HEADER HYDROLASE/HYDROLASE INHIBITOR 16-APR-19 6OL9
TITLE STRUCTURE OF THE M5 MUSCARINIC ACETYLCHOLINE RECEPTOR (M5-T4L) BOUND
TITLE 2 TO TIOTROPIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M5, T4 LYSOZYME FUSION;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LYSIS PROTEIN,LYSOZYME,MURAMIDASE;
COMPND 5 EC: 3.2.1.17;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 10665;
SOURCE 5 GENE: CHRM5, E, T4TP126;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS GPCR INHIBITOR COMPLEX, MEMBRANE PROTEIN, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.VUCKOVIC,A.CHRISTOPOULOS,D.M.THAL
REVDAT 2 01-JAN-20 6OL9 1 JRNL
REVDAT 1 11-DEC-19 6OL9 0
JRNL AUTH Z.VUCKOVIC,P.R.GENTRY,A.E.BERIZZI,K.HIRATA,S.VARGHESE,
JRNL AUTH 2 G.THOMPSON,E.T.VAN DER WESTHUIZEN,W.A.C.BURGER,R.RAHMANI,
JRNL AUTH 3 C.VALANT,C.J.LANGMEAD,C.W.LINDSLEY,J.B.BAELL,A.B.TOBIN,
JRNL AUTH 4 P.M.SEXTON,A.CHRISTOPOULOS,D.M.THAL
JRNL TITL CRYSTAL STRUCTURE OF THE M5MUSCARINIC ACETYLCHOLINE
JRNL TITL 2 RECEPTOR.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 26001 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31772027
JRNL DOI 10.1073/PNAS.1914446116
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.16_3549
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) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 17928
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 882
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 47.9000 - 4.6169 1.00 2940 143 0.2401 0.2510
REMARK 3 2 4.6169 - 3.6650 1.00 2866 150 0.2181 0.2583
REMARK 3 3 3.6650 - 3.2018 1.00 2850 147 0.2382 0.2370
REMARK 3 4 3.2018 - 2.9091 1.00 2864 138 0.2426 0.2689
REMARK 3 5 2.9091 - 2.7006 1.00 2845 160 0.2527 0.2865
REMARK 3 6 2.7006 - 2.5414 0.95 2681 144 0.2756 0.2985
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.86
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 26:202 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.827 18.904 -46.705
REMARK 3 T TENSOR
REMARK 3 T11: 0.4129 T22: 0.3718
REMARK 3 T33: 0.3620 T12: -0.0139
REMARK 3 T13: -0.0624 T23: -0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 3.0944 L22: 2.6978
REMARK 3 L33: 4.1696 L12: -0.0025
REMARK 3 L13: -0.8999 L23: 0.4669
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: 0.0157 S13: -0.0460
REMARK 3 S21: 0.2050 S22: -0.1221 S23: -0.0874
REMARK 3 S31: 0.4012 S32: 0.1304 S33: 0.1439
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 203-224 OR 1001:1009 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.731 31.234 -67.005
REMARK 3 T TENSOR
REMARK 3 T11: 0.8339 T22: 0.8388
REMARK 3 T33: 0.6298 T12: 0.0161
REMARK 3 T13: 0.0762 T23: 0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 4.1451 L22: 4.2837
REMARK 3 L33: 3.2459 L12: -0.1867
REMARK 3 L13: -2.2509 L23: 3.0398
REMARK 3 S TENSOR
REMARK 3 S11: 0.1609 S12: 1.3137 S13: 0.4685
REMARK 3 S21: -1.3665 S22: -0.2134 S23: -0.0666
REMARK 3 S31: -1.8562 S32: 0.2412 S33: 0.0003
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 1010:1029 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.188 21.500 -73.760
REMARK 3 T TENSOR
REMARK 3 T11: 0.8337 T22: 1.4808
REMARK 3 T33: 0.9605 T12: 0.1079
REMARK 3 T13: 0.1958 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 6.9833 L22: 8.6242
REMARK 3 L33: 6.0509 L12: 3.7389
REMARK 3 L13: 3.5890 L23: -3.3578
REMARK 3 S TENSOR
REMARK 3 S11: 0.4656 S12: 0.6940 S13: -0.1032
REMARK 3 S21: -2.0538 S22: 0.5891 S23: -1.2284
REMARK 3 S31: 0.8494 S32: 0.6676 S33: -0.8713
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 1030:1078 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.428 32.898 -82.042
REMARK 3 T TENSOR
REMARK 3 T11: 0.5780 T22: 1.5453
REMARK 3 T33: 0.9700 T12: -0.2085
REMARK 3 T13: 0.1308 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 2.5544 L22: 3.7180
REMARK 3 L33: 9.3077 L12: 1.0729
REMARK 3 L13: 4.5664 L23: 0.4007
REMARK 3 S TENSOR
REMARK 3 S11: -1.0556 S12: -0.1250 S13: 1.4293
REMARK 3 S21: -0.9315 S22: -0.5351 S23: 0.0579
REMARK 3 S31: 0.2745 S32: 0.2361 S33: 1.1157
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 1079:1124 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.363 26.556 -97.263
REMARK 3 T TENSOR
REMARK 3 T11: 1.9728 T22: 1.3278
REMARK 3 T33: 0.9235 T12: 0.2686
REMARK 3 T13: 0.5347 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 3.4481 L22: 3.6668
REMARK 3 L33: 2.3203 L12: 1.8651
REMARK 3 L13: 1.3236 L23: -0.1633
REMARK 3 S TENSOR
REMARK 3 S11: 0.0442 S12: 0.4441 S13: -0.3177
REMARK 3 S21: -2.2999 S22: 0.4024 S23: -1.0673
REMARK 3 S31: -0.7894 S32: 0.5689 S33: -0.3676
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN A AND RESID 1125:1157 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.431 20.770 -91.583
REMARK 3 T TENSOR
REMARK 3 T11: 1.8108 T22: 1.0285
REMARK 3 T33: 0.8715 T12: -0.0755
REMARK 3 T13: 0.1301 T23: 0.0714
REMARK 3 L TENSOR
REMARK 3 L11: 6.7510 L22: 4.9128
REMARK 3 L33: 2.0926 L12: -1.1209
REMARK 3 L13: -1.3494 L23: 3.0843
REMARK 3 S TENSOR
REMARK 3 S11: 0.3307 S12: -0.0383 S13: -1.2015
REMARK 3 S21: -2.1358 S22: -0.0132 S23: 0.5034
REMARK 3 S31: 0.2092 S32: -1.3891 S33: -0.1645
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN A AND RESID 466:1158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.533 30.803 -57.017
REMARK 3 T TENSOR
REMARK 3 T11: 0.4268 T22: 0.6918
REMARK 3 T33: 0.4457 T12: 0.0082
REMARK 3 T13: -0.0526 T23: -0.0431
REMARK 3 L TENSOR
REMARK 3 L11: 2.1076 L22: 3.7482
REMARK 3 L33: 4.8872 L12: 0.4068
REMARK 3 L13: -2.1557 L23: 0.8183
REMARK 3 S TENSOR
REMARK 3 S11: 0.2862 S12: 0.8042 S13: -0.0125
REMARK 3 S21: -0.3637 S22: 0.0752 S23: 0.0530
REMARK 3 S31: -0.0051 S32: 0.4622 S33: -0.4278
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN A AND RESID 467:513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.943 29.117 -50.090
REMARK 3 T TENSOR
REMARK 3 T11: 0.3658 T22: 0.5066
REMARK 3 T33: 0.4436 T12: 0.0936
REMARK 3 T13: 0.0282 T23: -0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 4.3546 L22: 3.6786
REMARK 3 L33: 6.5973 L12: -0.1483
REMARK 3 L13: -0.5111 L23: 0.3514
REMARK 3 S TENSOR
REMARK 3 S11: 0.1250 S12: 0.8100 S13: 0.1868
REMARK 3 S21: -0.1018 S22: -0.2149 S23: 0.2405
REMARK 3 S31: 0.0551 S32: -0.2660 S33: 0.0005
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 6OL9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1000240754.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL32XU
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 : F
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17944
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 48.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 56.50
REMARK 200 R MERGE (I) : 0.30200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 41.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: 4U15
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RECONSTITUTED IN 10:1
REMARK 280 MONOOLEIN:CHOLESTEROL MIX, 100 MM D-L MALIC ACID PH 6.0, 220-280
REMARK 280 MM AMMONIUM TARTRATE DIBASIC, 37-41% PEG 400, LIPIDIC CUBIC
REMARK 280 PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 48.53000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.65500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 48.53000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.65500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 19
REMARK 465 ALA A 20
REMARK 465 PRO A 21
REMARK 465 LEU A 22
REMARK 465 GLU A 23
REMARK 465 ARG A 24
REMARK 465 HIS A 25
REMARK 465 LEU A 1032
REMARK 465 THR A 1033
REMARK 465 LYS A 1034
REMARK 465 SER A 1035
REMARK 465 PRO A 1036
REMARK 465 SER A 1037
REMARK 465 LEU A 1038
REMARK 465 ASN A 1039
REMARK 465 ALA A 1040
REMARK 465 ALA A 1041
REMARK 465 LYS A 1042
REMARK 465 SER A 1043
REMARK 465 GLU A 1044
REMARK 465 LEU A 1045
REMARK 465 ASP A 1046
REMARK 465 LYS A 1047
REMARK 465 ALA A 1048
REMARK 465 ILE A 1049
REMARK 465 GLY A 1050
REMARK 465 ARG A 1051
REMARK 465 ASN A 1052
REMARK 465 CYS A 1053
REMARK 465 ASN A 1054
REMARK 465 GLY A 1055
REMARK 465 VAL A 1056
REMARK 465 ILE A 1057
REMARK 465 TRP A 514
REMARK 465 LYS A 515
REMARK 465 LYS A 516
REMARK 465 LYS A 517
REMARK 465 LYS A 518
REMARK 465 VAL A 519
REMARK 465 GLU A 520
REMARK 465 GLU A 521
REMARK 465 LYS A 522
REMARK 465 LEU A 523
REMARK 465 TYR A 524
REMARK 465 TRP A 525
REMARK 465 GLN A 526
REMARK 465 GLY A 527
REMARK 465 ASN A 528
REMARK 465 SER A 529
REMARK 465 LYS A 530
REMARK 465 LEU A 531
REMARK 465 PRO A 532
REMARK 465 SER A 533
REMARK 465 SER A 534
REMARK 465 HIS A 535
REMARK 465 HIS A 536
REMARK 465 HIS A 537
REMARK 465 HIS A 538
REMARK 465 HIS A 539
REMARK 465 HIS A 540
REMARK 465 HIS A 541
REMARK 465 HIS A 542
REMARK 465 HIS A 543
REMARK 465 HIS A 544
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 26 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 60 CG CD OE1 NE2
REMARK 470 LEU A 172 CG CD1 CD2
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 ARG A 176 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 178 CG1 CG2
REMARK 470 LEU A 180 CG CD1 CD2
REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2
REMARK 470 THR A 220 OG1 CG2
REMARK 470 LYS A 222 CG CD CE NZ
REMARK 470 ARG A 223 CG CD NE CZ NH1 NH2
REMARK 470 ASN A1001 CG OD1 ND2
REMARK 470 ILE A1002 CG1 CG2 CD1
REMARK 470 GLU A1010 CG CD OE1 OE2
REMARK 470 LEU A1014 CG CD1 CD2
REMARK 470 ILE A1016 CG1 CG2 CD1
REMARK 470 LYS A1018 CG CD CE NZ
REMARK 470 GLU A1021 CG CD OE1 OE2
REMARK 470 TYR A1024 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A1059 CG CD CE NZ
REMARK 470 ASP A1060 CG OD1 OD2
REMARK 470 GLU A1063 CG CD OE1 OE2
REMARK 470 LYS A1064 CG CD CE NZ
REMARK 470 GLN A1068 CG CD OE1 NE2
REMARK 470 LEU A1078 CG CD1 CD2
REMARK 470 ARG A1079 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1084 CG CD CE NZ
REMARK 470 MET A1105 CG SD CE
REMARK 470 GLU A1107 CG CD OE1 OE2
REMARK 470 VAL A1110 CG1 CG2
REMARK 470 GLN A1122 CG CD OE1 NE2
REMARK 470 ARG A1124 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1127 CG CD OE1 OE2
REMARK 470 ASN A1131 CG OD1 ND2
REMARK 470 LYS A1134 CG CD CE NZ
REMARK 470 GLN A1140 CG CD OE1 NE2
REMARK 470 LYS A1146 CG CD CE NZ
REMARK 470 ARG A 431 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 438 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 439 CG CD CE NZ
REMARK 470 ASP A 469 CG OD1 OD2
REMARK 470 LYS A 470 CG CD CE NZ
REMARK 470 ARG A 500 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 504 CG CD CE NZ
REMARK 470 ARG A 513 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 202 -51.75 -130.54
REMARK 500 ASP A1019 -168.25 -75.63
REMARK 500 ILE A1028 69.17 -108.67
REMARK 500 GLU A1061 77.51 -103.11
REMARK 500 PHE A1113 56.34 -92.63
REMARK 500 PHE A 467 34.05 -96.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLA A 1201
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 0HK A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P33 A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1205
DBREF 6OL9 A 21 224 UNP P08912 ACM5_HUMAN 21 224
DBREF 6OL9 A 1001 1160 UNP D9IEF7 D9IEF7_BPT4 2 161
DBREF 6OL9 A 431 532 UNP P08912 ACM5_HUMAN 431 532
SEQADV 6OL9 GLY A 19 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 ALA A 20 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 ARG A 117 UNP P08912 SER 117 CONFLICT
SEQADV 6OL9 ALA A 1096 UNP D9IEF7 CYS 97 CONFLICT
SEQADV 6OL9 SER A 533 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 SER A 534 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 535 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 536 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 537 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 538 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 539 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 540 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 541 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 542 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 543 UNP P08912 EXPRESSION TAG
SEQADV 6OL9 HIS A 544 UNP P08912 EXPRESSION TAG
SEQRES 1 A 480 GLY ALA PRO LEU GLU ARG HIS ARG LEU TRP GLU VAL ILE
SEQRES 2 A 480 THR ILE ALA ALA VAL THR ALA VAL VAL SER LEU ILE THR
SEQRES 3 A 480 ILE VAL GLY ASN VAL LEU VAL MET ILE SER PHE LYS VAL
SEQRES 4 A 480 ASN SER GLN LEU LYS THR VAL ASN ASN TYR TYR LEU LEU
SEQRES 5 A 480 SER LEU ALA CYS ALA ASP LEU ILE ILE GLY ILE PHE SER
SEQRES 6 A 480 MET ASN LEU TYR THR THR TYR ILE LEU MET GLY ARG TRP
SEQRES 7 A 480 ALA LEU GLY SER LEU ALA CYS ASP LEU TRP LEU ALA LEU
SEQRES 8 A 480 ASP TYR VAL ALA SER ASN ALA ARG VAL MET ASN LEU LEU
SEQRES 9 A 480 VAL ILE SER PHE ASP ARG TYR PHE SER ILE THR ARG PRO
SEQRES 10 A 480 LEU THR TYR ARG ALA LYS ARG THR PRO LYS ARG ALA GLY
SEQRES 11 A 480 ILE MET ILE GLY LEU ALA TRP LEU ILE SER PHE ILE LEU
SEQRES 12 A 480 TRP ALA PRO ALA ILE LEU CYS TRP GLN TYR LEU VAL GLY
SEQRES 13 A 480 LYS ARG THR VAL PRO LEU ASP GLU CYS GLN ILE GLN PHE
SEQRES 14 A 480 LEU SER GLU PRO THR ILE THR PHE GLY THR ALA ILE ALA
SEQRES 15 A 480 ALA PHE TYR ILE PRO VAL SER VAL MET THR ILE LEU TYR
SEQRES 16 A 480 CYS ARG ILE TYR ARG GLU THR GLU LYS ARG THR ASN ILE
SEQRES 17 A 480 PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG LEU LYS
SEQRES 18 A 480 ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE GLY ILE
SEQRES 19 A 480 GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN ALA ALA
SEQRES 20 A 480 LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN CYS ASN
SEQRES 21 A 480 GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU PHE ASN
SEQRES 22 A 480 GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU ARG ASN
SEQRES 23 A 480 ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP ALA VAL
SEQRES 24 A 480 ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN MET GLY
SEQRES 25 A 480 GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU ARG MET
SEQRES 26 A 480 LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL ASN LEU
SEQRES 27 A 480 ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN ARG ALA
SEQRES 28 A 480 LYS ARG VAL ILE THR THR PHE ARG THR GLY THR TRP ASP
SEQRES 29 A 480 ALA TYR ARG VAL VAL LEU VAL LYS GLU ARG LYS ALA ALA
SEQRES 30 A 480 GLN THR LEU SER ALA ILE LEU LEU ALA PHE ILE ILE THR
SEQRES 31 A 480 TRP THR PRO TYR ASN ILE MET VAL LEU VAL SER THR PHE
SEQRES 32 A 480 CYS ASP LYS CYS VAL PRO VAL THR LEU TRP HIS LEU GLY
SEQRES 33 A 480 TYR TRP LEU CYS TYR VAL ASN SER THR VAL ASN PRO ILE
SEQRES 34 A 480 CYS TYR ALA LEU CYS ASN ARG THR PHE ARG LYS THR PHE
SEQRES 35 A 480 LYS MET LEU LEU LEU CYS ARG TRP LYS LYS LYS LYS VAL
SEQRES 36 A 480 GLU GLU LYS LEU TYR TRP GLN GLY ASN SER LYS LEU PRO
SEQRES 37 A 480 SER SER HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET OLA A1201 12
HET OLA A1202 20
HET 0HK A1203 26
HET P33 A1204 22
HET OLC A1205 25
HETNAM OLA OLEIC ACID
HETNAM 0HK (1R,2R,4S,5S,7S)-7-{[HYDROXY(DITHIOPHEN-2-YL)
HETNAM 2 0HK ACETYL]OXY}-9,9-DIMETHYL-3-OXA-9-
HETNAM 3 0HK AZONIATRICYCLO[3.3.1.0~2,4~]NONANE
HETNAM P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN 0HK TIOTROPIUM
HETSYN P33 HEPTAETHYLENE GLYCOL, PEG330
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 OLA 2(C18 H34 O2)
FORMUL 4 0HK C19 H22 N O4 S2 1+
FORMUL 5 P33 C14 H30 O8
FORMUL 6 OLC C21 H40 O4
FORMUL 7 HOH *7(H2 O)
HELIX 1 AA1 ARG A 26 ASN A 58 1 33
HELIX 2 AA2 SER A 59 LYS A 62 5 4
HELIX 3 AA3 THR A 63 PHE A 82 1 20
HELIX 4 AA4 PHE A 82 GLY A 94 1 13
HELIX 5 AA5 GLY A 99 ARG A 134 1 36
HELIX 6 AA6 TYR A 138 ARG A 142 5 5
HELIX 7 AA7 THR A 143 GLY A 174 1 32
HELIX 8 AA8 GLN A 186 SER A 189 5 4
HELIX 9 AA9 GLU A 190 PHE A 202 1 13
HELIX 10 AB1 PHE A 202 GLU A 219 1 18
HELIX 11 AB2 ASN A 1001 GLU A 1010 1 10
HELIX 12 AB3 ALA A 1062 ARG A 1079 1 18
HELIX 13 AB4 LEU A 1083 LEU A 1090 1 8
HELIX 14 AB5 ASP A 1091 MET A 1105 1 15
HELIX 15 AB6 GLY A 1106 GLY A 1112 1 7
HELIX 16 AB7 PHE A 1113 GLN A 1122 1 10
HELIX 17 AB8 ARG A 1124 ALA A 1133 1 10
HELIX 18 AB9 SER A 1135 THR A 1141 1 7
HELIX 19 AC1 THR A 1141 GLY A 1155 1 15
HELIX 20 AC2 TRP A 1157 PHE A 467 1 41
HELIX 21 AC3 PRO A 473 ASN A 499 1 27
HELIX 22 AC4 ASN A 499 CYS A 512 1 14
SHEET 1 AA1 2 ARG A1013 LYS A1018 0
SHEET 2 AA1 2 TYR A1024 GLY A1027 -1 O THR A1025 N TYR A1017
SSBOND 1 CYS A 103 CYS A 183 1555 1555 2.03
SSBOND 2 CYS A 468 CYS A 471 1555 1555 2.03
SITE 1 AC1 1 VAL A 490
SITE 1 AC2 8 ASN A 115 MET A 119 PRO A 164 ALA A 165
SITE 2 AC2 8 CYS A 168 TRP A 169 LEU A 172 ALA A 200
SITE 1 AC3 14 ASP A 110 TYR A 111 SER A 114 ASN A 115
SITE 2 AC3 14 THR A 194 THR A 197 ALA A 198 PHE A 202
SITE 3 AC3 14 TRP A 455 TYR A 458 ASN A 459 TYR A 481
SITE 4 AC3 14 CYS A 484 TYR A 485
SITE 1 AC4 9 TYR A 87 TYR A 111 CYS A 183 GLN A 184
SITE 2 AC4 9 ILE A 185 LEU A 188 SER A 189 TRP A 477
SITE 3 AC4 9 HIS A 478
SITE 1 AC5 8 LYS A 62 TYR A 67 PRO A 144 LYS A 145
SITE 2 AC5 8 GLY A 148 PHE A 159 CYS A 471 LEU A 476
CRYST1 97.060 63.310 91.620 90.00 102.11 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010303 0.000000 0.002210 0.00000
SCALE2 0.000000 0.015795 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011163 0.00000
ATOM 1 N ARG A 26 13.579 35.824 -25.153 1.00 92.65 N
ANISOU 1 N ARG A 26 12581 11797 10824 -43 2779 -3841 N
ATOM 2 CA ARG A 26 14.340 34.684 -25.643 1.00 92.19 C
ANISOU 2 CA ARG A 26 12528 11821 10679 -232 2522 -3563 C
ATOM 3 C ARG A 26 13.474 33.771 -26.506 1.00 91.03 C
ANISOU 3 C ARG A 26 12071 11838 10678 -197 2536 -3354 C
ATOM 4 O ARG A 26 13.953 33.204 -27.484 1.00 87.49 O
ANISOU 4 O ARG A 26 11549 11361 10334 -233 2308 -3126 O
ATOM 5 CB ARG A 26 14.936 33.895 -24.475 1.00 94.94 C
ANISOU 5 CB ARG A 26 13121 12334 10617 -488 2511 -3573 C
ATOM 6 N LEU A 27 12.198 33.639 -26.135 1.00 93.43 N
ANISOU 6 N LEU A 27 12186 12328 10985 -136 2813 -3450 N
ATOM 7 CA LEU A 27 11.274 32.796 -26.894 1.00 91.43 C
ANISOU 7 CA LEU A 27 11607 12262 10869 -130 2845 -3291 C
ATOM 8 C LEU A 27 11.025 33.352 -28.290 1.00 86.81 C
ANISOU 8 C LEU A 27 10777 11566 10642 112 2701 -3199 C
ATOM 9 O LEU A 27 11.000 32.601 -29.274 1.00 78.39 O
ANISOU 9 O LEU A 27 9544 10567 9675 68 2537 -2994 O
ATOM 10 CB LEU A 27 9.951 32.669 -26.144 1.00 91.52 C
ANISOU 10 CB LEU A 27 11441 12515 10818 -118 3195 -3446 C
ATOM 11 CG LEU A 27 8.896 31.797 -26.827 1.00 93.87 C
ANISOU 11 CG LEU A 27 11368 13046 11251 -151 3258 -3322 C
ATOM 12 CD1 LEU A 27 9.368 30.364 -27.008 1.00 91.99 C
ANISOU 12 CD1 LEU A 27 11209 12882 10860 -447 3117 -3092 C
ATOM 13 CD2 LEU A 27 7.585 31.859 -26.073 1.00100.65 C
ANISOU 13 CD2 LEU A 27 12018 14149 12077 -121 3628 -3507 C
ATOM 14 N TRP A 28 10.786 34.664 -28.373 1.00 88.89 N
ANISOU 14 N TRP A 28 11027 11658 11091 379 2776 -3353 N
ATOM 15 CA TRP A 28 10.689 35.371 -29.646 1.00 91.67 C
ANISOU 15 CA TRP A 28 11216 11854 11761 641 2630 -3253 C
ATOM 16 C TRP A 28 11.934 35.107 -30.490 1.00 86.79 C
ANISOU 16 C TRP A 28 10741 11074 11159 532 2310 -3039 C
ATOM 17 O TRP A 28 11.837 34.842 -31.698 1.00 79.37 O
ANISOU 17 O TRP A 28 9615 10159 10385 610 2143 -2846 O
ATOM 18 CB TRP A 28 10.449 36.856 -29.339 1.00103.24 C
ANISOU 18 CB TRP A 28 12761 13091 13374 919 2783 -3467 C
ATOM 19 CG TRP A 28 10.302 37.865 -30.461 1.00111.94 C
ANISOU 19 CG TRP A 28 13761 13971 14801 1247 2688 -3389 C
ATOM 20 CD1 TRP A 28 10.797 37.806 -31.735 1.00112.52 C
ANISOU 20 CD1 TRP A 28 13785 13945 15021 1294 2424 -3143 C
ATOM 21 CD2 TRP A 28 9.536 39.076 -30.389 1.00117.99 C
ANISOU 21 CD2 TRP A 28 14463 14593 15772 1598 2879 -3550 C
ATOM 22 NE1 TRP A 28 10.412 38.921 -32.445 1.00115.55 N
ANISOU 22 NE1 TRP A 28 14099 14129 15676 1645 2433 -3125 N
ATOM 23 CE2 TRP A 28 9.634 39.713 -31.641 1.00119.36 C
ANISOU 23 CE2 TRP A 28 14572 14570 16211 1848 2708 -3369 C
ATOM 24 CE3 TRP A 28 8.786 39.686 -29.378 1.00121.94 C
ANISOU 24 CE3 TRP A 28 14971 15109 16253 1738 3191 -3831 C
ATOM 25 CZ2 TRP A 28 9.011 40.931 -31.908 1.00123.98 C
ANISOU 25 CZ2 TRP A 28 15107 14951 17047 2246 2828 -3441 C
ATOM 26 CZ3 TRP A 28 8.170 40.894 -29.644 1.00127.96 C
ANISOU 26 CZ3 TRP A 28 15670 15671 17278 2136 3318 -3926 C
ATOM 27 CH2 TRP A 28 8.285 41.504 -30.899 1.00128.91 C
ANISOU 27 CH2 TRP A 28 15736 15577 17668 2393 3132 -3722 C
ATOM 28 N GLU A 29 13.112 35.171 -29.859 1.00 86.43 N
ANISOU 28 N GLU A 29 11016 10890 10933 351 2223 -3080 N
ATOM 29 CA GLU A 29 14.365 34.902 -30.557 1.00 87.63 C
ANISOU 29 CA GLU A 29 11295 10914 11088 235 1938 -2894 C
ATOM 30 C GLU A 29 14.409 33.470 -31.079 1.00 88.26 C
ANISOU 30 C GLU A 29 11253 11195 11087 72 1809 -2675 C
ATOM 31 O GLU A 29 14.844 33.231 -32.211 1.00 86.35 O
ANISOU 31 O GLU A 29 10939 10901 10968 95 1606 -2487 O
ATOM 32 CB GLU A 29 15.549 35.162 -29.626 1.00 91.53 C
ANISOU 32 CB GLU A 29 12114 11288 11374 55 1881 -3007 C
ATOM 33 CG GLU A 29 15.611 36.572 -29.063 1.00101.60 C
ANISOU 33 CG GLU A 29 13555 12333 12714 170 2008 -3258 C
ATOM 34 CD GLU A 29 16.659 36.716 -27.975 1.00102.91 C
ANISOU 34 CD GLU A 29 14023 12456 12622 -49 1963 -3414 C
ATOM 35 OE1 GLU A 29 17.305 35.704 -27.629 1.00101.74 O
ANISOU 35 OE1 GLU A 29 13944 12475 12236 -262 1832 -3307 O
ATOM 36 OE2 GLU A 29 16.835 37.840 -27.463 1.00105.82 O
ANISOU 36 OE2 GLU A 29 14562 12623 13020 -4 2055 -3648 O
ATOM 37 N VAL A 30 13.981 32.504 -30.256 1.00 89.30 N
ANISOU 37 N VAL A 30 11384 11542 11005 -100 1938 -2700 N
ATOM 38 CA VAL A 30 13.992 31.097 -30.661 1.00 88.77 C
ANISOU 38 CA VAL A 30 11238 11630 10859 -274 1846 -2506 C
ATOM 39 C VAL A 30 13.080 30.879 -31.862 1.00 87.52 C
ANISOU 39 C VAL A 30 10750 11571 10932 -155 1821 -2411 C
ATOM 40 O VAL A 30 13.454 30.197 -32.826 1.00 88.06 O
ANISOU 40 O VAL A 30 10763 11644 11053 -210 1632 -2233 O
ATOM 41 CB VAL A 30 13.604 30.194 -29.473 1.00 94.78 C
ANISOU 41 CB VAL A 30 12086 12578 11348 -480 2035 -2553 C
ATOM 42 CG1 VAL A 30 13.366 28.766 -29.932 1.00 95.20 C
ANISOU 42 CG1 VAL A 30 12041 12766 11365 -651 1993 -2369 C
ATOM 43 CG2 VAL A 30 14.703 30.203 -28.426 1.00 95.12 C
ANISOU 43 CG2 VAL A 30 12469 12554 11118 -613 1980 -2594 C
ATOM 44 N ILE A 31 11.877 31.464 -31.827 1.00 86.73 N
ANISOU 44 N ILE A 31 10419 11568 10967 19 2008 -2537 N
ATOM 45 CA ILE A 31 10.934 31.327 -32.937 1.00 84.83 C
ANISOU 45 CA ILE A 31 9826 11468 10937 152 1973 -2463 C
ATOM 46 C ILE A 31 11.507 31.941 -34.210 1.00 80.57 C
ANISOU 46 C ILE A 31 9272 10755 10583 336 1730 -2326 C
ATOM 47 O ILE A 31 11.434 31.341 -35.292 1.00 75.91 O
ANISOU 47 O ILE A 31 8525 10253 10063 319 1569 -2176 O
ATOM 48 CB ILE A 31 9.575 31.952 -32.568 1.00 87.22 C
ANISOU 48 CB ILE A 31 9869 11922 11350 343 2224 -2637 C
ATOM 49 CG1 ILE A 31 8.949 31.217 -31.380 1.00 89.93 C
ANISOU 49 CG1 ILE A 31 10201 12474 11494 127 2488 -2755 C
ATOM 50 CG2 ILE A 31 8.629 31.938 -33.761 1.00 87.94 C
ANISOU 50 CG2 ILE A 31 9568 12182 11663 519 2150 -2563 C
ATOM 51 CD1 ILE A 31 7.658 31.844 -30.890 1.00 90.39 C
ANISOU 51 CD1 ILE A 31 10003 12697 11644 310 2771 -2952 C
ATOM 52 N THR A 32 12.098 33.138 -34.097 1.00 82.53 N
ANISOU 52 N THR A 32 9703 10751 10904 496 1711 -2382 N
ATOM 53 CA THR A 32 12.656 33.820 -35.264 1.00 83.66 C
ANISOU 53 CA THR A 32 9863 10704 11221 667 1512 -2242 C
ATOM 54 C THR A 32 13.807 33.027 -35.880 1.00 80.64 C
ANISOU 54 C THR A 32 9609 10279 10752 473 1281 -2061 C
ATOM 55 O THR A 32 13.865 32.841 -37.105 1.00 79.92 O
ANISOU 55 O THR A 32 9396 10211 10758 541 1117 -1897 O
ATOM 56 CB THR A 32 13.121 35.222 -34.870 1.00 87.02 C
ANISOU 56 CB THR A 32 10505 10830 11729 822 1572 -2355 C
ATOM 57 OG1 THR A 32 12.005 35.973 -34.378 1.00 94.53 O
ANISOU 57 OG1 THR A 32 11327 11809 12780 1047 1798 -2527 O
ATOM 58 CG2 THR A 32 13.722 35.944 -36.067 1.00 89.59 C
ANISOU 58 CG2 THR A 32 10876 10935 12231 979 1392 -2190 C
ATOM 59 N ILE A 33 14.735 32.557 -35.040 1.00 74.44 N
ANISOU 59 N ILE A 33 9066 9445 9773 244 1266 -2091 N
ATOM 60 CA ILE A 33 15.873 31.783 -35.526 1.00 70.20 C
ANISOU 60 CA ILE A 33 8647 8875 9152 79 1060 -1930 C
ATOM 61 C ILE A 33 15.406 30.485 -36.169 1.00 70.63 C
ANISOU 61 C ILE A 33 8527 9132 9177 -20 1005 -1809 C
ATOM 62 O ILE A 33 15.865 30.121 -37.258 1.00 69.32 O
ANISOU 62 O ILE A 33 8322 8952 9064 -18 830 -1659 O
ATOM 63 CB ILE A 33 16.874 31.532 -34.382 1.00 69.68 C
ANISOU 63 CB ILE A 33 8852 8755 8870 -118 1056 -1994 C
ATOM 64 CG1 ILE A 33 17.497 32.853 -33.924 1.00 73.96 C
ANISOU 64 CG1 ILE A 33 9570 9077 9453 -51 1072 -2124 C
ATOM 65 CG2 ILE A 33 17.941 30.534 -34.792 1.00 64.24 C
ANISOU 65 CG2 ILE A 33 8249 8077 8083 -272 862 -1827 C
ATOM 66 CD1 ILE A 33 18.316 32.738 -32.658 1.00 79.00 C
ANISOU 66 CD1 ILE A 33 10450 9709 9857 -234 1079 -2237 C
ATOM 67 N ALA A 34 14.459 29.789 -35.529 1.00 70.92 N
ANISOU 67 N ALA A 34 8459 9358 9130 -119 1167 -1886 N
ATOM 68 CA ALA A 34 13.934 28.545 -36.082 1.00 69.26 C
ANISOU 68 CA ALA A 34 8088 9327 8900 -251 1140 -1800 C
ATOM 69 C ALA A 34 13.271 28.769 -37.436 1.00 71.87 C
ANISOU 69 C ALA A 34 8140 9747 9420 -87 1041 -1739 C
ATOM 70 O ALA A 34 13.491 27.992 -38.373 1.00 69.75 O
ANISOU 70 O ALA A 34 7821 9527 9155 -162 893 -1623 O
ATOM 71 CB ALA A 34 12.949 27.912 -35.100 1.00 68.27 C
ANISOU 71 CB ALA A 34 7888 9382 8669 -397 1373 -1908 C
ATOM 72 N ALA A 35 12.473 29.835 -37.562 1.00 74.52 N
ANISOU 72 N ALA A 35 8302 10108 9905 154 1115 -1815 N
ATOM 73 CA ALA A 35 11.786 30.117 -38.819 1.00 74.35 C
ANISOU 73 CA ALA A 35 8004 10200 10044 348 1008 -1746 C
ATOM 74 C ALA A 35 12.773 30.450 -39.932 1.00 74.53 C
ANISOU 74 C ALA A 35 8144 10060 10115 439 782 -1579 C
ATOM 75 O ALA A 35 12.672 29.910 -41.044 1.00 73.59 O
ANISOU 75 O ALA A 35 7892 10060 10011 431 631 -1472 O
ATOM 76 CB ALA A 35 10.792 31.260 -38.622 1.00 74.82 C
ANISOU 76 CB ALA A 35 7878 10296 10253 632 1142 -1851 C
ATOM 77 N VAL A 36 13.739 31.336 -39.647 1.00 75.12 N
ANISOU 77 N VAL A 36 8468 9870 10204 506 766 -1565 N
ATOM 78 CA VAL A 36 14.714 31.747 -40.658 1.00 70.89 C
ANISOU 78 CA VAL A 36 8048 9169 9717 579 585 -1406 C
ATOM 79 C VAL A 36 15.550 30.558 -41.115 1.00 72.26 C
ANISOU 79 C VAL A 36 8300 9389 9768 360 446 -1303 C
ATOM 80 O VAL A 36 15.755 30.349 -42.319 1.00 75.63 O
ANISOU 80 O VAL A 36 8663 9855 10218 404 297 -1170 O
ATOM 81 CB VAL A 36 15.595 32.890 -40.116 1.00 68.17 C
ANISOU 81 CB VAL A 36 7957 8531 9414 636 624 -1443 C
ATOM 82 CG1 VAL A 36 16.808 33.114 -41.010 1.00 68.11 C
ANISOU 82 CG1 VAL A 36 8094 8359 9426 620 458 -1282 C
ATOM 83 CG2 VAL A 36 14.787 34.172 -40.004 1.00 68.79 C
ANISOU 83 CG2 VAL A 36 7970 8514 9654 914 744 -1516 C
ATOM 84 N THR A 37 16.004 29.734 -40.170 1.00 69.51 N
ANISOU 84 N THR A 37 8093 9043 9275 134 499 -1360 N
ATOM 85 CA THR A 37 16.837 28.598 -40.542 1.00 69.61 C
ANISOU 85 CA THR A 37 8200 9070 9181 -44 379 -1263 C
ATOM 86 C THR A 37 16.039 27.504 -41.242 1.00 69.39 C
ANISOU 86 C THR A 37 7981 9246 9138 -123 351 -1239 C
ATOM 87 O THR A 37 16.582 26.824 -42.118 1.00 69.72 O
ANISOU 87 O THR A 37 8048 9295 9149 -181 220 -1143 O
ATOM 88 CB THR A 37 17.558 28.059 -39.315 1.00 69.77 C
ANISOU 88 CB THR A 37 8438 9028 9044 -227 434 -1310 C
ATOM 89 OG1 THR A 37 16.602 27.633 -38.339 1.00 77.40 O
ANISOU 89 OG1 THR A 37 9354 10115 9938 -317 609 -1423 O
ATOM 90 CG2 THR A 37 18.471 29.139 -38.732 1.00 67.52 C
ANISOU 90 CG2 THR A 37 8334 8557 8765 -177 427 -1349 C
ATOM 91 N ALA A 38 14.767 27.307 -40.875 1.00 68.54 N
ANISOU 91 N ALA A 38 7680 9311 9051 -141 480 -1343 N
ATOM 92 CA ALA A 38 13.920 26.383 -41.624 1.00 65.54 C
ANISOU 92 CA ALA A 38 7080 9144 8678 -230 447 -1345 C
ATOM 93 C ALA A 38 13.745 26.847 -43.065 1.00 66.42 C
ANISOU 93 C ALA A 38 7024 9330 8881 -44 278 -1260 C
ATOM 94 O ALA A 38 13.790 26.032 -43.997 1.00 65.93 O
ANISOU 94 O ALA A 38 6908 9362 8780 -132 160 -1215 O
ATOM 95 CB ALA A 38 12.562 26.235 -40.941 1.00 64.44 C
ANISOU 95 CB ALA A 38 6721 9199 8562 -282 630 -1484 C
ATOM 96 N VAL A 39 13.541 28.154 -43.264 1.00 65.17 N
ANISOU 96 N VAL A 39 6804 9123 8834 220 270 -1238 N
ATOM 97 CA VAL A 39 13.415 28.695 -44.616 1.00 71.35 C
ANISOU 97 CA VAL A 39 7462 9966 9683 429 108 -1123 C
ATOM 98 C VAL A 39 14.706 28.484 -45.400 1.00 66.93 C
ANISOU 98 C VAL A 39 7110 9263 9057 382 -36 -984 C
ATOM 99 O VAL A 39 14.679 28.059 -46.562 1.00 65.35 O
ANISOU 99 O VAL A 39 6824 9187 8817 389 -176 -910 O
ATOM 100 CB VAL A 39 13.014 30.182 -44.557 1.00 75.04 C
ANISOU 100 CB VAL A 39 7877 10347 10287 738 153 -1107 C
ATOM 101 CG1 VAL A 39 13.200 30.853 -45.911 1.00 71.64 C
ANISOU 101 CG1 VAL A 39 7419 9901 9901 966 -16 -933 C
ATOM 102 CG2 VAL A 39 11.566 30.308 -44.109 1.00 79.06 C
ANISOU 102 CG2 VAL A 39 8091 11078 10870 831 273 -1238 C
ATOM 103 N VAL A 40 15.853 28.752 -44.769 1.00 67.06 N
ANISOU 103 N VAL A 40 7388 9041 9050 323 -2 -961 N
ATOM 104 CA VAL A 40 17.139 28.600 -45.449 1.00 66.93 C
ANISOU 104 CA VAL A 40 7546 8901 8983 281 -119 -838 C
ATOM 105 C VAL A 40 17.405 27.133 -45.780 1.00 66.04 C
ANISOU 105 C VAL A 40 7448 8890 8755 77 -177 -841 C
ATOM 106 O VAL A 40 17.895 26.806 -46.870 1.00 70.00 O
ANISOU 106 O VAL A 40 7962 9421 9214 84 -294 -751 O
ATOM 107 CB VAL A 40 18.265 29.218 -44.597 1.00 62.28 C
ANISOU 107 CB VAL A 40 7195 8069 8402 247 -69 -840 C
ATOM 108 CG1 VAL A 40 19.639 28.857 -45.148 1.00 57.96 C
ANISOU 108 CG1 VAL A 40 6795 7432 7794 162 -172 -733 C
ATOM 109 CG2 VAL A 40 18.108 30.732 -44.548 1.00 61.67 C
ANISOU 109 CG2 VAL A 40 7136 7842 8454 453 -22 -826 C
ATOM 110 N SER A 41 17.042 26.226 -44.868 1.00 67.94 N
ANISOU 110 N SER A 41 7698 9179 8939 -104 -80 -946 N
ATOM 111 CA SER A 41 17.220 24.799 -45.112 1.00 67.27 C
ANISOU 111 CA SER A 41 7653 9147 8758 -300 -109 -957 C
ATOM 112 C SER A 41 16.335 24.322 -46.256 1.00 67.72 C
ANISOU 112 C SER A 41 7496 9416 8818 -306 -189 -978 C
ATOM 113 O SER A 41 16.788 23.553 -47.112 1.00 69.65 O
ANISOU 113 O SER A 41 7789 9676 8998 -376 -281 -946 O
ATOM 114 CB SER A 41 16.924 24.014 -43.833 1.00 67.98 C
ANISOU 114 CB SER A 41 7817 9223 8787 -489 35 -1047 C
ATOM 115 OG SER A 41 16.909 22.617 -44.070 1.00 69.18 O
ANISOU 115 OG SER A 41 8013 9406 8868 -681 32 -1061 O
ATOM 116 N LEU A 42 15.078 24.781 -46.295 1.00 68.69 N
ANISOU 116 N LEU A 42 7372 9718 9010 -225 -158 -1044 N
ATOM 117 CA LEU A 42 14.191 24.434 -47.403 1.00 72.53 C
ANISOU 117 CA LEU A 42 7614 10454 9491 -218 -261 -1074 C
ATOM 118 C LEU A 42 14.717 24.962 -48.731 1.00 68.24 C
ANISOU 118 C LEU A 42 7084 9923 8922 -39 -433 -942 C
ATOM 119 O LEU A 42 14.633 24.270 -49.753 1.00 75.47 O
ANISOU 119 O LEU A 42 7940 10979 9757 -107 -546 -951 O
ATOM 120 CB LEU A 42 12.780 24.965 -47.152 1.00 80.86 C
ANISOU 120 CB LEU A 42 8366 11723 10634 -122 -203 -1161 C
ATOM 121 CG LEU A 42 11.868 24.153 -46.237 1.00 86.01 C
ANISOU 121 CG LEU A 42 8895 12493 11291 -352 -41 -1317 C
ATOM 122 CD1 LEU A 42 10.448 24.629 -46.425 1.00 92.00 C
ANISOU 122 CD1 LEU A 42 9271 13545 12138 -234 -32 -1400 C
ATOM 123 CD2 LEU A 42 11.979 22.663 -46.526 1.00 87.14 C
ANISOU 123 CD2 LEU A 42 9103 12662 11345 -655 -55 -1374 C
ATOM 124 N ILE A 43 15.248 26.190 -48.740 1.00 63.29 N
ANISOU 124 N ILE A 43 6547 9148 8354 178 -444 -826 N
ATOM 125 CA ILE A 43 15.796 26.757 -49.973 1.00 64.66 C
ANISOU 125 CA ILE A 43 6762 9314 8494 344 -581 -673 C
ATOM 126 C ILE A 43 16.995 25.942 -50.445 1.00 62.65 C
ANISOU 126 C ILE A 43 6706 8966 8134 200 -628 -631 C
ATOM 127 O ILE A 43 17.122 25.641 -51.639 1.00 64.91 O
ANISOU 127 O ILE A 43 6967 9370 8326 221 -743 -580 O
ATOM 128 CB ILE A 43 16.139 28.247 -49.777 1.00 66.13 C
ANISOU 128 CB ILE A 43 7036 9309 8782 576 -548 -558 C
ATOM 129 CG1 ILE A 43 14.856 29.062 -49.576 1.00 68.03 C
ANISOU 129 CG1 ILE A 43 7054 9667 9127 783 -518 -589 C
ATOM 130 CG2 ILE A 43 16.928 28.799 -50.962 1.00 61.85 C
ANISOU 130 CG2 ILE A 43 6600 8706 8194 706 -655 -374 C
ATOM 131 CD1 ILE A 43 15.093 30.528 -49.278 1.00 66.11 C
ANISOU 131 CD1 ILE A 43 6921 9192 9006 1016 -455 -499 C
ATOM 132 N THR A 44 17.866 25.540 -49.512 1.00 62.66 N
ANISOU 132 N THR A 44 6899 8774 8135 62 -539 -659 N
ATOM 133 CA THR A 44 19.015 24.699 -49.852 1.00 63.57 C
ANISOU 133 CA THR A 44 7188 8803 8164 -54 -569 -629 C
ATOM 134 C THR A 44 18.573 23.367 -50.455 1.00 62.74 C
ANISOU 134 C THR A 44 7025 8845 7968 -207 -610 -722 C
ATOM 135 O THR A 44 19.087 22.941 -51.504 1.00 65.06 O
ANISOU 135 O THR A 44 7364 9179 8175 -208 -690 -688 O
ATOM 136 CB THR A 44 19.865 24.450 -48.603 1.00 63.37 C
ANISOU 136 CB THR A 44 7345 8582 8151 -159 -477 -650 C
ATOM 137 OG1 THR A 44 20.072 25.682 -47.904 1.00 63.99 O
ANISOU 137 OG1 THR A 44 7462 8538 8315 -53 -428 -616 O
ATOM 138 CG2 THR A 44 21.210 23.849 -48.977 1.00 57.51 C
ANISOU 138 CG2 THR A 44 6766 7742 7344 -207 -515 -590 C
ATOM 139 N ILE A 45 17.623 22.694 -49.792 1.00 62.75 N
ANISOU 139 N ILE A 45 6933 8923 7985 -354 -540 -852 N
ATOM 140 CA ILE A 45 17.145 21.393 -50.261 1.00 61.98 C
ANISOU 140 CA ILE A 45 6793 8937 7818 -546 -557 -968 C
ATOM 141 C ILE A 45 16.528 21.516 -51.648 1.00 61.61 C
ANISOU 141 C ILE A 45 6560 9135 7712 -476 -700 -982 C
ATOM 142 O ILE A 45 16.868 20.753 -52.559 1.00 61.51 O
ANISOU 142 O ILE A 45 6610 9163 7600 -551 -768 -1015 O
ATOM 143 CB ILE A 45 16.152 20.784 -49.253 1.00 59.32 C
ANISOU 143 CB ILE A 45 6374 8643 7523 -734 -431 -1099 C
ATOM 144 CG1 ILE A 45 16.850 20.486 -47.925 1.00 62.09 C
ANISOU 144 CG1 ILE A 45 6952 8759 7879 -816 -299 -1074 C
ATOM 145 CG2 ILE A 45 15.532 19.508 -49.810 1.00 52.51 C
ANISOU 145 CG2 ILE A 45 5448 7897 6606 -963 -443 -1236 C
ATOM 146 CD1 ILE A 45 15.891 20.234 -46.779 1.00 63.25 C
ANISOU 146 CD1 ILE A 45 7028 8946 8060 -959 -145 -1167 C
ATOM 147 N VAL A 46 15.626 22.488 -51.828 1.00 62.04 N
ANISOU 147 N VAL A 46 6392 9363 7818 -315 -749 -957 N
ATOM 148 CA VAL A 46 14.933 22.657 -53.104 1.00 65.07 C
ANISOU 148 CA VAL A 46 6573 10025 8126 -223 -908 -959 C
ATOM 149 C VAL A 46 15.920 23.003 -54.215 1.00 67.54 C
ANISOU 149 C VAL A 46 7031 10297 8332 -84 -1011 -815 C
ATOM 150 O VAL A 46 15.823 22.476 -55.330 1.00 74.33 O
ANISOU 150 O VAL A 46 7853 11333 9055 -124 -1125 -854 O
ATOM 151 CB VAL A 46 13.820 23.714 -52.964 1.00 65.32 C
ANISOU 151 CB VAL A 46 6338 10234 8247 -23 -935 -934 C
ATOM 152 CG1 VAL A 46 13.325 24.184 -54.329 1.00 64.89 C
ANISOU 152 CG1 VAL A 46 6108 10450 8097 164 -1129 -864 C
ATOM 153 CG2 VAL A 46 12.665 23.146 -52.158 1.00 62.18 C
ANISOU 153 CG2 VAL A 46 5728 9978 7921 -200 -842 -1113 C
ATOM 154 N GLY A 47 16.911 23.849 -53.917 1.00 63.14 N
ANISOU 154 N GLY A 47 6650 9514 7827 54 -961 -662 N
ATOM 155 CA GLY A 47 17.885 24.226 -54.930 1.00 63.97 C
ANISOU 155 CA GLY A 47 6891 9578 7837 169 -1027 -515 C
ATOM 156 C GLY A 47 18.739 23.061 -55.396 1.00 66.32 C
ANISOU 156 C GLY A 47 7343 9834 8022 6 -1022 -580 C
ATOM 157 O GLY A 47 18.925 22.850 -56.600 1.00 67.15 O
ANISOU 157 O GLY A 47 7459 10075 7980 36 -1111 -558 O
ATOM 158 N ASN A 48 19.269 22.279 -54.449 1.00 64.62 N
ANISOU 158 N ASN A 48 7259 9431 7862 -153 -913 -660 N
ATOM 159 CA ASN A 48 20.138 21.181 -54.866 1.00 65.10 C
ANISOU 159 CA ASN A 48 7481 9421 7833 -268 -896 -714 C
ATOM 160 C ASN A 48 19.346 20.025 -55.473 1.00 67.30 C
ANISOU 160 C ASN A 48 7691 9864 8017 -434 -942 -894 C
ATOM 161 O ASN A 48 19.850 19.336 -56.373 1.00 70.34 O
ANISOU 161 O ASN A 48 8170 10275 8281 -473 -970 -942 O
ATOM 162 CB ASN A 48 21.009 20.729 -53.697 1.00 65.86 C
ANISOU 162 CB ASN A 48 7749 9266 8009 -348 -780 -717 C
ATOM 163 CG ASN A 48 22.017 21.791 -53.292 1.00 69.85 C
ANISOU 163 CG ASN A 48 8331 9627 8582 -213 -751 -564 C
ATOM 164 OD1 ASN A 48 23.040 21.961 -53.952 1.00 74.72 O
ANISOU 164 OD1 ASN A 48 9028 10210 9152 -144 -762 -477 O
ATOM 165 ND2 ASN A 48 21.728 22.517 -52.217 1.00 69.79 N
ANISOU 165 ND2 ASN A 48 8296 9541 8682 -189 -703 -543 N
ATOM 166 N VAL A 49 18.094 19.832 -55.048 1.00 67.69 N
ANISOU 166 N VAL A 49 7565 10040 8115 -538 -946 -1008 N
ATOM 167 CA VAL A 49 17.230 18.873 -55.728 1.00 69.73 C
ANISOU 167 CA VAL A 49 7715 10495 8283 -715 -1007 -1193 C
ATOM 168 C VAL A 49 16.936 19.340 -57.152 1.00 69.85 C
ANISOU 168 C VAL A 49 7604 10789 8147 -586 -1176 -1164 C
ATOM 169 O VAL A 49 16.892 18.529 -58.082 1.00 71.38 O
ANISOU 169 O VAL A 49 7822 11102 8199 -698 -1240 -1291 O
ATOM 170 CB VAL A 49 15.951 18.628 -54.902 1.00 63.85 C
ANISOU 170 CB VAL A 49 6777 9847 7638 -871 -958 -1321 C
ATOM 171 CG1 VAL A 49 14.920 17.854 -55.695 1.00 65.31 C
ANISOU 171 CG1 VAL A 49 6780 10299 7737 -1057 -1047 -1519 C
ATOM 172 CG2 VAL A 49 16.296 17.823 -53.660 1.00 61.20 C
ANISOU 172 CG2 VAL A 49 6625 9237 7391 -1049 -784 -1365 C
ATOM 173 N LEU A 50 16.758 20.653 -57.350 1.00 68.44 N
ANISOU 173 N LEU A 50 7313 10707 7985 -343 -1248 -993 N
ATOM 174 CA LEU A 50 16.585 21.187 -58.700 1.00 76.41 C
ANISOU 174 CA LEU A 50 8240 11966 8826 -182 -1409 -912 C
ATOM 175 C LEU A 50 17.819 20.941 -59.556 1.00 74.05 C
ANISOU 175 C LEU A 50 8172 11581 8383 -155 -1400 -849 C
ATOM 176 O LEU A 50 17.701 20.634 -60.746 1.00 70.02 O
ANISOU 176 O LEU A 50 7644 11289 7670 -158 -1510 -897 O
ATOM 177 CB LEU A 50 16.278 22.683 -58.650 1.00 80.12 C
ANISOU 177 CB LEU A 50 8601 12480 9362 100 -1457 -704 C
ATOM 178 CG LEU A 50 14.814 23.111 -58.661 1.00 86.97 C
ANISOU 178 CG LEU A 50 9151 13632 10261 184 -1566 -744 C
ATOM 179 CD1 LEU A 50 14.717 24.627 -58.743 1.00 88.50 C
ANISOU 179 CD1 LEU A 50 9303 13810 10511 515 -1603 -506 C
ATOM 180 CD2 LEU A 50 14.088 22.461 -59.830 1.00 89.14 C
ANISOU 180 CD2 LEU A 50 9261 14275 10333 106 -1745 -875 C
ATOM 181 N VAL A 51 19.008 21.094 -58.966 1.00 72.09 N
ANISOU 181 N VAL A 51 8125 11040 8224 -126 -1268 -748 N
ATOM 182 CA VAL A 51 20.252 20.798 -59.680 1.00 70.03 C
ANISOU 182 CA VAL A 51 8063 10696 7848 -108 -1228 -702 C
ATOM 183 C VAL A 51 20.280 19.336 -60.122 1.00 73.48 C
ANISOU 183 C VAL A 51 8577 11166 8177 -304 -1219 -927 C
ATOM 184 O VAL A 51 20.606 19.021 -61.275 1.00 76.63 O
ANISOU 184 O VAL A 51 9038 11694 8383 -291 -1264 -962 O
ATOM 185 CB VAL A 51 21.467 21.153 -58.807 1.00 66.64 C
ANISOU 185 CB VAL A 51 7790 9968 7561 -65 -1092 -581 C
ATOM 186 CG1 VAL A 51 22.744 20.570 -59.398 1.00 62.67 C
ANISOU 186 CG1 VAL A 51 7462 9386 6964 -76 -1026 -582 C
ATOM 187 CG2 VAL A 51 21.584 22.666 -58.666 1.00 67.97 C
ANISOU 187 CG2 VAL A 51 7924 10096 7806 125 -1098 -363 C
ATOM 188 N MET A 52 19.921 18.423 -59.212 1.00 73.68 N
ANISOU 188 N MET A 52 8615 11064 8316 -494 -1147 -1086 N
ATOM 189 CA MET A 52 19.943 16.996 -59.540 1.00 72.54 C
ANISOU 189 CA MET A 52 8579 10887 8097 -695 -1113 -1307 C
ATOM 190 C MET A 52 18.904 16.641 -60.606 1.00 80.17 C
ANISOU 190 C MET A 52 9399 12171 8893 -796 -1254 -1476 C
ATOM 191 O MET A 52 19.199 15.888 -61.545 1.00 80.11 O
ANISOU 191 O MET A 52 9498 12219 8722 -866 -1271 -1611 O
ATOM 192 CB MET A 52 19.724 16.177 -58.269 1.00 70.18 C
ANISOU 192 CB MET A 52 8342 10361 7963 -877 -993 -1408 C
ATOM 193 CG MET A 52 20.830 16.357 -57.238 1.00 73.60 C
ANISOU 193 CG MET A 52 8937 10500 8526 -786 -871 -1263 C
ATOM 194 SD MET A 52 20.461 15.627 -55.628 1.00 77.36 S
ANISOU 194 SD MET A 52 9484 10744 9168 -966 -740 -1323 S
ATOM 195 CE MET A 52 21.944 16.052 -54.718 1.00 70.68 C
ANISOU 195 CE MET A 52 8808 9642 8407 -796 -659 -1130 C
ATOM 196 N ILE A 53 17.689 17.184 -60.488 1.00 82.58 N
ANISOU 196 N ILE A 53 9448 12704 9226 -797 -1361 -1482 N
ATOM 197 CA ILE A 53 16.640 16.908 -61.467 1.00 84.60 C
ANISOU 197 CA ILE A 53 9514 13315 9315 -890 -1525 -1645 C
ATOM 198 C ILE A 53 17.012 17.491 -62.826 1.00 85.12 C
ANISOU 198 C ILE A 53 9601 13603 9139 -697 -1656 -1537 C
ATOM 199 O ILE A 53 16.762 16.875 -63.870 1.00 90.38 O
ANISOU 199 O ILE A 53 10262 14488 9591 -797 -1755 -1705 O
ATOM 200 CB ILE A 53 15.283 17.441 -60.963 1.00 85.82 C
ANISOU 200 CB ILE A 53 9349 13685 9572 -897 -1607 -1656 C
ATOM 201 CG1 ILE A 53 14.844 16.694 -59.703 1.00 83.65 C
ANISOU 201 CG1 ILE A 53 9062 13223 9499 -1141 -1458 -1794 C
ATOM 202 CG2 ILE A 53 14.201 17.298 -62.023 1.00 92.19 C
ANISOU 202 CG2 ILE A 53 9910 14924 10196 -959 -1815 -1805 C
ATOM 203 CD1 ILE A 53 13.554 17.219 -59.108 1.00 79.94 C
ANISOU 203 CD1 ILE A 53 8266 12961 9147 -1147 -1498 -1811 C
ATOM 204 N SER A 54 17.654 18.663 -62.832 1.00 80.56 N
ANISOU 204 N SER A 54 9069 12960 8582 -434 -1644 -1260 N
ATOM 205 CA SER A 54 18.105 19.274 -64.077 1.00 83.13 C
ANISOU 205 CA SER A 54 9451 13462 8674 -247 -1733 -1114 C
ATOM 206 C SER A 54 19.170 18.424 -64.746 1.00 82.60 C
ANISOU 206 C SER A 54 9625 13300 8458 -325 -1643 -1212 C
ATOM 207 O SER A 54 19.145 18.235 -65.968 1.00 80.96 O
ANISOU 207 O SER A 54 9443 13337 7980 -313 -1737 -1270 O
ATOM 208 CB SER A 54 18.637 20.678 -63.804 1.00 81.23 C
ANISOU 208 CB SER A 54 9242 13098 8525 15 -1694 -796 C
ATOM 209 OG SER A 54 17.582 21.525 -63.400 1.00 83.85 O
ANISOU 209 OG SER A 54 9349 13553 8958 133 -1791 -709 O
ATOM 210 N PHE A 55 20.132 17.932 -63.960 1.00 81.12 N
ANISOU 210 N PHE A 55 9617 12771 8433 -384 -1460 -1226 N
ATOM 211 CA PHE A 55 21.136 17.018 -64.492 1.00 85.73 C
ANISOU 211 CA PHE A 55 10420 13244 8910 -444 -1353 -1342 C
ATOM 212 C PHE A 55 20.495 15.744 -65.034 1.00 95.07 C
ANISOU 212 C PHE A 55 11617 14542 9961 -673 -1401 -1664 C
ATOM 213 O PHE A 55 20.998 15.158 -66.000 1.00101.23 O
ANISOU 213 O PHE A 55 12538 15385 10540 -694 -1379 -1785 O
ATOM 214 CB PHE A 55 22.163 16.694 -63.407 1.00 81.21 C
ANISOU 214 CB PHE A 55 9999 12297 8560 -450 -1168 -1299 C
ATOM 215 CG PHE A 55 23.369 15.956 -63.910 1.00 85.91 C
ANISOU 215 CG PHE A 55 10803 12766 9072 -434 -1041 -1366 C
ATOM 216 CD1 PHE A 55 24.491 16.656 -64.323 1.00 87.85 C
ANISOU 216 CD1 PHE A 55 11112 13000 9267 -257 -972 -1173 C
ATOM 217 CD2 PHE A 55 23.398 14.570 -63.944 1.00 91.08 C
ANISOU 217 CD2 PHE A 55 11591 13299 9714 -595 -973 -1622 C
ATOM 218 CE1 PHE A 55 25.610 15.992 -64.784 1.00 91.51 C
ANISOU 218 CE1 PHE A 55 11737 13372 9661 -225 -840 -1240 C
ATOM 219 CE2 PHE A 55 24.515 13.900 -64.404 1.00 94.75 C
ANISOU 219 CE2 PHE A 55 12246 13641 10114 -545 -843 -1689 C
ATOM 220 CZ PHE A 55 25.622 14.612 -64.823 1.00 95.22 C
ANISOU 220 CZ PHE A 55 12335 13726 10117 -352 -777 -1499 C
ATOM 221 N LYS A 56 19.380 15.310 -64.440 1.00 94.03 N
ANISOU 221 N LYS A 56 11342 14447 9938 -859 -1454 -1819 N
ATOM 222 CA LYS A 56 18.774 14.053 -64.864 1.00 94.25 C
ANISOU 222 CA LYS A 56 11392 14547 9872 -1127 -1480 -2148 C
ATOM 223 C LYS A 56 17.905 14.200 -66.112 1.00 95.21 C
ANISOU 223 C LYS A 56 11348 15113 9715 -1155 -1695 -2261 C
ATOM 224 O LYS A 56 17.878 13.285 -66.942 1.00100.44 O
ANISOU 224 O LYS A 56 12109 15864 10190 -1315 -1715 -2516 O
ATOM 225 CB LYS A 56 17.947 13.458 -63.721 1.00 98.69 C
ANISOU 225 CB LYS A 56 11870 14966 10661 -1359 -1426 -2279 C
ATOM 226 CG LYS A 56 17.421 12.053 -63.995 1.00107.22 C
ANISOU 226 CG LYS A 56 13019 16025 11693 -1685 -1403 -2629 C
ATOM 227 CD LYS A 56 16.771 11.440 -62.765 1.00112.20 C
ANISOU 227 CD LYS A 56 13616 16448 12565 -1924 -1295 -2722 C
ATOM 228 CE LYS A 56 16.278 10.028 -63.052 1.00117.24 C
ANISOU 228 CE LYS A 56 14364 16986 13197 -2242 -1232 -3023 C
ATOM 229 NZ LYS A 56 15.691 9.386 -61.844 1.00117.96 N
ANISOU 229 NZ LYS A 56 14459 16835 13525 -2476 -1089 -3074 N
ATOM 230 N VAL A 57 17.216 15.328 -66.290 1.00 94.66 N
ANISOU 230 N VAL A 57 11038 15330 9600 -991 -1861 -2080 N
ATOM 231 CA VAL A 57 16.212 15.452 -67.346 1.00 94.34 C
ANISOU 231 CA VAL A 57 10814 15682 9349 -998 -2065 -2147 C
ATOM 232 C VAL A 57 16.682 16.325 -68.508 1.00 95.55 C
ANISOU 232 C VAL A 57 11021 16054 9230 -733 -2163 -1934 C
ATOM 233 O VAL A 57 15.911 16.566 -69.445 1.00 99.85 O
ANISOU 233 O VAL A 57 11447 16876 9616 -679 -2316 -1912 O
ATOM 234 CB VAL A 57 14.871 15.965 -66.788 1.00 93.07 C
ANISOU 234 CB VAL A 57 10330 15680 9353 -997 -2171 -2099 C
ATOM 235 CG1 VAL A 57 14.487 15.192 -65.536 1.00 95.52 C
ANISOU 235 CG1 VAL A 57 10602 15759 9933 -1255 -2037 -2270 C
ATOM 236 CG2 VAL A 57 14.932 17.464 -66.501 1.00 86.01 C
ANISOU 236 CG2 VAL A 57 9308 14879 8492 -676 -2246 -1779 C
ATOM 237 N ASN A 58 17.934 16.775 -68.501 1.00 90.56 N
ANISOU 237 N ASN A 58 10585 15267 8557 -567 -2050 -1756 N
ATOM 238 CA ASN A 58 18.485 17.548 -69.615 1.00 85.69 C
ANISOU 238 CA ASN A 58 10056 14842 7662 -340 -2104 -1547 C
ATOM 239 C ASN A 58 19.830 16.931 -69.982 1.00 83.30 C
ANISOU 239 C ASN A 58 10045 14325 7280 -365 -1902 -1605 C
ATOM 240 O ASN A 58 20.818 17.112 -69.263 1.00 80.90 O
ANISOU 240 O ASN A 58 9865 13684 7188 -296 -1711 -1466 O
ATOM 241 CB ASN A 58 18.620 19.026 -69.256 1.00 83.21 C
ANISOU 241 CB ASN A 58 9679 14474 7463 -59 -2110 -1161 C
ATOM 242 CG ASN A 58 18.885 19.912 -70.471 1.00 86.80 C
ANISOU 242 CG ASN A 58 10195 15180 7605 172 -2199 -920 C
ATOM 243 OD1 ASN A 58 19.143 19.428 -71.574 1.00 89.13 O
ANISOU 243 OD1 ASN A 58 10609 15647 7608 130 -2218 -1022 O
ATOM 244 ND2 ASN A 58 18.822 21.222 -70.265 1.00 86.35 N
ANISOU 244 ND2 ASN A 58 10085 15094 7632 416 -2226 -587 N
ATOM 245 N SER A 59 19.851 16.185 -71.094 1.00 86.53 N
ANISOU 245 N SER A 59 10552 14934 7391 -462 -1943 -1823 N
ATOM 246 CA SER A 59 21.074 15.521 -71.539 1.00 89.92 C
ANISOU 246 CA SER A 59 11247 15205 7713 -477 -1748 -1923 C
ATOM 247 C SER A 59 22.168 16.519 -71.902 1.00 90.68 C
ANISOU 247 C SER A 59 11452 15267 7737 -226 -1635 -1591 C
ATOM 248 O SER A 59 23.356 16.182 -71.841 1.00 87.17 O
ANISOU 248 O SER A 59 11184 14590 7345 -199 -1419 -1592 O
ATOM 249 CB SER A 59 20.773 14.612 -72.732 1.00 94.92 C
ANISOU 249 CB SER A 59 11974 15991 8100 -611 -1787 -2182 C
ATOM 250 OG SER A 59 20.128 15.329 -73.771 1.00 98.41 O
ANISOU 250 OG SER A 59 12321 16758 8313 -497 -1965 -2031 O
ATOM 251 N GLN A 60 21.790 17.746 -72.281 1.00 92.67 N
ANISOU 251 N GLN A 60 11595 15742 7872 -41 -1771 -1300 N
ATOM 252 CA GLN A 60 22.770 18.788 -72.580 1.00 88.48 C
ANISOU 252 CA GLN A 60 11171 15154 7293 173 -1651 -959 C
ATOM 253 C GLN A 60 23.590 19.197 -71.357 1.00 81.08 C
ANISOU 253 C GLN A 60 10255 13810 6740 217 -1464 -791 C
ATOM 254 O GLN A 60 24.643 19.824 -71.515 1.00 75.28 O
ANISOU 254 O GLN A 60 9627 12969 6006 332 -1308 -570 O
ATOM 255 CB GLN A 60 22.066 20.012 -73.170 1.00 89.34 C
ANISOU 255 CB GLN A 60 11176 15552 7217 367 -1843 -672 C
ATOM 256 N LEU A 61 23.130 18.872 -70.148 1.00 79.48 N
ANISOU 256 N LEU A 61 9950 13398 6852 115 -1473 -893 N
ATOM 257 CA LEU A 61 23.869 19.159 -68.927 1.00 76.81 C
ANISOU 257 CA LEU A 61 9634 12695 6857 138 -1314 -770 C
ATOM 258 C LEU A 61 24.794 18.027 -68.503 1.00 76.24 C
ANISOU 258 C LEU A 61 9698 12370 6901 28 -1131 -968 C
ATOM 259 O LEU A 61 25.621 18.228 -67.608 1.00 73.21 O
ANISOU 259 O LEU A 61 9344 11714 6758 65 -995 -861 O
ATOM 260 CB LEU A 61 22.904 19.468 -67.780 1.00 78.76 C
ANISOU 260 CB LEU A 61 9709 12851 7367 106 -1407 -754 C
ATOM 261 CG LEU A 61 22.261 20.851 -67.784 1.00 82.04 C
ANISOU 261 CG LEU A 61 9993 13382 7794 284 -1529 -484 C
ATOM 262 CD1 LEU A 61 21.162 20.923 -66.736 1.00 81.97 C
ANISOU 262 CD1 LEU A 61 9795 13335 8016 234 -1617 -547 C
ATOM 263 CD2 LEU A 61 23.320 21.904 -67.521 1.00 80.97 C
ANISOU 263 CD2 LEU A 61 9957 13031 7775 426 -1384 -193 C
ATOM 264 N LYS A 62 24.685 16.849 -69.119 1.00 82.08 N
ANISOU 264 N LYS A 62 10523 13189 7474 -96 -1128 -1256 N
ATOM 265 CA LYS A 62 25.489 15.689 -68.728 1.00 86.22 C
ANISOU 265 CA LYS A 62 11195 13450 8116 -177 -953 -1456 C
ATOM 266 C LYS A 62 26.877 15.786 -69.369 1.00 88.38 C
ANISOU 266 C LYS A 62 11598 13703 8280 -45 -773 -1371 C
ATOM 267 O LYS A 62 27.253 15.020 -70.259 1.00 93.18 O
ANISOU 267 O LYS A 62 12334 14393 8676 -65 -698 -1561 O
ATOM 268 CB LYS A 62 24.772 14.404 -69.120 1.00 93.65 C
ANISOU 268 CB LYS A 62 12194 14450 8939 -373 -1006 -1814 C
ATOM 269 CG LYS A 62 23.519 14.107 -68.301 1.00 96.33 C
ANISOU 269 CG LYS A 62 12399 14757 9444 -549 -1131 -1931 C
ATOM 270 CD LYS A 62 23.085 12.653 -68.446 1.00103.18 C
ANISOU 270 CD LYS A 62 13374 15554 10276 -786 -1110 -2305 C
ATOM 271 CE LYS A 62 24.022 11.695 -67.727 1.00106.13 C
ANISOU 271 CE LYS A 62 13951 15517 10855 -802 -894 -2393 C
ATOM 272 NZ LYS A 62 23.599 11.441 -66.323 1.00105.94 N
ANISOU 272 NZ LYS A 62 13888 15228 11138 -908 -868 -2373 N
ATOM 273 N THR A 63 27.650 16.751 -68.882 1.00 84.36 N
ANISOU 273 N THR A 63 11047 13083 7922 81 -690 -1093 N
ATOM 274 CA THR A 63 29.032 16.959 -69.287 1.00 80.38 C
ANISOU 274 CA THR A 63 10617 12547 7376 193 -498 -984 C
ATOM 275 C THR A 63 29.966 16.598 -68.138 1.00 76.73 C
ANISOU 275 C THR A 63 10157 11773 7223 213 -359 -981 C
ATOM 276 O THR A 63 29.541 16.445 -66.989 1.00 84.17 O
ANISOU 276 O THR A 63 11051 12525 8403 154 -418 -999 O
ATOM 277 CB THR A 63 29.268 18.406 -69.738 1.00 86.38 C
ANISOU 277 CB THR A 63 11326 13447 8047 304 -502 -659 C
ATOM 278 OG1 THR A 63 30.538 18.497 -70.395 1.00106.70 O
ANISOU 278 OG1 THR A 63 13972 16057 10514 378 -301 -590 O
ATOM 279 CG2 THR A 63 29.269 19.346 -68.551 1.00 77.27 C
ANISOU 279 CG2 THR A 63 10067 12094 7198 329 -523 -444 C
ATOM 280 N VAL A 64 31.251 16.447 -68.476 1.00 69.38 N
ANISOU 280 N VAL A 64 9275 10816 6270 302 -172 -961 N
ATOM 281 CA VAL A 64 32.276 16.094 -67.491 1.00 72.52 C
ANISOU 281 CA VAL A 64 9654 10966 6934 354 -45 -952 C
ATOM 282 C VAL A 64 32.363 17.149 -66.390 1.00 80.16 C
ANISOU 282 C VAL A 64 10495 11815 8146 358 -94 -716 C
ATOM 283 O VAL A 64 32.528 16.818 -65.207 1.00 79.23 O
ANISOU 283 O VAL A 64 10353 11484 8267 348 -100 -737 O
ATOM 284 CB VAL A 64 33.630 15.890 -68.199 1.00 69.17 C
ANISOU 284 CB VAL A 64 9258 10604 6420 465 165 -959 C
ATOM 285 CG1 VAL A 64 34.738 15.591 -67.202 1.00 65.06 C
ANISOU 285 CG1 VAL A 64 8676 9874 6172 547 278 -934 C
ATOM 286 CG2 VAL A 64 33.529 14.781 -69.235 1.00 76.79 C
ANISOU 286 CG2 VAL A 64 10371 11662 7142 464 228 -1231 C
ATOM 287 N ASN A 65 32.260 18.432 -66.764 1.00 85.95 N
ANISOU 287 N ASN A 65 11166 12677 8813 376 -125 -489 N
ATOM 288 CA ASN A 65 32.305 19.521 -65.787 1.00 84.30 C
ANISOU 288 CA ASN A 65 10859 12345 8827 370 -163 -280 C
ATOM 289 C ASN A 65 31.198 19.396 -64.748 1.00 76.84 C
ANISOU 289 C ASN A 65 9883 11277 8037 303 -315 -340 C
ATOM 290 O ASN A 65 31.422 19.647 -63.558 1.00 80.74 O
ANISOU 290 O ASN A 65 10324 11592 8762 288 -317 -288 O
ATOM 291 CB ASN A 65 32.198 20.872 -66.495 1.00 96.22 C
ANISOU 291 CB ASN A 65 12351 13990 10217 402 -169 -35 C
ATOM 292 CG ASN A 65 33.425 21.206 -67.314 1.00106.25 C
ANISOU 292 CG ASN A 65 13635 15355 11378 443 19 74 C
ATOM 293 OD1 ASN A 65 34.514 20.688 -67.066 1.00114.15 O
ANISOU 293 OD1 ASN A 65 14602 16295 12474 457 157 3 O
ATOM 294 ND2 ASN A 65 33.257 22.082 -68.296 1.00108.77 N
ANISOU 294 ND2 ASN A 65 14000 15835 11493 472 31 258 N
ATOM 295 N ASN A 66 30.001 19.002 -65.176 1.00 69.52 N
ANISOU 295 N ASN A 66 8977 10464 6973 254 -440 -461 N
ATOM 296 CA ASN A 66 28.835 19.039 -64.307 1.00 70.45 C
ANISOU 296 CA ASN A 66 9033 10515 7218 183 -575 -501 C
ATOM 297 C ASN A 66 28.737 17.842 -63.368 1.00 73.21 C
ANISOU 297 C ASN A 66 9427 10673 7715 95 -556 -697 C
ATOM 298 O ASN A 66 27.943 17.892 -62.425 1.00 79.26 O
ANISOU 298 O ASN A 66 10141 11353 8622 27 -629 -713 O
ATOM 299 CB ASN A 66 27.562 19.150 -65.147 1.00 72.00 C
ANISOU 299 CB ASN A 66 9193 10950 7213 160 -726 -547 C
ATOM 300 CG ASN A 66 27.437 20.498 -65.839 1.00 71.27 C
ANISOU 300 CG ASN A 66 9060 11016 7004 272 -774 -298 C
ATOM 301 OD1 ASN A 66 28.169 21.440 -65.529 1.00 72.95 O
ANISOU 301 OD1 ASN A 66 9270 11117 7330 338 -691 -90 O
ATOM 302 ND2 ASN A 66 26.516 20.592 -66.791 1.00 66.13 N
ANISOU 302 ND2 ASN A 66 8383 10624 6120 292 -908 -316 N
ATOM 303 N TYR A 67 29.505 16.771 -63.595 1.00 68.29 N
ANISOU 303 N TYR A 67 8910 9975 7062 103 -448 -841 N
ATOM 304 CA TYR A 67 29.550 15.687 -62.615 1.00 66.51 C
ANISOU 304 CA TYR A 67 8758 9516 6994 47 -411 -980 C
ATOM 305 C TYR A 67 30.136 16.171 -61.294 1.00 63.44 C
ANISOU 305 C TYR A 67 8316 8952 6835 91 -387 -830 C
ATOM 306 O TYR A 67 29.674 15.780 -60.212 1.00 64.46 O
ANISOU 306 O TYR A 67 8467 8925 7101 22 -417 -869 O
ATOM 307 CB TYR A 67 30.352 14.506 -63.163 1.00 67.25 C
ANISOU 307 CB TYR A 67 8991 9543 7018 93 -285 -1147 C
ATOM 308 CG TYR A 67 29.575 13.662 -64.145 1.00 72.84 C
ANISOU 308 CG TYR A 67 9795 10354 7528 -9 -314 -1383 C
ATOM 309 CD1 TYR A 67 28.588 12.789 -63.708 1.00 75.45 C
ANISOU 309 CD1 TYR A 67 10189 10571 7908 -170 -366 -1565 C
ATOM 310 CD2 TYR A 67 29.829 13.732 -65.506 1.00 79.13 C
ANISOU 310 CD2 TYR A 67 10620 11367 8077 36 -282 -1433 C
ATOM 311 CE1 TYR A 67 27.872 12.012 -64.601 1.00 79.35 C
ANISOU 311 CE1 TYR A 67 10761 11164 8223 -299 -397 -1810 C
ATOM 312 CE2 TYR A 67 29.114 12.965 -66.411 1.00 82.66 C
ANISOU 312 CE2 TYR A 67 11157 11931 8320 -72 -322 -1675 C
ATOM 313 CZ TYR A 67 28.139 12.105 -65.952 1.00 85.39 C
ANISOU 313 CZ TYR A 67 11554 12159 8733 -247 -385 -1873 C
ATOM 314 OH TYR A 67 27.428 11.333 -66.842 1.00 92.05 O
ANISOU 314 OH TYR A 67 12478 13120 9376 -388 -428 -2141 O
ATOM 315 N TYR A 68 31.146 17.041 -61.367 1.00 64.35 N
ANISOU 315 N TYR A 68 8364 9104 6982 189 -331 -661 N
ATOM 316 CA TYR A 68 31.686 17.662 -60.163 1.00 66.15 C
ANISOU 316 CA TYR A 68 8521 9204 7407 210 -330 -527 C
ATOM 317 C TYR A 68 30.647 18.544 -59.482 1.00 68.67 C
ANISOU 317 C TYR A 68 8777 9513 7803 140 -435 -450 C
ATOM 318 O TYR A 68 30.567 18.587 -58.247 1.00 78.84 O
ANISOU 318 O TYR A 68 10054 10663 9239 108 -457 -434 O
ATOM 319 CB TYR A 68 32.917 18.488 -60.510 1.00 68.79 C
ANISOU 319 CB TYR A 68 8777 9607 7753 288 -245 -379 C
ATOM 320 CG TYR A 68 34.060 17.758 -61.177 1.00 72.42 C
ANISOU 320 CG TYR A 68 9259 10109 8149 381 -116 -442 C
ATOM 321 CD1 TYR A 68 34.956 16.998 -60.432 1.00 75.69 C
ANISOU 321 CD1 TYR A 68 9672 10400 8688 456 -64 -490 C
ATOM 322 CD2 TYR A 68 34.276 17.870 -62.543 1.00 70.90 C
ANISOU 322 CD2 TYR A 68 9083 10092 7763 413 -41 -445 C
ATOM 323 CE1 TYR A 68 36.016 16.343 -61.037 1.00 75.08 C
ANISOU 323 CE1 TYR A 68 9593 10367 8566 574 65 -551 C
ATOM 324 CE2 TYR A 68 35.333 17.222 -63.154 1.00 71.83 C
ANISOU 324 CE2 TYR A 68 9212 10259 7821 508 102 -515 C
ATOM 325 CZ TYR A 68 36.200 16.463 -62.397 1.00 73.56 C
ANISOU 325 CZ TYR A 68 9412 10348 8189 595 157 -573 C
ATOM 326 OH TYR A 68 37.251 15.820 -63.005 1.00 80.48 O
ANISOU 326 OH TYR A 68 10281 11279 9019 721 309 -648 O
ATOM 327 N LEU A 69 29.867 19.285 -60.275 1.00 69.53 N
ANISOU 327 N LEU A 69 8842 9775 7801 134 -497 -394 N
ATOM 328 CA LEU A 69 28.793 20.102 -59.719 1.00 64.86 C
ANISOU 328 CA LEU A 69 8179 9185 7280 102 -592 -332 C
ATOM 329 C LEU A 69 27.730 19.235 -59.055 1.00 67.08 C
ANISOU 329 C LEU A 69 8468 9416 7602 -1 -647 -493 C
ATOM 330 O LEU A 69 27.129 19.640 -58.055 1.00 70.29 O
ANISOU 330 O LEU A 69 8823 9750 8133 -37 -679 -470 O
ATOM 331 CB LEU A 69 28.185 20.978 -60.814 1.00 60.65 C
ANISOU 331 CB LEU A 69 7601 8843 6602 156 -654 -230 C
ATOM 332 CG LEU A 69 29.172 21.850 -61.601 1.00 58.67 C
ANISOU 332 CG LEU A 69 7366 8642 6283 238 -577 -52 C
ATOM 333 CD1 LEU A 69 28.417 22.830 -62.479 1.00 57.23 C
ANISOU 333 CD1 LEU A 69 7160 8615 5969 310 -652 91 C
ATOM 334 CD2 LEU A 69 30.124 22.593 -60.669 1.00 58.08 C
ANISOU 334 CD2 LEU A 69 7269 8394 6405 237 -500 66 C
ATOM 335 N LEU A 70 27.499 18.036 -59.593 1.00 66.64 N
ANISOU 335 N LEU A 70 8485 9392 7443 -63 -639 -667 N
ATOM 336 CA LEU A 70 26.580 17.090 -58.967 1.00 68.99 C
ANISOU 336 CA LEU A 70 8810 9614 7789 -198 -661 -830 C
ATOM 337 C LEU A 70 27.116 16.605 -57.622 1.00 65.70 C
ANISOU 337 C LEU A 70 8473 8957 7534 -215 -590 -821 C
ATOM 338 O LEU A 70 26.356 16.470 -56.653 1.00 66.29 O
ANISOU 338 O LEU A 70 8533 8955 7698 -310 -602 -852 O
ATOM 339 CB LEU A 70 26.341 15.909 -59.906 1.00 72.24 C
ANISOU 339 CB LEU A 70 9311 10082 8054 -277 -651 -1032 C
ATOM 340 CG LEU A 70 25.038 15.132 -59.729 1.00 80.45 C
ANISOU 340 CG LEU A 70 10337 11140 9090 -464 -700 -1219 C
ATOM 341 CD1 LEU A 70 23.842 16.061 -59.870 1.00 85.95 C
ANISOU 341 CD1 LEU A 70 10837 12061 9761 -485 -828 -1173 C
ATOM 342 CD2 LEU A 70 24.960 13.985 -60.726 1.00 82.24 C
ANISOU 342 CD2 LEU A 70 10677 11405 9167 -554 -680 -1441 C
ATOM 343 N SER A 71 28.418 16.309 -57.561 1.00 57.53 N
ANISOU 343 N SER A 71 7515 7820 6524 -119 -513 -779 N
ATOM 344 CA SER A 71 29.072 15.997 -56.288 1.00 58.42 C
ANISOU 344 CA SER A 71 7686 7740 6770 -93 -471 -733 C
ATOM 345 C SER A 71 28.887 17.126 -55.269 1.00 54.54 C
ANISOU 345 C SER A 71 7098 7240 6383 -100 -515 -607 C
ATOM 346 O SER A 71 28.580 16.881 -54.088 1.00 54.10 O
ANISOU 346 O SER A 71 7084 7067 6406 -156 -513 -613 O
ATOM 347 CB SER A 71 30.554 15.725 -56.537 1.00 61.12 C
ANISOU 347 CB SER A 71 8063 8044 7116 47 -400 -691 C
ATOM 348 OG SER A 71 31.228 15.395 -55.336 1.00 68.39 O
ANISOU 348 OG SER A 71 9028 8811 8148 97 -383 -639 O
ATOM 349 N LEU A 72 29.101 18.370 -55.714 1.00 49.83 N
ANISOU 349 N LEU A 72 6395 6756 5781 -44 -541 -492 N
ATOM 350 CA LEU A 72 28.874 19.533 -54.858 1.00 51.02 C
ANISOU 350 CA LEU A 72 6471 6883 6032 -51 -573 -393 C
ATOM 351 C LEU A 72 27.432 19.588 -54.375 1.00 55.48 C
ANISOU 351 C LEU A 72 7002 7462 6617 -136 -614 -455 C
ATOM 352 O LEU A 72 27.177 19.895 -53.208 1.00 54.89 O
ANISOU 352 O LEU A 72 6922 7304 6629 -171 -610 -443 O
ATOM 353 CB LEU A 72 29.230 20.826 -55.589 1.00 51.41 C
ANISOU 353 CB LEU A 72 6442 7021 6069 15 -577 -261 C
ATOM 354 CG LEU A 72 30.672 21.310 -55.491 1.00 55.09 C
ANISOU 354 CG LEU A 72 6890 7453 6589 61 -524 -165 C
ATOM 355 CD1 LEU A 72 30.837 22.598 -56.286 1.00 52.73 C
ANISOU 355 CD1 LEU A 72 6540 7221 6275 94 -507 -28 C
ATOM 356 CD2 LEU A 72 31.062 21.510 -54.036 1.00 55.68 C
ANISOU 356 CD2 LEU A 72 6961 7406 6789 28 -534 -159 C
ATOM 357 N ALA A 73 26.479 19.326 -55.273 1.00 53.19 N
ANISOU 357 N ALA A 73 6672 7302 6236 -170 -654 -529 N
ATOM 358 CA ALA A 73 25.070 19.343 -54.902 1.00 52.58 C
ANISOU 358 CA ALA A 73 6515 7283 6180 -255 -692 -603 C
ATOM 359 C ALA A 73 24.752 18.266 -53.874 1.00 57.78 C
ANISOU 359 C ALA A 73 7257 7809 6888 -385 -637 -710 C
ATOM 360 O ALA A 73 23.897 18.478 -53.013 1.00 65.94 O
ANISOU 360 O ALA A 73 8233 8835 7985 -453 -627 -733 O
ATOM 361 CB ALA A 73 24.190 19.174 -56.142 1.00 49.07 C
ANISOU 361 CB ALA A 73 5991 7044 5610 -275 -765 -677 C
ATOM 362 N CYS A 74 25.425 17.113 -53.947 1.00 55.93 N
ANISOU 362 N CYS A 74 7166 7461 6624 -413 -587 -771 N
ATOM 363 CA CYS A 74 25.241 16.076 -52.929 1.00 59.21 C
ANISOU 363 CA CYS A 74 7706 7706 7083 -523 -520 -836 C
ATOM 364 C CYS A 74 25.724 16.554 -51.563 1.00 65.40 C
ANISOU 364 C CYS A 74 8521 8380 7947 -480 -496 -728 C
ATOM 365 O CYS A 74 25.027 16.385 -50.548 1.00 75.86 O
ANISOU 365 O CYS A 74 9867 9650 9305 -580 -457 -750 O
ATOM 366 CB CYS A 74 25.977 14.794 -53.323 1.00 58.48 C
ANISOU 366 CB CYS A 74 7788 7481 6950 -516 -464 -903 C
ATOM 367 SG CYS A 74 25.279 13.915 -54.734 1.00 68.26 S
ANISOU 367 SG CYS A 74 9045 8811 8078 -628 -471 -1098 S
ATOM 368 N ALA A 75 26.932 17.136 -51.522 1.00 57.61 N
ANISOU 368 N ALA A 75 7533 7376 6978 -345 -515 -619 N
ATOM 369 CA ALA A 75 27.440 17.699 -50.267 1.00 55.35 C
ANISOU 369 CA ALA A 75 7260 7021 6750 -314 -516 -534 C
ATOM 370 C ALA A 75 26.508 18.780 -49.728 1.00 53.98 C
ANISOU 370 C ALA A 75 6982 6910 6620 -359 -528 -529 C
ATOM 371 O ALA A 75 26.205 18.818 -48.527 1.00 63.52 O
ANISOU 371 O ALA A 75 8230 8058 7848 -413 -498 -533 O
ATOM 372 CB ALA A 75 28.847 18.261 -50.466 1.00 53.04 C
ANISOU 372 CB ALA A 75 6935 6743 6476 -189 -543 -440 C
ATOM 373 N ASP A 76 25.999 19.631 -50.616 1.00 49.74 N
ANISOU 373 N ASP A 76 6318 6493 6087 -325 -564 -520 N
ATOM 374 CA ASP A 76 25.137 20.728 -50.203 1.00 50.28 C
ANISOU 374 CA ASP A 76 6282 6611 6212 -321 -570 -509 C
ATOM 375 C ASP A 76 23.772 20.237 -49.742 1.00 51.72 C
ANISOU 375 C ASP A 76 6420 6835 6394 -433 -534 -613 C
ATOM 376 O ASP A 76 23.174 20.835 -48.843 1.00 44.85 O
ANISOU 376 O ASP A 76 5505 5961 5574 -448 -498 -625 O
ATOM 377 CB ASP A 76 24.987 21.720 -51.353 1.00 47.17 C
ANISOU 377 CB ASP A 76 5782 6327 5815 -222 -620 -445 C
ATOM 378 CG ASP A 76 26.290 22.419 -51.687 1.00 56.91 C
ANISOU 378 CG ASP A 76 7046 7513 7065 -140 -624 -332 C
ATOM 379 OD1 ASP A 76 27.251 22.292 -50.894 1.00 53.00 O
ANISOU 379 OD1 ASP A 76 6617 6919 6600 -157 -603 -318 O
ATOM 380 OD2 ASP A 76 26.356 23.090 -52.741 1.00 61.32 O
ANISOU 380 OD2 ASP A 76 7557 8145 7598 -64 -648 -255 O
ATOM 381 N LEU A 77 23.270 19.149 -50.330 1.00 45.20 N
ANISOU 381 N LEU A 77 5606 6053 5515 -526 -531 -702 N
ATOM 382 CA LEU A 77 22.011 18.575 -49.874 1.00 54.99 C
ANISOU 382 CA LEU A 77 6796 7335 6762 -676 -480 -812 C
ATOM 383 C LEU A 77 22.165 17.945 -48.499 1.00 62.92 C
ANISOU 383 C LEU A 77 7949 8183 7777 -771 -383 -814 C
ATOM 384 O LEU A 77 21.257 18.045 -47.664 1.00 61.47 O
ANISOU 384 O LEU A 77 7712 8026 7617 -861 -313 -859 O
ATOM 385 CB LEU A 77 21.502 17.546 -50.882 1.00 53.20 C
ANISOU 385 CB LEU A 77 6556 7184 6474 -786 -499 -927 C
ATOM 386 CG LEU A 77 20.067 17.068 -50.645 1.00 57.52 C
ANISOU 386 CG LEU A 77 6987 7831 7037 -971 -457 -1061 C
ATOM 387 CD1 LEU A 77 19.094 18.233 -50.649 1.00 59.81 C
ANISOU 387 CD1 LEU A 77 7033 8320 7374 -896 -500 -1053 C
ATOM 388 CD2 LEU A 77 19.654 16.025 -51.669 1.00 61.71 C
ANISOU 388 CD2 LEU A 77 7516 8430 7502 -1111 -484 -1202 C
ATOM 389 N ILE A 78 23.295 17.269 -48.265 1.00 63.07 N
ANISOU 389 N ILE A 78 8150 8048 7764 -740 -373 -760 N
ATOM 390 CA ILE A 78 23.607 16.758 -46.931 1.00 56.99 C
ANISOU 390 CA ILE A 78 7542 7133 6977 -787 -302 -720 C
ATOM 391 C ILE A 78 23.615 17.896 -45.917 1.00 56.07 C
ANISOU 391 C ILE A 78 7374 7048 6880 -738 -300 -674 C
ATOM 392 O ILE A 78 23.038 17.784 -44.827 1.00 57.54 O
ANISOU 392 O ILE A 78 7606 7211 7045 -828 -218 -693 O
ATOM 393 CB ILE A 78 24.948 16.006 -46.942 1.00 57.75 C
ANISOU 393 CB ILE A 78 7813 7089 7040 -696 -322 -649 C
ATOM 394 CG1 ILE A 78 24.822 14.690 -47.706 1.00 61.66 C
ANISOU 394 CG1 ILE A 78 8416 7497 7515 -765 -282 -722 C
ATOM 395 CG2 ILE A 78 25.438 15.763 -45.525 1.00 55.41 C
ANISOU 395 CG2 ILE A 78 7668 6680 6704 -686 -289 -568 C
ATOM 396 CD1 ILE A 78 26.124 13.896 -47.759 1.00 62.97 C
ANISOU 396 CD1 ILE A 78 8753 7513 7660 -637 -287 -656 C
ATOM 397 N ILE A 79 24.284 19.002 -46.261 1.00 53.66 N
ANISOU 397 N ILE A 79 6990 6788 6611 -606 -376 -619 N
ATOM 398 CA ILE A 79 24.318 20.174 -45.385 1.00 53.98 C
ANISOU 398 CA ILE A 79 6992 6838 6680 -566 -371 -602 C
ATOM 399 C ILE A 79 22.910 20.715 -45.135 1.00 59.94 C
ANISOU 399 C ILE A 79 7621 7679 7474 -614 -307 -679 C
ATOM 400 O ILE A 79 22.558 21.074 -44.003 1.00 61.31 O
ANISOU 400 O ILE A 79 7819 7839 7636 -649 -238 -710 O
ATOM 401 CB ILE A 79 25.248 21.250 -45.977 1.00 49.63 C
ANISOU 401 CB ILE A 79 6381 6297 6178 -444 -448 -536 C
ATOM 402 CG1 ILE A 79 26.694 20.750 -45.983 1.00 53.74 C
ANISOU 402 CG1 ILE A 79 6994 6760 6665 -398 -498 -470 C
ATOM 403 CG2 ILE A 79 25.139 22.569 -45.207 1.00 35.96 C
ANISOU 403 CG2 ILE A 79 4614 4554 4497 -418 -433 -547 C
ATOM 404 CD1 ILE A 79 27.251 20.503 -44.610 1.00 56.43 C
ANISOU 404 CD1 ILE A 79 7450 7042 6949 -421 -497 -455 C
ATOM 405 N GLY A 80 22.079 20.764 -46.178 1.00 58.25 N
ANISOU 405 N GLY A 80 7261 7577 7295 -609 -329 -718 N
ATOM 406 CA GLY A 80 20.773 21.392 -46.046 1.00 60.48 C
ANISOU 406 CA GLY A 80 7374 7977 7630 -611 -284 -786 C
ATOM 407 C GLY A 80 19.783 20.560 -45.251 1.00 64.20 C
ANISOU 407 C GLY A 80 7838 8479 8075 -781 -168 -878 C
ATOM 408 O GLY A 80 18.953 21.102 -44.516 1.00 65.64 O
ANISOU 408 O GLY A 80 7929 8723 8290 -789 -83 -933 O
ATOM 409 N ILE A 81 19.845 19.236 -45.392 1.00 65.14 N
ANISOU 409 N ILE A 81 8061 8550 8141 -921 -144 -900 N
ATOM 410 CA ILE A 81 18.906 18.372 -44.679 1.00 63.65 C
ANISOU 410 CA ILE A 81 7884 8370 7930 -1120 -11 -979 C
ATOM 411 C ILE A 81 19.335 18.186 -43.228 1.00 66.48 C
ANISOU 411 C ILE A 81 8441 8598 8220 -1162 89 -928 C
ATOM 412 O ILE A 81 18.590 18.505 -42.296 1.00 66.73 O
ANISOU 412 O ILE A 81 8426 8685 8244 -1222 205 -973 O
ATOM 413 CB ILE A 81 18.755 17.019 -45.396 1.00 63.21 C
ANISOU 413 CB ILE A 81 7890 8278 7850 -1276 -6 -1032 C
ATOM 414 CG1 ILE A 81 18.204 17.217 -46.808 1.00 60.93 C
ANISOU 414 CG1 ILE A 81 7388 8169 7593 -1251 -113 -1105 C
ATOM 415 CG2 ILE A 81 17.851 16.094 -44.598 1.00 65.35 C
ANISOU 415 CG2 ILE A 81 8204 8523 8104 -1518 157 -1102 C
ATOM 416 CD1 ILE A 81 18.139 15.936 -47.617 1.00 62.00 C
ANISOU 416 CD1 ILE A 81 7597 8268 7693 -1409 -120 -1189 C
ATOM 417 N PHE A 82 20.541 17.666 -43.017 1.00 70.64 N
ANISOU 417 N PHE A 82 9186 8969 8685 -1119 44 -833 N
ATOM 418 CA PHE A 82 20.971 17.238 -41.692 1.00 66.25 C
ANISOU 418 CA PHE A 82 8845 8300 8029 -1162 119 -768 C
ATOM 419 C PHE A 82 21.713 18.329 -40.925 1.00 66.71 C
ANISOU 419 C PHE A 82 8926 8367 8051 -1029 66 -725 C
ATOM 420 O PHE A 82 21.348 18.632 -39.785 1.00 72.87 O
ANISOU 420 O PHE A 82 9752 9171 8764 -1076 157 -746 O
ATOM 421 CB PHE A 82 21.838 15.984 -41.808 1.00 66.02 C
ANISOU 421 CB PHE A 82 9042 8100 7944 -1171 98 -685 C
ATOM 422 CG PHE A 82 21.181 14.871 -42.567 1.00 76.06 C
ANISOU 422 CG PHE A 82 10326 9322 9250 -1323 159 -750 C
ATOM 423 CD1 PHE A 82 20.258 14.045 -41.941 1.00 79.99 C
ANISOU 423 CD1 PHE A 82 10905 9769 9719 -1538 321 -785 C
ATOM 424 CD2 PHE A 82 21.478 14.650 -43.903 1.00 75.52 C
ANISOU 424 CD2 PHE A 82 10197 9261 9236 -1271 66 -789 C
ATOM 425 CE1 PHE A 82 19.644 13.015 -42.632 1.00 81.81 C
ANISOU 425 CE1 PHE A 82 11152 9943 9990 -1717 384 -870 C
ATOM 426 CE2 PHE A 82 20.867 13.621 -44.603 1.00 77.36 C
ANISOU 426 CE2 PHE A 82 10453 9451 9491 -1432 119 -882 C
ATOM 427 CZ PHE A 82 19.949 12.801 -43.966 1.00 78.30 C
ANISOU 427 CZ PHE A 82 10649 9505 9597 -1664 276 -929 C
ATOM 428 N SER A 83 22.757 18.908 -41.530 1.00 63.69 N
ANISOU 428 N SER A 83 8519 7973 7709 -882 -71 -677 N
ATOM 429 CA SER A 83 23.678 19.786 -40.806 1.00 65.17 C
ANISOU 429 CA SER A 83 8753 8150 7858 -789 -135 -643 C
ATOM 430 C SER A 83 22.979 21.022 -40.253 1.00 65.49 C
ANISOU 430 C SER A 83 8692 8260 7932 -783 -76 -730 C
ATOM 431 O SER A 83 23.153 21.372 -39.076 1.00 69.10 O
ANISOU 431 O SER A 83 9243 8713 8298 -801 -40 -751 O
ATOM 432 CB SER A 83 24.824 20.202 -41.726 1.00 60.91 C
ANISOU 432 CB SER A 83 8164 7599 7381 -664 -270 -589 C
ATOM 433 OG SER A 83 25.644 19.090 -42.033 1.00 63.21 O
ANISOU 433 OG SER A 83 8566 7821 7630 -638 -316 -513 O
ATOM 434 N MET A 84 22.185 21.696 -41.091 1.00 61.47 N
ANISOU 434 N MET A 84 7997 7817 7541 -742 -66 -785 N
ATOM 435 CA MET A 84 21.517 22.924 -40.672 1.00 62.61 C
ANISOU 435 CA MET A 84 8041 8004 7742 -691 -4 -867 C
ATOM 436 C MET A 84 20.537 22.662 -39.534 1.00 62.04 C
ANISOU 436 C MET A 84 7991 7985 7598 -797 156 -948 C
ATOM 437 O MET A 84 20.540 23.371 -38.523 1.00 60.48 O
ANISOU 437 O MET A 84 7849 7779 7352 -784 219 -1008 O
ATOM 438 CB MET A 84 20.805 23.566 -41.864 1.00 58.54 C
ANISOU 438 CB MET A 84 7321 7559 7362 -595 -32 -882 C
ATOM 439 CG MET A 84 21.742 24.276 -42.817 1.00 61.59 C
ANISOU 439 CG MET A 84 7697 7890 7816 -474 -156 -802 C
ATOM 440 SD MET A 84 20.909 24.943 -44.272 1.00 64.85 S
ANISOU 440 SD MET A 84 7899 8397 8342 -341 -203 -780 S
ATOM 441 CE MET A 84 22.312 25.590 -45.178 1.00 69.17 C
ANISOU 441 CE MET A 84 8513 8847 8922 -246 -316 -657 C
ATOM 442 N ASN A 85 19.723 21.614 -39.665 1.00 58.18 N
ANISOU 442 N ASN A 85 7469 7548 7089 -920 236 -959 N
ATOM 443 CA ASN A 85 18.684 21.355 -38.677 1.00 67.84 C
ANISOU 443 CA ASN A 85 8684 8840 8251 -1043 419 -1035 C
ATOM 444 C ASN A 85 19.277 20.897 -37.348 1.00 70.43 C
ANISOU 444 C ASN A 85 9265 9097 8398 -1119 476 -990 C
ATOM 445 O ASN A 85 18.864 21.380 -36.286 1.00 72.34 O
ANISOU 445 O ASN A 85 9538 9387 8561 -1143 599 -1060 O
ATOM 446 CB ASN A 85 17.700 20.330 -39.233 1.00 70.82 C
ANISOU 446 CB ASN A 85 8953 9291 8665 -1192 491 -1064 C
ATOM 447 CG ASN A 85 17.005 20.826 -40.485 1.00 72.13 C
ANISOU 447 CG ASN A 85 8844 9583 8980 -1110 419 -1118 C
ATOM 448 OD1 ASN A 85 16.641 21.999 -40.581 1.00 67.59 O
ANISOU 448 OD1 ASN A 85 8116 9078 8487 -961 411 -1164 O
ATOM 449 ND2 ASN A 85 16.837 19.942 -41.460 1.00 77.78 N
ANISOU 449 ND2 ASN A 85 9510 10322 9721 -1197 363 -1114 N
ATOM 450 N LEU A 86 20.260 19.991 -37.388 1.00 63.40 N
ANISOU 450 N LEU A 86 8561 8101 7426 -1138 388 -873 N
ATOM 451 CA LEU A 86 20.927 19.554 -36.163 1.00 61.20 C
ANISOU 451 CA LEU A 86 8530 7768 6955 -1173 407 -801 C
ATOM 452 C LEU A 86 21.643 20.713 -35.474 1.00 58.97 C
ANISOU 452 C LEU A 86 8280 7513 6614 -1071 333 -842 C
ATOM 453 O LEU A 86 21.570 20.850 -34.245 1.00 61.42 O
ANISOU 453 O LEU A 86 8716 7861 6759 -1117 414 -870 O
ATOM 454 CB LEU A 86 21.901 18.416 -36.468 1.00 61.48 C
ANISOU 454 CB LEU A 86 8737 7683 6941 -1158 306 -658 C
ATOM 455 CG LEU A 86 21.232 17.112 -36.906 1.00 64.37 C
ANISOU 455 CG LEU A 86 9151 7976 7332 -1298 408 -627 C
ATOM 456 CD1 LEU A 86 22.251 16.094 -37.376 1.00 62.52 C
ANISOU 456 CD1 LEU A 86 9080 7592 7082 -1237 305 -503 C
ATOM 457 CD2 LEU A 86 20.414 16.552 -35.764 1.00 65.67 C
ANISOU 457 CD2 LEU A 86 9447 8144 7362 -1467 611 -619 C
ATOM 458 N TYR A 87 22.317 21.573 -36.246 1.00 60.32 N
ANISOU 458 N TYR A 87 8344 7666 6909 -949 191 -856 N
ATOM 459 CA TYR A 87 23.029 22.692 -35.633 1.00 64.12 C
ANISOU 459 CA TYR A 87 8858 8154 7352 -886 124 -916 C
ATOM 460 C TYR A 87 22.072 23.694 -35.006 1.00 71.86 C
ANISOU 460 C TYR A 87 9776 9182 8345 -895 268 -1069 C
ATOM 461 O TYR A 87 22.337 24.221 -33.915 1.00 76.65 O
ANISOU 461 O TYR A 87 10495 9809 8819 -914 293 -1145 O
ATOM 462 CB TYR A 87 23.904 23.392 -36.664 1.00 61.84 C
ANISOU 462 CB TYR A 87 8467 7817 7211 -783 -29 -894 C
ATOM 463 CG TYR A 87 24.830 24.407 -36.049 1.00 65.86 C
ANISOU 463 CG TYR A 87 9025 8316 7682 -760 -111 -954 C
ATOM 464 CD1 TYR A 87 25.914 24.003 -35.296 1.00 71.42 C
ANISOU 464 CD1 TYR A 87 9860 9052 8224 -780 -219 -905 C
ATOM 465 CD2 TYR A 87 24.625 25.768 -36.226 1.00 69.05 C
ANISOU 465 CD2 TYR A 87 9347 8678 8212 -718 -85 -1062 C
ATOM 466 CE1 TYR A 87 26.767 24.906 -34.728 1.00 72.28 C
ANISOU 466 CE1 TYR A 87 9994 9179 8290 -790 -307 -983 C
ATOM 467 CE2 TYR A 87 25.487 26.692 -35.658 1.00 75.59 C
ANISOU 467 CE2 TYR A 87 10231 9477 9011 -734 -152 -1142 C
ATOM 468 CZ TYR A 87 26.558 26.245 -34.910 1.00 73.60 C
ANISOU 468 CZ TYR A 87 10087 9287 8590 -785 -268 -1111 C
ATOM 469 OH TYR A 87 27.437 27.118 -34.325 1.00 76.59 O
ANISOU 469 OH TYR A 87 10504 9669 8926 -831 -351 -1211 O
ATOM 470 N THR A 88 20.955 23.971 -35.677 1.00 75.17 N
ANISOU 470 N THR A 88 10013 9633 8917 -870 362 -1125 N
ATOM 471 CA THR A 88 20.017 24.944 -35.139 1.00 81.00 C
ANISOU 471 CA THR A 88 10670 10417 9691 -837 511 -1274 C
ATOM 472 C THR A 88 19.284 24.402 -33.920 1.00 81.27 C
ANISOU 472 C THR A 88 10792 10537 9549 -960 699 -1328 C
ATOM 473 O THR A 88 19.037 25.150 -32.970 1.00 79.09 O
ANISOU 473 O THR A 88 10566 10289 9196 -950 807 -1455 O
ATOM 474 CB THR A 88 19.058 25.395 -36.227 1.00 85.58 C
ANISOU 474 CB THR A 88 11003 11032 10480 -742 539 -1304 C
ATOM 475 OG1 THR A 88 18.467 24.250 -36.856 1.00 98.04 O
ANISOU 475 OG1 THR A 88 12491 12684 12076 -829 555 -1240 O
ATOM 476 CG2 THR A 88 19.837 26.181 -37.234 1.00 84.51 C
ANISOU 476 CG2 THR A 88 10827 10800 10484 -612 379 -1252 C
ATOM 477 N THR A 89 18.946 23.107 -33.912 1.00 75.45 N
ANISOU 477 N THR A 89 10095 9832 8739 -1088 756 -1238 N
ATOM 478 CA THR A 89 18.376 22.525 -32.700 1.00 77.41 C
ANISOU 478 CA THR A 89 10472 10150 8792 -1227 947 -1257 C
ATOM 479 C THR A 89 19.382 22.561 -31.555 1.00 72.47 C
ANISOU 479 C THR A 89 10110 9501 7924 -1236 890 -1226 C
ATOM 480 O THR A 89 19.010 22.830 -30.407 1.00 72.49 O
ANISOU 480 O THR A 89 10209 9579 7755 -1287 1037 -1312 O
ATOM 481 CB THR A 89 17.889 21.094 -32.950 1.00 80.95 C
ANISOU 481 CB THR A 89 10944 10595 9217 -1384 1024 -1153 C
ATOM 482 OG1 THR A 89 18.971 20.283 -33.426 1.00 84.71 O
ANISOU 482 OG1 THR A 89 11567 10950 9668 -1370 848 -998 O
ATOM 483 CG2 THR A 89 16.722 21.068 -33.937 1.00 76.35 C
ANISOU 483 CG2 THR A 89 10072 10094 8845 -1411 1096 -1224 C
ATOM 484 N TYR A 90 20.664 22.331 -31.855 1.00 69.42 N
ANISOU 484 N TYR A 90 9828 9037 7513 -1179 673 -1114 N
ATOM 485 CA TYR A 90 21.693 22.393 -30.820 1.00 71.59 C
ANISOU 485 CA TYR A 90 10318 9328 7555 -1173 577 -1086 C
ATOM 486 C TYR A 90 21.803 23.794 -30.223 1.00 79.21 C
ANISOU 486 C TYR A 90 11267 10333 8496 -1130 583 -1273 C
ATOM 487 O TYR A 90 21.856 23.953 -28.998 1.00 86.88 O
ANISOU 487 O TYR A 90 12398 11382 9229 -1181 645 -1339 O
ATOM 488 CB TYR A 90 23.031 21.936 -31.399 1.00 69.38 C
ANISOU 488 CB TYR A 90 10085 8981 7294 -1099 338 -942 C
ATOM 489 CG TYR A 90 24.213 22.089 -30.469 1.00 71.01 C
ANISOU 489 CG TYR A 90 10455 9242 7284 -1071 187 -919 C
ATOM 490 CD1 TYR A 90 24.183 21.571 -29.182 1.00 76.97 C
ANISOU 490 CD1 TYR A 90 11428 10074 7741 -1132 249 -874 C
ATOM 491 CD2 TYR A 90 25.375 22.720 -30.894 1.00 68.89 C
ANISOU 491 CD2 TYR A 90 10115 8966 7095 -992 -21 -935 C
ATOM 492 CE1 TYR A 90 25.272 21.699 -28.333 1.00 80.59 C
ANISOU 492 CE1 TYR A 90 12023 10623 7976 -1098 81 -853 C
ATOM 493 CE2 TYR A 90 26.468 22.851 -30.055 1.00 72.25 C
ANISOU 493 CE2 TYR A 90 10652 9480 7321 -978 -179 -928 C
ATOM 494 CZ TYR A 90 26.411 22.337 -28.777 1.00 77.33 C
ANISOU 494 CZ TYR A 90 11504 10219 7658 -1023 -141 -889 C
ATOM 495 OH TYR A 90 27.495 22.464 -27.936 1.00 78.47 O
ANISOU 495 OH TYR A 90 11746 10489 7578 -1002 -324 -884 O
ATOM 496 N ILE A 91 21.843 24.827 -31.071 1.00 80.94 N
ANISOU 496 N ILE A 91 11315 10488 8949 -1037 525 -1363 N
ATOM 497 CA ILE A 91 21.990 26.180 -30.532 1.00 82.94 C
ANISOU 497 CA ILE A 91 11583 10729 9201 -1001 541 -1551 C
ATOM 498 C ILE A 91 20.702 26.667 -29.861 1.00 82.83 C
ANISOU 498 C ILE A 91 11538 10772 9161 -1011 794 -1716 C
ATOM 499 O ILE A 91 20.760 27.455 -28.909 1.00 79.72 O
ANISOU 499 O ILE A 91 11250 10398 8642 -1022 859 -1883 O
ATOM 500 CB ILE A 91 22.481 27.168 -31.610 1.00 87.36 C
ANISOU 500 CB ILE A 91 12007 11168 10018 -901 418 -1579 C
ATOM 501 CG1 ILE A 91 21.466 27.314 -32.743 1.00 93.52 C
ANISOU 501 CG1 ILE A 91 12577 11910 11045 -812 500 -1559 C
ATOM 502 CG2 ILE A 91 23.847 26.740 -32.134 1.00 88.95 C
ANISOU 502 CG2 ILE A 91 12234 11343 10219 -901 187 -1438 C
ATOM 503 CD1 ILE A 91 21.963 28.143 -33.913 1.00 98.13 C
ANISOU 503 CD1 ILE A 91 13053 12373 11860 -707 379 -1531 C
ATOM 504 N LEU A 92 19.527 26.223 -30.327 1.00 81.35 N
ANISOU 504 N LEU A 92 11196 10626 9086 -1011 947 -1691 N
ATOM 505 CA LEU A 92 18.285 26.682 -29.710 1.00 77.32 C
ANISOU 505 CA LEU A 92 10614 10198 8565 -1008 1202 -1853 C
ATOM 506 C LEU A 92 18.054 26.013 -28.362 1.00 80.82 C
ANISOU 506 C LEU A 92 11248 10761 8698 -1150 1358 -1863 C
ATOM 507 O LEU A 92 17.573 26.658 -27.423 1.00 86.55 O
ANISOU 507 O LEU A 92 12026 11552 9308 -1150 1533 -2039 O
ATOM 508 CB LEU A 92 17.096 26.441 -30.640 1.00 74.37 C
ANISOU 508 CB LEU A 92 9972 9873 8414 -969 1306 -1833 C
ATOM 509 CG LEU A 92 16.969 27.354 -31.865 1.00 72.77 C
ANISOU 509 CG LEU A 92 9560 9586 8503 -789 1210 -1854 C
ATOM 510 CD1 LEU A 92 15.616 27.162 -32.535 1.00 73.25 C
ANISOU 510 CD1 LEU A 92 9336 9764 8731 -747 1333 -1869 C
ATOM 511 CD2 LEU A 92 17.190 28.816 -31.499 1.00 73.41 C
ANISOU 511 CD2 LEU A 92 9692 9562 8640 -657 1232 -2019 C
ATOM 512 N MET A 93 18.388 24.724 -28.242 1.00 77.19 N
ANISOU 512 N MET A 93 10915 10324 8090 -1264 1310 -1674 N
ATOM 513 CA MET A 93 18.238 24.056 -26.954 1.00 76.55 C
ANISOU 513 CA MET A 93 11056 10345 7686 -1396 1455 -1644 C
ATOM 514 C MET A 93 19.287 24.506 -25.945 1.00 73.97 C
ANISOU 514 C MET A 93 10966 10045 7093 -1385 1332 -1694 C
ATOM 515 O MET A 93 19.114 24.270 -24.745 1.00 75.59 O
ANISOU 515 O MET A 93 11363 10363 6995 -1471 1465 -1717 O
ATOM 516 CB MET A 93 18.307 22.536 -27.123 1.00 78.87 C
ANISOU 516 CB MET A 93 11450 10614 7903 -1510 1445 -1409 C
ATOM 517 CG MET A 93 17.197 21.940 -27.967 1.00 82.84 C
ANISOU 517 CG MET A 93 11738 11116 8620 -1582 1588 -1381 C
ATOM 518 SD MET A 93 17.252 20.139 -27.990 1.00 88.87 S
ANISOU 518 SD MET A 93 12687 11807 9274 -1755 1622 -1131 S
ATOM 519 CE MET A 93 18.921 19.857 -28.587 1.00 87.48 C
ANISOU 519 CE MET A 93 12646 11483 9108 -1617 1267 -967 C
ATOM 520 N GLY A 94 20.368 25.143 -26.400 1.00 73.17 N
ANISOU 520 N GLY A 94 10851 9863 7086 -1296 1085 -1714 N
ATOM 521 CA GLY A 94 21.443 25.562 -25.525 1.00 74.02 C
ANISOU 521 CA GLY A 94 11149 10021 6956 -1305 933 -1774 C
ATOM 522 C GLY A 94 22.357 24.452 -25.064 1.00 74.04 C
ANISOU 522 C GLY A 94 11349 10084 6701 -1343 771 -1558 C
ATOM 523 O GLY A 94 23.327 24.727 -24.346 1.00 73.14 O
ANISOU 523 O GLY A 94 11372 10051 6368 -1346 605 -1594 O
ATOM 524 N ARG A 95 22.080 23.211 -25.451 1.00 73.79 N
ANISOU 524 N ARG A 95 11335 10014 6687 -1370 811 -1339 N
ATOM 525 CA ARG A 95 22.931 22.078 -25.128 1.00 78.29 C
ANISOU 525 CA ARG A 95 12100 10599 7047 -1366 663 -1102 C
ATOM 526 C ARG A 95 22.677 20.988 -26.158 1.00 78.94 C
ANISOU 526 C ARG A 95 12117 10546 7330 -1364 680 -909 C
ATOM 527 O ARG A 95 21.791 21.102 -27.009 1.00 76.73 O
ANISOU 527 O ARG A 95 11642 10202 7310 -1389 806 -970 O
ATOM 528 CB ARG A 95 22.672 21.571 -23.704 1.00 86.14 C
ANISOU 528 CB ARG A 95 13365 11723 7641 -1452 798 -1050 C
ATOM 529 CG ARG A 95 21.226 21.172 -23.424 1.00 94.48 C
ANISOU 529 CG ARG A 95 14429 12790 8679 -1578 1143 -1064 C
ATOM 530 CD ARG A 95 21.092 20.513 -22.055 1.00108.40 C
ANISOU 530 CD ARG A 95 16498 14673 10017 -1668 1276 -957 C
ATOM 531 NE ARG A 95 21.801 19.238 -21.979 1.00119.07 N
ANISOU 531 NE ARG A 95 18065 15957 11220 -1642 1146 -650 N
ATOM 532 CZ ARG A 95 21.215 18.051 -22.102 1.00125.23 C
ANISOU 532 CZ ARG A 95 18951 16627 12005 -1734 1317 -449 C
ATOM 533 NH1 ARG A 95 19.906 17.974 -22.296 1.00125.56 N
ANISOU 533 NH1 ARG A 95 18873 16651 12184 -1883 1619 -532 N
ATOM 534 NH2 ARG A 95 21.935 16.940 -22.023 1.00128.42 N
ANISOU 534 NH2 ARG A 95 19578 16936 12281 -1678 1193 -169 N
ATOM 535 N TRP A 96 23.474 19.930 -26.074 1.00 80.59 N
ANISOU 535 N TRP A 96 12492 10716 7412 -1324 544 -683 N
ATOM 536 CA TRP A 96 23.287 18.746 -26.898 1.00 82.55 C
ANISOU 536 CA TRP A 96 12747 10813 7805 -1333 576 -500 C
ATOM 537 C TRP A 96 22.530 17.701 -26.088 1.00 87.98 C
ANISOU 537 C TRP A 96 13667 11483 8278 -1463 804 -364 C
ATOM 538 O TRP A 96 23.034 17.218 -25.069 1.00 88.65 O
ANISOU 538 O TRP A 96 14015 11619 8050 -1445 768 -223 O
ATOM 539 CB TRP A 96 24.626 18.190 -27.380 1.00 76.79 C
ANISOU 539 CB TRP A 96 12062 10016 7098 -1185 309 -332 C
ATOM 540 CG TRP A 96 24.448 17.108 -28.381 1.00 74.69 C
ANISOU 540 CG TRP A 96 11788 9571 7021 -1183 343 -193 C
ATOM 541 CD1 TRP A 96 24.470 15.764 -28.150 1.00 71.29 C
ANISOU 541 CD1 TRP A 96 11593 9015 6478 -1196 403 22 C
ATOM 542 CD2 TRP A 96 24.191 17.272 -29.779 1.00 74.47 C
ANISOU 542 CD2 TRP A 96 11523 9455 7318 -1174 331 -267 C
ATOM 543 NE1 TRP A 96 24.250 15.080 -29.318 1.00 71.74 N
ANISOU 543 NE1 TRP A 96 11575 8903 6781 -1208 432 61 N
ATOM 544 CE2 TRP A 96 24.078 15.983 -30.336 1.00 73.07 C
ANISOU 544 CE2 TRP A 96 11446 9110 7206 -1194 380 -116 C
ATOM 545 CE3 TRP A 96 24.051 18.384 -30.616 1.00 71.17 C
ANISOU 545 CE3 TRP A 96 10837 9076 7130 -1145 284 -441 C
ATOM 546 CZ2 TRP A 96 23.827 15.774 -31.692 1.00 68.63 C
ANISOU 546 CZ2 TRP A 96 10714 8450 6913 -1199 376 -157 C
ATOM 547 CZ3 TRP A 96 23.807 18.175 -31.962 1.00 71.44 C
ANISOU 547 CZ3 TRP A 96 10704 9019 7421 -1133 275 -449 C
ATOM 548 CH2 TRP A 96 23.700 16.880 -32.487 1.00 67.97 C
ANISOU 548 CH2 TRP A 96 10359 8444 7024 -1165 316 -319 C
ATOM 549 N ALA A 97 21.327 17.356 -26.540 1.00 95.93 N
ANISOU 549 N ALA A 97 14576 12430 9445 -1601 1038 -400 N
ATOM 550 CA ALA A 97 20.459 16.416 -25.841 1.00106.34 C
ANISOU 550 CA ALA A 97 16084 13724 10595 -1776 1306 -293 C
ATOM 551 C ALA A 97 20.173 15.183 -26.692 1.00108.60 C
ANISOU 551 C ALA A 97 16399 13809 11056 -1858 1367 -149 C
ATOM 552 O ALA A 97 19.076 14.623 -26.655 1.00120.57 O
ANISOU 552 O ALA A 97 17912 15293 12606 -2059 1627 -152 O
ATOM 553 CB ALA A 97 19.154 17.091 -25.430 1.00108.68 C
ANISOU 553 CB ALA A 97 16233 14162 10900 -1915 1582 -495 C
ATOM 554 N LEU A 98 21.162 14.737 -27.465 1.00 99.86 N
ANISOU 554 N LEU A 98 15316 12565 10060 -1715 1138 -35 N
ATOM 555 CA LEU A 98 20.999 13.575 -28.327 1.00 90.85 C
ANISOU 555 CA LEU A 98 14225 11209 9087 -1778 1182 78 C
ATOM 556 C LEU A 98 22.007 12.468 -28.060 1.00 84.98 C
ANISOU 556 C LEU A 98 13801 10290 8196 -1660 1071 341 C
ATOM 557 O LEU A 98 21.947 11.430 -28.729 1.00 84.00 O
ANISOU 557 O LEU A 98 13767 9945 8202 -1702 1116 438 O
ATOM 558 CB LEU A 98 21.072 13.979 -29.808 1.00 89.00 C
ANISOU 558 CB LEU A 98 13689 10947 9182 -1711 1047 -55 C
ATOM 559 CG LEU A 98 19.851 14.596 -30.506 1.00 87.25 C
ANISOU 559 CG LEU A 98 13146 10822 9183 -1841 1180 -269 C
ATOM 560 CD1 LEU A 98 19.560 16.024 -30.066 1.00 84.48 C
ANISOU 560 CD1 LEU A 98 12609 10677 8813 -1789 1187 -448 C
ATOM 561 CD2 LEU A 98 20.032 14.533 -32.018 1.00 83.15 C
ANISOU 561 CD2 LEU A 98 12427 10228 8936 -1779 1040 -321 C
ATOM 562 N GLY A 99 22.917 12.643 -27.116 1.00 82.44 N
ANISOU 562 N GLY A 99 13654 10059 7609 -1509 926 453 N
ATOM 563 CA GLY A 99 23.898 11.609 -26.851 1.00 80.91 C
ANISOU 563 CA GLY A 99 13750 9717 7274 -1350 803 719 C
ATOM 564 C GLY A 99 25.212 11.857 -27.572 1.00 75.62 C
ANISOU 564 C GLY A 99 12946 9058 6727 -1093 489 727 C
ATOM 565 O GLY A 99 25.264 12.480 -28.640 1.00 65.06 O
ANISOU 565 O GLY A 99 11318 7745 5657 -1072 407 557 O
ATOM 566 N SER A 100 26.303 11.383 -26.955 1.00 76.48 N
ANISOU 566 N SER A 100 13262 9171 6624 -886 312 936 N
ATOM 567 CA SER A 100 27.650 11.625 -27.473 1.00 80.16 C
ANISOU 567 CA SER A 100 13586 9699 7173 -630 10 951 C
ATOM 568 C SER A 100 27.854 11.017 -28.858 1.00 77.73 C
ANISOU 568 C SER A 100 13183 9173 7179 -561 -6 955 C
ATOM 569 O SER A 100 28.525 11.613 -29.710 1.00 75.22 O
ANISOU 569 O SER A 100 12603 8931 7046 -450 -176 841 O
ATOM 570 CB SER A 100 28.688 11.074 -26.496 1.00 87.37 C
ANISOU 570 CB SER A 100 14745 10669 7784 -411 -165 1197 C
ATOM 571 OG SER A 100 28.570 9.667 -26.373 1.00 94.75 O
ANISOU 571 OG SER A 100 16009 11330 8662 -364 -44 1456 O
ATOM 572 N LEU A 101 27.309 9.820 -29.089 1.00 79.91 N
ANISOU 572 N LEU A 101 13684 9173 7507 -635 180 1081 N
ATOM 573 CA LEU A 101 27.461 9.175 -30.391 1.00 78.56 C
ANISOU 573 CA LEU A 101 13454 8781 7613 -584 183 1062 C
ATOM 574 C LEU A 101 26.758 9.970 -31.486 1.00 78.88 C
ANISOU 574 C LEU A 101 13163 8893 7917 -745 232 794 C
ATOM 575 O LEU A 101 27.278 10.095 -32.599 1.00 81.76 O
ANISOU 575 O LEU A 101 13343 9237 8485 -636 117 716 O
ATOM 576 CB LEU A 101 26.929 7.744 -30.330 1.00 81.42 C
ANISOU 576 CB LEU A 101 14157 8810 7967 -673 398 1228 C
ATOM 577 CG LEU A 101 26.875 6.923 -31.621 1.00 84.40 C
ANISOU 577 CG LEU A 101 14536 8915 8616 -677 457 1183 C
ATOM 578 CD1 LEU A 101 28.234 6.894 -32.321 1.00 81.08 C
ANISOU 578 CD1 LEU A 101 14012 8500 8296 -350 215 1215 C
ATOM 579 CD2 LEU A 101 26.383 5.511 -31.334 1.00 87.64 C
ANISOU 579 CD2 LEU A 101 15344 8969 8987 -784 683 1359 C
ATOM 580 N ALA A 102 25.583 10.531 -31.181 1.00 78.25 N
ANISOU 580 N ALA A 102 12996 8912 7824 -986 403 658 N
ATOM 581 CA ALA A 102 24.880 11.367 -32.153 1.00 72.86 C
ANISOU 581 CA ALA A 102 11986 8325 7372 -1107 435 418 C
ATOM 582 C ALA A 102 25.657 12.644 -32.442 1.00 68.60 C
ANISOU 582 C ALA A 102 11186 7993 6887 -955 217 305 C
ATOM 583 O ALA A 102 25.722 13.093 -33.596 1.00 62.07 O
ANISOU 583 O ALA A 102 10124 7183 6275 -926 150 185 O
ATOM 584 CB ALA A 102 23.474 11.697 -31.653 1.00 73.81 C
ANISOU 584 CB ALA A 102 12058 8529 7458 -1366 668 305 C
ATOM 585 N CYS A 103 26.250 13.236 -31.403 1.00 63.77 N
ANISOU 585 N CYS A 103 10621 7539 6070 -870 110 341 N
ATOM 586 CA CYS A 103 27.089 14.416 -31.581 1.00 62.41 C
ANISOU 586 CA CYS A 103 10226 7547 5940 -751 -95 235 C
ATOM 587 C CYS A 103 28.277 14.113 -32.483 1.00 62.98 C
ANISOU 587 C CYS A 103 10219 7568 6142 -553 -284 301 C
ATOM 588 O CYS A 103 28.588 14.882 -33.399 1.00 55.95 O
ANISOU 588 O CYS A 103 9084 6739 5436 -518 -372 182 O
ATOM 589 CB CYS A 103 27.566 14.918 -30.220 1.00 66.82 C
ANISOU 589 CB CYS A 103 10887 8280 6220 -713 -182 261 C
ATOM 590 SG CYS A 103 29.001 15.997 -30.310 1.00 68.38 S
ANISOU 590 SG CYS A 103 10876 8672 6432 -554 -479 184 S
ATOM 591 N ASP A 104 28.940 12.981 -32.241 1.00 66.92 N
ANISOU 591 N ASP A 104 10931 7949 6546 -412 -333 499 N
ATOM 592 CA ASP A 104 30.106 12.615 -33.036 1.00 69.92 C
ANISOU 592 CA ASP A 104 11236 8290 7042 -194 -496 565 C
ATOM 593 C ASP A 104 29.718 12.290 -34.474 1.00 71.05 C
ANISOU 593 C ASP A 104 11274 8280 7443 -236 -408 480 C
ATOM 594 O ASP A 104 30.440 12.653 -35.408 1.00 69.01 O
ANISOU 594 O ASP A 104 10814 8075 7333 -125 -522 421 O
ATOM 595 CB ASP A 104 30.828 11.440 -32.381 1.00 70.43 C
ANISOU 595 CB ASP A 104 11572 8249 6939 -2 -554 807 C
ATOM 596 CG ASP A 104 31.436 11.810 -31.043 1.00 72.20 C
ANISOU 596 CG ASP A 104 11868 8683 6883 81 -702 895 C
ATOM 597 OD1 ASP A 104 31.398 13.006 -30.687 1.00 71.16 O
ANISOU 597 OD1 ASP A 104 11562 8771 6704 -15 -766 740 O
ATOM 598 OD2 ASP A 104 31.941 10.908 -30.343 1.00 77.68 O
ANISOU 598 OD2 ASP A 104 12803 9318 7394 246 -755 1116 O
ATOM 599 N LEU A 105 28.572 11.631 -34.673 1.00 74.46 N
ANISOU 599 N LEU A 105 11831 8542 7920 -413 -203 462 N
ATOM 600 CA LEU A 105 28.104 11.332 -36.025 1.00 70.91 C
ANISOU 600 CA LEU A 105 11279 7975 7689 -483 -126 354 C
ATOM 601 C LEU A 105 27.749 12.604 -36.785 1.00 70.26 C
ANISOU 601 C LEU A 105 10879 8071 7746 -556 -163 164 C
ATOM 602 O LEU A 105 28.067 12.729 -37.976 1.00 67.06 O
ANISOU 602 O LEU A 105 10320 7665 7494 -494 -219 95 O
ATOM 603 CB LEU A 105 26.909 10.382 -35.968 1.00 72.14 C
ANISOU 603 CB LEU A 105 11623 7934 7850 -698 100 356 C
ATOM 604 CG LEU A 105 27.262 8.930 -35.636 1.00 77.09 C
ANISOU 604 CG LEU A 105 12595 8288 8407 -619 164 545 C
ATOM 605 CD1 LEU A 105 26.007 8.082 -35.500 1.00 75.12 C
ANISOU 605 CD1 LEU A 105 12534 7843 8165 -893 414 535 C
ATOM 606 CD2 LEU A 105 28.197 8.360 -36.698 1.00 74.27 C
ANISOU 606 CD2 LEU A 105 12229 7803 8186 -412 70 557 C
ATOM 607 N TRP A 106 27.080 13.553 -36.121 1.00 71.38 N
ANISOU 607 N TRP A 106 10933 8358 7828 -677 -121 81 N
ATOM 608 CA TRP A 106 26.752 14.820 -36.766 1.00 63.53 C
ANISOU 608 CA TRP A 106 9663 7509 6966 -716 -153 -80 C
ATOM 609 C TRP A 106 28.011 15.598 -37.123 1.00 60.27 C
ANISOU 609 C TRP A 106 9104 7198 6598 -549 -344 -81 C
ATOM 610 O TRP A 106 28.118 16.145 -38.226 1.00 58.69 O
ANISOU 610 O TRP A 106 8715 7032 6552 -523 -386 -156 O
ATOM 611 CB TRP A 106 25.845 15.662 -35.871 1.00 60.43 C
ANISOU 611 CB TRP A 106 9231 7232 6497 -847 -57 -170 C
ATOM 612 CG TRP A 106 25.810 17.094 -36.309 1.00 62.72 C
ANISOU 612 CG TRP A 106 9277 7652 6901 -824 -120 -306 C
ATOM 613 CD1 TRP A 106 25.428 17.575 -37.533 1.00 61.29 C
ANISOU 613 CD1 TRP A 106 8893 7487 6906 -824 -125 -393 C
ATOM 614 CD2 TRP A 106 26.200 18.231 -35.537 1.00 65.89 C
ANISOU 614 CD2 TRP A 106 9635 8171 7230 -795 -186 -365 C
ATOM 615 NE1 TRP A 106 25.547 18.942 -37.561 1.00 59.59 N
ANISOU 615 NE1 TRP A 106 8526 7367 6749 -785 -179 -480 N
ATOM 616 CE2 TRP A 106 26.017 19.369 -36.347 1.00 62.42 C
ANISOU 616 CE2 TRP A 106 8978 7777 6960 -778 -212 -480 C
ATOM 617 CE3 TRP A 106 26.678 18.399 -34.235 1.00 73.08 C
ANISOU 617 CE3 TRP A 106 10682 9152 7935 -785 -228 -337 C
ATOM 618 CZ2 TRP A 106 26.297 20.651 -35.899 1.00 66.03 C
ANISOU 618 CZ2 TRP A 106 9366 8309 7414 -763 -259 -575 C
ATOM 619 CZ3 TRP A 106 26.955 19.672 -33.793 1.00 75.28 C
ANISOU 619 CZ3 TRP A 106 10872 9536 8194 -783 -288 -455 C
ATOM 620 CH2 TRP A 106 26.766 20.781 -34.621 1.00 73.02 C
ANISOU 620 CH2 TRP A 106 10384 9256 8106 -777 -295 -576 C
ATOM 621 N LEU A 107 28.968 15.678 -36.189 1.00 55.55 N
ANISOU 621 N LEU A 107 8585 6669 5855 -447 -461 3 N
ATOM 622 CA LEU A 107 30.227 16.370 -36.458 1.00 57.61 C
ANISOU 622 CA LEU A 107 8687 7047 6157 -314 -642 -4 C
ATOM 623 C LEU A 107 30.993 15.705 -37.597 1.00 58.80 C
ANISOU 623 C LEU A 107 8783 7125 6432 -174 -696 52 C
ATOM 624 O LEU A 107 31.588 16.390 -38.440 1.00 52.39 O
ANISOU 624 O LEU A 107 7770 6390 5744 -127 -769 -4 O
ATOM 625 CB LEU A 107 31.083 16.415 -35.192 1.00 62.00 C
ANISOU 625 CB LEU A 107 9334 7716 6509 -236 -772 73 C
ATOM 626 CG LEU A 107 30.604 17.347 -34.081 1.00 69.09 C
ANISOU 626 CG LEU A 107 10252 8731 7266 -362 -750 -23 C
ATOM 627 CD1 LEU A 107 31.565 17.321 -32.909 1.00 72.91 C
ANISOU 627 CD1 LEU A 107 10822 9358 7521 -277 -910 50 C
ATOM 628 CD2 LEU A 107 30.448 18.758 -34.610 1.00 70.61 C
ANISOU 628 CD2 LEU A 107 10224 8992 7613 -441 -755 -198 C
ATOM 629 N ALA A 108 30.985 14.369 -37.637 1.00 62.00 N
ANISOU 629 N ALA A 108 9381 7373 6805 -108 -642 161 N
ATOM 630 CA ALA A 108 31.677 13.641 -38.693 1.00 57.97 C
ANISOU 630 CA ALA A 108 8847 6773 6405 39 -667 198 C
ATOM 631 C ALA A 108 31.038 13.897 -40.050 1.00 56.16 C
ANISOU 631 C ALA A 108 8482 6515 6341 -56 -586 70 C
ATOM 632 O ALA A 108 31.739 14.198 -41.021 1.00 58.01 O
ANISOU 632 O ALA A 108 8555 6809 6676 37 -646 38 O
ATOM 633 CB ALA A 108 31.689 12.146 -38.374 1.00 57.36 C
ANISOU 633 CB ALA A 108 9052 6484 6260 123 -601 334 C
ATOM 634 N LEU A 109 29.707 13.773 -40.134 1.00 54.20 N
ANISOU 634 N LEU A 109 8287 6198 6110 -242 -450 -2 N
ATOM 635 CA LEU A 109 28.976 14.103 -41.358 1.00 53.89 C
ANISOU 635 CA LEU A 109 8099 6177 6199 -338 -395 -129 C
ATOM 636 C LEU A 109 29.280 15.527 -41.813 1.00 55.47 C
ANISOU 636 C LEU A 109 8056 6550 6469 -314 -481 -191 C
ATOM 637 O LEU A 109 29.587 15.769 -42.988 1.00 56.67 O
ANISOU 637 O LEU A 109 8080 6739 6711 -264 -509 -228 O
ATOM 638 CB LEU A 109 27.475 13.926 -41.122 1.00 60.13 C
ANISOU 638 CB LEU A 109 8935 6928 6983 -550 -253 -201 C
ATOM 639 CG LEU A 109 26.568 14.143 -42.328 1.00 67.45 C
ANISOU 639 CG LEU A 109 9705 7901 8021 -656 -208 -333 C
ATOM 640 CD1 LEU A 109 26.994 13.199 -43.442 1.00 71.60 C
ANISOU 640 CD1 LEU A 109 10290 8318 8596 -597 -210 -347 C
ATOM 641 CD2 LEU A 109 25.109 13.934 -41.961 1.00 70.06 C
ANISOU 641 CD2 LEU A 109 10048 8228 8344 -870 -70 -407 C
ATOM 642 N ASP A 110 29.220 16.473 -40.870 1.00 51.25 N
ANISOU 642 N ASP A 110 7479 6112 5883 -354 -513 -202 N
ATOM 643 CA ASP A 110 29.487 17.884 -41.124 1.00 58.12 C
ANISOU 643 CA ASP A 110 8159 7104 6822 -350 -576 -261 C
ATOM 644 C ASP A 110 30.862 18.084 -41.759 1.00 56.66 C
ANISOU 644 C ASP A 110 7867 6972 6688 -219 -686 -218 C
ATOM 645 O ASP A 110 30.987 18.608 -42.877 1.00 49.41 O
ANISOU 645 O ASP A 110 6812 6088 5872 -204 -688 -248 O
ATOM 646 CB ASP A 110 29.400 18.626 -39.789 1.00 70.04 C
ANISOU 646 CB ASP A 110 9700 8676 8236 -405 -592 -285 C
ATOM 647 CG ASP A 110 28.261 19.613 -39.734 1.00 81.65 C
ANISOU 647 CG ASP A 110 11090 10176 9758 -510 -506 -393 C
ATOM 648 OD1 ASP A 110 28.508 20.829 -39.639 1.00 86.20 O
ANISOU 648 OD1 ASP A 110 11567 10806 10380 -511 -545 -452 O
ATOM 649 OD2 ASP A 110 27.103 19.156 -39.761 1.00 88.70 O
ANISOU 649 OD2 ASP A 110 12018 11034 10651 -594 -390 -425 O
ATOM 650 N TYR A 111 31.909 17.639 -41.056 1.00 55.75 N
ANISOU 650 N TYR A 111 7809 6881 6493 -118 -774 -140 N
ATOM 651 CA TYR A 111 33.275 17.932 -41.473 1.00 51.51 C
ANISOU 651 CA TYR A 111 7127 6442 6004 -3 -880 -110 C
ATOM 652 C TYR A 111 33.664 17.140 -42.716 1.00 56.76 C
ANISOU 652 C TYR A 111 7767 7054 6745 107 -846 -83 C
ATOM 653 O TYR A 111 34.364 17.666 -43.587 1.00 60.36 O
ANISOU 653 O TYR A 111 8057 7594 7285 147 -868 -98 O
ATOM 654 CB TYR A 111 34.242 17.666 -40.317 1.00 52.74 C
ANISOU 654 CB TYR A 111 7323 6677 6040 89 -1002 -38 C
ATOM 655 CG TYR A 111 34.349 18.830 -39.349 1.00 59.74 C
ANISOU 655 CG TYR A 111 8148 7684 6866 -17 -1074 -104 C
ATOM 656 CD1 TYR A 111 33.254 19.224 -38.583 1.00 58.34 C
ANISOU 656 CD1 TYR A 111 8081 7468 6617 -151 -1001 -165 C
ATOM 657 CD2 TYR A 111 35.542 19.531 -39.197 1.00 61.05 C
ANISOU 657 CD2 TYR A 111 8142 8008 7048 5 -1204 -124 C
ATOM 658 CE1 TYR A 111 33.341 20.289 -37.702 1.00 59.68 C
ANISOU 658 CE1 TYR A 111 8217 7734 6726 -246 -1052 -252 C
ATOM 659 CE2 TYR A 111 35.642 20.597 -38.312 1.00 55.20 C
ANISOU 659 CE2 TYR A 111 7361 7364 6250 -117 -1268 -215 C
ATOM 660 CZ TYR A 111 34.534 20.973 -37.573 1.00 57.24 C
ANISOU 660 CZ TYR A 111 7757 7561 6430 -236 -1189 -283 C
ATOM 661 OH TYR A 111 34.619 22.029 -36.697 1.00 62.83 O
ANISOU 661 OH TYR A 111 8446 8350 7075 -355 -1238 -399 O
ATOM 662 N VAL A 112 33.196 15.891 -42.840 1.00 52.78 N
ANISOU 662 N VAL A 112 7438 6406 6211 143 -774 -54 N
ATOM 663 CA VAL A 112 33.479 15.100 -44.037 1.00 54.22 C
ANISOU 663 CA VAL A 112 7625 6520 6456 238 -723 -62 C
ATOM 664 C VAL A 112 32.825 15.723 -45.266 1.00 56.39 C
ANISOU 664 C VAL A 112 7784 6835 6807 137 -665 -156 C
ATOM 665 O VAL A 112 33.467 15.871 -46.310 1.00 58.74 O
ANISOU 665 O VAL A 112 7968 7196 7157 212 -664 -169 O
ATOM 666 CB VAL A 112 33.044 13.634 -43.840 1.00 57.87 C
ANISOU 666 CB VAL A 112 8336 6779 6875 269 -644 -28 C
ATOM 667 CG1 VAL A 112 33.089 12.886 -45.160 1.00 54.15 C
ANISOU 667 CG1 VAL A 112 7888 6218 6467 324 -568 -89 C
ATOM 668 CG2 VAL A 112 33.980 12.934 -42.867 1.00 58.57 C
ANISOU 668 CG2 VAL A 112 8537 6830 6887 449 -716 102 C
ATOM 669 N ALA A 113 31.544 16.112 -45.165 1.00 56.55 N
ANISOU 669 N ALA A 113 7822 6838 6825 -22 -613 -216 N
ATOM 670 CA ALA A 113 30.863 16.687 -46.325 1.00 52.92 C
ANISOU 670 CA ALA A 113 7250 6436 6420 -92 -578 -289 C
ATOM 671 C ALA A 113 31.460 18.033 -46.717 1.00 54.59 C
ANISOU 671 C ALA A 113 7282 6774 6685 -68 -629 -271 C
ATOM 672 O ALA A 113 31.616 18.327 -47.909 1.00 58.81 O
ANISOU 672 O ALA A 113 7728 7366 7251 -41 -616 -280 O
ATOM 673 CB ALA A 113 29.368 16.832 -46.045 1.00 47.74 C
ANISOU 673 CB ALA A 113 6619 5764 5757 -245 -520 -354 C
ATOM 674 N SER A 114 31.834 18.851 -45.734 1.00 57.04 N
ANISOU 674 N SER A 114 7552 7124 6998 -88 -682 -247 N
ATOM 675 CA SER A 114 32.381 20.159 -46.069 1.00 58.25 C
ANISOU 675 CA SER A 114 7555 7360 7217 -99 -713 -239 C
ATOM 676 C SER A 114 33.800 20.047 -46.618 1.00 61.63 C
ANISOU 676 C SER A 114 7886 7861 7671 -2 -746 -192 C
ATOM 677 O SER A 114 34.173 20.777 -47.550 1.00 71.53 O
ANISOU 677 O SER A 114 9025 9172 8981 -8 -723 -178 O
ATOM 678 CB SER A 114 32.329 21.058 -44.847 1.00 55.19 C
ANISOU 678 CB SER A 114 7166 6982 6823 -174 -751 -263 C
ATOM 679 OG SER A 114 31.007 21.174 -44.351 1.00 50.62 O
ANISOU 679 OG SER A 114 6660 6352 6222 -251 -697 -314 O
ATOM 680 N ASN A 115 34.609 19.142 -46.057 1.00 57.76 N
ANISOU 680 N ASN A 115 7435 7374 7138 97 -792 -158 N
ATOM 681 CA ASN A 115 35.920 18.870 -46.632 1.00 54.12 C
ANISOU 681 CA ASN A 115 6858 7000 6707 219 -810 -122 C
ATOM 682 C ASN A 115 35.794 18.285 -48.031 1.00 50.69 C
ANISOU 682 C ASN A 115 6435 6542 6284 280 -720 -138 C
ATOM 683 O ASN A 115 36.633 18.558 -48.895 1.00 48.42 O
ANISOU 683 O ASN A 115 6012 6351 6033 331 -690 -125 O
ATOM 684 CB ASN A 115 36.705 17.928 -45.726 1.00 50.78 C
ANISOU 684 CB ASN A 115 6481 6582 6230 356 -885 -73 C
ATOM 685 CG ASN A 115 38.177 17.922 -46.044 1.00 57.32 C
ANISOU 685 CG ASN A 115 7122 7556 7102 483 -927 -42 C
ATOM 686 OD1 ASN A 115 38.617 17.214 -46.948 1.00 68.78 O
ANISOU 686 OD1 ASN A 115 8552 9003 8578 614 -864 -36 O
ATOM 687 ND2 ASN A 115 38.950 18.716 -45.311 1.00 51.74 N
ANISOU 687 ND2 ASN A 115 6264 6990 6404 438 -1028 -38 N
ATOM 688 N ALA A 116 34.755 17.481 -48.266 1.00 52.46 N
ANISOU 688 N ALA A 116 6815 6650 6467 260 -667 -178 N
ATOM 689 CA ALA A 116 34.483 16.974 -49.604 1.00 59.00 C
ANISOU 689 CA ALA A 116 7668 7467 7282 286 -589 -226 C
ATOM 690 C ALA A 116 34.170 18.112 -50.560 1.00 64.40 C
ANISOU 690 C ALA A 116 8235 8252 7982 208 -567 -228 C
ATOM 691 O ALA A 116 34.602 18.093 -51.716 1.00 61.57 O
ANISOU 691 O ALA A 116 7823 7967 7606 259 -515 -233 O
ATOM 692 CB ALA A 116 33.325 15.978 -49.560 1.00 50.60 C
ANISOU 692 CB ALA A 116 6786 6264 6174 227 -545 -291 C
ATOM 693 N ARG A 117 33.392 19.095 -50.099 1.00 64.04 N
ANISOU 693 N ARG A 117 8166 8207 7958 97 -595 -221 N
ATOM 694 CA ARG A 117 33.126 20.284 -50.906 1.00 60.94 C
ANISOU 694 CA ARG A 117 7681 7886 7588 48 -578 -192 C
ATOM 695 C ARG A 117 34.417 21.020 -51.254 1.00 60.25 C
ANISOU 695 C ARG A 117 7466 7880 7547 75 -564 -127 C
ATOM 696 O ARG A 117 34.609 21.439 -52.404 1.00 56.00 O
ANISOU 696 O ARG A 117 6876 7411 6992 86 -510 -89 O
ATOM 697 CB ARG A 117 32.146 21.202 -50.170 1.00 50.96 C
ANISOU 697 CB ARG A 117 6421 6580 6360 -43 -604 -198 C
ATOM 698 CG ARG A 117 32.286 22.684 -50.492 1.00 59.52 C
ANISOU 698 CG ARG A 117 7420 7688 7506 -75 -595 -139 C
ATOM 699 CD ARG A 117 31.131 23.512 -49.920 1.00 67.00 C
ANISOU 699 CD ARG A 117 8387 8579 8492 -128 -601 -160 C
ATOM 700 NE ARG A 117 29.959 23.520 -50.793 1.00 69.79 N
ANISOU 700 NE ARG A 117 8736 8971 8810 -104 -591 -163 N
ATOM 701 CZ ARG A 117 29.835 24.293 -51.870 1.00 67.91 C
ANISOU 701 CZ ARG A 117 8457 8778 8569 -61 -578 -87 C
ATOM 702 NH1 ARG A 117 30.813 25.121 -52.215 1.00 68.82 N
ANISOU 702 NH1 ARG A 117 8545 8877 8727 -60 -547 0 N
ATOM 703 NH2 ARG A 117 28.737 24.238 -52.610 1.00 68.77 N
ANISOU 703 NH2 ARG A 117 8547 8957 8624 -26 -595 -93 N
ATOM 704 N VAL A 118 35.312 21.184 -50.271 1.00 57.41 N
ANISOU 704 N VAL A 118 7049 7530 7235 74 -611 -113 N
ATOM 705 CA VAL A 118 36.601 21.837 -50.520 1.00 57.77 C
ANISOU 705 CA VAL A 118 6939 7675 7337 70 -597 -69 C
ATOM 706 C VAL A 118 37.403 21.067 -51.568 1.00 57.49 C
ANISOU 706 C VAL A 118 6847 7726 7270 186 -529 -60 C
ATOM 707 O VAL A 118 37.960 21.654 -52.509 1.00 61.72 O
ANISOU 707 O VAL A 118 7284 8348 7820 166 -452 -17 O
ATOM 708 CB VAL A 118 37.390 21.999 -49.209 1.00 59.35 C
ANISOU 708 CB VAL A 118 7071 7905 7573 47 -687 -81 C
ATOM 709 CG1 VAL A 118 38.765 22.585 -49.492 1.00 55.75 C
ANISOU 709 CG1 VAL A 118 6415 7583 7185 22 -672 -55 C
ATOM 710 CG2 VAL A 118 36.633 22.895 -48.242 1.00 59.40 C
ANISOU 710 CG2 VAL A 118 7139 7832 7600 -79 -731 -112 C
ATOM 711 N MET A 119 37.472 19.739 -51.417 1.00 62.12 N
ANISOU 711 N MET A 119 7512 8279 7812 311 -538 -99 N
ATOM 712 CA MET A 119 38.225 18.915 -52.363 1.00 64.86 C
ANISOU 712 CA MET A 119 7823 8690 8132 448 -459 -114 C
ATOM 713 C MET A 119 37.609 18.962 -53.759 1.00 60.22 C
ANISOU 713 C MET A 119 7292 8121 7469 424 -367 -136 C
ATOM 714 O MET A 119 38.333 18.968 -54.761 1.00 56.75 O
ANISOU 714 O MET A 119 6770 7791 7002 479 -273 -128 O
ATOM 715 CB MET A 119 38.283 17.466 -51.888 1.00 71.66 C
ANISOU 715 CB MET A 119 8806 9454 8967 595 -478 -154 C
ATOM 716 CG MET A 119 38.964 17.167 -50.575 1.00 82.40 C
ANISOU 716 CG MET A 119 10132 10813 10362 675 -578 -116 C
ATOM 717 SD MET A 119 40.720 17.519 -50.596 1.00 92.60 S
ANISOU 717 SD MET A 119 11137 12323 11724 779 -592 -76 S
ATOM 718 CE MET A 119 41.173 16.902 -48.981 1.00 95.74 C
ANISOU 718 CE MET A 119 11556 12709 12113 900 -748 -33 C
ATOM 719 N ASN A 120 36.274 18.962 -53.840 1.00 55.31 N
ANISOU 719 N ASN A 120 6799 7418 6798 346 -391 -168 N
ATOM 720 CA ASN A 120 35.595 19.098 -55.126 1.00 54.80 C
ANISOU 720 CA ASN A 120 6777 7408 6639 319 -339 -186 C
ATOM 721 C ASN A 120 35.916 20.433 -55.784 1.00 59.89 C
ANISOU 721 C ASN A 120 7315 8155 7288 264 -298 -82 C
ATOM 722 O ASN A 120 36.144 20.487 -56.993 1.00 59.17 O
ANISOU 722 O ASN A 120 7211 8165 7104 293 -218 -65 O
ATOM 723 CB ASN A 120 34.086 18.929 -54.955 1.00 56.04 C
ANISOU 723 CB ASN A 120 7046 7491 6757 239 -394 -241 C
ATOM 724 CG ASN A 120 33.682 17.481 -54.789 1.00 72.90 C
ANISOU 724 CG ASN A 120 9319 9524 8855 266 -388 -355 C
ATOM 725 OD1 ASN A 120 33.535 16.753 -55.767 1.00 78.57 O
ANISOU 725 OD1 ASN A 120 10104 10267 9484 293 -338 -441 O
ATOM 726 ND2 ASN A 120 33.504 17.053 -53.547 1.00 81.89 N
ANISOU 726 ND2 ASN A 120 10522 10540 10053 249 -429 -361 N
ATOM 727 N LEU A 121 35.932 21.521 -55.007 1.00 55.22 N
ANISOU 727 N LEU A 121 6664 7524 6792 179 -342 -14 N
ATOM 728 CA LEU A 121 36.308 22.817 -55.570 1.00 57.16 C
ANISOU 728 CA LEU A 121 6835 7821 7064 113 -284 95 C
ATOM 729 C LEU A 121 37.743 22.795 -56.089 1.00 56.69 C
ANISOU 729 C LEU A 121 6645 7878 7017 138 -186 127 C
ATOM 730 O LEU A 121 38.040 23.363 -57.150 1.00 56.65 O
ANISOU 730 O LEU A 121 6613 7953 6957 116 -84 207 O
ATOM 731 CB LEU A 121 36.115 23.916 -54.529 1.00 50.46 C
ANISOU 731 CB LEU A 121 5967 6872 6333 8 -338 130 C
ATOM 732 CG LEU A 121 34.656 24.195 -54.186 1.00 56.50 C
ANISOU 732 CG LEU A 121 6835 7543 7090 -9 -402 113 C
ATOM 733 CD1 LEU A 121 34.580 25.216 -53.090 1.00 59.59 C
ANISOU 733 CD1 LEU A 121 7216 7828 7596 -98 -436 120 C
ATOM 734 CD2 LEU A 121 33.895 24.672 -55.413 1.00 54.85 C
ANISOU 734 CD2 LEU A 121 6670 7376 6795 19 -370 188 C
ATOM 735 N LEU A 122 38.642 22.132 -55.353 1.00 53.60 N
ANISOU 735 N LEU A 122 6166 7513 6688 193 -210 73 N
ATOM 736 CA LEU A 122 40.029 22.020 -55.793 1.00 62.41 C
ANISOU 736 CA LEU A 122 7114 8771 7827 237 -117 87 C
ATOM 737 C LEU A 122 40.134 21.242 -57.104 1.00 67.68 C
ANISOU 737 C LEU A 122 7823 9525 8367 351 0 57 C
ATOM 738 O LEU A 122 40.849 21.658 -58.029 1.00 68.36 O
ANISOU 738 O LEU A 122 7814 9740 8420 333 133 109 O
ATOM 739 CB LEU A 122 40.862 21.352 -54.699 1.00 62.28 C
ANISOU 739 CB LEU A 122 6992 8781 7892 319 -195 34 C
ATOM 740 CG LEU A 122 41.635 22.264 -53.743 1.00 62.23 C
ANISOU 740 CG LEU A 122 6816 8825 8005 198 -257 59 C
ATOM 741 CD1 LEU A 122 42.376 21.448 -52.693 1.00 67.07 C
ANISOU 741 CD1 LEU A 122 7331 9496 8655 319 -364 12 C
ATOM 742 CD2 LEU A 122 42.605 23.127 -54.515 1.00 62.35 C
ANISOU 742 CD2 LEU A 122 6647 8976 8066 96 -127 115 C
ATOM 743 N VAL A 123 39.418 20.116 -57.210 1.00 63.40 N
ANISOU 743 N VAL A 123 7432 8912 7745 450 -33 -36 N
ATOM 744 CA VAL A 123 39.520 19.314 -58.429 1.00 64.35 C
ANISOU 744 CA VAL A 123 7610 9107 7733 552 79 -102 C
ATOM 745 C VAL A 123 38.829 20.011 -59.604 1.00 63.27 C
ANISOU 745 C VAL A 123 7546 9040 7455 472 130 -47 C
ATOM 746 O VAL A 123 39.263 19.855 -60.749 1.00 66.09 O
ANISOU 746 O VAL A 123 7896 9527 7690 519 258 -55 O
ATOM 747 CB VAL A 123 39.022 17.865 -58.219 1.00 64.01 C
ANISOU 747 CB VAL A 123 7725 8944 7653 664 43 -238 C
ATOM 748 CG1 VAL A 123 39.800 17.183 -57.094 1.00 58.21 C
ANISOU 748 CG1 VAL A 123 6932 8143 7041 781 -3 -255 C
ATOM 749 CG2 VAL A 123 37.537 17.789 -57.971 1.00 68.05 C
ANISOU 749 CG2 VAL A 123 8399 9335 8120 568 -58 -275 C
ATOM 750 N ILE A 124 37.766 20.792 -59.354 1.00 58.73 N
ANISOU 750 N ILE A 124 7040 8394 6883 369 36 15 N
ATOM 751 CA ILE A 124 37.168 21.614 -60.412 1.00 61.23 C
ANISOU 751 CA ILE A 124 7411 8786 7068 318 68 109 C
ATOM 752 C ILE A 124 38.179 22.627 -60.929 1.00 64.66 C
ANISOU 752 C ILE A 124 7739 9310 7519 267 199 251 C
ATOM 753 O ILE A 124 38.332 22.816 -62.147 1.00 66.79 O
ANISOU 753 O ILE A 124 8039 9708 7629 280 308 309 O
ATOM 754 CB ILE A 124 35.893 22.321 -59.910 1.00 53.40 C
ANISOU 754 CB ILE A 124 6486 7694 6111 250 -59 158 C
ATOM 755 CG1 ILE A 124 34.779 21.324 -59.660 1.00 51.79 C
ANISOU 755 CG1 ILE A 124 6379 7441 5858 272 -161 17 C
ATOM 756 CG2 ILE A 124 35.417 23.387 -60.893 1.00 51.84 C
ANISOU 756 CG2 ILE A 124 6330 7565 5803 227 -34 305 C
ATOM 757 CD1 ILE A 124 33.562 21.912 -58.968 1.00 56.37 C
ANISOU 757 CD1 ILE A 124 6984 7936 6499 215 -277 42 C
ATOM 758 N SER A 125 38.873 23.301 -60.005 1.00 59.87 N
ANISOU 758 N SER A 125 7011 8644 7093 189 194 303 N
ATOM 759 CA SER A 125 39.892 24.276 -60.385 1.00 60.92 C
ANISOU 759 CA SER A 125 7026 8848 7272 94 331 425 C
ATOM 760 C SER A 125 40.977 23.637 -61.246 1.00 63.47 C
ANISOU 760 C SER A 125 7247 9355 7515 167 492 389 C
ATOM 761 O SER A 125 41.321 24.155 -62.317 1.00 63.49 O
ANISOU 761 O SER A 125 7250 9466 7408 127 644 491 O
ATOM 762 CB SER A 125 40.494 24.902 -59.129 1.00 55.76 C
ANISOU 762 CB SER A 125 6243 8114 6831 -16 279 430 C
ATOM 763 OG SER A 125 39.474 25.467 -58.324 1.00 60.14 O
ANISOU 763 OG SER A 125 6903 8498 7450 -71 149 442 O
ATOM 764 N PHE A 126 41.514 22.497 -60.796 1.00 66.32 N
ANISOU 764 N PHE A 126 7529 9750 7920 288 471 251 N
ATOM 765 CA PHE A 126 42.578 21.832 -61.547 1.00 65.07 C
ANISOU 765 CA PHE A 126 7256 9764 7703 392 635 196 C
ATOM 766 C PHE A 126 42.078 21.294 -62.884 1.00 67.39 C
ANISOU 766 C PHE A 126 7711 10136 7759 472 727 155 C
ATOM 767 O PHE A 126 42.814 21.322 -63.876 1.00 71.49 O
ANISOU 767 O PHE A 126 8167 10823 8172 493 914 175 O
ATOM 768 CB PHE A 126 43.196 20.707 -60.720 1.00 61.93 C
ANISOU 768 CB PHE A 126 6759 9359 7413 548 580 66 C
ATOM 769 CG PHE A 126 44.253 21.171 -59.766 1.00 60.85 C
ANISOU 769 CG PHE A 126 6372 9280 7466 495 552 98 C
ATOM 770 CD1 PHE A 126 45.548 21.389 -60.204 1.00 65.08 C
ANISOU 770 CD1 PHE A 126 6663 10019 8045 490 712 117 C
ATOM 771 CD2 PHE A 126 43.958 21.372 -58.427 1.00 59.42 C
ANISOU 771 CD2 PHE A 126 6190 8977 7411 442 368 96 C
ATOM 772 CE1 PHE A 126 46.531 21.816 -59.329 1.00 68.13 C
ANISOU 772 CE1 PHE A 126 6786 10495 8604 422 671 128 C
ATOM 773 CE2 PHE A 126 44.931 21.795 -57.544 1.00 64.32 C
ANISOU 773 CE2 PHE A 126 6575 9681 8183 382 321 106 C
ATOM 774 CZ PHE A 126 46.222 22.018 -57.996 1.00 69.38 C
ANISOU 774 CZ PHE A 126 6952 10536 8875 367 464 119 C
ATOM 775 N ASP A 127 40.834 20.801 -62.929 1.00 63.07 N
ANISOU 775 N ASP A 127 7362 9488 7115 504 602 87 N
ATOM 776 CA ASP A 127 40.258 20.295 -64.171 1.00 62.92 C
ANISOU 776 CA ASP A 127 7500 9560 6849 557 657 23 C
ATOM 777 C ASP A 127 40.142 21.399 -65.212 1.00 66.40 C
ANISOU 777 C ASP A 127 7976 10124 7131 469 747 195 C
ATOM 778 O ASP A 127 40.559 21.223 -66.364 1.00 64.16 O
ANISOU 778 O ASP A 127 7716 10010 6653 508 905 187 O
ATOM 779 CB ASP A 127 38.889 19.672 -63.889 1.00 64.24 C
ANISOU 779 CB ASP A 127 7838 9603 6967 564 484 -84 C
ATOM 780 CG ASP A 127 38.218 19.137 -65.141 1.00 71.11 C
ANISOU 780 CG ASP A 127 8864 10586 7571 594 511 -180 C
ATOM 781 OD1 ASP A 127 38.817 18.278 -65.822 1.00 75.75 O
ANISOU 781 OD1 ASP A 127 9474 11255 8052 688 642 -311 O
ATOM 782 OD2 ASP A 127 37.086 19.574 -65.441 1.00 70.59 O
ANISOU 782 OD2 ASP A 127 8889 10537 7394 530 396 -135 O
ATOM 783 N ARG A 128 39.585 22.550 -64.816 1.00 64.86 N
ANISOU 783 N ARG A 128 7799 9836 7008 358 658 356 N
ATOM 784 CA ARG A 128 39.489 23.692 -65.725 1.00 66.73 C
ANISOU 784 CA ARG A 128 8093 10148 7112 285 745 560 C
ATOM 785 C ARG A 128 40.871 24.158 -66.173 1.00 65.51 C
ANISOU 785 C ARG A 128 7803 10110 6978 225 976 653 C
ATOM 786 O ARG A 128 41.090 24.423 -67.366 1.00 64.83 O
ANISOU 786 O ARG A 128 7777 10177 6678 221 1131 747 O
ATOM 787 CB ARG A 128 38.728 24.841 -65.060 1.00 70.10 C
ANISOU 787 CB ARG A 128 8565 10406 7665 198 621 709 C
ATOM 788 CG ARG A 128 37.217 24.885 -65.317 1.00 77.27 C
ANISOU 788 CG ARG A 128 9626 11291 8440 251 453 721 C
ATOM 789 CD ARG A 128 36.490 23.665 -64.762 1.00 84.83 C
ANISOU 789 CD ARG A 128 10602 12215 9413 312 304 497 C
ATOM 790 NE ARG A 128 35.045 23.863 -64.684 1.00 91.44 N
ANISOU 790 NE ARG A 128 11524 13019 10200 328 130 506 N
ATOM 791 CZ ARG A 128 34.189 22.944 -64.247 1.00 93.56 C
ANISOU 791 CZ ARG A 128 11816 13257 10474 346 -1 328 C
ATOM 792 NH1 ARG A 128 32.890 23.212 -64.203 1.00 91.59 N
ANISOU 792 NH1 ARG A 128 11603 13013 10186 352 -149 341 N
ATOM 793 NH2 ARG A 128 34.632 21.754 -63.861 1.00 91.84 N
ANISOU 793 NH2 ARG A 128 11584 13005 10306 361 24 142 N
ATOM 794 N TYR A 129 41.818 24.251 -65.229 1.00 63.79 N
ANISOU 794 N TYR A 129 7391 9843 7003 171 1004 624 N
ATOM 795 CA TYR A 129 43.161 24.734 -65.546 1.00 67.23 C
ANISOU 795 CA TYR A 129 7646 10406 7493 83 1222 699 C
ATOM 796 C TYR A 129 43.866 23.817 -66.542 1.00 73.30 C
ANISOU 796 C TYR A 129 8365 11396 8089 204 1406 598 C
ATOM 797 O TYR A 129 44.455 24.284 -67.525 1.00 76.27 O
ANISOU 797 O TYR A 129 8719 11926 8334 145 1624 705 O
ATOM 798 CB TYR A 129 43.980 24.866 -64.262 1.00 61.26 C
ANISOU 798 CB TYR A 129 6662 9591 7024 13 1172 647 C
ATOM 799 CG TYR A 129 45.425 25.225 -64.505 1.00 66.91 C
ANISOU 799 CG TYR A 129 7128 10475 7819 -84 1387 685 C
ATOM 800 CD1 TYR A 129 45.788 26.524 -64.825 1.00 72.66 C
ANISOU 800 CD1 TYR A 129 7835 11190 8583 -303 1529 867 C
ATOM 801 CD2 TYR A 129 46.431 24.267 -64.396 1.00 62.43 C
ANISOU 801 CD2 TYR A 129 6341 10076 7304 43 1457 539 C
ATOM 802 CE1 TYR A 129 47.104 26.860 -65.049 1.00 73.23 C
ANISOU 802 CE1 TYR A 129 7659 11431 8736 -428 1741 894 C
ATOM 803 CE2 TYR A 129 47.755 24.596 -64.614 1.00 61.61 C
ANISOU 803 CE2 TYR A 129 5964 10164 7282 -47 1658 563 C
ATOM 804 CZ TYR A 129 48.085 25.897 -64.940 1.00 71.04 C
ANISOU 804 CZ TYR A 129 7125 11359 8507 -301 1802 736 C
ATOM 805 OH TYR A 129 49.396 26.245 -65.162 1.00 79.73 O
ANISOU 805 OH TYR A 129 7935 12661 9697 -429 2019 755 O
ATOM 806 N PHE A 130 43.811 22.506 -66.306 1.00 70.26 N
ANISOU 806 N PHE A 130 7979 11017 7700 377 1339 390 N
ATOM 807 CA PHE A 130 44.503 21.572 -67.183 1.00 72.34 C
ANISOU 807 CA PHE A 130 8202 11465 7818 518 1524 260 C
ATOM 808 C PHE A 130 43.788 21.437 -68.522 1.00 70.76 C
ANISOU 808 C PHE A 130 8233 11367 7285 546 1587 263 C
ATOM 809 O PHE A 130 44.437 21.156 -69.538 1.00 69.91 O
ANISOU 809 O PHE A 130 8106 11456 7000 599 1808 226 O
ATOM 810 CB PHE A 130 44.645 20.215 -66.494 1.00 69.11 C
ANISOU 810 CB PHE A 130 7756 10985 7518 707 1437 42 C
ATOM 811 CG PHE A 130 45.663 20.199 -65.388 1.00 66.10 C
ANISOU 811 CG PHE A 130 7105 10597 7411 728 1416 32 C
ATOM 812 CD1 PHE A 130 46.856 20.897 -65.514 1.00 64.48 C
ANISOU 812 CD1 PHE A 130 6638 10565 7295 639 1587 120 C
ATOM 813 CD2 PHE A 130 45.419 19.496 -64.215 1.00 60.65 C
ANISOU 813 CD2 PHE A 130 6420 9745 6881 827 1223 -62 C
ATOM 814 CE1 PHE A 130 47.795 20.887 -64.494 1.00 65.10 C
ANISOU 814 CE1 PHE A 130 6438 10681 7617 653 1543 97 C
ATOM 815 CE2 PHE A 130 46.349 19.482 -63.187 1.00 55.82 C
ANISOU 815 CE2 PHE A 130 5558 9158 6492 862 1177 -64 C
ATOM 816 CZ PHE A 130 47.538 20.179 -63.326 1.00 63.63 C
ANISOU 816 CZ PHE A 130 6261 10346 7568 777 1326 7 C
ATOM 817 N SER A 131 42.460 21.618 -68.543 1.00 65.45 N
ANISOU 817 N SER A 131 7768 10589 6513 517 1396 296 N
ATOM 818 CA SER A 131 41.740 21.713 -69.810 1.00 67.26 C
ANISOU 818 CA SER A 131 8201 10950 6407 524 1424 335 C
ATOM 819 C SER A 131 42.234 22.891 -70.638 1.00 75.48 C
ANISOU 819 C SER A 131 9237 12121 7321 416 1613 584 C
ATOM 820 O SER A 131 42.358 22.789 -71.865 1.00 74.26 O
ANISOU 820 O SER A 131 9179 12168 6867 447 1766 599 O
ATOM 821 CB SER A 131 40.242 21.839 -69.553 1.00 61.99 C
ANISOU 821 CB SER A 131 7697 10163 5694 507 1165 348 C
ATOM 822 OG SER A 131 39.789 20.767 -68.753 1.00 67.70 O
ANISOU 822 OG SER A 131 8432 10751 6541 574 1015 129 O
ATOM 823 N ILE A 132 42.507 24.024 -69.986 1.00 77.32 N
ANISOU 823 N ILE A 132 9378 12233 7768 279 1612 779 N
ATOM 824 CA ILE A 132 42.998 25.183 -70.728 1.00 79.43 C
ANISOU 824 CA ILE A 132 9662 12580 7939 151 1813 1033 C
ATOM 825 C ILE A 132 44.433 24.959 -71.201 1.00 81.86 C
ANISOU 825 C ILE A 132 9781 13085 8239 127 2110 995 C
ATOM 826 O ILE A 132 44.765 25.230 -72.362 1.00 93.29 O
ANISOU 826 O ILE A 132 11299 14716 9430 101 2329 1103 O
ATOM 827 CB ILE A 132 42.874 26.462 -69.878 1.00 77.87 C
ANISOU 827 CB ILE A 132 9440 12158 7989 -7 1742 1231 C
ATOM 828 CG1 ILE A 132 41.410 26.752 -69.558 1.00 75.77 C
ANISOU 828 CG1 ILE A 132 9362 11727 7701 43 1479 1283 C
ATOM 829 CG2 ILE A 132 43.475 27.649 -70.600 1.00 79.81 C
ANISOU 829 CG2 ILE A 132 9715 12444 8164 -163 1981 1497 C
ATOM 830 CD1 ILE A 132 40.534 26.832 -70.772 1.00 78.44 C
ANISOU 830 CD1 ILE A 132 9925 12195 7684 129 1454 1387 C
ATOM 831 N THR A 133 45.299 24.436 -70.330 1.00 79.16 N
ANISOU 831 N THR A 133 9188 12729 8160 148 2126 842 N
ATOM 832 CA THR A 133 46.734 24.452 -70.597 1.00 87.13 C
ANISOU 832 CA THR A 133 9946 13928 9231 101 2404 832 C
ATOM 833 C THR A 133 47.286 23.171 -71.215 1.00 88.53 C
ANISOU 833 C THR A 133 10060 14309 9268 303 2549 606 C
ATOM 834 O THR A 133 48.426 23.184 -71.691 1.00 88.15 O
ANISOU 834 O THR A 133 9814 14468 9211 283 2821 603 O
ATOM 835 CB THR A 133 47.513 24.746 -69.307 1.00 88.36 C
ANISOU 835 CB THR A 133 9815 13999 9760 5 2350 809 C
ATOM 836 OG1 THR A 133 47.384 23.648 -68.394 1.00 86.38 O
ANISOU 836 OG1 THR A 133 9494 13674 9651 186 2153 591 O
ATOM 837 CG2 THR A 133 47.013 26.030 -68.657 1.00 86.62 C
ANISOU 837 CG2 THR A 133 9668 13555 9690 -204 2227 1001 C
ATOM 838 N ARG A 134 46.532 22.070 -71.226 1.00 87.84 N
ANISOU 838 N ARG A 134 10131 14166 9080 488 2394 409 N
ATOM 839 CA ARG A 134 47.032 20.793 -71.744 1.00 85.94 C
ANISOU 839 CA ARG A 134 9859 14067 8729 694 2532 166 C
ATOM 840 C ARG A 134 45.969 20.120 -72.600 1.00 82.68 C
ANISOU 840 C ARG A 134 9758 13665 7993 786 2459 45 C
ATOM 841 O ARG A 134 45.177 19.303 -72.110 1.00 82.00 O
ANISOU 841 O ARG A 134 9794 13414 7948 879 2247 -119 O
ATOM 842 CB ARG A 134 47.480 19.865 -70.612 1.00 85.11 C
ANISOU 842 CB ARG A 134 9573 13849 8915 850 2424 -20 C
ATOM 843 CG ARG A 134 48.605 20.422 -69.750 1.00 87.59 C
ANISOU 843 CG ARG A 134 9539 14206 9535 773 2475 63 C
ATOM 844 CD ARG A 134 48.980 19.496 -68.614 1.00 88.59 C
ANISOU 844 CD ARG A 134 9507 14236 9917 957 2334 -97 C
ATOM 845 NE ARG A 134 49.894 20.153 -67.685 1.00 89.68 N
ANISOU 845 NE ARG A 134 9315 14425 10335 851 2316 -10 N
ATOM 846 CZ ARG A 134 50.543 19.528 -66.708 1.00 92.34 C
ANISOU 846 CZ ARG A 134 9428 14760 10897 1005 2224 -111 C
ATOM 847 NH1 ARG A 134 50.382 18.224 -66.534 1.00 94.73 N
ANISOU 847 NH1 ARG A 134 9824 14974 11193 1283 2160 -285 N
ATOM 848 NH2 ARG A 134 51.350 20.209 -65.906 1.00 91.92 N
ANISOU 848 NH2 ARG A 134 9064 14790 11071 878 2192 -37 N
ATOM 849 N PRO A 135 45.929 20.436 -73.898 1.00 80.40 N
ANISOU 849 N PRO A 135 9605 13581 7363 748 2637 119 N
ATOM 850 CA PRO A 135 44.862 19.915 -74.764 1.00 79.48 C
ANISOU 850 CA PRO A 135 9783 13514 6900 806 2542 10 C
ATOM 851 C PRO A 135 45.035 18.449 -75.134 1.00 82.13 C
ANISOU 851 C PRO A 135 10177 13899 7132 995 2620 -330 C
ATOM 852 O PRO A 135 44.047 17.722 -75.267 1.00 86.68 O
ANISOU 852 O PRO A 135 10960 14399 7574 1042 2444 -506 O
ATOM 853 CB PRO A 135 44.952 20.818 -75.999 1.00 82.56 C
ANISOU 853 CB PRO A 135 10282 14134 6952 705 2732 229 C
ATOM 854 CG PRO A 135 46.390 21.214 -76.059 1.00 88.93 C
ANISOU 854 CG PRO A 135 10834 15068 7886 656 3045 314 C
ATOM 855 CD PRO A 135 46.868 21.299 -74.631 1.00 86.23 C
ANISOU 855 CD PRO A 135 10231 14528 8003 633 2936 308 C
ATOM 856 N LEU A 136 46.279 18.004 -75.312 1.00 87.62 N
ANISOU 856 N LEU A 136 10686 14716 7890 1102 2890 -434 N
ATOM 857 CA LEU A 136 46.543 16.632 -75.728 1.00 94.92 C
ANISOU 857 CA LEU A 136 11675 15672 8717 1308 3009 -761 C
ATOM 858 C LEU A 136 46.653 15.683 -74.542 1.00 99.81 C
ANISOU 858 C LEU A 136 12207 16034 9683 1460 2868 -936 C
ATOM 859 O LEU A 136 46.070 14.594 -74.556 1.00100.78 O
ANISOU 859 O LEU A 136 12525 16015 9753 1571 2779 -1183 O
ATOM 860 CB LEU A 136 47.826 16.574 -76.561 1.00 92.39 C
ANISOU 860 CB LEU A 136 11197 15626 8282 1385 3394 -798 C
ATOM 861 CG LEU A 136 47.757 17.239 -77.932 1.00 96.26 C
ANISOU 861 CG LEU A 136 11831 16396 8346 1270 3588 -672 C
ATOM 862 CD1 LEU A 136 49.109 17.163 -78.630 1.00101.59 C
ANISOU 862 CD1 LEU A 136 12311 17343 8946 1341 3999 -713 C
ATOM 863 CD2 LEU A 136 46.675 16.586 -78.773 1.00 98.06 C
ANISOU 863 CD2 LEU A 136 12409 16654 8196 1305 3478 -862 C
ATOM 864 N THR A 137 47.384 16.088 -73.505 1.00103.14 N
ANISOU 864 N THR A 137 12348 16391 10450 1457 2845 -809 N
ATOM 865 CA THR A 137 47.630 15.192 -72.384 1.00106.95 C
ANISOU 865 CA THR A 137 12735 16660 11241 1632 2728 -948 C
ATOM 866 C THR A 137 46.459 15.149 -71.410 1.00105.40 C
ANISOU 866 C THR A 137 12694 16180 11173 1553 2389 -920 C
ATOM 867 O THR A 137 46.269 14.134 -70.731 1.00116.96 O
ANISOU 867 O THR A 137 14227 17430 12782 1699 2282 -1082 O
ATOM 868 CB THR A 137 48.915 15.595 -71.658 1.00109.84 C
ANISOU 868 CB THR A 137 12716 17116 11903 1670 2823 -838 C
ATOM 869 OG1 THR A 137 48.803 16.944 -71.193 1.00112.29 O
ANISOU 869 OG1 THR A 137 12914 17436 12313 1419 2719 -571 O
ATOM 870 CG2 THR A 137 50.106 15.491 -72.596 1.00112.23 C
ANISOU 870 CG2 THR A 137 12832 17713 12098 1770 3182 -898 C
ATOM 871 N TYR A 138 45.667 16.219 -71.317 1.00 95.23 N
ANISOU 871 N TYR A 138 11469 14876 9836 1334 2233 -715 N
ATOM 872 CA TYR A 138 44.552 16.242 -70.375 1.00 81.11 C
ANISOU 872 CA TYR A 138 9802 12844 8174 1258 1931 -688 C
ATOM 873 C TYR A 138 43.199 16.403 -71.058 1.00 75.82 C
ANISOU 873 C TYR A 138 9397 12177 7234 1143 1798 -694 C
ATOM 874 O TYR A 138 42.327 15.549 -70.861 1.00 74.29 O
ANISOU 874 O TYR A 138 9379 11831 7017 1173 1652 -870 O
ATOM 875 CB TYR A 138 44.754 17.346 -69.327 1.00 76.71 C
ANISOU 875 CB TYR A 138 9051 12222 7872 1124 1815 -455 C
ATOM 876 CG TYR A 138 43.741 17.296 -68.196 1.00 76.37 C
ANISOU 876 CG TYR A 138 9101 11928 7988 1071 1529 -446 C
ATOM 877 CD1 TYR A 138 43.974 16.521 -67.067 1.00 70.89 C
ANISOU 877 CD1 TYR A 138 8344 11061 7529 1189 1430 -541 C
ATOM 878 CD2 TYR A 138 42.557 18.030 -68.253 1.00 75.37 C
ANISOU 878 CD2 TYR A 138 9121 11747 7768 918 1365 -332 C
ATOM 879 CE1 TYR A 138 43.057 16.468 -66.031 1.00 71.57 C
ANISOU 879 CE1 TYR A 138 8523 10930 7741 1131 1193 -528 C
ATOM 880 CE2 TYR A 138 41.639 17.986 -67.223 1.00 72.46 C
ANISOU 880 CE2 TYR A 138 8818 11171 7544 870 1130 -334 C
ATOM 881 CZ TYR A 138 41.893 17.204 -66.114 1.00 70.78 C
ANISOU 881 CZ TYR A 138 8551 10790 7551 964 1053 -433 C
ATOM 882 OH TYR A 138 40.977 17.153 -65.087 1.00 65.42 O
ANISOU 882 OH TYR A 138 7946 9914 6995 907 841 -431 O
ATOM 883 N ARG A 139 42.986 17.477 -71.833 1.00 76.70 N
ANISOU 883 N ARG A 139 9540 12459 7143 1012 1841 -500 N
ATOM 884 CA ARG A 139 41.635 17.832 -72.275 1.00 76.91 C
ANISOU 884 CA ARG A 139 9774 12496 6951 911 1656 -450 C
ATOM 885 C ARG A 139 41.034 16.777 -73.198 1.00 79.98 C
ANISOU 885 C ARG A 139 10377 12965 7045 972 1657 -712 C
ATOM 886 O ARG A 139 39.840 16.470 -73.102 1.00 80.91 O
ANISOU 886 O ARG A 139 10640 13008 7096 921 1440 -803 O
ATOM 887 CB ARG A 139 41.628 19.196 -72.969 1.00 80.15 C
ANISOU 887 CB ARG A 139 10189 13071 7193 794 1721 -162 C
ATOM 888 CG ARG A 139 40.210 19.715 -73.205 1.00 81.26 C
ANISOU 888 CG ARG A 139 10502 13207 7165 720 1486 -62 C
ATOM 889 CD ARG A 139 40.149 21.138 -73.742 1.00 82.69 C
ANISOU 889 CD ARG A 139 10712 13490 7217 630 1529 267 C
ATOM 890 NE ARG A 139 40.530 21.227 -75.148 1.00 81.45 N
ANISOU 890 NE ARG A 139 10656 13606 6686 647 1736 311 N
ATOM 891 CZ ARG A 139 41.574 21.915 -75.598 1.00 79.17 C
ANISOU 891 CZ ARG A 139 10291 13427 6363 598 2000 492 C
ATOM 892 NH1 ARG A 139 42.344 22.583 -74.748 1.00 72.24 N
ANISOU 892 NH1 ARG A 139 9222 12409 5816 517 2077 633 N
ATOM 893 NH2 ARG A 139 41.844 21.940 -76.898 1.00 86.09 N
ANISOU 893 NH2 ARG A 139 11283 14566 6862 614 2194 525 N
ATOM 894 N ALA A 140 41.845 16.200 -74.088 1.00 79.69 N
ANISOU 894 N ALA A 140 10358 13091 6830 1073 1905 -857 N
ATOM 895 CA ALA A 140 41.346 15.156 -74.975 1.00 83.31 C
ANISOU 895 CA ALA A 140 11035 13619 7001 1123 1924 -1146 C
ATOM 896 C ALA A 140 41.063 13.846 -74.249 1.00 87.75 C
ANISOU 896 C ALA A 140 11672 13913 7757 1204 1834 -1428 C
ATOM 897 O ALA A 140 40.420 12.966 -74.828 1.00 93.36 O
ANISOU 897 O ALA A 140 12589 14621 8263 1199 1801 -1690 O
ATOM 898 CB ALA A 140 42.338 14.909 -76.112 1.00 87.12 C
ANISOU 898 CB ALA A 140 11522 14344 7236 1218 2244 -1237 C
ATOM 899 N LYS A 141 41.514 13.701 -73.003 1.00 89.73 N
ANISOU 899 N LYS A 141 11774 13937 8382 1266 1792 -1379 N
ATOM 900 CA LYS A 141 41.332 12.478 -72.235 1.00 89.94 C
ANISOU 900 CA LYS A 141 11885 13680 8607 1358 1726 -1603 C
ATOM 901 C LYS A 141 40.211 12.574 -71.206 1.00 90.25 C
ANISOU 901 C LYS A 141 11972 13504 8816 1230 1442 -1547 C
ATOM 902 O LYS A 141 39.949 11.587 -70.512 1.00 93.28 O
ANISOU 902 O LYS A 141 12451 13631 9361 1277 1380 -1708 O
ATOM 903 CB LYS A 141 42.643 12.105 -71.528 1.00 91.17 C
ANISOU 903 CB LYS A 141 11852 13741 9047 1556 1876 -1595 C
ATOM 904 CG LYS A 141 43.754 11.574 -72.441 1.00 97.12 C
ANISOU 904 CG LYS A 141 12570 14656 9676 1740 2184 -1745 C
ATOM 905 CD LYS A 141 43.222 10.822 -73.657 1.00102.78 C
ANISOU 905 CD LYS A 141 13559 15443 10051 1735 2270 -2019 C
ATOM 906 CE LYS A 141 44.341 10.526 -74.649 1.00110.63 C
ANISOU 906 CE LYS A 141 14501 16651 10882 1902 2603 -2141 C
ATOM 907 NZ LYS A 141 43.840 9.918 -75.913 1.00112.19 N
ANISOU 907 NZ LYS A 141 14970 16961 10694 1877 2695 -2411 N
ATOM 908 N ARG A 142 39.561 13.733 -71.073 1.00 86.28 N
ANISOU 908 N ARG A 142 11409 13086 8285 1078 1286 -1317 N
ATOM 909 CA ARG A 142 38.530 13.925 -70.053 1.00 80.17 C
ANISOU 909 CA ARG A 142 10647 12130 7683 965 1037 -1254 C
ATOM 910 C ARG A 142 37.307 13.080 -70.382 1.00 83.56 C
ANISOU 910 C ARG A 142 11283 12506 7962 876 910 -1490 C
ATOM 911 O ARG A 142 36.615 13.332 -71.374 1.00 87.34 O
ANISOU 911 O ARG A 142 11845 13191 8149 792 858 -1525 O
ATOM 912 CB ARG A 142 38.140 15.396 -69.937 1.00 73.32 C
ANISOU 912 CB ARG A 142 9675 11370 6811 849 925 -964 C
ATOM 913 CG ARG A 142 39.242 16.306 -69.435 1.00 69.08 C
ANISOU 913 CG ARG A 142 8933 10849 6466 877 1027 -735 C
ATOM 914 CD ARG A 142 38.850 17.774 -69.557 1.00 67.16 C
ANISOU 914 CD ARG A 142 8642 10698 6178 759 955 -461 C
ATOM 915 NE ARG A 142 37.889 18.198 -68.539 1.00 62.89 N
ANISOU 915 NE ARG A 142 8095 9989 5810 676 730 -384 N
ATOM 916 CZ ARG A 142 36.594 18.401 -68.760 1.00 62.42 C
ANISOU 916 CZ ARG A 142 8136 9957 5624 610 557 -380 C
ATOM 917 NH1 ARG A 142 36.083 18.225 -69.970 1.00 63.71 N
ANISOU 917 NH1 ARG A 142 8419 10317 5472 609 556 -445 N
ATOM 918 NH2 ARG A 142 35.806 18.790 -67.769 1.00 61.64 N
ANISOU 918 NH2 ARG A 142 8005 9710 5705 549 382 -316 N
ATOM 919 N THR A 143 37.047 12.075 -69.556 1.00 83.05 N
ANISOU 919 N THR A 143 11300 12171 8086 888 860 -1650 N
ATOM 920 CA THR A 143 35.859 11.245 -69.620 1.00 82.24 C
ANISOU 920 CA THR A 143 11375 11963 7908 760 736 -1877 C
ATOM 921 C THR A 143 35.120 11.366 -68.293 1.00 85.71 C
ANISOU 921 C THR A 143 11772 12193 8601 664 558 -1783 C
ATOM 922 O THR A 143 35.709 11.793 -67.291 1.00 83.14 O
ANISOU 922 O THR A 143 11319 11757 8513 736 558 -1597 O
ATOM 923 CB THR A 143 36.222 9.775 -69.900 1.00 80.39 C
ANISOU 923 CB THR A 143 11332 11552 7661 848 887 -2186 C
ATOM 924 OG1 THR A 143 37.010 9.255 -68.826 1.00 83.04 O
ANISOU 924 OG1 THR A 143 11639 11613 8298 1001 960 -2147 O
ATOM 925 CG2 THR A 143 37.001 9.650 -71.203 1.00 74.22 C
ANISOU 925 CG2 THR A 143 10591 10989 6620 958 1091 -2297 C
ATOM 926 N PRO A 144 33.819 11.048 -68.253 1.00 89.33 N
ANISOU 926 N PRO A 144 12317 12621 9003 489 404 -1910 N
ATOM 927 CA PRO A 144 33.112 11.050 -66.959 1.00 88.37 C
ANISOU 927 CA PRO A 144 12164 12294 9121 392 268 -1843 C
ATOM 928 C PRO A 144 33.685 10.083 -65.933 1.00 92.00 C
ANISOU 928 C PRO A 144 12711 12418 9827 482 355 -1897 C
ATOM 929 O PRO A 144 33.521 10.314 -64.729 1.00 87.50 O
ANISOU 929 O PRO A 144 12081 11699 9467 460 277 -1759 O
ATOM 930 CB PRO A 144 31.672 10.684 -67.345 1.00 88.68 C
ANISOU 930 CB PRO A 144 12279 12397 9019 181 127 -2030 C
ATOM 931 CG PRO A 144 31.546 11.099 -68.762 1.00 89.56 C
ANISOU 931 CG PRO A 144 12386 12837 8806 174 116 -2072 C
ATOM 932 CD PRO A 144 32.884 10.858 -69.380 1.00 89.27 C
ANISOU 932 CD PRO A 144 12403 12821 8697 355 330 -2095 C
ATOM 933 N LYS A 145 34.356 9.010 -66.366 1.00 99.54 N
ANISOU 933 N LYS A 145 13817 13250 10753 598 516 -2090 N
ATOM 934 CA LYS A 145 34.918 8.056 -65.414 1.00 96.46 C
ANISOU 934 CA LYS A 145 13531 12526 10592 723 599 -2122 C
ATOM 935 C LYS A 145 36.137 8.627 -64.696 1.00 93.73 C
ANISOU 935 C LYS A 145 13004 12191 10420 931 642 -1882 C
ATOM 936 O LYS A 145 36.309 8.402 -63.493 1.00 90.39 O
ANISOU 936 O LYS A 145 12579 11558 10206 987 602 -1780 O
ATOM 937 CB LYS A 145 35.272 6.753 -66.126 1.00100.94 C
ANISOU 937 CB LYS A 145 14327 12942 11086 812 769 -2406 C
ATOM 938 CG LYS A 145 34.064 5.882 -66.416 1.00107.08 C
ANISOU 938 CG LYS A 145 15324 13584 11776 579 724 -2674 C
ATOM 939 CD LYS A 145 33.344 5.495 -65.136 1.00107.50 C
ANISOU 939 CD LYS A 145 15449 13350 12046 452 634 -2622 C
ATOM 940 CE LYS A 145 32.139 4.621 -65.432 1.00109.21 C
ANISOU 940 CE LYS A 145 15867 13438 12191 179 606 -2903 C
ATOM 941 NZ LYS A 145 31.169 5.304 -66.333 1.00108.95 N
ANISOU 941 NZ LYS A 145 15713 13765 11920 -36 463 -2979 N
ATOM 942 N ARG A 146 37.004 9.344 -65.420 1.00 88.96 N
ANISOU 942 N ARG A 146 12243 11838 9720 1037 729 -1796 N
ATOM 943 CA ARG A 146 38.110 10.063 -64.786 1.00 82.28 C
ANISOU 943 CA ARG A 146 11174 11057 9031 1181 755 -1570 C
ATOM 944 C ARG A 146 37.599 11.065 -63.755 1.00 72.78 C
ANISOU 944 C ARG A 146 9843 9856 7954 1049 577 -1354 C
ATOM 945 O ARG A 146 38.138 11.164 -62.638 1.00 74.12 O
ANISOU 945 O ARG A 146 9920 9922 8321 1130 538 -1227 O
ATOM 946 CB ARG A 146 38.933 10.779 -65.855 1.00 84.53 C
ANISOU 946 CB ARG A 146 11313 11639 9165 1244 887 -1517 C
ATOM 947 CG ARG A 146 39.508 9.859 -66.913 1.00 94.02 C
ANISOU 947 CG ARG A 146 12629 12872 10223 1387 1090 -1739 C
ATOM 948 CD ARG A 146 40.590 8.965 -66.353 1.00 99.70 C
ANISOU 948 CD ARG A 146 13332 13413 11135 1648 1214 -1788 C
ATOM 949 NE ARG A 146 41.866 9.671 -66.302 1.00100.54 N
ANISOU 949 NE ARG A 146 13158 13723 11321 1786 1312 -1622 N
ATOM 950 CZ ARG A 146 42.697 9.787 -67.334 1.00103.77 C
ANISOU 950 CZ ARG A 146 13475 14357 11595 1886 1516 -1673 C
ATOM 951 NH1 ARG A 146 42.392 9.238 -68.503 1.00107.27 N
ANISOU 951 NH1 ARG A 146 14108 14852 11798 1877 1637 -1890 N
ATOM 952 NH2 ARG A 146 43.835 10.453 -67.196 1.00105.64 N
ANISOU 952 NH2 ARG A 146 13427 14783 11929 1979 1605 -1518 N
ATOM 953 N ALA A 147 36.560 11.822 -64.126 1.00 66.25 N
ANISOU 953 N ALA A 147 9009 9160 7005 860 464 -1317 N
ATOM 954 CA ALA A 147 35.950 12.773 -63.206 1.00 66.72 C
ANISOU 954 CA ALA A 147 8966 9210 7176 740 308 -1138 C
ATOM 955 C ALA A 147 35.377 12.057 -61.992 1.00 67.00 C
ANISOU 955 C ALA A 147 9102 8983 7370 697 225 -1180 C
ATOM 956 O ALA A 147 35.500 12.543 -60.865 1.00 69.01 O
ANISOU 956 O ALA A 147 9269 9169 7781 695 152 -1032 O
ATOM 957 CB ALA A 147 34.866 13.578 -63.927 1.00 64.13 C
ANISOU 957 CB ALA A 147 8627 9065 6676 584 209 -1110 C
ATOM 958 N GLY A 148 34.771 10.887 -62.205 1.00 65.88 N
ANISOU 958 N GLY A 148 9160 8690 7182 650 249 -1386 N
ATOM 959 CA GLY A 148 34.246 10.111 -61.096 1.00 61.78 C
ANISOU 959 CA GLY A 148 8770 7899 6805 596 205 -1421 C
ATOM 960 C GLY A 148 35.328 9.570 -60.185 1.00 60.42 C
ANISOU 960 C GLY A 148 8619 7540 6799 801 266 -1343 C
ATOM 961 O GLY A 148 35.119 9.460 -58.974 1.00 60.94 O
ANISOU 961 O GLY A 148 8715 7446 6995 781 199 -1250 O
ATOM 962 N ILE A 149 36.488 9.221 -60.752 1.00 54.70 N
ANISOU 962 N ILE A 149 7872 6850 6061 1011 395 -1379 N
ATOM 963 CA ILE A 149 37.640 8.840 -59.936 1.00 57.05 C
ANISOU 963 CA ILE A 149 8128 7036 6514 1249 436 -1282 C
ATOM 964 C ILE A 149 38.033 9.990 -59.023 1.00 62.11 C
ANISOU 964 C ILE A 149 8535 7812 7252 1240 323 -1055 C
ATOM 965 O ILE A 149 38.211 9.810 -57.811 1.00 59.91 O
ANISOU 965 O ILE A 149 8265 7401 7097 1299 250 -951 O
ATOM 966 CB ILE A 149 38.825 8.412 -60.822 1.00 58.56 C
ANISOU 966 CB ILE A 149 8277 7305 6668 1483 604 -1365 C
ATOM 967 CG1 ILE A 149 38.543 7.083 -61.522 1.00 61.48 C
ANISOU 967 CG1 ILE A 149 8924 7468 6968 1527 732 -1614 C
ATOM 968 CG2 ILE A 149 40.093 8.302 -59.982 1.00 50.71 C
ANISOU 968 CG2 ILE A 149 7140 6290 5836 1743 618 -1229 C
ATOM 969 CD1 ILE A 149 39.665 6.609 -62.428 1.00 55.39 C
ANISOU 969 CD1 ILE A 149 8128 6767 6152 1774 923 -1727 C
ATOM 970 N MET A 150 38.173 11.189 -59.600 1.00 65.11 N
ANISOU 970 N MET A 150 8721 8451 7566 1159 310 -977 N
ATOM 971 CA MET A 150 38.560 12.364 -58.816 1.00 64.08 C
ANISOU 971 CA MET A 150 8377 8440 7529 1121 217 -785 C
ATOM 972 C MET A 150 37.520 12.691 -57.739 1.00 62.24 C
ANISOU 972 C MET A 150 8204 8093 7353 960 70 -721 C
ATOM 973 O MET A 150 37.875 13.014 -56.596 1.00 59.44 O
ANISOU 973 O MET A 150 7769 7707 7107 984 -10 -607 O
ATOM 974 CB MET A 150 38.791 13.546 -59.759 1.00 65.66 C
ANISOU 974 CB MET A 150 8413 8895 7641 1043 259 -719 C
ATOM 975 CG MET A 150 40.019 13.347 -60.645 1.00 75.70 C
ANISOU 975 CG MET A 150 9577 10313 8872 1206 425 -754 C
ATOM 976 SD MET A 150 40.250 14.575 -61.950 1.00 88.10 S
ANISOU 976 SD MET A 150 11014 12170 10291 1103 523 -678 S
ATOM 977 CE MET A 150 40.625 16.041 -60.997 1.00 92.39 C
ANISOU 977 CE MET A 150 11334 12779 10990 986 428 -460 C
ATOM 978 N ILE A 151 36.233 12.589 -58.087 1.00 60.68 N
ANISOU 978 N ILE A 151 8134 7850 7070 794 36 -807 N
ATOM 979 CA ILE A 151 35.147 12.853 -57.139 1.00 56.67 C
ANISOU 979 CA ILE A 151 7672 7250 6609 636 -77 -768 C
ATOM 980 C ILE A 151 35.176 11.849 -55.989 1.00 57.62 C
ANISOU 980 C ILE A 151 7940 7131 6822 692 -86 -770 C
ATOM 981 O ILE A 151 35.087 12.223 -54.808 1.00 59.53 O
ANISOU 981 O ILE A 151 8151 7330 7140 661 -167 -661 O
ATOM 982 CB ILE A 151 33.793 12.833 -57.874 1.00 57.77 C
ANISOU 982 CB ILE A 151 7888 7428 6635 459 -103 -882 C
ATOM 983 CG1 ILE A 151 33.646 14.072 -58.762 1.00 62.24 C
ANISOU 983 CG1 ILE A 151 8307 8235 7107 410 -130 -812 C
ATOM 984 CG2 ILE A 151 32.630 12.705 -56.896 1.00 51.65 C
ANISOU 984 CG2 ILE A 151 7182 6528 5915 305 -181 -889 C
ATOM 985 CD1 ILE A 151 32.621 13.912 -59.869 1.00 63.84 C
ANISOU 985 CD1 ILE A 151 8569 8545 7144 303 -148 -940 C
ATOM 986 N GLY A 152 35.273 10.556 -56.323 1.00 58.67 N
ANISOU 986 N GLY A 152 8259 7094 6940 773 4 -896 N
ATOM 987 CA GLY A 152 35.315 9.525 -55.303 1.00 62.65 C
ANISOU 987 CA GLY A 152 8946 7334 7524 845 14 -879 C
ATOM 988 C GLY A 152 36.537 9.626 -54.417 1.00 65.30 C
ANISOU 988 C GLY A 152 9182 7680 7948 1063 -21 -723 C
ATOM 989 O GLY A 152 36.462 9.341 -53.222 1.00 71.87 O
ANISOU 989 O GLY A 152 10099 8376 8831 1084 -77 -627 O
ATOM 990 N LEU A 153 37.671 10.042 -54.984 1.00 62.13 N
ANISOU 990 N LEU A 153 8589 7464 7554 1220 12 -696 N
ATOM 991 CA LEU A 153 38.863 10.271 -54.177 1.00 62.46 C
ANISOU 991 CA LEU A 153 8468 7585 7678 1410 -42 -558 C
ATOM 992 C LEU A 153 38.657 11.436 -53.221 1.00 64.96 C
ANISOU 992 C LEU A 153 8640 8022 8019 1265 -181 -432 C
ATOM 993 O LEU A 153 39.095 11.374 -52.067 1.00 71.42 O
ANISOU 993 O LEU A 153 9437 8815 8883 1351 -271 -326 O
ATOM 994 CB LEU A 153 40.074 10.524 -55.074 1.00 62.16 C
ANISOU 994 CB LEU A 153 8219 7754 7646 1573 42 -575 C
ATOM 995 CG LEU A 153 40.701 9.298 -55.731 1.00 68.34 C
ANISOU 995 CG LEU A 153 9111 8422 8432 1818 184 -684 C
ATOM 996 CD1 LEU A 153 41.849 9.701 -56.640 1.00 73.75 C
ANISOU 996 CD1 LEU A 153 9548 9361 9113 1952 287 -703 C
ATOM 997 CD2 LEU A 153 41.191 8.360 -54.651 1.00 70.38 C
ANISOU 997 CD2 LEU A 153 9476 8487 8780 2050 143 -605 C
ATOM 998 N ALA A 154 38.021 12.513 -53.696 1.00 58.48 N
ANISOU 998 N ALA A 154 7726 7335 7160 1060 -199 -442 N
ATOM 999 CA ALA A 154 37.666 13.632 -52.824 1.00 62.65 C
ANISOU 999 CA ALA A 154 8154 7936 7714 910 -311 -349 C
ATOM 1000 C ALA A 154 36.857 13.164 -51.617 1.00 61.27 C
ANISOU 1000 C ALA A 154 8155 7583 7541 846 -377 -325 C
ATOM 1001 O ALA A 154 37.229 13.418 -50.460 1.00 67.31 O
ANISOU 1001 O ALA A 154 8879 8363 8334 875 -466 -234 O
ATOM 1002 CB ALA A 154 36.886 14.675 -53.627 1.00 59.69 C
ANISOU 1002 CB ALA A 154 7715 7671 7294 726 -302 -371 C
ATOM 1003 N TRP A 155 35.771 12.428 -51.880 1.00 58.49 N
ANISOU 1003 N TRP A 155 8002 7073 7149 751 -325 -414 N
ATOM 1004 CA TRP A 155 34.901 11.952 -50.803 1.00 56.78 C
ANISOU 1004 CA TRP A 155 7961 6684 6927 656 -352 -394 C
ATOM 1005 C TRP A 155 35.622 10.969 -49.881 1.00 59.90 C
ANISOU 1005 C TRP A 155 8492 6925 7343 842 -360 -311 C
ATOM 1006 O TRP A 155 35.499 11.058 -48.653 1.00 62.95 O
ANISOU 1006 O TRP A 155 8928 7274 7717 822 -428 -215 O
ATOM 1007 CB TRP A 155 33.641 11.314 -51.387 1.00 59.27 C
ANISOU 1007 CB TRP A 155 8438 6877 7205 493 -280 -526 C
ATOM 1008 CG TRP A 155 32.654 12.320 -51.906 1.00 62.04 C
ANISOU 1008 CG TRP A 155 8663 7383 7525 303 -311 -574 C
ATOM 1009 CD1 TRP A 155 32.512 12.746 -53.195 1.00 60.31 C
ANISOU 1009 CD1 TRP A 155 8348 7310 7257 274 -295 -647 C
ATOM 1010 CD2 TRP A 155 31.670 13.028 -51.139 1.00 58.57 C
ANISOU 1010 CD2 TRP A 155 8184 6977 7094 141 -362 -545 C
ATOM 1011 NE1 TRP A 155 31.501 13.674 -53.278 1.00 56.69 N
ANISOU 1011 NE1 TRP A 155 7791 6968 6781 122 -347 -650 N
ATOM 1012 CE2 TRP A 155 30.968 13.865 -52.030 1.00 56.23 C
ANISOU 1012 CE2 TRP A 155 7757 6841 6768 42 -382 -597 C
ATOM 1013 CE3 TRP A 155 31.311 13.030 -49.786 1.00 59.70 C
ANISOU 1013 CE3 TRP A 155 8394 7038 7253 83 -385 -479 C
ATOM 1014 CZ2 TRP A 155 29.932 14.700 -51.612 1.00 56.72 C
ANISOU 1014 CZ2 TRP A 155 7738 6973 6841 -92 -423 -589 C
ATOM 1015 CZ3 TRP A 155 30.280 13.860 -49.372 1.00 57.29 C
ANISOU 1015 CZ3 TRP A 155 8010 6808 6948 -72 -411 -488 C
ATOM 1016 CH2 TRP A 155 29.603 14.683 -50.282 1.00 57.72 C
ANISOU 1016 CH2 TRP A 155 7920 7013 6998 -148 -429 -544 C
ATOM 1017 N LEU A 156 36.395 10.041 -50.454 1.00 61.46 N
ANISOU 1017 N LEU A 156 8754 7037 7560 1044 -289 -343 N
ATOM 1018 CA LEU A 156 37.061 9.008 -49.666 1.00 63.93 C
ANISOU 1018 CA LEU A 156 9219 7177 7894 1267 -290 -252 C
ATOM 1019 C LEU A 156 38.156 9.592 -48.781 1.00 67.02 C
ANISOU 1019 C LEU A 156 9415 7751 8299 1426 -420 -108 C
ATOM 1020 O LEU A 156 38.299 9.189 -47.619 1.00 65.83 O
ANISOU 1020 O LEU A 156 9375 7514 8122 1514 -490 14 O
ATOM 1021 CB LEU A 156 37.636 7.945 -50.600 1.00 63.63 C
ANISOU 1021 CB LEU A 156 9284 7006 7885 1469 -169 -340 C
ATOM 1022 CG LEU A 156 38.342 6.740 -49.981 1.00 66.37 C
ANISOU 1022 CG LEU A 156 9820 7130 8269 1756 -145 -251 C
ATOM 1023 CD1 LEU A 156 37.444 6.050 -48.975 1.00 70.24 C
ANISOU 1023 CD1 LEU A 156 10613 7342 8732 1648 -138 -181 C
ATOM 1024 CD2 LEU A 156 38.763 5.769 -51.071 1.00 71.41 C
ANISOU 1024 CD2 LEU A 156 10569 7621 8942 1933 6 -385 C
ATOM 1025 N ILE A 157 38.936 10.541 -49.308 1.00 72.06 N
ANISOU 1025 N ILE A 157 9763 8651 8966 1450 -454 -119 N
ATOM 1026 CA ILE A 157 39.991 11.165 -48.517 1.00 71.70 C
ANISOU 1026 CA ILE A 157 9492 8812 8937 1559 -584 -12 C
ATOM 1027 C ILE A 157 39.387 12.004 -47.400 1.00 68.64 C
ANISOU 1027 C ILE A 157 9102 8475 8502 1362 -699 44 C
ATOM 1028 O ILE A 157 39.861 11.959 -46.255 1.00 67.57 O
ANISOU 1028 O ILE A 157 8956 8387 8330 1452 -819 146 O
ATOM 1029 CB ILE A 157 40.927 11.989 -49.423 1.00 69.55 C
ANISOU 1029 CB ILE A 157 8909 8799 8718 1584 -561 -52 C
ATOM 1030 CG1 ILE A 157 41.765 11.055 -50.302 1.00 75.02 C
ANISOU 1030 CG1 ILE A 157 9587 9468 9449 1845 -448 -97 C
ATOM 1031 CG2 ILE A 157 41.834 12.895 -48.602 1.00 67.40 C
ANISOU 1031 CG2 ILE A 157 8372 8769 8467 1591 -704 27 C
ATOM 1032 CD1 ILE A 157 42.785 11.773 -51.166 1.00 75.08 C
ANISOU 1032 CD1 ILE A 157 9277 9748 9501 1883 -398 -129 C
ATOM 1033 N SER A 158 38.328 12.769 -47.710 1.00 65.18 N
ANISOU 1033 N SER A 158 8675 8038 8053 1105 -666 -24 N
ATOM 1034 CA SER A 158 37.614 13.521 -46.680 1.00 66.39 C
ANISOU 1034 CA SER A 158 8852 8211 8162 923 -744 5 C
ATOM 1035 C SER A 158 37.119 12.604 -45.565 1.00 65.72 C
ANISOU 1035 C SER A 158 9021 7945 8004 952 -759 75 C
ATOM 1036 O SER A 158 37.288 12.906 -44.373 1.00 60.05 O
ANISOU 1036 O SER A 158 8304 7290 7221 948 -862 151 O
ATOM 1037 CB SER A 158 36.451 14.278 -47.316 1.00 65.02 C
ANISOU 1037 CB SER A 158 8672 8035 7998 692 -682 -82 C
ATOM 1038 OG SER A 158 36.935 15.339 -48.117 1.00 65.75 O
ANISOU 1038 OG SER A 158 8542 8300 8140 652 -682 -106 O
ATOM 1039 N PHE A 159 36.524 11.466 -45.942 1.00 67.55 N
ANISOU 1039 N PHE A 159 9483 7948 8234 972 -649 48 N
ATOM 1040 CA PHE A 159 36.011 10.515 -44.959 1.00 63.92 C
ANISOU 1040 CA PHE A 159 9302 7277 7709 980 -627 128 C
ATOM 1041 C PHE A 159 37.132 9.966 -44.084 1.00 71.96 C
ANISOU 1041 C PHE A 159 10357 8301 8685 1249 -724 279 C
ATOM 1042 O PHE A 159 37.068 10.058 -42.852 1.00 80.87 O
ANISOU 1042 O PHE A 159 11562 9453 9714 1240 -807 385 O
ATOM 1043 CB PHE A 159 35.265 9.381 -45.668 1.00 54.20 C
ANISOU 1043 CB PHE A 159 8307 5781 6505 935 -475 50 C
ATOM 1044 CG PHE A 159 34.753 8.311 -44.740 1.00 49.79 C
ANISOU 1044 CG PHE A 159 8067 4958 5891 928 -417 141 C
ATOM 1045 CD1 PHE A 159 33.573 8.500 -44.034 1.00 51.75 C
ANISOU 1045 CD1 PHE A 159 8420 5161 6082 678 -378 140 C
ATOM 1046 CD2 PHE A 159 35.428 7.105 -44.600 1.00 51.43 C
ANISOU 1046 CD2 PHE A 159 8481 4953 6108 1175 -382 231 C
ATOM 1047 CE1 PHE A 159 33.087 7.517 -43.180 1.00 47.44 C
ANISOU 1047 CE1 PHE A 159 8180 4368 5476 646 -298 236 C
ATOM 1048 CE2 PHE A 159 34.947 6.115 -43.752 1.00 49.76 C
ANISOU 1048 CE2 PHE A 159 8599 4465 5842 1163 -311 339 C
ATOM 1049 CZ PHE A 159 33.777 6.323 -43.042 1.00 49.40 C
ANISOU 1049 CZ PHE A 159 8659 4383 5729 883 -265 345 C
ATOM 1050 N ILE A 160 38.181 9.408 -44.701 1.00 69.37 N
ANISOU 1050 N ILE A 160 9963 7976 8418 1506 -719 290 N
ATOM 1051 CA ILE A 160 39.221 8.740 -43.920 1.00 76.56 C
ANISOU 1051 CA ILE A 160 10912 8884 9293 1811 -812 444 C
ATOM 1052 C ILE A 160 40.055 9.729 -43.118 1.00 73.21 C
ANISOU 1052 C ILE A 160 10217 8780 8818 1846 -1004 508 C
ATOM 1053 O ILE A 160 40.750 9.325 -42.179 1.00 70.29 O
ANISOU 1053 O ILE A 160 9876 8459 8373 2060 -1127 651 O
ATOM 1054 CB ILE A 160 40.146 7.874 -44.802 1.00 81.21 C
ANISOU 1054 CB ILE A 160 11480 9402 9975 2109 -745 428 C
ATOM 1055 CG1 ILE A 160 40.965 8.745 -45.757 1.00 84.08 C
ANISOU 1055 CG1 ILE A 160 11477 10052 10419 2128 -759 328 C
ATOM 1056 CG2 ILE A 160 39.344 6.814 -45.550 1.00 80.04 C
ANISOU 1056 CG2 ILE A 160 11634 8909 9867 2066 -554 341 C
ATOM 1057 CD1 ILE A 160 41.862 7.956 -46.686 1.00 91.00 C
ANISOU 1057 CD1 ILE A 160 12307 10889 11381 2418 -666 288 C
ATOM 1058 N LEU A 161 40.018 11.016 -43.461 1.00 73.81 N
ANISOU 1058 N LEU A 161 10039 9078 8929 1643 -1037 406 N
ATOM 1059 CA LEU A 161 40.706 11.992 -42.628 1.00 75.44 C
ANISOU 1059 CA LEU A 161 10015 9565 9085 1619 -1211 438 C
ATOM 1060 C LEU A 161 39.844 12.415 -41.445 1.00 78.78 C
ANISOU 1060 C LEU A 161 10588 9968 9378 1424 -1267 465 C
ATOM 1061 O LEU A 161 40.311 12.416 -40.301 1.00 87.66 O
ANISOU 1061 O LEU A 161 11718 11209 10380 1508 -1414 560 O
ATOM 1062 CB LEU A 161 41.116 13.208 -43.458 1.00 71.04 C
ANISOU 1062 CB LEU A 161 9140 9225 8629 1479 -1207 322 C
ATOM 1063 CG LEU A 161 42.327 13.001 -44.367 1.00 73.58 C
ANISOU 1063 CG LEU A 161 9224 9681 9053 1685 -1186 307 C
ATOM 1064 CD1 LEU A 161 42.699 14.307 -45.053 1.00 70.28 C
ANISOU 1064 CD1 LEU A 161 8509 9478 8717 1501 -1172 213 C
ATOM 1065 CD2 LEU A 161 43.503 12.440 -43.575 1.00 73.62 C
ANISOU 1065 CD2 LEU A 161 9125 9827 9021 1977 -1336 419 C
ATOM 1066 N TRP A 162 38.579 12.764 -41.691 1.00 72.48 N
ANISOU 1066 N TRP A 162 9907 9043 8589 1173 -1150 381 N
ATOM 1067 CA TRP A 162 37.805 13.402 -40.632 1.00 66.51 C
ANISOU 1067 CA TRP A 162 9232 8316 7721 975 -1186 375 C
ATOM 1068 C TRP A 162 37.001 12.435 -39.766 1.00 65.81 C
ANISOU 1068 C TRP A 162 9475 8022 7507 973 -1127 474 C
ATOM 1069 O TRP A 162 36.872 12.675 -38.561 1.00 68.64 O
ANISOU 1069 O TRP A 162 9912 8454 7715 927 -1203 530 O
ATOM 1070 CB TRP A 162 36.895 14.473 -41.233 1.00 59.80 C
ANISOU 1070 CB TRP A 162 8292 7482 6949 717 -1101 235 C
ATOM 1071 CG TRP A 162 37.626 15.757 -41.456 1.00 59.06 C
ANISOU 1071 CG TRP A 162 7912 7609 6918 656 -1187 166 C
ATOM 1072 CD1 TRP A 162 37.913 16.341 -42.655 1.00 51.33 C
ANISOU 1072 CD1 TRP A 162 6745 6688 6071 623 -1137 97 C
ATOM 1073 CD2 TRP A 162 38.155 16.630 -40.445 1.00 62.53 C
ANISOU 1073 CD2 TRP A 162 8239 8235 7284 599 -1327 153 C
ATOM 1074 NE1 TRP A 162 38.598 17.516 -42.454 1.00 57.02 N
ANISOU 1074 NE1 TRP A 162 7246 7596 6822 539 -1223 53 N
ATOM 1075 CE2 TRP A 162 38.757 17.717 -41.108 1.00 62.57 C
ANISOU 1075 CE2 TRP A 162 7986 8382 7406 516 -1346 71 C
ATOM 1076 CE3 TRP A 162 38.179 16.596 -39.045 1.00 59.18 C
ANISOU 1076 CE3 TRP A 162 7918 7876 6692 597 -1434 198 C
ATOM 1077 CZ2 TRP A 162 39.375 18.763 -40.419 1.00 66.43 C
ANISOU 1077 CZ2 TRP A 162 8314 9056 7871 413 -1467 13 C
ATOM 1078 CZ3 TRP A 162 38.797 17.633 -38.363 1.00 57.58 C
ANISOU 1078 CZ3 TRP A 162 7550 7886 6443 510 -1570 132 C
ATOM 1079 CH2 TRP A 162 39.384 18.702 -39.050 1.00 62.45 C
ANISOU 1079 CH2 TRP A 162 7907 8622 7201 409 -1584 32 C
ATOM 1080 N ALA A 163 36.432 11.362 -40.333 1.00 60.37 N
ANISOU 1080 N ALA A 163 8995 7077 6866 999 -982 489 N
ATOM 1081 CA ALA A 163 35.650 10.445 -39.503 1.00 58.12 C
ANISOU 1081 CA ALA A 163 9039 6574 6469 961 -900 590 C
ATOM 1082 C ALA A 163 36.496 9.718 -38.454 1.00 62.98 C
ANISOU 1082 C ALA A 163 9799 7184 6945 1214 -1013 790 C
ATOM 1083 O ALA A 163 36.076 9.690 -37.282 1.00 59.14 O
ANISOU 1083 O ALA A 163 9484 6698 6288 1146 -1030 882 O
ATOM 1084 CB ALA A 163 34.855 9.482 -40.394 1.00 59.03 C
ANISOU 1084 CB ALA A 163 9342 6406 6681 894 -713 536 C
ATOM 1085 N PRO A 164 37.662 9.110 -38.775 1.00 66.72 N
ANISOU 1085 N PRO A 164 10219 7664 7467 1521 -1089 871 N
ATOM 1086 CA PRO A 164 38.461 8.503 -37.692 1.00 68.11 C
ANISOU 1086 CA PRO A 164 10514 7874 7492 1790 -1227 1080 C
ATOM 1087 C PRO A 164 38.895 9.490 -36.619 1.00 69.95 C
ANISOU 1087 C PRO A 164 10578 8439 7563 1751 -1429 1101 C
ATOM 1088 O PRO A 164 38.844 9.144 -35.435 1.00 72.23 O
ANISOU 1088 O PRO A 164 11069 8730 7645 1811 -1497 1257 O
ATOM 1089 CB PRO A 164 39.658 7.891 -38.431 1.00 66.64 C
ANISOU 1089 CB PRO A 164 10204 7689 7426 2130 -1272 1117 C
ATOM 1090 CG PRO A 164 39.190 7.672 -39.794 1.00 68.61 C
ANISOU 1090 CG PRO A 164 10453 7757 7858 2032 -1087 962 C
ATOM 1091 CD PRO A 164 38.282 8.813 -40.085 1.00 65.07 C
ANISOU 1091 CD PRO A 164 9870 7421 7434 1670 -1042 793 C
ATOM 1092 N ALA A 165 39.335 10.693 -37.001 1.00 69.62 N
ANISOU 1092 N ALA A 165 10187 8669 7597 1645 -1520 948 N
ATOM 1093 CA ALA A 165 39.750 11.700 -36.025 1.00 67.03 C
ANISOU 1093 CA ALA A 165 9693 8650 7125 1569 -1707 925 C
ATOM 1094 C ALA A 165 38.622 12.013 -35.045 1.00 66.06 C
ANISOU 1094 C ALA A 165 9794 8477 6830 1329 -1648 917 C
ATOM 1095 O ALA A 165 38.767 11.821 -33.831 1.00 71.73 O
ANISOU 1095 O ALA A 165 10653 9285 7318 1394 -1758 1038 O
ATOM 1096 CB ALA A 165 40.212 12.967 -36.746 1.00 62.76 C
ANISOU 1096 CB ALA A 165 8780 8333 6732 1429 -1754 738 C
ATOM 1097 N ILE A 166 37.472 12.448 -35.572 1.00 56.96 N
ANISOU 1097 N ILE A 166 8677 7190 5776 1066 -1469 781 N
ATOM 1098 CA ILE A 166 36.347 12.878 -34.741 1.00 59.76 C
ANISOU 1098 CA ILE A 166 9190 7520 5995 826 -1385 738 C
ATOM 1099 C ILE A 166 35.809 11.720 -33.900 1.00 68.68 C
ANISOU 1099 C ILE A 166 10688 8457 6948 879 -1300 922 C
ATOM 1100 O ILE A 166 35.435 11.902 -32.732 1.00 69.82 O
ANISOU 1100 O ILE A 166 10978 8677 6871 794 -1315 967 O
ATOM 1101 CB ILE A 166 35.253 13.488 -35.639 1.00 55.67 C
ANISOU 1101 CB ILE A 166 8601 6902 5650 580 -1209 563 C
ATOM 1102 CG1 ILE A 166 35.775 14.752 -36.331 1.00 50.41 C
ANISOU 1102 CG1 ILE A 166 7606 6420 5127 517 -1287 407 C
ATOM 1103 CG2 ILE A 166 33.986 13.800 -34.845 1.00 54.45 C
ANISOU 1103 CG2 ILE A 166 8604 6707 5377 352 -1084 516 C
ATOM 1104 CD1 ILE A 166 34.781 15.362 -37.291 1.00 52.64 C
ANISOU 1104 CD1 ILE A 166 7812 6615 5574 326 -1136 263 C
ATOM 1105 N LEU A 167 35.819 10.503 -34.449 1.00 73.42 N
ANISOU 1105 N LEU A 167 11462 8802 7632 1024 -1205 1035 N
ATOM 1106 CA LEU A 167 35.199 9.380 -33.756 1.00 72.00 C
ANISOU 1106 CA LEU A 167 11667 8376 7314 1036 -1080 1211 C
ATOM 1107 C LEU A 167 36.134 8.650 -32.801 1.00 73.06 C
ANISOU 1107 C LEU A 167 11968 8546 7246 1336 -1234 1459 C
ATOM 1108 O LEU A 167 35.647 7.992 -31.874 1.00 78.02 O
ANISOU 1108 O LEU A 167 12924 9042 7679 1322 -1159 1628 O
ATOM 1109 CB LEU A 167 34.617 8.381 -34.762 1.00 74.96 C
ANISOU 1109 CB LEU A 167 12201 8408 7873 1009 -875 1201 C
ATOM 1110 CG LEU A 167 33.435 8.878 -35.600 1.00 75.37 C
ANISOU 1110 CG LEU A 167 12153 8402 8081 697 -704 985 C
ATOM 1111 CD1 LEU A 167 33.242 8.005 -36.832 1.00 75.56 C
ANISOU 1111 CD1 LEU A 167 12244 8164 8302 716 -570 931 C
ATOM 1112 CD2 LEU A 167 32.166 8.909 -34.760 1.00 72.11 C
ANISOU 1112 CD2 LEU A 167 11928 7932 7540 430 -548 988 C
ATOM 1113 N CYS A 168 37.454 8.749 -32.977 1.00 75.84 N
ANISOU 1113 N CYS A 168 12099 9088 7627 1610 -1446 1495 N
ATOM 1114 CA CYS A 168 38.370 7.932 -32.195 1.00 89.21 C
ANISOU 1114 CA CYS A 168 13937 10810 9148 1951 -1602 1747 C
ATOM 1115 C CYS A 168 39.517 8.723 -31.578 1.00 97.72 C
ANISOU 1115 C CYS A 168 14720 12315 10092 2089 -1902 1741 C
ATOM 1116 O CYS A 168 40.463 8.109 -31.073 1.00104.95 O
ANISOU 1116 O CYS A 168 15668 13320 10887 2423 -2076 1939 O
ATOM 1117 CB CYS A 168 38.947 6.799 -33.056 1.00 95.31 C
ANISOU 1117 CB CYS A 168 14781 11331 10100 2253 -1551 1847 C
ATOM 1118 SG CYS A 168 37.741 5.891 -34.058 1.00 97.27 S
ANISOU 1118 SG CYS A 168 15317 11085 10554 2071 -1209 1784 S
ATOM 1119 N TRP A 169 39.483 10.059 -31.610 1.00101.67 N
ANISOU 1119 N TRP A 169 14932 13083 10615 1849 -1971 1518 N
ATOM 1120 CA TRP A 169 40.495 10.804 -30.870 1.00110.83 C
ANISOU 1120 CA TRP A 169 15843 14650 11618 1926 -2253 1496 C
ATOM 1121 C TRP A 169 40.343 10.605 -29.363 1.00114.60 C
ANISOU 1121 C TRP A 169 16580 15238 11726 1954 -2357 1655 C
ATOM 1122 O TRP A 169 41.343 10.630 -28.631 1.00116.75 O
ANISOU 1122 O TRP A 169 16744 15807 11809 2160 -2623 1748 O
ATOM 1123 CB TRP A 169 40.441 12.286 -31.242 1.00113.68 C
ANISOU 1123 CB TRP A 169 15879 15218 12095 1632 -2275 1212 C
ATOM 1124 CG TRP A 169 41.542 13.084 -30.615 1.00125.14 C
ANISOU 1124 CG TRP A 169 17042 17084 13423 1671 -2559 1147 C
ATOM 1125 CD1 TRP A 169 41.438 13.961 -29.577 1.00130.59 C
ANISOU 1125 CD1 TRP A 169 17720 18010 13888 1483 -2676 1045 C
ATOM 1126 CD2 TRP A 169 42.927 13.064 -30.987 1.00132.78 C
ANISOU 1126 CD2 TRP A 169 17675 18292 14484 1903 -2760 1161 C
ATOM 1127 NE1 TRP A 169 42.671 14.495 -29.282 1.00137.56 N
ANISOU 1127 NE1 TRP A 169 18284 19267 14717 1561 -2950 985 N
ATOM 1128 CE2 TRP A 169 43.601 13.960 -30.134 1.00136.55 C
ANISOU 1128 CE2 TRP A 169 17937 19160 14788 1818 -3006 1060 C
ATOM 1129 CE3 TRP A 169 43.661 12.378 -31.961 1.00135.40 C
ANISOU 1129 CE3 TRP A 169 17858 18559 15028 2169 -2746 1233 C
ATOM 1130 CZ2 TRP A 169 44.975 14.184 -30.221 1.00139.90 C
ANISOU 1130 CZ2 TRP A 169 17978 19925 15251 1977 -3246 1035 C
ATOM 1131 CZ3 TRP A 169 45.024 12.603 -32.048 1.00137.79 C
ANISOU 1131 CZ3 TRP A 169 17782 19199 15372 2350 -2969 1215 C
ATOM 1132 CH2 TRP A 169 45.667 13.498 -31.183 1.00140.09 C
ANISOU 1132 CH2 TRP A 169 17840 19893 15496 2246 -3220 1119 C
ATOM 1133 N GLN A 170 39.104 10.423 -28.884 1.00112.48 N
ANISOU 1133 N GLN A 170 16637 14762 11340 1743 -2152 1683 N
ATOM 1134 CA GLN A 170 38.880 10.098 -27.477 1.00114.47 C
ANISOU 1134 CA GLN A 170 17191 15085 11217 1773 -2205 1863 C
ATOM 1135 C GLN A 170 39.569 8.791 -27.102 1.00121.44 C
ANISOU 1135 C GLN A 170 18300 15873 11970 2167 -2305 2194 C
ATOM 1136 O GLN A 170 40.135 8.666 -26.010 1.00126.95 O
ANISOU 1136 O GLN A 170 19081 16806 12350 2340 -2517 2359 O
ATOM 1137 CB GLN A 170 37.381 9.984 -27.181 1.00110.85 C
ANISOU 1137 CB GLN A 170 17044 14380 10694 1481 -1910 1846 C
ATOM 1138 CG GLN A 170 36.509 11.137 -27.633 1.00108.96 C
ANISOU 1138 CG GLN A 170 16621 14167 10613 1122 -1764 1540 C
ATOM 1139 CD GLN A 170 35.051 10.728 -27.819 1.00106.13 C
ANISOU 1139 CD GLN A 170 16509 13497 10319 888 -1435 1532 C
ATOM 1140 OE1 GLN A 170 34.206 11.543 -28.191 1.00 99.12 O
ANISOU 1140 OE1 GLN A 170 15494 12606 9562 622 -1294 1308 O
ATOM 1141 NE2 GLN A 170 34.756 9.451 -27.565 1.00110.73 N
ANISOU 1141 NE2 GLN A 170 17442 13813 10819 990 -1309 1778 N
ATOM 1142 N TYR A 171 39.527 7.805 -28.000 1.00122.53 N
ANISOU 1142 N TYR A 171 18551 15662 12343 2324 -2155 2294 N
ATOM 1143 CA TYR A 171 40.203 6.534 -27.759 1.00126.90 C
ANISOU 1143 CA TYR A 171 19330 16068 12820 2736 -2227 2608 C
ATOM 1144 C TYR A 171 41.713 6.662 -27.922 1.00126.30 C
ANISOU 1144 C TYR A 171 18840 16311 12836 3030 -2499 2600 C
ATOM 1145 O TYR A 171 42.468 5.935 -27.267 1.00130.01 O
ANISOU 1145 O TYR A 171 19321 16845 13233 3274 -2605 2800 O
ATOM 1146 CB TYR A 171 39.631 5.461 -28.689 1.00129.63 C
ANISOU 1146 CB TYR A 171 19927 15908 13417 2766 -1944 2670 C
ATOM 1147 CG TYR A 171 38.117 5.381 -28.648 1.00130.24 C
ANISOU 1147 CG TYR A 171 20290 15700 13496 2377 -1634 2607 C
ATOM 1148 CD1 TYR A 171 37.422 5.536 -27.449 1.00134.81 C
ANISOU 1148 CD1 TYR A 171 21116 16344 13763 2195 -1588 2699 C
ATOM 1149 CD2 TYR A 171 37.382 5.181 -29.806 1.00126.71 C
ANISOU 1149 CD2 TYR A 171 19842 14952 13350 2183 -1387 2442 C
ATOM 1150 CE1 TYR A 171 36.041 5.476 -27.406 1.00134.44 C
ANISOU 1150 CE1 TYR A 171 21289 16068 13726 1835 -1292 2632 C
ATOM 1151 CE2 TYR A 171 36.002 5.119 -29.769 1.00126.48 C
ANISOU 1151 CE2 TYR A 171 20025 14704 13327 1822 -1116 2373 C
ATOM 1152 CZ TYR A 171 35.336 5.268 -28.570 1.00129.15 C
ANISOU 1152 CZ TYR A 171 20585 15111 13376 1649 -1062 2468 C
ATOM 1153 OH TYR A 171 33.961 5.206 -28.539 1.00125.48 O
ANISOU 1153 OH TYR A 171 20295 14453 12928 1287 -777 2390 O
ATOM 1154 N LEU A 172 42.162 7.557 -28.804 1.00123.20 N
ANISOU 1154 N LEU A 172 18062 16117 12631 2984 -2593 2366 N
ATOM 1155 CA LEU A 172 43.593 7.778 -28.995 1.00124.26 C
ANISOU 1155 CA LEU A 172 17756 16587 12869 3211 -2830 2329 C
ATOM 1156 C LEU A 172 44.229 8.392 -27.752 1.00126.76 C
ANISOU 1156 C LEU A 172 17889 17338 12935 3155 -3086 2328 C
ATOM 1157 O LEU A 172 45.301 7.959 -27.312 1.00133.97 O
ANISOU 1157 O LEU A 172 18638 18435 13829 3391 -3259 2453 O
ATOM 1158 CB LEU A 172 43.830 8.667 -30.214 1.00120.88 C
ANISOU 1158 CB LEU A 172 16948 16266 12715 3087 -2818 2057 C
ATOM 1159 N VAL A 173 43.583 9.405 -27.169 1.00123.63 N
ANISOU 1159 N VAL A 173 17524 17106 12342 2840 -3114 2176 N
ATOM 1160 CA VAL A 173 44.132 10.032 -25.969 1.00127.93 C
ANISOU 1160 CA VAL A 173 17920 18056 12633 2749 -3348 2144 C
ATOM 1161 C VAL A 173 43.831 9.209 -24.718 1.00143.79 C
ANISOU 1161 C VAL A 173 20293 19997 14344 2824 -3334 2407 C
ATOM 1162 O VAL A 173 44.595 9.261 -23.744 1.00148.24 O
ANISOU 1162 O VAL A 173 20747 20863 14714 2888 -3558 2478 O
ATOM 1163 CB VAL A 173 43.584 11.469 -25.863 1.00114.94 C
ANISOU 1163 CB VAL A 173 16165 16602 10906 2378 -3366 1843 C
ATOM 1164 CG1 VAL A 173 44.147 12.224 -24.656 1.00116.76 C
ANISOU 1164 CG1 VAL A 173 16238 17245 10879 2237 -3600 1756 C
ATOM 1165 CG2 VAL A 173 43.887 12.226 -27.129 1.00106.65 C
ANISOU 1165 CG2 VAL A 173 14765 15597 10161 2309 -3368 1606 C
ATOM 1166 N GLY A 174 42.799 8.373 -24.752 1.00156.46 N
ANISOU 1166 N GLY A 174 22327 21199 15921 2824 -3075 2567 N
ATOM 1167 CA GLY A 174 42.478 7.529 -23.620 1.00158.17 C
ANISOU 1167 CA GLY A 174 22902 21320 15875 2884 -3025 2833 C
ATOM 1168 C GLY A 174 41.196 7.964 -22.942 1.00155.32 C
ANISOU 1168 C GLY A 174 22841 20906 15266 2560 -2850 2777 C
ATOM 1169 O GLY A 174 40.425 7.130 -22.458 1.00156.06 O
ANISOU 1169 O GLY A 174 23328 20728 15240 2542 -2645 2980 O
ATOM 1170 N LYS A 175 40.961 9.273 -22.900 1.00153.41 N
ANISOU 1170 N LYS A 175 22414 20917 14957 2292 -2913 2491 N
ATOM 1171 CA LYS A 175 39.799 9.833 -22.231 1.00152.76 C
ANISOU 1171 CA LYS A 175 22575 20831 14638 1978 -2751 2389 C
ATOM 1172 C LYS A 175 39.045 10.746 -23.189 1.00150.25 C
ANISOU 1172 C LYS A 175 22187 20401 14502 1733 -2622 2100 C
ATOM 1173 O LYS A 175 39.606 11.283 -24.148 1.00147.21 O
ANISOU 1173 O LYS A 175 21442 20078 14412 1739 -2706 1918 O
ATOM 1174 CB LYS A 175 40.196 10.610 -20.967 1.00152.77 C
ANISOU 1174 CB LYS A 175 22463 21273 14308 1863 -2957 2303 C
ATOM 1175 N ARG A 176 37.755 10.916 -22.910 1.00154.63 N
ANISOU 1175 N ARG A 176 22985 20784 14984 1446 -2347 2032 N
ATOM 1176 CA ARG A 176 36.878 11.789 -23.683 1.00155.44 C
ANISOU 1176 CA ARG A 176 22916 20770 15373 1117 -2128 1727 C
ATOM 1177 C ARG A 176 36.649 13.055 -22.866 1.00163.42 C
ANISOU 1177 C ARG A 176 23837 22082 16173 872 -2184 1477 C
ATOM 1178 O ARG A 176 35.925 13.033 -21.865 1.00176.15 O
ANISOU 1178 O ARG A 176 25723 23726 17479 748 -2066 1516 O
ATOM 1179 CB ARG A 176 35.559 11.091 -24.010 1.00155.46 C
ANISOU 1179 CB ARG A 176 23201 20379 15489 963 -1764 1800 C
ATOM 1180 N THR A 177 37.264 14.160 -23.291 1.00154.00 N
ANISOU 1180 N THR A 177 22273 21100 15141 794 -2345 1214 N
ATOM 1181 CA THR A 177 37.217 15.413 -22.546 1.00146.90 C
ANISOU 1181 CA THR A 177 21276 20481 14058 573 -2424 948 C
ATOM 1182 C THR A 177 36.169 16.379 -23.090 1.00141.58 C
ANISOU 1182 C THR A 177 20516 19653 13627 270 -2167 664 C
ATOM 1183 O THR A 177 36.282 17.595 -22.898 1.00140.39 O
ANISOU 1183 O THR A 177 20191 19676 13475 93 -2231 386 O
ATOM 1184 CB THR A 177 38.597 16.072 -22.537 1.00139.55 C
ANISOU 1184 CB THR A 177 20004 19894 13126 655 -2771 828 C
ATOM 1185 OG1 THR A 177 38.525 17.331 -21.854 1.00137.65 O
ANISOU 1185 OG1 THR A 177 19682 19892 12726 405 -2832 532 O
ATOM 1186 CG2 THR A 177 39.100 16.289 -23.962 1.00133.59 C
ANISOU 1186 CG2 THR A 177 18910 19027 12820 688 -2777 741 C
ATOM 1187 N VAL A 178 35.140 15.860 -23.751 1.00139.18 N
ANISOU 1187 N VAL A 178 20333 19023 13528 210 -1879 725 N
ATOM 1188 CA VAL A 178 34.037 16.681 -24.244 1.00139.38 C
ANISOU 1188 CA VAL A 178 20283 18907 13769 -44 -1630 486 C
ATOM 1189 C VAL A 178 32.985 16.779 -23.145 1.00144.57 C
ANISOU 1189 C VAL A 178 21207 19591 14133 -207 -1433 454 C
ATOM 1190 O VAL A 178 32.581 15.746 -22.590 1.00154.95 O
ANISOU 1190 O VAL A 178 22817 20816 15241 -153 -1325 690 O
ATOM 1191 CB VAL A 178 33.443 16.105 -25.539 1.00138.75 C
ANISOU 1191 CB VAL A 178 20161 18510 14049 -39 -1433 543 C
ATOM 1192 N PRO A 179 32.554 17.987 -22.769 1.00139.77 N
ANISOU 1192 N PRO A 179 20520 19098 13487 -402 -1374 172 N
ATOM 1193 CA PRO A 179 31.491 18.120 -21.763 1.00135.51 C
ANISOU 1193 CA PRO A 179 20218 18590 12680 -557 -1149 115 C
ATOM 1194 C PRO A 179 30.190 17.485 -22.235 1.00129.66 C
ANISOU 1194 C PRO A 179 19583 17578 12104 -645 -814 196 C
ATOM 1195 O PRO A 179 29.891 17.451 -23.432 1.00132.96 O
ANISOU 1195 O PRO A 179 19826 17799 12895 -656 -732 163 O
ATOM 1196 CB PRO A 179 31.345 19.637 -21.598 1.00134.08 C
ANISOU 1196 CB PRO A 179 19870 18533 12543 -726 -1144 -245 C
ATOM 1197 CG PRO A 179 32.662 20.190 -22.033 1.00135.35 C
ANISOU 1197 CG PRO A 179 19776 18824 12827 -653 -1454 -329 C
ATOM 1198 CD PRO A 179 33.120 19.293 -23.146 1.00136.43 C
ANISOU 1198 CD PRO A 179 19806 18797 13236 -482 -1515 -108 C
ATOM 1199 N LEU A 180 29.428 16.959 -21.268 1.00122.46 N
ANISOU 1199 N LEU A 180 18961 16677 10892 -720 -619 303 N
ATOM 1200 CA LEU A 180 28.224 16.189 -21.579 1.00113.01 C
ANISOU 1200 CA LEU A 180 17885 15242 9811 -826 -297 407 C
ATOM 1201 C LEU A 180 27.163 17.031 -22.278 1.00103.70 C
ANISOU 1201 C LEU A 180 16478 13982 8941 -997 -76 139 C
ATOM 1202 O LEU A 180 26.402 16.510 -23.101 1.00101.10 O
ANISOU 1202 O LEU A 180 16098 13447 8870 -1059 107 183 O
ATOM 1203 CB LEU A 180 27.652 15.577 -20.300 1.00113.76 C
ANISOU 1203 CB LEU A 180 18333 15398 9492 -897 -118 563 C
ATOM 1204 N ASP A 181 27.098 18.324 -21.974 1.00 98.97 N
ANISOU 1204 N ASP A 181 15741 13539 8322 -1068 -95 -141 N
ATOM 1205 CA ASP A 181 26.085 19.187 -22.562 1.00 97.53 C
ANISOU 1205 CA ASP A 181 15353 13286 8419 -1190 111 -387 C
ATOM 1206 C ASP A 181 26.550 19.861 -23.847 1.00 91.54 C
ANISOU 1206 C ASP A 181 14292 12438 8051 -1127 -37 -505 C
ATOM 1207 O ASP A 181 25.728 20.465 -24.542 1.00 88.85 O
ANISOU 1207 O ASP A 181 13770 12010 7980 -1190 116 -663 O
ATOM 1208 CB ASP A 181 25.639 20.253 -21.552 1.00100.98 C
ANISOU 1208 CB ASP A 181 15829 13897 8641 -1294 221 -640 C
ATOM 1209 CG ASP A 181 26.753 21.214 -21.187 1.00104.23 C
ANISOU 1209 CG ASP A 181 16184 14473 8946 -1246 -54 -804 C
ATOM 1210 OD1 ASP A 181 27.867 20.744 -20.875 1.00106.22 O
ANISOU 1210 OD1 ASP A 181 16517 14830 9010 -1144 -316 -649 O
ATOM 1211 OD2 ASP A 181 26.517 22.440 -21.222 1.00104.52 O
ANISOU 1211 OD2 ASP A 181 16089 14529 9094 -1309 -8 -1091 O
ATOM 1212 N GLU A 182 27.829 19.765 -24.190 1.00 93.16 N
ANISOU 1212 N GLU A 182 14434 12674 8289 -997 -323 -423 N
ATOM 1213 CA GLU A 182 28.346 20.398 -25.391 1.00 97.78 C
ANISOU 1213 CA GLU A 182 14745 13188 9220 -947 -452 -520 C
ATOM 1214 C GLU A 182 28.732 19.357 -26.432 1.00 90.08 C
ANISOU 1214 C GLU A 182 13725 12063 8440 -831 -518 -307 C
ATOM 1215 O GLU A 182 28.919 18.175 -26.132 1.00 90.17 O
ANISOU 1215 O GLU A 182 13925 12033 8302 -756 -530 -78 O
ATOM 1216 CB GLU A 182 29.560 21.277 -25.073 1.00108.86 C
ANISOU 1216 CB GLU A 182 16053 14760 10546 -915 -716 -645 C
ATOM 1217 CG GLU A 182 29.221 22.568 -24.358 1.00117.94 C
ANISOU 1217 CG GLU A 182 17200 16009 11603 -1044 -651 -931 C
ATOM 1218 CD GLU A 182 30.428 23.465 -24.188 1.00126.18 C
ANISOU 1218 CD GLU A 182 18128 17196 12619 -1054 -908 -1082 C
ATOM 1219 OE1 GLU A 182 31.506 23.115 -24.713 1.00128.79 O
ANISOU 1219 OE1 GLU A 182 18338 17563 13032 -956 -1131 -961 O
ATOM 1220 OE2 GLU A 182 30.299 24.518 -23.529 1.00134.41 O
ANISOU 1220 OE2 GLU A 182 19194 18315 13561 -1167 -879 -1334 O
ATOM 1221 N CYS A 183 28.843 19.825 -27.674 1.00 80.92 N
ANISOU 1221 N CYS A 183 12327 10808 7612 -810 -550 -387 N
ATOM 1222 CA CYS A 183 29.166 18.986 -28.826 1.00 75.77 C
ANISOU 1222 CA CYS A 183 11603 10013 7173 -709 -595 -237 C
ATOM 1223 C CYS A 183 30.258 19.693 -29.625 1.00 74.44 C
ANISOU 1223 C CYS A 183 11200 9892 7191 -631 -798 -306 C
ATOM 1224 O CYS A 183 29.964 20.519 -30.493 1.00 74.52 O
ANISOU 1224 O CYS A 183 11026 9845 7442 -679 -750 -440 O
ATOM 1225 CB CYS A 183 27.930 18.722 -29.673 1.00 73.26 C
ANISOU 1225 CB CYS A 183 11234 9531 7071 -794 -370 -262 C
ATOM 1226 SG CYS A 183 28.267 17.710 -31.116 1.00 71.66 S
ANISOU 1226 SG CYS A 183 10963 9154 7111 -691 -412 -120 S
ATOM 1227 N GLN A 184 31.516 19.382 -29.324 1.00 76.01 N
ANISOU 1227 N GLN A 184 11402 10207 7273 -507 -1020 -206 N
ATOM 1228 CA GLN A 184 32.644 19.975 -30.025 1.00 77.49 C
ANISOU 1228 CA GLN A 184 11351 10468 7623 -447 -1206 -263 C
ATOM 1229 C GLN A 184 33.690 18.901 -30.281 1.00 79.75 C
ANISOU 1229 C GLN A 184 11636 10777 7888 -245 -1363 -57 C
ATOM 1230 O GLN A 184 33.702 17.851 -29.634 1.00 80.02 O
ANISOU 1230 O GLN A 184 11881 10799 7725 -145 -1373 123 O
ATOM 1231 CB GLN A 184 33.250 21.145 -29.235 1.00 88.34 C
ANISOU 1231 CB GLN A 184 12650 12040 8877 -534 -1344 -442 C
ATOM 1232 CG GLN A 184 34.331 20.751 -28.235 1.00101.73 C
ANISOU 1232 CG GLN A 184 14401 13962 10289 -440 -1578 -355 C
ATOM 1233 CD GLN A 184 33.783 20.050 -27.001 1.00111.85 C
ANISOU 1233 CD GLN A 184 15976 15289 11230 -428 -1522 -248 C
ATOM 1234 OE1 GLN A 184 32.583 20.087 -26.728 1.00116.49 O
ANISOU 1234 OE1 GLN A 184 16711 15770 11780 -539 -1295 -293 O
ATOM 1235 NE2 GLN A 184 34.668 19.409 -26.247 1.00113.89 N
ANISOU 1235 NE2 GLN A 184 16316 15725 11233 -288 -1725 -96 N
ATOM 1236 N ILE A 185 34.562 19.166 -31.254 1.00 79.67 N
ANISOU 1236 N ILE A 185 11392 10790 8087 -177 -1471 -78 N
ATOM 1237 CA ILE A 185 35.637 18.238 -31.582 1.00 80.92 C
ANISOU 1237 CA ILE A 185 11503 10988 8256 40 -1616 92 C
ATOM 1238 C ILE A 185 36.754 18.411 -30.563 1.00 91.18 C
ANISOU 1238 C ILE A 185 12753 12559 9331 115 -1863 109 C
ATOM 1239 O ILE A 185 37.058 19.529 -30.125 1.00 92.95 O
ANISOU 1239 O ILE A 185 12853 12952 9513 -25 -1954 -69 O
ATOM 1240 CB ILE A 185 36.119 18.464 -33.027 1.00 77.96 C
ANISOU 1240 CB ILE A 185 10885 10558 8178 79 -1612 53 C
ATOM 1241 CG1 ILE A 185 34.990 18.146 -34.000 1.00 73.51 C
ANISOU 1241 CG1 ILE A 185 10388 9752 7789 22 -1391 50 C
ATOM 1242 CG2 ILE A 185 37.327 17.597 -33.377 1.00 75.79 C
ANISOU 1242 CG2 ILE A 185 10520 10350 7925 321 -1755 202 C
ATOM 1243 CD1 ILE A 185 35.351 18.440 -35.411 1.00 67.14 C
ANISOU 1243 CD1 ILE A 185 9370 8906 7236 44 -1372 5 C
ATOM 1244 N GLN A 186 37.356 17.284 -30.180 1.00 98.49 N
ANISOU 1244 N GLN A 186 13784 13524 10112 340 -1975 321 N
ATOM 1245 CA GLN A 186 38.280 17.230 -29.054 1.00107.35 C
ANISOU 1245 CA GLN A 186 14907 14925 10957 446 -2221 381 C
ATOM 1246 C GLN A 186 39.545 18.042 -29.326 1.00105.89 C
ANISOU 1246 C GLN A 186 14365 15000 10868 447 -2439 252 C
ATOM 1247 O GLN A 186 39.866 18.982 -28.588 1.00102.19 O
ANISOU 1247 O GLN A 186 13806 14757 10263 300 -2570 89 O
ATOM 1248 CB GLN A 186 38.615 15.765 -28.743 1.00117.16 C
ANISOU 1248 CB GLN A 186 16349 16111 12056 733 -2277 671 C
ATOM 1249 CG GLN A 186 37.425 14.862 -28.338 1.00124.76 C
ANISOU 1249 CG GLN A 186 17697 16812 12893 711 -2055 822 C
ATOM 1250 CD GLN A 186 36.536 14.446 -29.510 1.00126.29 C
ANISOU 1250 CD GLN A 186 17937 16675 13372 644 -1798 810 C
ATOM 1251 OE1 GLN A 186 36.902 14.611 -30.676 1.00122.29 O
ANISOU 1251 OE1 GLN A 186 17207 16120 13139 677 -1794 738 O
ATOM 1252 NE2 GLN A 186 35.362 13.909 -29.199 1.00130.22 N
ANISOU 1252 NE2 GLN A 186 18718 16966 13794 534 -1578 874 N
ATOM 1253 N PHE A 187 40.281 17.692 -30.384 1.00105.89 N
ANISOU 1253 N PHE A 187 14157 14977 11101 598 -2469 310 N
ATOM 1254 CA PHE A 187 41.606 18.264 -30.604 1.00106.48 C
ANISOU 1254 CA PHE A 187 13874 15330 11255 626 -2679 224 C
ATOM 1255 C PHE A 187 41.564 19.697 -31.126 1.00106.81 C
ANISOU 1255 C PHE A 187 13702 15392 11489 336 -2621 -32 C
ATOM 1256 O PHE A 187 42.577 20.400 -31.042 1.00108.43 O
ANISOU 1256 O PHE A 187 13628 15852 11720 267 -2792 -150 O
ATOM 1257 CB PHE A 187 42.418 17.388 -31.566 1.00101.90 C
ANISOU 1257 CB PHE A 187 13137 14725 10857 898 -2703 370 C
ATOM 1258 CG PHE A 187 41.699 17.038 -32.842 1.00 96.65 C
ANISOU 1258 CG PHE A 187 12540 13737 10445 892 -2448 387 C
ATOM 1259 CD1 PHE A 187 41.822 17.841 -33.965 1.00 95.30 C
ANISOU 1259 CD1 PHE A 187 12135 13541 10534 749 -2357 242 C
ATOM 1260 CD2 PHE A 187 40.931 15.885 -32.930 1.00 93.22 C
ANISOU 1260 CD2 PHE A 187 12410 13030 9979 1022 -2303 551 C
ATOM 1261 CE1 PHE A 187 41.172 17.516 -35.144 1.00 91.05 C
ANISOU 1261 CE1 PHE A 187 11659 12741 10195 750 -2143 256 C
ATOM 1262 CE2 PHE A 187 40.280 15.557 -34.103 1.00 89.78 C
ANISOU 1262 CE2 PHE A 187 12027 12324 9761 998 -2087 541 C
ATOM 1263 CZ PHE A 187 40.401 16.372 -35.212 1.00 88.34 C
ANISOU 1263 CZ PHE A 187 11603 12151 9812 871 -2017 393 C
ATOM 1264 N LEU A 188 40.425 20.151 -31.650 1.00100.58 N
ANISOU 1264 N LEU A 188 13034 14345 10837 164 -2386 -119 N
ATOM 1265 CA LEU A 188 40.313 21.492 -32.212 1.00 91.84 C
ANISOU 1265 CA LEU A 188 11765 13204 9927 -83 -2308 -332 C
ATOM 1266 C LEU A 188 40.106 22.574 -31.154 1.00 99.12 C
ANISOU 1266 C LEU A 188 12737 14232 10692 -311 -2361 -534 C
ATOM 1267 O LEU A 188 39.856 23.730 -31.513 1.00101.20 O
ANISOU 1267 O LEU A 188 12928 14413 11112 -522 -2268 -717 O
ATOM 1268 CB LEU A 188 39.182 21.541 -33.244 1.00 76.81 C
ANISOU 1268 CB LEU A 188 9959 10995 8231 -138 -2050 -332 C
ATOM 1269 CG LEU A 188 39.420 20.725 -34.517 1.00 71.09 C
ANISOU 1269 CG LEU A 188 9153 10162 7698 32 -1980 -198 C
ATOM 1270 CD1 LEU A 188 38.278 20.917 -35.507 1.00 67.27 C
ANISOU 1270 CD1 LEU A 188 8748 9422 7390 -52 -1751 -227 C
ATOM 1271 CD2 LEU A 188 40.752 21.102 -35.158 1.00 63.04 C
ANISOU 1271 CD2 LEU A 188 7811 9322 6821 59 -2093 -229 C
ATOM 1272 N SER A 189 40.191 22.235 -29.867 1.00106.55 N
ANISOU 1272 N SER A 189 13820 15344 11319 -268 -2498 -507 N
ATOM 1273 CA SER A 189 40.126 23.262 -28.834 1.00114.83 C
ANISOU 1273 CA SER A 189 14909 16530 12190 -486 -2565 -728 C
ATOM 1274 C SER A 189 41.440 24.021 -28.711 1.00119.67 C
ANISOU 1274 C SER A 189 15223 17423 12825 -593 -2792 -880 C
ATOM 1275 O SER A 189 41.431 25.213 -28.382 1.00122.15 O
ANISOU 1275 O SER A 189 15498 17764 13148 -847 -2791 -1130 O
ATOM 1276 CB SER A 189 39.747 22.639 -27.489 1.00119.11 C
ANISOU 1276 CB SER A 189 15722 17183 12350 -413 -2628 -647 C
ATOM 1277 OG SER A 189 38.494 21.984 -27.566 1.00120.85 O
ANISOU 1277 OG SER A 189 16212 17148 12559 -361 -2393 -524 O
ATOM 1278 N GLU A 190 42.562 23.357 -28.963 1.00120.47 N
ANISOU 1278 N GLU A 190 15105 17729 12941 -407 -2978 -744 N
ATOM 1279 CA GLU A 190 43.857 24.024 -28.910 1.00124.41 C
ANISOU 1279 CA GLU A 190 15263 18527 13479 -516 -3194 -889 C
ATOM 1280 C GLU A 190 43.982 24.999 -30.077 1.00121.08 C
ANISOU 1280 C GLU A 190 14640 17948 13415 -720 -3042 -1028 C
ATOM 1281 O GLU A 190 43.650 24.640 -31.214 1.00119.28 O
ANISOU 1281 O GLU A 190 14409 17494 13418 -620 -2862 -904 O
ATOM 1282 CB GLU A 190 44.991 23.001 -28.949 1.00129.03 C
ANISOU 1282 CB GLU A 190 15639 19380 14008 -224 -3415 -692 C
ATOM 1283 CG GLU A 190 46.378 23.619 -29.038 1.00134.18 C
ANISOU 1283 CG GLU A 190 15868 20374 14740 -329 -3629 -835 C
ATOM 1284 CD GLU A 190 47.484 22.586 -28.982 1.00140.22 C
ANISOU 1284 CD GLU A 190 16439 21361 15476 -7 -3816 -621 C
ATOM 1285 OE1 GLU A 190 47.178 21.400 -28.740 1.00141.90 O
ANISOU 1285 OE1 GLU A 190 16855 21532 15530 306 -3840 -380 O
ATOM 1286 OE2 GLU A 190 48.660 22.960 -29.182 1.00143.75 O
ANISOU 1286 OE2 GLU A 190 16548 21991 16079 -67 -3915 -687 O
ATOM 1287 N PRO A 191 44.428 26.237 -29.836 1.00119.86 N
ANISOU 1287 N PRO A 191 14340 17896 13306 -1017 -3098 -1286 N
ATOM 1288 CA PRO A 191 44.531 27.208 -30.938 1.00116.40 C
ANISOU 1288 CA PRO A 191 13747 17274 13205 -1225 -2931 -1398 C
ATOM 1289 C PRO A 191 45.562 26.850 -31.997 1.00112.23 C
ANISOU 1289 C PRO A 191 12886 16863 12892 -1123 -2962 -1284 C
ATOM 1290 O PRO A 191 45.350 27.182 -33.169 1.00114.35 O
ANISOU 1290 O PRO A 191 13114 16907 13428 -1174 -2758 -1255 O
ATOM 1291 CB PRO A 191 44.896 28.516 -30.220 1.00120.74 C
ANISOU 1291 CB PRO A 191 14235 17931 13710 -1570 -3015 -1707 C
ATOM 1292 CG PRO A 191 44.421 28.322 -28.814 1.00122.62 C
ANISOU 1292 CG PRO A 191 14717 18286 13588 -1551 -3129 -1772 C
ATOM 1293 CD PRO A 191 44.636 26.868 -28.522 1.00122.03 C
ANISOU 1293 CD PRO A 191 14659 18396 13313 -1204 -3274 -1500 C
ATOM 1294 N THR A 192 46.667 26.190 -31.635 1.00107.94 N
ANISOU 1294 N THR A 192 12100 16677 12234 -966 -3206 -1214 N
ATOM 1295 CA THR A 192 47.692 25.881 -32.632 1.00103.71 C
ANISOU 1295 CA THR A 192 11216 16280 11910 -864 -3219 -1125 C
ATOM 1296 C THR A 192 47.235 24.774 -33.577 1.00 97.99 C
ANISOU 1296 C THR A 192 10604 15341 11287 -551 -3057 -875 C
ATOM 1297 O THR A 192 47.481 24.846 -34.788 1.00 96.56 O
ANISOU 1297 O THR A 192 10270 15067 11352 -549 -2903 -835 O
ATOM 1298 CB THR A 192 49.000 25.485 -31.949 1.00108.00 C
ANISOU 1298 CB THR A 192 11481 17222 12334 -749 -3497 -1105 C
ATOM 1299 OG1 THR A 192 48.827 24.229 -31.284 1.00110.91 O
ANISOU 1299 OG1 THR A 192 12017 17665 12457 -398 -3628 -897 O
ATOM 1300 CG2 THR A 192 49.414 26.541 -30.932 1.00111.12 C
ANISOU 1300 CG2 THR A 192 11864 17703 12654 -1047 -3603 -1326 C
ATOM 1301 N ILE A 193 46.574 23.744 -33.043 1.00 93.64 N
ANISOU 1301 N ILE A 193 10331 14708 10541 -301 -3080 -713 N
ATOM 1302 CA ILE A 193 46.036 22.677 -33.883 1.00 88.29 C
ANISOU 1302 CA ILE A 193 9806 13790 9952 -36 -2915 -502 C
ATOM 1303 C ILE A 193 44.940 23.220 -34.794 1.00 83.23 C
ANISOU 1303 C ILE A 193 9338 12789 9498 -196 -2633 -545 C
ATOM 1304 O ILE A 193 44.863 22.868 -35.978 1.00 83.49 O
ANISOU 1304 O ILE A 193 9331 12675 9716 -100 -2477 -457 O
ATOM 1305 CB ILE A 193 45.529 21.517 -33.008 1.00 91.80 C
ANISOU 1305 CB ILE A 193 10540 14200 10137 219 -2988 -326 C
ATOM 1306 CG1 ILE A 193 46.624 21.063 -32.043 1.00100.39 C
ANISOU 1306 CG1 ILE A 193 11461 15672 11011 393 -3294 -272 C
ATOM 1307 CG2 ILE A 193 45.087 20.347 -33.869 1.00 89.96 C
ANISOU 1307 CG2 ILE A 193 10456 13719 10005 482 -2826 -125 C
ATOM 1308 CD1 ILE A 193 47.883 20.577 -32.728 1.00105.35 C
ANISOU 1308 CD1 ILE A 193 11726 16517 11786 611 -3389 -193 C
ATOM 1309 N THR A 194 44.088 24.098 -34.258 1.00 80.39 N
ANISOU 1309 N THR A 194 9167 12295 9083 -430 -2568 -686 N
ATOM 1310 CA THR A 194 43.029 24.708 -35.056 1.00 75.73 C
ANISOU 1310 CA THR A 194 8726 11384 8666 -565 -2319 -729 C
ATOM 1311 C THR A 194 43.609 25.597 -36.150 1.00 73.53 C
ANISOU 1311 C THR A 194 8208 11084 8645 -726 -2229 -801 C
ATOM 1312 O THR A 194 43.090 25.635 -37.273 1.00 70.19 O
ANISOU 1312 O THR A 194 7829 10449 8391 -707 -2038 -737 O
ATOM 1313 CB THR A 194 42.102 25.510 -34.143 1.00 66.13 C
ANISOU 1313 CB THR A 194 7736 10059 7332 -759 -2278 -882 C
ATOM 1314 OG1 THR A 194 41.897 24.784 -32.927 1.00 67.94 O
ANISOU 1314 OG1 THR A 194 8136 10404 7272 -644 -2404 -832 O
ATOM 1315 CG2 THR A 194 40.764 25.756 -34.805 1.00 56.88 C
ANISOU 1315 CG2 THR A 194 6767 8560 6285 -791 -2032 -870 C
ATOM 1316 N PHE A 195 44.705 26.295 -35.841 1.00 76.13 N
ANISOU 1316 N PHE A 195 8281 11649 8997 -892 -2365 -931 N
ATOM 1317 CA PHE A 195 45.373 27.142 -36.822 1.00 77.61 C
ANISOU 1317 CA PHE A 195 8229 11836 9425 -1075 -2270 -994 C
ATOM 1318 C PHE A 195 45.999 26.306 -37.931 1.00 77.69 C
ANISOU 1318 C PHE A 195 8044 11920 9553 -861 -2220 -830 C
ATOM 1319 O PHE A 195 45.885 26.652 -39.113 1.00 75.31 O
ANISOU 1319 O PHE A 195 7710 11466 9439 -915 -2029 -793 O
ATOM 1320 CB PHE A 195 46.425 28.001 -36.118 1.00 81.71 C
ANISOU 1320 CB PHE A 195 8505 12616 9924 -1327 -2438 -1189 C
ATOM 1321 CG PHE A 195 47.177 28.926 -37.029 1.00 86.02 C
ANISOU 1321 CG PHE A 195 8800 13168 10716 -1565 -2331 -1264 C
ATOM 1322 CD1 PHE A 195 46.629 30.145 -37.397 1.00 86.06 C
ANISOU 1322 CD1 PHE A 195 8943 12884 10870 -1835 -2146 -1371 C
ATOM 1323 CD2 PHE A 195 48.451 28.608 -37.471 1.00 92.08 C
ANISOU 1323 CD2 PHE A 195 9192 14230 11563 -1523 -2408 -1228 C
ATOM 1324 CE1 PHE A 195 47.320 31.013 -38.221 1.00 89.38 C
ANISOU 1324 CE1 PHE A 195 9165 13285 11511 -2073 -2028 -1421 C
ATOM 1325 CE2 PHE A 195 49.149 29.473 -38.294 1.00 95.35 C
ANISOU 1325 CE2 PHE A 195 9373 14657 12198 -1773 -2285 -1294 C
ATOM 1326 CZ PHE A 195 48.582 30.678 -38.669 1.00 94.34 C
ANISOU 1326 CZ PHE A 195 9416 14216 12211 -2059 -2092 -1384 C
ATOM 1327 N GLY A 196 46.679 25.216 -37.561 1.00 77.80 N
ANISOU 1327 N GLY A 196 7936 12172 9451 -605 -2386 -731 N
ATOM 1328 CA GLY A 196 47.211 24.299 -38.558 1.00 79.06 C
ANISOU 1328 CA GLY A 196 7944 12383 9711 -354 -2324 -582 C
ATOM 1329 C GLY A 196 46.127 23.713 -39.443 1.00 77.24 C
ANISOU 1329 C GLY A 196 7983 11834 9531 -216 -2115 -461 C
ATOM 1330 O GLY A 196 46.317 23.555 -40.653 1.00 73.57 O
ANISOU 1330 O GLY A 196 7426 11316 9213 -158 -1964 -403 O
ATOM 1331 N THR A 197 44.981 23.369 -38.846 1.00 74.34 N
ANISOU 1331 N THR A 197 7944 11272 9031 -170 -2101 -429 N
ATOM 1332 CA THR A 197 43.864 22.831 -39.617 1.00 67.47 C
ANISOU 1332 CA THR A 197 7319 10115 8200 -73 -1915 -338 C
ATOM 1333 C THR A 197 43.329 23.871 -40.595 1.00 67.36 C
ANISOU 1333 C THR A 197 7318 9923 8353 -280 -1727 -399 C
ATOM 1334 O THR A 197 43.002 23.544 -41.740 1.00 68.78 O
ANISOU 1334 O THR A 197 7531 9978 8624 -201 -1577 -326 O
ATOM 1335 CB THR A 197 42.765 22.345 -38.669 1.00 63.34 C
ANISOU 1335 CB THR A 197 7114 9451 7500 -26 -1934 -308 C
ATOM 1336 OG1 THR A 197 43.298 21.330 -37.810 1.00 63.71 O
ANISOU 1336 OG1 THR A 197 7176 9652 7381 190 -2103 -214 O
ATOM 1337 CG2 THR A 197 41.599 21.751 -39.444 1.00 59.40 C
ANISOU 1337 CG2 THR A 197 6841 8682 7046 49 -1749 -232 C
ATOM 1338 N ALA A 198 43.232 25.131 -40.158 1.00 67.67 N
ANISOU 1338 N ALA A 198 7347 9943 8421 -539 -1732 -532 N
ATOM 1339 CA ALA A 198 42.791 26.201 -41.051 1.00 66.25 C
ANISOU 1339 CA ALA A 198 7190 9578 8403 -723 -1557 -571 C
ATOM 1340 C ALA A 198 43.776 26.425 -42.195 1.00 68.87 C
ANISOU 1340 C ALA A 198 7270 10007 8889 -754 -1479 -533 C
ATOM 1341 O ALA A 198 43.366 26.659 -43.340 1.00 63.71 O
ANISOU 1341 O ALA A 198 6665 9204 8336 -761 -1309 -469 O
ATOM 1342 CB ALA A 198 42.588 27.493 -40.261 1.00 60.91 C
ANISOU 1342 CB ALA A 198 6569 8842 7734 -985 -1577 -733 C
ATOM 1343 N ILE A 199 45.077 26.383 -41.896 1.00 66.42 N
ANISOU 1343 N ILE A 199 6679 9969 8587 -776 -1602 -572 N
ATOM 1344 CA ILE A 199 46.096 26.546 -42.932 1.00 69.85 C
ANISOU 1344 CA ILE A 199 6839 10537 9164 -809 -1514 -541 C
ATOM 1345 C ILE A 199 45.997 25.419 -43.957 1.00 72.56 C
ANISOU 1345 C ILE A 199 7204 10856 9510 -533 -1413 -400 C
ATOM 1346 O ILE A 199 45.827 25.658 -45.158 1.00 74.43 O
ANISOU 1346 O ILE A 199 7452 10989 9838 -561 -1229 -345 O
ATOM 1347 CB ILE A 199 47.500 26.618 -42.306 1.00 74.18 C
ANISOU 1347 CB ILE A 199 7043 11430 9713 -870 -1685 -623 C
ATOM 1348 CG1 ILE A 199 47.663 27.905 -41.491 1.00 75.93 C
ANISOU 1348 CG1 ILE A 199 7231 11664 9954 -1213 -1754 -799 C
ATOM 1349 CG2 ILE A 199 48.572 26.535 -43.384 1.00 73.32 C
ANISOU 1349 CG2 ILE A 199 6620 11498 9741 -852 -1580 -578 C
ATOM 1350 CD1 ILE A 199 47.280 29.163 -42.237 1.00 76.40 C
ANISOU 1350 CD1 ILE A 199 7382 11471 10175 -1488 -1543 -836 C
ATOM 1351 N ALA A 200 46.077 24.172 -43.489 1.00 68.89 N
ANISOU 1351 N ALA A 200 6769 10473 8932 -262 -1527 -340 N
ATOM 1352 CA ALA A 200 46.112 23.032 -44.397 1.00 68.43 C
ANISOU 1352 CA ALA A 200 6728 10391 8880 7 -1435 -233 C
ATOM 1353 C ALA A 200 44.769 22.751 -45.063 1.00 65.70 C
ANISOU 1353 C ALA A 200 6693 9757 8514 46 -1289 -183 C
ATOM 1354 O ALA A 200 44.744 22.099 -46.110 1.00 67.67 O
ANISOU 1354 O ALA A 200 6959 9964 8788 191 -1166 -126 O
ATOM 1355 CB ALA A 200 46.582 21.783 -43.650 1.00 68.74 C
ANISOU 1355 CB ALA A 200 6743 10564 8813 297 -1595 -177 C
ATOM 1356 N ALA A 201 43.661 23.243 -44.505 1.00 62.02 N
ANISOU 1356 N ALA A 201 6457 9108 7999 -83 -1297 -216 N
ATOM 1357 CA ALA A 201 42.334 22.855 -44.961 1.00 56.60 C
ANISOU 1357 CA ALA A 201 6039 8187 7278 -31 -1192 -176 C
ATOM 1358 C ALA A 201 41.556 23.983 -45.621 1.00 56.21 C
ANISOU 1358 C ALA A 201 6067 7987 7305 -219 -1064 -197 C
ATOM 1359 O ALA A 201 40.587 23.704 -46.336 1.00 56.51 O
ANISOU 1359 O ALA A 201 6261 7880 7329 -168 -966 -159 O
ATOM 1360 CB ALA A 201 41.506 22.303 -43.790 1.00 56.39 C
ANISOU 1360 CB ALA A 201 6234 8071 7121 20 -1285 -180 C
ATOM 1361 N PHE A 202 41.942 25.237 -45.399 1.00 57.27 N
ANISOU 1361 N PHE A 202 6100 8145 7515 -431 -1066 -258 N
ATOM 1362 CA PHE A 202 41.204 26.348 -45.982 1.00 57.83 C
ANISOU 1362 CA PHE A 202 6270 8039 7664 -584 -942 -259 C
ATOM 1363 C PHE A 202 42.142 27.324 -46.682 1.00 65.48 C
ANISOU 1363 C PHE A 202 7056 9065 8756 -749 -855 -253 C
ATOM 1364 O PHE A 202 41.927 27.640 -47.854 1.00 69.23 O
ANISOU 1364 O PHE A 202 7560 9465 9279 -757 -710 -171 O
ATOM 1365 CB PHE A 202 40.371 27.077 -44.918 1.00 46.65 C
ANISOU 1365 CB PHE A 202 5012 6489 6225 -704 -987 -348 C
ATOM 1366 CG PHE A 202 39.720 28.347 -45.423 1.00 40.12 C
ANISOU 1366 CG PHE A 202 4278 5466 5499 -845 -863 -351 C
ATOM 1367 CD1 PHE A 202 38.561 28.294 -46.180 1.00 42.96 C
ANISOU 1367 CD1 PHE A 202 4788 5679 5856 -754 -768 -279 C
ATOM 1368 CD2 PHE A 202 40.262 29.590 -45.131 1.00 40.25 C
ANISOU 1368 CD2 PHE A 202 4236 5442 5613 -1063 -845 -428 C
ATOM 1369 CE1 PHE A 202 37.962 29.457 -46.648 1.00 45.00 C
ANISOU 1369 CE1 PHE A 202 5135 5758 6204 -839 -663 -258 C
ATOM 1370 CE2 PHE A 202 39.662 30.754 -45.596 1.00 44.98 C
ANISOU 1370 CE2 PHE A 202 4956 5821 6315 -1168 -719 -413 C
ATOM 1371 CZ PHE A 202 38.512 30.683 -46.354 1.00 42.74 C
ANISOU 1371 CZ PHE A 202 4821 5396 6024 -1034 -631 -316 C
ATOM 1372 N TYR A 203 43.193 27.785 -45.996 1.00 59.08 N
ANISOU 1372 N TYR A 203 6348 7175 8923 -267 612 -861 N
ATOM 1373 CA TYR A 203 44.013 28.864 -46.546 1.00 62.11 C
ANISOU 1373 CA TYR A 203 6712 7647 9240 -536 532 -824 C
ATOM 1374 C TYR A 203 44.849 28.393 -47.733 1.00 65.47 C
ANISOU 1374 C TYR A 203 6918 8313 9646 -523 527 -720 C
ATOM 1375 O TYR A 203 44.943 29.096 -48.750 1.00 62.76 O
ANISOU 1375 O TYR A 203 6626 7908 9314 -646 540 -676 O
ATOM 1376 CB TYR A 203 44.884 29.471 -45.446 1.00 54.26 C
ANISOU 1376 CB TYR A 203 5710 6818 8088 -771 453 -880 C
ATOM 1377 CG TYR A 203 44.081 30.358 -44.526 1.00 58.20 C
ANISOU 1377 CG TYR A 203 6457 7040 8616 -886 479 -1011 C
ATOM 1378 CD1 TYR A 203 43.749 31.652 -44.908 1.00 61.01 C
ANISOU 1378 CD1 TYR A 203 6977 7132 9074 -1088 509 -1061 C
ATOM 1379 CD2 TYR A 203 43.620 29.896 -43.297 1.00 60.08 C
ANISOU 1379 CD2 TYR A 203 6789 7253 8785 -784 501 -1083 C
ATOM 1380 CE1 TYR A 203 43.002 32.470 -44.087 1.00 63.80 C
ANISOU 1380 CE1 TYR A 203 7538 7210 9494 -1193 550 -1205 C
ATOM 1381 CE2 TYR A 203 42.866 30.708 -42.466 1.00 59.80 C
ANISOU 1381 CE2 TYR A 203 6973 6962 8786 -910 551 -1236 C
ATOM 1382 CZ TYR A 203 42.562 31.996 -42.868 1.00 66.16 C
ANISOU 1382 CZ TYR A 203 7896 7512 9728 -1116 571 -1310 C
ATOM 1383 OH TYR A 203 41.817 32.819 -42.053 1.00 66.76 O
ANISOU 1383 OH TYR A 203 8171 7317 9879 -1245 636 -1485 O
ATOM 1384 N ILE A 204 45.450 27.212 -47.634 1.00 65.81 N
ANISOU 1384 N ILE A 204 6734 8614 9656 -368 528 -675 N
ATOM 1385 CA ILE A 204 46.221 26.659 -48.746 1.00 70.52 C
ANISOU 1385 CA ILE A 204 7092 9441 10262 -350 550 -610 C
ATOM 1386 C ILE A 204 45.277 26.269 -49.888 1.00 70.13 C
ANISOU 1386 C ILE A 204 7078 9234 10335 -179 639 -611 C
ATOM 1387 O ILE A 204 45.594 26.604 -51.042 1.00 73.53 O
ANISOU 1387 O ILE A 204 7475 9728 10734 -278 655 -571 O
ATOM 1388 CB ILE A 204 47.124 25.495 -48.287 1.00 69.37 C
ANISOU 1388 CB ILE A 204 6678 9597 10081 -203 524 -575 C
ATOM 1389 CG1 ILE A 204 48.239 26.017 -47.379 1.00 71.46 C
ANISOU 1389 CG1 ILE A 204 6851 10107 10193 -389 383 -610 C
ATOM 1390 CG2 ILE A 204 47.717 24.751 -49.476 1.00 65.64 C
ANISOU 1390 CG2 ILE A 204 5945 9317 9676 -146 589 -543 C
ATOM 1391 CD1 ILE A 204 49.095 24.924 -46.767 1.00 73.61 C
ANISOU 1391 CD1 ILE A 204 6878 10681 10408 -185 303 -570 C
ATOM 1392 N PRO A 205 44.132 25.576 -49.662 1.00 69.89 N
ANISOU 1392 N PRO A 205 7108 9012 10434 67 713 -681 N
ATOM 1393 CA PRO A 205 43.201 25.373 -50.792 1.00 71.16 C
ANISOU 1393 CA PRO A 205 7277 9052 10708 211 767 -747 C
ATOM 1394 C PRO A 205 42.718 26.659 -51.446 1.00 69.04 C
ANISOU 1394 C PRO A 205 7226 8607 10398 100 686 -736 C
ATOM 1395 O PRO A 205 42.633 26.706 -52.679 1.00 69.83 O
ANISOU 1395 O PRO A 205 7305 8764 10463 138 677 -712 O
ATOM 1396 CB PRO A 205 42.040 24.591 -50.159 1.00 68.46 C
ANISOU 1396 CB PRO A 205 6972 8501 10540 442 880 -887 C
ATOM 1397 CG PRO A 205 42.661 23.845 -49.062 1.00 65.35 C
ANISOU 1397 CG PRO A 205 6516 8209 10105 483 933 -825 C
ATOM 1398 CD PRO A 205 43.692 24.767 -48.498 1.00 70.59 C
ANISOU 1398 CD PRO A 205 7227 9019 10575 243 782 -722 C
ATOM 1399 N VAL A 206 42.427 27.707 -50.664 1.00 64.43 N
ANISOU 1399 N VAL A 206 6864 7810 9805 -31 634 -747 N
ATOM 1400 CA VAL A 206 41.927 28.953 -51.244 1.00 66.18 C
ANISOU 1400 CA VAL A 206 7322 7807 10016 -104 571 -718 C
ATOM 1401 C VAL A 206 43.015 29.632 -52.068 1.00 70.19 C
ANISOU 1401 C VAL A 206 7856 8453 10360 -335 569 -560 C
ATOM 1402 O VAL A 206 42.750 30.137 -53.167 1.00 73.06 O
ANISOU 1402 O VAL A 206 8358 8739 10663 -302 551 -479 O
ATOM 1403 CB VAL A 206 41.369 29.880 -50.143 1.00 64.47 C
ANISOU 1403 CB VAL A 206 7320 7305 9871 -200 552 -795 C
ATOM 1404 CG1 VAL A 206 41.297 31.321 -50.612 1.00 59.96 C
ANISOU 1404 CG1 VAL A 206 6997 6510 9273 -349 511 -716 C
ATOM 1405 CG2 VAL A 206 39.979 29.427 -49.724 1.00 59.83 C
ANISOU 1405 CG2 VAL A 206 6762 6497 9476 40 582 -981 C
ATOM 1406 N SER A 207 44.257 29.623 -51.568 1.00 70.35 N
ANISOU 1406 N SER A 207 7743 8691 10297 -560 596 -528 N
ATOM 1407 CA SER A 207 45.383 30.147 -52.341 1.00 69.75 C
ANISOU 1407 CA SER A 207 7641 8765 10095 -813 650 -431 C
ATOM 1408 C SER A 207 45.567 29.398 -53.660 1.00 71.66 C
ANISOU 1408 C SER A 207 7752 9197 10280 -699 697 -373 C
ATOM 1409 O SER A 207 45.763 30.024 -54.712 1.00 73.02 O
ANISOU 1409 O SER A 207 8073 9333 10337 -806 751 -270 O
ATOM 1410 CB SER A 207 46.663 30.085 -51.510 1.00 68.30 C
ANISOU 1410 CB SER A 207 7247 8836 9870 -1040 655 -486 C
ATOM 1411 OG SER A 207 46.514 30.817 -50.308 1.00 75.25 O
ANISOU 1411 OG SER A 207 8247 9573 10770 -1166 612 -568 O
ATOM 1412 N VAL A 208 45.493 28.060 -53.623 1.00 69.96 N
ANISOU 1412 N VAL A 208 7277 9169 10135 -483 701 -441 N
ATOM 1413 CA VAL A 208 45.681 27.260 -54.836 1.00 68.76 C
ANISOU 1413 CA VAL A 208 6958 9219 9948 -386 765 -434 C
ATOM 1414 C VAL A 208 44.580 27.557 -55.850 1.00 69.99 C
ANISOU 1414 C VAL A 208 7319 9218 10058 -217 729 -422 C
ATOM 1415 O VAL A 208 44.851 27.775 -57.041 1.00 74.54 O
ANISOU 1415 O VAL A 208 7954 9889 10478 -273 768 -346 O
ATOM 1416 CB VAL A 208 45.742 25.758 -54.491 1.00 65.34 C
ANISOU 1416 CB VAL A 208 6213 8963 9650 -177 807 -530 C
ATOM 1417 CG1 VAL A 208 45.690 24.905 -55.758 1.00 60.19 C
ANISOU 1417 CG1 VAL A 208 5387 8481 8999 -55 892 -578 C
ATOM 1418 CG2 VAL A 208 47.010 25.447 -53.715 1.00 68.36 C
ANISOU 1418 CG2 VAL A 208 6374 9567 10032 -307 810 -518 C
ATOM 1419 N MET A 209 43.323 27.576 -55.389 1.00 61.99 N
ANISOU 1419 N MET A 209 6413 7972 9168 -2 653 -514 N
ATOM 1420 CA MET A 209 42.202 27.850 -56.286 1.00 64.61 C
ANISOU 1420 CA MET A 209 6901 8175 9473 210 570 -547 C
ATOM 1421 C MET A 209 42.277 29.258 -56.867 1.00 73.28 C
ANISOU 1421 C MET A 209 8346 9105 10393 84 518 -361 C
ATOM 1422 O MET A 209 41.956 29.464 -58.042 1.00 78.22 O
ANISOU 1422 O MET A 209 9098 9763 10859 201 469 -296 O
ATOM 1423 CB MET A 209 40.874 27.630 -55.563 1.00 64.13 C
ANISOU 1423 CB MET A 209 6850 7889 9628 444 514 -735 C
ATOM 1424 CG MET A 209 40.650 26.191 -55.141 1.00 70.94 C
ANISOU 1424 CG MET A 209 7416 8865 10672 595 624 -921 C
ATOM 1425 SD MET A 209 39.091 25.905 -54.286 1.00 77.96 S
ANISOU 1425 SD MET A 209 8319 9463 11838 824 640 -1191 S
ATOM 1426 CE MET A 209 39.348 26.764 -52.746 1.00 75.34 C
ANISOU 1426 CE MET A 209 8200 8907 11518 618 637 -1100 C
ATOM 1427 N THR A 210 42.697 30.240 -56.061 1.00 70.28 N
ANISOU 1427 N THR A 210 8138 8539 10028 -149 540 -278 N
ATOM 1428 CA THR A 210 42.807 31.610 -56.552 1.00 71.70 C
ANISOU 1428 CA THR A 210 8674 8495 10074 -289 549 -95 C
ATOM 1429 C THR A 210 43.896 31.734 -57.616 1.00 76.17 C
ANISOU 1429 C THR A 210 9275 9255 10412 -495 682 60 C
ATOM 1430 O THR A 210 43.692 32.400 -58.639 1.00 78.20 O
ANISOU 1430 O THR A 210 9827 9404 10482 -451 685 225 O
ATOM 1431 CB THR A 210 43.062 32.561 -55.377 1.00 66.20 C
ANISOU 1431 CB THR A 210 8107 7562 9485 -530 589 -100 C
ATOM 1432 OG1 THR A 210 41.894 32.617 -54.551 1.00 67.84 O
ANISOU 1432 OG1 THR A 210 8356 7537 9884 -332 484 -239 O
ATOM 1433 CG2 THR A 210 43.375 33.968 -55.861 1.00 65.40 C
ANISOU 1433 CG2 THR A 210 8368 7205 9274 -732 676 89 C
ATOM 1434 N ILE A 211 45.047 31.083 -57.408 1.00 74.82 N
ANISOU 1434 N ILE A 211 8812 9370 10246 -705 796 5 N
ATOM 1435 CA ILE A 211 46.117 31.121 -58.409 1.00 76.49 C
ANISOU 1435 CA ILE A 211 9010 9779 10271 -927 960 98 C
ATOM 1436 C ILE A 211 45.665 30.452 -59.708 1.00 76.04 C
ANISOU 1436 C ILE A 211 8943 9892 10055 -694 933 120 C
ATOM 1437 O ILE A 211 45.869 30.987 -60.813 1.00 76.26 O
ANISOU 1437 O ILE A 211 9227 9911 9839 -765 1019 276 O
ATOM 1438 CB ILE A 211 47.396 30.473 -57.849 1.00 78.40 C
ANISOU 1438 CB ILE A 211 8871 10313 10602 -1159 1060 -23 C
ATOM 1439 CG1 ILE A 211 47.979 31.337 -56.729 1.00 85.29 C
ANISOU 1439 CG1 ILE A 211 9779 11060 11566 -1438 1092 -61 C
ATOM 1440 CG2 ILE A 211 48.429 30.259 -58.954 1.00 76.06 C
ANISOU 1440 CG2 ILE A 211 8482 10261 10157 -1359 1246 7 C
ATOM 1441 CD1 ILE A 211 49.296 30.826 -56.178 1.00 91.73 C
ANISOU 1441 CD1 ILE A 211 10211 12192 12452 -1655 1152 -204 C
ATOM 1442 N LEU A 212 45.028 29.278 -59.591 1.00 69.78 N
ANISOU 1442 N LEU A 212 7872 9252 9388 -416 834 -49 N
ATOM 1443 CA LEU A 212 44.544 28.573 -60.776 1.00 68.16 C
ANISOU 1443 CA LEU A 212 7603 9241 9053 -193 805 -100 C
ATOM 1444 C LEU A 212 43.491 29.387 -61.518 1.00 70.44 C
ANISOU 1444 C LEU A 212 8264 9339 9160 28 657 8 C
ATOM 1445 O LEU A 212 43.514 29.465 -62.754 1.00 80.89 O
ANISOU 1445 O LEU A 212 9733 10798 10206 78 669 95 O
ATOM 1446 CB LEU A 212 43.996 27.198 -60.393 1.00 61.17 C
ANISOU 1446 CB LEU A 212 6343 8502 8396 48 766 -345 C
ATOM 1447 CG LEU A 212 45.049 26.187 -59.932 1.00 59.40 C
ANISOU 1447 CG LEU A 212 5740 8511 8319 -90 911 -433 C
ATOM 1448 CD1 LEU A 212 44.401 24.935 -59.369 1.00 58.70 C
ANISOU 1448 CD1 LEU A 212 5362 8456 8488 163 908 -642 C
ATOM 1449 CD2 LEU A 212 45.981 25.840 -61.078 1.00 57.64 C
ANISOU 1449 CD2 LEU A 212 5396 8577 7929 -245 1059 -418 C
ATOM 1450 N TYR A 213 42.588 30.038 -60.782 1.00 65.11 N
ANISOU 1450 N TYR A 213 7763 8352 8622 169 514 7 N
ATOM 1451 CA TYR A 213 41.562 30.838 -61.436 1.00 64.78 C
ANISOU 1451 CA TYR A 213 8063 8114 8437 429 341 105 C
ATOM 1452 C TYR A 213 42.158 32.079 -62.084 1.00 71.58 C
ANISOU 1452 C TYR A 213 9368 8806 9022 240 437 423 C
ATOM 1453 O TYR A 213 41.681 32.516 -63.134 1.00 70.47 O
ANISOU 1453 O TYR A 213 9523 8641 8612 446 340 570 O
ATOM 1454 CB TYR A 213 40.459 31.235 -60.452 1.00 52.89 C
ANISOU 1454 CB TYR A 213 6607 6294 7195 619 186 -8 C
ATOM 1455 CG TYR A 213 39.515 32.247 -61.065 1.00 58.16 C
ANISOU 1455 CG TYR A 213 7650 6715 7734 885 -2 120 C
ATOM 1456 CD1 TYR A 213 38.563 31.853 -61.992 1.00 62.76 C
ANISOU 1456 CD1 TYR A 213 8195 7451 8200 1267 -208 9 C
ATOM 1457 CD2 TYR A 213 39.605 33.604 -60.750 1.00 64.34 C
ANISOU 1457 CD2 TYR A 213 8819 7117 8508 768 27 344 C
ATOM 1458 CE1 TYR A 213 37.719 32.774 -62.582 1.00 67.88 C
ANISOU 1458 CE1 TYR A 213 9186 7899 8707 1565 -420 136 C
ATOM 1459 CE2 TYR A 213 38.764 34.532 -61.338 1.00 68.70 C
ANISOU 1459 CE2 TYR A 213 9738 7419 8947 1053 -146 492 C
ATOM 1460 CZ TYR A 213 37.821 34.110 -62.249 1.00 67.65 C
ANISOU 1460 CZ TYR A 213 9565 7462 8679 1471 -390 399 C
ATOM 1461 OH TYR A 213 36.976 35.026 -62.835 1.00 74.17 O
ANISOU 1461 OH TYR A 213 10749 8057 9374 1811 -606 551 O
ATOM 1462 N CYS A 214 43.171 32.683 -61.454 1.00 72.98 N
ANISOU 1462 N CYS A 214 9614 8854 9261 -139 634 522 N
ATOM 1463 CA CYS A 214 43.855 33.815 -62.069 1.00 79.78 C
ANISOU 1463 CA CYS A 214 10888 9534 9890 -381 817 797 C
ATOM 1464 C CYS A 214 44.465 33.429 -63.409 1.00 82.25 C
ANISOU 1464 C CYS A 214 11246 10134 9873 -442 946 893 C
ATOM 1465 O CYS A 214 44.374 34.190 -64.379 1.00 85.56 O
ANISOU 1465 O CYS A 214 12104 10422 9984 -396 992 1143 O
ATOM 1466 CB CYS A 214 44.921 34.360 -61.122 1.00 86.93 C
ANISOU 1466 CB CYS A 214 11748 10318 10964 -819 1036 783 C
ATOM 1467 SG CYS A 214 44.283 35.610 -59.989 1.00 98.41 S
ANISOU 1467 SG CYS A 214 13468 11272 12652 -831 981 812 S
ATOM 1468 N ARG A 215 45.073 32.241 -63.486 1.00 81.28 N
ANISOU 1468 N ARG A 215 10688 10395 9800 -533 1016 699 N
ATOM 1469 CA ARG A 215 45.619 31.783 -64.766 1.00 78.44 C
ANISOU 1469 CA ARG A 215 10329 10333 9140 -596 1153 739 C
ATOM 1470 C ARG A 215 44.511 31.535 -65.797 1.00 79.94 C
ANISOU 1470 C ARG A 215 10669 10634 9072 -178 930 760 C
ATOM 1471 O ARG A 215 44.606 31.991 -66.954 1.00 86.75 O
ANISOU 1471 O ARG A 215 11891 11527 9541 -164 994 964 O
ATOM 1472 CB ARG A 215 46.457 30.526 -64.532 1.00 75.88 C
ANISOU 1472 CB ARG A 215 9464 10372 8993 -757 1269 491 C
ATOM 1473 CG ARG A 215 47.599 30.769 -63.548 1.00 81.78 C
ANISOU 1473 CG ARG A 215 10037 11070 9967 -1139 1447 443 C
ATOM 1474 CD ARG A 215 48.645 29.665 -63.536 1.00 89.87 C
ANISOU 1474 CD ARG A 215 10573 12458 11116 -1313 1590 239 C
ATOM 1475 NE ARG A 215 49.726 29.967 -62.599 1.00100.95 N
ANISOU 1475 NE ARG A 215 11797 13842 12718 -1647 1716 169 N
ATOM 1476 CZ ARG A 215 50.818 29.225 -62.444 1.00109.14 C
ANISOU 1476 CZ ARG A 215 12411 15164 13892 -1834 1841 -8 C
ATOM 1477 NH1 ARG A 215 50.985 28.126 -63.167 1.00113.05 N
ANISOU 1477 NH1 ARG A 215 12631 15954 14369 -1738 1890 -121 N
ATOM 1478 NH2 ARG A 215 51.744 29.581 -61.563 1.00111.15 N
ANISOU 1478 NH2 ARG A 215 12498 15419 14316 -2108 1911 -100 N
ATOM 1479 N ILE A 216 43.423 30.878 -65.367 1.00 76.95 N
ANISOU 1479 N ILE A 216 10037 10301 8898 169 672 542 N
ATOM 1480 CA ILE A 216 42.285 30.601 -66.248 1.00 79.18 C
ANISOU 1480 CA ILE A 216 10378 10721 8984 591 422 473 C
ATOM 1481 C ILE A 216 41.666 31.900 -66.756 1.00 82.16 C
ANISOU 1481 C ILE A 216 11324 10805 9088 794 276 771 C
ATOM 1482 O ILE A 216 41.267 32.007 -67.924 1.00 84.26 O
ANISOU 1482 O ILE A 216 11825 11220 8968 1032 157 869 O
ATOM 1483 CB ILE A 216 41.251 29.733 -65.497 1.00 77.99 C
ANISOU 1483 CB ILE A 216 9827 10612 9194 875 225 132 C
ATOM 1484 CG1 ILE A 216 41.815 28.340 -65.206 1.00 75.92 C
ANISOU 1484 CG1 ILE A 216 9043 10647 9155 737 386 -138 C
ATOM 1485 CG2 ILE A 216 39.925 29.636 -66.249 1.00 75.95 C
ANISOU 1485 CG2 ILE A 216 9616 10449 8794 1334 -72 2 C
ATOM 1486 CD1 ILE A 216 41.030 27.577 -64.151 1.00 69.26 C
ANISOU 1486 CD1 ILE A 216 7854 9734 8726 911 305 -430 C
ATOM 1487 N TYR A 217 41.632 32.924 -65.905 1.00 82.93 N
ANISOU 1487 N TYR A 217 11667 10481 9363 700 297 928 N
ATOM 1488 CA TYR A 217 41.031 34.199 -66.267 1.00 84.08 C
ANISOU 1488 CA TYR A 217 12360 10272 9315 909 177 1221 C
ATOM 1489 C TYR A 217 41.947 34.983 -67.193 1.00 83.99 C
ANISOU 1489 C TYR A 217 12831 10181 8901 668 440 1584 C
ATOM 1490 O TYR A 217 41.469 35.665 -68.107 1.00 83.81 O
ANISOU 1490 O TYR A 217 13280 10047 8517 936 331 1849 O
ATOM 1491 CB TYR A 217 40.710 35.001 -65.006 1.00 80.85 C
ANISOU 1491 CB TYR A 217 12025 9420 9275 858 156 1228 C
ATOM 1492 CG TYR A 217 40.048 36.331 -65.272 1.00 86.43 C
ANISOU 1492 CG TYR A 217 13279 9699 9861 1094 43 1517 C
ATOM 1493 CD1 TYR A 217 38.691 36.408 -65.559 1.00 89.67 C
ANISOU 1493 CD1 TYR A 217 13745 10068 10257 1622 -326 1454 C
ATOM 1494 CD2 TYR A 217 40.775 37.513 -65.217 1.00 93.18 C
ANISOU 1494 CD2 TYR A 217 14580 10175 10648 797 316 1830 C
ATOM 1495 CE1 TYR A 217 38.078 37.625 -65.797 1.00 95.80 C
ANISOU 1495 CE1 TYR A 217 15023 10437 10941 1886 -449 1729 C
ATOM 1496 CE2 TYR A 217 40.172 38.734 -65.452 1.00100.84 C
ANISOU 1496 CE2 TYR A 217 16077 10703 11534 1031 241 2116 C
ATOM 1497 CZ TYR A 217 38.824 38.785 -65.741 1.00101.43 C
ANISOU 1497 CZ TYR A 217 16211 10742 11585 1595 -157 2081 C
ATOM 1498 OH TYR A 217 38.222 40.001 -65.976 1.00108.65 O
ANISOU 1498 OH TYR A 217 17651 11203 12430 1873 -249 2376 O
ATOM 1499 N ARG A 218 43.263 34.924 -66.943 1.00 86.42 N
ANISOU 1499 N ARG A 218 13037 10528 9269 169 797 1593 N
ATOM 1500 CA ARG A 218 44.231 35.549 -67.839 1.00 95.65 C
ANISOU 1500 CA ARG A 218 14618 11643 10081 -128 1128 1876 C
ATOM 1501 C ARG A 218 44.130 34.987 -69.251 1.00106.50 C
ANISOU 1501 C ARG A 218 16089 13389 10988 58 1081 1924 C
ATOM 1502 O ARG A 218 44.401 35.703 -70.222 1.00113.87 O
ANISOU 1502 O ARG A 218 17557 14213 11494 21 1245 2243 O
ATOM 1503 CB ARG A 218 45.647 35.365 -67.291 1.00 91.04 C
ANISOU 1503 CB ARG A 218 13760 11126 9706 -690 1499 1753 C
ATOM 1504 N GLU A 219 43.737 33.718 -69.389 1.00110.07 N
ANISOU 1504 N GLU A 219 16050 14272 11501 254 884 1606 N
ATOM 1505 CA GLU A 219 43.535 33.141 -70.715 1.00116.26 C
ANISOU 1505 CA GLU A 219 16882 15448 11842 454 811 1589 C
ATOM 1506 C GLU A 219 42.109 33.314 -71.249 1.00120.35 C
ANISOU 1506 C GLU A 219 17600 15993 12133 1044 378 1621 C
ATOM 1507 O GLU A 219 41.734 32.631 -72.209 1.00122.47 O
ANISOU 1507 O GLU A 219 17773 16668 12092 1278 229 1488 O
ATOM 1508 CB GLU A 219 43.950 31.669 -70.735 1.00117.42 C
ANISOU 1508 CB GLU A 219 16395 16062 12158 326 880 1201 C
ATOM 1509 CG GLU A 219 45.436 31.475 -70.471 1.00123.12 C
ANISOU 1509 CG GLU A 219 16930 16828 13024 -221 1295 1168 C
ATOM 1510 CD GLU A 219 46.312 32.352 -71.371 1.00134.12 C
ANISOU 1510 CD GLU A 219 18850 18111 13999 -525 1635 1486 C
ATOM 1511 OE1 GLU A 219 46.030 32.457 -72.589 1.00139.67 O
ANISOU 1511 OE1 GLU A 219 19900 18969 14199 -353 1606 1635 O
ATOM 1512 OE2 GLU A 219 47.278 32.953 -70.856 1.00136.58 O
ANISOU 1512 OE2 GLU A 219 19240 18181 14474 -942 1944 1573 O
ATOM 1513 N THR A 220 41.314 34.216 -70.668 1.00122.97 N
ANISOU 1513 N THR A 220 18190 15919 12616 1294 170 1766 N
ATOM 1514 CA THR A 220 39.952 34.448 -71.138 1.00127.91 C
ANISOU 1514 CA THR A 220 18984 16556 13059 1886 -268 1776 C
ATOM 1515 C THR A 220 39.650 35.921 -71.399 1.00137.38 C
ANISOU 1515 C THR A 220 20896 17287 14016 2081 -320 2238 C
ATOM 1516 O THR A 220 38.486 36.269 -71.632 1.00142.61 O
ANISOU 1516 O THR A 220 21712 17885 14590 2609 -714 2262 O
ATOM 1517 CB THR A 220 38.931 33.888 -70.139 1.00121.75 C
ANISOU 1517 CB THR A 220 17699 15772 12789 2137 -557 1379 C
ATOM 1518 N GLU A 221 40.658 36.791 -71.370 1.00141.67 N
ANISOU 1518 N GLU A 221 21867 17490 14471 1678 77 2583 N
ATOM 1519 CA GLU A 221 40.457 38.211 -71.631 1.00150.99 C
ANISOU 1519 CA GLU A 221 23771 18163 15437 1830 110 3049 C
ATOM 1520 C GLU A 221 40.618 38.574 -73.102 1.00156.21 C
ANISOU 1520 C GLU A 221 25033 18930 15390 1989 165 3425 C
ATOM 1521 O GLU A 221 39.926 39.477 -73.588 1.00163.21 O
ANISOU 1521 O GLU A 221 26483 19540 15989 2416 -33 3770 O
ATOM 1522 CB GLU A 221 41.440 39.038 -70.797 1.00155.28 C
ANISOU 1522 CB GLU A 221 24487 18231 16282 1291 563 3202 C
ATOM 1523 CG GLU A 221 41.175 39.005 -69.301 1.00153.14 C
ANISOU 1523 CG GLU A 221 23783 17754 16651 1188 490 2915 C
ATOM 1524 CD GLU A 221 42.264 39.698 -68.506 1.00155.53 C
ANISOU 1524 CD GLU A 221 24173 17693 17227 610 944 2986 C
ATOM 1525 OE1 GLU A 221 43.448 39.561 -68.881 1.00157.53 O
ANISOU 1525 OE1 GLU A 221 24451 18077 17327 162 1329 3028 O
ATOM 1526 OE2 GLU A 221 41.939 40.383 -67.514 1.00155.47 O
ANISOU 1526 OE2 GLU A 221 24193 17283 17598 593 927 2964 O
ATOM 1527 N LYS A 222 41.512 37.896 -73.816 1.00152.93 N
ANISOU 1527 N LYS A 222 24525 18902 14680 1668 434 3368 N
ATOM 1528 CA LYS A 222 41.828 38.242 -75.194 1.00156.55 C
ANISOU 1528 CA LYS A 222 25591 19460 14433 1726 578 3728 C
ATOM 1529 C LYS A 222 40.721 37.800 -76.146 1.00153.45 C
ANISOU 1529 C LYS A 222 25227 19492 13586 2366 62 3674 C
ATOM 1530 O LYS A 222 40.016 36.817 -75.903 1.00148.96 O
ANISOU 1530 O LYS A 222 24034 19317 13246 2608 -296 3224 O
ATOM 1531 CB LYS A 222 43.154 37.607 -75.615 1.00157.70 C
ANISOU 1531 CB LYS A 222 25569 19903 14447 1143 1056 3617 C
ATOM 1532 N ARG A 223 40.576 38.544 -77.241 1.00156.84 N
ANISOU 1532 N ARG A 223 26397 19838 13356 2644 41 4125 N
ATOM 1533 CA ARG A 223 39.626 38.187 -78.282 1.00156.85 C
ANISOU 1533 CA ARG A 223 26489 20296 12812 3256 -447 4096 C
ATOM 1534 C ARG A 223 40.205 37.080 -79.162 1.00151.53 C
ANISOU 1534 C ARG A 223 25536 20270 11769 3024 -302 3837 C
ATOM 1535 O ARG A 223 41.341 36.633 -78.981 1.00147.94 O
ANISOU 1535 O ARG A 223 24845 19876 11491 2408 177 3708 O
ATOM 1536 CB ARG A 223 39.260 39.417 -79.112 1.00165.56 C
ANISOU 1536 CB ARG A 223 28381 21070 13454 3600 -533 4628 C
ATOM 1537 N THR A 224 39.411 36.626 -80.130 1.00149.35 N
ANISOU 1537 N THR A 224 25261 20502 10985 3530 -730 3724 N
ATOM 1538 CA THR A 224 39.831 35.533 -80.999 1.00146.81 C
ANISOU 1538 CA THR A 224 24638 20833 10308 3353 -631 3418 C
ATOM 1539 C THR A 224 40.908 36.015 -81.965 1.00152.44 C
ANISOU 1539 C THR A 224 26010 21485 10424 2976 -127 3839 C
ATOM 1540 O THR A 224 40.658 36.890 -82.799 1.00158.39 O
ANISOU 1540 O THR A 224 27285 22064 10833 3155 -213 4204 O
ATOM 1541 CB THR A 224 38.635 34.981 -81.769 1.00145.84 C
ANISOU 1541 CB THR A 224 24330 21283 9799 4008 -1242 3142 C
ATOM 1542 OG1 THR A 224 37.565 34.705 -80.859 1.00142.49 O
ANISOU 1542 OG1 THR A 224 23342 20823 9977 4359 -1685 2762 O
ATOM 1543 CG2 THR A 224 39.019 33.692 -82.474 1.00141.78 C
ANISOU 1543 CG2 THR A 224 23332 21460 9078 3781 -1131 2689 C
ATOM 1544 N ASN A1001 42.106 35.448 -81.851 1.00148.84 N
ANISOU 1544 N ASN A1001 25292 21129 10130 2326 406 3670 N
ATOM 1545 CA ASN A1001 43.226 35.835 -82.699 1.00149.94 C
ANISOU 1545 CA ASN A1001 25949 21203 9820 1861 961 3976 C
ATOM 1546 C ASN A1001 44.075 34.598 -82.975 1.00142.68 C
ANISOU 1546 C ASN A1001 24489 20804 8919 1403 1284 3532 C
ATOM 1547 O ASN A1001 43.649 33.464 -82.736 1.00137.63 O
ANISOU 1547 O ASN A1001 23088 20609 8595 1517 1003 3004 O
ATOM 1548 CB ASN A1001 44.038 36.960 -82.046 1.00150.96 C
ANISOU 1548 CB ASN A1001 26456 20608 10294 1419 1438 4343 C
ATOM 1549 N ILE A1002 45.288 34.826 -83.482 1.00142.45 N
ANISOU 1549 N ILE A1002 24765 20686 8674 838 1890 3697 N
ATOM 1550 CA ILE A1002 46.194 33.724 -83.795 1.00138.33 C
ANISOU 1550 CA ILE A1002 23745 20617 8196 359 2254 3278 C
ATOM 1551 C ILE A1002 46.735 33.111 -82.510 1.00128.41 C
ANISOU 1551 C ILE A1002 21678 19253 7859 -29 2395 2876 C
ATOM 1552 O ILE A1002 46.925 31.889 -82.416 1.00123.32 O
ANISOU 1552 O ILE A1002 20298 19042 7514 -166 2386 2372 O
ATOM 1553 CB ILE A1002 47.328 34.206 -84.718 1.00134.39 C
ANISOU 1553 CB ILE A1002 23636 20040 7384 -150 2818 3507 C
ATOM 1554 N PHE A1003 47.014 33.960 -81.515 1.00118.63 N
ANISOU 1554 N PHE A1003 20581 17430 7065 -208 2543 3096 N
ATOM 1555 CA PHE A1003 47.525 33.502 -80.227 1.00115.65 C
ANISOU 1555 CA PHE A1003 19499 16929 7515 -544 2650 2759 C
ATOM 1556 C PHE A1003 46.542 32.551 -79.558 1.00109.98 C
ANISOU 1556 C PHE A1003 18078 16483 7226 -145 2119 2356 C
ATOM 1557 O PHE A1003 46.925 31.471 -79.095 1.00103.56 O
ANISOU 1557 O PHE A1003 16542 15939 6867 -356 2182 1916 O
ATOM 1558 CB PHE A1003 47.813 34.713 -79.333 1.00117.23 C
ANISOU 1558 CB PHE A1003 20052 16460 8029 -728 2840 3080 C
ATOM 1559 CG PHE A1003 48.261 34.360 -77.940 1.00112.44 C
ANISOU 1559 CG PHE A1003 18775 15721 8226 -1020 2893 2760 C
ATOM 1560 CD1 PHE A1003 49.590 34.069 -77.682 1.00111.09 C
ANISOU 1560 CD1 PHE A1003 18280 15581 8349 -1630 3380 2548 C
ATOM 1561 CD2 PHE A1003 47.361 34.345 -76.885 1.00111.08 C
ANISOU 1561 CD2 PHE A1003 18309 15398 8500 -678 2458 2665 C
ATOM 1562 CE1 PHE A1003 50.011 33.756 -76.404 1.00106.96 C
ANISOU 1562 CE1 PHE A1003 17157 14968 8514 -1856 3391 2264 C
ATOM 1563 CE2 PHE A1003 47.774 34.024 -75.606 1.00110.33 C
ANISOU 1563 CE2 PHE A1003 17643 15198 9079 -931 2504 2391 C
ATOM 1564 CZ PHE A1003 49.102 33.730 -75.366 1.00108.84 C
ANISOU 1564 CZ PHE A1003 17145 15067 9141 -1503 2952 2202 C
ATOM 1565 N GLU A1004 45.264 32.940 -79.495 1.00110.61 N
ANISOU 1565 N GLU A1004 18363 16477 7185 440 1611 2490 N
ATOM 1566 CA GLU A1004 44.259 32.078 -78.880 1.00106.84 C
ANISOU 1566 CA GLU A1004 17242 16234 7120 817 1139 2080 C
ATOM 1567 C GLU A1004 44.026 30.803 -79.682 1.00108.00 C
ANISOU 1567 C GLU A1004 16934 17034 7067 933 1018 1651 C
ATOM 1568 O GLU A1004 43.772 29.750 -79.089 1.00 96.30 O
ANISOU 1568 O GLU A1004 14737 15770 6084 956 895 1190 O
ATOM 1569 CB GLU A1004 42.945 32.838 -78.702 1.00109.13 C
ANISOU 1569 CB GLU A1004 17857 16285 7321 1417 638 2289 C
ATOM 1570 CG GLU A1004 42.992 33.891 -77.611 1.00107.94 C
ANISOU 1570 CG GLU A1004 17947 15489 7576 1331 703 2569 C
ATOM 1571 CD GLU A1004 43.419 33.310 -76.279 1.00105.58 C
ANISOU 1571 CD GLU A1004 16983 15094 8038 995 832 2231 C
ATOM 1572 OE1 GLU A1004 42.766 32.354 -75.811 1.00103.37 O
ANISOU 1572 OE1 GLU A1004 16096 15073 8108 1203 549 1817 O
ATOM 1573 OE2 GLU A1004 44.411 33.799 -75.701 1.00107.34 O
ANISOU 1573 OE2 GLU A1004 17292 14989 8502 525 1225 2366 O
ATOM 1574 N MET A1005 44.132 30.867 -81.015 1.00114.13 N
ANISOU 1574 N MET A1005 18122 18120 7121 988 1084 1784 N
ATOM 1575 CA MET A1005 44.008 29.661 -81.834 1.00113.43 C
ANISOU 1575 CA MET A1005 17600 18677 6823 1038 1024 1341 C
ATOM 1576 C MET A1005 45.109 28.661 -81.508 1.00107.39 C
ANISOU 1576 C MET A1005 16217 18064 6522 484 1463 973 C
ATOM 1577 O MET A1005 44.839 27.486 -81.212 1.00 99.26 O
ANISOU 1577 O MET A1005 14474 17341 5899 533 1354 474 O
ATOM 1578 CB MET A1005 44.032 30.023 -83.321 1.00119.98 C
ANISOU 1578 CB MET A1005 19063 19793 6729 1155 1060 1592 C
ATOM 1579 CG MET A1005 44.246 28.825 -84.244 1.00122.24 C
ANISOU 1579 CG MET A1005 18940 20742 6763 1037 1160 1134 C
ATOM 1580 SD MET A1005 44.457 29.281 -85.978 1.00131.95 S
ANISOU 1580 SD MET A1005 20974 22312 6850 1085 1291 1449 S
ATOM 1581 CE MET A1005 45.618 30.623 -85.796 1.00138.23 C
ANISOU 1581 CE MET A1005 22557 22423 7543 609 1867 2101 C
ATOM 1582 N LEU A1006 46.364 29.114 -81.541 1.00106.67 N
ANISOU 1582 N LEU A1006 16384 17741 6407 -43 1980 1198 N
ATOM 1583 CA LEU A1006 47.460 28.200 -81.254 1.00104.83 C
ANISOU 1583 CA LEU A1006 15556 17655 6620 -549 2387 842 C
ATOM 1584 C LEU A1006 47.517 27.816 -79.780 1.00100.37 C
ANISOU 1584 C LEU A1006 14399 16848 6891 -613 2315 635 C
ATOM 1585 O LEU A1006 48.126 26.796 -79.451 1.00 93.89 O
ANISOU 1585 O LEU A1006 12948 16217 6508 -867 2508 259 O
ATOM 1586 CB LEU A1006 48.796 28.795 -81.705 1.00106.45 C
ANISOU 1586 CB LEU A1006 16163 17694 6590 -1107 2973 1081 C
ATOM 1587 CG LEU A1006 49.263 28.377 -83.109 1.00113.89 C
ANISOU 1587 CG LEU A1006 17266 19078 6928 -1295 3261 980 C
ATOM 1588 CD1 LEU A1006 48.308 28.805 -84.195 1.00115.96 C
ANISOU 1588 CD1 LEU A1006 18139 19548 6374 -833 2948 1228 C
ATOM 1589 CD2 LEU A1006 50.627 28.920 -83.419 1.00119.94 C
ANISOU 1589 CD2 LEU A1006 18358 19639 7573 -1901 3898 1152 C
ATOM 1590 N ARG A1007 46.880 28.589 -78.892 1.00101.57 N
ANISOU 1590 N ARG A1007 14742 16589 7263 -370 2043 868 N
ATOM 1591 CA ARG A1007 46.773 28.184 -77.494 1.00 94.23 C
ANISOU 1591 CA ARG A1007 13270 15466 7066 -371 1928 658 C
ATOM 1592 C ARG A1007 45.738 27.077 -77.312 1.00 92.38 C
ANISOU 1592 C ARG A1007 12482 15537 7082 17 1569 240 C
ATOM 1593 O ARG A1007 45.967 26.143 -76.535 1.00 97.09 O
ANISOU 1593 O ARG A1007 12468 16189 8235 -92 1633 -87 O
ATOM 1594 CB ARG A1007 46.434 29.400 -76.620 1.00 94.67 C
ANISOU 1594 CB ARG A1007 13724 14981 7266 -269 1790 1016 C
ATOM 1595 CG ARG A1007 46.697 29.248 -75.107 1.00 89.90 C
ANISOU 1595 CG ARG A1007 12682 14107 7368 -424 1803 881 C
ATOM 1596 CD ARG A1007 45.530 28.611 -74.353 1.00 88.75 C
ANISOU 1596 CD ARG A1007 12122 14003 7596 -8 1392 616 C
ATOM 1597 NE ARG A1007 44.314 29.409 -74.469 1.00 92.34 N
ANISOU 1597 NE ARG A1007 12989 14271 7823 445 1015 820 N
ATOM 1598 CZ ARG A1007 43.084 28.918 -74.353 1.00 91.19 C
ANISOU 1598 CZ ARG A1007 12596 14264 7789 892 628 575 C
ATOM 1599 NH1 ARG A1007 42.901 27.624 -74.127 1.00 89.67 N
ANISOU 1599 NH1 ARG A1007 11772 14373 7926 925 604 128 N
ATOM 1600 NH2 ARG A1007 42.036 29.721 -74.474 1.00 92.25 N
ANISOU 1600 NH2 ARG A1007 13107 14221 7724 1308 284 758 N
ATOM 1601 N ILE A1008 44.582 27.195 -77.976 1.00 90.22 N
ANISOU 1601 N ILE A1008 12418 15441 6420 485 1193 240 N
ATOM 1602 CA ILE A1008 43.603 26.108 -77.987 1.00 86.65 C
ANISOU 1602 CA ILE A1008 11425 15333 6167 825 898 -233 C
ATOM 1603 C ILE A1008 44.231 24.832 -78.530 1.00 86.20 C
ANISOU 1603 C ILE A1008 10859 15714 6178 570 1179 -645 C
ATOM 1604 O ILE A1008 44.115 23.758 -77.927 1.00 78.88 O
ANISOU 1604 O ILE A1008 9302 14879 5788 563 1204 -1047 O
ATOM 1605 CB ILE A1008 42.351 26.504 -78.793 1.00 93.21 C
ANISOU 1605 CB ILE A1008 12578 16353 6485 1361 451 -194 C
ATOM 1606 CG1 ILE A1008 41.602 27.651 -78.116 1.00 96.47 C
ANISOU 1606 CG1 ILE A1008 13389 16303 6964 1669 143 144 C
ATOM 1607 CG2 ILE A1008 41.424 25.307 -78.981 1.00 90.81 C
ANISOU 1607 CG2 ILE A1008 11668 16480 6356 1656 206 -776 C
ATOM 1608 CD1 ILE A1008 40.350 28.062 -78.857 1.00103.38 C
ANISOU 1608 CD1 ILE A1008 14554 17355 7370 2252 -342 174 C
ATOM 1609 N ASP A1009 44.927 24.935 -79.666 1.00 91.35 N
ANISOU 1609 N ASP A1009 11795 16616 6297 345 1430 -547 N
ATOM 1610 CA ASP A1009 45.512 23.742 -80.270 1.00 94.57 C
ANISOU 1610 CA ASP A1009 11726 17454 6752 98 1713 -964 C
ATOM 1611 C ASP A1009 46.724 23.248 -79.485 1.00 94.21 C
ANISOU 1611 C ASP A1009 11268 17239 7290 -361 2117 -1061 C
ATOM 1612 O ASP A1009 46.867 22.042 -79.251 1.00 86.57 O
ANISOU 1612 O ASP A1009 9665 16464 6762 -425 2228 -1487 O
ATOM 1613 CB ASP A1009 45.875 24.022 -81.726 1.00101.08 C
ANISOU 1613 CB ASP A1009 13000 18604 6803 -12 1873 -843 C
ATOM 1614 CG ASP A1009 44.655 24.280 -82.586 1.00106.13 C
ANISOU 1614 CG ASP A1009 13950 19532 6841 498 1430 -835 C
ATOM 1615 OD1 ASP A1009 43.554 23.828 -82.202 1.00104.91 O
ANISOU 1615 OD1 ASP A1009 13437 19471 6953 895 1046 -1129 O
ATOM 1616 OD2 ASP A1009 44.795 24.925 -83.646 1.00113.64 O
ANISOU 1616 OD2 ASP A1009 15503 20625 7051 510 1472 -550 O
ATOM 1617 N GLU A1010 47.604 24.154 -79.066 1.00113.48 N
ANISOU 1617 N GLU A1010 14500 17619 10998 -1138 -479 4225 N
ATOM 1618 CA GLU A1010 48.783 23.807 -78.275 1.00121.35 C
ANISOU 1618 CA GLU A1010 15183 18762 12162 -758 2 3512 C
ATOM 1619 C GLU A1010 48.738 24.624 -76.990 1.00127.54 C
ANISOU 1619 C GLU A1010 15113 19713 13634 -506 192 3473 C
ATOM 1620 O GLU A1010 48.999 25.830 -77.014 1.00133.33 O
ANISOU 1620 O GLU A1010 15560 20427 14671 -502 566 3496 O
ATOM 1621 CB GLU A1010 50.069 24.070 -79.056 1.00124.47 C
ANISOU 1621 CB GLU A1010 15860 19152 12279 -752 664 3054 C
ATOM 1622 N GLY A1011 48.414 23.964 -75.877 1.00127.95 N
ANISOU 1622 N GLY A1011 14804 19917 13894 -330 -84 3411 N
ATOM 1623 CA GLY A1011 48.250 24.656 -74.609 1.00127.34 C
ANISOU 1623 CA GLY A1011 13993 20029 14361 -129 71 3362 C
ATOM 1624 C GLY A1011 49.493 25.403 -74.163 1.00128.79 C
ANISOU 1624 C GLY A1011 13857 20252 14826 58 691 2836 C
ATOM 1625 O GLY A1011 50.608 25.173 -74.635 1.00139.97 O
ANISOU 1625 O GLY A1011 15494 21619 16068 88 1016 2462 O
ATOM 1626 N LEU A1012 49.286 26.308 -73.212 1.00121.33 N
ANISOU 1626 N LEU A1012 12368 19396 14333 183 858 2811 N
ATOM 1627 CA LEU A1012 50.351 27.151 -72.687 1.00113.51 C
ANISOU 1627 CA LEU A1012 11066 18408 13655 303 1356 2379 C
ATOM 1628 C LEU A1012 50.829 26.593 -71.355 1.00111.03 C
ANISOU 1628 C LEU A1012 10397 18324 13465 446 1346 1999 C
ATOM 1629 O LEU A1012 50.040 26.445 -70.418 1.00109.02 O
ANISOU 1629 O LEU A1012 9863 18256 13303 487 1121 2105 O
ATOM 1630 CB LEU A1012 49.861 28.588 -72.518 1.00109.58 C
ANISOU 1630 CB LEU A1012 10289 17773 13576 327 1520 2552 C
ATOM 1631 CG LEU A1012 50.852 29.597 -71.940 1.00110.74 C
ANISOU 1631 CG LEU A1012 10149 17853 14073 403 1951 2152 C
ATOM 1632 CD1 LEU A1012 52.050 29.782 -72.849 1.00115.27 C
ANISOU 1632 CD1 LEU A1012 10958 18328 14511 263 2262 2017 C
ATOM 1633 CD2 LEU A1012 50.151 30.924 -71.697 1.00113.51 C
ANISOU 1633 CD2 LEU A1012 10264 17990 14873 470 2011 2319 C
ATOM 1634 N ARG A1013 52.124 26.305 -71.273 1.00111.82 N
ANISOU 1634 N ARG A1013 10478 18432 13575 493 1591 1592 N
ATOM 1635 CA ARG A1013 52.741 25.754 -70.076 1.00110.27 C
ANISOU 1635 CA ARG A1013 9962 18415 13521 568 1525 1267 C
ATOM 1636 C ARG A1013 53.828 26.707 -69.601 1.00112.36 C
ANISOU 1636 C ARG A1013 9922 18649 14121 578 1935 946 C
ATOM 1637 O ARG A1013 54.662 27.152 -70.395 1.00113.22 O
ANISOU 1637 O ARG A1013 10117 18626 14277 557 2279 863 O
ATOM 1638 CB ARG A1013 53.284 24.349 -70.351 1.00105.05 C
ANISOU 1638 CB ARG A1013 9518 17740 12655 617 1308 1129 C
ATOM 1639 CG ARG A1013 52.171 23.372 -70.734 1.00102.58 C
ANISOU 1639 CG ARG A1013 9553 17417 12004 551 788 1471 C
ATOM 1640 CD ARG A1013 52.542 21.932 -70.451 1.00101.55 C
ANISOU 1640 CD ARG A1013 9528 17270 11786 602 403 1322 C
ATOM 1641 NE ARG A1013 53.136 21.768 -69.130 1.00101.82 N
ANISOU 1641 NE ARG A1013 9093 17477 12116 624 335 1104 N
ATOM 1642 CZ ARG A1013 53.400 20.591 -68.576 1.00103.50 C
ANISOU 1642 CZ ARG A1013 9272 17691 12363 626 -104 1039 C
ATOM 1643 NH1 ARG A1013 53.128 19.473 -69.236 1.00105.68 N
ANISOU 1643 NH1 ARG A1013 9976 17766 12413 653 -496 1128 N
ATOM 1644 NH2 ARG A1013 53.957 20.532 -67.374 1.00102.13 N
ANISOU 1644 NH2 ARG A1013 8675 17679 12451 572 -197 895 N
ATOM 1645 N LEU A1014 53.809 27.015 -68.304 1.00116.30 N
ANISOU 1645 N LEU A1014 10084 19289 14816 566 1884 788 N
ATOM 1646 CA LEU A1014 54.772 27.935 -67.714 1.00115.20 C
ANISOU 1646 CA LEU A1014 9692 19093 14985 514 2170 503 C
ATOM 1647 C LEU A1014 56.090 27.265 -67.360 1.00113.44 C
ANISOU 1647 C LEU A1014 9291 18928 14883 484 2159 257 C
ATOM 1648 O LEU A1014 57.097 27.960 -67.196 1.00116.18 O
ANISOU 1648 O LEU A1014 9448 19195 15501 406 2400 92 O
ATOM 1649 CB LEU A1014 54.176 28.587 -66.465 1.00118.87 C
ANISOU 1649 CB LEU A1014 9951 19664 15551 484 2124 399 C
ATOM 1650 N LYS A1015 56.107 25.943 -67.237 1.00110.67 N
ANISOU 1650 N LYS A1015 8974 18682 14394 534 1841 266 N
ATOM 1651 CA LYS A1015 57.302 25.204 -66.867 1.00110.02 C
ANISOU 1651 CA LYS A1015 8666 18609 14525 544 1759 69 C
ATOM 1652 C LYS A1015 57.720 24.290 -68.010 1.00108.71 C
ANISOU 1652 C LYS A1015 8715 18313 14278 735 1837 45 C
ATOM 1653 O LYS A1015 56.894 23.870 -68.826 1.00108.27 O
ANISOU 1653 O LYS A1015 9050 18199 13887 798 1745 201 O
ATOM 1654 CB LYS A1015 57.065 24.388 -65.586 1.00112.43 C
ANISOU 1654 CB LYS A1015 8805 19104 14809 425 1249 74 C
ATOM 1655 CG LYS A1015 55.774 23.569 -65.588 1.00115.67 C
ANISOU 1655 CG LYS A1015 9446 19632 14870 427 849 324 C
ATOM 1656 CD LYS A1015 55.529 22.915 -64.232 1.00116.67 C
ANISOU 1656 CD LYS A1015 9376 20015 14938 216 360 381 C
ATOM 1657 CE LYS A1015 54.214 22.147 -64.206 1.00113.25 C
ANISOU 1657 CE LYS A1015 9117 19749 14164 161 -52 710 C
ATOM 1658 NZ LYS A1015 53.036 23.037 -64.403 1.00111.79 N
ANISOU 1658 NZ LYS A1015 8993 19679 13801 185 192 879 N
ATOM 1659 N ILE A1016 59.023 24.007 -68.070 1.00109.51 N
ANISOU 1659 N ILE A1016 8555 18357 14695 821 2016 -154 N
ATOM 1660 CA ILE A1016 59.564 23.165 -69.129 1.00113.91 C
ANISOU 1660 CA ILE A1016 9284 18786 15211 1061 2206 -278 C
ATOM 1661 C ILE A1016 59.051 21.744 -68.954 1.00114.16 C
ANISOU 1661 C ILE A1016 9533 18735 15106 1174 1662 -269 C
ATOM 1662 O ILE A1016 59.070 21.189 -67.848 1.00113.72 O
ANISOU 1662 O ILE A1016 9230 18728 15249 1094 1180 -236 O
ATOM 1663 CB ILE A1016 61.098 23.210 -69.125 1.00119.23 C
ANISOU 1663 CB ILE A1016 9497 19443 16363 1162 2552 -476 C
ATOM 1664 N TYR A1017 58.585 21.149 -70.048 1.00114.27 N
ANISOU 1664 N TYR A1017 10054 18609 14755 1308 1686 -272 N
ATOM 1665 CA TYR A1017 57.978 19.830 -70.009 1.00113.30 C
ANISOU 1665 CA TYR A1017 10250 18342 14458 1377 1104 -225 C
ATOM 1666 C TYR A1017 58.491 19.003 -71.177 1.00119.62 C
ANISOU 1666 C TYR A1017 11434 18879 15136 1665 1327 -507 C
ATOM 1667 O TYR A1017 59.147 19.509 -72.091 1.00123.09 O
ANISOU 1667 O TYR A1017 11929 19326 15514 1775 1981 -695 O
ATOM 1668 CB TYR A1017 56.447 19.917 -70.030 1.00110.63 C
ANISOU 1668 CB TYR A1017 10268 18085 13681 1157 715 147 C
ATOM 1669 CG TYR A1017 55.845 20.365 -71.348 1.00110.96 C
ANISOU 1669 CG TYR A1017 10827 18050 13283 1117 989 272 C
ATOM 1670 CD1 TYR A1017 55.828 21.708 -71.703 1.00108.99 C
ANISOU 1670 CD1 TYR A1017 10490 17904 13018 1011 1467 362 C
ATOM 1671 CD2 TYR A1017 55.268 19.449 -72.222 1.00111.86 C
ANISOU 1671 CD2 TYR A1017 11555 17955 12990 1133 690 337 C
ATOM 1672 CE1 TYR A1017 55.272 22.127 -72.901 1.00108.62 C
ANISOU 1672 CE1 TYR A1017 10917 17779 12577 904 1639 549 C
ATOM 1673 CE2 TYR A1017 54.709 19.859 -73.424 1.00111.80 C
ANISOU 1673 CE2 TYR A1017 12067 17879 12532 1011 872 500 C
ATOM 1674 CZ TYR A1017 54.713 21.199 -73.756 1.00110.44 C
ANISOU 1674 CZ TYR A1017 11759 17838 12366 887 1342 627 C
ATOM 1675 OH TYR A1017 54.159 21.614 -74.947 1.00112.15 O
ANISOU 1675 OH TYR A1017 12489 17977 12145 701 1452 858 O
ATOM 1676 N LYS A1018 58.178 17.714 -71.136 1.00122.96 N
ANISOU 1676 N LYS A1018 12148 19069 15502 1770 773 -540 N
ATOM 1677 CA LYS A1018 58.505 16.791 -72.212 1.00128.63 C
ANISOU 1677 CA LYS A1018 13364 19463 16047 2061 898 -862 C
ATOM 1678 C LYS A1018 57.289 16.635 -73.112 1.00128.55 C
ANISOU 1678 C LYS A1018 14136 19361 15347 1875 664 -651 C
ATOM 1679 O LYS A1018 56.187 16.349 -72.633 1.00125.98 O
ANISOU 1679 O LYS A1018 13958 19059 14851 1625 -7 -267 O
ATOM 1680 CB LYS A1018 58.938 15.433 -71.659 1.00129.70 C
ANISOU 1680 CB LYS A1018 13399 19283 16600 2297 354 -1041 C
ATOM 1681 N ASP A1019 57.494 16.823 -74.413 1.00133.38 N
ANISOU 1681 N ASP A1019 15235 19896 15549 1953 1205 -864 N
ATOM 1682 CA ASP A1019 56.414 16.756 -75.388 1.00137.34 C
ANISOU 1682 CA ASP A1019 16531 20298 15355 1708 991 -635 C
ATOM 1683 C ASP A1019 56.035 15.293 -75.627 1.00142.27 C
ANISOU 1683 C ASP A1019 17771 20509 15777 1805 349 -761 C
ATOM 1684 O ASP A1019 56.433 14.390 -74.884 1.00143.53 O
ANISOU 1684 O ASP A1019 17680 20472 16382 2027 -37 -930 O
ATOM 1685 CB ASP A1019 56.840 17.461 -76.674 1.00146.49 C
ANISOU 1685 CB ASP A1019 18031 21539 16091 1683 1777 -812 C
ATOM 1686 CG ASP A1019 55.673 18.061 -77.430 1.00150.17 C
ANISOU 1686 CG ASP A1019 19047 22056 15955 1256 1594 -346 C
ATOM 1687 OD1 ASP A1019 54.545 17.540 -77.300 1.00149.86 O
ANISOU 1687 OD1 ASP A1019 19359 21877 15705 1051 846 8 O
ATOM 1688 OD2 ASP A1019 55.888 19.052 -78.160 1.00152.93 O
ANISOU 1688 OD2 ASP A1019 19451 22583 16072 1095 2158 -281 O
ATOM 1689 N THR A1020 55.232 15.040 -76.666 1.00145.68 N
ANISOU 1689 N THR A1020 19049 20764 15538 1594 145 -638 N
ATOM 1690 CA THR A1020 54.861 13.666 -76.983 1.00149.13 C
ANISOU 1690 CA THR A1020 20190 20739 15732 1648 -508 -770 C
ATOM 1691 C THR A1020 56.066 12.860 -77.453 1.00152.40 C
ANISOU 1691 C THR A1020 20796 20818 16291 2157 -62 -1527 C
ATOM 1692 O THR A1020 56.155 11.659 -77.172 1.00155.25 O
ANISOU 1692 O THR A1020 21359 20752 16878 2374 -616 -1740 O
ATOM 1693 CB THR A1020 53.766 13.647 -78.048 1.00151.85 C
ANISOU 1693 CB THR A1020 21451 20958 15285 1244 -833 -450 C
ATOM 1694 OG1 THR A1020 54.229 14.328 -79.221 1.00156.66 O
ANISOU 1694 OG1 THR A1020 22433 21668 15421 1226 -18 -710 O
ATOM 1695 CG2 THR A1020 52.512 14.336 -77.530 1.00144.50 C
ANISOU 1695 CG2 THR A1020 20243 20320 14340 793 -1340 342 C
ATOM 1696 N GLU A1021 57.001 13.503 -78.156 1.00151.08 N
ANISOU 1696 N GLU A1021 20534 20833 16037 2357 931 -1921 N
ATOM 1697 CA GLU A1021 58.217 12.842 -78.606 1.00154.34 C
ANISOU 1697 CA GLU A1021 20993 21003 16647 2899 1523 -2660 C
ATOM 1698 C GLU A1021 59.308 12.815 -77.541 1.00150.19 C
ANISOU 1698 C GLU A1021 19421 20553 17093 3288 1718 -2831 C
ATOM 1699 O GLU A1021 60.344 12.178 -77.757 1.00159.30 O
ANISOU 1699 O GLU A1021 20452 21467 18608 3804 2137 -3409 O
ATOM 1700 CB GLU A1021 58.745 13.519 -79.875 1.00159.72 C
ANISOU 1700 CB GLU A1021 22015 21917 16754 2899 2546 -2969 C
ATOM 1701 N GLY A1022 59.105 13.481 -76.405 1.00138.87 N
ANISOU 1701 N GLY A1022 17240 19429 16095 3051 1423 -2350 N
ATOM 1702 CA GLY A1022 60.065 13.466 -75.321 1.00136.10 C
ANISOU 1702 CA GLY A1022 15942 19144 16627 3301 1465 -2423 C
ATOM 1703 C GLY A1022 61.031 14.630 -75.287 1.00135.90 C
ANISOU 1703 C GLY A1022 15202 19538 16895 3341 2336 -2467 C
ATOM 1704 O GLY A1022 61.861 14.693 -74.371 1.00135.71 O
ANISOU 1704 O GLY A1022 14367 19579 17618 3488 2343 -2471 O
ATOM 1705 N TYR A1023 60.951 15.555 -76.239 1.00136.48 N
ANISOU 1705 N TYR A1023 15553 19887 16416 3158 3000 -2444 N
ATOM 1706 CA TYR A1023 61.887 16.669 -76.262 1.00135.19 C
ANISOU 1706 CA TYR A1023 14730 20110 16524 3147 3793 -2440 C
ATOM 1707 C TYR A1023 61.436 17.773 -75.313 1.00125.97 C
ANISOU 1707 C TYR A1023 13084 19235 15544 2737 3511 -1920 C
ATOM 1708 O TYR A1023 60.256 17.903 -74.980 1.00118.40 O
ANISOU 1708 O TYR A1023 12420 18271 14296 2426 2911 -1552 O
ATOM 1709 CB TYR A1023 62.060 17.211 -77.683 1.00135.30 C
ANISOU 1709 CB TYR A1023 15229 20313 15867 3073 4618 -2604 C
ATOM 1710 CG TYR A1023 62.592 16.179 -78.649 1.00137.40 C
ANISOU 1710 CG TYR A1023 15993 20325 15889 3503 5047 -3220 C
ATOM 1711 CD1 TYR A1023 63.959 15.984 -78.788 1.00142.13 C
ANISOU 1711 CD1 TYR A1023 16019 20991 16995 3970 5805 -3661 C
ATOM 1712 CD2 TYR A1023 61.736 15.395 -79.412 1.00136.79 C
ANISOU 1712 CD2 TYR A1023 16953 19924 15098 3449 4694 -3366 C
ATOM 1713 CE1 TYR A1023 64.461 15.041 -79.660 1.00151.26 C
ANISOU 1713 CE1 TYR A1023 17614 21903 17956 4435 6281 -4300 C
ATOM 1714 CE2 TYR A1023 62.230 14.443 -80.292 1.00144.67 C
ANISOU 1714 CE2 TYR A1023 18492 20640 15838 3863 5105 -4015 C
ATOM 1715 CZ TYR A1023 63.594 14.273 -80.410 1.00152.16 C
ANISOU 1715 CZ TYR A1023 18846 21664 17303 4387 5938 -4514 C
ATOM 1716 OH TYR A1023 64.096 13.332 -81.280 1.00161.47 O
ANISOU 1716 OH TYR A1023 20547 22554 18248 4867 6430 -5231 O
ATOM 1717 N TYR A1024 62.404 18.579 -74.881 1.00130.55 N
ANISOU 1717 N TYR A1024 12908 20063 16629 2744 3963 -1896 N
ATOM 1718 CA TYR A1024 62.152 19.665 -73.937 1.00130.83 C
ANISOU 1718 CA TYR A1024 12488 20330 16893 2388 3753 -1498 C
ATOM 1719 C TYR A1024 61.452 20.819 -74.641 1.00132.33 C
ANISOU 1719 C TYR A1024 13041 20706 16534 2031 4013 -1217 C
ATOM 1720 O TYR A1024 62.086 21.636 -75.311 1.00137.14 O
ANISOU 1720 O TYR A1024 13523 21505 17079 1953 4669 -1225 O
ATOM 1721 CB TYR A1024 63.463 20.125 -73.307 1.00135.49 C
ANISOU 1721 CB TYR A1024 12214 21068 18198 2469 4091 -1550 C
ATOM 1722 N THR A1025 60.134 20.889 -74.476 1.00128.56 N
ANISOU 1722 N THR A1025 12972 20172 15702 1792 3463 -914 N
ATOM 1723 CA THR A1025 59.319 21.971 -74.999 1.00121.65 C
ANISOU 1723 CA THR A1025 12388 19405 14428 1450 3548 -566 C
ATOM 1724 C THR A1025 58.766 22.794 -73.844 1.00113.98 C
ANISOU 1724 C THR A1025 11012 18527 13768 1248 3195 -267 C
ATOM 1725 O THR A1025 58.731 22.342 -72.697 1.00112.21 O
ANISOU 1725 O THR A1025 10460 18301 13874 1310 2774 -294 O
ATOM 1726 CB THR A1025 58.167 21.433 -75.856 1.00122.06 C
ANISOU 1726 CB THR A1025 13245 19301 13829 1331 3210 -412 C
ATOM 1727 OG1 THR A1025 57.429 20.461 -75.104 1.00119.93 O
ANISOU 1727 OG1 THR A1025 13061 18883 13624 1390 2476 -340 O
ATOM 1728 CG2 THR A1025 58.705 20.790 -77.134 1.00129.26 C
ANISOU 1728 CG2 THR A1025 14692 20124 14295 1478 3658 -758 C
ATOM 1729 N ILE A1026 58.350 24.023 -74.153 1.00112.34 N
ANISOU 1729 N ILE A1026 10846 18389 13449 992 3371 10 N
ATOM 1730 CA ILE A1026 57.795 24.923 -73.147 1.00104.47 C
ANISOU 1730 CA ILE A1026 9522 17439 12733 838 3124 231 C
ATOM 1731 C ILE A1026 56.931 25.948 -73.874 1.00102.03 C
ANISOU 1731 C ILE A1026 9510 17077 12179 602 3175 588 C
ATOM 1732 O ILE A1026 57.063 26.147 -75.083 1.00104.61 O
ANISOU 1732 O ILE A1026 10197 17380 12170 488 3470 671 O
ATOM 1733 CB ILE A1026 58.925 25.586 -72.311 1.00101.81 C
ANISOU 1733 CB ILE A1026 8569 17189 12926 834 3378 67 C
ATOM 1734 CG1 ILE A1026 58.383 26.179 -71.003 1.00100.56 C
ANISOU 1734 CG1 ILE A1026 8128 17058 13023 722 3038 156 C
ATOM 1735 CG2 ILE A1026 59.658 26.647 -73.128 1.00 99.33 C
ANISOU 1735 CG2 ILE A1026 8188 16910 12644 686 3938 127 C
ATOM 1736 CD1 ILE A1026 59.415 26.904 -70.178 1.00102.79 C
ANISOU 1736 CD1 ILE A1026 7912 17379 13765 630 3199 23 C
ATOM 1737 N GLY A1027 56.028 26.593 -73.135 1.00 99.70 N
ANISOU 1737 N GLY A1027 9064 16762 12055 521 2881 810 N
ATOM 1738 CA GLY A1027 55.134 27.591 -73.688 1.00100.20 C
ANISOU 1738 CA GLY A1027 9317 16712 12042 338 2847 1185 C
ATOM 1739 C GLY A1027 54.085 27.058 -74.640 1.00 97.96 C
ANISOU 1739 C GLY A1027 9569 16348 11302 235 2544 1517 C
ATOM 1740 O GLY A1027 53.277 26.201 -74.269 1.00 91.69 O
ANISOU 1740 O GLY A1027 8870 15580 10389 296 2103 1613 O
ATOM 1741 N ILE A1028 54.099 27.548 -75.880 1.00100.21 N
ANISOU 1741 N ILE A1028 10226 16546 11304 15 2735 1737 N
ATOM 1742 CA ILE A1028 53.150 27.118 -76.902 1.00 99.03 C
ANISOU 1742 CA ILE A1028 10666 16295 10665 -183 2410 2101 C
ATOM 1743 C ILE A1028 53.893 26.271 -77.927 1.00105.58 C
ANISOU 1743 C ILE A1028 12004 17165 10946 -218 2679 1840 C
ATOM 1744 O ILE A1028 54.094 26.686 -79.075 1.00111.76 O
ANISOU 1744 O ILE A1028 13176 17939 11348 -487 2933 1985 O
ATOM 1745 CB ILE A1028 52.442 28.321 -77.556 1.00 98.66 C
ANISOU 1745 CB ILE A1028 10722 16089 10674 -475 2322 2623 C
ATOM 1746 CG1 ILE A1028 52.005 29.313 -76.476 1.00101.09 C
ANISOU 1746 CG1 ILE A1028 10453 16323 11633 -340 2240 2713 C
ATOM 1747 CG2 ILE A1028 51.216 27.867 -78.351 1.00 97.87 C
ANISOU 1747 CG2 ILE A1028 11143 15866 10176 -709 1797 3117 C
ATOM 1748 CD1 ILE A1028 51.074 30.397 -76.957 1.00104.96 C
ANISOU 1748 CD1 ILE A1028 10975 16571 12337 -541 2017 3262 C
ATOM 1749 N GLY A1029 54.313 25.080 -77.503 1.00108.07 N
ANISOU 1749 N GLY A1029 12320 17519 11221 49 2629 1445 N
ATOM 1750 CA GLY A1029 55.057 24.158 -78.339 1.00117.15 C
ANISOU 1750 CA GLY A1029 13917 18663 11930 133 2917 1075 C
ATOM 1751 C GLY A1029 56.354 24.719 -78.881 1.00123.29 C
ANISOU 1751 C GLY A1029 14534 19602 12707 138 3684 811 C
ATOM 1752 O GLY A1029 56.562 24.765 -80.096 1.00131.44 O
ANISOU 1752 O GLY A1029 16076 20676 13187 -64 4014 815 O
ATOM 1753 N HIS A1030 57.230 25.156 -77.982 1.00103.34 N
ANISOU 1753 N HIS A1030 10950 18092 10223 -1601 3354 -483 N
ATOM 1754 CA HIS A1030 58.476 25.810 -78.351 1.00113.39 C
ANISOU 1754 CA HIS A1030 11984 19372 11728 -1327 3407 -156 C
ATOM 1755 C HIS A1030 59.628 25.090 -77.677 1.00119.54 C
ANISOU 1755 C HIS A1030 13016 20001 12402 -1025 3593 36 C
ATOM 1756 O HIS A1030 59.558 24.779 -76.486 1.00118.31 O
ANISOU 1756 O HIS A1030 12870 19869 12214 -1062 3548 -141 O
ATOM 1757 CB HIS A1030 58.493 27.285 -77.943 1.00119.10 C
ANISOU 1757 CB HIS A1030 11979 20369 12904 -1416 3115 -292 C
ATOM 1758 CG HIS A1030 59.693 28.027 -78.441 1.00122.09 C
ANISOU 1758 CG HIS A1030 12082 20791 13517 -1242 3102 100 C
ATOM 1759 ND1 HIS A1030 60.137 27.937 -79.742 1.00125.58 N
ANISOU 1759 ND1 HIS A1030 12708 21176 13831 -1177 3252 456 N
ATOM 1760 CD2 HIS A1030 60.565 28.843 -77.803 1.00123.11 C
ANISOU 1760 CD2 HIS A1030 11784 21024 13966 -1152 2939 213 C
ATOM 1761 CE1 HIS A1030 61.218 28.683 -79.890 1.00126.19 C
ANISOU 1761 CE1 HIS A1030 12448 21362 14138 -1083 3178 779 C
ATOM 1762 NE2 HIS A1030 61.497 29.245 -78.728 1.00125.04 N
ANISOU 1762 NE2 HIS A1030 11928 21304 14276 -1075 2975 649 N
ATOM 1763 N LEU A1031 60.706 24.882 -78.423 1.00125.51 N
ANISOU 1763 N LEU A1031 13935 20652 13101 -748 3784 370 N
ATOM 1764 CA LEU A1031 61.865 24.178 -77.892 1.00129.37 C
ANISOU 1764 CA LEU A1031 14633 21056 13466 -455 3955 503 C
ATOM 1765 C LEU A1031 63.172 24.838 -78.317 1.00132.07 C
ANISOU 1765 C LEU A1031 14590 21573 14017 -245 3956 798 C
ATOM 1766 O LEU A1031 64.202 24.666 -77.664 1.00134.15 O
ANISOU 1766 O LEU A1031 14737 21929 14304 -31 3983 891 O
ATOM 1767 CB LEU A1031 61.831 22.708 -78.335 1.00131.56 C
ANISOU 1767 CB LEU A1031 15713 21019 13255 -322 4207 520 C
ATOM 1768 CG LEU A1031 61.897 22.339 -79.822 1.00133.66 C
ANISOU 1768 CG LEU A1031 16364 21130 13291 -246 4362 660 C
ATOM 1769 CD1 LEU A1031 63.315 21.983 -80.257 1.00137.44 C
ANISOU 1769 CD1 LEU A1031 16865 21709 13647 79 4486 839 C
ATOM 1770 CD2 LEU A1031 60.942 21.196 -80.127 1.00134.93 C
ANISOU 1770 CD2 LEU A1031 17302 20947 13019 -331 4455 557 C
ATOM 1771 N THR A1058 61.040 29.346 -68.495 1.00146.66 N
ANISOU 1771 N THR A1058 14041 24478 17207 -1167 2246 -1344 N
ATOM 1772 CA THR A1058 60.059 29.417 -67.421 1.00145.62 C
ANISOU 1772 CA THR A1058 13879 24519 16930 -1348 2133 -1858 C
ATOM 1773 C THR A1058 59.726 30.869 -67.091 1.00145.76 C
ANISOU 1773 C THR A1058 13448 24607 17327 -1291 1758 -2178 C
ATOM 1774 O THR A1058 60.434 31.518 -66.320 1.00148.45 O
ANISOU 1774 O THR A1058 13564 24956 17882 -1193 1576 -2160 O
ATOM 1775 CB THR A1058 60.561 28.702 -66.152 1.00146.93 C
ANISOU 1775 CB THR A1058 14222 24777 16829 -1396 2253 -1873 C
ATOM 1776 OG1 THR A1058 61.770 29.323 -65.697 1.00148.92 O
ANISOU 1776 OG1 THR A1058 14201 25029 17354 -1209 2138 -1646 O
ATOM 1777 CG2 THR A1058 60.826 27.229 -66.439 1.00144.61 C
ANISOU 1777 CG2 THR A1058 14446 24350 16147 -1422 2570 -1596 C
ATOM 1778 N LYS A1059 58.645 31.370 -67.679 1.00142.37 N
ANISOU 1778 N LYS A1059 12905 24206 16984 -1334 1610 -2479 N
ATOM 1779 CA LYS A1059 58.186 32.731 -67.430 1.00137.65 C
ANISOU 1779 CA LYS A1059 11946 23617 16740 -1215 1206 -2845 C
ATOM 1780 C LYS A1059 56.682 32.785 -67.674 1.00132.38 C
ANISOU 1780 C LYS A1059 11259 23109 15930 -1287 1155 -3343 C
ATOM 1781 O LYS A1059 56.039 31.763 -67.931 1.00130.90 O
ANISOU 1781 O LYS A1059 11318 23050 15367 -1495 1417 -3379 O
ATOM 1782 CB LYS A1059 58.952 33.730 -68.309 1.00137.51 C
ANISOU 1782 CB LYS A1059 11692 23344 17212 -1082 913 -2479 C
ATOM 1783 N ASP A1060 56.117 33.991 -67.592 1.00131.96 N
ANISOU 1783 N ASP A1060 10922 23031 16186 -1106 773 -3724 N
ATOM 1784 CA ASP A1060 54.695 34.191 -67.828 1.00135.81 C
ANISOU 1784 CA ASP A1060 11326 23695 16580 -1094 686 -4232 C
ATOM 1785 C ASP A1060 54.391 34.988 -69.086 1.00137.11 C
ANISOU 1785 C ASP A1060 11346 23616 17132 -961 377 -4171 C
ATOM 1786 O ASP A1060 53.265 34.909 -69.587 1.00136.08 O
ANISOU 1786 O ASP A1060 11183 23622 16899 -984 370 -4475 O
ATOM 1787 CB ASP A1060 54.048 34.899 -66.627 1.00139.70 C
ANISOU 1787 CB ASP A1060 11629 24407 17045 -924 487 -4861 C
ATOM 1788 N GLU A1061 55.354 35.749 -69.606 1.00138.38 N
ANISOU 1788 N GLU A1061 11417 23438 17723 -861 81 -3773 N
ATOM 1789 CA GLU A1061 55.143 36.563 -70.800 1.00138.02 C
ANISOU 1789 CA GLU A1061 11264 23124 18051 -791 -317 -3671 C
ATOM 1790 C GLU A1061 55.798 35.862 -71.986 1.00135.68 C
ANISOU 1790 C GLU A1061 11075 22785 17693 -1009 -46 -3090 C
ATOM 1791 O GLU A1061 56.881 36.222 -72.444 1.00133.89 O
ANISOU 1791 O GLU A1061 10791 22377 17702 -1051 -182 -2601 O
ATOM 1792 CB GLU A1061 55.690 37.975 -70.597 1.00139.82 C
ANISOU 1792 CB GLU A1061 11361 23001 18765 -600 -947 -3627 C
ATOM 1793 CG GLU A1061 55.016 38.756 -69.475 1.00144.48 C
ANISOU 1793 CG GLU A1061 11873 23616 19407 -315 -1237 -4249 C
ATOM 1794 CD GLU A1061 53.542 39.035 -69.733 1.00148.67 C
ANISOU 1794 CD GLU A1061 12341 24250 19897 -123 -1362 -4830 C
ATOM 1795 OE1 GLU A1061 53.130 39.095 -70.913 1.00148.92 O
ANISOU 1795 OE1 GLU A1061 12393 24144 20048 -171 -1497 -4707 O
ATOM 1796 OE2 GLU A1061 52.790 39.195 -68.749 1.00152.13 O
ANISOU 1796 OE2 GLU A1061 12688 24946 20169 80 -1325 -5428 O
ATOM 1797 N ALA A1062 55.115 34.835 -72.483 1.00138.26 N
ANISOU 1797 N ALA A1062 11562 23316 17655 -1168 343 -3148 N
ATOM 1798 CA ALA A1062 55.553 34.103 -73.662 1.00138.89 C
ANISOU 1798 CA ALA A1062 11793 23385 17596 -1348 639 -2672 C
ATOM 1799 C ALA A1062 54.991 34.693 -74.946 1.00143.03 C
ANISOU 1799 C ALA A1062 12187 23793 18365 -1388 317 -2682 C
ATOM 1800 O ALA A1062 55.203 34.119 -76.021 1.00139.62 O
ANISOU 1800 O ALA A1062 11869 23399 17780 -1562 562 -2336 O
ATOM 1801 CB ALA A1062 55.154 32.628 -73.550 1.00136.37 C
ANISOU 1801 CB ALA A1062 11818 23273 16724 -1530 1169 -2685 C
ATOM 1802 N GLU A1063 54.256 35.807 -74.842 1.00150.40 N
ANISOU 1802 N GLU A1063 12936 24568 19640 -1210 -240 -3081 N
ATOM 1803 CA GLU A1063 53.663 36.450 -76.010 1.00156.23 C
ANISOU 1803 CA GLU A1063 13609 25114 20639 -1220 -678 -3123 C
ATOM 1804 C GLU A1063 54.727 36.910 -76.999 1.00162.12 C
ANISOU 1804 C GLU A1063 14325 25651 21621 -1378 -915 -2550 C
ATOM 1805 O GLU A1063 54.562 36.749 -78.212 1.00164.05 O
ANISOU 1805 O GLU A1063 14603 25897 21830 -1573 -944 -2359 O
ATOM 1806 CB GLU A1063 52.791 37.628 -75.574 1.00157.26 C
ANISOU 1806 CB GLU A1063 13641 25031 21080 -910 -1277 -3632 C
ATOM 1807 N LYS A1064 55.819 37.500 -76.501 1.00166.76 N
ANISOU 1807 N LYS A1064 14843 26100 22417 -1344 -1106 -2260 N
ATOM 1808 CA LYS A1064 56.918 37.893 -77.380 1.00164.64 C
ANISOU 1808 CA LYS A1064 14550 25724 22284 -1569 -1283 -1634 C
ATOM 1809 C LYS A1064 57.596 36.675 -77.996 1.00161.38 C
ANISOU 1809 C LYS A1064 14396 25493 21429 -1723 -524 -1085 C
ATOM 1810 O LYS A1064 57.988 36.703 -79.170 1.00170.52 O
ANISOU 1810 O LYS A1064 15788 26482 22519 -1887 -511 -590 O
ATOM 1811 CB LYS A1064 57.929 38.740 -76.609 1.00168.25 C
ANISOU 1811 CB LYS A1064 14883 26025 23019 -1534 -1646 -1429 C
ATOM 1812 N LEU A1065 57.760 35.606 -77.211 1.00145.94 N
ANISOU 1812 N LEU A1065 12434 23875 19141 -1659 83 -1173 N
ATOM 1813 CA LEU A1065 58.282 34.351 -77.745 1.00132.61 C
ANISOU 1813 CA LEU A1065 11061 22336 16988 -1718 769 -755 C
ATOM 1814 C LEU A1065 57.359 33.792 -78.821 1.00126.44 C
ANISOU 1814 C LEU A1065 10591 21485 15965 -1825 917 -820 C
ATOM 1815 O LEU A1065 57.822 33.290 -79.854 1.00122.04 O
ANISOU 1815 O LEU A1065 10353 20863 15155 -1890 1203 -358 O
ATOM 1816 CB LEU A1065 58.467 33.351 -76.602 1.00125.04 C
ANISOU 1816 CB LEU A1065 10261 21527 15720 -1585 1229 -901 C
ATOM 1817 CG LEU A1065 58.986 31.934 -76.850 1.00120.44 C
ANISOU 1817 CG LEU A1065 10154 20970 14636 -1531 1844 -577 C
ATOM 1818 CD1 LEU A1065 59.894 31.545 -75.700 1.00119.01 C
ANISOU 1818 CD1 LEU A1065 10074 20750 14395 -1354 1987 -481 C
ATOM 1819 CD2 LEU A1065 57.845 30.930 -76.968 1.00119.70 C
ANISOU 1819 CD2 LEU A1065 10415 20899 14167 -1625 2087 -897 C
ATOM 1820 N PHE A1066 56.047 33.885 -78.596 1.00128.53 N
ANISOU 1820 N PHE A1066 10750 21799 16289 -1837 711 -1405 N
ATOM 1821 CA PHE A1066 55.079 33.433 -79.587 1.00130.52 C
ANISOU 1821 CA PHE A1066 11261 21987 16345 -1969 767 -1497 C
ATOM 1822 C PHE A1066 55.169 34.264 -80.861 1.00139.24 C
ANISOU 1822 C PHE A1066 12499 22717 17689 -2040 327 -1181 C
ATOM 1823 O PHE A1066 55.070 33.725 -81.970 1.00142.69 O
ANISOU 1823 O PHE A1066 13315 23042 17859 -2169 533 -894 O
ATOM 1824 CB PHE A1066 53.673 33.503 -78.998 1.00125.54 C
ANISOU 1824 CB PHE A1066 10354 21577 15766 -1967 576 -2214 C
ATOM 1825 CG PHE A1066 52.610 33.004 -79.919 1.00122.83 C
ANISOU 1825 CG PHE A1066 10229 21225 15215 -2137 613 -2338 C
ATOM 1826 CD1 PHE A1066 52.386 31.648 -80.051 1.00121.04 C
ANISOU 1826 CD1 PHE A1066 10365 21171 14454 -2332 1177 -2245 C
ATOM 1827 CD2 PHE A1066 51.834 33.886 -80.653 1.00125.28 C
ANISOU 1827 CD2 PHE A1066 10429 21319 15853 -2107 28 -2543 C
ATOM 1828 CE1 PHE A1066 51.409 31.180 -80.890 1.00122.43 C
ANISOU 1828 CE1 PHE A1066 10766 21329 14422 -2531 1178 -2339 C
ATOM 1829 CE2 PHE A1066 50.857 33.421 -81.505 1.00127.00 C
ANISOU 1829 CE2 PHE A1066 10840 21533 15881 -2276 36 -2646 C
ATOM 1830 CZ PHE A1066 50.641 32.064 -81.623 1.00125.10 C
ANISOU 1830 CZ PHE A1066 10939 21490 15104 -2507 622 -2537 C
ATOM 1831 N ASN A1067 55.327 35.583 -80.714 1.00143.69 N
ANISOU 1831 N ASN A1067 12810 23057 18728 -1975 -325 -1238 N
ATOM 1832 CA ASN A1067 55.494 36.459 -81.868 1.00146.12 C
ANISOU 1832 CA ASN A1067 13295 22970 19255 -2105 -829 -893 C
ATOM 1833 C ASN A1067 56.757 36.113 -82.642 1.00140.10 C
ANISOU 1833 C ASN A1067 12793 22199 18241 -2270 -450 -131 C
ATOM 1834 O ASN A1067 56.755 36.129 -83.876 1.00139.67 O
ANISOU 1834 O ASN A1067 13051 21957 18062 -2447 -494 209 O
ATOM 1835 CB ASN A1067 55.501 37.924 -81.434 1.00157.04 C
ANISOU 1835 CB ASN A1067 14429 24076 21164 -2015 -1661 -1091 C
ATOM 1836 CG ASN A1067 54.117 38.429 -81.069 1.00164.85 C
ANISOU 1836 CG ASN A1067 15198 25029 22407 -1796 -2169 -1860 C
ATOM 1837 OD1 ASN A1067 53.408 38.983 -81.909 1.00168.49 O
ANISOU 1837 OD1 ASN A1067 15791 25190 23038 -1812 -2692 -1974 O
ATOM 1838 ND2 ASN A1067 53.726 38.240 -79.815 1.00166.65 N
ANISOU 1838 ND2 ASN A1067 15078 25599 22644 -1580 -2028 -2405 N
ATOM 1839 N GLN A1068 57.851 35.817 -81.934 1.00136.48 N
ANISOU 1839 N GLN A1068 12188 21978 17690 -2206 -88 133 N
ATOM 1840 CA GLN A1068 59.088 35.439 -82.611 1.00132.50 C
ANISOU 1840 CA GLN A1068 11837 21596 16913 -2304 319 818 C
ATOM 1841 C GLN A1068 58.922 34.122 -83.363 1.00130.00 C
ANISOU 1841 C GLN A1068 11918 21410 16065 -2266 970 938 C
ATOM 1842 O GLN A1068 59.412 33.976 -84.490 1.00133.52 O
ANISOU 1842 O GLN A1068 12617 21840 16275 -2379 1140 1405 O
ATOM 1843 CB GLN A1068 60.229 35.342 -81.600 1.00127.13 C
ANISOU 1843 CB GLN A1068 10866 21187 16249 -2189 553 1009 C
ATOM 1844 N ASP A1069 58.201 33.165 -82.770 1.00125.98 N
ANISOU 1844 N ASP A1069 11507 21028 15331 -2136 1308 517 N
ATOM 1845 CA ASP A1069 57.977 31.889 -83.447 1.00126.30 C
ANISOU 1845 CA ASP A1069 12024 21124 14842 -2117 1847 606 C
ATOM 1846 C ASP A1069 57.076 32.041 -84.670 1.00125.36 C
ANISOU 1846 C ASP A1069 12209 20739 14683 -2304 1606 585 C
ATOM 1847 O ASP A1069 57.343 31.438 -85.714 1.00125.67 O
ANISOU 1847 O ASP A1069 12669 20736 14343 -2335 1916 929 O
ATOM 1848 CB ASP A1069 57.398 30.860 -82.478 1.00130.81 C
ANISOU 1848 CB ASP A1069 12675 21872 15156 -2032 2185 188 C
ATOM 1849 CG ASP A1069 58.434 30.316 -81.517 1.00137.84 C
ANISOU 1849 CG ASP A1069 13478 23000 15897 -1828 2562 325 C
ATOM 1850 OD1 ASP A1069 59.214 31.109 -80.952 1.00141.77 O
ANISOU 1850 OD1 ASP A1069 13578 23564 16725 -1764 2358 455 O
ATOM 1851 OD2 ASP A1069 58.465 29.082 -81.329 1.00139.90 O
ANISOU 1851 OD2 ASP A1069 14193 23218 15745 -1698 2953 303 O
ATOM 1852 N VAL A1070 56.013 32.846 -84.574 1.00122.88 N
ANISOU 1852 N VAL A1070 11698 20250 14742 -2397 1036 169 N
ATOM 1853 CA VAL A1070 55.154 33.021 -85.745 1.00121.91 C
ANISOU 1853 CA VAL A1070 11863 19856 14601 -2568 746 150 C
ATOM 1854 C VAL A1070 55.847 33.877 -86.802 1.00123.69 C
ANISOU 1854 C VAL A1070 12212 19835 14949 -2719 435 668 C
ATOM 1855 O VAL A1070 55.604 33.699 -88.000 1.00125.26 O
ANISOU 1855 O VAL A1070 12814 19851 14929 -2874 431 893 O
ATOM 1856 CB VAL A1070 53.767 33.583 -85.363 1.00122.96 C
ANISOU 1856 CB VAL A1070 11725 19920 15074 -2572 208 -487 C
ATOM 1857 CG1 VAL A1070 53.079 32.672 -84.355 1.00121.06 C
ANISOU 1857 CG1 VAL A1070 11351 20028 14620 -2520 569 -960 C
ATOM 1858 CG2 VAL A1070 53.849 35.005 -84.839 1.00126.02 C
ANISOU 1858 CG2 VAL A1070 11694 20159 16030 -2479 -479 -666 C
ATOM 1859 N ASP A1071 56.729 34.794 -86.389 1.00124.75 N
ANISOU 1859 N ASP A1071 12038 19971 15392 -2726 161 891 N
ATOM 1860 CA ASP A1071 57.548 35.537 -87.340 1.00128.56 C
ANISOU 1860 CA ASP A1071 12638 20306 15904 -2965 -81 1472 C
ATOM 1861 C ASP A1071 58.471 34.600 -88.107 1.00128.11 C
ANISOU 1861 C ASP A1071 12861 20515 15299 -2978 629 1998 C
ATOM 1862 O ASP A1071 58.572 34.678 -89.338 1.00129.77 O
ANISOU 1862 O ASP A1071 13405 20611 15290 -3189 608 2358 O
ATOM 1863 CB ASP A1071 58.350 36.608 -86.598 1.00133.53 C
ANISOU 1863 CB ASP A1071 12874 20933 16928 -3013 -498 1614 C
ATOM 1864 CG ASP A1071 59.309 37.354 -87.501 1.00143.88 C
ANISOU 1864 CG ASP A1071 14277 22176 18213 -3360 -729 2283 C
ATOM 1865 OD1 ASP A1071 58.840 38.127 -88.363 1.00149.52 O
ANISOU 1865 OD1 ASP A1071 15240 22506 19064 -3617 -1320 2367 O
ATOM 1866 OD2 ASP A1071 60.535 37.172 -87.344 1.00146.95 O
ANISOU 1866 OD2 ASP A1071 14481 22923 18429 -3397 -340 2730 O
ATOM 1867 N ALA A1072 59.139 33.691 -87.388 1.00125.91 N
ANISOU 1867 N ALA A1072 12473 20599 14769 -2723 1248 2021 N
ATOM 1868 CA ALA A1072 59.993 32.700 -88.037 1.00122.67 C
ANISOU 1868 CA ALA A1072 12330 20473 13804 -2604 1932 2429 C
ATOM 1869 C ALA A1072 59.180 31.775 -88.935 1.00119.40 C
ANISOU 1869 C ALA A1072 12495 19900 12973 -2587 2183 2315 C
ATOM 1870 O ALA A1072 59.650 31.362 -90.000 1.00120.85 O
ANISOU 1870 O ALA A1072 13019 20163 12735 -2600 2501 2689 O
ATOM 1871 CB ALA A1072 60.757 31.896 -86.986 1.00119.92 C
ANISOU 1871 CB ALA A1072 11786 20483 13297 -2270 2446 2390 C
ATOM 1872 N ALA A1073 57.951 31.450 -88.525 1.00116.58 N
ANISOU 1872 N ALA A1073 12246 19349 12698 -2579 2035 1800 N
ATOM 1873 CA ALA A1073 57.093 30.598 -89.341 1.00112.84 C
ANISOU 1873 CA ALA A1073 12331 18701 11841 -2629 2196 1687 C
ATOM 1874 C ALA A1073 56.694 31.286 -90.642 1.00112.83 C
ANISOU 1874 C ALA A1073 12576 18399 11896 -2910 1785 1889 C
ATOM 1875 O ALA A1073 56.736 30.664 -91.707 1.00110.89 O
ANISOU 1875 O ALA A1073 12847 18091 11196 -2945 2056 2130 O
ATOM 1876 CB ALA A1073 55.852 30.190 -88.549 1.00109.55 C
ANISOU 1876 CB ALA A1073 11877 18231 11515 -2642 2081 1102 C
ATOM 1877 N VAL A1074 56.312 32.567 -90.576 1.00115.44 N
ANISOU 1877 N VAL A1074 12594 18511 12756 -3098 1093 1787 N
ATOM 1878 CA VAL A1074 55.981 33.320 -91.788 1.00118.45 C
ANISOU 1878 CA VAL A1074 13241 18556 13210 -3390 603 2004 C
ATOM 1879 C VAL A1074 57.201 33.438 -92.694 1.00124.02 C
ANISOU 1879 C VAL A1074 14119 19405 13596 -3530 863 2664 C
ATOM 1880 O VAL A1074 57.101 33.270 -93.918 1.00126.30 O
ANISOU 1880 O VAL A1074 14876 19558 13553 -3709 902 2930 O
ATOM 1881 CB VAL A1074 55.405 34.704 -91.426 1.00115.55 C
ANISOU 1881 CB VAL A1074 12532 17892 13480 -3506 -271 1741 C
ATOM 1882 CG1 VAL A1074 55.202 35.554 -92.674 1.00113.74 C
ANISOU 1882 CG1 VAL A1074 12631 17266 13318 -3833 -854 2029 C
ATOM 1883 CG2 VAL A1074 54.084 34.555 -90.709 1.00114.29 C
ANISOU 1883 CG2 VAL A1074 12186 17677 13562 -3354 -509 1053 C
ATOM 1884 N ARG A1075 58.373 33.709 -92.108 1.00128.92 N
ANISOU 1884 N ARG A1075 14347 20355 14281 -3466 1058 2938 N
ATOM 1885 CA ARG A1075 59.592 33.830 -92.903 1.00137.59 C
ANISOU 1885 CA ARG A1075 15488 21742 15048 -3618 1343 3568 C
ATOM 1886 C ARG A1075 59.984 32.503 -93.549 1.00141.87 C
ANISOU 1886 C ARG A1075 16427 22569 14907 -3368 2134 3726 C
ATOM 1887 O ARG A1075 60.529 32.494 -94.659 1.00146.13 O
ANISOU 1887 O ARG A1075 17214 23256 15052 -3528 2327 4162 O
ATOM 1888 CB ARG A1075 60.726 34.381 -92.037 1.00138.07 C
ANISOU 1888 CB ARG A1075 14974 22147 15338 -3607 1358 3799 C
ATOM 1889 CG ARG A1075 60.510 35.837 -91.628 1.00140.19 C
ANISOU 1889 CG ARG A1075 14964 22089 16214 -3914 488 3759 C
ATOM 1890 CD ARG A1075 61.632 36.372 -90.753 1.00142.36 C
ANISOU 1890 CD ARG A1075 14708 22682 16700 -3946 464 4006 C
ATOM 1891 NE ARG A1075 61.393 37.758 -90.356 1.00144.00 N
ANISOU 1891 NE ARG A1075 14751 22499 17462 -4225 -440 3946 N
ATOM 1892 CZ ARG A1075 61.812 38.818 -91.039 1.00149.53 C
ANISOU 1892 CZ ARG A1075 15531 23046 18238 -4726 -988 4417 C
ATOM 1893 NH1 ARG A1075 62.498 38.659 -92.163 1.00152.06 N
ANISOU 1893 NH1 ARG A1075 16029 23649 18097 -5035 -666 4993 N
ATOM 1894 NH2 ARG A1075 61.546 40.040 -90.598 1.00152.27 N
ANISOU 1894 NH2 ARG A1075 15812 22958 19086 -4925 -1883 4307 N
ATOM 1895 N GLY A1076 59.715 31.378 -92.880 1.00141.86 N
ANISOU 1895 N GLY A1076 16532 22647 14722 -2984 2570 3373 N
ATOM 1896 CA GLY A1076 59.981 30.084 -93.483 1.00138.31 C
ANISOU 1896 CA GLY A1076 16580 22362 13608 -2698 3224 3461 C
ATOM 1897 C GLY A1076 58.972 29.687 -94.539 1.00131.88 C
ANISOU 1897 C GLY A1076 16425 21165 12517 -2849 3115 3365 C
ATOM 1898 O GLY A1076 59.321 28.993 -95.499 1.00134.67 O
ANISOU 1898 O GLY A1076 17278 21490 12399 -2667 3471 3520 O
ATOM 1899 N ILE A1077 57.714 30.110 -94.381 1.00123.43 N
ANISOU 1899 N ILE A1077 15382 19685 11832 -3078 2560 3007 N
ATOM 1900 CA ILE A1077 56.696 29.830 -95.391 1.00116.03 C
ANISOU 1900 CA ILE A1077 15033 18373 10681 -3271 2366 2921 C
ATOM 1901 C ILE A1077 56.972 30.635 -96.655 1.00122.45 C
ANISOU 1901 C ILE A1077 16038 19066 11421 -3600 2094 3356 C
ATOM 1902 O ILE A1077 56.914 30.107 -97.773 1.00127.76 O
ANISOU 1902 O ILE A1077 17298 19651 11591 -3652 2299 3551 O
ATOM 1903 CB ILE A1077 55.287 30.115 -94.838 1.00107.06 C
ANISOU 1903 CB ILE A1077 13760 16926 9994 -3410 1821 2400 C
ATOM 1904 CG1 ILE A1077 54.903 29.114 -93.747 1.00102.84 C
ANISOU 1904 CG1 ILE A1077 13176 16536 9362 -3180 2149 1995 C
ATOM 1905 CG2 ILE A1077 54.249 30.085 -95.945 1.00105.02 C
ANISOU 1905 CG2 ILE A1077 14019 16276 9609 -3672 1477 2354 C
ATOM 1906 CD1 ILE A1077 53.571 29.429 -93.102 1.00 90.55 C
ANISOU 1906 CD1 ILE A1077 11342 14839 8222 -3325 1662 1465 C
ATOM 1907 N LEU A1078 57.292 31.924 -96.494 1.00122.87 N
ANISOU 1907 N LEU A1078 15647 19099 11940 -3852 1600 3527 N
ATOM 1908 CA LEU A1078 57.593 32.784 -97.635 1.00123.05 C
ANISOU 1908 CA LEU A1078 15862 19001 11891 -4261 1264 3983 C
ATOM 1909 C LEU A1078 58.846 32.351 -98.391 1.00129.80 C
ANISOU 1909 C LEU A1078 16859 20334 12125 -4235 1912 4510 C
ATOM 1910 O LEU A1078 59.027 32.754 -99.546 1.00137.21 O
ANISOU 1910 O LEU A1078 18117 21223 12793 -4587 1782 4897 O
ATOM 1911 CB LEU A1078 57.741 34.234 -97.168 1.00119.41 C
ANISOU 1911 CB LEU A1078 14929 18401 12040 -4545 552 4060 C
ATOM 1912 N ARG A1079 59.710 31.545 -97.776 1.00156.27 N
ANISOU 1912 N ARG A1079 24261 18905 16210 347 9664 -763 N
ATOM 1913 CA ARG A1079 60.912 31.024 -98.417 1.00160.18 C
ANISOU 1913 CA ARG A1079 24471 19437 16954 180 10106 -995 C
ATOM 1914 C ARG A1079 60.766 29.537 -98.734 1.00159.68 C
ANISOU 1914 C ARG A1079 24207 19421 17043 441 10091 -1198 C
ATOM 1915 O ARG A1079 61.718 28.762 -98.620 1.00162.09 O
ANISOU 1915 O ARG A1079 23945 19817 17826 446 10348 -1407 O
ATOM 1916 CB ARG A1079 62.140 31.268 -97.543 1.00160.90 C
ANISOU 1916 CB ARG A1079 23869 19658 17609 6 10347 -1045 C
ATOM 1917 N ASN A1080 59.565 29.125 -99.138 1.00156.00 N
ANISOU 1917 N ASN A1080 24208 18877 16188 664 9772 -1138 N
ATOM 1918 CA ASN A1080 59.279 27.743 -99.503 1.00155.65 C
ANISOU 1918 CA ASN A1080 24079 18840 16220 916 9722 -1322 C
ATOM 1919 C ASN A1080 58.556 27.734-100.841 1.00153.00 C
ANISOU 1919 C ASN A1080 24518 18349 15265 881 9662 -1324 C
ATOM 1920 O ASN A1080 57.608 28.501-101.038 1.00148.65 O
ANISOU 1920 O ASN A1080 24530 17698 14251 868 9367 -1092 O
ATOM 1921 CB ASN A1080 58.436 27.042 -98.430 1.00157.20 C
ANISOU 1921 CB ASN A1080 23975 19123 16631 1272 9311 -1231 C
ATOM 1922 CG ASN A1080 58.371 25.539 -98.630 1.00160.22 C
ANISOU 1922 CG ASN A1080 24109 19506 17261 1527 9276 -1441 C
ATOM 1923 OD1 ASN A1080 57.584 25.039 -99.434 1.00160.91 O
ANISOU 1923 OD1 ASN A1080 24695 19488 16957 1652 9137 -1480 O
ATOM 1924 ND2 ASN A1080 59.201 24.809 -97.893 1.00160.58 N
ANISOU 1924 ND2 ASN A1080 23367 19655 17991 1592 9336 -1567 N
ATOM 1925 N ALA A1081 59.019 26.878-101.759 1.00155.33 N
ANISOU 1925 N ALA A1081 24830 18620 15569 861 9936 -1588 N
ATOM 1926 CA ALA A1081 58.509 26.885-103.129 1.00156.75 C
ANISOU 1926 CA ALA A1081 25730 18667 15161 759 9942 -1614 C
ATOM 1927 C ALA A1081 57.043 26.469-103.198 1.00151.69 C
ANISOU 1927 C ALA A1081 25527 17943 14165 1022 9435 -1473 C
ATOM 1928 O ALA A1081 56.267 27.047-103.968 1.00152.00 O
ANISOU 1928 O ALA A1081 26243 17856 13656 923 9236 -1305 O
ATOM 1929 CB ALA A1081 59.364 25.975-104.010 1.00163.05 C
ANISOU 1929 CB ALA A1081 26388 19480 16082 696 10362 -1967 C
ATOM 1930 N LYS A1082 56.643 25.474-102.406 1.00148.53 N
ANISOU 1930 N LYS A1082 24748 17605 14083 1356 9202 -1522 N
ATOM 1931 CA LYS A1082 55.263 25.005-102.436 1.00144.58 C
ANISOU 1931 CA LYS A1082 24633 17039 13263 1622 8710 -1387 C
ATOM 1932 C LYS A1082 54.326 25.832-101.562 1.00144.21 C
ANISOU 1932 C LYS A1082 24694 17020 13079 1735 8268 -1046 C
ATOM 1933 O LYS A1082 53.109 25.780-101.768 1.00144.83 O
ANISOU 1933 O LYS A1082 25225 17029 12774 1893 7830 -873 O
ATOM 1934 CB LYS A1082 55.197 23.535-102.010 1.00139.25 C
ANISOU 1934 CB LYS A1082 23540 16402 12968 1945 8641 -1587 C
ATOM 1935 CG LYS A1082 55.926 22.576-102.940 1.00142.75 C
ANISOU 1935 CG LYS A1082 23933 16782 13524 1894 9011 -1956 C
ATOM 1936 CD LYS A1082 55.312 22.588-104.333 1.00145.81 C
ANISOU 1936 CD LYS A1082 25104 17033 13265 1765 8951 -1977 C
ATOM 1937 CE LYS A1082 56.077 21.686-105.290 1.00149.33 C
ANISOU 1937 CE LYS A1082 25511 17436 13794 1694 9354 -2372 C
ATOM 1938 NZ LYS A1082 57.469 22.160-105.523 1.00153.78 N
ANISOU 1938 NZ LYS A1082 25748 18083 14601 1416 9901 -2535 N
ATOM 1939 N LEU A1083 54.856 26.601-100.606 1.00141.98 N
ANISOU 1939 N LEU A1083 24008 16840 13098 1655 8361 -950 N
ATOM 1940 CA LEU A1083 54.028 27.320 -99.644 1.00133.29 C
ANISOU 1940 CA LEU A1083 22834 15794 12015 1760 7838 -654 C
ATOM 1941 C LEU A1083 53.857 28.801 -99.962 1.00132.73 C
ANISOU 1941 C LEU A1083 23316 15597 11516 1545 7922 -467 C
ATOM 1942 O LEU A1083 52.900 29.417 -99.472 1.00133.05 O
ANISOU 1942 O LEU A1083 23491 15620 11442 1656 7436 -227 O
ATOM 1943 CB LEU A1083 54.622 27.189 -98.235 1.00128.24 C
ANISOU 1943 CB LEU A1083 21333 15357 12037 1809 7744 -650 C
ATOM 1944 CG LEU A1083 54.821 25.794 -97.639 1.00126.31 C
ANISOU 1944 CG LEU A1083 20419 15242 12333 2017 7567 -776 C
ATOM 1945 CD1 LEU A1083 55.314 25.894 -96.206 1.00124.85 C
ANISOU 1945 CD1 LEU A1083 19460 15256 12719 2014 7408 -700 C
ATOM 1946 CD2 LEU A1083 53.528 25.013 -97.684 1.00123.18 C
ANISOU 1946 CD2 LEU A1083 20188 14837 11778 2287 6982 -665 C
ATOM 1947 N LYS A1084 54.736 29.380-100.788 1.00135.46 N
ANISOU 1947 N LYS A1084 23852 15851 11765 1209 8327 -552 N
ATOM 1948 CA LYS A1084 54.657 30.819-101.043 1.00135.98 C
ANISOU 1948 CA LYS A1084 24349 15777 11542 971 8316 -355 C
ATOM 1949 C LYS A1084 53.455 31.223-101.898 1.00136.25 C
ANISOU 1949 C LYS A1084 25140 15611 11019 999 7938 -153 C
ATOM 1950 O LYS A1084 52.777 32.196-101.523 1.00132.22 O
ANISOU 1950 O LYS A1084 24880 15005 10354 1033 7644 81 O
ATOM 1951 CB LYS A1084 55.981 31.319-101.635 1.00142.52 C
ANISOU 1951 CB LYS A1084 25126 16581 12445 594 8848 -486 C
ATOM 1952 N PRO A1085 53.145 30.580-103.048 1.00138.30 N
ANISOU 1952 N PRO A1085 25793 15786 10968 977 7917 -228 N
ATOM 1953 CA PRO A1085 51.974 31.049-103.819 1.00138.47 C
ANISOU 1953 CA PRO A1085 26520 15607 10485 984 7505 1 C
ATOM 1954 C PRO A1085 50.656 30.882-103.080 1.00135.89 C
ANISOU 1954 C PRO A1085 26206 15295 10130 1344 6919 196 C
ATOM 1955 O PRO A1085 49.808 31.790-103.108 1.00137.25 O
ANISOU 1955 O PRO A1085 26766 15318 10067 1368 6561 449 O
ATOM 1956 CB PRO A1085 52.023 30.195-105.094 1.00141.02 C
ANISOU 1956 CB PRO A1085 27153 15882 10544 889 7633 -165 C
ATOM 1957 CG PRO A1085 53.409 29.743-105.203 1.00143.73 C
ANISOU 1957 CG PRO A1085 27075 16354 11184 721 8214 -463 C
ATOM 1958 CD PRO A1085 53.860 29.528-103.803 1.00141.16 C
ANISOU 1958 CD PRO A1085 26034 16204 11396 904 8273 -519 C
ATOM 1959 N VAL A1086 50.473 29.748-102.398 1.00134.35 N
ANISOU 1959 N VAL A1086 25578 15279 10191 1629 6809 86 N
ATOM 1960 CA VAL A1086 49.251 29.532-101.631 1.00129.29 C
ANISOU 1960 CA VAL A1086 24890 14701 9533 1975 6256 272 C
ATOM 1961 C VAL A1086 49.171 30.514-100.463 1.00128.70 C
ANISOU 1961 C VAL A1086 24454 14693 9752 2016 6064 420 C
ATOM 1962 O VAL A1086 48.097 31.054-100.178 1.00128.06 O
ANISOU 1962 O VAL A1086 24537 14554 9565 2169 5572 640 O
ATOM 1963 CB VAL A1086 49.138 28.055-101.188 1.00124.08 C
ANISOU 1963 CB VAL A1086 23695 14217 9234 2214 6064 127 C
ATOM 1964 CG1 VAL A1086 50.342 27.608-100.380 1.00121.63 C
ANISOU 1964 CG1 VAL A1086 22633 14089 9494 2178 6421 -85 C
ATOM 1965 CG2 VAL A1086 47.847 27.814-100.414 1.00119.82 C
ANISOU 1965 CG2 VAL A1086 22943 13768 8816 2512 5352 339 C
ATOM 1966 N TYR A1087 50.298 30.781 -99.782 1.00132.17 N
ANISOU 1966 N TYR A1087 24402 15247 10569 1875 6445 293 N
ATOM 1967 CA TYR A1087 50.272 31.730 -98.671 1.00133.01 C
ANISOU 1967 CA TYR A1087 24188 15413 10937 1886 6280 406 C
ATOM 1968 C TYR A1087 49.952 33.139 -99.161 1.00139.50 C
ANISOU 1968 C TYR A1087 25642 15980 11382 1735 6266 588 C
ATOM 1969 O TYR A1087 49.254 33.898 -98.477 1.00135.32 O
ANISOU 1969 O TYR A1087 25076 15421 10918 1858 5889 738 O
ATOM 1970 CB TYR A1087 51.605 31.711 -97.920 1.00130.86 C
ANISOU 1970 CB TYR A1087 23290 15302 11128 1728 6695 236 C
ATOM 1971 CG TYR A1087 51.645 32.597 -96.687 1.00130.06 C
ANISOU 1971 CG TYR A1087 22811 15288 11317 1722 6524 320 C
ATOM 1972 CD1 TYR A1087 51.216 32.120 -95.454 1.00127.33 C
ANISOU 1972 CD1 TYR A1087 21858 15181 11339 1939 6120 343 C
ATOM 1973 CD2 TYR A1087 52.128 33.901 -96.752 1.00131.97 C
ANISOU 1973 CD2 TYR A1087 23312 15375 11454 1477 6769 371 C
ATOM 1974 CE1 TYR A1087 51.254 32.920 -94.323 1.00125.16 C
ANISOU 1974 CE1 TYR A1087 21256 15003 11296 1916 5978 391 C
ATOM 1975 CE2 TYR A1087 52.166 34.709 -95.627 1.00129.76 C
ANISOU 1975 CE2 TYR A1087 22707 15161 11435 1468 6611 418 C
ATOM 1976 CZ TYR A1087 51.729 34.213 -94.416 1.00126.05 C
ANISOU 1976 CZ TYR A1087 21645 14943 11306 1689 6225 415 C
ATOM 1977 OH TYR A1087 51.768 35.012 -93.296 1.00122.79 O
ANISOU 1977 OH TYR A1087 20928 14609 11118 1661 6083 435 O
ATOM 1978 N ASP A1088 50.458 33.508-100.343 1.00148.33 N
ANISOU 1978 N ASP A1088 27335 16908 12114 1459 6666 572 N
ATOM 1979 CA ASP A1088 50.141 34.813-100.910 1.00153.44 C
ANISOU 1979 CA ASP A1088 28571 17278 12451 1282 6567 771 C
ATOM 1980 C ASP A1088 48.703 34.902-101.402 1.00150.48 C
ANISOU 1980 C ASP A1088 28700 16737 11740 1481 6001 989 C
ATOM 1981 O ASP A1088 48.163 36.010-101.490 1.00155.52 O
ANISOU 1981 O ASP A1088 29737 17150 12202 1456 5772 1195 O
ATOM 1982 CB ASP A1088 51.095 35.149-102.061 1.00161.56 C
ANISOU 1982 CB ASP A1088 29895 18174 13318 878 6997 695 C
ATOM 1983 CG ASP A1088 52.538 35.271-101.610 1.00164.02 C
ANISOU 1983 CG ASP A1088 29719 18622 13977 648 7538 511 C
ATOM 1984 OD1 ASP A1088 52.791 35.183-100.390 1.00160.86 O
ANISOU 1984 OD1 ASP A1088 28777 18397 13944 784 7565 457 O
ATOM 1985 OD2 ASP A1088 53.419 35.456-102.478 1.00167.26 O
ANISOU 1985 OD2 ASP A1088 30276 18977 14298 322 7927 424 O
ATOM 1986 N SER A1089 48.063 33.773-101.708 1.00143.30 N
ANISOU 1986 N SER A1089 27773 15913 10760 1679 5750 955 N
ATOM 1987 CA SER A1089 46.708 33.816-102.242 1.00136.61 C
ANISOU 1987 CA SER A1089 27373 14907 9627 1843 5188 1166 C
ATOM 1988 C SER A1089 45.620 33.693-101.183 1.00129.46 C
ANISOU 1988 C SER A1089 26183 14122 8882 2230 4671 1296 C
ATOM 1989 O SER A1089 44.459 33.991-101.482 1.00122.95 O
ANISOU 1989 O SER A1089 25703 13147 7866 2377 4179 1506 O
ATOM 1990 CB SER A1089 46.507 32.692-103.260 1.00136.22 C
ANISOU 1990 CB SER A1089 27509 14860 9389 1821 5140 1073 C
ATOM 1991 OG SER A1089 46.490 31.432-102.608 1.00132.02 O
ANISOU 1991 OG SER A1089 26497 14581 9085 2064 5115 929 O
ATOM 1992 N LEU A1090 45.956 33.284 -99.964 1.00125.49 N
ANISOU 1992 N LEU A1090 24919 13890 8871 2362 4682 1162 N
ATOM 1993 CA LEU A1090 44.949 32.989 -98.956 1.00125.95 C
ANISOU 1993 CA LEU A1090 24526 14124 9205 2687 4143 1240 C
ATOM 1994 C LEU A1090 44.584 34.216 -98.124 1.00132.26 C
ANISOU 1994 C LEU A1090 25218 14870 10164 2756 3943 1339 C
ATOM 1995 O LEU A1090 45.320 35.203 -98.058 1.00130.56 O
ANISOU 1995 O LEU A1090 25110 14527 9968 2549 4254 1312 O
ATOM 1996 CB LEU A1090 45.425 31.869 -98.030 1.00119.26 C
ANISOU 1996 CB LEU A1090 22913 13610 8790 2780 4204 1065 C
ATOM 1997 CG LEU A1090 45.357 30.447 -98.591 1.00117.63 C
ANISOU 1997 CG LEU A1090 22689 13478 8528 2846 4178 980 C
ATOM 1998 CD1 LEU A1090 45.758 29.437 -97.530 1.00116.27 C
ANISOU 1998 CD1 LEU A1090 21719 13612 8847 2950 4153 850 C
ATOM 1999 CD2 LEU A1090 43.976 30.143 -99.148 1.00111.92 C
ANISOU 1999 CD2 LEU A1090 22353 12661 7509 3039 3649 1166 C
ATOM 2000 N ASP A1091 43.418 34.131 -97.486 1.00142.76 N
ANISOU 2000 N ASP A1091 26326 16299 11617 3050 3418 1446 N
ATOM 2001 CA ASP A1091 42.954 35.140 -96.548 1.00151.86 C
ANISOU 2001 CA ASP A1091 27274 17449 12976 3175 3193 1492 C
ATOM 2002 C ASP A1091 43.842 35.131 -95.299 1.00148.75 C
ANISOU 2002 C ASP A1091 26203 17329 12987 3104 3443 1306 C
ATOM 2003 O ASP A1091 44.635 34.212 -95.074 1.00155.86 O
ANISOU 2003 O ASP A1091 26719 18446 14056 3016 3690 1175 O
ATOM 2004 CB ASP A1091 41.489 34.878 -96.185 1.00160.59 C
ANISOU 2004 CB ASP A1091 28248 18647 14124 3509 2597 1625 C
ATOM 2005 CG ASP A1091 40.785 36.100 -95.612 1.00168.51 C
ANISOU 2005 CG ASP A1091 29266 19525 15234 3658 2335 1692 C
ATOM 2006 OD1 ASP A1091 41.469 37.053 -95.184 1.00174.39 O
ANISOU 2006 OD1 ASP A1091 29976 20182 16102 3519 2594 1602 O
ATOM 2007 OD2 ASP A1091 39.535 36.100 -95.586 1.00171.64 O
ANISOU 2007 OD2 ASP A1091 29698 19907 15612 3917 1861 1826 O
ATOM 2008 N ALA A1092 43.708 36.188 -94.490 1.00143.36 N
ANISOU 2008 N ALA A1092 25383 16617 12470 3139 3365 1294 N
ATOM 2009 CA ALA A1092 44.458 36.284 -93.238 1.00139.13 C
ANISOU 2009 CA ALA A1092 24228 16341 12296 3061 3546 1129 C
ATOM 2010 C ALA A1092 44.133 35.128 -92.297 1.00133.01 C
ANISOU 2010 C ALA A1092 22788 15979 11771 3228 3315 1082 C
ATOM 2011 O ALA A1092 45.034 34.560 -91.666 1.00133.47 O
ANISOU 2011 O ALA A1092 22356 16276 12080 3098 3536 963 O
ATOM 2012 CB ALA A1092 44.174 37.624 -92.559 1.00138.90 C
ANISOU 2012 CB ALA A1092 24218 16190 12367 3099 3439 1113 C
ATOM 2013 N VAL A1093 42.849 34.772 -92.187 1.00130.08 N
ANISOU 2013 N VAL A1093 22383 15695 11348 3502 2851 1192 N
ATOM 2014 CA VAL A1093 42.437 33.633 -91.367 1.00124.16 C
ANISOU 2014 CA VAL A1093 21040 15334 10801 3644 2590 1187 C
ATOM 2015 C VAL A1093 43.018 32.332 -91.915 1.00120.84 C
ANISOU 2015 C VAL A1093 20548 14984 10384 3559 2737 1169 C
ATOM 2016 O VAL A1093 43.459 31.455 -91.158 1.00117.68 O
ANISOU 2016 O VAL A1093 19582 14878 10253 3526 2750 1104 O
ATOM 2017 CB VAL A1093 40.899 33.584 -91.279 1.00122.95 C
ANISOU 2017 CB VAL A1093 20920 15229 10566 3940 2072 1326 C
ATOM 2018 CG1 VAL A1093 40.400 34.646 -90.342 1.00122.23 C
ANISOU 2018 CG1 VAL A1093 20648 15191 10602 4048 1936 1275 C
ATOM 2019 CG2 VAL A1093 40.279 33.814 -92.647 1.00125.98 C
ANISOU 2019 CG2 VAL A1093 22008 15246 10613 4007 1942 1479 C
ATOM 2020 N ARG A1094 43.044 32.189 -93.238 1.00119.64 N
ANISOU 2020 N ARG A1094 20971 14551 9935 3513 2846 1219 N
ATOM 2021 CA ARG A1094 43.593 30.982 -93.835 1.00120.49 C
ANISOU 2021 CA ARG A1094 21053 14692 10036 3441 3012 1159 C
ATOM 2022 C ARG A1094 45.115 30.960 -93.773 1.00121.63 C
ANISOU 2022 C ARG A1094 21007 14847 10361 3185 3553 981 C
ATOM 2023 O ARG A1094 45.710 29.880 -93.661 1.00120.74 O
ANISOU 2023 O ARG A1094 20537 14881 10459 3152 3671 885 O
ATOM 2024 CB ARG A1094 43.081 30.849 -95.265 1.00121.99 C
ANISOU 2024 CB ARG A1094 21943 14596 9813 3459 2949 1253 C
ATOM 2025 CG ARG A1094 41.559 30.795 -95.320 1.00116.04 C
ANISOU 2025 CG ARG A1094 21332 13838 8921 3715 2376 1446 C
ATOM 2026 CD ARG A1094 41.080 30.502 -96.714 1.00112.34 C
ANISOU 2026 CD ARG A1094 21526 13108 8049 3710 2274 1546 C
ATOM 2027 NE ARG A1094 39.646 30.226 -96.786 1.00106.09 N
ANISOU 2027 NE ARG A1094 20809 12335 7163 3951 1697 1738 N
ATOM 2028 CZ ARG A1094 38.723 31.127 -97.110 1.00104.67 C
ANISOU 2028 CZ ARG A1094 21013 11954 6801 4055 1401 1912 C
ATOM 2029 NH1 ARG A1094 39.077 32.374 -97.391 1.00106.96 N
ANISOU 2029 NH1 ARG A1094 21672 11992 6975 3937 1614 1924 N
ATOM 2030 NH2 ARG A1094 37.445 30.778 -97.157 1.00103.99 N
ANISOU 2030 NH2 ARG A1094 20932 11909 6672 4274 875 2084 N
ATOM 2031 N ARG A1095 45.758 32.132 -93.814 1.00124.56 N
ANISOU 2031 N ARG A1095 21582 15059 10688 3003 3868 939 N
ATOM 2032 CA ARG A1095 47.188 32.187 -93.526 1.00125.53 C
ANISOU 2032 CA ARG A1095 21406 15238 11052 2757 4348 781 C
ATOM 2033 C ARG A1095 47.463 31.777 -92.088 1.00116.24 C
ANISOU 2033 C ARG A1095 19452 14406 10310 2785 4226 724 C
ATOM 2034 O ARG A1095 48.466 31.112 -91.808 1.00115.69 O
ANISOU 2034 O ARG A1095 18964 14468 10526 2661 4475 613 O
ATOM 2035 CB ARG A1095 47.745 33.585 -93.792 1.00134.11 C
ANISOU 2035 CB ARG A1095 22863 16086 12007 2542 4661 773 C
ATOM 2036 CG ARG A1095 47.893 33.942 -95.258 1.00142.75 C
ANISOU 2036 CG ARG A1095 24696 16855 12687 2396 4918 816 C
ATOM 2037 CD ARG A1095 48.468 35.339 -95.416 1.00148.51 C
ANISOU 2037 CD ARG A1095 25750 17354 13322 2156 5199 834 C
ATOM 2038 NE ARG A1095 48.638 35.705 -96.818 1.00155.62 N
ANISOU 2038 NE ARG A1095 27375 17959 13796 1968 5449 899 N
ATOM 2039 CZ ARG A1095 49.099 36.880 -97.233 1.00162.00 C
ANISOU 2039 CZ ARG A1095 28597 18516 14438 1720 5693 956 C
ATOM 2040 NH1 ARG A1095 49.437 37.812 -96.353 1.00163.46 N
ANISOU 2040 NH1 ARG A1095 28547 18693 14869 1646 5718 937 N
ATOM 2041 NH2 ARG A1095 49.220 37.124 -98.531 1.00167.04 N
ANISOU 2041 NH2 ARG A1095 29903 18913 14652 1525 5903 1035 N
ATOM 2042 N ALA A1096 46.566 32.138 -91.169 1.00111.34 N
ANISOU 2042 N ALA A1096 18621 13939 9745 2944 3833 801 N
ATOM 2043 CA ALA A1096 46.700 31.703 -89.782 1.00111.79 C
ANISOU 2043 CA ALA A1096 17961 14358 10155 2954 3667 768 C
ATOM 2044 C ALA A1096 46.549 30.189 -89.659 1.00 94.47 C
ANISOU 2044 C ALA A1096 15391 12376 8127 3055 3460 800 C
ATOM 2045 O ALA A1096 47.269 29.549 -88.885 1.00 93.46 O
ANISOU 2045 O ALA A1096 14699 12473 8337 2957 3507 750 O
ATOM 2046 CB ALA A1096 45.676 32.431 -88.913 1.00 94.78 C
ANISOU 2046 CB ALA A1096 15715 12328 7971 3103 3309 823 C
ATOM 2047 N ALA A1097 45.630 29.601 -90.429 1.00 94.35 N
ANISOU 2047 N ALA A1097 15688 12272 7889 3237 3208 895 N
ATOM 2048 CA ALA A1097 45.491 28.143 -90.442 1.00 93.11 C
ANISOU 2048 CA ALA A1097 15237 12259 7880 3325 3007 923 C
ATOM 2049 C ALA A1097 46.743 27.466 -91.005 1.00101.86 C
ANISOU 2049 C ALA A1097 16286 13262 9153 3174 3421 776 C
ATOM 2050 O ALA A1097 47.174 26.416 -90.504 1.00 97.96 O
ANISOU 2050 O ALA A1097 15284 12940 8998 3166 3357 747 O
ATOM 2051 CB ALA A1097 44.251 27.741 -91.240 1.00 93.06 C
ANISOU 2051 CB ALA A1097 15641 12143 7575 3530 2656 1051 C
ATOM 2052 N LEU A1098 47.327 28.045 -92.060 1.00 97.82 N
ANISOU 2052 N LEU A1098 16287 12466 8416 3048 3843 683 N
ATOM 2053 CA LEU A1098 48.569 27.510 -92.616 1.00100.10 C
ANISOU 2053 CA LEU A1098 16512 12661 8859 2894 4308 508 C
ATOM 2054 C LEU A1098 49.714 27.596 -91.609 1.00 99.74 C
ANISOU 2054 C LEU A1098 15846 12792 9259 2727 4531 422 C
ATOM 2055 O LEU A1098 50.517 26.662 -91.489 1.00100.22 O
ANISOU 2055 O LEU A1098 15495 12918 9667 2687 4673 319 O
ATOM 2056 CB LEU A1098 48.932 28.252 -93.902 1.00107.09 C
ANISOU 2056 CB LEU A1098 18085 13239 9363 2752 4731 440 C
ATOM 2057 CG LEU A1098 49.907 27.547 -94.847 1.00110.94 C
ANISOU 2057 CG LEU A1098 18675 13604 9875 2636 5195 244 C
ATOM 2058 CD1 LEU A1098 49.233 26.381 -95.549 1.00112.08 C
ANISOU 2058 CD1 LEU A1098 19011 13694 9881 2811 4961 232 C
ATOM 2059 CD2 LEU A1098 50.478 28.526 -95.860 1.00115.90 C
ANISOU 2059 CD2 LEU A1098 19890 13992 10156 2409 5684 184 C
ATOM 2060 N ILE A1099 49.799 28.709 -90.872 1.00 99.15 N
ANISOU 2060 N ILE A1099 15692 12781 9199 2628 4544 461 N
ATOM 2061 CA ILE A1099 50.804 28.848 -89.819 1.00 99.37 C
ANISOU 2061 CA ILE A1099 15130 12995 9633 2451 4689 402 C
ATOM 2062 C ILE A1099 50.557 27.844 -88.694 1.00100.06 C
ANISOU 2062 C ILE A1099 14558 13397 10065 2541 4281 476 C
ATOM 2063 O ILE A1099 51.508 27.317 -88.106 1.00 96.23 O
ANISOU 2063 O ILE A1099 13534 13039 9989 2418 4385 425 O
ATOM 2064 CB ILE A1099 50.826 30.304 -89.307 1.00100.72 C
ANISOU 2064 CB ILE A1099 15430 13142 9695 2326 4753 420 C
ATOM 2065 CG1 ILE A1099 51.289 31.253 -90.411 1.00104.44 C
ANISOU 2065 CG1 ILE A1099 16512 13290 9881 2176 5188 363 C
ATOM 2066 CG2 ILE A1099 51.734 30.472 -88.092 1.00 98.45 C
ANISOU 2066 CG2 ILE A1099 14528 13075 9803 2135 4821 377 C
ATOM 2067 CD1 ILE A1099 50.985 32.702 -90.107 1.00102.60 C
ANISOU 2067 CD1 ILE A1099 16559 12953 9471 2110 5155 408 C
ATOM 2068 N ASN A1100 49.288 27.541 -88.398 1.00 99.41 N
ANISOU 2068 N ASN A1100 14497 13441 9831 2743 3803 613 N
ATOM 2069 CA ASN A1100 48.966 26.510 -87.411 1.00 95.66 C
ANISOU 2069 CA ASN A1100 13436 13270 9640 2810 3390 713 C
ATOM 2070 C ASN A1100 49.477 25.143 -87.854 1.00 98.07 C
ANISOU 2070 C ASN A1100 13530 13519 10213 2843 3424 670 C
ATOM 2071 O ASN A1100 50.065 24.396 -87.059 1.00104.31 O
ANISOU 2071 O ASN A1100 13726 14486 11420 2769 3320 690 O
ATOM 2072 CB ASN A1100 47.450 26.462 -87.190 1.00 93.64 C
ANISOU 2072 CB ASN A1100 13307 13143 9131 3017 2905 867 C
ATOM 2073 CG ASN A1100 47.040 25.547 -86.037 1.00 91.71 C
ANISOU 2073 CG ASN A1100 12451 13259 9137 3043 2458 1001 C
ATOM 2074 OD1 ASN A1100 47.155 24.322 -86.120 1.00 93.18 O
ANISOU 2074 OD1 ASN A1100 12389 13475 9538 3081 2304 1045 O
ATOM 2075 ND2 ASN A1100 46.516 26.140 -84.973 1.00 85.44 N
ANISOU 2075 ND2 ASN A1100 11430 12733 8300 3018 2240 1064 N
ATOM 2076 N MET A1101 49.252 24.799 -89.127 1.00 93.83 N
ANISOU 2076 N MET A1101 13484 12723 9445 2950 3553 606 N
ATOM 2077 CA MET A1101 49.762 23.530 -89.645 1.00 95.28 C
ANISOU 2077 CA MET A1101 13515 12809 9878 2993 3628 513 C
ATOM 2078 C MET A1101 51.287 23.489 -89.634 1.00100.41 C
ANISOU 2078 C MET A1101 13853 13398 10901 2812 4104 337 C
ATOM 2079 O MET A1101 51.882 22.433 -89.386 1.00 97.75 O
ANISOU 2079 O MET A1101 13049 13093 10999 2821 4068 288 O
ATOM 2080 CB MET A1101 49.217 23.262 -91.045 1.00100.14 C
ANISOU 2080 CB MET A1101 14776 13158 10115 3117 3698 452 C
ATOM 2081 CG MET A1101 48.592 21.881 -91.153 1.00106.15 C
ANISOU 2081 CG MET A1101 15405 13939 10989 3288 3299 508 C
ATOM 2082 SD MET A1101 48.141 21.425 -92.829 1.00114.87 S
ANISOU 2082 SD MET A1101 17247 14718 11681 3396 3413 393 S
ATOM 2083 CE MET A1101 47.133 22.825 -93.249 1.00 97.79 C
ANISOU 2083 CE MET A1101 15740 12489 8925 3409 3339 536 C
ATOM 2084 N VAL A1102 51.937 24.620 -89.924 1.00105.05 N
ANISOU 2084 N VAL A1102 14686 13881 11348 2645 4543 245 N
ATOM 2085 CA VAL A1102 53.398 24.671 -89.871 1.00112.64 C
ANISOU 2085 CA VAL A1102 15318 14805 12676 2452 5005 89 C
ATOM 2086 C VAL A1102 53.884 24.501 -88.432 1.00118.80 C
ANISOU 2086 C VAL A1102 15358 15851 13929 2349 4779 180 C
ATOM 2087 O VAL A1102 54.896 23.838 -88.177 1.00124.80 O
ANISOU 2087 O VAL A1102 15617 16629 15172 2275 4919 102 O
ATOM 2088 CB VAL A1102 53.908 25.975 -90.516 1.00108.67 C
ANISOU 2088 CB VAL A1102 15278 14132 11878 2269 5500 0 C
ATOM 2089 CG1 VAL A1102 55.395 26.175 -90.267 1.00107.76 C
ANISOU 2089 CG1 VAL A1102 14756 14027 12163 2037 5947 -129 C
ATOM 2090 CG2 VAL A1102 53.656 25.931 -92.009 1.00107.34 C
ANISOU 2090 CG2 VAL A1102 15793 13702 11292 2323 5767 -103 C
ATOM 2091 N PHE A1103 53.168 25.089 -87.472 1.00117.50 N
ANISOU 2091 N PHE A1103 15109 15899 13638 2338 4421 342 N
ATOM 2092 CA PHE A1103 53.496 24.898 -86.062 1.00118.39 C
ANISOU 2092 CA PHE A1103 14553 16300 14130 2220 4147 448 C
ATOM 2093 C PHE A1103 53.384 23.433 -85.659 1.00116.54 C
ANISOU 2093 C PHE A1103 13840 16182 14258 2322 3772 538 C
ATOM 2094 O PHE A1103 54.220 22.924 -84.903 1.00114.30 O
ANISOU 2094 O PHE A1103 12960 16015 14452 2196 3713 567 O
ATOM 2095 CB PHE A1103 52.582 25.759 -85.196 1.00118.41 C
ANISOU 2095 CB PHE A1103 14621 16516 13854 2209 3833 576 C
ATOM 2096 CG PHE A1103 53.243 26.986 -84.653 1.00122.89 C
ANISOU 2096 CG PHE A1103 15148 17118 14427 1980 4075 522 C
ATOM 2097 CD1 PHE A1103 53.412 28.105 -85.451 1.00126.94 C
ANISOU 2097 CD1 PHE A1103 16202 17384 14646 1926 4462 417 C
ATOM 2098 CD2 PHE A1103 53.671 27.031 -83.335 1.00124.14 C
ANISOU 2098 CD2 PHE A1103 14747 17554 14869 1797 3888 589 C
ATOM 2099 CE1 PHE A1103 54.010 29.243 -84.949 1.00130.50 C
ANISOU 2099 CE1 PHE A1103 16628 17844 15112 1704 4662 371 C
ATOM 2100 CE2 PHE A1103 54.267 28.167 -82.827 1.00127.05 C
ANISOU 2100 CE2 PHE A1103 15094 17945 15233 1572 4091 530 C
ATOM 2101 CZ PHE A1103 54.435 29.275 -83.635 1.00129.47 C
ANISOU 2101 CZ PHE A1103 15937 17986 15270 1532 4479 416 C
ATOM 2102 N GLN A1104 52.355 22.740 -86.153 1.00118.17 N
ANISOU 2102 N GLN A1104 14299 16344 14258 2540 3486 599 N
ATOM 2103 CA GLN A1104 52.145 21.349 -85.756 1.00119.41 C
ANISOU 2103 CA GLN A1104 14028 16596 14747 2632 3075 708 C
ATOM 2104 C GLN A1104 53.160 20.419 -86.416 1.00126.13 C
ANISOU 2104 C GLN A1104 14700 17214 16010 2658 3347 539 C
ATOM 2105 O GLN A1104 53.773 19.579 -85.745 1.00126.60 O
ANISOU 2105 O GLN A1104 14164 17349 16590 2606 3169 592 O
ATOM 2106 CB GLN A1104 50.719 20.914 -86.090 1.00113.69 C
ANISOU 2106 CB GLN A1104 13630 15888 13679 2841 2675 829 C
ATOM 2107 CG GLN A1104 50.408 19.479 -85.702 1.00109.85 C
ANISOU 2107 CG GLN A1104 12740 15486 13510 2925 2209 966 C
ATOM 2108 CD GLN A1104 49.001 19.066 -86.084 1.00108.91 C
ANISOU 2108 CD GLN A1104 12955 15377 13049 3114 1820 1090 C
ATOM 2109 OE1 GLN A1104 48.280 19.814 -86.745 1.00109.42 O
ANISOU 2109 OE1 GLN A1104 13572 15354 12647 3202 1913 1061 O
ATOM 2110 NE2 GLN A1104 48.601 17.870 -85.666 1.00107.14 N
ANISOU 2110 NE2 GLN A1104 12390 15248 13070 3166 1356 1247 N
ATOM 2111 N MET A1105 53.348 20.550 -87.731 1.00131.15 N
ANISOU 2111 N MET A1105 15844 17563 16425 2733 3774 330 N
ATOM 2112 CA MET A1105 54.188 19.644 -88.510 1.00133.89 C
ANISOU 2112 CA MET A1105 16094 17673 17105 2791 4070 117 C
ATOM 2113 C MET A1105 55.512 20.259 -88.938 1.00139.76 C
ANISOU 2113 C MET A1105 16811 18290 18003 2628 4715 -104 C
ATOM 2114 O MET A1105 56.572 19.669 -88.705 1.00145.71 O
ANISOU 2114 O MET A1105 17041 19008 19314 2579 4866 -203 O
ATOM 2115 CB MET A1105 53.420 19.160 -89.751 1.00134.88 C
ANISOU 2115 CB MET A1105 16814 17576 16860 2984 4081 15 C
ATOM 2116 N GLY A1106 55.483 21.436 -89.550 1.00138.43 N
ANISOU 2116 N GLY A1106 17176 18048 17374 2535 5087 -171 N
ATOM 2117 CA GLY A1106 56.665 22.079 -90.089 1.00138.80 C
ANISOU 2117 CA GLY A1106 17278 17970 17489 2357 5726 -372 C
ATOM 2118 C GLY A1106 56.476 22.443 -91.547 1.00138.44 C
ANISOU 2118 C GLY A1106 17980 17691 16931 2378 6144 -541 C
ATOM 2119 O GLY A1106 55.457 22.146 -92.168 1.00143.47 O
ANISOU 2119 O GLY A1106 19088 18244 17180 2540 5927 -510 O
ATOM 2120 N GLU A1107 57.489 23.134 -92.078 1.00136.91 N
ANISOU 2120 N GLU A1107 17893 17403 16724 2182 6745 -706 N
ATOM 2121 CA GLU A1107 57.440 23.558 -93.474 1.00139.37 C
ANISOU 2121 CA GLU A1107 18921 17508 16524 2137 7196 -862 C
ATOM 2122 C GLU A1107 57.457 22.361 -94.418 1.00145.27 C
ANISOU 2122 C GLU A1107 19784 18100 17312 2300 7328 -1085 C
ATOM 2123 O GLU A1107 56.738 22.348 -95.424 1.00144.30 O
ANISOU 2123 O GLU A1107 20320 17840 16668 2365 7353 -1127 O
ATOM 2124 CB GLU A1107 58.605 24.500 -93.772 1.00139.55 C
ANISOU 2124 CB GLU A1107 18964 17490 16568 1856 7822 -981 C
ATOM 2125 N THR A1108 58.262 21.344 -94.100 1.00155.64 N
ANISOU 2125 N THR A1108 20466 19419 19252 2366 7389 -1232 N
ATOM 2126 CA THR A1108 58.338 20.150 -94.938 1.00164.07 C
ANISOU 2126 CA THR A1108 21591 20317 20433 2537 7514 -1485 C
ATOM 2127 C THR A1108 57.033 19.360 -94.906 1.00161.99 C
ANISOU 2127 C THR A1108 21531 20031 19987 2773 6891 -1347 C
ATOM 2128 O THR A1108 56.539 18.914 -95.955 1.00170.63 O
ANISOU 2128 O THR A1108 23148 20961 20722 2871 6960 -1491 O
ATOM 2129 CB THR A1108 59.509 19.277 -94.487 1.00169.95 C
ANISOU 2129 CB THR A1108 21543 21053 21977 2568 7673 -1659 C
ATOM 2130 OG1 THR A1108 59.321 18.895 -93.119 1.00169.72 O
ANISOU 2130 OG1 THR A1108 20889 21186 22410 2627 7076 -1400 O
ATOM 2131 CG2 THR A1108 60.819 20.044 -94.609 1.00174.21 C
ANISOU 2131 CG2 THR A1108 21879 21612 22699 2323 8322 -1807 C
ATOM 2132 N GLY A1109 56.458 19.198 -93.709 1.00147.30 N
ANISOU 2132 N GLY A1109 19273 18349 18347 2841 6280 -1063 N
ATOM 2133 CA GLY A1109 55.196 18.486 -93.575 1.00136.16 C
ANISOU 2133 CA GLY A1109 18003 16951 16780 3039 5662 -894 C
ATOM 2134 C GLY A1109 54.076 19.144 -94.355 1.00128.55 C
ANISOU 2134 C GLY A1109 17844 15930 15068 3060 5583 -808 C
ATOM 2135 O GLY A1109 53.322 18.474 -95.066 1.00126.63 O
ANISOU 2135 O GLY A1109 17979 15559 14575 3204 5389 -847 O
ATOM 2136 N VAL A1110 53.939 20.465 -94.210 1.00124.27 N
ANISOU 2136 N VAL A1110 17570 15470 14179 2914 5696 -679 N
ATOM 2137 CA VAL A1110 52.898 21.185 -94.935 1.00121.28 C
ANISOU 2137 CA VAL A1110 17946 15012 13121 2927 5603 -574 C
ATOM 2138 C VAL A1110 53.188 21.167 -96.432 1.00129.00 C
ANISOU 2138 C VAL A1110 19542 15752 13719 2869 6098 -820 C
ATOM 2139 O VAL A1110 52.261 21.130 -97.250 1.00131.28 O
ANISOU 2139 O VAL A1110 20445 15925 13513 2938 5931 -778 O
ATOM 2140 CB VAL A1110 52.760 22.622 -94.401 1.00115.09 C
ANISOU 2140 CB VAL A1110 17275 14337 12119 2786 5612 -395 C
ATOM 2141 N ALA A1111 54.472 21.197 -96.817 1.00134.84 N
ANISOU 2141 N ALA A1111 20131 16427 14673 2724 6714 -1078 N
ATOM 2142 CA ALA A1111 54.846 21.094 -98.224 1.00138.47 C
ANISOU 2142 CA ALA A1111 21133 16693 14786 2644 7242 -1351 C
ATOM 2143 C ALA A1111 54.477 19.740 -98.817 1.00139.62 C
ANISOU 2143 C ALA A1111 21365 16710 14974 2841 7085 -1527 C
ATOM 2144 O ALA A1111 54.348 19.626-100.042 1.00147.82 O
ANISOU 2144 O ALA A1111 23017 17590 15558 2799 7360 -1708 O
ATOM 2145 CB ALA A1111 56.345 21.349 -98.393 1.00143.23 C
ANISOU 2145 CB ALA A1111 21443 17292 15687 2448 7945 -1600 C
ATOM 2146 N GLY A1112 54.313 18.712 -97.978 1.00134.12 N
ANISOU 2146 N GLY A1112 20081 16073 14805 3034 6638 -1475 N
ATOM 2147 CA GLY A1112 53.874 17.414 -98.467 1.00133.06 C
ANISOU 2147 CA GLY A1112 20026 15795 14736 3228 6406 -1617 C
ATOM 2148 C GLY A1112 52.435 17.366 -98.959 1.00121.60 C
ANISOU 2148 C GLY A1112 19202 14290 12712 3318 5930 -1435 C
ATOM 2149 O GLY A1112 52.062 16.409 -99.645 1.00123.29 O
ANISOU 2149 O GLY A1112 19659 14346 12841 3435 5813 -1586 O
ATOM 2150 N PHE A1113 51.620 18.370 -98.627 1.00124.09 N
ANISOU 2150 N PHE A1113 19774 14719 12656 3270 5643 -1122 N
ATOM 2151 CA PHE A1113 50.220 18.435 -99.065 1.00120.44 C
ANISOU 2151 CA PHE A1113 19885 14210 11666 3353 5169 -917 C
ATOM 2152 C PHE A1113 50.074 19.226-100.369 1.00124.84 C
ANISOU 2152 C PHE A1113 21297 14608 11528 3197 5523 -989 C
ATOM 2153 O PHE A1113 49.306 20.181-100.443 1.00121.39 O
ANISOU 2153 O PHE A1113 21269 14188 10668 3150 5320 -743 O
ATOM 2154 CB PHE A1113 49.349 19.062 -97.980 1.00117.75 C
ANISOU 2154 CB PHE A1113 19330 14075 11334 3406 4637 -545 C
ATOM 2155 CG PHE A1113 49.244 18.255 -96.719 1.00118.72 C
ANISOU 2155 CG PHE A1113 18697 14380 12031 3534 4184 -415 C
ATOM 2156 CD1 PHE A1113 48.395 17.162 -96.649 1.00120.51 C
ANISOU 2156 CD1 PHE A1113 18856 14594 12339 3702 3653 -327 C
ATOM 2157 CD2 PHE A1113 49.958 18.618 -95.588 1.00117.93 C
ANISOU 2157 CD2 PHE A1113 17969 14470 12367 3461 4256 -355 C
ATOM 2158 CE1 PHE A1113 48.282 16.428 -95.479 1.00118.40 C
ANISOU 2158 CE1 PHE A1113 17906 14502 12580 3785 3213 -173 C
ATOM 2159 CE2 PHE A1113 49.850 17.889 -94.416 1.00114.96 C
ANISOU 2159 CE2 PHE A1113 16919 14277 12485 3541 3814 -207 C
ATOM 2160 CZ PHE A1113 49.011 16.793 -94.362 1.00114.84 C
ANISOU 2160 CZ PHE A1113 16842 14249 12544 3700 3294 -109 C
ATOM 2161 N THR A1114 50.800 18.795-101.410 1.00133.65 N
ANISOU 2161 N THR A1114 22685 15566 12530 3114 6044 -1331 N
ATOM 2162 CA THR A1114 50.809 19.522-102.684 1.00135.79 C
ANISOU 2162 CA THR A1114 23769 15703 12124 2909 6445 -1416 C
ATOM 2163 C THR A1114 49.420 19.609-103.318 1.00135.44 C
ANISOU 2163 C THR A1114 24414 15562 11485 2954 5952 -1199 C
ATOM 2164 O THR A1114 49.026 20.672-103.822 1.00131.54 O
ANISOU 2164 O THR A1114 24494 15021 10463 2803 5984 -1025 O
ATOM 2165 CB THR A1114 51.793 18.864-103.654 1.00139.88 C
ANISOU 2165 CB THR A1114 24411 16095 12641 2822 7078 -1858 C
ATOM 2166 OG1 THR A1114 51.525 17.458-103.731 1.00140.05 O
ANISOU 2166 OG1 THR A1114 24257 16027 12928 3033 6807 -2029 O
ATOM 2167 CG2 THR A1114 53.226 19.075-103.188 1.00140.30 C
ANISOU 2167 CG2 THR A1114 23870 16236 13202 2721 7657 -2056 C
ATOM 2168 N ASN A1115 48.664 18.506-103.289 1.00141.27 N
ANISOU 2168 N ASN A1115 25094 16258 12324 3153 5464 -1188 N
ATOM 2169 CA ASN A1115 47.307 18.497-103.835 1.00147.40 C
ANISOU 2169 CA ASN A1115 26465 16949 12591 3203 4936 -966 C
ATOM 2170 C ASN A1115 46.395 19.480-103.102 1.00137.85 C
ANISOU 2170 C ASN A1115 25229 15861 11287 3249 4466 -550 C
ATOM 2171 O ASN A1115 45.695 20.286-103.732 1.00140.66 O
ANISOU 2171 O ASN A1115 26213 16130 11101 3161 4338 -364 O
ATOM 2172 CB ASN A1115 46.742 17.074-103.787 1.00148.64 C
ANISOU 2172 CB ASN A1115 26451 17052 12975 3405 4484 -1028 C
ATOM 2173 CG ASN A1115 46.989 16.381-102.450 1.00148.31 C
ANISOU 2173 CG ASN A1115 25502 17163 13685 3583 4222 -980 C
ATOM 2174 OD1 ASN A1115 47.251 17.027-101.433 1.00146.83 O
ANISOU 2174 OD1 ASN A1115 24837 17159 13792 3578 4211 -812 O
ATOM 2175 ND2 ASN A1115 46.914 15.054-102.453 1.00148.62 N
ANISOU 2175 ND2 ASN A1115 25319 17116 14033 3724 3995 -1125 N
ATOM 2176 N SER A1116 46.395 19.433-101.766 1.00130.68 N
ANISOU 2176 N SER A1116 23594 15150 10908 3379 4202 -404 N
ATOM 2177 CA SER A1116 45.541 20.326-100.989 1.00129.87 C
ANISOU 2177 CA SER A1116 23407 15182 10755 3438 3778 -54 C
ATOM 2178 C SER A1116 45.979 21.779-101.117 1.00115.47 C
ANISOU 2178 C SER A1116 21851 13335 8688 3255 4156 -2 C
ATOM 2179 O SER A1116 45.132 22.680-101.111 1.00114.44 O
ANISOU 2179 O SER A1116 22035 13185 8260 3266 3868 253 O
ATOM 2180 CB SER A1116 45.528 19.902 -99.521 1.00110.35 C
ANISOU 2180 CB SER A1116 20092 12954 8884 3581 3456 58 C
ATOM 2181 OG SER A1116 45.019 18.588 -99.375 1.00111.46 O
ANISOU 2181 OG SER A1116 20000 13106 9242 3737 3034 62 O
ATOM 2182 N LEU A1117 47.287 22.025-101.229 1.00117.73 N
ANISOU 2182 N LEU A1117 22002 13609 9121 3087 4787 -236 N
ATOM 2183 CA LEU A1117 47.771 23.389-101.418 1.00123.10 C
ANISOU 2183 CA LEU A1117 22963 14246 9565 2877 5169 -190 C
ATOM 2184 C LEU A1117 47.298 23.953-102.753 1.00124.67 C
ANISOU 2184 C LEU A1117 24072 14230 9068 2729 5243 -133 C
ATOM 2185 O LEU A1117 46.878 25.115-102.827 1.00123.43 O
ANISOU 2185 O LEU A1117 24269 14006 8622 2648 5144 89 O
ATOM 2186 CB LEU A1117 49.297 23.428-101.332 1.00128.46 C
ANISOU 2186 CB LEU A1117 23294 14962 10553 2707 5840 -460 C
ATOM 2187 CG LEU A1117 49.965 23.256 -99.965 1.00125.13 C
ANISOU 2187 CG LEU A1117 21992 14746 10804 2772 5835 -476 C
ATOM 2188 CD1 LEU A1117 51.480 23.181-100.133 1.00126.08 C
ANISOU 2188 CD1 LEU A1117 21838 14864 11203 2596 6523 -768 C
ATOM 2189 CD2 LEU A1117 49.563 24.329 -98.974 1.00115.25 C
ANISOU 2189 CD2 LEU A1117 20559 13616 9614 2775 5561 -212 C
ATOM 2190 N ARG A1118 47.355 23.143-103.819 1.00131.02 N
ANISOU 2190 N ARG A1118 25276 14909 9596 2683 5400 -332 N
ATOM 2191 CA ARG A1118 46.857 23.607-105.113 1.00135.97 C
ANISOU 2191 CA ARG A1118 26803 15342 9519 2515 5424 -262 C
ATOM 2192 C ARG A1118 45.341 23.779-105.106 1.00137.12 C
ANISOU 2192 C ARG A1118 27254 15433 9412 2670 4690 78 C
ATOM 2193 O ARG A1118 44.817 24.649-105.811 1.00139.92 O
ANISOU 2193 O ARG A1118 28090 15633 9441 2502 4506 276 O
ATOM 2194 CB ARG A1118 47.275 22.646-106.228 1.00134.63 C
ANISOU 2194 CB ARG A1118 26899 15070 9183 2400 5715 -577 C
ATOM 2195 CG ARG A1118 48.768 22.615-106.496 1.00137.35 C
ANISOU 2195 CG ARG A1118 26964 15449 9775 2182 6431 -909 C
ATOM 2196 CD ARG A1118 49.092 21.780-107.726 1.00143.03 C
ANISOU 2196 CD ARG A1118 27988 16066 10291 2040 6686 -1215 C
ATOM 2197 NE ARG A1118 48.432 22.291-108.925 1.00145.74 N
ANISOU 2197 NE ARG A1118 29037 16264 10076 1802 6475 -1055 N
ATOM 2198 CZ ARG A1118 48.903 23.279-109.677 1.00149.60 C
ANISOU 2198 CZ ARG A1118 29802 16705 10332 1457 6748 -1004 C
ATOM 2199 NH1 ARG A1118 50.044 23.875-109.358 1.00156.32 N
ANISOU 2199 NH1 ARG A1118 30292 17651 11452 1303 7240 -1101 N
ATOM 2200 NH2 ARG A1118 48.233 23.675-110.750 1.00153.55 N
ANISOU 2200 NH2 ARG A1118 30941 17062 10339 1257 6510 -846 N
ATOM 2201 N MET A1119 44.623 22.972-104.319 1.00134.56 N
ANISOU 2201 N MET A1119 26460 15225 9443 2937 4162 166 N
ATOM 2202 CA MET A1119 43.178 23.162-104.202 1.00133.27 C
ANISOU 2202 CA MET A1119 26492 15041 9103 3093 3464 498 C
ATOM 2203 C MET A1119 42.844 24.443-103.440 1.00126.55 C
ANISOU 2203 C MET A1119 25504 14245 8334 3127 3300 757 C
ATOM 2204 O MET A1119 41.870 25.131-103.768 1.00124.65 O
ANISOU 2204 O MET A1119 25698 13890 7773 3151 2924 1019 O
ATOM 2205 CB MET A1119 42.533 21.955-103.522 1.00137.87 C
ANISOU 2205 CB MET A1119 26570 15758 10057 3343 2962 528 C
ATOM 2206 CG MET A1119 42.506 20.694-104.366 1.00142.60 C
ANISOU 2206 CG MET A1119 27421 16244 10518 3342 2950 322 C
ATOM 2207 SD MET A1119 41.738 19.316-103.495 1.00142.42 S
ANISOU 2207 SD MET A1119 26782 16362 10968 3614 2314 400 S
ATOM 2208 CE MET A1119 40.714 18.628-104.792 1.00145.55 C
ANISOU 2208 CE MET A1119 27938 16540 10823 3596 1923 435 C
ATOM 2209 N LEU A1120 43.636 24.773-102.416 1.00120.89 N
ANISOU 2209 N LEU A1120 24181 13691 8062 3130 3560 682 N
ATOM 2210 CA LEU A1120 43.384 25.983-101.640 1.00118.58 C
ANISOU 2210 CA LEU A1120 23738 13447 7870 3157 3432 882 C
ATOM 2211 C LEU A1120 43.753 27.235-102.428 1.00118.60 C
ANISOU 2211 C LEU A1120 24359 13233 7470 2916 3772 928 C
ATOM 2212 O LEU A1120 43.070 28.262-102.329 1.00118.34 O
ANISOU 2212 O LEU A1120 24563 13106 7296 2947 3499 1161 O
ATOM 2213 CB LEU A1120 44.162 25.933-100.325 1.00113.65 C
ANISOU 2213 CB LEU A1120 22304 13061 7817 3197 3606 779 C
ATOM 2214 CG LEU A1120 43.574 25.078 -99.201 1.00108.16 C
ANISOU 2214 CG LEU A1120 20937 12614 7543 3434 3136 850 C
ATOM 2215 CD1 LEU A1120 44.546 25.001 -98.039 1.00106.17 C
ANISOU 2215 CD1 LEU A1120 19947 12581 7812 3403 3376 730 C
ATOM 2216 CD2 LEU A1120 42.243 25.646 -98.748 1.00106.10 C
ANISOU 2216 CD2 LEU A1120 20713 12402 7197 3607 2571 1128 C
ATOM 2217 N GLN A1121 44.844 27.174-103.199 1.00122.12 N
ANISOU 2217 N GLN A1121 25056 13598 7747 2668 4371 707 N
ATOM 2218 CA GLN A1121 45.239 28.310-104.029 1.00129.05 C
ANISOU 2218 CA GLN A1121 26367 14269 8397 2351 4616 749 C
ATOM 2219 C GLN A1121 44.203 28.614-105.109 1.00128.49 C
ANISOU 2219 C GLN A1121 26894 13967 7960 2275 4180 942 C
ATOM 2220 O GLN A1121 44.059 29.770-105.525 1.00130.65 O
ANISOU 2220 O GLN A1121 27503 14059 8080 2105 4126 1101 O
ATOM 2221 CB GLN A1121 46.611 28.040-104.656 1.00129.56 C
ANISOU 2221 CB GLN A1121 26408 14333 8486 2071 5283 452 C
ATOM 2222 CG GLN A1121 47.193 29.207-105.443 1.00136.50 C
ANISOU 2222 CG GLN A1121 27653 15043 9169 1707 5581 490 C
ATOM 2223 CD GLN A1121 48.538 28.888-106.059 1.00137.67 C
ANISOU 2223 CD GLN A1121 27715 15230 9362 1432 6226 194 C
ATOM 2224 OE1 GLN A1121 49.029 27.764-105.963 1.00141.12 O
ANISOU 2224 OE1 GLN A1121 27831 15794 9993 1522 6456 -63 O
ATOM 2225 NE2 GLN A1121 49.132 29.875-106.718 1.00141.61 N
ANISOU 2225 NE2 GLN A1121 28499 15614 9690 1096 6512 227 N
ATOM 2226 N GLN A1122 43.446 27.607-105.547 1.00128.39 N
ANISOU 2226 N GLN A1122 27010 13948 7823 2400 3838 942 N
ATOM 2227 CA GLN A1122 42.414 27.794-106.556 1.00135.62 C
ANISOU 2227 CA GLN A1122 28431 14657 8441 2327 3385 1119 C
ATOM 2228 C GLN A1122 41.045 28.107-105.957 1.00130.82 C
ANISOU 2228 C GLN A1122 27692 14048 7966 2589 2698 1400 C
ATOM 2229 O GLN A1122 40.033 27.976-106.657 1.00130.43 O
ANISOU 2229 O GLN A1122 27916 13870 7771 2587 2236 1531 O
ATOM 2230 CB GLN A1122 42.325 26.554-107.450 1.00139.39 C
ANISOU 2230 CB GLN A1122 29138 15110 8714 2282 3379 952 C
ATOM 2231 N LYS A1123 40.997 28.496-104.679 1.00132.34 N
ANISOU 2231 N LYS A1123 27431 14396 8457 2802 2630 1476 N
ATOM 2232 CA LYS A1123 39.781 28.906-103.966 1.00132.97 C
ANISOU 2232 CA LYS A1123 27281 14510 8731 3053 2036 1711 C
ATOM 2233 C LYS A1123 38.722 27.804-103.902 1.00131.92 C
ANISOU 2233 C LYS A1123 26948 14481 8694 3255 1509 1769 C
ATOM 2234 O LYS A1123 37.538 28.090-103.693 1.00128.88 O
ANISOU 2234 O LYS A1123 26423 14087 8459 3392 973 1947 O
ATOM 2235 CB LYS A1123 39.179 30.188-104.568 1.00138.06 C
ANISOU 2235 CB LYS A1123 28314 14890 9252 2935 1798 1899 C
ATOM 2236 CG LYS A1123 39.655 31.503-103.940 1.00138.31 C
ANISOU 2236 CG LYS A1123 28316 14864 9372 2910 2018 1956 C
ATOM 2237 CD LYS A1123 41.165 31.678-103.956 1.00140.00 C
ANISOU 2237 CD LYS A1123 28570 15105 9520 2675 2717 1770 C
ATOM 2238 CE LYS A1123 41.579 32.921-103.186 1.00138.75 C
ANISOU 2238 CE LYS A1123 28326 14905 9486 2665 2897 1830 C
ATOM 2239 NZ LYS A1123 43.057 33.074-103.150 1.00138.80 N
ANISOU 2239 NZ LYS A1123 28272 14963 9502 2411 3576 1636 N
ATOM 2240 N ARG A1124 39.119 26.542-104.073 1.00132.38 N
ANISOU 2240 N ARG A1124 26962 14637 8699 3270 1656 1606 N
ATOM 2241 CA ARG A1124 38.201 25.409-103.950 1.00128.95 C
ANISOU 2241 CA ARG A1124 26317 14304 8374 3449 1167 1657 C
ATOM 2242 C ARG A1124 38.219 24.973-102.492 1.00124.23 C
ANISOU 2242 C ARG A1124 25074 14012 8117 3716 1072 1687 C
ATOM 2243 O ARG A1124 39.018 24.130-102.085 1.00125.05 O
ANISOU 2243 O ARG A1124 24937 14262 8316 3764 1358 1521 O
ATOM 2244 CB ARG A1124 38.604 24.279-104.889 1.00134.01 C
ANISOU 2244 CB ARG A1124 27292 14865 8760 3339 1351 1465 C
ATOM 2245 N TRP A1125 37.325 25.557-101.693 1.00141.92 N
ANISOU 2245 N TRP A1125 29280 15476 9167 1836 -554 -415 N
ATOM 2246 CA TRP A1125 37.356 25.327-100.252 1.00136.26 C
ANISOU 2246 CA TRP A1125 27648 14895 9228 1516 -402 -281 C
ATOM 2247 C TRP A1125 36.782 23.968 -99.870 1.00125.48 C
ANISOU 2247 C TRP A1125 25644 13689 8345 1086 -855 -487 C
ATOM 2248 O TRP A1125 37.366 23.254 -99.047 1.00124.03 O
ANISOU 2248 O TRP A1125 25020 13371 8734 713 -542 -459 O
ATOM 2249 CB TRP A1125 36.614 26.446 -99.519 1.00123.72 C
ANISOU 2249 CB TRP A1125 25605 13666 7738 1780 -547 -11 C
ATOM 2250 CG TRP A1125 36.975 27.831 -99.976 1.00124.61 C
ANISOU 2250 CG TRP A1125 26336 13611 7399 2246 -182 198 C
ATOM 2251 CD1 TRP A1125 36.130 28.772-100.489 1.00128.66 C
ANISOU 2251 CD1 TRP A1125 27098 14315 7474 2705 -570 324 C
ATOM 2252 CD2 TRP A1125 38.280 28.426 -99.973 1.00121.92 C
ANISOU 2252 CD2 TRP A1125 26438 12840 7044 2305 664 301 C
ATOM 2253 NE1 TRP A1125 36.824 29.919-100.790 1.00128.70 N
ANISOU 2253 NE1 TRP A1125 27689 14010 7203 3042 7 546 N
ATOM 2254 CE2 TRP A1125 38.146 29.730-100.485 1.00124.59 C
ANISOU 2254 CE2 TRP A1125 27231 13102 7006 2777 782 510 C
ATOM 2255 CE3 TRP A1125 39.549 27.985 -99.581 1.00117.87 C
ANISOU 2255 CE3 TRP A1125 25917 11984 6883 2004 1331 217 C
ATOM 2256 CZ2 TRP A1125 39.227 30.595-100.611 1.00123.38 C
ANISOU 2256 CZ2 TRP A1125 27243 12511 7124 2874 1540 605 C
ATOM 2257 CZ3 TRP A1125 40.620 28.839 -99.722 1.00116.61 C
ANISOU 2257 CZ3 TRP A1125 26023 11430 6856 2139 2055 286 C
ATOM 2258 CH2 TRP A1125 40.453 30.131-100.226 1.00119.35 C
ANISOU 2258 CH2 TRP A1125 26607 11681 7059 2543 2150 472 C
ATOM 2259 N ASP A1126 35.632 23.604-100.444 1.00130.53 N
ANISOU 2259 N ASP A1126 26206 14604 8787 1146 -1591 -698 N
ATOM 2260 CA ASP A1126 35.005 22.330-100.106 1.00131.62 C
ANISOU 2260 CA ASP A1126 25701 14863 9447 727 -2010 -922 C
ATOM 2261 C ASP A1126 35.850 21.152-100.576 1.00158.41 C
ANISOU 2261 C ASP A1126 29375 17835 12979 398 -1774 -1191 C
ATOM 2262 O ASP A1126 36.005 20.163 -99.847 1.00130.17 O
ANISOU 2262 O ASP A1126 25244 14150 10066 -29 -1681 -1203 O
ATOM 2263 CB ASP A1126 33.600 22.263-100.704 1.00137.58 C
ANISOU 2263 CB ASP A1126 26314 15995 9964 895 -2851 -1175 C
ATOM 2264 CG ASP A1126 32.690 23.360-100.180 1.00141.95 C
ANISOU 2264 CG ASP A1126 26489 16965 10480 1203 -3128 -945 C
ATOM 2265 OD1 ASP A1126 32.797 23.705 -98.983 1.00136.01 O
ANISOU 2265 OD1 ASP A1126 25164 16320 10193 1071 -2809 -654 O
ATOM 2266 OD2 ASP A1126 31.867 23.878-100.965 1.00146.44 O
ANISOU 2266 OD2 ASP A1126 27322 17769 10550 1593 -3677 -1074 O
ATOM 2267 N GLU A1127 36.413 21.250-101.786 1.00153.38 N
ANISOU 2267 N GLU A1127 29603 16949 11725 600 -1653 -1399 N
ATOM 2268 CA GLU A1127 37.261 20.184-102.312 1.00155.52 C
ANISOU 2268 CA GLU A1127 30176 16808 12108 305 -1401 -1711 C
ATOM 2269 C GLU A1127 38.512 20.004-101.459 1.00152.95 C
ANISOU 2269 C GLU A1127 29698 16117 12300 52 -662 -1511 C
ATOM 2270 O GLU A1127 38.892 18.872-101.134 1.00151.01 O
ANISOU 2270 O GLU A1127 29127 15627 12623 -342 -566 -1652 O
ATOM 2271 CB GLU A1127 37.635 20.480-103.764 1.00161.97 C
ANISOU 2271 CB GLU A1127 31987 17480 12074 610 -1358 -1956 C
ATOM 2272 N ALA A1128 39.159 21.112-101.083 1.00150.20 N
ANISOU 2272 N ALA A1128 29555 15717 11796 289 -143 -1201 N
ATOM 2273 CA ALA A1128 40.343 21.035-100.233 1.00145.18 C
ANISOU 2273 CA ALA A1128 28729 14785 11649 97 535 -1053 C
ATOM 2274 C ALA A1128 40.001 20.498 -98.848 1.00146.58 C
ANISOU 2274 C ALA A1128 27957 15167 12569 -200 419 -839 C
ATOM 2275 O ALA A1128 40.801 19.773 -98.249 1.00142.89 O
ANISOU 2275 O ALA A1128 27229 14442 12620 -480 755 -825 O
ATOM 2276 CB ALA A1128 41.006 22.407-100.123 1.00136.69 C
ANISOU 2276 CB ALA A1128 28014 13640 10281 429 1091 -821 C
ATOM 2277 N ALA A1129 38.819 20.843 -98.325 1.00155.89 N
ANISOU 2277 N ALA A1129 28615 16813 13803 -132 -46 -666 N
ATOM 2278 CA ALA A1129 38.400 20.348 -97.015 1.00147.78 C
ANISOU 2278 CA ALA A1129 26695 16027 13427 -416 -145 -442 C
ATOM 2279 C ALA A1129 38.203 18.835 -97.033 1.00145.97 C
ANISOU 2279 C ALA A1129 26165 15617 13681 -834 -389 -620 C
ATOM 2280 O ALA A1129 38.716 18.116 -96.161 1.00146.58 O
ANISOU 2280 O ALA A1129 25823 15546 14327 -1120 -128 -461 O
ATOM 2281 CB ALA A1129 37.115 21.054 -96.580 1.00150.14 C
ANISOU 2281 CB ALA A1129 26530 16861 13655 -255 -594 -287 C
ATOM 2282 N VAL A1130 37.485 18.331 -98.042 1.00142.67 N
ANISOU 2282 N VAL A1130 25964 15192 13052 -856 -887 -968 N
ATOM 2283 CA VAL A1130 37.258 16.894 -98.139 1.00138.73 C
ANISOU 2283 CA VAL A1130 25165 14479 13066 -1258 -1117 -1205 C
ATOM 2284 C VAL A1130 38.547 16.162 -98.515 1.00137.72 C
ANISOU 2284 C VAL A1130 25436 13793 13097 -1425 -668 -1380 C
ATOM 2285 O VAL A1130 38.711 14.982 -98.177 1.00138.60 O
ANISOU 2285 O VAL A1130 25189 13632 13841 -1791 -643 -1431 O
ATOM 2286 CB VAL A1130 36.097 16.630 -99.127 1.00140.07 C
ANISOU 2286 CB VAL A1130 25408 14843 12969 -1206 -1803 -1614 C
ATOM 2287 CG1 VAL A1130 35.759 15.147 -99.239 1.00142.95 C
ANISOU 2287 CG1 VAL A1130 25391 14980 13945 -1638 -2055 -1926 C
ATOM 2288 CG2 VAL A1130 34.856 17.387 -98.683 1.00138.61 C
ANISOU 2288 CG2 VAL A1130 24772 15201 12691 -1028 -2234 -1455 C
ATOM 2289 N ASN A1131 39.511 16.852 -99.133 1.00137.31 N
ANISOU 2289 N ASN A1131 26091 13537 12545 -1170 -257 -1449 N
ATOM 2290 CA ASN A1131 40.787 16.206 -99.422 1.00137.59 C
ANISOU 2290 CA ASN A1131 26458 13041 12779 -1332 218 -1639 C
ATOM 2291 C ASN A1131 41.672 16.147 -98.180 1.00133.89 C
ANISOU 2291 C ASN A1131 25578 12432 12860 -1452 713 -1295 C
ATOM 2292 O ASN A1131 42.399 15.169 -97.979 1.00131.69 O
ANISOU 2292 O ASN A1131 25177 11759 13099 -1713 930 -1379 O
ATOM 2293 CB ASN A1131 41.504 16.939-100.557 1.00138.82 C
ANISOU 2293 CB ASN A1131 27518 13016 12211 -1037 527 -1868 C
ATOM 2294 N LEU A1132 41.627 17.184 -97.340 1.00135.56 N
ANISOU 2294 N LEU A1132 25562 12971 12975 -1245 880 -930 N
ATOM 2295 CA LEU A1132 42.405 17.190 -96.106 1.00134.52 C
ANISOU 2295 CA LEU A1132 24993 12807 13311 -1315 1299 -626 C
ATOM 2296 C LEU A1132 41.827 16.254 -95.055 1.00137.41 C
ANISOU 2296 C LEU A1132 24581 13320 14307 -1619 1049 -357 C
ATOM 2297 O LEU A1132 42.566 15.801 -94.174 1.00137.71 O
ANISOU 2297 O LEU A1132 24299 13217 14808 -1741 1347 -155 O
ATOM 2298 CB LEU A1132 42.509 18.608 -95.547 1.00131.86 C
ANISOU 2298 CB LEU A1132 24620 12801 12681 -996 1554 -384 C
ATOM 2299 CG LEU A1132 43.519 19.507 -96.260 1.00130.69 C
ANISOU 2299 CG LEU A1132 25172 12375 12110 -729 2064 -568 C
ATOM 2300 CD1 LEU A1132 43.382 20.946 -95.797 1.00128.18 C
ANISOU 2300 CD1 LEU A1132 24788 12387 11528 -408 2244 -354 C
ATOM 2301 CD2 LEU A1132 44.927 18.991 -96.002 1.00128.49 C
ANISOU 2301 CD2 LEU A1132 24939 11654 12226 -859 2596 -691 C
ATOM 2302 N ALA A1133 40.527 15.956 -95.126 1.00139.47 N
ANISOU 2302 N ALA A1133 24529 13859 14604 -1734 519 -350 N
ATOM 2303 CA ALA A1133 39.929 15.030 -94.167 1.00133.36 C
ANISOU 2303 CA ALA A1133 23028 13186 14455 -2055 330 -87 C
ATOM 2304 C ALA A1133 40.350 13.576 -94.385 1.00132.96 C
ANISOU 2304 C ALA A1133 22945 12603 14969 -2392 356 -239 C
ATOM 2305 O ALA A1133 39.971 12.721 -93.575 1.00132.86 O
ANISOU 2305 O ALA A1133 22360 12579 15541 -2671 276 24 O
ATOM 2306 CB ALA A1133 38.403 15.135 -94.218 1.00137.63 C
ANISOU 2306 CB ALA A1133 23214 14148 14930 -2097 -217 -103 C
ATOM 2307 N LYS A1134 41.110 13.275 -95.443 1.00132.91 N
ANISOU 2307 N LYS A1134 23528 12149 14824 -2376 490 -651 N
ATOM 2308 CA LYS A1134 41.563 11.926 -95.767 1.00134.73 C
ANISOU 2308 CA LYS A1134 23758 11829 15604 -2680 527 -880 C
ATOM 2309 C LYS A1134 43.065 11.732 -95.550 1.00135.72 C
ANISOU 2309 C LYS A1134 24095 11523 15951 -2652 1058 -867 C
ATOM 2310 O LYS A1134 43.705 10.977 -96.286 1.00139.75 O
ANISOU 2310 O LYS A1134 24907 11531 16661 -2782 1166 -1244 O
ATOM 2311 CB LYS A1134 41.192 11.576 -97.207 1.00132.77 C
ANISOU 2311 CB LYS A1134 23959 11405 15082 -2719 219 -1470 C
ATOM 2312 N SER A1135 43.647 12.398 -94.557 1.00135.54 N
ANISOU 2312 N SER A1135 23888 11695 15914 -2480 1384 -491 N
ATOM 2313 CA SER A1135 45.084 12.342 -94.322 1.00138.14 C
ANISOU 2313 CA SER A1135 24385 11667 16437 -2403 1877 -525 C
ATOM 2314 C SER A1135 45.394 11.828 -92.920 1.00138.70 C
ANISOU 2314 C SER A1135 23845 11774 17078 -2484 1992 -43 C
ATOM 2315 O SER A1135 44.509 11.681 -92.073 1.00139.81 O
ANISOU 2315 O SER A1135 23463 12274 17384 -2581 1755 366 O
ATOM 2316 CB SER A1135 45.717 13.726 -94.506 1.00141.93 C
ANISOU 2316 CB SER A1135 25271 12321 16337 -2058 2233 -613 C
ATOM 2317 OG SER A1135 45.279 14.608 -93.487 1.00139.56 O
ANISOU 2317 OG SER A1135 24566 12570 15889 -1890 2217 -210 O
ATOM 2318 N ARG A1136 46.684 11.534 -92.695 1.00137.65 N
ANISOU 2318 N ARG A1136 23791 11266 17245 -2435 2366 -107 N
ATOM 2319 CA ARG A1136 47.135 11.117 -91.369 1.00136.65 C
ANISOU 2319 CA ARG A1136 23142 11191 17587 -2429 2487 348 C
ATOM 2320 C ARG A1136 46.957 12.238 -90.360 1.00133.54 C
ANISOU 2320 C ARG A1136 22446 11449 16845 -2181 2568 697 C
ATOM 2321 O ARG A1136 46.777 11.981 -89.163 1.00135.40 O
ANISOU 2321 O ARG A1136 22152 11970 17323 -2193 2521 1179 O
ATOM 2322 CB ARG A1136 48.606 10.696 -91.401 1.00135.56 C
ANISOU 2322 CB ARG A1136 23165 10537 17803 -2363 2852 128 C
ATOM 2323 CG ARG A1136 48.996 9.719 -92.491 1.00138.56 C
ANISOU 2323 CG ARG A1136 23896 10242 18509 -2575 2858 -338 C
ATOM 2324 CD ARG A1136 48.068 8.524 -92.515 1.00141.79 C
ANISOU 2324 CD ARG A1136 24016 10465 19391 -2904 2485 -180 C
ATOM 2325 NE ARG A1136 48.483 7.531 -93.497 1.00146.52 N
ANISOU 2325 NE ARG A1136 24884 10403 20385 -3113 2499 -666 N
ATOM 2326 CZ ARG A1136 47.693 6.569 -93.956 1.00153.72 C
ANISOU 2326 CZ ARG A1136 25680 11071 21656 -3414 2195 -781 C
ATOM 2327 NH1 ARG A1136 48.147 5.697 -94.847 1.00157.58 N
ANISOU 2327 NH1 ARG A1136 26395 10961 22519 -3593 2235 -1287 N
ATOM 2328 NH2 ARG A1136 46.435 6.496 -93.544 1.00156.66 N
ANISOU 2328 NH2 ARG A1136 25687 11803 22035 -3545 1865 -443 N
ATOM 2329 N TRP A1137 47.037 13.483 -90.831 1.00130.06 N
ANISOU 2329 N TRP A1137 22342 11235 15839 -1948 2715 453 N
ATOM 2330 CA TRP A1137 46.865 14.649 -89.976 1.00127.11 C
ANISOU 2330 CA TRP A1137 21691 11460 15144 -1703 2811 689 C
ATOM 2331 C TRP A1137 45.465 14.706 -89.378 1.00129.15 C
ANISOU 2331 C TRP A1137 21493 12253 15328 -1804 2429 1074 C
ATOM 2332 O TRP A1137 45.295 15.147 -88.236 1.00131.54 O
ANISOU 2332 O TRP A1137 21316 13056 15606 -1699 2465 1416 O
ATOM 2333 CB TRP A1137 47.180 15.901 -90.797 1.00124.27 C
ANISOU 2333 CB TRP A1137 21850 11109 14256 -1459 3057 320 C
ATOM 2334 CG TRP A1137 46.800 17.202 -90.181 1.00119.87 C
ANISOU 2334 CG TRP A1137 21069 11128 13347 -1216 3117 478 C
ATOM 2335 CD1 TRP A1137 47.197 17.688 -88.972 1.00117.63 C
ANISOU 2335 CD1 TRP A1137 20307 11223 13163 -1057 3310 683 C
ATOM 2336 CD2 TRP A1137 45.979 18.216 -90.773 1.00119.07 C
ANISOU 2336 CD2 TRP A1137 21214 11284 12742 -1077 2985 402 C
ATOM 2337 NE1 TRP A1137 46.656 18.935 -88.763 1.00117.67 N
ANISOU 2337 NE1 TRP A1137 20215 11696 12800 -856 3323 716 N
ATOM 2338 CE2 TRP A1137 45.906 19.282 -89.857 1.00115.89 C
ANISOU 2338 CE2 TRP A1137 20436 11383 12215 -858 3125 567 C
ATOM 2339 CE3 TRP A1137 45.292 18.321 -91.987 1.00121.80 C
ANISOU 2339 CE3 TRP A1137 22052 11501 12725 -1093 2739 200 C
ATOM 2340 CZ2 TRP A1137 45.172 20.439 -90.114 1.00111.86 C
ANISOU 2340 CZ2 TRP A1137 20020 11191 11290 -666 3043 553 C
ATOM 2341 CZ3 TRP A1137 44.564 19.470 -92.241 1.00120.53 C
ANISOU 2341 CZ3 TRP A1137 22011 11683 12104 -874 2631 218 C
ATOM 2342 CH2 TRP A1137 44.509 20.512 -91.308 1.00115.12 C
ANISOU 2342 CH2 TRP A1137 20938 11441 11363 -668 2790 402 C
ATOM 2343 N TYR A1138 44.455 14.252 -90.124 1.00131.46 N
ANISOU 2343 N TYR A1138 21892 12462 15593 -2008 2064 981 N
ATOM 2344 CA TYR A1138 43.091 14.261 -89.611 1.00129.82 C
ANISOU 2344 CA TYR A1138 21222 12729 15376 -2129 1706 1280 C
ATOM 2345 C TYR A1138 42.862 13.156 -88.586 1.00133.20 C
ANISOU 2345 C TYR A1138 21091 13157 16364 -2382 1642 1729 C
ATOM 2346 O TYR A1138 42.022 13.310 -87.692 1.00133.23 O
ANISOU 2346 O TYR A1138 20590 13655 16377 -2435 1515 2096 O
ATOM 2347 CB TYR A1138 42.100 14.135 -90.771 1.00127.81 C
ANISOU 2347 CB TYR A1138 21239 12388 14935 -2244 1319 965 C
ATOM 2348 CG TYR A1138 40.649 14.274 -90.370 1.00130.54 C
ANISOU 2348 CG TYR A1138 21116 13226 15259 -2346 937 1166 C
ATOM 2349 CD1 TYR A1138 40.072 15.530 -90.233 1.00129.28 C
ANISOU 2349 CD1 TYR A1138 20898 13590 14634 -2101 855 1189 C
ATOM 2350 CD2 TYR A1138 39.853 13.156 -90.143 1.00136.59 C
ANISOU 2350 CD2 TYR A1138 21478 13903 16518 -2693 680 1304 C
ATOM 2351 CE1 TYR A1138 38.745 15.672 -89.869 1.00133.72 C
ANISOU 2351 CE1 TYR A1138 20998 14601 15207 -2192 507 1324 C
ATOM 2352 CE2 TYR A1138 38.522 13.288 -89.777 1.00138.96 C
ANISOU 2352 CE2 TYR A1138 21315 14644 16839 -2804 363 1440 C
ATOM 2353 CZ TYR A1138 37.974 14.550 -89.643 1.00137.21 C
ANISOU 2353 CZ TYR A1138 21033 14966 16133 -2549 267 1437 C
ATOM 2354 OH TYR A1138 36.653 14.692 -89.282 1.00138.38 O
ANISOU 2354 OH TYR A1138 20691 15553 16335 -2657 -48 1526 O
ATOM 2355 N ASN A1139 43.593 12.045 -88.693 1.00137.05 N
ANISOU 2355 N ASN A1139 21659 13085 17329 -2535 1749 1717 N
ATOM 2356 CA ASN A1139 43.403 10.920 -87.785 1.00143.91 C
ANISOU 2356 CA ASN A1139 22052 13858 18770 -2767 1710 2186 C
ATOM 2357 C ASN A1139 44.243 11.025 -86.522 1.00144.51 C
ANISOU 2357 C ASN A1139 21833 14153 18920 -2574 1985 2602 C
ATOM 2358 O ASN A1139 43.832 10.507 -85.476 1.00146.88 O
ANISOU 2358 O ASN A1139 21660 14677 19471 -2683 1952 3135 O
ATOM 2359 CB ASN A1139 43.716 9.599 -88.494 1.00150.52 C
ANISOU 2359 CB ASN A1139 23075 13948 20167 -3025 1667 1986 C
ATOM 2360 CG ASN A1139 42.728 9.281 -89.599 1.00155.36 C
ANISOU 2360 CG ASN A1139 23843 14396 20790 -3258 1336 1597 C
ATOM 2361 OD1 ASN A1139 42.948 9.619 -90.761 1.00157.18 O
ANISOU 2361 OD1 ASN A1139 24578 14440 20703 -3178 1297 1064 O
ATOM 2362 ND2 ASN A1139 41.629 8.626 -89.239 1.00157.04 N
ANISOU 2362 ND2 ASN A1139 23615 14690 21363 -3542 1104 1845 N
ATOM 2363 N GLN A1140 45.424 11.646 -86.604 1.00143.37 N
ANISOU 2363 N GLN A1140 21956 13941 18576 -2288 2264 2356 N
ATOM 2364 CA GLN A1140 46.243 11.851 -85.412 1.00141.43 C
ANISOU 2364 CA GLN A1140 21405 13977 18356 -2052 2492 2664 C
ATOM 2365 C GLN A1140 45.528 12.740 -84.400 1.00140.38 C
ANISOU 2365 C GLN A1140 20830 14660 17846 -1929 2453 2988 C
ATOM 2366 O GLN A1140 45.353 12.362 -83.236 1.00143.50 O
ANISOU 2366 O GLN A1140 20767 15390 18366 -1939 2444 3504 O
ATOM 2367 CB GLN A1140 47.594 12.453 -85.804 1.00137.46 C
ANISOU 2367 CB GLN A1140 21253 13245 17730 -1777 2807 2211 C
ATOM 2368 N THR A1141 45.102 13.925 -84.829 1.00136.15 N
ANISOU 2368 N THR A1141 20431 14455 16845 -1804 2439 2697 N
ATOM 2369 CA THR A1141 44.367 14.860 -83.978 1.00136.07 C
ANISOU 2369 CA THR A1141 20000 15209 16491 -1689 2398 2911 C
ATOM 2370 C THR A1141 43.069 15.232 -84.683 1.00137.76 C
ANISOU 2370 C THR A1141 20284 15560 16499 -1832 2111 2776 C
ATOM 2371 O THR A1141 43.074 16.105 -85.568 1.00137.91 O
ANISOU 2371 O THR A1141 20689 15519 16192 -1684 2118 2374 O
ATOM 2372 CB THR A1141 45.191 16.107 -83.675 1.00134.22 C
ANISOU 2372 CB THR A1141 19782 15285 15931 -1327 2686 2659 C
ATOM 2373 OG1 THR A1141 45.604 16.719 -84.903 1.00132.42 O
ANISOU 2373 OG1 THR A1141 20128 14661 15524 -1228 2804 2140 O
ATOM 2374 CG2 THR A1141 46.421 15.759 -82.847 1.00134.85 C
ANISOU 2374 CG2 THR A1141 19690 15330 16217 -1152 2922 2769 C
ATOM 2375 N PRO A1142 41.943 14.597 -84.330 1.00138.77 N
ANISOU 2375 N PRO A1142 20048 15860 16817 -2106 1861 3096 N
ATOM 2376 CA PRO A1142 40.673 14.893 -85.015 1.00138.37 C
ANISOU 2376 CA PRO A1142 20015 15939 16622 -2236 1540 2911 C
ATOM 2377 C PRO A1142 40.143 16.305 -84.791 1.00133.07 C
ANISOU 2377 C PRO A1142 19190 15881 15491 -2001 1512 2807 C
ATOM 2378 O PRO A1142 39.725 16.964 -85.749 1.00132.84 O
ANISOU 2378 O PRO A1142 19484 15803 15188 -1902 1342 2455 O
ATOM 2379 CB PRO A1142 39.714 13.845 -84.434 1.00142.69 C
ANISOU 2379 CB PRO A1142 20090 16546 17579 -2592 1368 3308 C
ATOM 2380 CG PRO A1142 40.600 12.752 -83.928 1.00144.84 C
ANISOU 2380 CG PRO A1142 20335 16430 18270 -2679 1571 3627 C
ATOM 2381 CD PRO A1142 41.826 13.444 -83.423 1.00141.08 C
ANISOU 2381 CD PRO A1142 19950 16121 17534 -2325 1867 3614 C
ATOM 2382 N ASN A1143 40.160 16.776 -83.540 1.00129.63 N
ANISOU 2382 N ASN A1143 18266 16026 14964 -1891 1673 3104 N
ATOM 2383 CA ASN A1143 39.559 18.069 -83.209 1.00124.38 C
ANISOU 2383 CA ASN A1143 17347 15970 13943 -1696 1645 3007 C
ATOM 2384 C ASN A1143 40.342 19.223 -83.825 1.00114.69 C
ANISOU 2384 C ASN A1143 16547 14632 12399 -1352 1837 2604 C
ATOM 2385 O ASN A1143 39.756 20.135 -84.423 1.00111.56 O
ANISOU 2385 O ASN A1143 16296 14349 11742 -1218 1700 2359 O
ATOM 2386 CB ASN A1143 39.468 18.237 -81.691 1.00121.81 C
ANISOU 2386 CB ASN A1143 16379 16308 13594 -1666 1802 3385 C
ATOM 2387 CG ASN A1143 38.630 17.162 -81.035 1.00126.11 C
ANISOU 2387 CG ASN A1143 16500 16981 14435 -2013 1677 3836 C
ATOM 2388 OD1 ASN A1143 39.094 16.454 -80.142 1.00129.32 O
ANISOU 2388 OD1 ASN A1143 16687 17451 14997 -2068 1848 4240 O
ATOM 2389 ND2 ASN A1143 37.384 17.034 -81.475 1.00128.75 N
ANISOU 2389 ND2 ASN A1143 16713 17345 14862 -2237 1385 3768 N
ATOM 2390 N ARG A1144 41.668 19.205 -83.668 1.00111.63 N
ANISOU 2390 N ARG A1144 16348 14010 12055 -1195 2168 2533 N
ATOM 2391 CA ARG A1144 42.505 20.279 -84.194 1.00109.65 C
ANISOU 2391 CA ARG A1144 16478 13610 11575 -890 2442 2142 C
ATOM 2392 C ARG A1144 42.436 20.338 -85.715 1.00113.13 C
ANISOU 2392 C ARG A1144 17606 13498 11879 -895 2340 1818 C
ATOM 2393 O ARG A1144 42.316 21.425 -86.300 1.00121.40 O
ANISOU 2393 O ARG A1144 18927 14570 12630 -678 2394 1573 O
ATOM 2394 CB ARG A1144 43.945 20.078 -83.726 1.00107.56 C
ANISOU 2394 CB ARG A1144 16234 13165 11470 -758 2807 2091 C
ATOM 2395 CG ARG A1144 44.905 21.168 -84.151 1.00104.68 C
ANISOU 2395 CG ARG A1144 16189 12630 10956 -464 3176 1662 C
ATOM 2396 CD ARG A1144 46.304 20.904 -83.625 1.00102.07 C
ANISOU 2396 CD ARG A1144 15789 12146 10845 -340 3509 1561 C
ATOM 2397 NE ARG A1144 47.223 21.980 -83.982 1.00 99.18 N
ANISOU 2397 NE ARG A1144 15668 11613 10404 -78 3917 1106 N
ATOM 2398 CZ ARG A1144 48.494 22.037 -83.601 1.00 99.46 C
ANISOU 2398 CZ ARG A1144 15630 11527 10634 83 4256 870 C
ATOM 2399 NH1 ARG A1144 49.007 21.074 -82.847 1.00100.31 N
ANISOU 2399 NH1 ARG A1144 15448 11680 10984 44 4194 1076 N
ATOM 2400 NH2 ARG A1144 49.253 23.060 -83.972 1.00 99.66 N
ANISOU 2400 NH2 ARG A1144 15860 11369 10636 293 4664 424 N
ATOM 2401 N ALA A1145 42.499 19.173 -86.369 1.00110.35 N
ANISOU 2401 N ALA A1145 17540 12650 11739 -1131 2196 1816 N
ATOM 2402 CA ALA A1145 42.369 19.124 -87.821 1.00106.67 C
ANISOU 2402 CA ALA A1145 17714 11716 11100 -1147 2061 1491 C
ATOM 2403 C ALA A1145 40.996 19.601 -88.268 1.00105.41 C
ANISOU 2403 C ALA A1145 17518 11849 10685 -1142 1655 1460 C
ATOM 2404 O ALA A1145 40.881 20.296 -89.279 1.00105.10 O
ANISOU 2404 O ALA A1145 17977 11666 10291 -958 1605 1194 O
ATOM 2405 CB ALA A1145 42.636 17.713 -88.335 1.00108.67 C
ANISOU 2405 CB ALA A1145 18175 11426 11690 -1424 1964 1460 C
ATOM 2406 N LYS A1146 39.944 19.249 -87.520 1.00103.75 N
ANISOU 2406 N LYS A1146 16720 12052 10647 -1327 1371 1730 N
ATOM 2407 CA LYS A1146 38.599 19.697 -87.873 1.00104.48 C
ANISOU 2407 CA LYS A1146 16690 12452 10556 -1318 961 1662 C
ATOM 2408 C LYS A1146 38.479 21.213 -87.782 1.00104.38 C
ANISOU 2408 C LYS A1146 16681 12796 10181 -969 1055 1570 C
ATOM 2409 O LYS A1146 37.871 21.846 -88.653 1.00106.76 O
ANISOU 2409 O LYS A1146 17289 13089 10184 -801 806 1367 O
ATOM 2410 CB LYS A1146 37.566 19.020 -86.973 1.00103.36 C
ANISOU 2410 CB LYS A1146 15853 12681 10737 -1611 725 1957 C
ATOM 2411 N ARG A1147 39.073 21.814 -86.746 1.00102.98 N
ANISOU 2411 N ARG A1147 16167 12926 10035 -836 1410 1700 N
ATOM 2412 CA ARG A1147 39.046 23.271 -86.615 1.00101.94 C
ANISOU 2412 CA ARG A1147 15999 13088 9646 -507 1558 1576 C
ATOM 2413 C ARG A1147 39.810 23.952 -87.749 1.00 98.34 C
ANISOU 2413 C ARG A1147 16299 12148 8917 -247 1783 1291 C
ATOM 2414 O ARG A1147 39.322 24.925 -88.340 1.00 98.74 O
ANISOU 2414 O ARG A1147 16583 12242 8692 -7 1678 1167 O
ATOM 2415 CB ARG A1147 39.595 23.697 -85.252 1.00 99.94 C
ANISOU 2415 CB ARG A1147 15190 13269 9513 -430 1905 1706 C
ATOM 2416 CG ARG A1147 38.783 23.198 -84.066 1.00 95.98 C
ANISOU 2416 CG ARG A1147 13940 13335 9194 -651 1731 2019 C
ATOM 2417 CD ARG A1147 39.264 23.810 -82.761 1.00 89.67 C
ANISOU 2417 CD ARG A1147 12600 13065 8403 -509 2052 2091 C
ATOM 2418 NE ARG A1147 40.376 23.072 -82.166 1.00 88.57 N
ANISOU 2418 NE ARG A1147 12425 12809 8420 -555 2322 2232 N
ATOM 2419 CZ ARG A1147 40.235 22.153 -81.215 1.00 90.77 C
ANISOU 2419 CZ ARG A1147 12275 13359 8854 -759 2282 2602 C
ATOM 2420 NH1 ARG A1147 39.029 21.853 -80.754 1.00 93.40 N
ANISOU 2420 NH1 ARG A1147 12174 14085 9227 -975 2030 2850 N
ATOM 2421 NH2 ARG A1147 41.297 21.530 -80.725 1.00 89.56 N
ANISOU 2421 NH2 ARG A1147 12127 13074 8829 -738 2503 2728 N
ATOM 2422 N VAL A1148 41.024 23.470 -88.047 1.00100.14 N
ANISOU 2422 N VAL A1148 16913 11905 9229 -278 2119 1192 N
ATOM 2423 CA VAL A1148 41.826 24.060 -89.125 1.00101.20 C
ANISOU 2423 CA VAL A1148 17787 11550 9117 -64 2418 918 C
ATOM 2424 C VAL A1148 41.121 23.912 -90.476 1.00 99.13 C
ANISOU 2424 C VAL A1148 18101 11031 8533 -52 2048 801 C
ATOM 2425 O VAL A1148 41.111 24.843 -91.296 1.00 97.50 O
ANISOU 2425 O VAL A1148 18397 10680 7969 219 2128 670 O
ATOM 2426 CB VAL A1148 43.239 23.443 -89.139 1.00102.85 C
ANISOU 2426 CB VAL A1148 18228 11310 9542 -141 2839 796 C
ATOM 2427 CG1 VAL A1148 44.050 23.965 -90.316 1.00102.70 C
ANISOU 2427 CG1 VAL A1148 18993 10751 9275 34 3191 496 C
ATOM 2428 CG2 VAL A1148 43.961 23.759 -87.840 1.00101.92 C
ANISOU 2428 CG2 VAL A1148 17551 11495 9679 -68 3184 855 C
ATOM 2429 N ILE A1149 40.504 22.751 -90.719 1.00100.45 N
ANISOU 2429 N ILE A1149 18194 11147 8824 -329 1639 842 N
ATOM 2430 CA ILE A1149 39.806 22.509 -91.978 1.00105.00 C
ANISOU 2430 CA ILE A1149 19257 11536 9103 -320 1231 666 C
ATOM 2431 C ILE A1149 38.571 23.396 -92.085 1.00105.35 C
ANISOU 2431 C ILE A1149 19146 11998 8884 -110 833 701 C
ATOM 2432 O ILE A1149 38.267 23.925 -93.160 1.00107.02 O
ANISOU 2432 O ILE A1149 19912 12086 8665 130 655 551 O
ATOM 2433 CB ILE A1149 39.468 21.009 -92.112 1.00111.19 C
ANISOU 2433 CB ILE A1149 19891 12160 10197 -693 913 645 C
ATOM 2434 CG1 ILE A1149 40.728 20.197 -92.431 1.00110.48 C
ANISOU 2434 CG1 ILE A1149 20166 11523 10290 -833 1274 515 C
ATOM 2435 CG2 ILE A1149 38.402 20.754 -93.163 1.00117.46 C
ANISOU 2435 CG2 ILE A1149 20928 12955 10744 -700 356 440 C
ATOM 2436 CD1 ILE A1149 40.520 18.698 -92.350 1.00110.84 C
ANISOU 2436 CD1 ILE A1149 19963 11368 10781 -1212 1044 530 C
ATOM 2437 N THR A1150 37.855 23.594 -90.972 1.00102.83 N
ANISOU 2437 N THR A1150 18078 12187 8805 -176 696 897 N
ATOM 2438 CA THR A1150 36.715 24.508 -90.967 1.00 99.48 C
ANISOU 2438 CA THR A1150 17428 12171 8200 37 346 903 C
ATOM 2439 C THR A1150 37.162 25.941 -91.242 1.00 98.08 C
ANISOU 2439 C THR A1150 17615 11936 7715 449 659 861 C
ATOM 2440 O THR A1150 36.468 26.694 -91.936 1.00100.65 O
ANISOU 2440 O THR A1150 18204 12316 7724 729 373 798 O
ATOM 2441 CB THR A1150 35.979 24.406 -89.627 1.00101.53 C
ANISOU 2441 CB THR A1150 16776 12986 8814 -149 233 1100 C
ATOM 2442 OG1 THR A1150 35.464 23.078 -89.471 1.00105.42 O
ANISOU 2442 OG1 THR A1150 16966 13477 9613 -534 -49 1156 O
ATOM 2443 CG2 THR A1150 34.816 25.390 -89.545 1.00100.00 C
ANISOU 2443 CG2 THR A1150 16272 13227 8498 71 -107 1064 C
ATOM 2444 N THR A1151 38.338 26.323 -90.735 1.00 94.49 N
ANISOU 2444 N THR A1151 17189 11339 7374 504 1252 881 N
ATOM 2445 CA THR A1151 38.872 27.656 -91.009 1.00 93.47 C
ANISOU 2445 CA THR A1151 17410 11063 7039 868 1643 814 C
ATOM 2446 C THR A1151 39.206 27.829 -92.490 1.00104.01 C
ANISOU 2446 C THR A1151 19699 11882 7938 1060 1692 691 C
ATOM 2447 O THR A1151 38.898 28.866 -93.088 1.00104.57 O
ANISOU 2447 O THR A1151 20132 11900 7699 1400 1673 697 O
ATOM 2448 CB THR A1151 40.107 27.914 -90.145 1.00 89.46 C
ANISOU 2448 CB THR A1151 16677 10500 6811 854 2275 783 C
ATOM 2449 OG1 THR A1151 39.781 27.701 -88.766 1.00 96.47 O
ANISOU 2449 OG1 THR A1151 16699 11928 8026 691 2206 912 O
ATOM 2450 CG2 THR A1151 40.590 29.347 -90.319 1.00 88.70 C
ANISOU 2450 CG2 THR A1151 16828 10259 6613 1208 2717 683 C
ATOM 2451 N PHE A1152 39.863 26.830 -93.089 1.00101.07 N
ANISOU 2451 N PHE A1152 19750 11118 7533 859 1780 583 N
ATOM 2452 CA PHE A1152 40.103 26.850 -94.534 1.00102.05 C
ANISOU 2452 CA PHE A1152 20782 10807 7186 1009 1787 444 C
ATOM 2453 C PHE A1152 38.803 26.896 -95.331 1.00106.77 C
ANISOU 2453 C PHE A1152 21561 11605 7401 1158 1106 441 C
ATOM 2454 O PHE A1152 38.701 27.615 -96.332 1.00108.34 O
ANISOU 2454 O PHE A1152 22423 11638 7103 1489 1082 425 O
ATOM 2455 CB PHE A1152 40.925 25.635 -94.953 1.00102.82 C
ANISOU 2455 CB PHE A1152 21180 10507 7380 720 1940 279 C
ATOM 2456 CG PHE A1152 42.391 25.795 -94.730 1.00100.92 C
ANISOU 2456 CG PHE A1152 21119 9894 7332 702 2666 186 C
ATOM 2457 CD1 PHE A1152 43.026 26.983 -95.058 1.00103.20 C
ANISOU 2457 CD1 PHE A1152 21837 9956 7417 997 3185 151 C
ATOM 2458 CD2 PHE A1152 43.137 24.765 -94.189 1.00 96.23 C
ANISOU 2458 CD2 PHE A1152 20246 9153 7163 399 2841 122 C
ATOM 2459 CE1 PHE A1152 44.381 27.135 -94.858 1.00102.50 C
ANISOU 2459 CE1 PHE A1152 21869 9513 7564 969 3873 -3 C
ATOM 2460 CE2 PHE A1152 44.484 24.914 -93.982 1.00 94.38 C
ANISOU 2460 CE2 PHE A1152 20135 8589 7137 403 3478 -18 C
ATOM 2461 CZ PHE A1152 45.113 26.097 -94.319 1.00 98.90 C
ANISOU 2461 CZ PHE A1152 21108 8948 7523 677 4001 -109 C
ATOM 2462 N ARG A1153 37.802 26.134 -94.898 1.00110.14 N
ANISOU 2462 N ARG A1153 21402 12388 8058 930 553 451 N
ATOM 2463 CA ARG A1153 36.577 25.943 -95.662 1.00117.21 C
ANISOU 2463 CA ARG A1153 22395 13472 8667 1021 -149 351 C
ATOM 2464 C ARG A1153 35.674 27.170 -95.598 1.00122.00 C
ANISOU 2464 C ARG A1153 22861 14412 9082 1398 -417 457 C
ATOM 2465 O ARG A1153 35.020 27.515 -96.589 1.00125.26 O
ANISOU 2465 O ARG A1153 23720 14838 9034 1694 -839 383 O
ATOM 2466 CB ARG A1153 35.872 24.689 -95.136 1.00116.06 C
ANISOU 2466 CB ARG A1153 21595 13548 8953 608 -567 294 C
ATOM 2467 CG ARG A1153 34.451 24.441 -95.590 1.00122.93 C
ANISOU 2467 CG ARG A1153 22264 14720 9723 637 -1324 141 C
ATOM 2468 CD ARG A1153 33.966 23.139 -94.961 1.00128.30 C
ANISOU 2468 CD ARG A1153 22273 15517 10957 160 -1558 93 C
ATOM 2469 NE ARG A1153 32.574 22.832 -95.269 1.00139.78 N
ANISOU 2469 NE ARG A1153 23393 17271 12446 132 -2261 -112 N
ATOM 2470 CZ ARG A1153 31.553 23.146 -94.478 1.00145.98 C
ANISOU 2470 CZ ARG A1153 23456 18509 13503 103 -2530 -38 C
ATOM 2471 NH1 ARG A1153 30.314 22.830 -94.831 1.00152.84 N
ANISOU 2471 NH1 ARG A1153 24020 19617 14436 75 -3170 -294 N
ATOM 2472 NH2 ARG A1153 31.769 23.773 -93.330 1.00143.99 N
ANISOU 2472 NH2 ARG A1153 22754 18488 13469 101 -2157 246 N
ATOM 2473 N THR A1154 35.640 27.847 -94.452 1.00108.65 N
ANISOU 2473 N THR A1154 20554 12998 7731 1414 -186 614 N
ATOM 2474 CA THR A1154 34.770 28.998 -94.254 1.00109.83 C
ANISOU 2474 CA THR A1154 20450 13469 7813 1747 -424 690 C
ATOM 2475 C THR A1154 35.500 30.331 -94.318 1.00108.40 C
ANISOU 2475 C THR A1154 20635 13058 7494 2107 125 795 C
ATOM 2476 O THR A1154 34.914 31.322 -94.764 1.00111.25 O
ANISOU 2476 O THR A1154 21201 13463 7607 2501 -78 853 O
ATOM 2477 CB THR A1154 34.055 28.898 -92.901 1.00107.67 C
ANISOU 2477 CB THR A1154 19146 13723 8040 1521 -577 744 C
ATOM 2478 OG1 THR A1154 35.020 28.962 -91.843 1.00102.70 O
ANISOU 2478 OG1 THR A1154 18173 13104 7746 1353 33 838 O
ATOM 2479 CG2 THR A1154 33.287 27.589 -92.801 1.00109.62 C
ANISOU 2479 CG2 THR A1154 18993 14159 8498 1142 -1066 654 C
ATOM 2480 N GLY A1155 36.757 30.384 -93.889 1.00104.49 N
ANISOU 2480 N GLY A1155 20210 12300 7190 1994 814 806 N
ATOM 2481 CA GLY A1155 37.441 31.657 -93.774 1.00103.07 C
ANISOU 2481 CA GLY A1155 20222 11915 7024 2290 1391 858 C
ATOM 2482 C GLY A1155 36.975 32.487 -92.599 1.00112.61 C
ANISOU 2482 C GLY A1155 20610 13559 8620 2364 1421 893 C
ATOM 2483 O GLY A1155 37.029 33.719 -92.657 1.00110.45 O
ANISOU 2483 O GLY A1155 20446 13182 8338 2700 1672 928 O
ATOM 2484 N THR A1156 36.499 31.841 -91.535 1.00108.32 N
ANISOU 2484 N THR A1156 19239 13493 8422 2056 1188 882 N
ATOM 2485 CA THR A1156 36.035 32.512 -90.329 1.00103.40 C
ANISOU 2485 CA THR A1156 17764 13365 8158 2078 1215 878 C
ATOM 2486 C THR A1156 36.757 31.937 -89.116 1.00103.78 C
ANISOU 2486 C THR A1156 17224 13639 8567 1754 1580 858 C
ATOM 2487 O THR A1156 37.482 30.943 -89.206 1.00107.53 O
ANISOU 2487 O THR A1156 17913 13891 9051 1506 1728 869 O
ATOM 2488 CB THR A1156 34.515 32.370 -90.145 1.00103.41 C
ANISOU 2488 CB THR A1156 17246 13850 8194 2051 513 891 C
ATOM 2489 OG1 THR A1156 34.178 30.988 -89.961 1.00100.75 O
ANISOU 2489 OG1 THR A1156 16664 13676 7942 1649 193 907 O
ATOM 2490 CG2 THR A1156 33.760 32.928 -91.351 1.00104.41 C
ANISOU 2490 CG2 THR A1156 17937 13794 7940 2426 69 898 C
ATOM 2491 N TRP A1157 36.545 32.577 -87.968 1.00103.14 N
ANISOU 2491 N TRP A1157 16387 14021 8780 1778 1712 816 N
ATOM 2492 CA TRP A1157 37.089 32.125 -86.694 1.00 95.60 C
ANISOU 2492 CA TRP A1157 14788 13417 8118 1524 1998 806 C
ATOM 2493 C TRP A1157 36.117 31.269 -85.894 1.00 89.97 C
ANISOU 2493 C TRP A1157 13391 13262 7533 1214 1571 932 C
ATOM 2494 O TRP A1157 36.433 30.928 -84.749 1.00 89.99 O
ANISOU 2494 O TRP A1157 12816 13644 7733 1028 1775 973 O
ATOM 2495 CB TRP A1157 37.506 33.318 -85.831 1.00 99.25 C
ANISOU 2495 CB TRP A1157 14781 14111 8817 1727 2443 635 C
ATOM 2496 CG TRP A1157 38.688 34.071 -86.329 1.00103.96 C
ANISOU 2496 CG TRP A1157 15904 14169 9426 1959 3026 480 C
ATOM 2497 CD1 TRP A1157 38.690 35.317 -86.882 1.00107.35 C
ANISOU 2497 CD1 TRP A1157 16639 14301 9848 2305 3232 392 C
ATOM 2498 CD2 TRP A1157 40.051 33.631 -86.321 1.00103.42 C
ANISOU 2498 CD2 TRP A1157 16110 13760 9425 1862 3509 385 C
ATOM 2499 NE1 TRP A1157 39.970 35.684 -87.212 1.00106.29 N
ANISOU 2499 NE1 TRP A1157 16949 13654 9782 2403 3858 247 N
ATOM 2500 CE2 TRP A1157 40.825 34.666 -86.879 1.00104.22 C
ANISOU 2500 CE2 TRP A1157 16661 13368 9569 2135 4028 212 C
ATOM 2501 CE3 TRP A1157 40.691 32.463 -85.895 1.00102.59 C
ANISOU 2501 CE3 TRP A1157 15902 13695 9382 1579 3562 428 C
ATOM 2502 CZ2 TRP A1157 42.208 34.568 -87.028 1.00105.45 C
ANISOU 2502 CZ2 TRP A1157 17139 13088 9837 2113 4602 32 C
ATOM 2503 CZ3 TRP A1157 42.067 32.368 -86.042 1.00102.03 C
ANISOU 2503 CZ3 TRP A1157 16153 13202 9413 1588 4086 255 C
ATOM 2504 CH2 TRP A1157 42.809 33.414 -86.604 1.00102.65 C
ANISOU 2504 CH2 TRP A1157 16649 12811 9542 1843 4603 35 C
ATOM 2505 N ASP A1158 34.947 30.944 -86.462 1.00115.17 N
ANISOU 2505 N ASP A1158 18085 20376 5298 113 -971 -350 N
ATOM 2506 CA ASP A1158 33.827 30.387 -85.697 1.00117.89 C
ANISOU 2506 CA ASP A1158 18037 20788 5968 143 -1411 -410 C
ATOM 2507 C ASP A1158 34.196 29.091 -84.979 1.00116.79 C
ANISOU 2507 C ASP A1158 17625 20583 6165 12 -1339 -843 C
ATOM 2508 O ASP A1158 33.759 28.861 -83.841 1.00119.00 O
ANISOU 2508 O ASP A1158 17532 20824 6859 45 -1487 -873 O
ATOM 2509 CB ASP A1158 32.636 30.161 -86.627 1.00122.70 C
ANISOU 2509 CB ASP A1158 18768 21565 6285 141 -1875 -366 C
ATOM 2510 CG ASP A1158 32.284 31.399 -87.428 1.00130.87 C
ANISOU 2510 CG ASP A1158 20116 22658 6952 285 -1955 63 C
ATOM 2511 OD1 ASP A1158 32.952 32.436 -87.237 1.00132.63 O
ANISOU 2511 OD1 ASP A1158 20477 22757 7158 374 -1623 328 O
ATOM 2512 OD2 ASP A1158 31.352 31.334 -88.257 1.00137.29 O
ANISOU 2512 OD2 ASP A1158 21048 23630 7487 301 -2337 132 O
ATOM 2513 N ALA A1159 35.044 28.263 -85.605 1.00116.49 N
ANISOU 2513 N ALA A1159 17792 20507 5964 -121 -1077 -1171 N
ATOM 2514 CA ALA A1159 35.460 26.999 -85.001 1.00113.06 C
ANISOU 2514 CA ALA A1159 17154 19973 5830 -222 -970 -1581 C
ATOM 2515 C ALA A1159 36.242 27.221 -83.714 1.00106.96 C
ANISOU 2515 C ALA A1159 16078 19086 5478 -156 -698 -1587 C
ATOM 2516 O ALA A1159 36.243 26.356 -82.830 1.00102.63 O
ANISOU 2516 O ALA A1159 15268 18448 5279 -179 -729 -1830 O
ATOM 2517 CB ALA A1159 36.292 26.187 -85.994 1.00110.74 C
ANISOU 2517 CB ALA A1159 17172 19638 5266 -336 -688 -1896 C
ATOM 2518 N TYR A1160 36.908 28.366 -83.591 1.00106.40 N
ANISOU 2518 N TYR A1160 16056 19002 5370 -81 -422 -1327 N
ATOM 2519 CA TYR A1160 37.682 28.690 -82.403 1.00102.88 C
ANISOU 2519 CA TYR A1160 15325 18468 5295 -34 -154 -1322 C
ATOM 2520 C TYR A1160 36.941 29.652 -81.484 1.00100.97 C
ANISOU 2520 C TYR A1160 14876 18224 5262 86 -360 -971 C
ATOM 2521 O TYR A1160 37.137 29.609 -80.261 1.00 94.73 O
ANISOU 2521 O TYR A1160 13778 17229 4987 116 -310 -990 O
ATOM 2522 CB TYR A1160 39.023 29.302 -82.820 1.00101.45 C
ANISOU 2522 CB TYR A1160 15316 18247 4984 -73 362 -1304 C
ATOM 2523 CG TYR A1160 39.981 28.281 -83.390 1.00106.81 C
ANISOU 2523 CG TYR A1160 16090 18882 5609 -160 652 -1691 C
ATOM 2524 CD1 TYR A1160 40.745 27.467 -82.563 1.00 98.09 C
ANISOU 2524 CD1 TYR A1160 14696 17701 4874 -149 840 -1995 C
ATOM 2525 CD2 TYR A1160 40.101 28.117 -84.767 1.00105.40 C
ANISOU 2525 CD2 TYR A1160 16310 18729 5007 -226 736 -1745 C
ATOM 2526 CE1 TYR A1160 41.617 26.528 -83.094 1.00100.20 C
ANISOU 2526 CE1 TYR A1160 15050 17908 5113 -187 1121 -2332 C
ATOM 2527 CE2 TYR A1160 40.964 27.183 -85.305 1.00107.40 C
ANISOU 2527 CE2 TYR A1160 16665 18925 5219 -285 1024 -2090 C
ATOM 2528 CZ TYR A1160 41.720 26.392 -84.467 1.00108.00 C
ANISOU 2528 CZ TYR A1160 16432 18915 5688 -260 1222 -2378 C
ATOM 2529 OH TYR A1160 42.580 25.461 -85.005 1.00107.16 O
ANISOU 2529 OH TYR A1160 16424 18733 5559 -279 1524 -2705 O
ATOM 2530 N ARG A 431 36.085 30.507 -82.064 1.00107.75 N
ANISOU 2530 N ARG A 431 15915 19156 5868 165 -585 -627 N
ATOM 2531 CA ARG A 431 35.132 31.306 -81.294 1.00107.63 C
ANISOU 2531 CA ARG A 431 15711 19135 6047 311 -843 -291 C
ATOM 2532 C ARG A 431 34.269 30.436 -80.389 1.00103.12 C
ANISOU 2532 C ARG A 431 14782 18545 5852 306 -1189 -463 C
ATOM 2533 O ARG A 431 33.961 30.826 -79.253 1.00103.90 O
ANISOU 2533 O ARG A 431 14621 18460 6398 378 -1229 -316 O
ATOM 2534 CB ARG A 431 34.253 32.126 -82.241 1.00118.83 C
ANISOU 2534 CB ARG A 431 17390 20630 7131 421 -1077 58 C
ATOM 2535 N VAL A 432 33.865 29.257 -80.877 1.00102.42 N
ANISOU 2535 N VAL A 432 14703 18519 5692 193 -1399 -772 N
ATOM 2536 CA VAL A 432 32.971 28.400 -80.099 1.00102.40 C
ANISOU 2536 CA VAL A 432 14399 18484 6024 153 -1707 -947 C
ATOM 2537 C VAL A 432 33.687 27.884 -78.853 1.00 97.40 C
ANISOU 2537 C VAL A 432 13536 17639 5833 134 -1487 -1151 C
ATOM 2538 O VAL A 432 33.141 27.919 -77.739 1.00 97.80 O
ANISOU 2538 O VAL A 432 13316 17536 6310 176 -1616 -1081 O
ATOM 2539 CB VAL A 432 32.441 27.250 -80.977 1.00105.99 C
ANISOU 2539 CB VAL A 432 14969 19000 6302 -4 -1917 -1242 C
ATOM 2540 CG1 VAL A 432 31.886 26.121 -80.120 1.00107.28 C
ANISOU 2540 CG1 VAL A 432 14870 19059 6833 -105 -2078 -1530 C
ATOM 2541 CG2 VAL A 432 31.366 27.760 -81.919 1.00 99.68 C
ANISOU 2541 CG2 VAL A 432 14286 18374 5215 34 -2258 -1008 C
ATOM 2542 N VAL A 433 34.934 27.434 -79.019 1.00 98.92 N
ANISOU 2542 N VAL A 433 13836 17739 6010 80 -1128 -1380 N
ATOM 2543 CA VAL A 433 35.723 26.955 -77.889 1.00 95.51 C
ANISOU 2543 CA VAL A 433 13192 17041 6056 94 -902 -1547 C
ATOM 2544 C VAL A 433 36.000 28.095 -76.915 1.00 92.92 C
ANISOU 2544 C VAL A 433 12696 16548 6060 184 -769 -1240 C
ATOM 2545 O VAL A 433 35.948 27.909 -75.692 1.00 87.00 O
ANISOU 2545 O VAL A 433 11702 15599 5753 214 -792 -1259 O
ATOM 2546 CB VAL A 433 37.023 26.299 -78.394 1.00 96.45 C
ANISOU 2546 CB VAL A 433 13448 17143 6057 53 -539 -1843 C
ATOM 2547 CG1 VAL A 433 37.874 25.804 -77.232 1.00 96.87 C
ANISOU 2547 CG1 VAL A 433 13261 16956 6590 113 -329 -2000 C
ATOM 2548 CG2 VAL A 433 36.705 25.159 -79.358 1.00100.27 C
ANISOU 2548 CG2 VAL A 433 14139 17760 6198 -55 -648 -2163 C
ATOM 2549 N LEU A 434 36.260 29.302 -77.438 1.00 96.28 N
ANISOU 2549 N LEU A 434 13283 17042 6258 215 -619 -951 N
ATOM 2550 CA LEU A 434 36.538 30.440 -76.561 1.00104.54 C
ANISOU 2550 CA LEU A 434 14215 17914 7592 266 -451 -671 C
ATOM 2551 C LEU A 434 35.329 30.823 -75.711 1.00110.37 C
ANISOU 2551 C LEU A 434 14770 18565 8600 347 -754 -447 C
ATOM 2552 O LEU A 434 35.474 31.086 -74.509 1.00118.82 O
ANISOU 2552 O LEU A 434 15636 19424 10086 359 -677 -392 O
ATOM 2553 CB LEU A 434 37.018 31.644 -77.374 1.00109.02 C
ANISOU 2553 CB LEU A 434 15054 18542 7826 267 -194 -412 C
ATOM 2554 CG LEU A 434 38.432 31.604 -77.951 1.00113.64 C
ANISOU 2554 CG LEU A 434 15775 19155 8246 166 237 -589 C
ATOM 2555 CD1 LEU A 434 38.871 33.002 -78.334 1.00116.82 C
ANISOU 2555 CD1 LEU A 434 16405 19522 8460 144 542 -287 C
ATOM 2556 CD2 LEU A 434 39.390 31.031 -76.924 1.00109.63 C
ANISOU 2556 CD2 LEU A 434 14967 18510 8177 127 434 -846 C
ATOM 2557 N VAL A 435 34.131 30.855 -76.302 1.00108.97 N
ANISOU 2557 N VAL A 435 14651 18562 8190 403 -1098 -324 N
ATOM 2558 CA VAL A 435 32.965 31.219 -75.498 1.00106.54 C
ANISOU 2558 CA VAL A 435 14134 18184 8161 492 -1366 -119 C
ATOM 2559 C VAL A 435 32.612 30.102 -74.515 1.00104.47 C
ANISOU 2559 C VAL A 435 13607 17800 8288 422 -1513 -396 C
ATOM 2560 O VAL A 435 32.162 30.380 -73.391 1.00107.17 O
ANISOU 2560 O VAL A 435 13745 17956 9020 460 -1556 -283 O
ATOM 2561 CB VAL A 435 31.770 31.631 -76.385 1.00110.96 C
ANISOU 2561 CB VAL A 435 14781 19004 8377 600 -1706 108 C
ATOM 2562 CG1 VAL A 435 32.143 32.839 -77.233 1.00114.47 C
ANISOU 2562 CG1 VAL A 435 15536 19506 8451 702 -1522 434 C
ATOM 2563 CG2 VAL A 435 31.288 30.497 -77.267 1.00117.30 C
ANISOU 2563 CG2 VAL A 435 15620 20078 8871 502 -1988 -182 C
ATOM 2564 N LYS A 436 32.827 28.834 -74.899 1.00100.60 N
ANISOU 2564 N LYS A 436 13150 17381 7694 315 -1556 -760 N
ATOM 2565 CA LYS A 436 32.640 27.725 -73.963 1.00 95.24 C
ANISOU 2565 CA LYS A 436 12284 16531 7370 248 -1625 -1033 C
ATOM 2566 C LYS A 436 33.563 27.853 -72.749 1.00 86.68 C
ANISOU 2566 C LYS A 436 11079 15166 6688 280 -1355 -1037 C
ATOM 2567 O LYS A 436 33.129 27.692 -71.596 1.00 83.81 O
ANISOU 2567 O LYS A 436 10534 14610 6701 286 -1427 -1028 O
ATOM 2568 CB LYS A 436 32.878 26.401 -74.693 1.00 95.49 C
ANISOU 2568 CB LYS A 436 12448 16655 7178 135 -1639 -1421 C
ATOM 2569 CG LYS A 436 32.816 25.166 -73.813 1.00 97.98 C
ANISOU 2569 CG LYS A 436 12652 16755 7822 72 -1648 -1722 C
ATOM 2570 CD LYS A 436 33.104 23.911 -74.623 1.00105.71 C
ANISOU 2570 CD LYS A 436 13819 17795 8551 -35 -1606 -2103 C
ATOM 2571 CE LYS A 436 34.480 23.975 -75.272 1.00110.54 C
ANISOU 2571 CE LYS A 436 14606 18437 8957 15 -1274 -2176 C
ATOM 2572 NZ LYS A 436 34.755 22.776 -76.117 1.00114.78 N
ANISOU 2572 NZ LYS A 436 15359 19021 9233 -82 -1200 -2549 N
ATOM 2573 N GLU A 437 34.838 28.174 -72.994 1.00 79.54 N
ANISOU 2573 N GLU A 437 10270 14253 5698 291 -1040 -1051 N
ATOM 2574 CA GLU A 437 35.794 28.313 -71.900 1.00 80.37 C
ANISOU 2574 CA GLU A 437 10233 14154 6150 312 -799 -1072 C
ATOM 2575 C GLU A 437 35.476 29.527 -71.033 1.00 80.75 C
ANISOU 2575 C GLU A 437 10179 14071 6431 341 -780 -751 C
ATOM 2576 O GLU A 437 35.633 29.474 -69.806 1.00 78.18 O
ANISOU 2576 O GLU A 437 9689 13549 6465 344 -741 -763 O
ATOM 2577 CB GLU A 437 37.217 28.389 -72.456 1.00 82.14 C
ANISOU 2577 CB GLU A 437 10543 14452 6214 299 -464 -1184 C
ATOM 2578 CG GLU A 437 37.665 27.101 -73.140 1.00 92.99 C
ANISOU 2578 CG GLU A 437 12010 15900 7421 290 -422 -1534 C
ATOM 2579 CD GLU A 437 38.985 27.243 -73.880 1.00 97.93 C
ANISOU 2579 CD GLU A 437 12727 16635 7846 278 -74 -1637 C
ATOM 2580 OE1 GLU A 437 39.360 28.385 -74.221 1.00 98.98 O
ANISOU 2580 OE1 GLU A 437 12925 16837 7844 240 103 -1424 O
ATOM 2581 OE2 GLU A 437 39.644 26.208 -74.125 1.00 96.68 O
ANISOU 2581 OE2 GLU A 437 12586 16482 7668 306 49 -1937 O
ATOM 2582 N ARG A 438 35.021 30.624 -71.652 1.00 82.89 N
ANISOU 2582 N ARG A 438 10572 14435 6485 370 -796 -458 N
ATOM 2583 CA ARG A 438 34.629 31.804 -70.884 1.00 81.25 C
ANISOU 2583 CA ARG A 438 10309 14075 6487 410 -755 -143 C
ATOM 2584 C ARG A 438 33.441 31.511 -69.970 1.00 75.57 C
ANISOU 2584 C ARG A 438 9405 13238 6073 445 -1020 -110 C
ATOM 2585 O ARG A 438 33.410 31.962 -68.816 1.00 70.17 O
ANISOU 2585 O ARG A 438 8606 12338 5719 441 -939 -9 O
ATOM 2586 CB ARG A 438 34.304 32.961 -71.830 1.00 82.50 C
ANISOU 2586 CB ARG A 438 10681 14344 6320 477 -721 174 C
ATOM 2587 N LYS A 439 32.463 30.739 -70.465 1.00 77.23 N
ANISOU 2587 N LYS A 439 9584 13590 6170 455 -1322 -215 N
ATOM 2588 CA LYS A 439 31.311 30.374 -69.640 1.00 83.18 C
ANISOU 2588 CA LYS A 439 10142 14246 7216 458 -1556 -223 C
ATOM 2589 C LYS A 439 31.722 29.487 -68.467 1.00 81.11 C
ANISOU 2589 C LYS A 439 9768 13749 7299 385 -1478 -462 C
ATOM 2590 O LYS A 439 31.262 29.694 -67.329 1.00 83.18 O
ANISOU 2590 O LYS A 439 9900 13806 7896 387 -1487 -380 O
ATOM 2591 CB LYS A 439 30.255 29.678 -70.502 1.00 85.49 C
ANISOU 2591 CB LYS A 439 10412 14784 7287 438 -1884 -334 C
ATOM 2592 N ALA A 440 32.570 28.482 -68.736 1.00 81.22 N
ANISOU 2592 N ALA A 440 9850 13784 7227 338 -1395 -755 N
ATOM 2593 CA ALA A 440 33.120 27.651 -67.665 1.00 74.55 C
ANISOU 2593 CA ALA A 440 8936 12717 6674 320 -1302 -961 C
ATOM 2594 C ALA A 440 33.839 28.498 -66.618 1.00 68.66 C
ANISOU 2594 C ALA A 440 8117 11801 6169 345 -1097 -802 C
ATOM 2595 O ALA A 440 33.703 28.256 -65.409 1.00 64.07 O
ANISOU 2595 O ALA A 440 7445 11005 5893 339 -1102 -825 O
ATOM 2596 CB ALA A 440 34.067 26.601 -68.247 1.00 75.90 C
ANISOU 2596 CB ALA A 440 9210 12948 6682 319 -1196 -1262 C
ATOM 2597 N ALA A 441 34.595 29.508 -67.070 1.00 67.88 N
ANISOU 2597 N ALA A 441 8077 11795 5919 352 -903 -646 N
ATOM 2598 CA ALA A 441 35.348 30.354 -66.148 1.00 68.28 C
ANISOU 2598 CA ALA A 441 8064 11712 6167 327 -686 -525 C
ATOM 2599 C ALA A 441 34.418 31.189 -65.273 1.00 67.17 C
ANISOU 2599 C ALA A 441 7874 11394 6254 321 -739 -279 C
ATOM 2600 O ALA A 441 34.674 31.356 -64.074 1.00 64.04 O
ANISOU 2600 O ALA A 441 7398 10811 6123 284 -657 -270 O
ATOM 2601 CB ALA A 441 36.308 31.255 -66.926 1.00 62.98 C
ANISOU 2601 CB ALA A 441 7488 11179 5264 293 -433 -433 C
ATOM 2602 N GLN A 442 33.345 31.735 -65.858 1.00 69.27 N
ANISOU 2602 N GLN A 442 8188 11723 6408 370 -872 -75 N
ATOM 2603 CA GLN A 442 32.383 32.506 -65.068 1.00 77.29 C
ANISOU 2603 CA GLN A 442 9146 12568 7655 396 -909 160 C
ATOM 2604 C GLN A 442 31.710 31.639 -64.006 1.00 78.49 C
ANISOU 2604 C GLN A 442 9160 12552 8110 367 -1055 17 C
ATOM 2605 O GLN A 442 31.543 32.071 -62.854 1.00 77.66 O
ANISOU 2605 O GLN A 442 9008 12221 8277 337 -967 108 O
ATOM 2606 CB GLN A 442 31.338 33.150 -65.982 1.00 86.15 C
ANISOU 2606 CB GLN A 442 10316 13831 8587 505 -1054 401 C
ATOM 2607 CG GLN A 442 31.910 34.187 -66.939 1.00 95.77 C
ANISOU 2607 CG GLN A 442 11732 15155 9501 548 -873 606 C
ATOM 2608 CD GLN A 442 30.916 34.625 -68.000 1.00103.63 C
ANISOU 2608 CD GLN A 442 12800 16341 10234 697 -1068 828 C
ATOM 2609 OE1 GLN A 442 29.820 34.072 -68.110 1.00109.29 O
ANISOU 2609 OE1 GLN A 442 13374 17166 10984 753 -1367 791 O
ATOM 2610 NE2 GLN A 442 31.296 35.624 -68.787 1.00102.75 N
ANISOU 2610 NE2 GLN A 442 12911 16280 9850 759 -897 1058 N
ATOM 2611 N THR A 443 31.333 30.407 -64.373 1.00 76.35 N
ANISOU 2611 N THR A 443 8856 12370 7785 354 -1249 -218 N
ATOM 2612 CA THR A 443 30.743 29.483 -63.400 1.00 70.68 C
ANISOU 2612 CA THR A 443 8051 11468 7336 304 -1350 -381 C
ATOM 2613 C THR A 443 31.714 29.180 -62.256 1.00 66.69 C
ANISOU 2613 C THR A 443 7563 10751 7026 277 -1186 -486 C
ATOM 2614 O THR A 443 31.334 29.205 -61.070 1.00 67.45 O
ANISOU 2614 O THR A 443 7620 10617 7390 243 -1164 -453 O
ATOM 2615 CB THR A 443 30.319 28.196 -64.110 1.00 67.37 C
ANISOU 2615 CB THR A 443 7641 11176 6780 264 -1538 -645 C
ATOM 2616 OG1 THR A 443 29.356 28.506 -65.125 1.00 68.91 O
ANISOU 2616 OG1 THR A 443 7793 11609 6780 281 -1731 -547 O
ATOM 2617 CG2 THR A 443 29.708 27.209 -63.124 1.00 62.01 C
ANISOU 2617 CG2 THR A 443 6916 10275 6370 188 -1600 -824 C
ATOM 2618 N LEU A 444 32.972 28.871 -62.605 1.00 59.64 N
ANISOU 2618 N LEU A 444 6722 9949 5990 298 -1072 -620 N
ATOM 2619 CA LEU A 444 34.006 28.626 -61.601 1.00 59.42 C
ANISOU 2619 CA LEU A 444 6675 9789 6113 304 -940 -714 C
ATOM 2620 C LEU A 444 34.169 29.820 -60.666 1.00 62.67 C
ANISOU 2620 C LEU A 444 7052 10075 6685 249 -800 -504 C
ATOM 2621 O LEU A 444 34.283 29.647 -59.446 1.00 60.93 O
ANISOU 2621 O LEU A 444 6813 9664 6674 226 -778 -531 O
ATOM 2622 CB LEU A 444 35.333 28.295 -62.280 1.00 56.64 C
ANISOU 2622 CB LEU A 444 6335 9615 5571 352 -824 -866 C
ATOM 2623 CG LEU A 444 36.570 28.260 -61.378 1.00 55.19 C
ANISOU 2623 CG LEU A 444 6074 9387 5509 378 -687 -939 C
ATOM 2624 CD1 LEU A 444 36.459 27.128 -60.363 1.00 55.25 C
ANISOU 2624 CD1 LEU A 444 6096 9193 5704 449 -783 -1087 C
ATOM 2625 CD2 LEU A 444 37.849 28.126 -62.201 1.00 58.96 C
ANISOU 2625 CD2 LEU A 444 6514 10090 5798 424 -544 -1071 C
ATOM 2626 N SER A 445 34.197 31.037 -61.222 1.00 65.13 N
ANISOU 2626 N SER A 445 7389 10476 6882 222 -689 -295 N
ATOM 2627 CA SER A 445 34.388 32.227 -60.398 1.00 59.93 C
ANISOU 2627 CA SER A 445 6736 9678 6356 144 -510 -108 C
ATOM 2628 C SER A 445 33.225 32.412 -59.435 1.00 54.34 C
ANISOU 2628 C SER A 445 6018 8731 5896 130 -574 8 C
ATOM 2629 O SER A 445 33.427 32.788 -58.274 1.00 57.41 O
ANISOU 2629 O SER A 445 6412 8934 6466 53 -465 41 O
ATOM 2630 CB SER A 445 34.542 33.470 -61.271 1.00 60.56 C
ANISOU 2630 CB SER A 445 6902 9859 6248 126 -349 102 C
ATOM 2631 OG SER A 445 33.289 33.906 -61.763 1.00 68.91 O
ANISOU 2631 OG SER A 445 8004 10902 7276 207 -456 306 O
ATOM 2632 N ALA A 446 32.002 32.140 -59.901 1.00 48.49 N
ANISOU 2632 N ALA A 446 5255 8008 5160 194 -747 56 N
ATOM 2633 CA ALA A 446 30.833 32.276 -59.036 1.00 61.15 C
ANISOU 2633 CA ALA A 446 6816 9402 7017 182 -792 150 C
ATOM 2634 C ALA A 446 30.888 31.299 -57.859 1.00 62.11 C
ANISOU 2634 C ALA A 446 6934 9327 7339 123 -822 -41 C
ATOM 2635 O ALA A 446 30.671 31.692 -56.701 1.00 57.53 O
ANISOU 2635 O ALA A 446 6379 8515 6967 61 -719 30 O
ATOM 2636 CB ALA A 446 29.555 32.075 -59.852 1.00 45.58 C
ANISOU 2636 CB ALA A 446 4764 7555 5000 258 -994 201 C
ATOM 2637 N ILE A 447 31.200 30.024 -58.129 1.00 58.10 N
ANISOU 2637 N ILE A 447 6432 8887 6757 144 -941 -282 N
ATOM 2638 CA ILE A 447 31.223 29.054 -57.029 1.00 50.40 C
ANISOU 2638 CA ILE A 447 5505 7696 5951 115 -959 -444 C
ATOM 2639 C ILE A 447 32.400 29.320 -56.083 1.00 52.42 C
ANISOU 2639 C ILE A 447 5803 7870 6243 101 -826 -448 C
ATOM 2640 O ILE A 447 32.265 29.189 -54.854 1.00 62.08 O
ANISOU 2640 O ILE A 447 7086 8866 7637 56 -789 -452 O
ATOM 2641 CB ILE A 447 31.196 27.601 -57.556 1.00 54.04 C
ANISOU 2641 CB ILE A 447 6002 8206 6322 151 -1091 -698 C
ATOM 2642 CG1 ILE A 447 32.417 27.253 -58.408 1.00 62.62 C
ANISOU 2642 CG1 ILE A 447 7108 9505 7180 233 -1071 -818 C
ATOM 2643 CG2 ILE A 447 29.903 27.333 -58.335 1.00 48.63 C
ANISOU 2643 CG2 ILE A 447 5253 7608 5616 110 -1239 -720 C
ATOM 2644 CD1 ILE A 447 32.381 25.844 -58.969 1.00 62.64 C
ANISOU 2644 CD1 ILE A 447 7185 9528 7087 271 -1163 -1073 C
ATOM 2645 N LEU A 448 33.553 29.737 -56.623 1.00 54.34 N
ANISOU 2645 N LEU A 448 6012 8312 6321 124 -748 -451 N
ATOM 2646 CA LEU A 448 34.692 30.078 -55.773 1.00 60.12 C
ANISOU 2646 CA LEU A 448 6731 9032 7079 87 -634 -468 C
ATOM 2647 C LEU A 448 34.393 31.273 -54.876 1.00 61.98 C
ANISOU 2647 C LEU A 448 7000 9103 7447 -45 -496 -283 C
ATOM 2648 O LEU A 448 34.751 31.266 -53.690 1.00 53.48 O
ANISOU 2648 O LEU A 448 5957 7893 6468 -103 -461 -312 O
ATOM 2649 CB LEU A 448 35.930 30.354 -56.622 1.00 67.35 C
ANISOU 2649 CB LEU A 448 7568 10222 7801 107 -549 -522 C
ATOM 2650 CG LEU A 448 36.638 29.128 -57.198 1.00 77.60 C
ANISOU 2650 CG LEU A 448 8833 11667 8985 247 -631 -744 C
ATOM 2651 CD1 LEU A 448 37.960 29.514 -57.858 1.00 73.23 C
ANISOU 2651 CD1 LEU A 448 8170 11381 8274 248 -498 -803 C
ATOM 2652 CD2 LEU A 448 36.853 28.092 -56.106 1.00 78.83 C
ANISOU 2652 CD2 LEU A 448 9022 11666 9264 337 -718 -874 C
ATOM 2653 N LEU A 449 33.759 32.316 -55.425 1.00 67.53 N
ANISOU 2653 N LEU A 449 7715 9807 8137 -84 -410 -90 N
ATOM 2654 CA LEU A 449 33.433 33.483 -54.614 1.00 67.82 C
ANISOU 2654 CA LEU A 449 7816 9649 8303 -200 -236 89 C
ATOM 2655 C LEU A 449 32.420 33.143 -53.534 1.00 62.73 C
ANISOU 2655 C LEU A 449 7222 8730 7881 -220 -275 100 C
ATOM 2656 O LEU A 449 32.549 33.622 -52.402 1.00 61.64 O
ANISOU 2656 O LEU A 449 7161 8407 7851 -334 -150 134 O
ATOM 2657 CB LEU A 449 32.931 34.637 -55.480 1.00 68.83 C
ANISOU 2657 CB LEU A 449 7977 9811 8366 -185 -119 314 C
ATOM 2658 CG LEU A 449 34.072 35.490 -56.026 1.00 83.34 C
ANISOU 2658 CG LEU A 449 9842 11800 10023 -265 69 348 C
ATOM 2659 CD1 LEU A 449 33.537 36.660 -56.811 1.00 88.41 C
ANISOU 2659 CD1 LEU A 449 10583 12419 10590 -232 213 602 C
ATOM 2660 CD2 LEU A 449 34.952 35.981 -54.883 1.00 86.76 C
ANISOU 2660 CD2 LEU A 449 10299 12141 10526 -451 238 291 C
ATOM 2661 N ALA A 450 31.403 32.337 -53.868 1.00 61.10 N
ANISOU 2661 N ALA A 450 6979 8499 7737 -137 -432 57 N
ATOM 2662 CA ALA A 450 30.439 31.895 -52.860 1.00 59.24 C
ANISOU 2662 CA ALA A 450 6788 8002 7718 -176 -446 36 C
ATOM 2663 C ALA A 450 31.144 31.190 -51.702 1.00 60.53 C
ANISOU 2663 C ALA A 450 7057 8029 7911 -223 -446 -110 C
ATOM 2664 O ALA A 450 30.915 31.518 -50.525 1.00 59.60 O
ANISOU 2664 O ALA A 450 7042 7677 7926 -319 -335 -63 O
ATOM 2665 CB ALA A 450 29.395 30.981 -53.502 1.00 50.76 C
ANISOU 2665 CB ALA A 450 5635 6972 6678 -114 -619 -48 C
ATOM 2666 N PHE A 451 32.032 30.242 -52.032 1.00 56.88 N
ANISOU 2666 N PHE A 451 6586 7716 7311 -139 -563 -280 N
ATOM 2667 CA PHE A 451 32.798 29.513 -51.020 1.00 51.77 C
ANISOU 2667 CA PHE A 451 6036 6978 6658 -120 -593 -403 C
ATOM 2668 C PHE A 451 33.630 30.450 -50.149 1.00 52.29 C
ANISOU 2668 C PHE A 451 6120 7040 6707 -226 -475 -335 C
ATOM 2669 O PHE A 451 33.562 30.393 -48.911 1.00 51.97 O
ANISOU 2669 O PHE A 451 6209 6796 6741 -294 -441 -334 O
ATOM 2670 CB PHE A 451 33.699 28.492 -51.714 1.00 52.36 C
ANISOU 2670 CB PHE A 451 6067 7251 6578 33 -713 -574 C
ATOM 2671 CG PHE A 451 34.706 27.843 -50.810 1.00 49.43 C
ANISOU 2671 CG PHE A 451 5760 6856 6167 116 -756 -676 C
ATOM 2672 CD1 PHE A 451 34.303 26.966 -49.810 1.00 52.83 C
ANISOU 2672 CD1 PHE A 451 6377 7017 6678 152 -796 -729 C
ATOM 2673 CD2 PHE A 451 36.061 28.083 -50.980 1.00 50.25 C
ANISOU 2673 CD2 PHE A 451 5733 7217 6142 170 -756 -722 C
ATOM 2674 CE1 PHE A 451 35.237 26.349 -48.982 1.00 50.88 C
ANISOU 2674 CE1 PHE A 451 6209 6757 6365 275 -858 -798 C
ATOM 2675 CE2 PHE A 451 36.998 27.473 -50.155 1.00 52.56 C
ANISOU 2675 CE2 PHE A 451 6047 7534 6392 286 -829 -810 C
ATOM 2676 CZ PHE A 451 36.582 26.606 -49.155 1.00 53.10 C
ANISOU 2676 CZ PHE A 451 6323 7330 6521 356 -892 -835 C
ATOM 2677 N ILE A 452 34.416 31.324 -50.787 1.00 50.04 N
ANISOU 2677 N ILE A 452 5724 6981 6308 -267 -397 -288 N
ATOM 2678 CA ILE A 452 35.360 32.171 -50.064 1.00 49.06 C
ANISOU 2678 CA ILE A 452 5593 6907 6141 -406 -281 -272 C
ATOM 2679 C ILE A 452 34.622 33.162 -49.172 1.00 54.38 C
ANISOU 2679 C ILE A 452 6401 7314 6946 -580 -109 -129 C
ATOM 2680 O ILE A 452 34.982 33.345 -48.003 1.00 55.24 O
ANISOU 2680 O ILE A 452 6600 7323 7067 -698 -66 -158 O
ATOM 2681 CB ILE A 452 36.298 32.878 -51.062 1.00 57.28 C
ANISOU 2681 CB ILE A 452 6493 8236 7034 -443 -193 -271 C
ATOM 2682 CG1 ILE A 452 37.272 31.870 -51.672 1.00 57.21 C
ANISOU 2682 CG1 ILE A 452 6348 8491 6900 -280 -333 -447 C
ATOM 2683 CG2 ILE A 452 37.063 34.014 -50.396 1.00 55.18 C
ANISOU 2683 CG2 ILE A 452 6225 8000 6740 -664 -14 -245 C
ATOM 2684 CD1 ILE A 452 37.918 32.336 -52.951 1.00 55.34 C
ANISOU 2684 CD1 ILE A 452 5988 8520 6518 -286 -242 -455 C
ATOM 2685 N ILE A 453 33.545 33.769 -49.685 1.00 57.71 N
ANISOU 2685 N ILE A 453 6846 7619 7464 -584 -13 24 N
ATOM 2686 CA ILE A 453 32.796 34.757 -48.915 1.00 57.94 C
ANISOU 2686 CA ILE A 453 7002 7377 7636 -719 190 169 C
ATOM 2687 C ILE A 453 32.102 34.107 -47.724 1.00 59.64 C
ANISOU 2687 C ILE A 453 7344 7321 7994 -743 161 123 C
ATOM 2688 O ILE A 453 32.122 34.649 -46.612 1.00 60.20 O
ANISOU 2688 O ILE A 453 7560 7199 8114 -899 307 147 O
ATOM 2689 CB ILE A 453 31.802 35.494 -49.833 1.00 58.26 C
ANISOU 2689 CB ILE A 453 7009 7382 7745 -650 282 358 C
ATOM 2690 CG1 ILE A 453 32.557 36.415 -50.794 1.00 64.22 C
ANISOU 2690 CG1 ILE A 453 7730 8333 8337 -672 396 437 C
ATOM 2691 CG2 ILE A 453 30.793 36.302 -49.028 1.00 58.58 C
ANISOU 2691 CG2 ILE A 453 7171 7105 7984 -726 489 505 C
ATOM 2692 CD1 ILE A 453 31.657 37.220 -51.710 1.00 72.77 C
ANISOU 2692 CD1 ILE A 453 8818 9385 9446 -568 488 658 C
ATOM 2693 N THR A 454 31.503 32.925 -47.918 1.00 57.54 N
ANISOU 2693 N THR A 454 7054 7027 7780 -614 -7 40 N
ATOM 2694 CA THR A 454 30.782 32.312 -46.807 1.00 53.43 C
ANISOU 2694 CA THR A 454 6687 6219 7394 -656 7 -3 C
ATOM 2695 C THR A 454 31.722 31.726 -45.755 1.00 59.64 C
ANISOU 2695 C THR A 454 7616 6976 8071 -684 -60 -120 C
ATOM 2696 O THR A 454 31.374 31.709 -44.568 1.00 62.94 O
ANISOU 2696 O THR A 454 8225 7135 8553 -785 28 -115 O
ATOM 2697 CB THR A 454 29.818 31.242 -47.318 1.00 50.16 C
ANISOU 2697 CB THR A 454 6222 5765 7071 -551 -117 -74 C
ATOM 2698 OG1 THR A 454 30.518 30.336 -48.173 1.00 65.32 O
ANISOU 2698 OG1 THR A 454 8062 7921 8836 -417 -307 -202 O
ATOM 2699 CG2 THR A 454 28.668 31.879 -48.080 1.00 42.53 C
ANISOU 2699 CG2 THR A 454 5113 4807 6240 -533 -56 56 C
ATOM 2700 N TRP A 455 32.909 31.250 -46.146 1.00 53.22 N
ANISOU 2700 N TRP A 455 6713 6426 7083 -585 -212 -221 N
ATOM 2701 CA TRP A 455 33.788 30.597 -45.180 1.00 47.33 C
ANISOU 2701 CA TRP A 455 6075 5686 6223 -551 -317 -321 C
ATOM 2702 C TRP A 455 34.871 31.502 -44.602 1.00 49.35 C
ANISOU 2702 C TRP A 455 6299 6096 6358 -693 -268 -320 C
ATOM 2703 O TRP A 455 35.527 31.098 -43.635 1.00 55.35 O
ANISOU 2703 O TRP A 455 7152 6865 7012 -683 -363 -386 O
ATOM 2704 CB TRP A 455 34.467 29.365 -45.796 1.00 45.96 C
ANISOU 2704 CB TRP A 455 5823 5698 5939 -317 -519 -452 C
ATOM 2705 CG TRP A 455 33.576 28.180 -46.050 1.00 40.87 C
ANISOU 2705 CG TRP A 455 5286 4867 5376 -199 -578 -512 C
ATOM 2706 CD1 TRP A 455 32.273 28.189 -46.462 1.00 43.43 C
ANISOU 2706 CD1 TRP A 455 5616 5032 5854 -263 -506 -475 C
ATOM 2707 CD2 TRP A 455 33.934 26.802 -45.883 1.00 42.48 C
ANISOU 2707 CD2 TRP A 455 5610 5022 5508 -5 -708 -631 C
ATOM 2708 NE1 TRP A 455 31.805 26.898 -46.576 1.00 46.93 N
ANISOU 2708 NE1 TRP A 455 6170 5340 6323 -166 -577 -589 N
ATOM 2709 CE2 TRP A 455 32.806 26.030 -46.225 1.00 45.56 C
ANISOU 2709 CE2 TRP A 455 6098 5203 6010 -2 -685 -680 C
ATOM 2710 CE3 TRP A 455 35.106 26.148 -45.488 1.00 40.32 C
ANISOU 2710 CE3 TRP A 455 5367 4867 5085 179 -836 -702 C
ATOM 2711 CZ2 TRP A 455 32.814 24.635 -46.179 1.00 42.13 C
ANISOU 2711 CZ2 TRP A 455 5839 4631 5539 153 -750 -802 C
ATOM 2712 CZ3 TRP A 455 35.115 24.769 -45.447 1.00 43.91 C
ANISOU 2712 CZ3 TRP A 455 5991 5186 5505 386 -914 -796 C
ATOM 2713 CH2 TRP A 455 33.977 24.026 -45.792 1.00 43.26 C
ANISOU 2713 CH2 TRP A 455 6053 4852 5533 359 -854 -848 C
ATOM 2714 N THR A 456 35.094 32.687 -45.169 1.00 46.97 N
ANISOU 2714 N THR A 456 5875 5921 6048 -827 -123 -252 N
ATOM 2715 CA THR A 456 36.150 33.563 -44.664 1.00 51.43 C
ANISOU 2715 CA THR A 456 6401 6646 6494 -1016 -51 -286 C
ATOM 2716 C THR A 456 35.957 34.037 -43.213 1.00 52.30 C
ANISOU 2716 C THR A 456 6738 6523 6609 -1223 54 -268 C
ATOM 2717 O THR A 456 36.960 34.039 -42.474 1.00 51.70 O
ANISOU 2717 O THR A 456 6649 6613 6382 -1304 -34 -366 O
ATOM 2718 CB THR A 456 36.315 34.739 -45.647 1.00 59.40 C
ANISOU 2718 CB THR A 456 7289 7782 7498 -1133 137 -212 C
ATOM 2719 OG1 THR A 456 36.891 34.254 -46.868 1.00 65.34 O
ANISOU 2719 OG1 THR A 456 7832 8825 8170 -965 20 -271 O
ATOM 2720 CG2 THR A 456 37.212 35.838 -45.090 1.00 54.78 C
ANISOU 2720 CG2 THR A 456 6702 7296 6815 -1412 293 -250 C
ATOM 2721 N PRO A 457 34.754 34.436 -42.735 1.00 52.58 N
ANISOU 2721 N PRO A 457 6974 6202 6801 -1316 238 -161 N
ATOM 2722 CA PRO A 457 34.659 34.881 -41.324 1.00 55.96 C
ANISOU 2722 CA PRO A 457 7648 6409 7205 -1531 360 -165 C
ATOM 2723 C PRO A 457 35.056 33.828 -40.298 1.00 50.74 C
ANISOU 2723 C PRO A 457 7124 5739 6415 -1455 150 -260 C
ATOM 2724 O PRO A 457 35.753 34.166 -39.334 1.00 51.93 O
ANISOU 2724 O PRO A 457 7371 5949 6410 -1620 137 -319 O
ATOM 2725 CB PRO A 457 33.190 35.298 -41.184 1.00 62.73 C
ANISOU 2725 CB PRO A 457 8662 6887 8287 -1576 598 -35 C
ATOM 2726 CG PRO A 457 32.803 35.703 -42.542 1.00 61.19 C
ANISOU 2726 CG PRO A 457 8269 6786 8193 -1469 652 61 C
ATOM 2727 CD PRO A 457 33.491 34.739 -43.445 1.00 51.40 C
ANISOU 2727 CD PRO A 457 6821 5862 6847 -1262 379 -29 C
ATOM 2728 N TYR A 458 34.611 32.578 -40.458 1.00 49.78 N
ANISOU 2728 N TYR A 458 7040 5534 6341 -1217 -4 -275 N
ATOM 2729 CA TYR A 458 34.985 31.523 -39.516 1.00 51.11 C
ANISOU 2729 CA TYR A 458 7389 5661 6371 -1101 -190 -341 C
ATOM 2730 C TYR A 458 36.498 31.329 -39.443 1.00 57.52 C
ANISOU 2730 C TYR A 458 8031 6868 6957 -1017 -422 -437 C
ATOM 2731 O TYR A 458 37.066 31.213 -38.348 1.00 60.76 O
ANISOU 2731 O TYR A 458 8581 7312 7192 -1060 -525 -473 O
ATOM 2732 CB TYR A 458 34.289 30.215 -39.902 1.00 47.81 C
ANISOU 2732 CB TYR A 458 7038 5081 6045 -861 -279 -352 C
ATOM 2733 CG TYR A 458 34.500 29.090 -38.909 1.00 54.86 C
ANISOU 2733 CG TYR A 458 8202 5838 6805 -722 -419 -392 C
ATOM 2734 CD1 TYR A 458 33.621 28.894 -37.849 1.00 51.70 C
ANISOU 2734 CD1 TYR A 458 8150 5048 6444 -829 -280 -355 C
ATOM 2735 CD2 TYR A 458 35.551 28.188 -39.065 1.00 55.65 C
ANISOU 2735 CD2 TYR A 458 8226 6181 6738 -458 -672 -458 C
ATOM 2736 CE1 TYR A 458 33.813 27.858 -36.947 1.00 56.19 C
ANISOU 2736 CE1 TYR A 458 9021 5466 6862 -691 -392 -374 C
ATOM 2737 CE2 TYR A 458 35.747 27.155 -38.171 1.00 56.13 C
ANISOU 2737 CE2 TYR A 458 8568 6099 6660 -285 -796 -467 C
ATOM 2738 CZ TYR A 458 34.875 26.992 -37.118 1.00 56.15 C
ANISOU 2738 CZ TYR A 458 8952 5704 6680 -406 -658 -420 C
ATOM 2739 OH TYR A 458 35.076 25.957 -36.233 1.00 63.24 O
ANISOU 2739 OH TYR A 458 10180 6437 7410 -223 -767 -411 O
ATOM 2740 N ASN A 459 37.174 31.311 -40.591 1.00 51.00 N
ANISOU 2740 N ASN A 459 6892 6364 6121 -900 -506 -482 N
ATOM 2741 CA ASN A 459 38.610 31.061 -40.572 1.00 55.00 C
ANISOU 2741 CA ASN A 459 7182 7274 6440 -796 -720 -587 C
ATOM 2742 C ASN A 459 39.403 32.285 -40.118 1.00 56.68 C
ANISOU 2742 C ASN A 459 7286 7707 6543 -1104 -644 -636 C
ATOM 2743 O ASN A 459 40.475 32.133 -39.516 1.00 59.80 O
ANISOU 2743 O ASN A 459 7576 8389 6754 -1089 -831 -729 O
ATOM 2744 CB ASN A 459 39.061 30.565 -41.943 1.00 56.72 C
ANISOU 2744 CB ASN A 459 7117 7748 6688 -570 -803 -637 C
ATOM 2745 CG ASN A 459 38.517 29.180 -42.258 1.00 50.59 C
ANISOU 2745 CG ASN A 459 6464 6793 5966 -264 -911 -636 C
ATOM 2746 OD1 ASN A 459 39.139 28.166 -41.934 1.00 57.23 O
ANISOU 2746 OD1 ASN A 459 7330 7716 6701 -8 -1104 -691 O
ATOM 2747 ND2 ASN A 459 37.343 29.130 -42.875 1.00 44.09 N
ANISOU 2747 ND2 ASN A 459 5724 5721 5306 -289 -780 -578 N
ATOM 2748 N ILE A 460 38.889 33.496 -40.365 1.00 57.87 N
ANISOU 2748 N ILE A 460 7468 7726 6795 -1385 -367 -579 N
ATOM 2749 CA ILE A 460 39.481 34.687 -39.755 1.00 61.06 C
ANISOU 2749 CA ILE A 460 7866 8240 7095 -1739 -235 -635 C
ATOM 2750 C ILE A 460 39.339 34.629 -38.238 1.00 58.98 C
ANISOU 2750 C ILE A 460 7897 7799 6714 -1869 -273 -648 C
ATOM 2751 O ILE A 460 40.264 34.995 -37.502 1.00 57.45 O
ANISOU 2751 O ILE A 460 7654 7848 6325 -2053 -360 -758 O
ATOM 2752 CB ILE A 460 38.869 35.972 -40.351 1.00 67.55 C
ANISOU 2752 CB ILE A 460 8728 8884 8056 -1980 114 -549 C
ATOM 2753 CG1 ILE A 460 39.397 36.205 -41.769 1.00 74.29 C
ANISOU 2753 CG1 ILE A 460 9283 10013 8932 -1912 143 -564 C
ATOM 2754 CG2 ILE A 460 39.170 37.202 -39.488 1.00 66.48 C
ANISOU 2754 CG2 ILE A 460 8725 8704 7831 -2388 328 -599 C
ATOM 2755 CD1 ILE A 460 38.965 37.529 -42.369 1.00 77.97 C
ANISOU 2755 CD1 ILE A 460 9808 10329 9488 -2135 490 -468 C
ATOM 2756 N MET A 461 38.179 34.171 -37.746 1.00 58.39 N
ANISOU 2756 N MET A 461 8131 7312 6742 -1794 -205 -548 N
ATOM 2757 CA MET A 461 38.004 33.967 -36.309 1.00 64.08 C
ANISOU 2757 CA MET A 461 9181 7838 7330 -1889 -238 -554 C
ATOM 2758 C MET A 461 39.013 32.963 -35.770 1.00 63.33 C
ANISOU 2758 C MET A 461 9034 8029 6998 -1666 -603 -629 C
ATOM 2759 O MET A 461 39.546 33.144 -34.672 1.00 62.09 O
ANISOU 2759 O MET A 461 9007 7966 6619 -1812 -700 -686 O
ATOM 2760 CB MET A 461 36.584 33.491 -35.998 1.00 63.65 C
ANISOU 2760 CB MET A 461 9441 7297 7445 -1816 -89 -445 C
ATOM 2761 CG MET A 461 35.504 34.529 -36.175 1.00 57.84 C
ANISOU 2761 CG MET A 461 8806 6242 6929 -2034 280 -359 C
ATOM 2762 SD MET A 461 33.856 33.793 -36.144 1.00 62.28 S
ANISOU 2762 SD MET A 461 9587 6334 7744 -1889 421 -256 S
ATOM 2763 CE MET A 461 32.934 35.157 -36.864 1.00 63.05 C
ANISOU 2763 CE MET A 461 9593 6256 8107 -2051 790 -149 C
ATOM 2764 N VAL A 462 39.272 31.893 -36.528 1.00 55.81 N
ANISOU 2764 N VAL A 462 7908 7219 6080 -1301 -805 -629 N
ATOM 2765 CA VAL A 462 40.293 30.920 -36.136 1.00 65.15 C
ANISOU 2765 CA VAL A 462 9009 8692 7051 -1018 -1148 -685 C
ATOM 2766 C VAL A 462 41.667 31.582 -36.032 1.00 72.89 C
ANISOU 2766 C VAL A 462 9653 10188 7855 -1163 -1288 -814 C
ATOM 2767 O VAL A 462 42.408 31.361 -35.065 1.00 81.81 O
ANISOU 2767 O VAL A 462 10812 11528 8743 -1136 -1520 -864 O
ATOM 2768 CB VAL A 462 40.300 29.737 -37.123 1.00 67.50 C
ANISOU 2768 CB VAL A 462 9177 9022 7448 -608 -1274 -670 C
ATOM 2769 CG1 VAL A 462 41.506 28.837 -36.885 1.00 68.47 C
ANISOU 2769 CG1 VAL A 462 9146 9497 7371 -274 -1609 -727 C
ATOM 2770 CG2 VAL A 462 39.002 28.942 -36.989 1.00 62.95 C
ANISOU 2770 CG2 VAL A 462 8965 7949 7003 -492 -1164 -575 C
ATOM 2771 N LEU A 463 42.020 32.411 -37.021 1.00 73.35 N
ANISOU 2771 N LEU A 463 9391 10464 8017 -1329 -1146 -875 N
ATOM 2772 CA LEU A 463 43.292 33.140 -37.000 1.00 76.91 C
ANISOU 2772 CA LEU A 463 9496 11402 8323 -1537 -1219 -1028 C
ATOM 2773 C LEU A 463 43.396 34.065 -35.784 1.00 76.45 C
ANISOU 2773 C LEU A 463 9627 11322 8097 -1950 -1149 -1087 C
ATOM 2774 O LEU A 463 44.428 34.108 -35.095 1.00 78.96 O
ANISOU 2774 O LEU A 463 9786 12030 8186 -2023 -1377 -1211 O
ATOM 2775 CB LEU A 463 43.446 33.927 -38.305 1.00 80.21 C
ANISOU 2775 CB LEU A 463 9631 11948 8895 -1683 -990 -1065 C
ATOM 2776 CG LEU A 463 44.704 34.760 -38.554 1.00 85.17 C
ANISOU 2776 CG LEU A 463 9875 13062 9424 -1946 -976 -1242 C
ATOM 2777 CD1 LEU A 463 45.179 34.539 -39.976 1.00 85.97 C
ANISOU 2777 CD1 LEU A 463 9625 13407 9633 -1760 -951 -1278 C
ATOM 2778 CD2 LEU A 463 44.439 36.240 -38.314 1.00 84.60 C
ANISOU 2778 CD2 LEU A 463 9948 12837 9362 -2460 -635 -1268 C
ATOM 2779 N VAL A 464 42.330 34.823 -35.517 1.00 73.09 N
ANISOU 2779 N VAL A 464 9535 10456 7780 -2223 -829 -1006 N
ATOM 2780 CA VAL A 464 42.316 35.757 -34.392 1.00 77.18 C
ANISOU 2780 CA VAL A 464 10292 10885 8147 -2645 -695 -1068 C
ATOM 2781 C VAL A 464 42.422 35.002 -33.072 1.00 77.99 C
ANISOU 2781 C VAL A 464 10654 10973 8006 -2535 -964 -1064 C
ATOM 2782 O VAL A 464 43.172 35.398 -32.171 1.00 82.45 O
ANISOU 2782 O VAL A 464 11215 11801 8311 -2775 -1092 -1188 O
ATOM 2783 CB VAL A 464 41.053 36.638 -34.454 1.00 73.15 C
ANISOU 2783 CB VAL A 464 10100 9856 7839 -2889 -263 -962 C
ATOM 2784 CG1 VAL A 464 40.900 37.462 -33.185 1.00 76.16 C
ANISOU 2784 CG1 VAL A 464 10816 10058 8063 -3297 -96 -1021 C
ATOM 2785 CG2 VAL A 464 41.113 37.552 -35.676 1.00 68.92 C
ANISOU 2785 CG2 VAL A 464 9330 9379 7479 -3028 0 -965 C
ATOM 2786 N SER A 465 41.685 33.894 -32.945 1.00 75.32 N
ANISOU 2786 N SER A 465 10556 10333 7728 -2180 -1052 -927 N
ATOM 2787 CA SER A 465 41.752 33.063 -31.748 1.00 73.27 C
ANISOU 2787 CA SER A 465 10597 10019 7224 -2021 -1297 -893 C
ATOM 2788 C SER A 465 43.128 32.437 -31.574 1.00 82.37 C
ANISOU 2788 C SER A 465 11438 11728 8129 -1772 -1731 -978 C
ATOM 2789 O SER A 465 43.535 32.133 -30.447 1.00 86.73 O
ANISOU 2789 O SER A 465 12174 12395 8386 -1746 -1968 -989 O
ATOM 2790 CB SER A 465 40.681 31.977 -31.815 1.00 67.00 C
ANISOU 2790 CB SER A 465 10115 8770 6573 -1693 -1254 -739 C
ATOM 2791 OG SER A 465 41.032 30.878 -30.998 1.00 80.41 O
ANISOU 2791 OG SER A 465 12015 10507 8029 -1388 -1558 -696 O
ATOM 2792 N THR A 466 43.849 32.222 -32.676 1.00 91.62 N
ANISOU 2792 N THR A 466 12143 13259 9410 -1569 -1839 -1034 N
ATOM 2793 CA THR A 466 45.243 31.807 -32.573 1.00102.06 C
ANISOU 2793 CA THR A 466 13076 15175 10527 -1363 -2219 -1139 C
ATOM 2794 C THR A 466 46.100 32.932 -32.006 1.00111.46 C
ANISOU 2794 C THR A 466 14060 16771 11520 -1821 -2250 -1324 C
ATOM 2795 O THR A 466 46.966 32.695 -31.153 1.00111.60 O
ANISOU 2795 O THR A 466 13982 17174 11247 -1769 -2586 -1396 O
ATOM 2796 CB THR A 466 45.763 31.368 -33.942 1.00 96.52 C
ANISOU 2796 CB THR A 466 11925 14734 10015 -1066 -2262 -1171 C
ATOM 2797 OG1 THR A 466 44.959 30.287 -34.423 1.00 93.99 O
ANISOU 2797 OG1 THR A 466 11828 14032 9852 -670 -2234 -1023 O
ATOM 2798 CG2 THR A 466 47.210 30.905 -33.851 1.00 96.98 C
ANISOU 2798 CG2 THR A 466 11538 15422 9889 -814 -2642 -1284 C
ATOM 2799 N PHE A 467 45.855 34.170 -32.441 1.00129.32 N
ANISOU 2799 N PHE A 467 14028 19484 15626 -1402 -2599 -1111 N
ATOM 2800 CA PHE A 467 46.626 35.311 -31.955 1.00136.16 C
ANISOU 2800 CA PHE A 467 14692 20541 16500 -1948 -2788 -1323 C
ATOM 2801 C PHE A 467 45.934 36.051 -30.813 1.00140.07 C
ANISOU 2801 C PHE A 467 15682 20708 16831 -2216 -2858 -1566 C
ATOM 2802 O PHE A 467 46.071 37.274 -30.694 1.00147.67 O
ANISOU 2802 O PHE A 467 16689 21519 17898 -2734 -2855 -1766 O
ATOM 2803 CB PHE A 467 46.945 36.273 -33.100 1.00137.59 C
ANISOU 2803 CB PHE A 467 14626 20645 17007 -2351 -2566 -1297 C
ATOM 2804 CG PHE A 467 47.952 35.739 -34.082 1.00140.24 C
ANISOU 2804 CG PHE A 467 14361 21461 17461 -2202 -2542 -1119 C
ATOM 2805 CD1 PHE A 467 48.729 34.630 -33.772 1.00142.91 C
ANISOU 2805 CD1 PHE A 467 14345 22324 17631 -1787 -2780 -1046 C
ATOM 2806 CD2 PHE A 467 48.130 36.353 -35.309 1.00141.12 C
ANISOU 2806 CD2 PHE A 467 14272 21510 17839 -2455 -2270 -1016 C
ATOM 2807 CE1 PHE A 467 49.657 34.140 -34.670 1.00145.34 C
ANISOU 2807 CE1 PHE A 467 14085 23092 18046 -1608 -2735 -905 C
ATOM 2808 CE2 PHE A 467 49.058 35.868 -36.213 1.00143.95 C
ANISOU 2808 CE2 PHE A 467 14069 22346 18281 -2315 -2213 -866 C
ATOM 2809 CZ PHE A 467 49.822 34.760 -35.893 1.00145.77 C
ANISOU 2809 CZ PHE A 467 13926 23107 18354 -1882 -2441 -826 C
ATOM 2810 N CYS A 468 45.212 35.328 -29.961 1.00136.20 N
ANISOU 2810 N CYS A 468 15577 20098 16074 -1880 -2909 -1559 N
ATOM 2811 CA CYS A 468 44.665 35.863 -28.716 1.00134.81 C
ANISOU 2811 CA CYS A 468 15843 19728 15651 -2070 -3005 -1801 C
ATOM 2812 C CYS A 468 44.393 34.688 -27.780 1.00133.75 C
ANISOU 2812 C CYS A 468 15927 19741 15150 -1624 -3157 -1704 C
ATOM 2813 O CYS A 468 44.852 33.566 -28.017 1.00135.23 O
ANISOU 2813 O CYS A 468 15880 20217 15284 -1218 -3254 -1475 O
ATOM 2814 CB CYS A 468 43.406 36.700 -28.972 1.00132.49 C
ANISOU 2814 CB CYS A 468 16011 18799 15529 -2231 -2660 -1898 C
ATOM 2815 SG CYS A 468 41.880 35.746 -29.076 1.00128.86 S
ANISOU 2815 SG CYS A 468 15990 17954 15018 -1733 -2358 -1718 S
ATOM 2816 N ASP A 469 43.636 34.945 -26.711 1.00133.85 N
ANISOU 2816 N ASP A 469 16418 19540 14899 -1687 -3159 -1873 N
ATOM 2817 CA ASP A 469 43.341 33.938 -25.686 1.00136.82 C
ANISOU 2817 CA ASP A 469 17072 20042 14872 -1327 -3291 -1780 C
ATOM 2818 C ASP A 469 41.829 33.913 -25.474 1.00135.91 C
ANISOU 2818 C ASP A 469 17505 19414 14720 -1232 -2945 -1792 C
ATOM 2819 O ASP A 469 41.322 34.569 -24.560 1.00144.29 O
ANISOU 2819 O ASP A 469 18920 20336 15569 -1437 -2930 -2032 O
ATOM 2820 CB ASP A 469 44.097 34.237 -24.388 1.00141.54 C
ANISOU 2820 CB ASP A 469 17657 21051 15072 -1517 -3698 -1989 C
ATOM 2821 N LYS A 470 41.132 33.144 -26.322 1.00129.01 N
ANISOU 2821 N LYS A 470 16680 18293 14044 -924 -2669 -1551 N
ATOM 2822 CA LYS A 470 39.679 32.944 -26.244 1.00122.74 C
ANISOU 2822 CA LYS A 470 16323 17071 13242 -802 -2328 -1523 C
ATOM 2823 C LYS A 470 38.923 34.271 -26.297 1.00118.32 C
ANISOU 2823 C LYS A 470 15965 16149 12843 -1129 -2104 -1782 C
ATOM 2824 O LYS A 470 37.942 34.478 -25.579 1.00117.78 O
ANISOU 2824 O LYS A 470 16286 15858 12605 -1137 -1937 -1907 O
ATOM 2825 CB LYS A 470 39.290 32.144 -24.997 1.00121.90 C
ANISOU 2825 CB LYS A 470 16581 17044 12692 -595 -2400 -1466 C
ATOM 2826 N CYS A 471 39.382 35.178 -27.160 1.00113.85 N
ANISOU 2826 N CYS A 471 15140 15517 12602 -1387 -2085 -1856 N
ATOM 2827 CA CYS A 471 38.771 36.496 -27.263 1.00111.85 C
ANISOU 2827 CA CYS A 471 15092 14879 12528 -1682 -1889 -2086 C
ATOM 2828 C CYS A 471 37.547 36.516 -28.168 1.00104.11 C
ANISOU 2828 C CYS A 471 14245 13494 11821 -1514 -1514 -1970 C
ATOM 2829 O CYS A 471 36.720 37.422 -28.034 1.00103.12 O
ANISOU 2829 O CYS A 471 14390 13015 11777 -1627 -1314 -2147 O
ATOM 2830 CB CYS A 471 39.795 37.514 -27.771 1.00120.55 C
ANISOU 2830 CB CYS A 471 15900 16048 13855 -2074 -2023 -2197 C
ATOM 2831 SG CYS A 471 40.443 37.142 -29.414 1.00124.72 S
ANISOU 2831 SG CYS A 471 15930 16708 14748 -1991 -1959 -1892 S
ATOM 2832 N VAL A 472 37.404 35.547 -29.071 1.00 95.89 N
ANISOU 2832 N VAL A 472 13021 12503 10911 -1234 -1422 -1696 N
ATOM 2833 CA VAL A 472 36.262 35.493 -29.983 1.00 81.93 C
ANISOU 2833 CA VAL A 472 11333 10414 9381 -1076 -1102 -1586 C
ATOM 2834 C VAL A 472 35.064 34.888 -29.258 1.00 77.58 C
ANISOU 2834 C VAL A 472 11110 9735 8633 -874 -932 -1596 C
ATOM 2835 O VAL A 472 35.111 33.713 -28.866 1.00 79.16 O
ANISOU 2835 O VAL A 472 11343 10109 8627 -669 -998 -1457 O
ATOM 2836 CB VAL A 472 36.597 34.696 -31.254 1.00 69.43 C
ANISOU 2836 CB VAL A 472 9435 8954 7992 -886 -1076 -1326 C
ATOM 2837 CG1 VAL A 472 35.373 34.592 -32.153 1.00 61.57 C
ANISOU 2837 CG1 VAL A 472 8524 7673 7197 -729 -780 -1229 C
ATOM 2838 CG2 VAL A 472 37.759 35.340 -31.995 1.00 73.08 C
ANISOU 2838 CG2 VAL A 472 9552 9575 8642 -1107 -1197 -1308 C
ATOM 2839 N PRO A 473 33.989 35.648 -29.050 1.00 74.83 N
ANISOU 2839 N PRO A 473 11008 9085 8338 -920 -700 -1750 N
ATOM 2840 CA PRO A 473 32.818 35.113 -28.344 1.00 71.34 C
ANISOU 2840 CA PRO A 473 10838 8563 7706 -755 -501 -1770 C
ATOM 2841 C PRO A 473 32.114 34.012 -29.125 1.00 64.62 C
ANISOU 2841 C PRO A 473 9894 7691 6967 -517 -337 -1530 C
ATOM 2842 O PRO A 473 32.218 33.906 -30.349 1.00 67.52 O
ANISOU 2842 O PRO A 473 10027 8025 7603 -461 -310 -1390 O
ATOM 2843 CB PRO A 473 31.911 36.337 -28.173 1.00 76.36 C
ANISOU 2843 CB PRO A 473 11676 8889 8447 -839 -279 -2002 C
ATOM 2844 CG PRO A 473 32.369 37.308 -29.197 1.00 77.06 C
ANISOU 2844 CG PRO A 473 11594 8812 8872 -978 -306 -2003 C
ATOM 2845 CD PRO A 473 33.834 37.078 -29.368 1.00 77.24 C
ANISOU 2845 CD PRO A 473 11370 9108 8869 -1126 -607 -1924 C
ATOM 2846 N VAL A 474 31.389 33.177 -28.371 1.00 58.82 N
ANISOU 2846 N VAL A 474 9367 6984 5998 -402 -223 -1490 N
ATOM 2847 CA VAL A 474 30.704 32.010 -28.925 1.00 59.27 C
ANISOU 2847 CA VAL A 474 9386 7014 6118 -227 -73 -1284 C
ATOM 2848 C VAL A 474 29.590 32.414 -29.889 1.00 55.92 C
ANISOU 2848 C VAL A 474 8859 6395 5995 -192 183 -1299 C
ATOM 2849 O VAL A 474 29.253 31.656 -30.811 1.00 62.71 O
ANISOU 2849 O VAL A 474 9578 7240 7007 -88 251 -1145 O
ATOM 2850 CB VAL A 474 30.165 31.143 -27.767 1.00 67.78 C
ANISOU 2850 CB VAL A 474 10752 8147 6856 -177 15 -1242 C
ATOM 2851 CG1 VAL A 474 29.743 29.764 -28.251 1.00 69.26 C
ANISOU 2851 CG1 VAL A 474 10933 8302 7083 -40 110 -1010 C
ATOM 2852 CG2 VAL A 474 31.205 31.020 -26.664 1.00 70.43 C
ANISOU 2852 CG2 VAL A 474 11225 8694 6842 -209 -258 -1260 C
ATOM 2853 N THR A 475 29.013 33.607 -29.706 1.00 56.43 N
ANISOU 2853 N THR A 475 8994 6308 6138 -259 317 -1492 N
ATOM 2854 CA THR A 475 28.028 34.127 -30.652 1.00 61.32 C
ANISOU 2854 CA THR A 475 9491 6763 7047 -182 522 -1495 C
ATOM 2855 C THR A 475 28.624 34.267 -32.050 1.00 61.89 C
ANISOU 2855 C THR A 475 9304 6824 7389 -167 411 -1351 C
ATOM 2856 O THR A 475 28.003 33.865 -33.046 1.00 64.70 O
ANISOU 2856 O THR A 475 9501 7171 7911 -56 510 -1232 O
ATOM 2857 CB THR A 475 27.495 35.472 -30.151 1.00 65.63 C
ANISOU 2857 CB THR A 475 10189 7120 7626 -217 655 -1733 C
ATOM 2858 OG1 THR A 475 26.931 35.303 -28.844 1.00 65.66 O
ANISOU 2858 OG1 THR A 475 10433 7176 7339 -221 786 -1879 O
ATOM 2859 CG2 THR A 475 26.422 36.014 -31.081 1.00 68.28 C
ANISOU 2859 CG2 THR A 475 10396 7300 8248 -73 858 -1717 C
ATOM 2860 N LEU A 476 29.853 34.790 -32.134 1.00 61.73 N
ANISOU 2860 N LEU A 476 9225 6841 7389 -297 203 -1363 N
ATOM 2861 CA LEU A 476 30.526 34.927 -33.422 1.00 59.14 C
ANISOU 2861 CA LEU A 476 8646 6544 7281 -307 117 -1216 C
ATOM 2862 C LEU A 476 30.876 33.571 -34.017 1.00 52.59 C
ANISOU 2862 C LEU A 476 7651 5910 6419 -178 47 -1031 C
ATOM 2863 O LEU A 476 30.769 33.386 -35.233 1.00 57.96 O
ANISOU 2863 O LEU A 476 8151 6603 7269 -97 91 -907 O
ATOM 2864 CB LEU A 476 31.788 35.774 -33.283 1.00 63.16 C
ANISOU 2864 CB LEU A 476 9108 7083 7808 -525 -73 -1281 C
ATOM 2865 CG LEU A 476 31.587 37.245 -32.950 1.00 68.66 C
ANISOU 2865 CG LEU A 476 9983 7509 8596 -687 -10 -1468 C
ATOM 2866 CD1 LEU A 476 32.940 37.897 -32.813 1.00 76.58 C
ANISOU 2866 CD1 LEU A 476 10911 8579 9606 -969 -219 -1530 C
ATOM 2867 CD2 LEU A 476 30.758 37.912 -34.029 1.00 66.35 C
ANISOU 2867 CD2 LEU A 476 9660 6976 8572 -584 178 -1383 C
ATOM 2868 N TRP A 477 31.330 32.628 -33.184 1.00 50.92 N
ANISOU 2868 N TRP A 477 7522 5848 5978 -141 -68 -1011 N
ATOM 2869 CA TRP A 477 31.602 31.273 -33.662 1.00 53.14 C
ANISOU 2869 CA TRP A 477 7712 6251 6226 21 -117 -846 C
ATOM 2870 C TRP A 477 30.361 30.658 -34.297 1.00 51.88 C
ANISOU 2870 C TRP A 477 7572 5976 6164 121 93 -796 C
ATOM 2871 O TRP A 477 30.431 30.077 -35.390 1.00 52.51 O
ANISOU 2871 O TRP A 477 7496 6092 6362 217 98 -697 O
ATOM 2872 CB TRP A 477 32.106 30.395 -32.517 1.00 54.04 C
ANISOU 2872 CB TRP A 477 7989 6486 6058 77 -254 -816 C
ATOM 2873 CG TRP A 477 33.521 30.662 -32.079 1.00 56.26 C
ANISOU 2873 CG TRP A 477 8159 6986 6232 24 -527 -831 C
ATOM 2874 CD1 TRP A 477 33.927 31.076 -30.844 1.00 61.64 C
ANISOU 2874 CD1 TRP A 477 8982 7761 6679 -89 -669 -945 C
ATOM 2875 CD2 TRP A 477 34.713 30.503 -32.859 1.00 53.02 C
ANISOU 2875 CD2 TRP A 477 7444 6778 5924 77 -693 -743 C
ATOM 2876 NE1 TRP A 477 35.295 31.198 -30.808 1.00 59.55 N
ANISOU 2876 NE1 TRP A 477 8495 7755 6376 -126 -938 -935 N
ATOM 2877 CE2 TRP A 477 35.802 30.850 -32.032 1.00 54.74 C
ANISOU 2877 CE2 TRP A 477 7596 7222 5981 -20 -944 -806 C
ATOM 2878 CE3 TRP A 477 34.967 30.103 -34.176 1.00 54.49 C
ANISOU 2878 CE3 TRP A 477 7393 7006 6303 196 -649 -630 C
ATOM 2879 CZ2 TRP A 477 37.120 30.812 -32.478 1.00 61.26 C
ANISOU 2879 CZ2 TRP A 477 8085 8333 6859 -5 -1143 -751 C
ATOM 2880 CZ3 TRP A 477 36.275 30.067 -34.617 1.00 57.34 C
ANISOU 2880 CZ3 TRP A 477 7452 7633 6700 227 -821 -577 C
ATOM 2881 CH2 TRP A 477 37.336 30.419 -33.771 1.00 62.92 C
ANISOU 2881 CH2 TRP A 477 8057 8581 7270 127 -1061 -632 C
ATOM 2882 N HIS A 478 29.212 30.789 -33.620 1.00 57.32 N
ANISOU 2882 N HIS A 478 8434 6552 6791 89 270 -882 N
ATOM 2883 CA HIS A 478 27.955 30.274 -34.154 1.00 61.96 C
ANISOU 2883 CA HIS A 478 8995 7073 7474 141 471 -858 C
ATOM 2884 C HIS A 478 27.597 30.935 -35.478 1.00 64.86 C
ANISOU 2884 C HIS A 478 9138 7414 8091 179 517 -844 C
ATOM 2885 O HIS A 478 27.184 30.254 -36.431 1.00 69.09 O
ANISOU 2885 O HIS A 478 9551 7984 8715 242 556 -775 O
ATOM 2886 CB HIS A 478 26.832 30.479 -33.139 1.00 68.64 C
ANISOU 2886 CB HIS A 478 10014 7857 8210 88 671 -969 C
ATOM 2887 CG HIS A 478 26.975 29.642 -31.908 1.00 77.99 C
ANISOU 2887 CG HIS A 478 11449 9077 9108 54 667 -941 C
ATOM 2888 ND1 HIS A 478 27.614 28.421 -31.911 1.00 80.53 N
ANISOU 2888 ND1 HIS A 478 11840 9430 9326 109 548 -789 N
ATOM 2889 CD2 HIS A 478 26.566 29.851 -30.635 1.00 79.46 C
ANISOU 2889 CD2 HIS A 478 11856 9267 9067 -10 773 -1033 C
ATOM 2890 CE1 HIS A 478 27.591 27.912 -30.693 1.00 82.48 C
ANISOU 2890 CE1 HIS A 478 12353 9692 9296 80 569 -758 C
ATOM 2891 NE2 HIS A 478 26.961 28.759 -29.900 1.00 81.64 N
ANISOU 2891 NE2 HIS A 478 12337 9589 9094 -6 709 -908 N
ATOM 2892 N LEU A 479 27.746 32.264 -35.553 1.00 61.01 N
ANISOU 2892 N LEU A 479 8622 6855 7705 137 508 -908 N
ATOM 2893 CA LEU A 479 27.419 32.976 -36.785 1.00 59.12 C
ANISOU 2893 CA LEU A 479 8209 6573 7680 193 549 -855 C
ATOM 2894 C LEU A 479 28.325 32.552 -37.937 1.00 57.67 C
ANISOU 2894 C LEU A 479 7845 6515 7554 219 424 -714 C
ATOM 2895 O LEU A 479 27.850 32.356 -39.058 1.00 61.61 O
ANISOU 2895 O LEU A 479 8203 7061 8146 304 467 -640 O
ATOM 2896 CB LEU A 479 27.488 34.483 -36.553 1.00 58.85 C
ANISOU 2896 CB LEU A 479 8250 6370 7739 139 568 -936 C
ATOM 2897 CG LEU A 479 26.244 35.001 -35.829 1.00 64.59 C
ANISOU 2897 CG LEU A 479 9104 6973 8466 203 755 -1080 C
ATOM 2898 CD1 LEU A 479 26.494 36.362 -35.212 1.00 66.84 C
ANISOU 2898 CD1 LEU A 479 9567 7044 8784 136 764 -1219 C
ATOM 2899 CD2 LEU A 479 25.045 35.043 -36.773 1.00 63.22 C
ANISOU 2899 CD2 LEU A 479 8760 6813 8446 369 883 -1020 C
ATOM 2900 N GLY A 480 29.626 32.388 -37.675 1.00 54.80 N
ANISOU 2900 N GLY A 480 7466 6243 7114 157 269 -686 N
ATOM 2901 CA GLY A 480 30.544 31.946 -38.719 1.00 57.96 C
ANISOU 2901 CA GLY A 480 7669 6803 7551 204 177 -567 C
ATOM 2902 C GLY A 480 30.264 30.532 -39.198 1.00 62.52 C
ANISOU 2902 C GLY A 480 8223 7457 8075 347 197 -526 C
ATOM 2903 O GLY A 480 30.358 30.241 -40.398 1.00 60.66 O
ANISOU 2903 O GLY A 480 7838 7312 7897 424 207 -459 O
ATOM 2904 N TYR A 481 29.941 29.631 -38.261 1.00 65.66 N
ANISOU 2904 N TYR A 481 8796 7807 8344 371 208 -566 N
ATOM 2905 CA TYR A 481 29.558 28.259 -38.598 1.00 63.47 C
ANISOU 2905 CA TYR A 481 8570 7521 8026 470 248 -541 C
ATOM 2906 C TYR A 481 28.337 28.240 -39.517 1.00 64.29 C
ANISOU 2906 C TYR A 481 8594 7594 8238 464 380 -570 C
ATOM 2907 O TYR A 481 28.345 27.608 -40.591 1.00 72.24 O
ANISOU 2907 O TYR A 481 9506 8663 9277 536 374 -552 O
ATOM 2908 CB TYR A 481 29.277 27.502 -37.299 1.00 55.37 C
ANISOU 2908 CB TYR A 481 7799 6401 6840 450 270 -556 C
ATOM 2909 CG TYR A 481 29.593 26.033 -37.305 1.00 49.82 C
ANISOU 2909 CG TYR A 481 7221 5657 6051 566 233 -491 C
ATOM 2910 CD1 TYR A 481 28.653 25.110 -37.738 1.00 44.16 C
ANISOU 2910 CD1 TYR A 481 6586 4823 5369 546 359 -508 C
ATOM 2911 CD2 TYR A 481 30.826 25.561 -36.860 1.00 50.53 C
ANISOU 2911 CD2 TYR A 481 7353 5819 6028 698 66 -418 C
ATOM 2912 CE1 TYR A 481 28.931 23.755 -37.736 1.00 47.52 C
ANISOU 2912 CE1 TYR A 481 7189 5137 5729 647 338 -457 C
ATOM 2913 CE2 TYR A 481 31.113 24.202 -36.852 1.00 47.38 C
ANISOU 2913 CE2 TYR A 481 7110 5333 5557 859 36 -346 C
ATOM 2914 CZ TYR A 481 30.161 23.302 -37.297 1.00 49.46 C
ANISOU 2914 CZ TYR A 481 7511 5412 5868 828 181 -368 C
ATOM 2915 OH TYR A 481 30.425 21.944 -37.300 1.00 48.03 O
ANISOU 2915 OH TYR A 481 7544 5072 5632 979 166 -306 O
ATOM 2916 N TRP A 482 27.272 28.935 -39.103 1.00 53.12 N
ANISOU 2916 N TRP A 482 7206 6110 6867 392 497 -631 N
ATOM 2917 CA TRP A 482 26.066 29.014 -39.921 1.00 60.30 C
ANISOU 2917 CA TRP A 482 7987 7046 7877 401 600 -660 C
ATOM 2918 C TRP A 482 26.347 29.672 -41.273 1.00 56.38 C
ANISOU 2918 C TRP A 482 7297 6648 7477 477 540 -589 C
ATOM 2919 O TRP A 482 25.798 29.255 -42.302 1.00 52.75 O
ANISOU 2919 O TRP A 482 6716 6284 7042 519 549 -588 O
ATOM 2920 CB TRP A 482 24.978 29.777 -39.170 1.00 67.79 C
ANISOU 2920 CB TRP A 482 8964 7934 8859 362 738 -738 C
ATOM 2921 CG TRP A 482 23.741 29.921 -39.970 1.00 78.06 C
ANISOU 2921 CG TRP A 482 10077 9317 10265 401 822 -764 C
ATOM 2922 CD1 TRP A 482 23.294 31.053 -40.594 1.00 85.27 C
ANISOU 2922 CD1 TRP A 482 10849 10255 11297 506 832 -739 C
ATOM 2923 CD2 TRP A 482 22.784 28.899 -40.253 1.00 79.92 C
ANISOU 2923 CD2 TRP A 482 10240 9633 10494 336 894 -815 C
ATOM 2924 NE1 TRP A 482 22.112 30.796 -41.246 1.00 89.07 N
ANISOU 2924 NE1 TRP A 482 11138 10874 11832 543 886 -769 N
ATOM 2925 CE2 TRP A 482 21.778 29.479 -41.053 1.00 87.85 C
ANISOU 2925 CE2 TRP A 482 11007 10766 11605 410 925 -832 C
ATOM 2926 CE3 TRP A 482 22.675 27.551 -39.904 1.00 85.49 C
ANISOU 2926 CE3 TRP A 482 11069 10300 11114 213 933 -844 C
ATOM 2927 CZ2 TRP A 482 20.681 28.753 -41.512 1.00 92.63 C
ANISOU 2927 CZ2 TRP A 482 11448 11517 12231 337 977 -903 C
ATOM 2928 CZ3 TRP A 482 21.588 26.833 -40.358 1.00 91.03 C
ANISOU 2928 CZ3 TRP A 482 11650 11086 11851 109 1009 -914 C
ATOM 2929 CH2 TRP A 482 20.605 27.434 -41.155 1.00 92.46 C
ANISOU 2929 CH2 TRP A 482 11547 11449 12136 157 1023 -956 C
ATOM 2930 N LEU A 483 27.219 30.686 -41.294 1.00 54.08 N
ANISOU 2930 N LEU A 483 6984 6342 7223 472 478 -528 N
ATOM 2931 CA LEU A 483 27.576 31.339 -42.549 1.00 57.68 C
ANISOU 2931 CA LEU A 483 7286 6882 7746 520 442 -420 C
ATOM 2932 C LEU A 483 28.245 30.364 -43.511 1.00 52.87 C
ANISOU 2932 C LEU A 483 6580 6441 7068 582 384 -380 C
ATOM 2933 O LEU A 483 27.984 30.407 -44.718 1.00 46.81 O
ANISOU 2933 O LEU A 483 5692 5791 6302 647 389 -327 O
ATOM 2934 CB LEU A 483 28.476 32.548 -42.289 1.00 59.19 C
ANISOU 2934 CB LEU A 483 7499 6998 7993 438 403 -362 C
ATOM 2935 CG LEU A 483 28.629 33.482 -43.493 1.00 64.90 C
ANISOU 2935 CG LEU A 483 8114 7749 8796 460 412 -215 C
ATOM 2936 CD1 LEU A 483 27.276 33.777 -44.129 1.00 70.21 C
ANISOU 2936 CD1 LEU A 483 8750 8406 9522 590 479 -190 C
ATOM 2937 CD2 LEU A 483 29.317 34.770 -43.098 1.00 68.96 C
ANISOU 2937 CD2 LEU A 483 8702 8107 9394 322 403 -174 C
ATOM 2938 N CYS A 484 29.138 29.505 -42.999 1.00 49.61 N
ANISOU 2938 N CYS A 484 6225 6050 6576 591 323 -405 N
ATOM 2939 CA CYS A 484 29.720 28.458 -43.839 1.00 52.43 C
ANISOU 2939 CA CYS A 484 6518 6538 6865 700 289 -402 C
ATOM 2940 C CYS A 484 28.650 27.513 -44.377 1.00 58.17 C
ANISOU 2940 C CYS A 484 7287 7246 7568 729 342 -490 C
ATOM 2941 O CYS A 484 28.770 27.018 -45.506 1.00 56.80 O
ANISOU 2941 O CYS A 484 7035 7197 7349 808 335 -507 O
ATOM 2942 CB CYS A 484 30.775 27.665 -43.079 1.00 50.93 C
ANISOU 2942 CB CYS A 484 6398 6351 6600 761 211 -411 C
ATOM 2943 SG CYS A 484 32.206 28.583 -42.525 1.00 51.68 S
ANISOU 2943 SG CYS A 484 6373 6561 6701 701 107 -338 S
ATOM 2944 N TYR A 485 27.625 27.210 -43.563 1.00 62.51 N
ANISOU 2944 N TYR A 485 7961 7657 8133 646 401 -563 N
ATOM 2945 CA TYR A 485 26.476 26.450 -44.075 1.00 56.60 C
ANISOU 2945 CA TYR A 485 7210 6911 7383 603 456 -660 C
ATOM 2946 C TYR A 485 25.826 27.141 -45.277 1.00 55.72 C
ANISOU 2946 C TYR A 485 6895 6971 7304 632 448 -644 C
ATOM 2947 O TYR A 485 25.380 26.471 -46.214 1.00 59.07 O
ANISOU 2947 O TYR A 485 7263 7499 7682 635 431 -721 O
ATOM 2948 CB TYR A 485 25.424 26.229 -42.988 1.00 59.50 C
ANISOU 2948 CB TYR A 485 7689 7148 7771 471 553 -723 C
ATOM 2949 CG TYR A 485 25.727 25.168 -41.963 1.00 59.10 C
ANISOU 2949 CG TYR A 485 7888 6924 7645 427 576 -736 C
ATOM 2950 CD1 TYR A 485 26.754 24.256 -42.147 1.00 54.27 C
ANISOU 2950 CD1 TYR A 485 7393 6258 6969 537 501 -715 C
ATOM 2951 CD2 TYR A 485 24.962 25.075 -40.808 1.00 62.15 C
ANISOU 2951 CD2 TYR A 485 8401 7204 8009 297 687 -756 C
ATOM 2952 CE1 TYR A 485 27.012 23.284 -41.199 1.00 58.82 C
ANISOU 2952 CE1 TYR A 485 8232 6649 7468 536 513 -692 C
ATOM 2953 CE2 TYR A 485 25.211 24.113 -39.861 1.00 61.83 C
ANISOU 2953 CE2 TYR A 485 8626 6996 7869 256 715 -728 C
ATOM 2954 CZ TYR A 485 26.234 23.219 -40.054 1.00 61.65 C
ANISOU 2954 CZ TYR A 485 8742 6891 7790 384 617 -684 C
ATOM 2955 OH TYR A 485 26.475 22.260 -39.097 1.00 61.19 O
ANISOU 2955 OH TYR A 485 8983 6641 7624 381 635 -621 O
ATOM 2956 N VAL A 486 25.720 28.477 -45.242 1.00 51.66 N
ANISOU 2956 N VAL A 486 6294 6477 6859 655 454 -549 N
ATOM 2957 CA VAL A 486 24.997 29.236 -46.285 1.00 47.86 C
ANISOU 2957 CA VAL A 486 5644 6140 6402 722 440 -492 C
ATOM 2958 C VAL A 486 25.596 29.047 -47.698 1.00 53.00 C
ANISOU 2958 C VAL A 486 6206 6985 6948 802 376 -433 C
ATOM 2959 O VAL A 486 24.910 29.286 -48.707 1.00 48.19 O
ANISOU 2959 O VAL A 486 5471 6546 6294 862 340 -407 O
ATOM 2960 CB VAL A 486 24.934 30.733 -45.866 1.00 49.05 C
ANISOU 2960 CB VAL A 486 5793 6187 6656 758 470 -381 C
ATOM 2961 CG1 VAL A 486 24.142 31.603 -46.842 1.00 49.05 C
ANISOU 2961 CG1 VAL A 486 5653 6299 6686 880 452 -282 C
ATOM 2962 CG2 VAL A 486 24.261 30.859 -44.521 1.00 49.95 C
ANISOU 2962 CG2 VAL A 486 5997 6146 6834 699 555 -478 C
ATOM 2963 N ASN A 487 26.860 28.612 -47.791 1.00 52.76 N
ANISOU 2963 N ASN A 487 6224 6966 6857 823 359 -414 N
ATOM 2964 CA ASN A 487 27.479 28.255 -49.070 1.00 57.09 C
ANISOU 2964 CA ASN A 487 6695 7722 7276 908 334 -394 C
ATOM 2965 C ASN A 487 26.618 27.253 -49.835 1.00 58.31 C
ANISOU 2965 C ASN A 487 6841 7981 7333 914 308 -556 C
ATOM 2966 O ASN A 487 26.392 27.389 -51.047 1.00 56.76 O
ANISOU 2966 O ASN A 487 6545 8005 7016 973 273 -537 O
ATOM 2967 CB ASN A 487 28.860 27.653 -48.799 1.00 55.02 C
ANISOU 2967 CB ASN A 487 6476 7453 6977 953 338 -406 C
ATOM 2968 CG ASN A 487 29.711 27.496 -50.048 1.00 53.61 C
ANISOU 2968 CG ASN A 487 6189 7517 6662 1060 352 -369 C
ATOM 2969 OD1 ASN A 487 29.265 27.711 -51.178 1.00 52.86 O
ANISOU 2969 OD1 ASN A 487 6023 7598 6462 1092 353 -343 O
ATOM 2970 ND2 ASN A 487 30.946 27.051 -49.844 1.00 55.21 N
ANISOU 2970 ND2 ASN A 487 6372 7764 6842 1135 363 -375 N
ATOM 2971 N SER A 488 26.155 26.223 -49.125 1.00 58.06 N
ANISOU 2971 N SER A 488 6930 7792 7337 832 323 -717 N
ATOM 2972 CA SER A 488 25.325 25.183 -49.717 1.00 56.53 C
ANISOU 2972 CA SER A 488 6756 7650 7073 767 301 -907 C
ATOM 2973 C SER A 488 23.992 25.728 -50.209 1.00 59.16 C
ANISOU 2973 C SER A 488 6909 8158 7412 711 259 -918 C
ATOM 2974 O SER A 488 23.402 25.175 -51.145 1.00 60.64 O
ANISOU 2974 O SER A 488 7030 8518 7490 674 196 -1054 O
ATOM 2975 CB SER A 488 25.102 24.083 -48.683 1.00 49.82 C
ANISOU 2975 CB SER A 488 6107 6536 6286 648 352 -1035 C
ATOM 2976 OG SER A 488 26.334 23.690 -48.096 1.00 47.10 O
ANISOU 2976 OG SER A 488 5918 6040 5939 752 368 -987 O
ATOM 2977 N THR A 489 23.517 26.818 -49.609 1.00 61.52 N
ANISOU 2977 N THR A 489 7121 8429 7827 722 282 -790 N
ATOM 2978 CA THR A 489 22.284 27.452 -50.056 1.00 62.26 C
ANISOU 2978 CA THR A 489 7010 8710 7936 742 236 -773 C
ATOM 2979 C THR A 489 22.511 28.280 -51.314 1.00 63.44 C
ANISOU 2979 C THR A 489 7049 9089 7967 908 151 -613 C
ATOM 2980 O THR A 489 21.667 28.293 -52.217 1.00 62.37 O
ANISOU 2980 O THR A 489 6753 9211 7732 945 54 -645 O
ATOM 2981 CB THR A 489 21.724 28.338 -48.942 1.00 57.06 C
ANISOU 2981 CB THR A 489 6322 7916 7444 748 313 -701 C
ATOM 2982 OG1 THR A 489 21.747 27.619 -47.702 1.00 60.05 O
ANISOU 2982 OG1 THR A 489 6851 8076 7888 598 412 -808 O
ATOM 2983 CG2 THR A 489 20.291 28.751 -49.251 1.00 53.81 C
ANISOU 2983 CG2 THR A 489 5666 7712 7068 787 278 -728 C
ATOM 2984 N VAL A 490 23.651 28.965 -51.390 1.00 63.04 N
ANISOU 2984 N VAL A 490 7078 8966 7906 992 184 -434 N
ATOM 2985 CA VAL A 490 23.876 29.914 -52.477 1.00 66.84 C
ANISOU 2985 CA VAL A 490 7489 9627 8280 1130 140 -223 C
ATOM 2986 C VAL A 490 24.419 29.251 -53.747 1.00 65.71 C
ANISOU 2986 C VAL A 490 7337 9738 7893 1164 98 -265 C
ATOM 2987 O VAL A 490 24.190 29.773 -54.850 1.00 59.60 O
ANISOU 2987 O VAL A 490 6485 9205 6955 1270 34 -133 O
ATOM 2988 CB VAL A 490 24.797 31.042 -51.956 1.00 72.18 C
ANISOU 2988 CB VAL A 490 8255 10101 9069 1148 216 -8 C
ATOM 2989 CG1 VAL A 490 25.046 32.123 -52.993 1.00 79.05 C
ANISOU 2989 CG1 VAL A 490 9100 11090 9846 1259 202 259 C
ATOM 2990 CG2 VAL A 490 24.177 31.688 -50.731 1.00 73.70 C
ANISOU 2990 CG2 VAL A 490 8484 10048 9472 1129 260 -13 C
ATOM 2991 N ASN A 491 25.075 28.092 -53.629 1.00 69.95 N
ANISOU 2991 N ASN A 491 7967 10229 8383 1102 134 -451 N
ATOM 2992 CA ASN A 491 25.651 27.426 -54.803 1.00 69.53 C
ANISOU 2992 CA ASN A 491 7926 10406 8088 1162 123 -532 C
ATOM 2993 C ASN A 491 24.663 27.128 -55.949 1.00 72.06 C
ANISOU 2993 C ASN A 491 8157 11024 8198 1176 2 -643 C
ATOM 2994 O ASN A 491 25.039 27.352 -57.118 1.00 78.51 O
ANISOU 2994 O ASN A 491 8947 12113 8771 1277 -16 -560 O
ATOM 2995 CB ASN A 491 26.390 26.161 -54.337 1.00 69.62 C
ANISOU 2995 CB ASN A 491 8078 10256 8119 1132 183 -743 C
ATOM 2996 CG ASN A 491 27.588 25.833 -55.200 1.00 75.23 C
ANISOU 2996 CG ASN A 491 8804 11138 8642 1258 245 -749 C
ATOM 2997 OD1 ASN A 491 27.561 24.884 -55.978 1.00 85.09 O
ANISOU 2997 OD1 ASN A 491 10112 12505 9713 1297 233 -962 O
ATOM 2998 ND2 ASN A 491 28.650 26.618 -55.065 1.00 73.61 N
ANISOU 2998 ND2 ASN A 491 8540 10957 8472 1309 324 -532 N
ATOM 2999 N PRO A 492 23.436 26.621 -55.721 1.00 63.97 N
ANISOU 2999 N PRO A 492 7072 10006 7227 1065 -85 -829 N
ATOM 3000 CA PRO A 492 22.511 26.475 -56.864 1.00 68.48 C
ANISOU 3000 CA PRO A 492 7510 10930 7578 1073 -237 -924 C
ATOM 3001 C PRO A 492 22.104 27.799 -57.494 1.00 71.33 C
ANISOU 3001 C PRO A 492 7722 11525 7853 1244 -321 -630 C
ATOM 3002 O PRO A 492 21.865 27.852 -58.709 1.00 70.17 O
ANISOU 3002 O PRO A 492 7510 11728 7424 1326 -438 -616 O
ATOM 3003 CB PRO A 492 21.305 25.746 -56.252 1.00 60.94 C
ANISOU 3003 CB PRO A 492 6480 9914 6761 872 -292 -1169 C
ATOM 3004 CG PRO A 492 21.856 25.023 -55.099 1.00 53.76 C
ANISOU 3004 CG PRO A 492 5764 8617 6045 755 -151 -1270 C
ATOM 3005 CD PRO A 492 22.887 25.947 -54.527 1.00 49.51 C
ANISOU 3005 CD PRO A 492 5291 7908 5611 898 -47 -999 C
ATOM 3006 N ILE A 493 22.017 28.874 -56.703 1.00 72.31 N
ANISOU 3006 N ILE A 493 7821 11455 8199 1312 -266 -396 N
ATOM 3007 CA ILE A 493 21.771 30.196 -57.272 1.00 74.54 C
ANISOU 3007 CA ILE A 493 8032 11870 8420 1510 -323 -76 C
ATOM 3008 C ILE A 493 22.946 30.637 -58.143 1.00 76.46 C
ANISOU 3008 C ILE A 493 8395 12200 8457 1592 -257 146 C
ATOM 3009 O ILE A 493 22.750 31.314 -59.162 1.00 80.92 O
ANISOU 3009 O ILE A 493 8928 13013 8806 1741 -336 366 O
ATOM 3010 CB ILE A 493 21.483 31.208 -56.146 1.00 73.41 C
ANISOU 3010 CB ILE A 493 7889 11422 8579 1563 -251 85 C
ATOM 3011 CG1 ILE A 493 20.412 30.663 -55.198 1.00 74.44 C
ANISOU 3011 CG1 ILE A 493 7895 11489 8900 1457 -263 -154 C
ATOM 3012 CG2 ILE A 493 21.015 32.535 -56.726 1.00 74.32 C
ANISOU 3012 CG2 ILE A 493 7953 11631 8653 1803 -324 403 C
ATOM 3013 CD1 ILE A 493 19.928 31.670 -54.162 1.00 71.66 C
ANISOU 3013 CD1 ILE A 493 7520 10899 8808 1551 -191 -33 C
ATOM 3014 N CYS A 494 24.174 30.254 -57.769 1.00 73.18 N
ANISOU 3014 N CYS A 494 8105 11611 8088 1501 -109 103 N
ATOM 3015 CA CYS A 494 25.332 30.469 -58.636 1.00 73.96 C
ANISOU 3015 CA CYS A 494 8269 11861 7972 1546 -16 263 C
ATOM 3016 C CYS A 494 25.144 29.771 -59.974 1.00 80.20 C
ANISOU 3016 C CYS A 494 9033 13051 8387 1604 -100 131 C
ATOM 3017 O CYS A 494 25.390 30.367 -61.031 1.00 82.92 O
ANISOU 3017 O CYS A 494 9386 13656 8465 1706 -98 358 O
ATOM 3018 CB CYS A 494 26.615 29.982 -57.964 1.00 77.54 C
ANISOU 3018 CB CYS A 494 8794 12124 8544 1455 139 178 C
ATOM 3019 SG CYS A 494 27.077 30.874 -56.488 1.00 86.78 S
ANISOU 3019 SG CYS A 494 10010 12882 10081 1364 229 334 S
ATOM 3020 N TYR A 495 24.776 28.481 -59.942 1.00 83.18 N
ANISOU 3020 N TYR A 495 9412 13469 8724 1523 -159 -243 N
ATOM 3021 CA TYR A 495 24.517 27.748 -61.186 1.00 83.92 C
ANISOU 3021 CA TYR A 495 9503 13934 8450 1552 -256 -440 C
ATOM 3022 C TYR A 495 23.436 28.429 -62.024 1.00 90.64 C
ANISOU 3022 C TYR A 495 10228 15115 9095 1647 -454 -291 C
ATOM 3023 O TYR A 495 23.531 28.477 -63.256 1.00 98.61 O
ANISOU 3023 O TYR A 495 11250 16496 9721 1741 -511 -241 O
ATOM 3024 CB TYR A 495 24.102 26.304 -60.898 1.00 78.81 C
ANISOU 3024 CB TYR A 495 8904 13197 7844 1406 -305 -883 C
ATOM 3025 CG TYR A 495 25.097 25.452 -60.142 1.00 75.30 C
ANISOU 3025 CG TYR A 495 8612 12432 7566 1361 -139 -1050 C
ATOM 3026 CD1 TYR A 495 26.445 25.782 -60.088 1.00 75.76 C
ANISOU 3026 CD1 TYR A 495 8715 12444 7627 1466 33 -877 C
ATOM 3027 CD2 TYR A 495 24.678 24.308 -59.477 1.00 78.11 C
ANISOU 3027 CD2 TYR A 495 9060 12543 8074 1213 -157 -1371 C
ATOM 3028 CE1 TYR A 495 27.342 24.994 -59.392 1.00 79.75 C
ANISOU 3028 CE1 TYR A 495 9327 12697 8277 1474 157 -1022 C
ATOM 3029 CE2 TYR A 495 25.565 23.517 -58.779 1.00 80.53 C
ANISOU 3029 CE2 TYR A 495 9533 12544 8523 1220 -23 -1495 C
ATOM 3030 CZ TYR A 495 26.893 23.861 -58.742 1.00 82.16 C
ANISOU 3030 CZ TYR A 495 9755 12740 8722 1375 121 -1322 C
ATOM 3031 OH TYR A 495 27.775 23.071 -58.043 1.00 87.37 O
ANISOU 3031 OH TYR A 495 10548 13132 9515 1428 230 -1436 O
ATOM 3032 N ALA A 496 22.399 28.956 -61.368 1.00 91.83 N
ANISOU 3032 N ALA A 496 10249 15163 9478 1650 -560 -216 N
ATOM 3033 CA ALA A 496 21.302 29.596 -62.090 1.00 98.56 C
ANISOU 3033 CA ALA A 496 10942 16346 10160 1791 -772 -71 C
ATOM 3034 C ALA A 496 21.690 30.958 -62.657 1.00103.69 C
ANISOU 3034 C ALA A 496 11656 17056 10687 2007 -741 402 C
ATOM 3035 O ALA A 496 21.094 31.405 -63.644 1.00106.10 O
ANISOU 3035 O ALA A 496 11892 17719 10702 2173 -914 565 O
ATOM 3036 CB ALA A 496 20.088 29.747 -61.173 1.00 96.21 C
ANISOU 3036 CB ALA A 496 10453 15935 10166 1761 -868 -141 C
ATOM 3037 N LEU A 497 22.676 31.630 -62.063 1.00104.51 N
ANISOU 3037 N LEU A 497 11898 16817 10992 1996 -533 634 N
ATOM 3038 CA LEU A 497 23.036 32.973 -62.505 1.00105.08 C
ANISOU 3038 CA LEU A 497 12070 16861 10995 2150 -478 1099 C
ATOM 3039 C LEU A 497 24.139 32.996 -63.555 1.00105.34 C
ANISOU 3039 C LEU A 497 12227 17119 10680 2145 -352 1256 C
ATOM 3040 O LEU A 497 24.327 34.031 -64.206 1.00108.43 O
ANISOU 3040 O LEU A 497 12712 17573 10911 2264 -324 1661 O
ATOM 3041 CB LEU A 497 23.465 33.838 -61.315 1.00102.96 C
ANISOU 3041 CB LEU A 497 11891 16096 11134 2104 -322 1278 C
ATOM 3042 CG LEU A 497 22.353 34.359 -60.404 1.00104.19 C
ANISOU 3042 CG LEU A 497 11960 16028 11599 2200 -412 1278 C
ATOM 3043 CD1 LEU A 497 22.927 35.246 -59.311 1.00103.43 C
ANISOU 3043 CD1 LEU A 497 12008 15440 11850 2143 -241 1435 C
ATOM 3044 CD2 LEU A 497 21.306 35.112 -61.212 1.00108.15 C
ANISOU 3044 CD2 LEU A 497 12384 16776 11933 2480 -604 1521 C
ATOM 3045 N CYS A 498 24.874 31.898 -63.738 1.00101.72 N
ANISOU 3045 N CYS A 498 11782 16774 10095 2022 -257 957 N
ATOM 3046 CA CYS A 498 26.035 31.912 -64.618 1.00103.12 C
ANISOU 3046 CA CYS A 498 12049 17167 9967 2018 -80 1085 C
ATOM 3047 C CYS A 498 26.044 30.773 -65.631 1.00105.93 C
ANISOU 3047 C CYS A 498 12401 17939 9910 2040 -131 763 C
ATOM 3048 O CYS A 498 27.037 30.613 -66.352 1.00116.25 O
ANISOU 3048 O CYS A 498 13769 19461 10941 2048 45 800 O
ATOM 3049 CB CYS A 498 27.324 31.876 -63.789 1.00105.11 C
ANISOU 3049 CB CYS A 498 12329 17121 10488 1876 167 1082 C
ATOM 3050 SG CYS A 498 27.623 33.382 -62.833 1.00109.50 S
ANISOU 3050 SG CYS A 498 12943 17225 11435 1807 268 1491 S
ATOM 3051 N ASN A 499 24.977 29.984 -65.718 1.00100.03 N
ANISOU 3051 N ASN A 499 11581 17323 9103 2034 -355 432 N
ATOM 3052 CA ASN A 499 24.871 28.923 -66.716 1.00 97.85 C
ANISOU 3052 CA ASN A 499 11330 17430 8417 2033 -433 86 C
ATOM 3053 C ASN A 499 23.478 29.011 -67.326 1.00100.61 C
ANISOU 3053 C ASN A 499 11570 18110 8549 2095 -752 50 C
ATOM 3054 O ASN A 499 22.485 28.725 -66.650 1.00102.71 O
ANISOU 3054 O ASN A 499 11702 18249 9074 2014 -917 -140 O
ATOM 3055 CB ASN A 499 25.138 27.548 -66.094 1.00 92.02 C
ANISOU 3055 CB ASN A 499 10632 16471 7861 1894 -369 -402 C
ATOM 3056 CG ASN A 499 25.302 26.441 -67.133 1.00 92.74 C
ANISOU 3056 CG ASN A 499 10818 16890 7530 1899 -386 -786 C
ATOM 3057 OD1 ASN A 499 24.527 26.326 -68.080 1.00 98.70 O
ANISOU 3057 OD1 ASN A 499 11549 18034 7919 1922 -591 -883 O
ATOM 3058 ND2 ASN A 499 26.333 25.623 -66.955 1.00 89.70 N
ANISOU 3058 ND2 ASN A 499 10542 16356 7183 1897 -173 -1017 N
ATOM 3059 N ARG A 500 23.407 29.426 -68.596 1.00102.84 N
ANISOU 3059 N ARG A 500 11888 18847 8340 2237 -837 245 N
ATOM 3060 CA ARG A 500 22.116 29.587 -69.261 1.00107.45 C
ANISOU 3060 CA ARG A 500 12340 19822 8664 2333 -1175 248 C
ATOM 3061 C ARG A 500 21.393 28.258 -69.454 1.00108.45 C
ANISOU 3061 C ARG A 500 12383 20152 8672 2166 -1373 -330 C
ATOM 3062 O ARG A 500 20.158 28.234 -69.502 1.00110.00 O
ANISOU 3062 O ARG A 500 12376 20557 8861 2158 -1666 -428 O
ATOM 3063 CB ARG A 500 22.303 30.284 -70.610 1.00109.85 C
ANISOU 3063 CB ARG A 500 12742 20544 8450 2515 -1204 597 C
ATOM 3064 N THR A 501 22.129 27.148 -69.559 1.00105.14 N
ANISOU 3064 N THR A 501 12111 19669 8170 2031 -1217 -725 N
ATOM 3065 CA THR A 501 21.479 25.844 -69.672 1.00101.67 C
ANISOU 3065 CA THR A 501 11650 19322 7659 1831 -1382 -1301 C
ATOM 3066 C THR A 501 20.826 25.452 -68.352 1.00 95.45 C
ANISOU 3066 C THR A 501 10738 18107 7422 1633 -1416 -1487 C
ATOM 3067 O THR A 501 19.680 24.982 -68.328 1.00 95.99 O
ANISOU 3067 O THR A 501 10639 18324 7510 1473 -1662 -1759 O
ATOM 3068 CB THR A 501 22.483 24.782 -70.119 1.00100.52 C
ANISOU 3068 CB THR A 501 11743 19127 7322 1777 -1172 -1661 C
ATOM 3069 OG1 THR A 501 23.202 25.257 -71.263 1.00110.22 O
ANISOU 3069 OG1 THR A 501 13074 20606 8200 1933 -1044 -1405 O
ATOM 3070 CG2 THR A 501 21.760 23.497 -70.489 1.00100.97 C
ANISOU 3070 CG2 THR A 501 11835 19193 7334 1544 -1335 -2213 C
ATOM 3071 N PHE A 502 21.553 25.631 -67.242 1.00 87.97 N
ANISOU 3071 N PHE A 502 9861 16658 6908 1623 -1167 -1345 N
ATOM 3072 CA PHE A 502 20.972 25.424 -65.918 1.00 88.04 C
ANISOU 3072 CA PHE A 502 9767 16265 7419 1460 -1170 -1442 C
ATOM 3073 C PHE A 502 19.784 26.346 -65.686 1.00 91.86 C
ANISOU 3073 C PHE A 502 9980 16893 8029 1524 -1375 -1199 C
ATOM 3074 O PHE A 502 18.765 25.921 -65.137 1.00 95.51 O
ANISOU 3074 O PHE A 502 10265 17326 8699 1351 -1506 -1423 O
ATOM 3075 CB PHE A 502 22.022 25.644 -64.827 1.00 81.17 C
ANISOU 3075 CB PHE A 502 9020 14896 6925 1481 -886 -1271 C
ATOM 3076 CG PHE A 502 22.782 24.405 -64.454 1.00 80.67 C
ANISOU 3076 CG PHE A 502 9158 14541 6952 1365 -721 -1627 C
ATOM 3077 CD1 PHE A 502 22.125 23.323 -63.890 1.00 76.22 C
ANISOU 3077 CD1 PHE A 502 8624 13763 6572 1133 -785 -2013 C
ATOM 3078 CD2 PHE A 502 24.154 24.327 -64.651 1.00 82.98 C
ANISOU 3078 CD2 PHE A 502 9606 14768 7156 1493 -493 -1562 C
ATOM 3079 CE1 PHE A 502 22.819 22.180 -63.537 1.00 78.82 C
ANISOU 3079 CE1 PHE A 502 9188 13769 6991 1062 -635 -2315 C
ATOM 3080 CE2 PHE A 502 24.858 23.186 -64.301 1.00 83.17 C
ANISOU 3080 CE2 PHE A 502 9812 14520 7269 1454 -349 -1880 C
ATOM 3081 CZ PHE A 502 24.188 22.111 -63.742 1.00 82.69 C
ANISOU 3081 CZ PHE A 502 9832 14196 7390 1253 -424 -2249 C
ATOM 3082 N ARG A 503 19.901 27.613 -66.098 1.00 88.81 N
ANISOU 3082 N ARG A 503 9560 16661 7523 1779 -1393 -735 N
ATOM 3083 CA ARG A 503 18.819 28.572 -65.894 1.00 88.18 C
ANISOU 3083 CA ARG A 503 9241 16696 7567 1925 -1578 -472 C
ATOM 3084 C ARG A 503 17.575 28.179 -66.684 1.00 92.10 C
ANISOU 3084 C ARG A 503 9493 17724 7777 1898 -1920 -696 C
ATOM 3085 O ARG A 503 16.453 28.227 -66.160 1.00 95.11 O
ANISOU 3085 O ARG A 503 9591 18163 8383 1855 -2075 -775 O
ATOM 3086 CB ARG A 503 19.289 29.972 -66.295 1.00 89.00 C
ANISOU 3086 CB ARG A 503 9436 16816 7562 2218 -1518 83 C
ATOM 3087 CG ARG A 503 18.265 31.073 -66.070 1.00 95.54 C
ANISOU 3087 CG ARG A 503 10068 17695 8538 2451 -1685 400 C
ATOM 3088 CD ARG A 503 18.823 32.497 -66.256 1.00103.97 C
ANISOU 3088 CD ARG A 503 11311 18601 9592 2718 -1573 970 C
ATOM 3089 NE ARG A 503 19.812 32.628 -67.329 1.00118.56 N
ANISOU 3089 NE ARG A 503 13389 20642 11017 2757 -1476 1167 N
ATOM 3090 CZ ARG A 503 21.127 32.726 -67.146 1.00123.35 C
ANISOU 3090 CZ ARG A 503 14217 20967 11685 2652 -1176 1275 C
ATOM 3091 NH1 ARG A 503 21.633 32.710 -65.921 1.00127.30 N
ANISOU 3091 NH1 ARG A 503 14754 20970 12645 2507 -974 1204 N
ATOM 3092 NH2 ARG A 503 21.935 32.843 -68.192 1.00123.49 N
ANISOU 3092 NH2 ARG A 503 14400 21237 11282 2690 -1079 1453 N
ATOM 3093 N LYS A 504 17.760 27.761 -67.941 1.00 89.19 N
ANISOU 3093 N LYS A 504 9210 17779 6898 1911 -2038 -823 N
ATOM 3094 CA LYS A 504 16.639 27.323 -68.766 1.00 92.20 C
ANISOU 3094 CA LYS A 504 9393 18592 7045 1825 -2329 -1063 C
ATOM 3095 C LYS A 504 15.990 26.064 -68.205 1.00 91.65 C
ANISOU 3095 C LYS A 504 9198 18454 7172 1453 -2404 -1613 C
ATOM 3096 O LYS A 504 14.757 25.960 -68.172 1.00 96.66 O
ANISOU 3096 O LYS A 504 9539 19266 7923 1341 -2600 -1732 O
ATOM 3097 CB LYS A 504 17.107 27.094 -70.204 1.00 92.44 C
ANISOU 3097 CB LYS A 504 9629 18896 6598 1863 -2331 -1090 C
ATOM 3098 N THR A 505 16.801 25.095 -67.764 1.00 90.84 N
ANISOU 3098 N THR A 505 9333 18040 7142 1246 -2214 -1937 N
ATOM 3099 CA THR A 505 16.243 23.874 -67.189 1.00 93.33 C
ANISOU 3099 CA THR A 505 9606 18174 7682 858 -2238 -2436 C
ATOM 3100 C THR A 505 15.511 24.160 -65.881 1.00 86.01 C
ANISOU 3100 C THR A 505 8438 16969 7273 763 -2195 -2343 C
ATOM 3101 O THR A 505 14.460 23.564 -65.612 1.00 82.02 O
ANISOU 3101 O THR A 505 7693 16581 6890 477 -2342 -2643 O
ATOM 3102 CB THR A 505 17.344 22.835 -66.981 1.00 94.94 C
ANISOU 3102 CB THR A 505 10196 17946 7933 715 -1974 -2725 C
ATOM 3103 OG1 THR A 505 18.211 22.828 -68.121 1.00100.44 O
ANISOU 3103 OG1 THR A 505 11113 18889 8161 898 -1938 -2714 O
ATOM 3104 CG2 THR A 505 16.734 21.451 -66.834 1.00 96.01 C
ANISOU 3104 CG2 THR A 505 10365 17980 8134 304 -2053 -3291 C
ATOM 3105 N PHE A 506 16.032 25.094 -65.074 1.00 82.01 N
ANISOU 3105 N PHE A 506 7980 16120 7059 982 -1990 -1936 N
ATOM 3106 CA PHE A 506 15.360 25.477 -63.835 1.00 82.38 C
ANISOU 3106 CA PHE A 506 7813 15925 7561 937 -1928 -1834 C
ATOM 3107 C PHE A 506 14.012 26.116 -64.128 1.00 91.45 C
ANISOU 3107 C PHE A 506 8528 17558 8661 1053 -2209 -1737 C
ATOM 3108 O PHE A 506 13.016 25.811 -63.464 1.00 89.38 O
ANISOU 3108 O PHE A 506 7977 17335 8648 851 -2260 -1920 O
ATOM 3109 CB PHE A 506 16.216 26.447 -63.013 1.00 75.58 C
ANISOU 3109 CB PHE A 506 7115 14633 6970 1169 -1675 -1428 C
ATOM 3110 CG PHE A 506 17.447 25.837 -62.396 1.00 73.74 C
ANISOU 3110 CG PHE A 506 7225 13907 6886 1052 -1397 -1518 C
ATOM 3111 CD1 PHE A 506 17.634 24.468 -62.359 1.00 72.17 C
ANISOU 3111 CD1 PHE A 506 7186 13567 6667 770 -1352 -1935 C
ATOM 3112 CD2 PHE A 506 18.419 26.653 -61.838 1.00 69.72 C
ANISOU 3112 CD2 PHE A 506 6879 13068 6545 1232 -1188 -1183 C
ATOM 3113 CE1 PHE A 506 18.775 23.925 -61.788 1.00 67.55 C
ANISOU 3113 CE1 PHE A 506 6908 12540 6218 730 -1110 -1991 C
ATOM 3114 CE2 PHE A 506 19.557 26.118 -61.263 1.00 64.49 C
ANISOU 3114 CE2 PHE A 506 6480 12011 6012 1152 -960 -1255 C
ATOM 3115 CZ PHE A 506 19.735 24.752 -61.238 1.00 64.93 C
ANISOU 3115 CZ PHE A 506 6682 11949 6039 930 -924 -1648 C
ATOM 3116 N LYS A 507 13.970 27.035 -65.101 1.00 98.18 N
ANISOU 3116 N LYS A 507 9320 18794 9192 1394 -2385 -1424 N
ATOM 3117 CA LYS A 507 12.706 27.678 -65.450 1.00103.00 C
ANISOU 3117 CA LYS A 507 9566 19787 9781 1558 -2617 -1283 C
ATOM 3118 C LYS A 507 11.707 26.688 -66.041 1.00110.79 C
ANISOU 3118 C LYS A 507 10358 21095 10644 1234 -2807 -1692 C
ATOM 3119 O LYS A 507 10.502 26.787 -65.761 1.00114.07 O
ANISOU 3119 O LYS A 507 10421 21673 11247 1179 -2909 -1737 O
ATOM 3120 CB LYS A 507 12.958 28.824 -66.430 1.00106.56 C
ANISOU 3120 CB LYS A 507 10143 20388 9957 1964 -2675 -819 C
ATOM 3121 CG LYS A 507 13.700 29.996 -65.813 1.00109.62 C
ANISOU 3121 CG LYS A 507 10692 20427 10532 2283 -2492 -358 C
ATOM 3122 CD LYS A 507 14.023 31.079 -66.830 1.00116.97 C
ANISOU 3122 CD LYS A 507 11812 21451 11181 2625 -2519 105 C
ATOM 3123 CE LYS A 507 14.783 32.226 -66.175 1.00114.27 C
ANISOU 3123 CE LYS A 507 11670 20688 11058 2883 -2313 553 C
ATOM 3124 NZ LYS A 507 15.175 33.284 -67.148 1.00118.05 N
ANISOU 3124 NZ LYS A 507 12385 21195 11275 3164 -2304 1021 N
ATOM 3125 N MET A 508 12.196 25.686 -66.784 1.00116.38 N
ANISOU 3125 N MET A 508 11295 21861 11062 997 -2830 -2014 N
ATOM 3126 CA MET A 508 11.318 24.643 -67.309 1.00123.18 C
ANISOU 3126 CA MET A 508 12022 22954 11829 635 -2993 -2438 C
ATOM 3127 C MET A 508 10.746 23.795 -66.180 1.00123.42 C
ANISOU 3127 C MET A 508 11893 22756 12245 222 -2911 -2776 C
ATOM 3128 O MET A 508 9.565 23.425 -66.211 1.00134.61 O
ANISOU 3128 O MET A 508 13004 24390 13753 -13 -3042 -2962 O
ATOM 3129 CB MET A 508 12.076 23.776 -68.320 1.00127.54 C
ANISOU 3129 CB MET A 508 12925 23529 12006 499 -2992 -2708 C
ATOM 3130 CG MET A 508 11.481 22.388 -68.549 1.00135.16 C
ANISOU 3130 CG MET A 508 13888 24504 12964 20 -3075 -3243 C
ATOM 3131 SD MET A 508 12.594 21.235 -69.374 1.00138.93 S
ANISOU 3131 SD MET A 508 14881 24785 13122 -136 -2969 -3609 S
ATOM 3132 CE MET A 508 11.696 19.698 -69.169 1.00141.90 C
ANISOU 3132 CE MET A 508 15234 25002 13678 -739 -3034 -4190 C
ATOM 3133 N LEU A 509 11.562 23.492 -65.167 1.00113.14 N
ANISOU 3133 N LEU A 509 10794 21023 11173 120 -2687 -2845 N
ATOM 3134 CA LEU A 509 11.084 22.653 -64.073 1.00107.37 C
ANISOU 3134 CA LEU A 509 9967 20025 10803 -301 -2573 -3150 C
ATOM 3135 C LEU A 509 10.112 23.421 -63.183 1.00105.41 C
ANISOU 3135 C LEU A 509 9296 19862 10891 -211 -2556 -2932 C
ATOM 3136 O LEU A 509 9.081 22.876 -62.769 1.00110.60 O
ANISOU 3136 O LEU A 509 9696 20578 11748 -546 -2559 -3145 O
ATOM 3137 CB LEU A 509 12.263 22.117 -63.262 1.00 99.74 C
ANISOU 3137 CB LEU A 509 9428 18457 10013 -400 -2281 -3225 C
ATOM 3138 CG LEU A 509 13.088 21.041 -63.974 1.00 98.50 C
ANISOU 3138 CG LEU A 509 9695 18143 9589 -565 -2252 -3562 C
ATOM 3139 CD1 LEU A 509 14.405 20.815 -63.255 1.00 92.71 C
ANISOU 3139 CD1 LEU A 509 9411 16762 9050 -472 -1912 -3454 C
ATOM 3140 CD2 LEU A 509 12.306 19.743 -64.110 1.00102.52 C
ANISOU 3140 CD2 LEU A 509 10196 18627 10130 -1076 -2324 -4040 C
ATOM 3141 N LEU A 510 10.435 24.680 -62.864 1.00 98.17 N
ANISOU 3141 N LEU A 510 8329 18921 10051 239 -2507 -2503 N
ATOM 3142 CA LEU A 510 9.586 25.485 -61.988 1.00 95.82 C
ANISOU 3142 CA LEU A 510 7688 18636 10084 394 -2444 -2285 C
ATOM 3143 C LEU A 510 8.234 25.765 -62.637 1.00105.73 C
ANISOU 3143 C LEU A 510 8577 20334 11260 454 -2650 -2257 C
ATOM 3144 O LEU A 510 7.184 25.551 -62.019 1.00111.16 O
ANISOU 3144 O LEU A 510 8938 21106 12189 255 -2616 -2383 O
ATOM 3145 CB LEU A 510 10.294 26.788 -61.611 1.00 89.56 C
ANISOU 3145 CB LEU A 510 7009 17640 9379 884 -2335 -1829 C
ATOM 3146 CG LEU A 510 11.523 26.657 -60.704 1.00 88.72 C
ANISOU 3146 CG LEU A 510 7376 16836 9497 821 -1980 -1752 C
ATOM 3147 CD1 LEU A 510 12.201 28.003 -60.494 1.00 86.96 C
ANISOU 3147 CD1 LEU A 510 7327 16367 9347 1266 -1862 -1287 C
ATOM 3148 CD2 LEU A 510 11.142 26.036 -59.366 1.00 86.47 C
ANISOU 3148 CD2 LEU A 510 7036 16233 9588 487 -1759 -1956 C
ATOM 3149 N LEU A 511 8.233 26.251 -63.885 1.00109.01 N
ANISOU 3149 N LEU A 511 9038 21053 11329 728 -2858 -2085 N
ATOM 3150 CA LEU A 511 6.966 26.477 -64.575 1.00119.35 C
ANISOU 3150 CA LEU A 511 9996 22817 12534 791 -3089 -2074 C
ATOM 3151 C LEU A 511 6.273 25.187 -65.004 1.00128.66 C
ANISOU 3151 C LEU A 511 11036 24229 13618 283 -3218 -2535 C
ATOM 3152 O LEU A 511 5.128 25.258 -65.467 1.00136.09 O
ANISOU 3152 O LEU A 511 11628 25574 14506 271 -3414 -2574 O
ATOM 3153 CB LEU A 511 7.167 27.382 -65.793 1.00121.37 C
ANISOU 3153 CB LEU A 511 10361 23319 12434 1227 -3274 -1740 C
ATOM 3154 CG LEU A 511 7.741 28.771 -65.522 1.00114.63 C
ANISOU 3154 CG LEU A 511 9667 22225 11662 1739 -3163 -1238 C
ATOM 3155 CD1 LEU A 511 7.883 29.551 -66.818 1.00115.37 C
ANISOU 3155 CD1 LEU A 511 9894 22563 11377 2101 -3342 -920 C
ATOM 3156 CD2 LEU A 511 6.834 29.510 -64.553 1.00111.91 C
ANISOU 3156 CD2 LEU A 511 9011 21811 11697 1925 -3090 -1087 C
ATOM 3157 N CYS A 512 6.938 24.032 -64.861 1.00132.12 N
ANISOU 3157 N CYS A 512 11756 24402 14042 -128 -3112 -2880 N
ATOM 3158 CA CYS A 512 6.420 22.717 -65.259 1.00137.87 C
ANISOU 3158 CA CYS A 512 12464 25226 14695 -651 -3202 -3336 C
ATOM 3159 C CYS A 512 6.072 22.690 -66.748 1.00144.59 C
ANISOU 3159 C CYS A 512 13279 26527 15130 -571 -3497 -3384 C
ATOM 3160 O CYS A 512 4.962 22.336 -67.149 1.00156.99 O
ANISOU 3160 O CYS A 512 14535 28448 16664 -784 -3684 -3564 O
ATOM 3161 CB CYS A 512 5.220 22.299 -64.401 1.00139.63 C
ANISOU 3161 CB CYS A 512 12302 25499 15253 -1004 -3145 -3507 C
ATOM 3162 SG CYS A 512 5.522 22.369 -62.625 1.00133.85 S
ANISOU 3162 SG CYS A 512 11593 24271 14992 -1101 -2781 -3435 S
ATOM 3163 N ARG A 513 7.046 23.070 -67.569 1.00139.70 N
ANISOU 3163 N ARG A 513 12983 25910 14185 -269 -3532 -3217 N
ATOM 3164 CA ARG A 513 6.896 23.039 -69.017 1.00140.33 C
ANISOU 3164 CA ARG A 513 13103 26390 13825 -181 -3785 -3252 C
ATOM 3165 C ARG A 513 7.303 21.679 -69.575 1.00143.55 C
ANISOU 3165 C ARG A 513 13824 26675 14043 -601 -3789 -3719 C
ATOM 3166 O ARG A 513 7.970 21.594 -70.606 1.00147.27 O
ANISOU 3166 O ARG A 513 14585 27238 14132 -477 -3851 -3734 O
ATOM 3167 CB ARG A 513 7.727 24.148 -69.666 1.00138.53 C
ANISOU 3167 CB ARG A 513 13089 26225 13322 347 -3790 -2813 C
TER 3168 ARG A 513
HETATM 3169 C1 OLA A1201 27.064 34.993 -53.700 1.00 94.69 C
HETATM 3170 O1 OLA A1201 27.624 34.200 -54.488 1.00 97.72 O
HETATM 3171 O2 OLA A1201 25.842 35.252 -53.762 1.00 98.82 O
HETATM 3172 C2 OLA A1201 27.907 35.657 -52.634 1.00 87.63 C
HETATM 3173 C3 OLA A1201 27.695 34.989 -51.279 1.00 84.26 C
HETATM 3174 C4 OLA A1201 26.445 35.504 -50.574 1.00 80.09 C
HETATM 3175 C5 OLA A1201 26.573 35.389 -49.062 1.00 79.04 C
HETATM 3176 C6 OLA A1201 25.202 35.490 -48.408 1.00 80.08 C
HETATM 3177 C7 OLA A1201 25.313 35.690 -46.902 1.00 82.11 C
HETATM 3178 C8 OLA A1201 23.942 35.550 -46.248 1.00 84.40 C
HETATM 3179 C9 OLA A1201 23.983 36.075 -44.834 1.00 83.84 C
HETATM 3180 C10 OLA A1201 23.013 36.876 -44.403 1.00 83.72 C
HETATM 3181 C1 OLA A1202 42.592 8.452 -34.214 1.00101.50 C
HETATM 3182 O1 OLA A1202 43.375 7.982 -33.363 1.00100.56 O
HETATM 3183 O2 OLA A1202 41.864 9.445 -33.994 1.00101.09 O
HETATM 3184 C2 OLA A1202 42.525 7.778 -35.565 1.00102.13 C
HETATM 3185 C3 OLA A1202 42.671 8.819 -36.668 1.00102.46 C
HETATM 3186 C4 OLA A1202 43.973 9.600 -36.571 1.00104.88 C
HETATM 3187 C5 OLA A1202 43.698 11.092 -36.709 1.00108.00 C
HETATM 3188 C6 OLA A1202 44.985 11.861 -36.979 1.00110.75 C
HETATM 3189 C7 OLA A1202 44.813 13.346 -36.680 1.00110.82 C
HETATM 3190 C8 OLA A1202 43.784 14.006 -37.593 1.00110.08 C
HETATM 3191 C9 OLA A1202 43.703 15.471 -37.230 1.00106.02 C
HETATM 3192 C10 OLA A1202 43.571 16.426 -38.148 1.00 99.74 C
HETATM 3193 C11 OLA A1202 43.469 16.118 -39.623 1.00 94.27 C
HETATM 3194 C12 OLA A1202 42.912 17.352 -40.325 1.00 93.05 C
HETATM 3195 C13 OLA A1202 42.545 17.069 -41.776 1.00 90.88 C
HETATM 3196 C14 OLA A1202 42.967 18.227 -42.673 1.00 89.24 C
HETATM 3197 C15 OLA A1202 42.258 18.165 -44.020 1.00 89.84 C
HETATM 3198 C16 OLA A1202 43.018 18.961 -45.074 1.00 91.78 C
HETATM 3199 C17 OLA A1202 42.152 19.197 -46.306 1.00 93.31 C
HETATM 3200 C18 OLA A1202 42.959 19.736 -47.468 1.00 92.89 C
HETATM 3201 C28 0HK A1203 36.420 25.486 -41.497 1.00 56.58 C
HETATM 3202 O29 0HK A1203 36.257 26.500 -42.114 1.00 56.97 O
HETATM 3203 C31 0HK A1203 38.221 24.573 -39.917 1.00 65.21 C
HETATM 3204 C32 0HK A1203 37.617 23.355 -42.023 1.00 58.31 C
HETATM 3205 C34 0HK A1203 37.546 24.127 -38.773 1.00 49.04 C
HETATM 3206 C35 0HK A1203 38.364 24.104 -37.632 1.00 57.73 C
HETATM 3207 C36 0HK A1203 39.615 24.517 -37.897 1.00 70.66 C
HETATM 3208 C41 0HK A1203 37.288 22.119 -41.468 1.00 37.65 C
HETATM 3209 C42 0HK A1203 37.244 21.085 -42.440 1.00 51.01 C
HETATM 3210 C43 0HK A1203 37.532 21.527 -43.682 1.00 60.94 C
HETATM 3211 O10 0HK A1203 33.169 21.366 -41.480 1.00 61.96 O
HETATM 3212 O11 0HK A1203 35.471 24.833 -40.820 1.00 58.30 O
HETATM 3213 O33 0HK A1203 38.744 25.461 -42.089 1.00 51.36 O
HETATM 3214 S37 0HK A1203 39.846 24.948 -39.520 1.00 75.99 S
HETATM 3215 S44 0HK A1203 37.866 23.204 -43.723 1.00 71.91 S
HETATM 3216 C1 0HK A1203 30.694 24.802 -40.971 1.00 55.05 C
HETATM 3217 C3 0HK A1203 32.580 23.365 -39.987 1.00 58.10 C
HETATM 3218 C4 0HK A1203 33.343 24.671 -39.671 1.00 57.95 C
HETATM 3219 C5 0HK A1203 34.088 25.314 -40.840 1.00 60.44 C
HETATM 3220 C6 0HK A1203 33.412 25.057 -42.185 1.00 60.10 C
HETATM 3221 C7 0HK A1203 32.645 23.727 -42.312 1.00 58.23 C
HETATM 3222 C8 0HK A1203 33.656 22.621 -42.001 1.00 60.73 C
HETATM 3223 C9 0HK A1203 33.610 22.391 -40.563 1.00 61.01 C
HETATM 3224 C12 0HK A1203 30.500 22.630 -41.356 1.00 40.48 C
HETATM 3225 C30 0HK A1203 37.763 24.731 -41.372 1.00 59.33 C
HETATM 3226 N2 0HK A1203 31.622 23.624 -41.160 1.00 56.65 N
HETATM 3227 O22 P33 A1204 37.705 26.244 -25.441 1.00117.91 O
HETATM 3228 C21 P33 A1204 37.411 27.085 -26.563 1.00119.98 C
HETATM 3229 C20 P33 A1204 38.134 26.570 -27.805 1.00120.50 C
HETATM 3230 O19 P33 A1204 37.665 27.281 -28.951 1.00119.35 O
HETATM 3231 C18 P33 A1204 38.131 26.717 -30.177 1.00117.97 C
HETATM 3232 C17 P33 A1204 37.184 27.125 -31.300 1.00115.90 C
HETATM 3233 O16 P33 A1204 35.848 26.997 -30.815 1.00115.01 O
HETATM 3234 C15 P33 A1204 34.863 27.066 -31.843 1.00110.40 C
HETATM 3235 C14 P33 A1204 33.483 27.124 -31.195 1.00105.91 C
HETATM 3236 O13 P33 A1204 32.483 26.772 -32.150 1.00101.74 O
HETATM 3237 C12 P33 A1204 31.166 26.911 -31.619 1.00 96.24 C
HETATM 3238 C11 P33 A1204 30.195 26.104 -32.472 1.00 94.70 C
HETATM 3239 O10 P33 A1204 30.584 24.731 -32.421 1.00 97.20 O
HETATM 3240 C9 P33 A1204 29.804 23.917 -33.291 1.00 89.83 C
HETATM 3241 C8 P33 A1204 30.417 22.529 -33.401 1.00 84.08 C
HETATM 3242 O7 P33 A1204 31.797 22.611 -33.059 1.00 85.47 O
HETATM 3243 C6 P33 A1204 32.619 21.971 -34.032 1.00 83.93 C
HETATM 3244 C5 P33 A1204 33.961 21.628 -33.403 1.00 86.00 C
HETATM 3245 O4 P33 A1204 34.436 22.708 -32.603 1.00 92.59 O
HETATM 3246 C3 P33 A1204 35.617 22.343 -31.890 1.00 98.25 C
HETATM 3247 C2 P33 A1204 36.164 23.542 -31.124 1.00103.85 C
HETATM 3248 O1 P33 A1204 35.180 24.028 -30.204 1.00107.46 O
HETATM 3249 C18 OLC A1205 31.001 8.932 -47.057 1.00 79.21 C
HETATM 3250 C10 OLC A1205 31.277 7.219 -54.822 1.00 81.27 C
HETATM 3251 C9 OLC A1205 31.677 7.855 -55.935 1.00 84.48 C
HETATM 3252 C17 OLC A1205 32.317 8.406 -47.588 1.00 75.04 C
HETATM 3253 C11 OLC A1205 32.230 7.084 -53.659 1.00 78.93 C
HETATM 3254 C8 OLC A1205 30.722 7.988 -57.097 1.00 85.25 C
HETATM 3255 C24 OLC A1205 26.283 9.319 -62.758 1.00117.99 C
HETATM 3256 C16 OLC A1205 32.130 7.874 -48.989 1.00 71.86 C
HETATM 3257 C12 OLC A1205 31.430 6.740 -52.424 1.00 77.55 C
HETATM 3258 C7 OLC A1205 31.330 8.911 -58.124 1.00 83.50 C
HETATM 3259 C15 OLC A1205 33.435 7.282 -49.474 1.00 73.74 C
HETATM 3260 C13 OLC A1205 32.344 6.137 -51.380 1.00 78.54 C
HETATM 3261 C6 OLC A1205 31.332 8.201 -59.453 1.00 85.10 C
HETATM 3262 C14 OLC A1205 33.402 7.143 -50.981 1.00 75.72 C
HETATM 3263 C5 OLC A1205 30.215 8.747 -60.316 1.00 87.52 C
HETATM 3264 C4 OLC A1205 30.625 10.111 -60.825 1.00 93.00 C
HETATM 3265 C3 OLC A1205 30.624 10.207 -62.340 1.00 95.65 C
HETATM 3266 C2 OLC A1205 31.055 8.929 -63.029 1.00 97.50 C
HETATM 3267 C21 OLC A1205 27.674 8.428 -64.624 1.00114.69 C
HETATM 3268 C1 OLC A1205 29.965 8.533 -63.998 1.00102.55 C
HETATM 3269 C22 OLC A1205 26.267 8.584 -64.082 1.00118.02 C
HETATM 3270 O19 OLC A1205 30.249 8.130 -65.108 1.00101.16 O
HETATM 3271 O25 OLC A1205 25.099 9.039 -62.046 1.00116.87 O
HETATM 3272 O23 OLC A1205 25.491 9.310 -65.007 1.00119.70 O
HETATM 3273 O20 OLC A1205 28.620 8.641 -63.600 1.00110.31 O
HETATM 3274 O HOH A1301 30.945 27.048 -53.984 1.00 56.58 O
HETATM 3275 O HOH A1302 28.503 24.690 -46.765 1.00 42.71 O
HETATM 3276 O HOH A1303 32.985 19.330 -69.749 1.00 70.48 O
HETATM 3277 O HOH A1304 32.063 31.923 -41.736 1.00 60.34 O
HETATM 3278 O HOH A1305 29.846 23.817 -44.545 1.00 58.64 O
HETATM 3279 O HOH A1306 49.768 19.049 -72.949 1.00 81.21 O
HETATM 3280 O HOH A1307 39.865 19.784 -78.140 1.00 70.97 O
CONECT 590 1226
CONECT 1226 590
CONECT 2815 2831
CONECT 2831 2815
CONECT 3169 3170 3171 3172
CONECT 3170 3169
CONECT 3171 3169
CONECT 3172 3169 3173
CONECT 3173 3172 3174
CONECT 3174 3173 3175
CONECT 3175 3174 3176
CONECT 3176 3175 3177
CONECT 3177 3176 3178
CONECT 3178 3177 3179
CONECT 3179 3178 3180
CONECT 3180 3179
CONECT 3181 3182 3183 3184
CONECT 3182 3181
CONECT 3183 3181
CONECT 3184 3181 3185
CONECT 3185 3184 3186
CONECT 3186 3185 3187
CONECT 3187 3186 3188
CONECT 3188 3187 3189
CONECT 3189 3188 3190
CONECT 3190 3189 3191
CONECT 3191 3190 3192
CONECT 3192 3191 3193
CONECT 3193 3192 3194
CONECT 3194 3193 3195
CONECT 3195 3194 3196
CONECT 3196 3195 3197
CONECT 3197 3196 3198
CONECT 3198 3197 3199
CONECT 3199 3198 3200
CONECT 3200 3199
CONECT 3201 3202 3212 3225
CONECT 3202 3201
CONECT 3203 3205 3214 3225
CONECT 3204 3208 3215 3225
CONECT 3205 3203 3206
CONECT 3206 3205 3207
CONECT 3207 3206 3214
CONECT 3208 3204 3209
CONECT 3209 3208 3210
CONECT 3210 3209 3215
CONECT 3211 3222 3223
CONECT 3212 3201 3219
CONECT 3213 3225
CONECT 3214 3203 3207
CONECT 3215 3204 3210
CONECT 3216 3226
CONECT 3217 3218 3223 3226
CONECT 3218 3217 3219
CONECT 3219 3212 3218 3220
CONECT 3220 3219 3221
CONECT 3221 3220 3222 3226
CONECT 3222 3211 3221 3223
CONECT 3223 3211 3217 3222
CONECT 3224 3226
CONECT 3225 3201 3203 3204 3213
CONECT 3226 3216 3217 3221 3224
CONECT 3227 3228
CONECT 3228 3227 3229
CONECT 3229 3228 3230
CONECT 3230 3229 3231
CONECT 3231 3230 3232
CONECT 3232 3231 3233
CONECT 3233 3232 3234
CONECT 3234 3233 3235
CONECT 3235 3234 3236
CONECT 3236 3235 3237
CONECT 3237 3236 3238
CONECT 3238 3237 3239
CONECT 3239 3238 3240
CONECT 3240 3239 3241
CONECT 3241 3240 3242
CONECT 3242 3241 3243
CONECT 3243 3242 3244
CONECT 3244 3243 3245
CONECT 3245 3244 3246
CONECT 3246 3245 3247
CONECT 3247 3246 3248
CONECT 3248 3247
CONECT 3249 3252
CONECT 3250 3251 3253
CONECT 3251 3250 3254
CONECT 3252 3249 3256
CONECT 3253 3250 3257
CONECT 3254 3251 3258
CONECT 3255 3269 3271
CONECT 3256 3252 3259
CONECT 3257 3253 3260
CONECT 3258 3254 3261
CONECT 3259 3256 3262
CONECT 3260 3257 3262
CONECT 3261 3258 3263
CONECT 3262 3259 3260
CONECT 3263 3261 3264
CONECT 3264 3263 3265
CONECT 3265 3264 3266
CONECT 3266 3265 3268
CONECT 3267 3269 3273
CONECT 3268 3266 3270 3273
CONECT 3269 3255 3267 3272
CONECT 3270 3268
CONECT 3271 3255
CONECT 3272 3269
CONECT 3273 3267 3268
MASTER 489 0 5 22 2 0 12 6 3279 1 109 37
END