374 1.00126.72 C
ANISOU 2477 CB THR B 360 24000 13794 10354 -4117 22 2087 C
ATOM 2478 OG1 THR B 360 -2.603 47.551 17.899 1.00133.03 O
ANISOU 2478 OG1 THR B 360 24958 14407 11182 -4209 -51 2393 O
ATOM 2479 CG2 THR B 360 -2.434 46.211 19.896 1.00109.50 C
ANISOU 2479 CG2 THR B 360 21496 11473 8637 -4088 39 1978 C
ATOM 2480 N PHE B 361 -1.878 43.266 17.326 1.00112.47 N
ANISOU 2480 N PHE B 361 22219 12627 7889 -3969 338 1488 N
ATOM 2481 CA PHE B 361 -1.896 41.817 17.500 1.00132.07 C
ANISOU 2481 CA PHE B 361 24577 15292 10313 -3822 376 1143 C
ATOM 2482 C PHE B 361 -0.491 41.243 17.379 1.00132.23 C
ANISOU 2482 C PHE B 361 24402 15611 10227 -3925 949 941 C
ATOM 2483 O PHE B 361 -0.088 40.402 18.178 1.00127.76 O
ANISOU 2483 O PHE B 361 23527 15156 9860 -3862 1126 695 O
ATOM 2484 CB PHE B 361 -2.821 41.164 16.469 1.00122.36 C
ANISOU 2484 CB PHE B 361 23632 14082 8778 -3670 25 1061 C
ATOM 2485 CG PHE B 361 -2.982 39.676 16.640 1.00139.10 C
ANISOU 2485 CG PHE B 361 25621 16333 10895 -3499 -2 683 C
ATOM 2486 CD1 PHE B 361 -4.062 39.159 17.337 1.00112.63 C
ANISOU 2486 CD1 PHE B 361 22123 12808 7863 -3298 -429 590 C
ATOM 2487 CD2 PHE B 361 -2.065 38.794 16.089 1.00158.61 C
ANISOU 2487 CD2 PHE B 361 28047 19077 13140 -3507 406 413 C
ATOM 2488 CE1 PHE B 361 -4.219 37.794 17.488 1.00110.73 C
ANISOU 2488 CE1 PHE B 361 21662 12654 7757 -3115 -459 230 C
ATOM 2489 CE2 PHE B 361 -2.214 37.429 16.241 1.00129.46 C
ANISOU 2489 CE2 PHE B 361 24219 15472 9499 -3339 385 48 C
ATOM 2490 CZ PHE B 361 -3.292 36.929 16.942 1.00114.15 C
ANISOU 2490 CZ PHE B 361 22132 13350 7891 -3152 -58 -45 C
ATOM 2491 N LEU B 362 0.243 41.693 16.367 1.00114.37 N
ANISOU 2491 N LEU B 362 22296 13478 7681 -4064 1239 1054 N
ATOM 2492 CA LEU B 362 1.605 41.226 16.136 1.00103.31 C
ANISOU 2492 CA LEU B 362 20703 12351 6200 -4154 1808 900 C
ATOM 2493 C LEU B 362 2.519 41.638 17.286 1.00109.98 C
ANISOU 2493 C LEU B 362 21149 13192 7448 -4307 2098 934 C
ATOM 2494 O LEU B 362 3.371 40.861 17.730 1.00102.39 O
ANISOU 2494 O LEU B 362 19862 12421 6622 -4303 2447 713 O
ATOM 2495 CB LEU B 362 2.131 41.768 14.806 1.00115.71 C
ANISOU 2495 CB LEU B 362 22545 14034 7386 -4266 2044 1074 C
ATOM 2496 CG LEU B 362 1.353 41.303 13.571 1.00113.11 C
ANISOU 2496 CG LEU B 362 22620 13755 6604 -4129 1790 1022 C
ATOM 2497 CD1 LEU B 362 1.812 42.038 12.319 1.00119.94 C
ANISOU 2497 CD1 LEU B 362 23780 14715 7075 -4247 1999 1262 C
ATOM 2498 CD2 LEU B 362 1.484 39.797 13.392 1.00112.68 C
ANISOU 2498 CD2 LEU B 362 22486 13891 6435 -3962 1917 617 C
ATOM 2499 N LEU B 363 2.327 42.863 17.767 1.00110.81 N
ANISOU 2499 N LEU B 363 21266 13068 7771 -4436 1936 1205 N
ATOM 2500 CA LEU B 363 3.073 43.370 18.915 1.00117.43 C
ANISOU 2500 CA LEU B 363 21744 13853 9020 -4595 2121 1241 C
ATOM 2501 C LEU B 363 2.856 42.483 20.143 1.00117.52 C
ANISOU 2501 C LEU B 363 21412 13883 9359 -4437 2015 985 C
ATOM 2502 O LEU B 363 3.816 42.001 20.756 1.00119.05 O
ANISOU 2502 O LEU B 363 21175 14247 9812 -4459 2309 812 O
ATOM 2503 CB LEU B 363 2.662 44.812 19.219 1.00118.25 C
ANISOU 2503 CB LEU B 363 21957 13647 9326 -4709 1873 1536 C
ATOM 2504 CG LEU B 363 3.265 45.485 20.454 1.00132.87 C
ANISOU 2504 CG LEU B 363 23477 15374 11632 -4876 1961 1566 C
ATOM 2505 CD1 LEU B 363 4.783 45.412 20.423 1.00122.92 C
ANISOU 2505 CD1 LEU B 363 21907 14348 10450 -5081 2462 1517 C
ATOM 2506 CD2 LEU B 363 2.798 46.931 20.548 1.00128.25 C
ANISOU 2506 CD2 LEU B 363 23051 14460 11220 -4956 1713 1833 C
ATOM 2507 N LEU B 364 1.590 42.259 20.485 1.00109.33 N
ANISOU 2507 N LEU B 364 20436 12665 8438 -4202 1548 938 N
ATOM 2508 CA LEU B 364 1.235 41.415 21.622 1.00119.51 C
ANISOU 2508 CA LEU B 364 21308 13950 10153 -3951 1376 682 C
ATOM 2509 C LEU B 364 1.767 39.992 21.456 1.00127.90 C
ANISOU 2509 C LEU B 364 22141 15286 11171 -3819 1622 374 C
ATOM 2510 O LEU B 364 2.204 39.367 22.427 1.00162.51 O
ANISOU 2510 O LEU B 364 26069 19756 15921 -3716 1717 190 O
ATOM 2511 CB LEU B 364 -0.282 41.388 21.812 1.00126.65 C
ANISOU 2511 CB LEU B 364 22353 14610 11159 -3722 863 716 C
ATOM 2512 CG LEU B 364 -0.950 42.679 22.284 1.00 95.02 C
ANISOU 2512 CG LEU B 364 18471 10282 7349 -3769 588 976 C
ATOM 2513 CD1 LEU B 364 -2.447 42.474 22.465 1.00 87.11 C
ANISOU 2513 CD1 LEU B 364 17539 9059 6499 -3505 114 992 C
ATOM 2514 CD2 LEU B 364 -0.311 43.155 23.576 1.00 83.72 C
ANISOU 2514 CD2 LEU B 364 16675 8805 6332 -3838 721 934 C
ATOM 2515 N LYS B 365 1.718 39.487 20.226 1.00103.39 N
ANISOU 2515 N LYS B 365 19370 12306 7608 -3817 1719 321 N
ATOM 2516 CA LYS B 365 2.272 38.178 19.900 1.00104.05 C
ANISOU 2516 CA LYS B 365 19299 12628 7607 -3704 2002 18 C
ATOM 2517 C LYS B 365 3.749 38.147 20.256 1.00108.39 C
ANISOU 2517 C LYS B 365 19473 13378 8333 -3846 2514 -24 C
ATOM 2518 O LYS B 365 4.247 37.172 20.818 1.00114.17 O
ANISOU 2518 O LYS B 365 19792 14239 9348 -3707 2679 -259 O
ATOM 2519 CB LYS B 365 2.081 37.857 18.415 1.00118.76 C
ANISOU 2519 CB LYS B 365 21672 14588 8861 -3728 2064 -19 C
ATOM 2520 CG LYS B 365 2.595 36.484 18.004 1.00107.41 C
ANISOU 2520 CG LYS B 365 20128 13364 7318 -3596 2366 -370 C
ATOM 2521 CD LYS B 365 2.673 36.347 16.491 1.00128.46 C
ANISOU 2521 CD LYS B 365 23211 16137 9459 -3616 2485 -397 C
ATOM 2522 CE LYS B 365 3.729 37.271 15.903 1.00140.91 C
ANISOU 2522 CE LYS B 365 24819 17825 10896 -3829 2891 -159 C
ATOM 2523 NZ LYS B 365 3.816 37.151 14.420 1.00122.76 N
ANISOU 2523 NZ LYS B 365 22882 15638 8124 -3806 3002 -172 N
ATOM 2524 N LYS B 366 4.441 39.232 19.930 1.00102.76 N
ANISOU 2524 N LYS B 366 18887 12676 7483 -4127 2753 228 N
ATOM 2525 CA LYS B 366 5.851 39.362 20.268 1.00112.21 C
ANISOU 2525 CA LYS B 366 19701 14037 8895 -4303 3217 235 C
ATOM 2526 C LYS B 366 6.059 39.493 21.778 1.00101.42 C
ANISOU 2526 C LYS B 366 17823 12603 8111 -4272 3064 197 C
ATOM 2527 O LYS B 366 7.129 39.166 22.290 1.00 99.96 O
ANISOU 2527 O LYS B 366 17191 12579 8209 -4321 3358 110 O
ATOM 2528 CB LYS B 366 6.465 40.564 19.544 1.00124.91 C
ANISOU 2528 CB LYS B 366 21563 15632 10265 -4620 3475 544 C
ATOM 2529 N LEU B 367 5.036 39.962 22.488 1.00102.87 N
ANISOU 2529 N LEU B 367 18071 12549 8467 -4181 2603 262 N
ATOM 2530 CA LEU B 367 5.143 40.174 23.935 1.00117.70 C
ANISOU 2530 CA LEU B 367 19541 14352 10830 -4148 2435 226 C
ATOM 2531 C LEU B 367 4.671 38.979 24.773 1.00102.80 C
ANISOU 2531 C LEU B 367 17337 12508 9214 -3826 2250 -17 C
ATOM 2532 O LEU B 367 4.782 38.986 26.011 1.00 99.37 O
ANISOU 2532 O LEU B 367 16557 12051 9149 -3765 2126 -64 O
ATOM 2533 CB LEU B 367 4.349 41.417 24.338 1.00103.21 C
ANISOU 2533 CB LEU B 367 17939 12214 9060 -4225 2090 432 C
ATOM 2534 CG LEU B 367 4.776 42.741 23.701 1.00 97.89 C
ANISOU 2534 CG LEU B 367 17552 11430 8210 -4554 2232 713 C
ATOM 2535 CD1 LEU B 367 3.829 43.862 24.099 1.00 96.72 C
ANISOU 2535 CD1 LEU B 367 17649 10939 8162 -4571 1859 893 C
ATOM 2536 CD2 LEU B 367 6.208 43.087 24.079 1.00 98.63 C
ANISOU 2536 CD2 LEU B 367 17294 11656 8525 -4817 2580 731 C
ATOM 2537 N ASP B 368 4.146 37.963 24.092 1.00103.17 N
ANISOU 2537 N ASP B 368 17521 12610 9068 -3627 2228 -167 N
ATOM 2538 CA ASP B 368 3.565 36.788 24.741 1.00106.67 C
ANISOU 2538 CA ASP B 368 17711 13054 9764 -3317 2043 -376 C
ATOM 2539 C ASP B 368 4.486 36.155 25.783 1.00112.67 C
ANISOU 2539 C ASP B 368 17916 13977 10917 -3252 2225 -499 C
ATOM 2540 O ASP B 368 4.077 35.929 26.923 1.00101.71 O
ANISOU 2540 O ASP B 368 16273 12522 9851 -3089 1994 -530 O
ATOM 2541 CB ASP B 368 3.189 35.737 23.692 1.00104.25 C
ANISOU 2541 CB ASP B 368 17616 12809 9186 -3172 2088 -554 C
ATOM 2542 CG ASP B 368 2.487 34.534 24.297 1.00110.11 C
ANISOU 2542 CG ASP B 368 18117 13501 10220 -2862 1874 -752 C
ATOM 2543 OD1 ASP B 368 2.853 33.391 23.950 1.00115.50 O
ANISOU 2543 OD1 ASP B 368 18670 14307 10906 -2740 2078 -973 O
ATOM 2544 OD2 ASP B 368 1.565 34.730 25.116 1.00131.76 O
ANISOU 2544 OD2 ASP B 368 20796 16063 13202 -2736 1522 -683 O
ATOM 2545 N SER B 369 5.726 35.879 25.390 1.00104.40 N
ANISOU 2545 N SER B 369 16679 13144 9843 -3373 2643 -551 N
ATOM 2546 CA SER B 369 6.686 35.225 26.277 1.00103.30 C
ANISOU 2546 CA SER B 369 15988 13175 10088 -3311 2822 -649 C
ATOM 2547 C SER B 369 7.021 36.072 27.501 1.00115.04 C
ANISOU 2547 C SER B 369 17218 14626 11864 -3436 2662 -525 C
ATOM 2548 O SER B 369 7.197 35.541 28.599 1.00128.43 O
ANISOU 2548 O SER B 369 18524 16382 13892 -3291 2561 -592 O
ATOM 2549 CB SER B 369 7.969 34.885 25.516 1.00122.24 C
ANISOU 2549 CB SER B 369 18235 15794 12416 -3434 3331 -700 C
ATOM 2550 OG SER B 369 7.783 33.749 24.690 1.00105.14 O
ANISOU 2550 OG SER B 369 16178 13686 10084 -3241 3496 -903 O
ATOM 2551 N LEU B 370 7.109 37.385 27.314 1.00111.83 N
ANISOU 2551 N LEU B 370 17049 14114 11326 -3707 2633 -344 N
ATOM 2552 CA LEU B 370 7.379 38.289 28.425 1.00 97.99 C
ANISOU 2552 CA LEU B 370 15120 12288 9822 -3851 2458 -253 C
ATOM 2553 C LEU B 370 6.226 38.263 29.422 1.00 96.76 C
ANISOU 2553 C LEU B 370 15010 11959 9794 -3623 2045 -287 C
ATOM 2554 O LEU B 370 6.441 38.153 30.635 1.00 96.83 O
ANISOU 2554 O LEU B 370 14707 12009 10075 -3558 1912 -335 O
ATOM 2555 CB LEU B 370 7.617 39.715 27.924 1.00 97.77 C
ANISOU 2555 CB LEU B 370 15382 12128 9639 -4188 2511 -52 C
ATOM 2556 CG LEU B 370 7.926 40.752 29.008 1.00 96.72 C
ANISOU 2556 CG LEU B 370 15110 11880 9759 -4376 2327 16 C
ATOM 2557 CD1 LEU B 370 9.147 40.340 29.815 1.00114.51 C
ANISOU 2557 CD1 LEU B 370 16813 14357 12338 -4441 2453 -67 C
ATOM 2558 CD2 LEU B 370 8.121 42.134 28.403 1.00 95.76 C
ANISOU 2558 CD2 LEU B 370 15296 11582 9506 -4712 2395 225 C
ATOM 2559 N CYS B 371 5.002 38.353 28.907 1.00 96.58 N
ANISOU 2559 N CYS B 371 15374 11748 9573 -3499 1845 -253 N
ATOM 2560 CA CYS B 371 3.825 38.290 29.770 1.00110.93 C
ANISOU 2560 CA CYS B 371 17230 13387 11533 -3262 1493 -269 C
ATOM 2561 C CYS B 371 3.750 36.957 30.523 1.00102.64 C
ANISOU 2561 C CYS B 371 15811 12466 10723 -2971 1467 -423 C
ATOM 2562 O CYS B 371 3.410 36.922 31.712 1.00 96.17 O
ANISOU 2562 O CYS B 371 14820 11601 10120 -2832 1280 -434 O
ATOM 2563 CB CYS B 371 2.551 38.512 28.954 1.00114.03 C
ANISOU 2563 CB CYS B 371 18055 13562 11707 -3175 1290 -193 C
ATOM 2564 SG CYS B 371 2.442 40.149 28.195 1.00117.36 S
ANISOU 2564 SG CYS B 371 18935 13775 11882 -3478 1256 45 S
ATOM 2565 N VAL B 372 4.085 35.867 29.835 1.00 94.28 N
ANISOU 2565 N VAL B 372 14642 11561 9621 -2878 1672 -537 N
ATOM 2566 CA VAL B 372 4.068 34.542 30.449 1.00 93.89 C
ANISOU 2566 CA VAL B 372 14236 11611 9825 -2604 1675 -669 C
ATOM 2567 C VAL B 372 5.138 34.429 31.535 1.00 86.26 C
ANISOU 2567 C VAL B 372 12819 10828 9129 -2638 1764 -672 C
ATOM 2568 O VAL B 372 4.918 33.790 32.563 1.00 92.54 O
ANISOU 2568 O VAL B 372 13349 11647 10163 -2423 1633 -698 O
ATOM 2569 CB VAL B 372 4.265 33.425 29.398 1.00116.36 C
ANISOU 2569 CB VAL B 372 17082 14554 12574 -2509 1903 -816 C
ATOM 2570 CG1 VAL B 372 4.474 32.072 30.072 1.00 97.81 C
ANISOU 2570 CG1 VAL B 372 14309 12303 10552 -2249 1954 -938 C
ATOM 2571 CG2 VAL B 372 3.067 33.365 28.464 1.00123.29 C
ANISOU 2571 CG2 VAL B 372 18388 15250 13206 -2434 1721 -835 C
ATOM 2572 N SER B 373 6.287 35.060 31.314 1.00 85.77 N
ANISOU 2572 N SER B 373 12665 10891 9034 -2914 1973 -626 N
ATOM 2573 CA SER B 373 7.343 35.076 32.322 1.00 86.10 C
ANISOU 2573 CA SER B 373 12274 11102 9339 -2987 2007 -614 C
ATOM 2574 C SER B 373 6.874 35.831 33.561 1.00 87.61 C
ANISOU 2574 C SER B 373 12500 11182 9607 -2989 1678 -559 C
ATOM 2575 O SER B 373 7.075 35.386 34.704 1.00 87.27 O
ANISOU 2575 O SER B 373 12147 11238 9772 -2855 1554 -579 O
ATOM 2576 CB SER B 373 8.616 35.712 31.762 1.00 86.27 C
ANISOU 2576 CB SER B 373 12195 11247 9337 -3316 2289 -558 C
ATOM 2577 OG SER B 373 8.438 37.100 31.534 1.00 87.28 O
ANISOU 2577 OG SER B 373 12658 11212 9293 -3584 2203 -444 O
ATOM 2578 N PHE B 374 6.236 36.973 33.323 1.00103.56 N
ANISOU 2578 N PHE B 374 14916 12987 11446 -3131 1544 -485 N
ATOM 2579 CA PHE B 374 5.693 37.776 34.407 1.00 91.09 C
ANISOU 2579 CA PHE B 374 13441 11256 9913 -3125 1261 -457 C
ATOM 2580 C PHE B 374 4.675 36.971 35.209 1.00 97.33 C
ANISOU 2580 C PHE B 374 14179 12000 10803 -2766 1074 -496 C
ATOM 2581 O PHE B 374 4.615 37.074 36.435 1.00 87.60 O
ANISOU 2581 O PHE B 374 12824 10783 9676 -2684 911 -509 O
ATOM 2582 CB PHE B 374 5.054 39.051 33.866 1.00 81.09 C
ANISOU 2582 CB PHE B 374 12628 9721 8461 -3296 1172 -365 C
ATOM 2583 CG PHE B 374 4.789 40.079 34.921 1.00 80.81 C
ANISOU 2583 CG PHE B 374 12698 9519 8487 -3363 945 -357 C
ATOM 2584 CD1 PHE B 374 5.837 40.768 35.507 1.00 82.24 C
ANISOU 2584 CD1 PHE B 374 12718 9769 8761 -3629 943 -376 C
ATOM 2585 CD2 PHE B 374 3.498 40.353 35.334 1.00 85.80 C
ANISOU 2585 CD2 PHE B 374 13583 9916 9102 -3161 736 -342 C
ATOM 2586 CE1 PHE B 374 5.602 41.713 36.482 1.00 91.34 C
ANISOU 2586 CE1 PHE B 374 14001 10753 9951 -3696 728 -410 C
ATOM 2587 CE2 PHE B 374 3.256 41.299 36.308 1.00 92.15 C
ANISOU 2587 CE2 PHE B 374 14508 10553 9952 -3206 563 -363 C
ATOM 2588 CZ PHE B 374 4.310 41.980 36.883 1.00106.91 C
ANISOU 2588 CZ PHE B 374 16256 12488 11876 -3476 554 -412 C
ATOM 2589 N ALA B 375 3.884 36.164 34.511 1.00 98.52 N
ANISOU 2589 N ALA B 375 14428 12091 10913 -2559 1101 -514 N
ATOM 2590 CA ALA B 375 2.969 35.244 35.176 1.00 81.63 C
ANISOU 2590 CA ALA B 375 12184 9908 8924 -2221 966 -536 C
ATOM 2591 C ALA B 375 3.736 34.185 35.964 1.00 84.65 C
ANISOU 2591 C ALA B 375 12114 10526 9524 -2082 1043 -579 C
ATOM 2592 O ALA B 375 3.294 33.744 37.024 1.00 84.36 O
ANISOU 2592 O ALA B 375 11936 10491 9628 -1861 913 -555 O
ATOM 2593 CB ALA B 375 2.055 34.588 34.162 1.00 77.76 C
ANISOU 2593 CB ALA B 375 11873 9296 8376 -2069 965 -558 C
ATOM 2594 N TYR B 376 4.892 33.796 35.434 1.00105.62 N
ANISOU 2594 N TYR B 376 14542 13376 12213 -2209 1269 -622 N
ATOM 2595 CA TYR B 376 5.696 32.714 35.989 1.00102.29 C
ANISOU 2595 CA TYR B 376 13663 13170 12032 -2072 1367 -648 C
ATOM 2596 C TYR B 376 6.384 33.132 37.279 1.00 87.58 C
ANISOU 2596 C TYR B 376 11562 11445 10271 -2145 1229 -595 C
ATOM 2597 O TYR B 376 6.802 32.284 38.068 1.00 86.98 O
ANISOU 2597 O TYR B 376 11126 11525 10397 -1979 1208 -573 O
ATOM 2598 CB TYR B 376 6.741 32.251 34.971 1.00 95.92 C
ANISOU 2598 CB TYR B 376 12685 12511 11248 -2188 1684 -710 C
ATOM 2599 CG TYR B 376 6.642 30.795 34.582 1.00 98.68 C
ANISOU 2599 CG TYR B 376 12844 12891 11756 -1925 1834 -796 C
ATOM 2600 CD1 TYR B 376 6.253 30.424 33.302 1.00104.33 C
ANISOU 2600 CD1 TYR B 376 13806 13515 12318 -1904 1989 -900 C
ATOM 2601 CD2 TYR B 376 6.942 29.792 35.492 1.00105.31 C
ANISOU 2601 CD2 TYR B 376 13276 13841 12897 -1699 1810 -774 C
ATOM 2602 CE1 TYR B 376 6.168 29.093 32.939 1.00104.61 C
ANISOU 2602 CE1 TYR B 376 13686 13548 12512 -1672 2122 -1015 C
ATOM 2603 CE2 TYR B 376 6.857 28.458 35.141 1.00118.01 C
ANISOU 2603 CE2 TYR B 376 14706 15438 14695 -1458 1954 -854 C
ATOM 2604 CZ TYR B 376 6.469 28.113 33.863 1.00121.53 C
ANISOU 2604 CZ TYR B 376 15403 15771 15000 -1449 2112 -992 C
ATOM 2605 OH TYR B 376 6.384 26.784 33.509 1.00122.50 O
ANISOU 2605 OH TYR B 376 15368 15852 15324 -1216 2250 -1107 O
ATOM 2606 N ILE B 377 6.510 34.441 37.482 1.00 88.98 N
ANISOU 2606 N ILE B 377 11947 11554 10308 -2399 1119 -574 N
ATOM 2607 CA ILE B 377 7.046 34.980 38.737 1.00 90.70 C
ANISOU 2607 CA ILE B 377 12018 11868 10575 -2491 928 -556 C
ATOM 2608 C ILE B 377 6.290 34.446 39.974 1.00 88.41 C
ANISOU 2608 C ILE B 377 11685 11577 10328 -2183 729 -530 C
ATOM 2609 O ILE B 377 6.856 34.325 41.073 1.00 91.31 O
ANISOU 2609 O ILE B 377 11817 12113 10764 -2161 592 -509 O
ATOM 2610 CB ILE B 377 7.014 36.531 38.715 1.00104.15 C
ANISOU 2610 CB ILE B 377 14049 13408 12115 -2791 821 -563 C
ATOM 2611 CG1 ILE B 377 7.797 37.054 37.506 1.00105.16 C
ANISOU 2611 CG1 ILE B 377 14208 13540 12207 -3102 1046 -547 C
ATOM 2612 CG2 ILE B 377 7.562 37.114 40.011 1.00109.82 C
ANISOU 2612 CG2 ILE B 377 14653 14210 12865 -2904 595 -588 C
ATOM 2613 CD1 ILE B 377 7.951 38.551 37.473 1.00117.36 C
ANISOU 2613 CD1 ILE B 377 16018 14921 13654 -3430 962 -530 C
ATOM 2614 N ASN B 378 5.020 34.102 39.777 1.00 85.62 N
ANISOU 2614 N ASN B 378 11553 11040 9940 -1946 714 -515 N
ATOM 2615 CA ASN B 378 4.194 33.500 40.824 1.00 86.00 C
ANISOU 2615 CA ASN B 378 11559 11065 10052 -1632 589 -461 C
ATOM 2616 C ASN B 378 4.765 32.210 41.403 1.00 89.23 C
ANISOU 2616 C ASN B 378 11538 11695 10669 -1430 628 -406 C
ATOM 2617 O ASN B 378 4.451 31.837 42.534 1.00117.32 O
ANISOU 2617 O ASN B 378 15010 15308 14260 -1223 511 -331 O
ATOM 2618 CB ASN B 378 2.789 33.218 40.285 1.00 82.51 C
ANISOU 2618 CB ASN B 378 11356 10377 9616 -1426 601 -441 C
ATOM 2619 CG ASN B 378 1.877 34.420 40.379 1.00 84.24 C
ANISOU 2619 CG ASN B 378 11976 10353 9679 -1487 481 -438 C
ATOM 2620 OD1 ASN B 378 1.693 34.993 41.453 1.00107.53 O
ANISOU 2620 OD1 ASN B 378 15011 13284 12563 -1457 363 -431 O
ATOM 2621 ND2 ASN B 378 1.302 34.813 39.251 1.00 81.27 N
ANISOU 2621 ND2 ASN B 378 11861 9784 9234 -1565 509 -445 N
ATOM 2622 N CYS B 379 5.594 31.528 40.620 1.00 86.23 N
ANISOU 2622 N CYS B 379 10896 11435 10432 -1480 809 -433 N
ATOM 2623 CA CYS B 379 6.110 30.218 40.998 1.00 87.36 C
ANISOU 2623 CA CYS B 379 10616 11746 10830 -1267 877 -374 C
ATOM 2624 C CYS B 379 7.404 30.324 41.797 1.00 97.72 C
ANISOU 2624 C CYS B 379 11589 13321 12221 -1388 795 -325 C
ATOM 2625 O CYS B 379 8.056 29.319 42.076 1.00114.70 O
ANISOU 2625 O CYS B 379 13340 15629 14610 -1245 848 -257 O
ATOM 2626 CB CYS B 379 6.329 29.360 39.752 1.00 86.60 C
ANISOU 2626 CB CYS B 379 10404 11623 10876 -1227 1134 -448 C
ATOM 2627 SG CYS B 379 4.849 29.157 38.737 1.00 99.42 S
ANISOU 2627 SG CYS B 379 12413 12948 12413 -1101 1172 -520 S
ATOM 2628 N CYS B 380 7.773 31.546 42.163 1.00 91.97 N
ANISOU 2628 N CYS B 380 11011 12620 11315 -1656 647 -358 N
ATOM 2629 CA CYS B 380 8.964 31.760 42.972 1.00102.89 C
ANISOU 2629 CA CYS B 380 12087 14240 12766 -1805 500 -320 C
ATOM 2630 C CYS B 380 8.747 32.869 43.989 1.00 96.38 C
ANISOU 2630 C CYS B 380 11527 13392 11702 -1933 217 -351 C
ATOM 2631 O CYS B 380 9.564 33.051 44.894 1.00 95.82 O
ANISOU 2631 O CYS B 380 11253 13514 11642 -2030 9 -326 O
ATOM 2632 CB CYS B 380 10.170 32.093 42.090 1.00 98.06 C
ANISOU 2632 CB CYS B 380 11263 13720 12277 -2108 667 -364 C
ATOM 2633 SG CYS B 380 10.279 33.826 41.585 1.00 93.81 S
ANISOU 2633 SG CYS B 380 11097 13031 11516 -2536 632 -457 S
ATOM 2634 N ILE B 381 7.652 33.611 43.839 1.00 91.86 N
ANISOU 2634 N ILE B 381 11407 12576 10920 -1931 199 -411 N
ATOM 2635 CA ILE B 381 7.389 34.734 44.732 1.00 92.39 C
ANISOU 2635 CA ILE B 381 11774 12573 10758 -2048 -31 -476 C
ATOM 2636 C ILE B 381 7.006 34.303 46.160 1.00 99.97 C
ANISOU 2636 C ILE B 381 12722 13642 11618 -1786 -216 -414 C
ATOM 2637 O ILE B 381 7.248 35.049 47.110 1.00 90.94 O
ANISOU 2637 O ILE B 381 11709 12553 10293 -1901 -442 -478 O
ATOM 2638 CB ILE B 381 6.282 35.654 44.157 1.00 97.38 C
ANISOU 2638 CB ILE B 381 12887 12884 11231 -2092 23 -543 C
ATOM 2639 CG1 ILE B 381 6.279 37.012 44.867 1.00 83.22 C
ANISOU 2639 CG1 ILE B 381 11396 10984 9240 -2300 -178 -651 C
ATOM 2640 CG2 ILE B 381 4.920 34.983 44.231 1.00 88.97 C
ANISOU 2640 CG2 ILE B 381 11966 11674 10165 -1731 90 -477 C
ATOM 2641 CD1 ILE B 381 7.559 37.801 44.675 1.00 81.68 C
ANISOU 2641 CD1 ILE B 381 11075 10872 9090 -2704 -252 -718 C
ATOM 2642 N ASN B 382 6.438 33.106 46.318 1.00113.13 N
ANISOU 2642 N ASN B 382 14245 15341 13399 -1443 -121 -289 N
ATOM 2643 CA ASN B 382 5.976 32.648 47.633 1.00 95.38 C
ANISOU 2643 CA ASN B 382 12008 13186 11044 -1169 -251 -187 C
ATOM 2644 C ASN B 382 7.102 32.505 48.668 1.00100.05 C
ANISOU 2644 C ASN B 382 12331 14087 11598 -1233 -487 -137 C
ATOM 2645 O ASN B 382 6.983 33.052 49.775 1.00113.16 O
ANISOU 2645 O ASN B 382 14200 15807 12989 -1231 -695 -168 O
ATOM 2646 CB ASN B 382 5.209 31.322 47.507 1.00 98.41 C
ANISOU 2646 CB ASN B 382 12241 13524 11626 -805 -81 -33 C
ATOM 2647 CG ASN B 382 3.930 31.461 46.712 1.00101.03 C
ANISOU 2647 CG ASN B 382 12859 13549 11979 -710 79 -70 C
ATOM 2648 OD1 ASN B 382 3.941 31.889 45.557 1.00114.82 O
ANISOU 2648 OD1 ASN B 382 14708 15158 13760 -894 174 -172 O
ATOM 2649 ND2 ASN B 382 2.818 31.086 47.325 1.00 94.71 N
ANISOU 2649 ND2 ASN B 382 12180 12642 11165 -421 109 32 N
ATOM 2650 N PRO B 383 8.194 31.778 48.329 1.00100.35 N
ANISOU 2650 N PRO B 383 11908 14318 11901 -1284 -464 -62 N
ATOM 2651 CA PRO B 383 9.278 31.722 49.318 1.00104.25 C
ANISOU 2651 CA PRO B 383 12131 15103 12376 -1364 -741 0 C
ATOM 2652 C PRO B 383 9.857 33.099 49.638 1.00109.33 C
ANISOU 2652 C PRO B 383 12962 15762 12814 -1735 -984 -174 C
ATOM 2653 O PRO B 383 10.319 33.309 50.756 1.00117.52 O
ANISOU 2653 O PRO B 383 13981 16988 13683 -1776 -1292 -165 O
ATOM 2654 CB PRO B 383 10.331 30.829 48.647 1.00103.87 C
ANISOU 2654 CB PRO B 383 11546 15200 12719 -1382 -620 95 C
ATOM 2655 CG PRO B 383 9.996 30.848 47.198 1.00109.59 C
ANISOU 2655 CG PRO B 383 12349 15707 13582 -1445 -293 1 C
ATOM 2656 CD PRO B 383 8.507 30.955 47.145 1.00106.70 C
ANISOU 2656 CD PRO B 383 12416 15095 13028 -1253 -203 -28 C
ATOM 2657 N ILE B 384 9.817 34.019 48.679 1.00105.67 N
ANISOU 2657 N ILE B 384 12695 15096 12361 -2004 -861 -325 N
ATOM 2658 CA ILE B 384 10.282 35.382 48.915 1.00111.33 C
ANISOU 2658 CA ILE B 384 13617 15762 12921 -2370 -1071 -496 C
ATOM 2659 C ILE B 384 9.439 36.065 49.991 1.00123.95 C
ANISOU 2659 C ILE B 384 15684 17266 14147 -2286 -1258 -599 C
ATOM 2660 O ILE B 384 9.977 36.665 50.924 1.00128.33 O
ANISOU 2660 O ILE B 384 16302 17934 14526 -2450 -1570 -694 O
ATOM 2661 CB ILE B 384 10.252 36.220 47.622 1.00116.29 C
ANISOU 2661 CB ILE B 384 14406 16148 13633 -2644 -861 -599 C
ATOM 2662 CG1 ILE B 384 11.267 35.672 46.618 1.00128.04 C
ANISOU 2662 CG1 ILE B 384 15437 17755 15457 -2772 -664 -519 C
ATOM 2663 CG2 ILE B 384 10.557 37.678 47.924 1.00117.98 C
ANISOU 2663 CG2 ILE B 384 14888 16241 13698 -3005 -1073 -774 C
ATOM 2664 CD1 ILE B 384 12.679 35.607 47.161 1.00136.35 C
ANISOU 2664 CD1 ILE B 384 16037 19078 16692 -2970 -888 -481 C
ATOM 2665 N ILE B 385 8.120 35.962 49.857 1.00108.81 N
ANISOU 2665 N ILE B 385 14088 15137 12119 -2027 -1067 -586 N
ATOM 2666 CA ILE B 385 7.188 36.501 50.843 1.00103.27 C
ANISOU 2666 CA ILE B 385 13826 14327 11086 -1882 -1159 -668 C
ATOM 2667 C ILE B 385 7.443 35.896 52.219 1.00122.17 C
ANISOU 2667 C ILE B 385 16122 17008 13290 -1691 -1379 -577 C
ATOM 2668 O ILE B 385 7.520 36.614 53.228 1.00134.12 O
ANISOU 2668 O ILE B 385 17906 18565 14489 -1771 -1618 -712 O
ATOM 2669 CB ILE B 385 5.723 36.238 50.431 1.00 95.24 C
ANISOU 2669 CB ILE B 385 13055 13055 10076 -1584 -882 -608 C
ATOM 2670 CG1 ILE B 385 5.374 37.034 49.173 1.00 87.85 C
ANISOU 2670 CG1 ILE B 385 12312 11818 9249 -1781 -724 -703 C
ATOM 2671 CG2 ILE B 385 4.766 36.586 51.563 1.00 95.38 C
ANISOU 2671 CG2 ILE B 385 13460 12995 9785 -1366 -923 -651 C
ATOM 2672 CD1 ILE B 385 3.942 36.854 48.707 1.00 81.72 C
ANISOU 2672 CD1 ILE B 385 11762 10777 8511 -1515 -502 -642 C
ATOM 2673 N TYR B 386 7.588 34.572 52.246 1.00114.43 N
ANISOU 2673 N TYR B 386 14767 16215 12495 -1441 -1302 -350 N
ATOM 2674 CA TYR B 386 7.846 33.856 53.495 1.00112.69 C
ANISOU 2674 CA TYR B 386 14419 16280 12118 -1233 -1501 -197 C
ATOM 2675 C TYR B 386 9.121 34.370 54.168 1.00123.51 C
ANISOU 2675 C TYR B 386 15658 17895 13374 -1524 -1897 -283 C
ATOM 2676 O TYR B 386 9.146 34.616 55.378 1.00121.95 O
ANISOU 2676 O TYR B 386 15669 17845 12819 -1483 -2159 -315 O
ATOM 2677 CB TYR B 386 7.959 32.347 53.246 1.00106.10 C
ANISOU 2677 CB TYR B 386 13137 15577 11599 -956 -1352 76 C
ATOM 2678 CG TYR B 386 6.775 31.720 52.532 1.00 99.68 C
ANISOU 2678 CG TYR B 386 12392 14522 10961 -687 -995 162 C
ATOM 2679 CD1 TYR B 386 5.529 32.337 52.523 1.00 93.84 C
ANISOU 2679 CD1 TYR B 386 12096 13520 10040 -599 -854 68 C
ATOM 2680 CD2 TYR B 386 6.905 30.505 51.868 1.00 98.35 C
ANISOU 2680 CD2 TYR B 386 11830 14371 11168 -520 -811 331 C
ATOM 2681 CE1 TYR B 386 4.451 31.765 51.868 1.00 89.73 C
ANISOU 2681 CE1 TYR B 386 11604 12775 9715 -369 -571 154 C
ATOM 2682 CE2 TYR B 386 5.832 29.925 51.213 1.00 94.32 C
ANISOU 2682 CE2 TYR B 386 11379 13628 10832 -296 -528 390 C
ATOM 2683 CZ TYR B 386 4.607 30.559 51.216 1.00 90.69 C
ANISOU 2683 CZ TYR B 386 11341 12922 10194 -228 -425 308 C
ATOM 2684 OH TYR B 386 3.537 29.986 50.566 1.00 87.02 O
ANISOU 2684 OH TYR B 386 10905 12221 9936 -20 -184 374 O
ATOM 2685 N VAL B 387 10.173 34.539 53.371 1.00120.23 N
ANISOU 2685 N VAL B 387 14900 17519 13262 -1824 -1937 -322 N
ATOM 2686 CA VAL B 387 11.461 35.013 53.871 1.00125.35 C
ANISOU 2686 CA VAL B 387 15338 18381 13908 -2139 -2320 -391 C
ATOM 2687 C VAL B 387 11.368 36.446 54.391 1.00132.91 C
ANISOU 2687 C VAL B 387 16762 19206 14530 -2416 -2553 -678 C
ATOM 2688 O VAL B 387 11.970 36.777 55.411 1.00128.14 O
ANISOU 2688 O VAL B 387 16191 18792 13703 -2542 -2949 -750 O
ATOM 2689 CB VAL B 387 12.553 34.933 52.778 1.00118.71 C
ANISOU 2689 CB VAL B 387 14012 17568 13524 -2408 -2235 -363 C
ATOM 2690 CG1 VAL B 387 13.801 35.706 53.189 1.00133.12 C
ANISOU 2690 CG1 VAL B 387 15656 19538 15385 -2807 -2627 -472 C
ATOM 2691 CG2 VAL B 387 12.905 33.483 52.487 1.00119.52 C
ANISOU 2691 CG2 VAL B 387 13600 17845 13966 -2144 -2080 -97 C
ATOM 2692 N VAL B 388 10.612 37.290 53.692 1.00130.59 N
ANISOU 2692 N VAL B 388 16835 18576 14206 -2509 -2324 -843 N
ATOM 2693 CA VAL B 388 10.436 38.674 54.119 1.00119.93 C
ANISOU 2693 CA VAL B 388 15954 17035 12580 -2755 -2501 -1127 C
ATOM 2694 C VAL B 388 9.707 38.749 55.455 1.00122.02 C
ANISOU 2694 C VAL B 388 16639 17353 12371 -2509 -2641 -1196 C
ATOM 2695 O VAL B 388 10.169 39.421 56.375 1.00138.38 O
ANISOU 2695 O VAL B 388 18903 19509 14167 -2692 -2996 -1381 O
ATOM 2696 CB VAL B 388 9.667 39.507 53.078 1.00113.63 C
ANISOU 2696 CB VAL B 388 15467 15838 11869 -2854 -2201 -1246 C
ATOM 2697 CG1 VAL B 388 9.251 40.850 53.674 1.00111.54 C
ANISOU 2697 CG1 VAL B 388 15746 15332 11302 -3012 -2350 -1532 C
ATOM 2698 CG2 VAL B 388 10.521 39.711 51.837 1.00124.25 C
ANISOU 2698 CG2 VAL B 388 16477 17130 13603 -3177 -2099 -1217 C
ATOM 2699 N ALA B 389 8.576 38.060 55.566 1.00112.73 N
ANISOU 2699 N ALA B 389 15609 16124 11100 -2102 -2359 -1052 N
ATOM 2700 CA ALA B 389 7.838 38.029 56.826 1.00112.59 C
ANISOU 2700 CA ALA B 389 15977 16170 10632 -1828 -2416 -1077 C
ATOM 2701 C ALA B 389 8.722 37.494 57.964 1.00132.38 C
ANISOU 2701 C ALA B 389 18298 19081 12919 -1809 -2801 -983 C
ATOM 2702 O ALA B 389 8.770 38.045 59.075 1.00135.32 O
ANISOU 2702 O ALA B 389 19022 19545 12849 -1845 -3071 -1150 O
ATOM 2703 CB ALA B 389 6.585 37.184 56.669 1.00102.87 C
ANISOU 2703 CB ALA B 389 14801 14841 9445 -1394 -2028 -866 C
ATOM 2704 N GLY B 390 9.441 36.422 57.662 1.00150.25 N
ANISOU 2704 N GLY B 390 20011 21581 15496 -1752 -2835 -719 N
ATOM 2705 CA GLY B 390 10.370 35.851 58.615 1.00150.69 C
ANISOU 2705 CA GLY B 390 19806 22022 15427 -1740 -3222 -579 C
ATOM 2706 C GLY B 390 11.413 36.849 59.079 1.00152.37 C
ANISOU 2706 C GLY B 390 20067 22329 15497 -2160 -3697 -829 C
ATOM 2707 O GLY B 390 11.745 36.903 60.261 1.00147.88 O
ANISOU 2707 O GLY B 390 19645 22003 14540 -2152 -4077 -858 O
ATOM 2708 N GLN B 391 11.932 37.641 58.145 1.00150.61 N
ANISOU 2708 N GLN B 391 19726 21911 15588 -2534 -3685 -1005 N
ATOM 2709 CA GLN B 391 12.900 38.685 58.464 1.00147.97 C
ANISOU 2709 CA GLN B 391 19422 21598 15200 -2981 -4118 -1260 C
ATOM 2710 C GLN B 391 12.245 39.738 59.346 1.00145.98 C
ANISOU 2710 C GLN B 391 19859 21191 14417 -3020 -4257 -1584 C
ATOM 2711 O GLN B 391 12.889 40.337 60.207 1.00145.82 O
ANISOU 2711 O GLN B 391 19978 21292 14135 -3257 -4721 -1783 O
ATOM 2712 CB GLN B 391 13.450 39.327 57.188 1.00139.70 C
ANISOU 2712 CB GLN B 391 18133 20322 14626 -3356 -3982 -1352 C
ATOM 2713 N GLY B 392 10.952 39.949 59.122 1.00140.31 N
ANISOU 2713 N GLY B 392 19565 20192 13554 -2779 -3854 -1642 N
ATOM 2714 CA GLY B 392 10.170 40.867 59.928 1.00145.01 C
ANISOU 2714 CA GLY B 392 20829 20606 13664 -2738 -3882 -1936 C
ATOM 2715 C GLY B 392 9.743 40.240 61.241 1.00147.57 C
ANISOU 2715 C GLY B 392 21396 21204 13469 -2381 -3977 -1841 C
ATOM 2716 O GLY B 392 9.048 40.859 62.047 1.00153.94 O
ANISOU 2716 O GLY B 392 22778 21905 13808 -2279 -3964 -2068 O
ATOM 2717 N PHE B 393 10.163 39.002 61.467 1.00144.91 N
ANISOU 2717 N PHE B 393 20629 21216 13216 -2181 -4054 -1496 N
ATOM 2718 CA PHE B 393 9.932 38.370 62.760 1.00148.03 C
ANISOU 2718 CA PHE B 393 21219 21917 13110 -1870 -4198 -1357 C
ATOM 2719 C PHE B 393 11.147 38.505 63.689 1.00149.53 C
ANISOU 2719 C PHE B 393 21318 22451 13045 -2115 -4837 -1427 C
ATOM 2720 O PHE B 393 11.053 38.267 64.895 1.00145.45 O
ANISOU 2720 O PHE B 393 21085 22192 11989 -1933 -5059 -1391 O
ATOM 2721 CB PHE B 393 9.573 36.897 62.571 1.00143.77 C
ANISOU 2721 CB PHE B 393 20301 21536 12789 -1466 -3910 -906 C
ATOM 2722 N GLN B 394 12.284 38.900 63.130 1.00151.03 N
ANISOU 2722 N GLN B 394 21115 22646 13621 -2532 -5138 -1518 N
ATOM 2723 CA GLN B 394 13.511 38.984 63.908 1.00154.17 C
ANISOU 2723 CA GLN B 394 21325 23367 13884 -2792 -5783 -1556 C
ATOM 2724 C GLN B 394 13.437 40.119 64.922 1.00150.94 C
ANISOU 2724 C GLN B 394 21563 22911 12875 -2982 -6139 -1980 C
ATOM 2725 O GLN B 394 14.196 41.083 64.837 1.00148.08 O
ANISOU 2725 O GLN B 394 21179 22430 12655 -3398 -6461 -2277 O
ATOM 2726 CB GLN B 394 14.713 39.173 62.983 1.00150.90 C
ANISOU 2726 CB GLN B 394 20298 22931 14108 -3204 -5966 -1546 C
ATOM 2727 N SER B 400 18.297 30.096 61.661 1.00146.97 N
ANISOU 2727 N SER B 400 15445 23951 16446 -1608 -5696 1343 N
ATOM 2728 CA SER B 400 18.624 29.792 60.273 1.00143.86 C
ANISOU 2728 CA SER B 400 14565 23358 16736 -1672 -5269 1356 C
ATOM 2729 C SER B 400 17.418 29.989 59.360 1.00144.19 C
ANISOU 2729 C SER B 400 15002 23041 16742 -1573 -4661 1175 C
ATOM 2730 O SER B 400 16.307 30.246 59.827 1.00135.72 O
ANISOU 2730 O SER B 400 14520 21871 15175 -1413 -4548 1084 O
ATOM 2731 CB SER B 400 19.145 28.360 60.146 1.00140.33 C
ANISOU 2731 CB SER B 400 13470 23053 16797 -1363 -5189 1776 C
ATOM 2732 OG SER B 400 18.157 27.422 60.536 1.00130.45 O
ANISOU 2732 OG SER B 400 12437 21781 15347 -909 -4943 2017 O
ATOM 2733 N LEU B 401 17.648 29.865 58.056 1.00145.02 N
ANISOU 2733 N LEU B 401 14775 22953 17373 -1665 -4270 1131 N
ATOM 2734 CA LEU B 401 16.592 30.045 57.062 1.00131.18 C
ANISOU 2734 CA LEU B 401 13349 20862 15630 -1598 -3726 967 C
ATOM 2735 C LEU B 401 15.484 28.985 57.171 1.00123.83 C
ANISOU 2735 C LEU B 401 12568 19853 14630 -1125 -3396 1179 C
ATOM 2736 O LEU B 401 14.301 29.343 57.217 1.00122.50 O
ANISOU 2736 O LEU B 401 12933 19493 14118 -1019 -3187 1052 O
ATOM 2737 CB LEU B 401 17.191 30.049 55.649 1.00131.59 C
ANISOU 2737 CB LEU B 401 12989 20765 16245 -1792 -3397 902 C
ATOM 2738 CG LEU B 401 16.367 30.700 54.534 1.00127.25 C
ANISOU 2738 CG LEU B 401 12811 19874 15663 -1900 -2957 652 C
ATOM 2739 CD1 LEU B 401 16.160 32.182 54.805 1.00129.78 C
ANISOU 2739 CD1 LEU B 401 13629 20085 15595 -2238 -3166 348 C
ATOM 2740 CD2 LEU B 401 17.033 30.498 53.184 1.00121.98 C
ANISOU 2740 CD2 LEU B 401 11705 19111 15530 -2040 -2617 645 C
ATOM 2741 N PRO B 402 15.847 27.682 57.215 1.00124.05 N
ANISOU 2741 N PRO B 402 12110 20004 15018 -839 -3340 1510 N
ATOM 2742 CA PRO B 402 14.755 26.712 57.349 1.00121.55 C
ANISOU 2742 CA PRO B 402 11950 19580 14654 -410 -3033 1712 C
ATOM 2743 C PRO B 402 14.028 26.846 58.677 1.00122.62 C
ANISOU 2743 C PRO B 402 12564 19839 14188 -233 -3253 1796 C
ATOM 2744 O PRO B 402 12.815 26.660 58.703 1.00118.32 O
ANISOU 2744 O PRO B 402 12384 19114 13457 3 -2950 1810 O
ATOM 2745 CB PRO B 402 15.467 25.358 57.261 1.00135.53 C
ANISOU 2745 CB PRO B 402 13080 21467 16946 -170 -3005 2056 C
ATOM 2746 CG PRO B 402 16.868 25.639 57.668 1.00137.17 C
ANISOU 2746 CG PRO B 402 12881 21955 17284 -416 -3464 2104 C
ATOM 2747 CD PRO B 402 17.154 27.002 57.122 1.00127.76 C
ANISOU 2747 CD PRO B 402 11878 20675 15992 -864 -3513 1727 C
ATOM 2748 N SER B 403 14.761 27.153 59.747 1.00135.97 N
ANISOU 2748 N SER B 403 14245 21832 15586 -344 -3768 1854 N
ATOM 2749 CA SER B 403 14.168 27.377 61.065 1.00137.32 C
ANISOU 2749 CA SER B 403 14919 22155 15103 -202 -4003 1906 C
ATOM 2750 C SER B 403 13.163 28.523 61.007 1.00136.66 C
ANISOU 2750 C SER B 403 15502 21845 14578 -326 -3831 1543 C
ATOM 2751 O SER B 403 12.039 28.420 61.513 1.00141.13 O
ANISOU 2751 O SER B 403 16506 22334 14784 -65 -3625 1592 O
ATOM 2752 CB SER B 403 15.254 27.672 62.107 1.00139.28 C
ANISOU 2752 CB SER B 403 15056 22765 15098 -379 -4646 1961 C
ATOM 2753 OG SER B 403 14.697 27.668 63.408 1.00151.29 O
ANISOU 2753 OG SER B 403 17048 24466 15968 -180 -4850 2068 O
ATOM 2754 N LEU B 404 13.588 29.612 60.375 1.00124.56 N
ANISOU 2754 N LEU B 404 14019 20191 13116 -723 -3900 1198 N
ATOM 2755 CA LEU B 404 12.740 30.777 60.169 1.00117.61 C
ANISOU 2755 CA LEU B 404 13721 19050 11914 -876 -3737 841 C
ATOM 2756 C LEU B 404 11.462 30.399 59.427 1.00111.59 C
ANISOU 2756 C LEU B 404 13132 17980 11287 -614 -3176 871 C
ATOM 2757 O LEU B 404 10.365 30.793 59.827 1.00107.85 O
ANISOU 2757 O LEU B 404 13174 17368 10435 -473 -3013 778 O
ATOM 2758 CB LEU B 404 13.494 31.859 59.394 1.00115.03 C
ANISOU 2758 CB LEU B 404 13306 18606 11793 -1345 -3850 527 C
ATOM 2759 CG LEU B 404 12.847 33.244 59.306 1.00117.22 C
ANISOU 2759 CG LEU B 404 14177 18624 11736 -1570 -3796 141 C
ATOM 2760 CD1 LEU B 404 12.606 33.787 60.702 1.00131.94 C
ANISOU 2760 CD1 LEU B 404 16543 20634 12953 -1546 -4138 24 C
ATOM 2761 CD2 LEU B 404 13.720 34.195 58.499 1.00121.37 C
ANISOU 2761 CD2 LEU B 404 14529 19036 12550 -2041 -3908 -102 C
ATOM 2762 N LEU B 405 11.607 29.626 58.354 1.00113.86 N
ANISOU 2762 N LEU B 405 12983 18156 12122 -545 -2885 998 N
ATOM 2763 CA LEU B 405 10.451 29.180 57.582 1.00113.57 C
ANISOU 2763 CA LEU B 405 13062 17828 12264 -310 -2397 1031 C
ATOM 2764 C LEU B 405 9.528 28.287 58.409 1.00119.81 C
ANISOU 2764 C LEU B 405 13991 18654 12876 116 -2267 1313 C
ATOM 2765 O LEU B 405 8.304 28.366 58.292 1.00115.57 O
ANISOU 2765 O LEU B 405 13793 17888 12231 288 -1961 1279 O
ATOM 2766 CB LEU B 405 10.908 28.447 56.322 1.00126.04 C
ANISOU 2766 CB LEU B 405 14137 19307 14444 -321 -2148 1101 C
ATOM 2767 CG LEU B 405 11.639 29.310 55.291 1.00122.55 C
ANISOU 2767 CG LEU B 405 13582 18773 14210 -723 -2143 838 C
ATOM 2768 CD1 LEU B 405 12.039 28.474 54.089 1.00113.85 C
ANISOU 2768 CD1 LEU B 405 12012 17587 13659 -682 -1845 919 C
ATOM 2769 CD2 LEU B 405 10.779 30.492 54.867 1.00116.05 C
ANISOU 2769 CD2 LEU B 405 13290 17674 13129 -892 -2000 545 C
ATOM 2770 N ARG B 406 10.125 27.436 59.237 1.00137.61 N
ANISOU 2770 N ARG B 406 15965 21193 15129 286 -2497 1616 N
ATOM 2771 CA ARG B 406 9.373 26.602 60.161 1.00128.62 C
ANISOU 2771 CA ARG B 406 14956 20128 13788 679 -2409 1932 C
ATOM 2772 C ARG B 406 8.512 27.468 61.065 1.00121.22 C
ANISOU 2772 C ARG B 406 14663 19184 12213 711 -2430 1787 C
ATOM 2773 O ARG B 406 7.327 27.191 61.260 1.00115.70 O
ANISOU 2773 O ARG B 406 14225 18327 11408 985 -2104 1890 O
ATOM 2774 CB ARG B 406 10.317 25.733 60.997 1.00119.39 C
ANISOU 2774 CB ARG B 406 13409 19299 12654 806 -2744 2281 C
ATOM 2775 CG ARG B 406 10.981 24.608 60.221 1.00116.45 C
ANISOU 2775 CG ARG B 406 12386 18900 12959 898 -2635 2503 C
ATOM 2776 CD ARG B 406 11.944 23.827 61.100 1.00117.06 C
ANISOU 2776 CD ARG B 406 12085 19310 13080 1024 -3006 2864 C
ATOM 2777 NE ARG B 406 12.562 22.715 60.385 1.00116.78 N
ANISOU 2777 NE ARG B 406 11415 19222 13733 1146 -2871 3083 N
ATOM 2778 CZ ARG B 406 13.773 22.235 60.653 1.00131.31 C
ANISOU 2778 CZ ARG B 406 12753 21301 15836 1127 -3196 3297 C
ATOM 2779 NH1 ARG B 406 14.507 22.779 61.615 1.00135.64 N
ANISOU 2779 NH1 ARG B 406 13359 22174 16007 969 -3718 3322 N
ATOM 2780 NH2 ARG B 406 14.254 21.217 59.954 1.00136.68 N
ANISOU 2780 NH2 ARG B 406 12872 21887 17174 1266 -3007 3477 N
ATOM 2781 N ASN B 407 9.107 28.527 61.606 1.00133.14 N
ANISOU 2781 N ASN B 407 16420 20847 13321 426 -2803 1536 N
ATOM 2782 CA ASN B 407 8.375 29.408 62.505 1.00136.81 C
ANISOU 2782 CA ASN B 407 17526 21305 13151 447 -2834 1352 C
ATOM 2783 C ASN B 407 7.299 30.211 61.768 1.00122.77 C
ANISOU 2783 C ASN B 407 16107 19140 11399 399 -2453 1066 C
ATOM 2784 O ASN B 407 6.257 30.539 62.340 1.00117.70 O
ANISOU 2784 O ASN B 407 15934 18396 10389 582 -2253 1021 O
ATOM 2785 CB ASN B 407 9.340 30.348 63.239 1.00141.73 C
ANISOU 2785 CB ASN B 407 18324 22167 13362 128 -3367 1118 C
ATOM 2786 CG ASN B 407 9.993 29.686 64.452 1.00158.90 C
ANISOU 2786 CG ASN B 407 20394 24749 15231 269 -3765 1416 C
ATOM 2787 OD1 ASN B 407 9.452 28.732 65.013 1.00162.10 O
ANISOU 2787 OD1 ASN B 407 20801 25247 15543 642 -3598 1773 O
ATOM 2788 ND2 ASN B 407 11.149 30.198 64.867 1.00167.29 N
ANISOU 2788 ND2 ASN B 407 21364 26052 16147 -35 -4308 1287 N
ATOM 2789 N VAL B 408 7.539 30.514 60.494 1.00121.48 N
ANISOU 2789 N VAL B 408 15721 18760 11677 167 -2340 892 N
ATOM 2790 CA VAL B 408 6.598 31.338 59.734 1.00114.03 C
ANISOU 2790 CA VAL B 408 15105 17451 10773 94 -2032 633 C
ATOM 2791 C VAL B 408 5.379 30.539 59.277 1.00110.56 C
ANISOU 2791 C VAL B 408 14635 16781 10589 434 -1579 833 C
ATOM 2792 O VAL B 408 4.246 31.015 59.367 1.00106.03 O
ANISOU 2792 O VAL B 408 14453 15983 9850 555 -1333 741 O
ATOM 2793 CB VAL B 408 7.269 31.985 58.501 1.00114.48 C
ANISOU 2793 CB VAL B 408 14965 17355 11178 -284 -2067 395 C
ATOM 2794 CG1 VAL B 408 6.227 32.645 57.607 1.00118.83 C
ANISOU 2794 CG1 VAL B 408 15805 17517 11826 -309 -1729 207 C
ATOM 2795 CG2 VAL B 408 8.298 33.008 58.937 1.00116.48 C
ANISOU 2795 CG2 VAL B 408 15316 17754 11187 -658 -2493 148 C
ATOM 2796 N LEU B 409 5.611 29.320 58.803 1.00115.72 N
ANISOU 2796 N LEU B 409 14813 17477 11677 588 -1473 1106 N
ATOM 2797 CA LEU B 409 4.542 28.505 58.235 1.00121.42 C
ANISOU 2797 CA LEU B 409 15448 17955 12731 869 -1076 1280 C
ATOM 2798 C LEU B 409 3.897 27.587 59.269 1.00130.79 C
ANISOU 2798 C LEU B 409 16668 19244 13783 1258 -959 1628 C
ATOM 2799 O LEU B 409 3.476 26.476 58.945 1.00126.82 O
ANISOU 2799 O LEU B 409 15880 18641 13666 1499 -732 1886 O
ATOM 2800 CB LEU B 409 5.081 27.676 57.068 1.00121.37 C
ANISOU 2800 CB LEU B 409 14934 17885 13298 825 -988 1354 C
ATOM 2801 CG LEU B 409 5.876 28.471 56.030 1.00114.16 C
ANISOU 2801 CG LEU B 409 13932 16911 12532 441 -1083 1062 C
ATOM 2802 CD1 LEU B 409 6.435 27.560 54.948 1.00117.75 C
ANISOU 2802 CD1 LEU B 409 13894 17327 13519 434 -956 1144 C
ATOM 2803 CD2 LEU B 409 5.010 29.563 55.426 1.00109.50 C
ANISOU 2803 CD2 LEU B 409 13755 16022 11829 305 -924 790 C
ATOM 2804 N THR B 410 3.819 28.053 60.512 1.00134.15 N
ANISOU 2804 N THR B 410 17456 19859 13658 1316 -1107 1631 N
ATOM 2805 CA THR B 410 3.227 27.263 61.586 1.00121.73 C
ANISOU 2805 CA THR B 410 15966 18409 11876 1682 -983 1980 C
ATOM 2806 C THR B 410 2.662 28.154 62.687 1.00115.88 C
ANISOU 2806 C THR B 410 15816 17733 10481 1737 -984 1850 C
ATOM 2807 O THR B 410 1.489 28.046 63.046 1.00121.83 O
ANISOU 2807 O THR B 410 16814 18338 11138 2002 -637 1963 O
ATOM 2808 CB THR B 410 4.251 26.290 62.201 1.00122.13 C
ANISOU 2808 CB THR B 410 15652 18800 11951 1767 -1263 2304 C
ATOM 2809 OG1 THR B 410 4.634 25.313 61.226 1.00112.28 O
ANISOU 2809 OG1 THR B 410 13855 17454 11351 1791 -1178 2455 O
ATOM 2810 CG2 THR B 410 3.654 25.582 63.408 1.00135.87 C
ANISOU 2810 CG2 THR B 410 17547 20687 13390 2134 -1148 2683 C
TER 2811 THR B 410
HETATM 2812 C ACE L 0 -3.580 29.678 14.202 1.00100.43 C
HETATM 2813 O ACE L 0 -3.704 29.766 15.423 1.00 98.63 O
HETATM 2814 CH3 ACE L 0 -4.630 30.175 13.253 1.00120.91 C
ATOM 2815 N PHE L 1 -2.511 29.130 13.633 1.00104.99 N
ATOM 2816 CA PHE L 1 -1.400 28.639 14.438 1.00 92.08 C
ATOM 2817 C PHE L 1 -0.650 29.796 15.086 1.00 91.00 C
ATOM 2818 O PHE L 1 -0.541 30.879 14.511 1.00 98.03 O
ATOM 2819 CB PHE L 1 -0.442 27.801 13.588 1.00 75.81 C
ATOM 2820 CG PHE L 1 0.754 27.295 14.344 1.00 71.79 C
ATOM 2821 CD1 PHE L 1 0.648 26.196 15.181 1.00 71.64 C
ATOM 2822 CD2 PHE L 1 1.986 27.919 14.219 1.00 68.89 C
ATOM 2823 CE1 PHE L 1 1.746 25.729 15.879 1.00 65.85 C
ATOM 2824 CE2 PHE L 1 3.088 27.456 14.915 1.00 67.14 C
ATOM 2825 CZ PHE L 1 2.967 26.359 15.745 1.00 62.03 C
HETATM 2826 N ORN L 2 -0.136 29.559 16.287 1.00 89.14 N
HETATM 2827 CA ORN L 2 0.607 30.577 17.014 1.00 91.28 C
HETATM 2828 CB ORN L 2 -0.356 31.508 17.753 1.00 90.39 C
HETATM 2829 CG ORN L 2 0.264 32.819 18.197 1.00 87.49 C
HETATM 2830 CD ORN L 2 -0.720 33.777 18.848 1.00106.24 C
HETATM 2831 NE ORN L 2 -1.148 33.313 20.164 1.00 96.94 N
HETATM 2832 C ORN L 2 1.567 29.922 17.997 1.00 99.56 C
HETATM 2833 O ORN L 2 1.140 29.199 18.896 1.00126.73 O
ATOM 2834 N PRO L 3 2.873 30.173 17.827 1.00 87.38 N
ATOM 2835 CA PRO L 3 3.894 29.577 18.695 1.00 91.74 C
ATOM 2836 C PRO L 3 3.816 30.105 20.124 1.00108.78 C
ATOM 2837 O PRO L 3 3.403 31.245 20.339 1.00115.02 O
ATOM 2838 CB PRO L 3 5.207 29.996 18.029 1.00 84.57 C
ATOM 2839 CG PRO L 3 4.871 31.256 17.310 1.00 79.82 C
ATOM 2840 CD PRO L 3 3.462 31.074 16.821 1.00 81.32 C
HETATM 2841 C1 ZAL L 4 6.491 28.676 22.255 1.00 77.48 C
HETATM 2842 C2 ZAL L 4 7.260 29.966 22.008 1.00 86.50 C
HETATM 2843 C3 ZAL L 4 8.222 30.333 23.116 1.00 82.27 C
HETATM 2844 C4 ZAL L 4 9.129 29.175 23.479 1.00 78.09 C
HETATM 2845 C5 ZAL L 4 8.312 27.970 23.892 1.00 81.32 C
HETATM 2846 C6 ZAL L 4 7.344 27.543 22.810 1.00 92.85 C
HETATM 2847 N ZAL L 4 4.203 29.277 21.088 1.00 91.84 N
HETATM 2848 CA ZAL L 4 4.221 29.682 22.451 1.00 79.60 C
HETATM 2849 CB ZAL L 4 5.316 28.947 23.197 1.00 74.88 C
HETATM 2850 C ZAL L 4 2.884 29.393 23.094 1.00 74.01 C
HETATM 2851 O ZAL L 4 2.375 28.243 23.024 1.00 70.97 O
ATOM 2852 N TRP L 5 2.295 30.412 23.712 1.00 79.31 N
ATOM 2853 CA TRP L 5 1.061 30.237 24.470 1.00 84.33 C
ATOM 2854 C TRP L 5 -0.127 30.953 23.831 1.00 74.42 C
ATOM 2855 O TRP L 5 -1.251 30.451 23.857 1.00 68.71 O
ATOM 2856 CB TRP L 5 1.261 30.721 25.907 1.00 87.78 C
ATOM 2857 CG TRP L 5 2.233 29.876 26.676 1.00 87.15 C
ATOM 2858 CD1 TRP L 5 1.948 28.753 27.396 1.00 79.93 C
ATOM 2859 CD2 TRP L 5 3.648 30.079 26.793 1.00 84.77 C
ATOM 2860 NE1 TRP L 5 3.094 28.246 27.958 1.00 81.34 N
ATOM 2861 CE2 TRP L 5 4.152 29.041 27.603 1.00 80.79 C
ATOM 2862 CE3 TRP L 5 4.537 31.036 26.294 1.00 79.43 C
ATOM 2863 CZ2 TRP L 5 5.503 28.935 27.926 1.00 75.77 C
ATOM 2864 CZ3 TRP L 5 5.878 30.929 26.617 1.00 71.97 C
ATOM 2865 CH2 TRP L 5 6.348 29.886 27.424 1.00 69.29 C
ATOM 2866 N ARG L 6 0.121 32.132 23.270 1.00 78.38 N
ATOM 2867 CA ARG L 6 -0.910 32.858 22.535 1.00 86.45 C
ATOM 2868 C ARG L 6 -0.349 33.393 21.223 1.00 95.16 C
ATOM 2869 O ARG L 6 0.783 33.875 21.173 1.00 97.30 O
ATOM 2870 CB ARG L 6 -1.481 34.008 23.369 1.00 89.00 C
ATOM 2871 CG ARG L 6 -2.446 33.585 24.469 1.00 93.30 C
ATOM 2872 CD ARG L 6 -1.713 33.229 25.751 1.00 92.22 C
ATOM 2873 NE ARG L 6 -0.788 34.284 26.150 1.00 91.04 N
ATOM 2874 CZ ARG L 6 -1.123 35.325 26.905 1.00 96.69 C
ATOM 2875 NH1 ARG L 6 -0.215 36.238 27.218 1.00 91.07 N
ATOM 2876 NH2 ARG L 6 -2.365 35.448 27.353 1.00 96.91 N
TER 2877 ARG L 6
HETATM 2878 C15 9P2 B 501 -15.925 28.241 39.572 1.00 75.23 C
HETATM 2879 C16 9P2 B 501 -14.479 28.243 39.480 1.00114.18 C
HETATM 2880 C17 9P2 B 501 -13.743 27.193 40.029 1.00 82.04 C
HETATM 2881 C18 9P2 B 501 -14.399 26.089 40.691 1.00 66.20 C
HETATM 2882 C20 9P2 B 501 -12.332 28.515 38.951 1.00 69.46 C
HETATM 2883 C01 9P2 B 501 -14.723 28.755 43.517 1.00 57.14 C
HETATM 2884 N02 9P2 B 501 -15.997 29.223 43.244 1.00 37.75 N
HETATM 2885 C03 9P2 B 501 -16.922 28.171 43.335 1.00 81.18 C
HETATM 2886 C04 9P2 B 501 -16.142 27.003 43.692 1.00 51.12 C
HETATM 2887 N05 9P2 B 501 -14.795 27.402 43.771 1.00107.27 N
HETATM 2888 C06 9P2 B 501 -13.648 26.477 44.137 1.00 90.71 C
HETATM 2889 C07 9P2 B 501 -13.791 26.130 45.630 1.00 78.74 C
HETATM 2890 C08 9P2 B 501 -12.475 26.236 46.418 1.00 88.39 C
HETATM 2891 C09 9P2 B 501 -12.697 26.137 47.933 1.00 55.87 C
HETATM 2892 C10 9P2 B 501 -16.717 25.520 43.885 1.00 55.13 C
HETATM 2893 N11 9P2 B 501 -16.071 24.646 42.829 1.00 78.06 N
HETATM 2894 C12 9P2 B 501 -16.587 24.942 41.466 1.00 59.64 C
HETATM 2895 C13 9P2 B 501 -15.833 26.077 40.779 1.00 79.83 C
HETATM 2896 C14 9P2 B 501 -16.575 27.157 40.217 1.00 71.86 C
HETATM 2897 O19 9P2 B 501 -12.367 27.487 39.780 1.00 84.31 O
HETATM 2898 O21 9P2 B 501 -13.550 29.138 38.926 1.00 83.40 O
HETATM 2899 C22 9P2 B 501 -16.228 23.194 43.153 1.00 39.13 C
HETATM 2900 C23 9P2 B 501 -15.251 22.767 44.273 1.00 55.27 C
HETATM 2901 C24 9P2 B 501 -13.845 22.938 44.110 1.00 60.98 C
HETATM 2902 C25 9P2 B 501 -12.963 22.528 45.182 1.00 61.44 C
HETATM 2903 O26 9P2 B 501 -11.550 22.582 45.290 1.00 51.74 O
HETATM 2904 C27 9P2 B 501 -11.275 22.358 46.692 1.00102.72 C
HETATM 2905 O28 9P2 B 501 -12.390 21.668 47.229 1.00 93.02 O
HETATM 2906 C29 9P2 B 501 -13.480 21.968 46.370 1.00 65.31 C
HETATM 2907 C30 9P2 B 501 -14.898 21.794 46.537 1.00 49.28 C
HETATM 2908 C31 9P2 B 501 -15.765 22.191 45.496 1.00 42.26 C
HETATM 2909 C32 9P2 B 501 -18.481 28.174 43.130 1.00100.76 C
HETATM 2910 C33 9P2 B 501 -19.092 28.643 41.939 1.00 92.16 C
HETATM 2911 C34 9P2 B 501 -20.491 28.612 41.802 1.00118.27 C
HETATM 2912 C35 9P2 B 501 -21.287 28.115 42.835 1.00119.67 C
HETATM 2913 C36 9P2 B 501 -20.691 27.643 44.020 1.00 63.95 C
HETATM 2914 C37 9P2 B 501 -19.296 27.678 44.152 1.00 61.13 C
HETATM 2915 C38 9P2 B 501 -13.427 29.639 43.482 1.00 78.03 C
HETATM 2916 C39 9P2 B 501 -12.242 29.170 42.918 1.00 55.22 C
HETATM 2917 C40 9P2 B 501 -11.100 29.957 42.862 1.00 50.87 C
HETATM 2918 C41 9P2 B 501 -11.150 31.264 43.364 1.00 69.66 C
HETATM 2919 C42 9P2 B 501 -12.325 31.749 43.905 1.00 69.21 C
HETATM 2920 C43 9P2 B 501 -13.460 30.960 43.959 1.00 78.91 C
CONECT 1216 1826
CONECT 1476 1488
CONECT 1488 1476 1489
CONECT 1489 1488 1490 1496
CONECT 1490 1489 1491
CONECT 1491 1490 1492
CONECT 1492 1491 1493
CONECT 1493 1492 1494 1495
CONECT 1494 1493
CONECT 1495 1493
CONECT 1496 1489 1497 1498
CONECT 1497 1496
CONECT 1498 1496
CONECT 1826 1216
CONECT 2812 2813 2814 2815
CONECT 2813 2812
CONECT 2814 2812
CONECT 2815 2812
CONECT 2817 2826
CONECT 2826 2817 2827
CONECT 2827 2826 2828 2832
CONECT 2828 2827 2829
CONECT 2829 2828 2830
CONECT 2830 2829 2831
CONECT 2831 2830 2868
CONECT 2832 2827 2833 2834
CONECT 2833 2832
CONECT 2834 2832
CONECT 2836 2847
CONECT 2841 2842 2846 2849
CONECT 2842 2841 2843
CONECT 2843 2842 2844
CONECT 2844 2843 2845
CONECT 2845 2844 2846
CONECT 2846 2841 2845
CONECT 2847 2836 2848
CONECT 2848 2847 2849 2850
CONECT 2849 2841 2848
CONECT 2850 2848 2851 2852
CONECT 2851 2850
CONECT 2852 2850
CONECT 2868 2831
CONECT 2878 2879 2896
CONECT 2879 2878 2880 2898
CONECT 2880 2879 2881 2897
CONECT 2881 2880 2895
CONECT 2882 2897 2898
CONECT 2883 2884 2887 2915
CONECT 2884 2883 2885
CONECT 2885 2884 2886 2909
CONECT 2886 2885 2887 2892
CONECT 2887 2883 2886 2888
CONECT 2888 2887 2889
CONECT 2889 2888 2890
CONECT 2890 2889 2891
CONECT 2891 2890
CONECT 2892 2886 2893
CONECT 2893 2892 2894 2899
CONECT 2894 2893 2895
CONECT 2895 2881 2894 2896
CONECT 2896 2878 2895
CONECT 2897 2880 2882
CONECT 2898 2879 2882
CONECT 2899 2893 2900
CONECT 2900 2899 2901 2908
CONECT 2901 2900 2902
CONECT 2902 2901 2903 2906
CONECT 2903 2902 2904
CONECT 2904 2903 2905
CONECT 2905 2904 2906
CONECT 2906 2902 2905 2907
CONECT 2907 2906 2908
CONECT 2908 2900 2907
CONECT 2909 2885 2910 2914
CONECT 2910 2909 2911
CONECT 2911 2910 2912
CONECT 2912 2911 2913
CONECT 2913 2912 2914
CONECT 2914 2909 2913
CONECT 2915 2883 2916 2920
CONECT 2916 2915 2917
CONECT 2917 2916 2918
CONECT 2918 2917 2919
CONECT 2919 2918 2920
CONECT 2920 2915 2919
MASTER 430 0 5 17 3 0 7 6 2918 2 85 34
END