HEADER MEMBRANE PROTEIN 30-OCT-20 7DDZ
TITLE THE CRYSTAL STRUCTURE OF HUMAN NEUROPEPTIDE Y Y2 RECEPTOR WITH JNJ-
TITLE 2 31020028
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN NEUROPEPTIDE Y Y2 RECEPTOR FUSION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LYSIS PROTEIN,LYSOZYME,MURAMIDASE,NPY2-R,NPY-Y2 RECEPTOR,Y2
COMPND 5 RECEPTOR;
COMPND 6 EC: 3.2.1.17;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE RB59, HOMO SAPIENS,
SOURCE 3 DESULFOVIBRIO VULGARIS STR. HILDENBOROUGH;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 697290, 9606, 882;
SOURCE 6 STRAIN: HILDENBOROUGH;
SOURCE 7 GENE: E, RB59_126, NPY2R, DVU_2680;
SOURCE 8 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PULTRABAC-1;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 326201
KEYWDS NEUROPEPTIDE Y Y2 RECEPTOR, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.TANG,S.HAN,Q.ZHAO,B.WU
REVDAT 2 17-FEB-21 7DDZ 1 JRNL
REVDAT 1 27-JAN-21 7DDZ 0
JRNL AUTH T.TANG,C.HARTIG,Q.CHEN,W.ZHAO,A.KAISER,X.ZHANG,H.ZHANG,H.QU,
JRNL AUTH 2 C.YI,L.MA,S.HAN,Q.ZHAO,A.G.BECK-SICKINGER,B.WU
JRNL TITL STRUCTURAL BASIS FOR LIGAND RECOGNITION OF THE NEUROPEPTIDE
JRNL TITL 2 Y Y 2 RECEPTOR.
JRNL REF NAT COMMUN V. 12 737 2021
JRNL REFN ESSN 2041-1723
JRNL PMID 33531491
JRNL DOI 10.1038/S41467-021-21030-9
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 21815
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.258
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.260
REMARK 3 FREE R VALUE TEST SET COUNT : 2020
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 2.9000 - 2.8000 0.84 0 0 0.3080 0.3790
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) : 0.393
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 3569
REMARK 3 ANGLE : 1.212 4864
REMARK 3 CHIRALITY : 0.061 564
REMARK 3 PLANARITY : 0.006 596
REMARK 3 DIHEDRAL : 23.166 1240
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9097 7.9181 24.4218
REMARK 3 T TENSOR
REMARK 3 T11: 0.3655 T22: 0.3640
REMARK 3 T33: 0.4661 T12: 0.0307
REMARK 3 T13: -0.0271 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 1.0203 L22: 1.1569
REMARK 3 L33: 6.5334 L12: 0.3041
REMARK 3 L13: -0.8281 L23: -0.8327
REMARK 3 S TENSOR
REMARK 3 S11: -0.0028 S12: -0.3696 S13: -0.0758
REMARK 3 S21: 0.3767 S22: -0.0691 S23: -0.0071
REMARK 3 S31: 0.1848 S32: -0.0851 S33: 0.0614
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 7DDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-20.
REMARK 100 THE DEPOSITION ID IS D_1300019212.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-18
REMARK 200 TEMPERATURE (KELVIN) : 80
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 : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21815
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: 5ZBQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.0-7.5, 250-350 MM
REMARK 280 (NH4)2SO4, AND 20-30% PEG500DME, OR 0.1 M MES, PH 6.0-6.5, 380-
REMARK 280 420 MM NH4 TARTRATE, AND 24-26% PEG500DME, LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293.15K
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 48.21000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.43150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 48.21000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.43150
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 TOTAL BURIED SURFACE AREA: 790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -162
REMARK 465 ALA A -161
REMARK 465 PRO A -160
REMARK 465 ASN A -159
REMARK 465 ILE A -158
REMARK 465 PHE A -157
REMARK 465 GLU A -156
REMARK 465 MET A -155
REMARK 465 LEU A -154
REMARK 465 ARG A -153
REMARK 465 ILE A -152
REMARK 465 ASP A -151
REMARK 465 GLU A -150
REMARK 465 GLY A -149
REMARK 465 LEU A -148
REMARK 465 ARG A -147
REMARK 465 LEU A -146
REMARK 465 LYS A -145
REMARK 465 ILE A -144
REMARK 465 TYR A -143
REMARK 465 LYS A -142
REMARK 465 ASP A -141
REMARK 465 THR A -140
REMARK 465 GLU A -139
REMARK 465 GLY A -138
REMARK 465 TYR A -137
REMARK 465 TYR A -136
REMARK 465 THR A -135
REMARK 465 ILE A -134
REMARK 465 GLY A -133
REMARK 465 ILE A -132
REMARK 465 GLY A -131
REMARK 465 HIS A -130
REMARK 465 LEU A -129
REMARK 465 LEU A -128
REMARK 465 THR A -127
REMARK 465 LYS A -126
REMARK 465 SER A -125
REMARK 465 PRO A -124
REMARK 465 SER A -123
REMARK 465 LEU A -122
REMARK 465 ASN A -121
REMARK 465 ALA A -120
REMARK 465 ALA A -119
REMARK 465 LYS A -118
REMARK 465 SER A -117
REMARK 465 GLU A -116
REMARK 465 LEU A -115
REMARK 465 ASP A -114
REMARK 465 LYS A -113
REMARK 465 ALA A -112
REMARK 465 ILE A -111
REMARK 465 GLY A -110
REMARK 465 ARG A -109
REMARK 465 ASN A -108
REMARK 465 THR A -107
REMARK 465 ASN A -106
REMARK 465 GLY A -105
REMARK 465 VAL A -104
REMARK 465 ILE A -103
REMARK 465 THR A -102
REMARK 465 LYS A -101
REMARK 465 ASP A -100
REMARK 465 GLU A -99
REMARK 465 ALA A -98
REMARK 465 GLU A -97
REMARK 465 LYS A -96
REMARK 465 LEU A -95
REMARK 465 PHE A -94
REMARK 465 ASN A -93
REMARK 465 GLN A -92
REMARK 465 ASP A -91
REMARK 465 VAL A -90
REMARK 465 ASP A -89
REMARK 465 ALA A -88
REMARK 465 ALA A -87
REMARK 465 VAL A -86
REMARK 465 ARG A -85
REMARK 465 GLY A -84
REMARK 465 ILE A -83
REMARK 465 LEU A -82
REMARK 465 ARG A -81
REMARK 465 ASN A -80
REMARK 465 ALA A -79
REMARK 465 LYS A -78
REMARK 465 LEU A -77
REMARK 465 LYS A -76
REMARK 465 PRO A -75
REMARK 465 VAL A -74
REMARK 465 TYR A -73
REMARK 465 ASP A -72
REMARK 465 SER A -71
REMARK 465 LEU A -70
REMARK 465 ASP A -69
REMARK 465 ALA A -68
REMARK 465 VAL A -67
REMARK 465 ARG A -66
REMARK 465 ARG A -65
REMARK 465 ALA A -64
REMARK 465 ALA A -63
REMARK 465 LEU A -62
REMARK 465 ILE A -61
REMARK 465 ASN A -60
REMARK 465 MET A -59
REMARK 465 VAL A -58
REMARK 465 PHE A -57
REMARK 465 GLN A -56
REMARK 465 MET A -55
REMARK 465 GLY A -54
REMARK 465 GLU A -53
REMARK 465 THR A -52
REMARK 465 GLY A -51
REMARK 465 VAL A -50
REMARK 465 ALA A -49
REMARK 465 GLY A -48
REMARK 465 PHE A -47
REMARK 465 THR A -46
REMARK 465 ASN A -45
REMARK 465 SER A -44
REMARK 465 LEU A -43
REMARK 465 ARG A -42
REMARK 465 MET A -41
REMARK 465 LEU A -40
REMARK 465 GLN A -39
REMARK 465 GLN A -38
REMARK 465 LYS A -37
REMARK 465 ARG A -36
REMARK 465 TRP A -35
REMARK 465 ASP A -34
REMARK 465 GLU A -33
REMARK 465 ALA A -32
REMARK 465 ALA A -31
REMARK 465 VAL A -30
REMARK 465 ASN A -29
REMARK 465 LEU A -28
REMARK 465 ALA A -27
REMARK 465 LYS A -26
REMARK 465 SER A -25
REMARK 465 ARG A -24
REMARK 465 TRP A -23
REMARK 465 TYR A -22
REMARK 465 ASN A -21
REMARK 465 GLN A -20
REMARK 465 THR A -19
REMARK 465 PRO A -18
REMARK 465 ASN A -17
REMARK 465 ARG A -16
REMARK 465 ALA A -15
REMARK 465 LYS A -14
REMARK 465 ARG A -13
REMARK 465 VAL A -12
REMARK 465 ILE A -11
REMARK 465 THR A -10
REMARK 465 THR A -9
REMARK 465 PHE A -8
REMARK 465 ARG A -7
REMARK 465 THR A -6
REMARK 465 GLY A -5
REMARK 465 THR A -4
REMARK 465 TRP A -3
REMARK 465 ASP A -2
REMARK 465 ALA A -1
REMARK 465 TYR A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 PRO A 3
REMARK 465 ILE A 4
REMARK 465 GLY A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 ASP A 9
REMARK 465 GLU A 10
REMARK 465 ASN A 11
REMARK 465 GLN A 12
REMARK 465 THR A 13
REMARK 465 VAL A 14
REMARK 465 GLU A 15
REMARK 465 GLU A 16
REMARK 465 MET A 17
REMARK 465 LYS A 18
REMARK 465 VAL A 19
REMARK 465 GLU A 20
REMARK 465 GLN A 21
REMARK 465 TYR A 22
REMARK 465 GLY A 23
REMARK 465 PRO A 24
REMARK 465 GLN A 25
REMARK 465 THR A 26
REMARK 465 THR A 27
REMARK 465 PRO A 28
REMARK 465 ARG A 29
REMARK 465 GLY A 30
REMARK 465 GLU A 31
REMARK 465 LEU A 32
REMARK 465 VAL A 33
REMARK 465 PRO A 34
REMARK 465 ASP A 35
REMARK 465 PRO A 36
REMARK 465 GLU A 37
REMARK 465 PRO A 38
REMARK 465 GLU A 39
REMARK 465 LEU A 40
REMARK 465 ILE A 41
REMARK 465 ASP A 42
REMARK 465 SER A 43
REMARK 465 THR A 44
REMARK 465 LYS A 45
REMARK 465 LEU A 46
REMARK 465 ILE A 47
REMARK 465 GLN A 344
REMARK 465 ARG A 345
REMARK 465 LEU A 346
REMARK 465 ASP A 347
REMARK 465 ALA A 348
REMARK 465 ILE A 349
REMARK 465 HIS A 350
REMARK 465 SER A 351
REMARK 465 GLU A 352
REMARK 465 VAL A 353
REMARK 465 GLU A 354
REMARK 465 PHE A 355
REMARK 465 LEU A 356
REMARK 465 GLU A 357
REMARK 465 VAL A 358
REMARK 465 LEU A 359
REMARK 465 PHE A 360
REMARK 465 GLN A 361
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 LYS A 117 CG CD CE NZ
REMARK 470 SER A 161 OG
REMARK 470 LYS A 304 CG CD CE NZ
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 186 32.53 -85.14
REMARK 500 PRO A 196 44.09 -74.79
REMARK 500 TYR A 228 -41.26 -136.75
REMARK 500 TRP A1058 -159.01 -139.25
REMARK 500 ASP A 299 34.19 -81.98
REMARK 500 PHE A 340 1.05 -68.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7DDZ A -159 0 UNP A0A097J809_BPT4
DBREF2 7DDZ A A0A097J809 2 161
DBREF 7DDZ A 1 250 UNP P49146 NPY2R_HUMAN 1 250
DBREF 7DDZ A 1001 1146 UNP P00323 FLAV_DESVH 3 148
DBREF 7DDZ A 257 353 UNP P49146 NPY2R_HUMAN 257 353
SEQADV 7DDZ GLY A -162 UNP A0A097J80 EXPRESSION TAG
SEQADV 7DDZ ALA A -161 UNP A0A097J80 EXPRESSION TAG
SEQADV 7DDZ PRO A -160 UNP A0A097J80 EXPRESSION TAG
SEQADV 7DDZ THR A -107 UNP A0A097J80 CYS 54 ENGINEERED MUTATION
SEQADV 7DDZ ALA A -64 UNP A0A097J80 CYS 97 ENGINEERED MUTATION
SEQADV 7DDZ TYR A 149 UNP P49146 HIS 149 ENGINEERED MUTATION
SEQADV 7DDZ ALA A 1000 UNP P49146 LINKER
SEQADV 7DDZ TRP A 1096 UNP P00323 TYR 98 ENGINEERED MUTATION
SEQADV 7DDZ CYS A 280 UNP P49146 SER 280 ENGINEERED MUTATION
SEQADV 7DDZ GLU A 354 UNP P49146 EXPRESSION TAG
SEQADV 7DDZ PHE A 355 UNP P49146 EXPRESSION TAG
SEQADV 7DDZ LEU A 356 UNP P49146 EXPRESSION TAG
SEQADV 7DDZ GLU A 357 UNP P49146 EXPRESSION TAG
SEQADV 7DDZ VAL A 358 UNP P49146 EXPRESSION TAG
SEQADV 7DDZ LEU A 359 UNP P49146 EXPRESSION TAG
SEQADV 7DDZ PHE A 360 UNP P49146 EXPRESSION TAG
SEQADV 7DDZ GLN A 361 UNP P49146 EXPRESSION TAG
SEQRES 1 A 665 GLY ALA PRO ASN ILE PHE GLU MET LEU ARG ILE ASP GLU
SEQRES 2 A 665 GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR
SEQRES 3 A 665 TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO
SEQRES 4 A 665 SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE
SEQRES 5 A 665 GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA
SEQRES 6 A 665 GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG
SEQRES 7 A 665 GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP
SEQRES 8 A 665 SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET
SEQRES 9 A 665 VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR
SEQRES 10 A 665 ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU
SEQRES 11 A 665 ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN
SEQRES 12 A 665 THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG
SEQRES 13 A 665 THR GLY THR TRP ASP ALA TYR MET GLY PRO ILE GLY ALA
SEQRES 14 A 665 GLU ALA ASP GLU ASN GLN THR VAL GLU GLU MET LYS VAL
SEQRES 15 A 665 GLU GLN TYR GLY PRO GLN THR THR PRO ARG GLY GLU LEU
SEQRES 16 A 665 VAL PRO ASP PRO GLU PRO GLU LEU ILE ASP SER THR LYS
SEQRES 17 A 665 LEU ILE GLU VAL GLN VAL VAL LEU ILE LEU ALA TYR CYS
SEQRES 18 A 665 SER ILE ILE LEU LEU GLY VAL ILE GLY ASN SER LEU VAL
SEQRES 19 A 665 ILE HIS VAL VAL ILE LYS PHE LYS SER MET ARG THR VAL
SEQRES 20 A 665 THR ASN PHE PHE ILE ALA ASN LEU ALA VAL ALA ASP LEU
SEQRES 21 A 665 LEU VAL ASN THR LEU CYS LEU PRO PHE THR LEU THR TYR
SEQRES 22 A 665 THR LEU MET GLY GLU TRP LYS MET GLY PRO VAL LEU CYS
SEQRES 23 A 665 HIS LEU VAL PRO TYR ALA GLN GLY LEU ALA VAL GLN VAL
SEQRES 24 A 665 SER THR ILE THR LEU THR VAL ILE ALA LEU ASP ARG TYR
SEQRES 25 A 665 ARG CYS ILE VAL TYR HIS LEU GLU SER LYS ILE SER LYS
SEQRES 26 A 665 ARG ILE SER PHE LEU ILE ILE GLY LEU ALA TRP GLY ILE
SEQRES 27 A 665 SER ALA LEU LEU ALA SER PRO LEU ALA ILE PHE ARG GLU
SEQRES 28 A 665 TYR SER LEU ILE GLU ILE ILE PRO ASP PHE GLU ILE VAL
SEQRES 29 A 665 ALA CYS THR GLU LYS TRP PRO GLY GLU GLU LYS SER ILE
SEQRES 30 A 665 TYR GLY THR VAL TYR SER LEU SER SER LEU LEU ILE LEU
SEQRES 31 A 665 TYR VAL LEU PRO LEU GLY ILE ILE SER PHE SER TYR THR
SEQRES 32 A 665 ARG ILE TRP SER LYS LEU LYS ASN HIS VAL ALA LYS ALA
SEQRES 33 A 665 LEU ILE VAL TYR GLY SER THR THR GLY ASN THR GLU TYR
SEQRES 34 A 665 THR ALA GLU THR ILE ALA ARG GLU LEU ALA ASP ALA GLY
SEQRES 35 A 665 TYR GLU VAL ASP SER ARG ASP ALA ALA SER VAL GLU ALA
SEQRES 36 A 665 GLY GLY LEU PHE GLU GLY PHE ASP LEU VAL LEU LEU GLY
SEQRES 37 A 665 CYS SER THR TRP GLY ASP ASP SER ILE GLU LEU GLN ASP
SEQRES 38 A 665 ASP PHE ILE PRO LEU PHE ASP SER LEU GLU GLU THR GLY
SEQRES 39 A 665 ALA GLN GLY ARG LYS VAL ALA CYS PHE GLY CYS GLY ASP
SEQRES 40 A 665 SER SER TRP GLU TYR PHE CYS GLY ALA VAL ASP ALA ILE
SEQRES 41 A 665 GLU GLU LYS LEU LYS ASN LEU GLY ALA GLU ILE VAL GLN
SEQRES 42 A 665 ASP GLY LEU ARG ILE ASP GLY ASP PRO ARG ALA ALA ARG
SEQRES 43 A 665 ASP ASP ILE VAL GLY TRP ALA HIS ASP VAL ARG GLY ALA
SEQRES 44 A 665 ILE ASP HIS TYR HIS GLN ARG ARG GLN LYS THR THR LYS
SEQRES 45 A 665 MET LEU VAL CYS VAL VAL VAL VAL PHE ALA VAL CYS TRP
SEQRES 46 A 665 LEU PRO LEU HIS ALA PHE GLN LEU ALA VAL ASP ILE ASP
SEQRES 47 A 665 SER GLN VAL LEU ASP LEU LYS GLU TYR LYS LEU ILE PHE
SEQRES 48 A 665 THR VAL PHE HIS ILE ILE ALA MET CYS SER THR PHE ALA
SEQRES 49 A 665 ASN PRO LEU LEU TYR GLY TRP MET ASN SER ASN TYR ARG
SEQRES 50 A 665 LYS ALA PHE LEU SER ALA PHE ARG CYS GLU GLN ARG LEU
SEQRES 51 A 665 ASP ALA ILE HIS SER GLU VAL GLU PHE LEU GLU VAL LEU
SEQRES 52 A 665 PHE GLN
HET H46 A1201 42
HET FMN A1202 31
HETNAM H46 ~{N}-[4-[4-[(1~{S})-2-(DIETHYLAMINO)-2-OXIDANYLIDENE-1-
HETNAM 2 H46 PHENYL-ETHYL]PIPERAZIN-1-YL]-3-FLUORANYL-PHENYL]-2-
HETNAM 3 H46 PYRIDIN-3-YL-BENZAMIDE
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 H46 C34 H36 F N5 O2
FORMUL 3 FMN C17 H21 N4 O9 P
HELIX 1 AA1 GLU A 48 PHE A 78 1 31
HELIX 2 AA2 THR A 83 THR A 101 1 19
HELIX 3 AA3 LEU A 102 MET A 113 1 12
HELIX 4 AA4 GLY A 119 TYR A 154 1 36
HELIX 5 AA5 ARG A 163 ALA A 180 1 18
HELIX 6 AA6 SER A 181 PHE A 186 1 6
HELIX 7 AA7 SER A 213 LEU A 227 1 15
HELIX 8 AA8 TYR A 228 ASN A 248 1 21
HELIX 9 AA9 GLY A 1011 ALA A 1027 1 17
HELIX 10 AB1 ALA A 1037 VAL A 1039 5 3
HELIX 11 AB2 PHE A 1069 SER A 1075 1 7
HELIX 12 AB3 LEU A 1076 THR A 1079 5 4
HELIX 13 AB4 CYS A 1100 LEU A 1113 1 14
HELIX 14 AB5 ASP A 1127 ALA A 1130 5 4
HELIX 15 AB6 ALA A 1131 VAL A 291 1 51
HELIX 16 AB7 ASP A 299 ASN A 329 1 31
HELIX 17 AB8 ASN A 329 PHE A 340 1 12
SHEET 1 AA1 2 ARG A 187 LEU A 191 0
SHEET 2 AA1 2 VAL A 201 GLU A 205 -1 O THR A 204 N GLU A 188
SHEET 1 AA2 5 GLU A1030 ASP A1035 0
SHEET 2 AA2 5 LYS A1001 GLY A1007 1 N ILE A1004 O ASP A1032
SHEET 3 AA2 5 LEU A1050 CYS A1055 1 O LEU A1052 N LEU A1003
SHEET 4 AA2 5 LYS A1085 GLY A1092 1 O ALA A1087 N LEU A1053
SHEET 5 AA2 5 GLU A1116 ILE A1117 1 O GLU A1116 N VAL A1086
SHEET 1 AA3 5 GLU A1030 ASP A1035 0
SHEET 2 AA3 5 LYS A1001 GLY A1007 1 N ILE A1004 O ASP A1032
SHEET 3 AA3 5 LEU A1050 CYS A1055 1 O LEU A1052 N LEU A1003
SHEET 4 AA3 5 LYS A1085 GLY A1092 1 O ALA A1087 N LEU A1053
SHEET 5 AA3 5 LEU A1122 ASP A1125 1 O LEU A1122 N CYS A1088
SHEET 1 AA4 2 THR A1057 TRP A1058 0
SHEET 2 AA4 2 GLU A1064 LEU A1065 -1 O GLU A1064 N TRP A1058
SSBOND 1 CYS A 123 CYS A 203 1555 1555 2.04
CRYST1 96.420 50.863 184.629 90.00 90.67 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 0.010371 0.000000 0.000121 0.00000
SCALE2 0.000000 0.019661 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005417 0.00000
ATOM 1 N GLU A 48 -32.004 -15.932 56.682 1.00118.37 N
ANISOU 1 N GLU A 48 21330 14325 9320 -4486 2011 2769 N
ATOM 2 CA GLU A 48 -30.868 -15.230 57.276 1.00121.44 C
ANISOU 2 CA GLU A 48 21682 14741 9720 -4000 1903 2853 C
ATOM 3 C GLU A 48 -30.471 -14.006 56.443 1.00118.52 C
ANISOU 3 C GLU A 48 20925 14565 9544 -3782 1826 2755 C
ATOM 4 O GLU A 48 -30.015 -14.135 55.308 1.00114.48 O
ANISOU 4 O GLU A 48 20479 13821 9199 -3671 1772 2731 O
ATOM 5 CB GLU A 48 -29.676 -16.178 57.425 1.00123.97 C
ANISOU 5 CB GLU A 48 22512 14585 10007 -3645 1819 3014 C
ATOM 6 CG GLU A 48 -28.599 -15.688 58.379 1.00121.12 C
ANISOU 6 CG GLU A 48 22147 14300 9574 -3194 1704 3135 C
ATOM 7 CD GLU A 48 -28.922 -16.024 59.815 1.00122.10 C
ANISOU 7 CD GLU A 48 22401 14530 9463 -3298 1758 3225 C
ATOM 8 OE1 GLU A 48 -29.716 -16.964 60.028 1.00122.63 O
ANISOU 8 OE1 GLU A 48 22711 14462 9420 -3646 1873 3235 O
ATOM 9 OE2 GLU A 48 -28.391 -15.351 60.725 1.00124.04 O
ANISOU 9 OE2 GLU A 48 22513 14998 9620 -3050 1681 3277 O
ATOM 10 N VAL A 49 -30.639 -12.815 57.023 1.00118.08 N
ANISOU 10 N VAL A 49 20485 14927 9453 -3715 1825 2692 N
ATOM 11 CA VAL A 49 -30.432 -11.581 56.268 1.00112.82 C
ANISOU 11 CA VAL A 49 19440 14484 8944 -3563 1773 2573 C
ATOM 12 C VAL A 49 -28.949 -11.323 56.026 1.00112.52 C
ANISOU 12 C VAL A 49 19548 14218 8985 -3099 1600 2646 C
ATOM 13 O VAL A 49 -28.572 -10.772 54.983 1.00113.19 O
ANISOU 13 O VAL A 49 19368 14284 9354 -2905 1505 2524 O
ATOM 14 CB VAL A 49 -31.121 -10.407 56.994 1.00109.39 C
ANISOU 14 CB VAL A 49 18580 14563 8419 -3627 1844 2462 C
ATOM 15 CG1 VAL A 49 -30.606 -9.059 56.498 1.00102.86 C
ANISOU 15 CG1 VAL A 49 17325 13910 7848 -3273 1721 2292 C
ATOM 16 CG2 VAL A 49 -32.637 -10.501 56.815 1.00108.18 C
ANISOU 16 CG2 VAL A 49 18147 14708 8247 -4048 2008 2369 C
ATOM 17 N GLN A 50 -28.081 -11.741 56.950 1.00113.70 N
ANISOU 17 N GLN A 50 19981 14214 9006 -2834 1515 2793 N
ATOM 18 CA GLN A 50 -26.655 -11.473 56.790 1.00111.53 C
ANISOU 18 CA GLN A 50 19732 13810 8835 -2346 1321 2849 C
ATOM 19 C GLN A 50 -26.078 -12.188 55.570 1.00115.29 C
ANISOU 19 C GLN A 50 20449 13897 9459 -2204 1285 2908 C
ATOM 20 O GLN A 50 -25.265 -11.612 54.838 1.00117.80 O
ANISOU 20 O GLN A 50 20516 14220 10023 -1879 1142 2831 O
ATOM 21 CB GLN A 50 -25.902 -11.864 58.058 1.00114.88 C
ANISOU 21 CB GLN A 50 20436 14195 9019 -2120 1250 3035 C
ATOM 22 CG GLN A 50 -25.855 -10.753 59.097 1.00114.26 C
ANISOU 22 CG GLN A 50 20028 14519 8868 -2046 1186 2946 C
ATOM 23 CD GLN A 50 -24.982 -11.104 60.282 1.00115.22 C
ANISOU 23 CD GLN A 50 20417 14626 8736 -1803 1088 3142 C
ATOM 24 OE1 GLN A 50 -25.161 -12.147 60.915 1.00114.75 O
ANISOU 24 OE1 GLN A 50 20648 14396 8555 -1864 1154 3271 O
ATOM 25 NE2 GLN A 50 -24.023 -10.233 60.585 1.00114.46 N
ANISOU 25 NE2 GLN A 50 20048 14740 8703 -1480 897 3093 N
ATOM 26 N VAL A 51 -26.497 -13.429 55.317 1.00114.45 N
ANISOU 26 N VAL A 51 20689 13475 9322 -2400 1388 2966 N
ATOM 27 CA VAL A 51 -25.959 -14.161 54.170 1.00111.90 C
ANISOU 27 CA VAL A 51 20604 12765 9149 -2244 1363 2992 C
ATOM 28 C VAL A 51 -26.578 -13.683 52.849 1.00109.27 C
ANISOU 28 C VAL A 51 20025 12487 9005 -2484 1408 2830 C
ATOM 29 O VAL A 51 -25.900 -13.669 51.813 1.00109.88 O
ANISOU 29 O VAL A 51 20131 12372 9245 -2251 1340 2822 O
ATOM 30 CB VAL A 51 -26.139 -15.679 54.382 1.00117.35 C
ANISOU 30 CB VAL A 51 21780 13077 9732 -2350 1450 3079 C
ATOM 31 CG1 VAL A 51 -27.579 -16.016 54.674 1.00118.71 C
ANISOU 31 CG1 VAL A 51 21945 13358 9800 -2915 1601 2993 C
ATOM 32 CG2 VAL A 51 -25.641 -16.477 53.183 1.00115.58 C
ANISOU 32 CG2 VAL A 51 21834 12440 9640 -2197 1445 3077 C
ATOM 33 N VAL A 52 -27.853 -13.279 52.851 1.00107.32 N
ANISOU 33 N VAL A 52 19506 12534 8738 -2928 1520 2702 N
ATOM 34 CA VAL A 52 -28.472 -12.748 51.638 1.00102.63 C
ANISOU 34 CA VAL A 52 18615 12068 8311 -3148 1558 2553 C
ATOM 35 C VAL A 52 -27.787 -11.458 51.203 1.00104.78 C
ANISOU 35 C VAL A 52 18389 12552 8872 -2753 1400 2413 C
ATOM 36 O VAL A 52 -27.736 -11.158 50.003 1.00105.63 O
ANISOU 36 O VAL A 52 18298 12623 9213 -2710 1361 2301 O
ATOM 37 CB VAL A 52 -29.991 -12.584 51.868 1.00100.42 C
ANISOU 37 CB VAL A 52 18050 12151 7955 -3643 1696 2444 C
ATOM 38 CG1 VAL A 52 -30.630 -11.623 50.886 1.00 97.12 C
ANISOU 38 CG1 VAL A 52 17146 12054 7701 -3783 1718 2282 C
ATOM 39 CG2 VAL A 52 -30.677 -13.935 51.764 1.00105.36 C
ANISOU 39 CG2 VAL A 52 19001 12534 8497 -3996 1781 2457 C
ATOM 40 N LEU A 53 -27.207 -10.709 52.141 1.00107.52 N
ANISOU 40 N LEU A 53 18538 13103 9210 -2460 1299 2410 N
ATOM 41 CA LEU A 53 -26.383 -9.554 51.801 1.00107.03 C
ANISOU 41 CA LEU A 53 18067 13197 9402 -2078 1131 2284 C
ATOM 42 C LEU A 53 -24.903 -9.902 51.639 1.00102.27 C
ANISOU 42 C LEU A 53 17670 12340 8849 -1641 978 2409 C
ATOM 43 O LEU A 53 -24.155 -9.092 51.080 1.00 96.83 O
ANISOU 43 O LEU A 53 16673 11738 8381 -1359 839 2314 O
ATOM 44 CB LEU A 53 -26.555 -8.453 52.859 1.00107.01 C
ANISOU 44 CB LEU A 53 17736 13578 9345 -2026 1104 2191 C
ATOM 45 CG LEU A 53 -28.006 -8.098 53.224 1.00105.09 C
ANISOU 45 CG LEU A 53 17282 13647 8999 -2397 1274 2093 C
ATOM 46 CD1 LEU A 53 -28.034 -6.958 54.230 1.00102.13 C
ANISOU 46 CD1 LEU A 53 16627 13609 8568 -2269 1248 1993 C
ATOM 47 CD2 LEU A 53 -28.882 -7.780 51.998 1.00101.32 C
ANISOU 47 CD2 LEU A 53 16512 13278 8707 -2597 1348 1949 C
ATOM 48 N ILE A 54 -24.469 -11.082 52.104 1.00100.20 N
ANISOU 48 N ILE A 54 17922 11781 8369 -1570 1006 2628 N
ATOM 49 CA ILE A 54 -23.106 -11.553 51.835 1.00 97.95 C
ANISOU 49 CA ILE A 54 17853 11258 8105 -1119 885 2775 C
ATOM 50 C ILE A 54 -22.874 -11.673 50.332 1.00 98.37 C
ANISOU 50 C ILE A 54 17878 11104 8396 -1038 876 2705 C
ATOM 51 O ILE A 54 -21.930 -11.092 49.784 1.00104.15 O
ANISOU 51 O ILE A 54 18344 11910 9319 -694 734 2662 O
ATOM 52 CB ILE A 54 -22.836 -12.894 52.546 1.00100.69 C
ANISOU 52 CB ILE A 54 18827 11286 8143 -1057 956 3037 C
ATOM 53 CG1 ILE A 54 -22.437 -12.684 54.008 1.00 98.64 C
ANISOU 53 CG1 ILE A 54 18559 11248 7670 -910 883 3149 C
ATOM 54 CG2 ILE A 54 -21.726 -13.672 51.842 1.00101.03 C
ANISOU 54 CG2 ILE A 54 19185 10988 8214 -638 906 3186 C
ATOM 55 CD1 ILE A 54 -20.959 -12.364 54.205 1.00 97.46 C
ANISOU 55 CD1 ILE A 54 18268 11215 7548 -375 679 3248 C
ATOM 56 N LEU A 55 -23.734 -12.429 49.641 1.00 95.67 N
ANISOU 56 N LEU A 55 17813 10514 8025 -1382 1029 2690 N
ATOM 57 CA LEU A 55 -23.534 -12.711 48.223 1.00 96.68 C
ANISOU 57 CA LEU A 55 18007 10395 8332 -1330 1037 2639 C
ATOM 58 C LEU A 55 -24.181 -11.683 47.299 1.00 94.51 C
ANISOU 58 C LEU A 55 17204 10379 8327 -1523 1020 2398 C
ATOM 59 O LEU A 55 -23.895 -11.684 46.093 1.00 89.04 O
ANISOU 59 O LEU A 55 16469 9545 7819 -1430 995 2334 O
ATOM 60 CB LEU A 55 -24.042 -14.119 47.887 1.00 97.48 C
ANISOU 60 CB LEU A 55 18734 10062 8243 -1604 1205 2743 C
ATOM 61 CG LEU A 55 -25.460 -14.509 48.287 1.00 97.38 C
ANISOU 61 CG LEU A 55 18759 10132 8108 -2175 1346 2666 C
ATOM 62 CD1 LEU A 55 -26.450 -14.093 47.208 1.00 96.21 C
ANISOU 62 CD1 LEU A 55 18351 10120 8085 -2582 1409 2497 C
ATOM 63 CD2 LEU A 55 -25.529 -16.007 48.562 1.00 99.73 C
ANISOU 63 CD2 LEU A 55 19566 10056 8270 -2238 1424 2727 C
ATOM 64 N ALA A 56 -25.039 -10.805 47.825 1.00 97.17 N
ANISOU 64 N ALA A 56 17151 11094 8676 -1762 1040 2270 N
ATOM 65 CA ALA A 56 -25.496 -9.675 47.026 1.00 92.78 C
ANISOU 65 CA ALA A 56 16067 10813 8371 -1827 1007 2057 C
ATOM 66 C ALA A 56 -24.371 -8.666 46.821 1.00 91.14 C
ANISOU 66 C ALA A 56 15526 10726 8376 -1395 828 1989 C
ATOM 67 O ALA A 56 -24.253 -8.068 45.748 1.00 86.73 O
ANISOU 67 O ALA A 56 14696 10203 8053 -1322 776 1862 O
ATOM 68 CB ALA A 56 -26.709 -9.017 47.683 1.00 88.83 C
ANISOU 68 CB ALA A 56 15266 10693 7794 -2141 1097 1955 C
ATOM 69 N TYR A 57 -23.516 -8.483 47.825 1.00 94.28 N
ANISOU 69 N TYR A 57 15949 11199 8676 -1125 728 2080 N
ATOM 70 CA TYR A 57 -22.461 -7.484 47.724 1.00 94.23 C
ANISOU 70 CA TYR A 57 15615 11360 8827 -782 554 2016 C
ATOM 71 C TYR A 57 -21.206 -7.993 47.034 1.00 95.76 C
ANISOU 71 C TYR A 57 15951 11339 9095 -427 455 2129 C
ATOM 72 O TYR A 57 -20.470 -7.189 46.457 1.00 97.42 O
ANISOU 72 O TYR A 57 15852 11673 9491 -215 330 2046 O
ATOM 73 CB TYR A 57 -22.085 -6.950 49.109 1.00 94.44 C
ANISOU 73 CB TYR A 57 15558 11631 8693 -681 476 2051 C
ATOM 74 CG TYR A 57 -22.768 -5.649 49.461 1.00 93.27 C
ANISOU 74 CG TYR A 57 15034 11804 8599 -829 486 1853 C
ATOM 75 CD1 TYR A 57 -22.481 -4.474 48.770 1.00 95.01 C
ANISOU 75 CD1 TYR A 57 14892 12166 9041 -722 398 1681 C
ATOM 76 CD2 TYR A 57 -23.698 -5.591 50.482 1.00 91.46 C
ANISOU 76 CD2 TYR A 57 14840 11729 8181 -1062 598 1841 C
ATOM 77 CE1 TYR A 57 -23.108 -3.278 49.097 1.00 95.89 C
ANISOU 77 CE1 TYR A 57 14726 12533 9176 -820 427 1503 C
ATOM 78 CE2 TYR A 57 -24.324 -4.402 50.817 1.00 93.08 C
ANISOU 78 CE2 TYR A 57 14734 12220 8411 -1146 629 1664 C
ATOM 79 CZ TYR A 57 -24.026 -3.254 50.126 1.00 95.59 C
ANISOU 79 CZ TYR A 57 14735 12642 8941 -1013 547 1497 C
ATOM 80 OH TYR A 57 -24.654 -2.084 50.470 1.00 93.67 O
ANISOU 80 OH TYR A 57 14250 12645 8695 -1064 598 1327 O
ATOM 81 N CYS A 58 -20.925 -9.291 47.071 1.00 96.76 N
ANISOU 81 N CYS A 58 16551 11150 9065 -342 517 2321 N
ATOM 82 CA CYS A 58 -19.688 -9.750 46.452 1.00 97.51 C
ANISOU 82 CA CYS A 58 16772 11071 9205 67 436 2442 C
ATOM 83 C CYS A 58 -19.857 -10.157 44.992 1.00 96.84 C
ANISOU 83 C CYS A 58 16794 10717 9284 25 507 2381 C
ATOM 84 O CYS A 58 -18.941 -9.929 44.191 1.00 95.09 O
ANISOU 84 O CYS A 58 16423 10493 9212 331 417 2376 O
ATOM 85 CB CYS A 58 -19.082 -10.901 47.257 1.00 98.25 C
ANISOU 85 CB CYS A 58 17347 10962 9022 304 459 2705 C
ATOM 86 SG CYS A 58 -20.201 -12.245 47.546 1.00105.27 S
ANISOU 86 SG CYS A 58 18864 11463 9669 -63 681 2804 S
ATOM 87 N SER A 59 -20.997 -10.745 44.606 1.00 95.16 N
ANISOU 87 N SER A 59 16825 10302 9030 -367 664 2333 N
ATOM 88 CA SER A 59 -21.219 -10.961 43.179 1.00 88.75 C
ANISOU 88 CA SER A 59 16055 9288 8378 -455 717 2242 C
ATOM 89 C SER A 59 -21.183 -9.637 42.425 1.00 83.31 C
ANISOU 89 C SER A 59 14785 8891 7979 -429 613 2041 C
ATOM 90 O SER A 59 -20.702 -9.589 41.287 1.00 83.33 O
ANISOU 90 O SER A 59 14729 8786 8147 -272 581 1996 O
ATOM 91 CB SER A 59 -22.532 -11.721 42.925 1.00 86.35 C
ANISOU 91 CB SER A 59 16064 8792 7954 -962 893 2213 C
ATOM 92 OG SER A 59 -23.688 -11.026 43.356 1.00 83.04 O
ANISOU 92 OG SER A 59 15314 8698 7539 -1347 929 2085 O
ATOM 93 N ILE A 60 -21.638 -8.547 43.055 1.00 77.70 N
ANISOU 93 N ILE A 60 13671 8537 7316 -554 565 1923 N
ATOM 94 CA ILE A 60 -21.377 -7.218 42.507 1.00 83.27 C
ANISOU 94 CA ILE A 60 13876 9502 8262 -449 453 1755 C
ATOM 95 C ILE A 60 -19.878 -6.984 42.396 1.00 83.56 C
ANISOU 95 C ILE A 60 13822 9565 8362 -20 302 1827 C
ATOM 96 O ILE A 60 -19.381 -6.485 41.376 1.00 75.59 O
ANISOU 96 O ILE A 60 12594 8576 7551 117 235 1746 O
ATOM 97 CB ILE A 60 -22.030 -6.124 43.371 1.00 82.78 C
ANISOU 97 CB ILE A 60 13486 9782 8183 -605 442 1635 C
ATOM 98 CG1 ILE A 60 -23.545 -6.247 43.384 1.00 81.08 C
ANISOU 98 CG1 ILE A 60 13267 9632 7908 -1012 596 1562 C
ATOM 99 CG2 ILE A 60 -21.654 -4.746 42.850 1.00 80.30 C
ANISOU 99 CG2 ILE A 60 12738 9687 8087 -472 331 1472 C
ATOM 100 CD1 ILE A 60 -24.199 -5.075 44.087 1.00 77.74 C
ANISOU 100 CD1 ILE A 60 12497 9560 7479 -1102 604 1433 C
ATOM 101 N ILE A 61 -19.138 -7.311 43.461 1.00 85.38 N
ANISOU 101 N ILE A 61 14194 9839 8408 191 242 1986 N
ATOM 102 CA ILE A 61 -17.699 -7.068 43.467 1.00 82.45 C
ANISOU 102 CA ILE A 61 13684 9591 8054 590 88 2076 C
ATOM 103 C ILE A 61 -17.040 -7.852 42.347 1.00 80.72 C
ANISOU 103 C ILE A 61 13656 9113 7901 843 112 2162 C
ATOM 104 O ILE A 61 -16.236 -7.311 41.584 1.00 78.04 O
ANISOU 104 O ILE A 61 13047 8888 7716 1049 15 2120 O
ATOM 105 CB ILE A 61 -17.089 -7.414 44.843 1.00 85.19 C
ANISOU 105 CB ILE A 61 14171 10052 8146 766 27 2260 C
ATOM 106 CG1 ILE A 61 -17.505 -6.385 45.887 1.00 87.18 C
ANISOU 106 CG1 ILE A 61 14162 10615 8347 562 -27 2148 C
ATOM 107 CG2 ILE A 61 -15.572 -7.436 44.785 1.00 74.14 C
ANISOU 107 CG2 ILE A 61 12662 8793 6713 1203 -120 2403 C
ATOM 108 CD1 ILE A 61 -17.230 -6.797 47.305 1.00 87.31 C
ANISOU 108 CD1 ILE A 61 14363 10723 8086 637 -56 2314 C
ATOM 109 N LEU A 62 -17.416 -9.127 42.203 1.00 81.42 N
ANISOU 109 N LEU A 62 14238 8837 7860 807 254 2277 N
ATOM 110 CA LEU A 62 -16.799 -10.010 41.218 1.00 80.81 C
ANISOU 110 CA LEU A 62 14453 8458 7794 1076 306 2375 C
ATOM 111 C LEU A 62 -17.285 -9.720 39.793 1.00 81.22 C
ANISOU 111 C LEU A 62 14380 8404 8077 892 352 2195 C
ATOM 112 O LEU A 62 -16.469 -9.574 38.875 1.00 81.86 O
ANISOU 112 O LEU A 62 14333 8483 8286 1163 301 2190 O
ATOM 113 CB LEU A 62 -17.069 -11.468 41.594 1.00 84.74 C
ANISOU 113 CB LEU A 62 15606 8556 8036 1076 459 2555 C
ATOM 114 CG LEU A 62 -16.299 -12.408 40.669 1.00 87.25 C
ANISOU 114 CG LEU A 62 16290 8539 8321 1438 524 2676 C
ATOM 115 CD1 LEU A 62 -14.798 -12.314 40.967 1.00 91.67 C
ANISOU 115 CD1 LEU A 62 16684 9318 8827 2022 396 2851 C
ATOM 116 CD2 LEU A 62 -16.811 -13.839 40.745 1.00 84.38 C
ANISOU 116 CD2 LEU A 62 16628 7697 7737 1325 711 2780 C
ATOM 117 N LEU A 63 -18.608 -9.661 39.578 1.00 78.54 N
ANISOU 117 N LEU A 63 14066 8001 7773 433 450 2057 N
ATOM 118 CA LEU A 63 -19.129 -9.249 38.273 1.00 79.29 C
ANISOU 118 CA LEU A 63 13976 8072 8080 240 475 1881 C
ATOM 119 C LEU A 63 -18.554 -7.904 37.838 1.00 75.51 C
ANISOU 119 C LEU A 63 12945 7912 7834 397 328 1755 C
ATOM 120 O LEU A 63 -18.353 -7.663 36.639 1.00 76.07 O
ANISOU 120 O LEU A 63 12890 7935 8077 449 315 1670 O
ATOM 121 CB LEU A 63 -20.659 -9.156 38.306 1.00 78.99 C
ANISOU 121 CB LEU A 63 13914 8074 8023 -277 575 1758 C
ATOM 122 CG LEU A 63 -21.570 -10.389 38.313 1.00 77.39 C
ANISOU 122 CG LEU A 63 14224 7566 7616 -624 742 1820 C
ATOM 123 CD1 LEU A 63 -22.973 -9.984 38.737 1.00 84.79 C
ANISOU 123 CD1 LEU A 63 14960 8747 8511 -1099 804 1714 C
ATOM 124 CD2 LEU A 63 -21.648 -11.024 36.961 1.00 70.10 C
ANISOU 124 CD2 LEU A 63 13554 6342 6739 -699 815 1784 C
ATOM 125 N GLY A 64 -18.277 -7.026 38.792 1.00 72.46 N
ANISOU 125 N GLY A 64 12258 7837 7436 455 221 1740 N
ATOM 126 CA GLY A 64 -17.806 -5.693 38.495 1.00 71.76 C
ANISOU 126 CA GLY A 64 11696 8040 7530 537 90 1611 C
ATOM 127 C GLY A 64 -16.305 -5.529 38.415 1.00 73.38 C
ANISOU 127 C GLY A 64 11769 8367 7745 927 -42 1710 C
ATOM 128 O GLY A 64 -15.846 -4.556 37.821 1.00 72.66 O
ANISOU 128 O GLY A 64 11333 8459 7815 977 -136 1604 O
ATOM 129 N VAL A 65 -15.518 -6.423 39.014 1.00 78.50 N
ANISOU 129 N VAL A 65 12670 8951 8207 1208 -51 1919 N
ATOM 130 CA VAL A 65 -14.076 -6.332 38.806 1.00 77.25 C
ANISOU 130 CA VAL A 65 12348 8963 8042 1605 -168 2032 C
ATOM 131 C VAL A 65 -13.706 -6.947 37.468 1.00 75.16 C
ANISOU 131 C VAL A 65 12224 8460 7873 1802 -100 2058 C
ATOM 132 O VAL A 65 -12.983 -6.339 36.673 1.00 71.94 O
ANISOU 132 O VAL A 65 11514 8216 7604 1944 -180 2009 O
ATOM 133 CB VAL A 65 -13.267 -6.963 39.966 1.00 81.05 C
ANISOU 133 CB VAL A 65 12985 9546 8265 1896 -219 2266 C
ATOM 134 CG1 VAL A 65 -13.462 -6.185 41.255 1.00 78.13 C
ANISOU 134 CG1 VAL A 65 12417 9469 7798 1711 -312 2228 C
ATOM 135 CG2 VAL A 65 -13.594 -8.423 40.172 1.00 86.43 C
ANISOU 135 CG2 VAL A 65 14233 9840 8766 1989 -66 2431 C
ATOM 136 N ILE A 66 -14.226 -8.140 37.174 1.00 77.53 N
ANISOU 136 N ILE A 66 13007 8362 8088 1783 56 2126 N
ATOM 137 CA ILE A 66 -13.911 -8.777 35.898 1.00 78.53 C
ANISOU 137 CA ILE A 66 13335 8223 8278 1964 139 2144 C
ATOM 138 C ILE A 66 -14.507 -7.970 34.754 1.00 79.42 C
ANISOU 138 C ILE A 66 13174 8358 8643 1685 136 1917 C
ATOM 139 O ILE A 66 -13.827 -7.658 33.767 1.00 78.44 O
ANISOU 139 O ILE A 66 12860 8293 8650 1873 97 1884 O
ATOM 140 CB ILE A 66 -14.394 -10.240 35.878 1.00 76.12 C
ANISOU 140 CB ILE A 66 13689 7445 7787 1954 320 2256 C
ATOM 141 CG1 ILE A 66 -14.203 -10.885 37.254 1.00 79.71 C
ANISOU 141 CG1 ILE A 66 14420 7885 7982 2095 329 2453 C
ATOM 142 CG2 ILE A 66 -13.606 -11.042 34.841 1.00 69.03 C
ANISOU 142 CG2 ILE A 66 13071 6291 6866 2335 399 2351 C
ATOM 143 CD1 ILE A 66 -14.945 -12.198 37.415 1.00 78.67 C
ANISOU 143 CD1 ILE A 66 14967 7279 7646 1945 514 2537 C
ATOM 144 N GLY A 67 -15.778 -7.595 34.888 1.00 80.36 N
ANISOU 144 N GLY A 67 13250 8465 8818 1248 177 1768 N
ATOM 145 CA GLY A 67 -16.427 -6.753 33.908 1.00 76.49 C
ANISOU 145 CA GLY A 67 12475 8043 8544 992 169 1564 C
ATOM 146 C GLY A 67 -15.664 -5.471 33.655 1.00 74.47 C
ANISOU 146 C GLY A 67 11729 8115 8452 1128 21 1483 C
ATOM 147 O GLY A 67 -15.265 -5.199 32.523 1.00 75.62 O
ANISOU 147 O GLY A 67 11740 8251 8743 1220 4 1424 O
ATOM 148 N ASN A 68 -15.440 -4.674 34.700 1.00 78.38 N
ANISOU 148 N ASN A 68 11977 8897 8905 1121 -82 1479 N
ATOM 149 CA ASN A 68 -14.792 -3.384 34.499 1.00 78.07 C
ANISOU 149 CA ASN A 68 11511 9159 8992 1170 -218 1386 C
ATOM 150 C ASN A 68 -13.300 -3.504 34.210 1.00 80.24 C
ANISOU 150 C ASN A 68 11677 9568 9243 1534 -308 1513 C
ATOM 151 O ASN A 68 -12.697 -2.523 33.764 1.00 76.79 O
ANISOU 151 O ASN A 68 10905 9358 8913 1553 -410 1438 O
ATOM 152 CB ASN A 68 -15.040 -2.473 35.705 1.00 69.00 C
ANISOU 152 CB ASN A 68 10179 8261 7775 1014 -292 1328 C
ATOM 153 CG ASN A 68 -16.444 -1.861 35.695 1.00 66.64 C
ANISOU 153 CG ASN A 68 9825 7942 7553 681 -217 1154 C
ATOM 154 OD1 ASN A 68 -16.741 -0.954 34.914 1.00 71.85 O
ANISOU 154 OD1 ASN A 68 10267 8657 8375 582 -230 1005 O
ATOM 155 ND2 ASN A 68 -17.305 -2.361 36.556 1.00 65.82 N
ANISOU 155 ND2 ASN A 68 9916 7777 7317 523 -133 1186 N
ATOM 156 N SER A 69 -12.696 -4.677 34.420 1.00 81.81 N
ANISOU 156 N SER A 69 12156 9641 9287 1830 -264 1711 N
ATOM 157 CA SER A 69 -11.303 -4.850 34.021 1.00 79.39 C
ANISOU 157 CA SER A 69 11725 9495 8944 2223 -329 1847 C
ATOM 158 C SER A 69 -11.173 -5.122 32.528 1.00 81.20 C
ANISOU 158 C SER A 69 12006 9532 9315 2324 -253 1801 C
ATOM 159 O SER A 69 -10.193 -4.688 31.909 1.00 80.85 O
ANISOU 159 O SER A 69 11681 9709 9328 2522 -327 1820 O
ATOM 160 CB SER A 69 -10.653 -5.981 34.816 1.00 82.31 C
ANISOU 160 CB SER A 69 12378 9828 9069 2577 -303 2097 C
ATOM 161 OG SER A 69 -10.888 -5.827 36.203 1.00 83.67 O
ANISOU 161 OG SER A 69 12551 10143 9095 2460 -360 2141 O
ATOM 162 N LEU A 70 -12.139 -5.840 31.940 1.00 79.39 N
ANISOU 162 N LEU A 70 12131 8911 9122 2167 -107 1743 N
ATOM 163 CA LEU A 70 -12.137 -6.058 30.494 1.00 72.70 C
ANISOU 163 CA LEU A 70 11353 7868 8403 2207 -32 1675 C
ATOM 164 C LEU A 70 -12.287 -4.755 29.723 1.00 67.85 C
ANISOU 164 C LEU A 70 10314 7454 8011 1996 -115 1484 C
ATOM 165 O LEU A 70 -11.686 -4.601 28.657 1.00 74.38 O
ANISOU 165 O LEU A 70 11020 8307 8935 2144 -120 1464 O
ATOM 166 CB LEU A 70 -13.264 -7.011 30.092 1.00 72.59 C
ANISOU 166 CB LEU A 70 11806 7422 8353 1982 131 1632 C
ATOM 167 CG LEU A 70 -13.082 -8.524 30.176 1.00 77.53 C
ANISOU 167 CG LEU A 70 13011 7678 8769 2214 273 1802 C
ATOM 168 CD1 LEU A 70 -14.382 -9.197 29.806 1.00 77.30 C
ANISOU 168 CD1 LEU A 70 13387 7276 8706 1823 412 1712 C
ATOM 169 CD2 LEU A 70 -11.973 -8.986 29.250 1.00 78.89 C
ANISOU 169 CD2 LEU A 70 13264 7784 8928 2657 312 1897 C
ATOM 170 N VAL A 71 -13.078 -3.809 30.235 1.00 61.59 N
ANISOU 170 N VAL A 71 9315 6798 7288 1669 -171 1348 N
ATOM 171 CA VAL A 71 -13.330 -2.574 29.496 1.00 60.82 C
ANISOU 171 CA VAL A 71 8882 6843 7384 1476 -230 1169 C
ATOM 172 C VAL A 71 -12.089 -1.695 29.463 1.00 64.01 C
ANISOU 172 C VAL A 71 8931 7576 7815 1642 -367 1190 C
ATOM 173 O VAL A 71 -11.721 -1.165 28.409 1.00 66.91 O
ANISOU 173 O VAL A 71 9114 7997 8312 1661 -391 1120 O
ATOM 174 CB VAL A 71 -14.525 -1.827 30.105 1.00 58.19 C
ANISOU 174 CB VAL A 71 8464 6562 7082 1135 -230 1033 C
ATOM 175 CG1 VAL A 71 -14.687 -0.456 29.442 1.00 54.07 C
ANISOU 175 CG1 VAL A 71 7619 6195 6732 993 -292 865 C
ATOM 176 CG2 VAL A 71 -15.789 -2.679 29.969 1.00 59.22 C
ANISOU 176 CG2 VAL A 71 8898 6425 7178 920 -93 1010 C
ATOM 177 N ILE A 72 -11.435 -1.511 30.616 1.00 62.40 N
ANISOU 177 N ILE A 72 8623 7618 7469 1733 -461 1287 N
ATOM 178 CA ILE A 72 -10.144 -0.829 30.648 1.00 62.70 C
ANISOU 178 CA ILE A 72 8332 8018 7475 1877 -596 1340 C
ATOM 179 C ILE A 72 -9.167 -1.504 29.693 1.00 68.26 C
ANISOU 179 C ILE A 72 9031 8727 8177 2217 -565 1461 C
ATOM 180 O ILE A 72 -8.473 -0.844 28.912 1.00 71.70 O
ANISOU 180 O ILE A 72 9192 9357 8692 2243 -624 1423 O
ATOM 181 CB ILE A 72 -9.594 -0.797 32.085 1.00 63.55 C
ANISOU 181 CB ILE A 72 8376 8393 7378 1938 -695 1461 C
ATOM 182 CG1 ILE A 72 -10.496 0.064 32.973 1.00 71.52 C
ANISOU 182 CG1 ILE A 72 9364 9425 8386 1597 -725 1318 C
ATOM 183 CG2 ILE A 72 -8.174 -0.257 32.111 1.00 58.59 C
ANISOU 183 CG2 ILE A 72 7400 8194 6667 2084 -837 1548 C
ATOM 184 CD1 ILE A 72 -10.306 -0.165 34.476 1.00 69.76 C
ANISOU 184 CD1 ILE A 72 9199 9361 7945 1624 -782 1431 C
ATOM 185 N HIS A 73 -9.134 -2.837 29.719 1.00 67.39 N
ANISOU 185 N HIS A 73 9259 8385 7962 2480 -457 1606 N
ATOM 186 CA HIS A 73 -8.128 -3.592 28.988 1.00 58.52 C
ANISOU 186 CA HIS A 73 8180 7273 6781 2889 -408 1754 C
ATOM 187 C HIS A 73 -8.292 -3.449 27.481 1.00 67.00 C
ANISOU 187 C HIS A 73 9243 8179 8034 2844 -339 1633 C
ATOM 188 O HIS A 73 -7.343 -3.079 26.782 1.00 75.57 O
ANISOU 188 O HIS A 73 10057 9506 9151 3012 -383 1661 O
ATOM 189 CB HIS A 73 -8.211 -5.056 29.390 1.00 65.21 C
ANISOU 189 CB HIS A 73 9495 7826 7454 3169 -281 1925 C
ATOM 190 CG HIS A 73 -7.072 -5.879 28.886 1.00 74.43 C
ANISOU 190 CG HIS A 73 10738 9041 8502 3686 -223 2118 C
ATOM 191 ND1 HIS A 73 -5.759 -5.474 28.995 1.00 77.60 N
ANISOU 191 ND1 HIS A 73 10721 9930 8834 3911 -329 2213 N
ATOM 192 CD2 HIS A 73 -7.047 -7.086 28.279 1.00 76.25 C
ANISOU 192 CD2 HIS A 73 11369 8928 8675 3880 -49 2149 C
ATOM 193 CE1 HIS A 73 -4.974 -6.395 28.473 1.00 78.67 C
ANISOU 193 CE1 HIS A 73 10965 10032 8895 4181 -205 2260 C
ATOM 194 NE2 HIS A 73 -5.730 -7.384 28.033 1.00 80.70 N
ANISOU 194 NE2 HIS A 73 11723 9784 9154 4180 -36 2220 N
ATOM 195 N VAL A 74 -9.490 -3.738 26.958 1.00 61.22 N
ANISOU 195 N VAL A 74 8790 7067 7404 2602 -231 1503 N
ATOM 196 CA VAL A 74 -9.675 -3.784 25.509 1.00 58.42 C
ANISOU 196 CA VAL A 74 8485 6525 7187 2575 -154 1404 C
ATOM 197 C VAL A 74 -9.568 -2.391 24.895 1.00 64.19 C
ANISOU 197 C VAL A 74 8794 7503 8093 2367 -259 1254 C
ATOM 198 O VAL A 74 -9.056 -2.231 23.781 1.00 72.19 O
ANISOU 198 O VAL A 74 9693 8550 9185 2471 -244 1231 O
ATOM 199 CB VAL A 74 -11.007 -4.473 25.142 1.00 54.72 C
ANISOU 199 CB VAL A 74 8419 5629 6745 2326 -22 1311 C
ATOM 200 CG1 VAL A 74 -11.076 -5.870 25.777 1.00 59.82 C
ANISOU 200 CG1 VAL A 74 9550 5995 7184 2507 91 1465 C
ATOM 201 CG2 VAL A 74 -12.217 -3.622 25.526 1.00 52.74 C
ANISOU 201 CG2 VAL A 74 8032 5413 6594 1888 -68 1148 C
ATOM 202 N VAL A 75 -10.036 -1.358 25.599 1.00 64.54 N
ANISOU 202 N VAL A 75 8628 7710 8184 2080 -356 1153 N
ATOM 203 CA VAL A 75 -9.891 -0.010 25.064 1.00 61.85 C
ANISOU 203 CA VAL A 75 7949 7575 7978 1894 -446 1019 C
ATOM 204 C VAL A 75 -8.410 0.337 24.950 1.00 61.77 C
ANISOU 204 C VAL A 75 7641 7922 7905 2107 -539 1122 C
ATOM 205 O VAL A 75 -8.021 1.140 24.096 1.00 60.56 O
ANISOU 205 O VAL A 75 7260 7901 7849 2034 -580 1047 O
ATOM 206 CB VAL A 75 -10.697 0.999 25.933 1.00 57.79 C
ANISOU 206 CB VAL A 75 7338 7133 7485 1575 -511 896 C
ATOM 207 CG1 VAL A 75 -10.341 2.441 25.634 1.00 50.90 C
ANISOU 207 CG1 VAL A 75 6162 6485 6691 1411 -612 784 C
ATOM 208 CG2 VAL A 75 -12.216 0.802 25.742 1.00 56.12 C
ANISOU 208 CG2 VAL A 75 7336 6635 7351 1350 -411 782 C
ATOM 209 N ILE A 76 -7.560 -0.308 25.741 1.00 58.97 N
ANISOU 209 N ILE A 76 7287 7747 7373 2382 -567 1307 N
ATOM 210 CA ILE A 76 -6.127 -0.031 25.694 1.00 68.26 C
ANISOU 210 CA ILE A 76 8135 9351 8451 2592 -659 1431 C
ATOM 211 C ILE A 76 -5.402 -0.934 24.696 1.00 72.92 C
ANISOU 211 C ILE A 76 8788 9903 9015 2984 -558 1552 C
ATOM 212 O ILE A 76 -4.604 -0.460 23.885 1.00 73.51 O
ANISOU 212 O ILE A 76 8588 10223 9121 3043 -589 1555 O
ATOM 213 CB ILE A 76 -5.514 -0.152 27.104 1.00 70.22 C
ANISOU 213 CB ILE A 76 8285 9908 8488 2696 -758 1584 C
ATOM 214 CG1 ILE A 76 -6.080 0.917 28.021 1.00 66.00 C
ANISOU 214 CG1 ILE A 76 7658 9457 7961 2297 -862 1450 C
ATOM 215 CG2 ILE A 76 -4.002 -0.002 27.046 1.00 69.10 C
ANISOU 215 CG2 ILE A 76 7777 10275 8202 2937 -850 1744 C
ATOM 216 CD1 ILE A 76 -5.586 0.772 29.417 1.00 68.59 C
ANISOU 216 CD1 ILE A 76 7925 10064 8072 2366 -957 1587 C
ATOM 217 N LYS A 77 -5.642 -2.248 24.731 1.00 70.63 N
ANISOU 217 N LYS A 77 8886 9303 8647 3262 -425 1656 N
ATOM 218 CA LYS A 77 -4.833 -3.147 23.913 1.00 64.37 C
ANISOU 218 CA LYS A 77 8190 8480 7786 3622 -309 1753 C
ATOM 219 C LYS A 77 -5.190 -3.069 22.431 1.00 70.22 C
ANISOU 219 C LYS A 77 9011 8978 8692 3538 -219 1617 C
ATOM 220 O LYS A 77 -4.342 -3.379 21.587 1.00 80.27 O
ANISOU 220 O LYS A 77 10217 10349 9934 3686 -150 1625 O
ATOM 221 CB LYS A 77 -4.961 -4.593 24.403 1.00 66.61 C
ANISOU 221 CB LYS A 77 8925 8470 7915 3843 -171 1853 C
ATOM 222 CG LYS A 77 -3.710 -5.431 24.149 1.00 70.35 C
ANISOU 222 CG LYS A 77 9388 9116 8227 4174 -78 1956 C
ATOM 223 CD LYS A 77 -3.986 -6.927 24.151 1.00 71.42 C
ANISOU 223 CD LYS A 77 10063 8843 8231 4375 108 2004 C
ATOM 224 CE LYS A 77 -2.791 -7.718 23.604 1.00 75.56 C
ANISOU 224 CE LYS A 77 10597 9514 8598 4730 231 2085 C
ATOM 225 NZ LYS A 77 -1.515 -7.499 24.357 1.00 80.33 N
ANISOU 225 NZ LYS A 77 10817 10657 9048 4950 153 2233 N
ATOM 226 N PHE A 78 -6.411 -2.655 22.084 1.00 64.28 N
ANISOU 226 N PHE A 78 8387 7934 8102 3217 -209 1454 N
ATOM 227 CA PHE A 78 -6.886 -2.698 20.702 1.00 60.23 C
ANISOU 227 CA PHE A 78 8001 7156 7726 3122 -116 1325 C
ATOM 228 C PHE A 78 -7.028 -1.290 20.141 1.00 59.68 C
ANISOU 228 C PHE A 78 7570 7276 7829 2793 -219 1164 C
ATOM 229 O PHE A 78 -7.876 -0.519 20.602 1.00 53.09 O
ANISOU 229 O PHE A 78 6673 6419 7078 2447 -287 1039 O
ATOM 230 CB PHE A 78 -8.221 -3.435 20.609 1.00 59.89 C
ANISOU 230 CB PHE A 78 8414 6636 7707 2923 -4 1238 C
ATOM 231 CG PHE A 78 -8.186 -4.804 21.188 1.00 61.28 C
ANISOU 231 CG PHE A 78 9027 6560 7695 3191 109 1387 C
ATOM 232 CD1 PHE A 78 -7.645 -5.858 20.472 1.00 69.16 C
ANISOU 232 CD1 PHE A 78 10272 7417 8589 3404 244 1420 C
ATOM 233 CD2 PHE A 78 -8.684 -5.043 22.453 1.00 61.92 C
ANISOU 233 CD2 PHE A 78 9242 6597 7688 3088 83 1433 C
ATOM 234 CE1 PHE A 78 -7.598 -7.149 21.015 1.00 77.05 C
ANISOU 234 CE1 PHE A 78 11675 8210 9392 3555 358 1509 C
ATOM 235 CE2 PHE A 78 -8.649 -6.319 23.006 1.00 70.96 C
ANISOU 235 CE2 PHE A 78 10829 7492 8641 3322 193 1575 C
ATOM 236 CZ PHE A 78 -8.099 -7.378 22.287 1.00 75.27 C
ANISOU 236 CZ PHE A 78 11612 7906 9083 3507 331 1585 C
ATOM 237 N LYS A 79 -6.224 -0.966 19.122 1.00 68.14 N
ANISOU 237 N LYS A 79 8430 8521 8939 2914 -217 1168 N
ATOM 238 CA LYS A 79 -6.364 0.335 18.468 1.00 65.96 C
ANISOU 238 CA LYS A 79 7871 8376 8813 2604 -298 1018 C
ATOM 239 C LYS A 79 -7.689 0.448 17.736 1.00 62.98 C
ANISOU 239 C LYS A 79 7707 7638 8586 2327 -239 845 C
ATOM 240 O LYS A 79 -8.119 1.558 17.408 1.00 58.31 O
ANISOU 240 O LYS A 79 6943 7098 8114 2042 -304 712 O
ATOM 241 CB LYS A 79 -5.206 0.583 17.497 1.00 67.84 C
ANISOU 241 CB LYS A 79 7852 8884 9040 2789 -295 1072 C
ATOM 242 CG LYS A 79 -5.190 1.991 16.906 1.00 71.61 C
ANISOU 242 CG LYS A 79 8039 9530 9640 2464 -387 939 C
ATOM 243 CD LYS A 79 -5.233 3.052 18.017 1.00 70.08 C
ANISOU 243 CD LYS A 79 7644 9559 9423 2180 -532 900 C
ATOM 244 CE LYS A 79 -5.515 4.462 17.489 1.00 66.81 C
ANISOU 244 CE LYS A 79 7078 9182 9123 1820 -601 742 C
ATOM 245 NZ LYS A 79 -6.931 4.648 17.062 1.00 64.03 N
ANISOU 245 NZ LYS A 79 6958 8447 8922 1622 -547 584 N
ATOM 246 N SER A 80 -8.338 -0.685 17.469 1.00 64.28 N
ANISOU 246 N SER A 80 8256 7446 8720 2402 -113 851 N
ATOM 247 CA SER A 80 -9.670 -0.666 16.882 1.00 59.38 C
ANISOU 247 CA SER A 80 7828 6532 8203 2104 -64 702 C
ATOM 248 C SER A 80 -10.639 0.090 17.772 1.00 58.76 C
ANISOU 248 C SER A 80 7659 6492 8174 1790 -143 614 C
ATOM 249 O SER A 80 -11.544 0.773 17.271 1.00 53.76 O
ANISOU 249 O SER A 80 6968 5808 7652 1526 -158 480 O
ATOM 250 CB SER A 80 -10.134 -2.110 16.665 1.00 63.48 C
ANISOU 250 CB SER A 80 8817 6681 8621 2203 82 742 C
ATOM 251 OG SER A 80 -11.386 -2.190 16.009 1.00 70.61 O
ANISOU 251 OG SER A 80 9899 7342 9589 1891 129 608 O
ATOM 252 N MET A 81 -10.417 0.010 19.095 1.00 63.24 N
ANISOU 252 N MET A 81 8206 7178 8646 1844 -193 698 N
ATOM 253 CA MET A 81 -11.297 0.480 20.158 1.00 55.86 C
ANISOU 253 CA MET A 81 7252 6262 7709 1604 -242 641 C
ATOM 254 C MET A 81 -10.889 1.821 20.754 1.00 55.58 C
ANISOU 254 C MET A 81 6892 6527 7700 1497 -372 601 C
ATOM 255 O MET A 81 -11.625 2.355 21.585 1.00 59.55 O
ANISOU 255 O MET A 81 7379 7048 8198 1304 -405 539 O
ATOM 256 CB MET A 81 -11.325 -0.542 21.293 1.00 56.48 C
ANISOU 256 CB MET A 81 7570 6254 7634 1724 -204 764 C
ATOM 257 CG MET A 81 -11.535 -1.954 20.845 1.00 60.93 C
ANISOU 257 CG MET A 81 8535 6498 8119 1855 -66 828 C
ATOM 258 SD MET A 81 -13.254 -2.289 20.494 1.00 66.95 S
ANISOU 258 SD MET A 81 9556 6966 8916 1473 20 697 S
ATOM 259 CE MET A 81 -13.993 -2.102 22.127 1.00 62.98 C
ANISOU 259 CE MET A 81 9044 6549 8337 1290 -21 710 C
ATOM 260 N ARG A 82 -9.736 2.363 20.395 1.00 53.39 N
ANISOU 260 N ARG A 82 6373 6491 7421 1604 -438 638 N
ATOM 261 CA ARG A 82 -9.343 3.652 20.941 1.00 55.23 C
ANISOU 261 CA ARG A 82 6347 6992 7646 1441 -559 592 C
ATOM 262 C ARG A 82 -10.131 4.720 20.195 1.00 57.98 C
ANISOU 262 C ARG A 82 6651 7246 8133 1194 -561 426 C
ATOM 263 O ARG A 82 -9.782 5.108 19.079 1.00 61.95 O
ANISOU 263 O ARG A 82 7057 7770 8713 1191 -557 389 O
ATOM 264 CB ARG A 82 -7.838 3.861 20.828 1.00 52.63 C
ANISOU 264 CB ARG A 82 5764 6999 7235 1592 -632 698 C
ATOM 265 CG ARG A 82 -7.025 2.691 21.303 1.00 60.67 C
ANISOU 265 CG ARG A 82 6824 8120 8108 1929 -608 888 C
ATOM 266 CD ARG A 82 -5.622 3.139 21.653 1.00 68.18 C
ANISOU 266 CD ARG A 82 7444 9536 8927 2013 -718 1001 C
ATOM 267 NE ARG A 82 -4.636 2.121 21.330 1.00 71.33 N
ANISOU 267 NE ARG A 82 7810 10073 9220 2422 -663 1183 N
ATOM 268 CZ ARG A 82 -3.375 2.154 21.728 1.00 74.24 C
ANISOU 268 CZ ARG A 82 7889 10896 9422 2596 -741 1339 C
ATOM 269 NH1 ARG A 82 -2.941 3.154 22.484 1.00 74.56 N
ANISOU 269 NH1 ARG A 82 7662 11289 9379 2340 -888 1325 N
ATOM 270 NH2 ARG A 82 -2.556 1.178 21.374 1.00 79.00 N
ANISOU 270 NH2 ARG A 82 8516 11575 9924 2962 -653 1479 N
ATOM 271 N THR A 83 -11.227 5.166 20.796 1.00 50.94 N
ANISOU 271 N THR A 83 5840 6256 7260 1010 -555 334 N
ATOM 272 CA THR A 83 -12.022 6.268 20.285 1.00 50.01 C
ANISOU 272 CA THR A 83 5688 6076 7239 818 -554 192 C
ATOM 273 C THR A 83 -12.269 7.246 21.430 1.00 57.60 C
ANISOU 273 C THR A 83 6625 7131 8129 672 -610 135 C
ATOM 274 O THR A 83 -11.900 6.992 22.579 1.00 63.47 O
ANISOU 274 O THR A 83 7376 7983 8756 695 -651 201 O
ATOM 275 CB THR A 83 -13.336 5.770 19.677 1.00 50.25 C
ANISOU 275 CB THR A 83 5862 5886 7346 769 -459 135 C
ATOM 276 OG1 THR A 83 -14.274 5.466 20.715 1.00 64.79 O
ANISOU 276 OG1 THR A 83 7812 7680 9125 697 -426 132 O
ATOM 277 CG2 THR A 83 -13.087 4.501 18.886 1.00 48.85 C
ANISOU 277 CG2 THR A 83 5804 5580 7178 910 -391 207 C
ATOM 278 N VAL A 84 -12.858 8.401 21.122 1.00 52.73 N
ANISOU 278 N VAL A 84 6001 6472 7563 534 -609 15 N
ATOM 279 CA VAL A 84 -13.145 9.330 22.209 1.00 48.34 C
ANISOU 279 CA VAL A 84 5485 5966 6916 413 -639 -47 C
ATOM 280 C VAL A 84 -14.290 8.802 23.065 1.00 49.40 C
ANISOU 280 C VAL A 84 5732 6022 7015 421 -572 -50 C
ATOM 281 O VAL A 84 -14.294 8.971 24.289 1.00 57.13 O
ANISOU 281 O VAL A 84 6756 7071 7878 378 -595 -45 O
ATOM 282 CB VAL A 84 -13.451 10.739 21.677 1.00 43.13 C
ANISOU 282 CB VAL A 84 4846 5252 6288 301 -636 -168 C
ATOM 283 CG1 VAL A 84 -14.034 11.592 22.797 1.00 42.79 C
ANISOU 283 CG1 VAL A 84 4923 5198 6139 214 -626 -243 C
ATOM 284 CG2 VAL A 84 -12.211 11.370 21.145 1.00 49.80 C
ANISOU 284 CG2 VAL A 84 5596 6211 7115 226 -714 -161 C
ATOM 285 N THR A 85 -15.277 8.149 22.447 1.00 48.28 N
ANISOU 285 N THR A 85 5636 5759 6951 450 -487 -56 N
ATOM 286 CA THR A 85 -16.389 7.656 23.250 1.00 57.35 C
ANISOU 286 CA THR A 85 6872 6876 8044 417 -419 -53 C
ATOM 287 C THR A 85 -15.938 6.540 24.195 1.00 58.14 C
ANISOU 287 C THR A 85 7052 6993 8047 468 -430 59 C
ATOM 288 O THR A 85 -16.316 6.532 25.377 1.00 62.19 O
ANISOU 288 O THR A 85 7621 7552 8456 427 -420 68 O
ATOM 289 CB THR A 85 -17.544 7.218 22.350 1.00 52.66 C
ANISOU 289 CB THR A 85 6290 6198 7522 383 -334 -79 C
ATOM 290 OG1 THR A 85 -18.229 8.379 21.884 1.00 56.03 O
ANISOU 290 OG1 THR A 85 6649 6649 7989 360 -313 -175 O
ATOM 291 CG2 THR A 85 -18.525 6.416 23.118 1.00 48.80 C
ANISOU 291 CG2 THR A 85 5883 5708 6952 319 -264 -46 C
ATOM 292 N ASN A 86 -15.072 5.638 23.722 1.00 46.85 N
ANISOU 292 N ASN A 86 5639 5532 6630 582 -446 154 N
ATOM 293 CA ASN A 86 -14.575 4.570 24.580 1.00 50.90 C
ANISOU 293 CA ASN A 86 6256 6053 7032 684 -450 281 C
ATOM 294 C ASN A 86 -13.634 5.069 25.678 1.00 55.94 C
ANISOU 294 C ASN A 86 6807 6892 7554 710 -550 325 C
ATOM 295 O ASN A 86 -13.462 4.376 26.688 1.00 59.88 O
ANISOU 295 O ASN A 86 7395 7425 7933 772 -556 422 O
ATOM 296 CB ASN A 86 -13.894 3.500 23.733 1.00 56.45 C
ANISOU 296 CB ASN A 86 7030 6662 7755 853 -421 376 C
ATOM 297 CG ASN A 86 -14.897 2.668 22.921 1.00 64.26 C
ANISOU 297 CG ASN A 86 8196 7427 8794 789 -313 351 C
ATOM 298 OD1 ASN A 86 -16.114 2.705 23.171 1.00 68.99 O
ANISOU 298 OD1 ASN A 86 8848 7980 9386 615 -261 291 O
ATOM 299 ND2 ASN A 86 -14.387 1.899 21.959 1.00 59.61 N
ANISOU 299 ND2 ASN A 86 7700 6721 8229 919 -273 400 N
ATOM 300 N PHE A 87 -13.031 6.250 25.527 1.00 56.36 N
ANISOU 300 N PHE A 87 6710 7084 7620 641 -629 260 N
ATOM 301 CA PHE A 87 -12.184 6.761 26.600 1.00 58.65 C
ANISOU 301 CA PHE A 87 6927 7590 7766 601 -731 294 C
ATOM 302 C PHE A 87 -13.020 7.234 27.781 1.00 58.93 C
ANISOU 302 C PHE A 87 7067 7612 7713 473 -714 226 C
ATOM 303 O PHE A 87 -12.617 7.075 28.937 1.00 58.28 O
ANISOU 303 O PHE A 87 7001 7661 7481 469 -767 290 O
ATOM 304 CB PHE A 87 -11.297 7.895 26.097 1.00 58.94 C
ANISOU 304 CB PHE A 87 6809 7779 7807 502 -817 240 C
ATOM 305 CG PHE A 87 -10.208 7.450 25.170 1.00 65.87 C
ANISOU 305 CG PHE A 87 7538 8769 8719 637 -850 333 C
ATOM 306 CD1 PHE A 87 -9.942 6.106 24.970 1.00 66.62 C
ANISOU 306 CD1 PHE A 87 7666 8831 8815 876 -806 467 C
ATOM 307 CD2 PHE A 87 -9.442 8.388 24.493 1.00 69.05 C
ANISOU 307 CD2 PHE A 87 7793 9309 9134 528 -912 290 C
ATOM 308 CE1 PHE A 87 -8.934 5.713 24.109 1.00 64.42 C
ANISOU 308 CE1 PHE A 87 7258 8669 8551 1044 -818 556 C
ATOM 309 CE2 PHE A 87 -8.440 7.998 23.630 1.00 64.37 C
ANISOU 309 CE2 PHE A 87 7039 8860 8560 659 -932 380 C
ATOM 310 CZ PHE A 87 -8.183 6.666 23.443 1.00 62.31 C
ANISOU 310 CZ PHE A 87 6793 8580 8301 936 -882 513 C
ATOM 311 N PHE A 88 -14.172 7.846 27.508 1.00 60.12 N
ANISOU 311 N PHE A 88 7279 7628 7935 385 -636 103 N
ATOM 312 CA PHE A 88 -15.128 8.124 28.571 1.00 66.90 C
ANISOU 312 CA PHE A 88 8244 8470 8704 311 -583 50 C
ATOM 313 C PHE A 88 -15.717 6.830 29.123 1.00 67.18 C
ANISOU 313 C PHE A 88 8374 8454 8698 363 -518 145 C
ATOM 314 O PHE A 88 -15.921 6.694 30.334 1.00 71.06 O
ANISOU 314 O PHE A 88 8941 9002 9056 331 -514 171 O
ATOM 315 CB PHE A 88 -16.229 9.043 28.044 1.00 62.81 C
ANISOU 315 CB PHE A 88 7749 7858 8259 261 -501 -82 C
ATOM 316 CG PHE A 88 -15.713 10.333 27.483 1.00 53.74 C
ANISOU 316 CG PHE A 88 6577 6710 7133 205 -549 -175 C
ATOM 317 CD1 PHE A 88 -14.761 11.066 28.166 1.00 54.30 C
ANISOU 317 CD1 PHE A 88 6672 6885 7076 102 -641 -194 C
ATOM 318 CD2 PHE A 88 -16.176 10.817 26.272 1.00 53.19 C
ANISOU 318 CD2 PHE A 88 6479 6543 7189 230 -502 -239 C
ATOM 319 CE1 PHE A 88 -14.276 12.265 27.657 1.00 53.61 C
ANISOU 319 CE1 PHE A 88 6610 6780 6980 0 -679 -280 C
ATOM 320 CE2 PHE A 88 -15.683 12.018 25.751 1.00 52.84 C
ANISOU 320 CE2 PHE A 88 6457 6473 7148 167 -539 -318 C
ATOM 321 CZ PHE A 88 -14.731 12.730 26.444 1.00 53.22 C
ANISOU 321 CZ PHE A 88 6557 6602 7062 40 -624 -340 C
ATOM 322 N ILE A 89 -15.984 5.864 28.248 1.00 55.43 N
ANISOU 322 N ILE A 89 6912 6845 7303 424 -462 196 N
ATOM 323 CA ILE A 89 -16.500 4.578 28.698 1.00 53.74 C
ANISOU 323 CA ILE A 89 6848 6545 7026 439 -392 290 C
ATOM 324 C ILE A 89 -15.488 3.870 29.592 1.00 57.23 C
ANISOU 324 C ILE A 89 7354 7054 7337 556 -454 429 C
ATOM 325 O ILE A 89 -15.849 3.274 30.614 1.00 61.46 O
ANISOU 325 O ILE A 89 8020 7581 7750 537 -422 493 O
ATOM 326 CB ILE A 89 -16.903 3.730 27.481 1.00 52.06 C
ANISOU 326 CB ILE A 89 6698 6168 6914 450 -320 306 C
ATOM 327 CG1 ILE A 89 -18.311 4.132 27.045 1.00 54.12 C
ANISOU 327 CG1 ILE A 89 6920 6414 7229 300 -237 202 C
ATOM 328 CG2 ILE A 89 -16.809 2.287 27.808 1.00 54.35 C
ANISOU 328 CG2 ILE A 89 7201 6336 7113 507 -272 436 C
ATOM 329 CD1 ILE A 89 -18.771 3.543 25.781 1.00 55.20 C
ANISOU 329 CD1 ILE A 89 7088 6432 7452 256 -181 193 C
ATOM 330 N ALA A 90 -14.205 3.933 29.240 1.00 58.54 N
ANISOU 330 N ALA A 90 7416 7318 7509 686 -544 490 N
ATOM 331 CA ALA A 90 -13.190 3.405 30.144 1.00 60.13 C
ANISOU 331 CA ALA A 90 7625 7663 7557 824 -617 636 C
ATOM 332 C ALA A 90 -13.071 4.251 31.402 1.00 62.34 C
ANISOU 332 C ALA A 90 7850 8133 7705 702 -694 600 C
ATOM 333 O ALA A 90 -12.729 3.719 32.461 1.00 67.64 O
ANISOU 333 O ALA A 90 8584 8899 8218 767 -728 712 O
ATOM 334 CB ALA A 90 -11.834 3.294 29.436 1.00 57.73 C
ANISOU 334 CB ALA A 90 7173 7494 7268 1005 -691 723 C
ATOM 335 N ASN A 91 -13.366 5.553 31.323 1.00 67.53 N
ANISOU 335 N ASN A 91 8426 8833 8401 532 -715 447 N
ATOM 336 CA ASN A 91 -13.303 6.405 32.518 1.00 69.51 C
ANISOU 336 CA ASN A 91 8683 9228 8500 396 -774 393 C
ATOM 337 C ASN A 91 -14.413 6.069 33.504 1.00 66.19 C
ANISOU 337 C ASN A 91 8425 8725 8000 347 -683 382 C
ATOM 338 O ASN A 91 -14.172 6.003 34.714 1.00 74.26 O
ANISOU 338 O ASN A 91 9497 9868 8849 321 -728 432 O
ATOM 339 CB ASN A 91 -13.381 7.882 32.142 1.00 66.39 C
ANISOU 339 CB ASN A 91 8241 8840 8143 237 -793 228 C
ATOM 340 CG ASN A 91 -13.166 8.785 33.327 1.00 69.58 C
ANISOU 340 CG ASN A 91 8701 9377 8359 80 -854 167 C
ATOM 341 OD1 ASN A 91 -12.080 8.826 33.891 1.00 66.28 O
ANISOU 341 OD1 ASN A 91 8206 9180 7797 39 -977 240 O
ATOM 342 ND2 ASN A 91 -14.200 9.523 33.710 1.00 76.25 N
ANISOU 342 ND2 ASN A 91 9683 10108 9181 -4 -766 36 N
ATOM 343 N LEU A 92 -15.645 5.920 33.006 1.00 61.60 N
ANISOU 343 N LEU A 92 7906 7974 7525 317 -558 315 N
ATOM 344 CA LEU A 92 -16.702 5.251 33.756 1.00 64.43 C
ANISOU 344 CA LEU A 92 8399 8272 7809 278 -455 343 C
ATOM 345 C LEU A 92 -16.222 3.938 34.361 1.00 67.76 C
ANISOU 345 C LEU A 92 8938 8685 8124 373 -471 517 C
ATOM 346 O LEU A 92 -16.416 3.683 35.560 1.00 72.83 O
ANISOU 346 O LEU A 92 9680 9384 8608 339 -463 566 O
ATOM 347 CB LEU A 92 -17.885 4.974 32.848 1.00 67.09 C
ANISOU 347 CB LEU A 92 8745 8476 8272 234 -334 291 C
ATOM 348 CG LEU A 92 -18.889 6.092 32.739 1.00 68.38 C
ANISOU 348 CG LEU A 92 8844 8672 8464 159 -265 145 C
ATOM 349 CD1 LEU A 92 -19.924 5.627 31.759 1.00 71.39 C
ANISOU 349 CD1 LEU A 92 9192 8982 8950 121 -165 131 C
ATOM 350 CD2 LEU A 92 -19.463 6.304 34.099 1.00 70.26 C
ANISOU 350 CD2 LEU A 92 9160 9000 8535 102 -216 130 C
ATOM 351 N ALA A 93 -15.620 3.074 33.537 1.00 60.05 N
ANISOU 351 N ALA A 93 7980 7621 7216 511 -482 616 N
ATOM 352 CA ALA A 93 -15.118 1.803 34.059 1.00 63.81 C
ANISOU 352 CA ALA A 93 8617 8057 7569 658 -482 796 C
ATOM 353 C ALA A 93 -14.139 2.017 35.208 1.00 66.49 C
ANISOU 353 C ALA A 93 8900 8630 7735 731 -602 884 C
ATOM 354 O ALA A 93 -14.166 1.274 36.198 1.00 64.16 O
ANISOU 354 O ALA A 93 8760 8337 7281 780 -589 1002 O
ATOM 355 CB ALA A 93 -14.455 0.979 32.949 1.00 58.68 C
ANISOU 355 CB ALA A 93 8007 7288 7000 850 -472 887 C
ATOM 356 N VAL A 94 -13.268 3.028 35.097 1.00 68.25 N
ANISOU 356 N VAL A 94 8908 9062 7962 715 -721 833 N
ATOM 357 CA VAL A 94 -12.250 3.227 36.128 1.00 72.07 C
ANISOU 357 CA VAL A 94 9308 9823 8252 752 -853 925 C
ATOM 358 C VAL A 94 -12.890 3.812 37.384 1.00 73.92 C
ANISOU 358 C VAL A 94 9624 10112 8352 563 -848 846 C
ATOM 359 O VAL A 94 -12.421 3.570 38.506 1.00 77.25 O
ANISOU 359 O VAL A 94 10075 10702 8573 589 -918 949 O
ATOM 360 CB VAL A 94 -11.091 4.097 35.588 1.00 65.39 C
ANISOU 360 CB VAL A 94 8207 9216 7421 738 -983 900 C
ATOM 361 CG1 VAL A 94 -10.079 4.400 36.669 1.00 62.92 C
ANISOU 361 CG1 VAL A 94 7779 9251 6876 712 -1132 986 C
ATOM 362 CG2 VAL A 94 -10.389 3.389 34.463 1.00 62.82 C
ANISOU 362 CG2 VAL A 94 7802 8874 7194 971 -978 1006 C
ATOM 363 N ALA A 95 -13.998 4.537 37.224 1.00 66.32 N
ANISOU 363 N ALA A 95 8706 9016 7478 395 -756 673 N
ATOM 364 CA ALA A 95 -14.737 5.022 38.381 1.00 68.83 C
ANISOU 364 CA ALA A 95 9128 9364 7659 251 -715 598 C
ATOM 365 C ALA A 95 -15.398 3.880 39.143 1.00 73.66 C
ANISOU 365 C ALA A 95 9918 9894 8176 290 -627 711 C
ATOM 366 O ALA A 95 -15.394 3.868 40.377 1.00 80.02 O
ANISOU 366 O ALA A 95 10805 10808 8792 244 -649 748 O
ATOM 367 CB ALA A 95 -15.791 6.022 37.937 1.00 70.01 C
ANISOU 367 CB ALA A 95 9280 9405 7915 129 -616 405 C
ATOM 368 N ASP A 96 -15.994 2.927 38.429 1.00 72.27 N
ANISOU 368 N ASP A 96 9827 9521 8110 345 -524 762 N
ATOM 369 CA ASP A 96 -16.694 1.831 39.081 1.00 74.45 C
ANISOU 369 CA ASP A 96 10314 9691 8281 330 -425 864 C
ATOM 370 C ASP A 96 -15.743 0.737 39.544 1.00 79.94 C
ANISOU 370 C ASP A 96 11135 10395 8843 521 -486 1075 C
ATOM 371 O ASP A 96 -16.110 -0.076 40.406 1.00 77.83 O
ANISOU 371 O ASP A 96 11074 10072 8424 511 -428 1180 O
ATOM 372 CB ASP A 96 -17.748 1.265 38.134 1.00 79.08 C
ANISOU 372 CB ASP A 96 10973 10071 9001 256 -287 830 C
ATOM 373 CG ASP A 96 -18.643 2.353 37.546 1.00 90.76 C
ANISOU 373 CG ASP A 96 12294 11581 10609 126 -230 643 C
ATOM 374 OD1 ASP A 96 -19.124 3.212 38.324 1.00 91.18 O
ANISOU 374 OD1 ASP A 96 12307 11756 10582 43 -209 550 O
ATOM 375 OD2 ASP A 96 -18.849 2.357 36.304 1.00 95.67 O
ANISOU 375 OD2 ASP A 96 12847 12106 11397 130 -202 594 O
ATOM 376 N LEU A 97 -14.529 0.701 38.996 1.00 80.19 N
ANISOU 376 N LEU A 97 11047 10512 8908 708 -593 1150 N
ATOM 377 CA LEU A 97 -13.511 -0.175 39.555 1.00 79.04 C
ANISOU 377 CA LEU A 97 10978 10457 8597 945 -664 1365 C
ATOM 378 C LEU A 97 -13.064 0.327 40.918 1.00 82.34 C
ANISOU 378 C LEU A 97 11330 11152 8803 894 -774 1398 C
ATOM 379 O LEU A 97 -12.904 -0.459 41.857 1.00 88.28 O
ANISOU 379 O LEU A 97 12246 11932 9366 997 -778 1557 O
ATOM 380 CB LEU A 97 -12.326 -0.268 38.605 1.00 76.52 C
ANISOU 380 CB LEU A 97 10497 10228 8350 1176 -745 1440 C
ATOM 381 CG LEU A 97 -11.396 -1.441 38.853 1.00 72.24 C
ANISOU 381 CG LEU A 97 10073 9721 7653 1516 -768 1690 C
ATOM 382 CD1 LEU A 97 -12.204 -2.656 39.225 1.00 74.32 C
ANISOU 382 CD1 LEU A 97 10731 9671 7838 1546 -625 1784 C
ATOM 383 CD2 LEU A 97 -10.647 -1.695 37.582 1.00 66.60 C
ANISOU 383 CD2 LEU A 97 9262 8986 7058 1742 -771 1734 C
ATOM 384 N LEU A 98 -12.873 1.641 41.044 1.00 79.79 N
ANISOU 384 N LEU A 98 10802 11023 8491 723 -861 1248 N
ATOM 385 CA LEU A 98 -12.531 2.245 42.324 1.00 76.91 C
ANISOU 385 CA LEU A 98 10401 10913 7908 611 -962 1245 C
ATOM 386 C LEU A 98 -13.581 1.958 43.393 1.00 83.78 C
ANISOU 386 C LEU A 98 11494 11680 8658 498 -858 1233 C
ATOM 387 O LEU A 98 -13.306 2.130 44.586 1.00 89.62 O
ANISOU 387 O LEU A 98 12264 12610 9179 445 -928 1276 O
ATOM 388 CB LEU A 98 -12.348 3.753 42.128 1.00 72.79 C
ANISOU 388 CB LEU A 98 9707 10526 7422 397 -1034 1049 C
ATOM 389 CG LEU A 98 -12.039 4.608 43.350 1.00 75.93 C
ANISOU 389 CG LEU A 98 10099 11165 7586 209 -1134 995 C
ATOM 390 CD1 LEU A 98 -10.658 4.273 43.849 1.00 70.72 C
ANISOU 390 CD1 LEU A 98 9293 10850 6727 315 -1310 1182 C
ATOM 391 CD2 LEU A 98 -12.201 6.103 43.046 1.00 80.26 C
ANISOU 391 CD2 LEU A 98 10603 11712 8182 -30 -1144 763 C
ATOM 392 N VAL A 99 -14.769 1.501 43.004 1.00 80.89 N
ANISOU 392 N VAL A 99 11276 11048 8410 445 -693 1183 N
ATOM 393 CA VAL A 99 -15.825 1.233 43.971 1.00 81.27 C
ANISOU 393 CA VAL A 99 11511 11032 8336 314 -579 1173 C
ATOM 394 C VAL A 99 -15.981 -0.265 44.210 1.00 81.46 C
ANISOU 394 C VAL A 99 11783 10893 8274 427 -506 1370 C
ATOM 395 O VAL A 99 -16.283 -0.695 45.324 1.00 83.11 O
ANISOU 395 O VAL A 99 12160 11128 8289 382 -473 1451 O
ATOM 396 CB VAL A 99 -17.141 1.881 43.511 1.00 75.94 C
ANISOU 396 CB VAL A 99 10810 10246 7799 133 -439 979 C
ATOM 397 CG1 VAL A 99 -18.342 1.384 44.346 1.00 72.76 C
ANISOU 397 CG1 VAL A 99 10583 9789 7274 3 -291 993 C
ATOM 398 CG2 VAL A 99 -16.998 3.376 43.617 1.00 72.47 C
ANISOU 398 CG2 VAL A 99 10224 9948 7364 37 -497 799 C
ATOM 399 N ASN A 100 -15.761 -1.083 43.188 1.00 79.97 N
ANISOU 399 N ASN A 100 11661 10518 8207 572 -472 1452 N
ATOM 400 CA ASN A 100 -15.888 -2.520 43.403 1.00 79.07 C
ANISOU 400 CA ASN A 100 11865 10197 7981 678 -388 1640 C
ATOM 401 C ASN A 100 -14.732 -3.079 44.225 1.00 83.01 C
ANISOU 401 C ASN A 100 12436 10837 8267 940 -498 1857 C
ATOM 402 O ASN A 100 -14.902 -4.093 44.916 1.00 84.61 O
ANISOU 402 O ASN A 100 12939 10916 8294 1002 -434 2017 O
ATOM 403 CB ASN A 100 -15.979 -3.250 42.069 1.00 79.39 C
ANISOU 403 CB ASN A 100 12015 9968 8181 760 -307 1660 C
ATOM 404 CG ASN A 100 -17.184 -2.839 41.273 1.00 83.08 C
ANISOU 404 CG ASN A 100 12420 10322 8825 498 -196 1473 C
ATOM 405 OD1 ASN A 100 -18.208 -2.444 41.833 1.00 85.02 O
ANISOU 405 OD1 ASN A 100 12648 10624 9030 262 -124 1377 O
ATOM 406 ND2 ASN A 100 -17.075 -2.923 39.957 1.00 82.05 N
ANISOU 406 ND2 ASN A 100 12242 10060 8875 550 -179 1428 N
ATOM 407 N THR A 101 -13.558 -2.444 44.167 1.00 78.41 N
ANISOU 407 N THR A 101 11583 10533 7675 1088 -662 1877 N
ATOM 408 CA THR A 101 -12.376 -2.972 44.840 1.00 80.41 C
ANISOU 408 CA THR A 101 11843 10997 7714 1372 -780 2105 C
ATOM 409 C THR A 101 -12.025 -2.229 46.121 1.00 83.63 C
ANISOU 409 C THR A 101 12109 11749 7916 1258 -911 2099 C
ATOM 410 O THR A 101 -11.473 -2.833 47.042 1.00 78.17 O
ANISOU 410 O THR A 101 11515 11199 6988 1429 -971 2299 O
ATOM 411 CB THR A 101 -11.149 -2.943 43.906 1.00 79.18 C
ANISOU 411 CB THR A 101 11459 10993 7631 1647 -881 2182 C
ATOM 412 OG1 THR A 101 -10.775 -1.586 43.603 1.00 74.53 O
ANISOU 412 OG1 THR A 101 10510 10670 7139 1468 -1000 2010 O
ATOM 413 CG2 THR A 101 -11.417 -3.715 42.606 1.00 77.49 C
ANISOU 413 CG2 THR A 101 11414 10428 7599 1782 -748 2191 C
ATOM 414 N LEU A 102 -12.308 -0.932 46.211 1.00 91.61 N
ANISOU 414 N LEU A 102 12919 12897 8990 981 -956 1881 N
ATOM 415 CA LEU A 102 -11.973 -0.181 47.416 1.00 90.68 C
ANISOU 415 CA LEU A 102 12709 13090 8654 838 -1076 1857 C
ATOM 416 C LEU A 102 -13.166 -0.078 48.366 1.00 88.21 C
ANISOU 416 C LEU A 102 12607 12656 8252 613 -958 1765 C
ATOM 417 O LEU A 102 -13.083 -0.498 49.522 1.00 90.78 O
ANISOU 417 O LEU A 102 13068 13087 8339 634 -983 1889 O
ATOM 418 CB LEU A 102 -11.441 1.206 47.034 1.00 90.41 C
ANISOU 418 CB LEU A 102 12386 13283 8682 665 -1197 1681 C
ATOM 419 CG LEU A 102 -10.798 2.003 48.169 1.00 94.97 C
ANISOU 419 CG LEU A 102 12861 14227 8997 504 -1355 1667 C
ATOM 420 CD1 LEU A 102 -9.740 1.160 48.871 1.00 93.72 C
ANISOU 420 CD1 LEU A 102 12659 14360 8591 747 -1486 1945 C
ATOM 421 CD2 LEU A 102 -10.197 3.303 47.644 1.00 95.96 C
ANISOU 421 CD2 LEU A 102 12745 14543 9171 309 -1469 1503 C
ATOM 422 N CYS A 103 -14.294 0.432 47.882 1.00 81.55 N
ANISOU 422 N CYS A 103 11789 11612 7585 419 -821 1563 N
ATOM 423 CA CYS A 103 -15.437 0.723 48.734 1.00 81.27 C
ANISOU 423 CA CYS A 103 11893 11527 7460 208 -701 1456 C
ATOM 424 C CYS A 103 -16.252 -0.509 49.094 1.00 82.01 C
ANISOU 424 C CYS A 103 12256 11417 7487 222 -554 1586 C
ATOM 425 O CYS A 103 -16.351 -0.863 50.270 1.00 88.61 O
ANISOU 425 O CYS A 103 13248 12328 8093 193 -548 1680 O
ATOM 426 CB CYS A 103 -16.330 1.751 48.054 1.00 83.29 C
ANISOU 426 CB CYS A 103 12050 11692 7905 37 -603 1210 C
ATOM 427 SG CYS A 103 -15.433 3.268 47.760 1.00 92.70 S
ANISOU 427 SG CYS A 103 13016 13082 9124 -35 -758 1047 S
ATOM 428 N LEU A 104 -16.850 -1.150 48.110 1.00 79.17 N
ANISOU 428 N LEU A 104 11973 10803 7305 235 -433 1589 N
ATOM 429 CA LEU A 104 -17.672 -2.330 48.341 1.00 83.21 C
ANISOU 429 CA LEU A 104 12776 11099 7742 184 -282 1702 C
ATOM 430 C LEU A 104 -16.999 -3.411 49.195 1.00 92.64 C
ANISOU 430 C LEU A 104 14219 12280 8699 364 -327 1955 C
ATOM 431 O LEU A 104 -17.702 -4.108 49.935 1.00 96.80 O
ANISOU 431 O LEU A 104 15005 12707 9067 254 -216 2035 O
ATOM 432 CB LEU A 104 -18.119 -2.924 47.006 1.00 80.56 C
ANISOU 432 CB LEU A 104 12499 10498 7613 181 -181 1688 C
ATOM 433 CG LEU A 104 -19.216 -2.114 46.313 1.00 82.72 C
ANISOU 433 CG LEU A 104 12595 10767 8069 -39 -81 1467 C
ATOM 434 CD1 LEU A 104 -19.894 -2.962 45.261 1.00 83.85 C
ANISOU 434 CD1 LEU A 104 12869 10659 8333 -119 44 1484 C
ATOM 435 CD2 LEU A 104 -20.229 -1.589 47.314 1.00 86.48 C
ANISOU 435 CD2 LEU A 104 13061 11384 8413 -251 13 1374 C
ATOM 436 N PRO A 105 -15.674 -3.609 49.131 1.00 92.37 N
ANISOU 436 N PRO A 105 14120 12362 8613 647 -480 2099 N
ATOM 437 CA PRO A 105 -15.068 -4.585 50.055 1.00 90.48 C
ANISOU 437 CA PRO A 105 14117 12149 8111 854 -520 2355 C
ATOM 438 C PRO A 105 -15.142 -4.197 51.528 1.00 96.79 C
ANISOU 438 C PRO A 105 14926 13187 8662 732 -572 2368 C
ATOM 439 O PRO A 105 -15.481 -5.053 52.356 1.00104.80 O
ANISOU 439 O PRO A 105 16242 14101 9476 735 -498 2517 O
ATOM 440 CB PRO A 105 -13.622 -4.672 49.554 1.00 88.59 C
ANISOU 440 CB PRO A 105 13706 12074 7880 1201 -678 2489 C
ATOM 441 CG PRO A 105 -13.747 -4.450 48.121 1.00 85.76 C
ANISOU 441 CG PRO A 105 13223 11555 7805 1195 -633 2361 C
ATOM 442 CD PRO A 105 -14.770 -3.349 47.994 1.00 88.49 C
ANISOU 442 CD PRO A 105 13411 11910 8302 836 -577 2087 C
ATOM 443 N PHE A 106 -14.827 -2.947 51.888 1.00 94.66 N
ANISOU 443 N PHE A 106 14373 13216 8377 612 -693 2219 N
ATOM 444 CA PHE A 106 -14.868 -2.526 53.289 1.00 95.63 C
ANISOU 444 CA PHE A 106 14524 13569 8243 481 -744 2217 C
ATOM 445 C PHE A 106 -16.279 -2.218 53.758 1.00 95.35 C
ANISOU 445 C PHE A 106 14608 13420 8200 190 -568 2056 C
ATOM 446 O PHE A 106 -16.578 -2.373 54.948 1.00 95.05 O
ANISOU 446 O PHE A 106 14724 13465 7924 102 -541 2111 O
ATOM 447 CB PHE A 106 -13.983 -1.299 53.508 1.00 95.42 C
ANISOU 447 CB PHE A 106 14200 13894 8163 425 -934 2112 C
ATOM 448 CG PHE A 106 -12.532 -1.556 53.270 1.00102.10 C
ANISOU 448 CG PHE A 106 14874 14978 8943 692 -1124 2294 C
ATOM 449 CD1 PHE A 106 -11.974 -2.777 53.603 1.00107.38 C
ANISOU 449 CD1 PHE A 106 15702 15649 9448 995 -1149 2582 C
ATOM 450 CD2 PHE A 106 -11.721 -0.587 52.700 1.00102.08 C
ANISOU 450 CD2 PHE A 106 14556 15210 9020 652 -1269 2190 C
ATOM 451 CE1 PHE A 106 -10.628 -3.026 53.383 1.00108.40 C
ANISOU 451 CE1 PHE A 106 15642 16053 9493 1294 -1315 2772 C
ATOM 452 CE2 PHE A 106 -10.375 -0.830 52.473 1.00102.15 C
ANISOU 452 CE2 PHE A 106 14359 15507 8945 896 -1441 2372 C
ATOM 453 CZ PHE A 106 -9.828 -2.048 52.815 1.00104.43 C
ANISOU 453 CZ PHE A 106 14771 15838 9071 1237 -1464 2667 C
ATOM 454 N THR A 107 -17.137 -1.760 52.846 1.00 97.05 N
ANISOU 454 N THR A 107 14734 13483 8656 51 -449 1866 N
ATOM 455 CA THR A 107 -18.554 -1.588 53.153 1.00 97.52 C
ANISOU 455 CA THR A 107 14879 13466 8710 -190 -258 1738 C
ATOM 456 C THR A 107 -19.177 -2.884 53.648 1.00100.08 C
ANISOU 456 C THR A 107 15513 13622 8890 -233 -126 1913 C
ATOM 457 O THR A 107 -19.834 -2.907 54.698 1.00100.35 O
ANISOU 457 O THR A 107 15669 13733 8728 -385 -41 1915 O
ATOM 458 CB THR A 107 -19.290 -1.108 51.912 1.00 95.56 C
ANISOU 458 CB THR A 107 14474 13092 8742 -273 -158 1559 C
ATOM 459 OG1 THR A 107 -18.956 0.284 51.724 1.00104.33 O
ANISOU 459 OG1 THR A 107 15353 14359 9928 -292 -244 1367 O
ATOM 460 CG2 THR A 107 -20.789 -1.258 52.075 1.00 92.65 C
ANISOU 460 CG2 THR A 107 14183 12664 8357 -490 55 1487 C
ATOM 461 N LEU A 108 -18.981 -3.975 52.897 1.00 96.93 N
ANISOU 461 N LEU A 108 15278 12982 8570 -110 -98 2060 N
ATOM 462 CA LEU A 108 -19.491 -5.288 53.294 1.00 98.72 C
ANISOU 462 CA LEU A 108 15878 12994 8637 -163 30 2240 C
ATOM 463 C LEU A 108 -19.161 -5.615 54.745 1.00101.92 C
ANISOU 463 C LEU A 108 16468 13528 8729 -118 -15 2397 C
ATOM 464 O LEU A 108 -20.043 -6.000 55.522 1.00103.45 O
ANISOU 464 O LEU A 108 16861 13690 8754 -325 119 2427 O
ATOM 465 CB LEU A 108 -18.900 -6.347 52.374 1.00 99.51 C
ANISOU 465 CB LEU A 108 16176 12820 8815 56 23 2399 C
ATOM 466 CG LEU A 108 -19.256 -7.816 52.561 1.00101.78 C
ANISOU 466 CG LEU A 108 16942 12795 8936 36 157 2601 C
ATOM 467 CD1 LEU A 108 -20.741 -8.011 52.341 1.00102.71 C
ANISOU 467 CD1 LEU A 108 17155 12788 9084 -363 357 2491 C
ATOM 468 CD2 LEU A 108 -18.434 -8.615 51.562 1.00 99.88 C
ANISOU 468 CD2 LEU A 108 16866 12302 8780 336 128 2733 C
ATOM 469 N THR A 109 -17.887 -5.481 55.125 1.00102.10 N
ANISOU 469 N THR A 109 16413 13727 8652 143 -205 2510 N
ATOM 470 CA THR A 109 -17.468 -5.924 56.451 1.00103.67 C
ANISOU 470 CA THR A 109 16802 14055 8533 225 -264 2698 C
ATOM 471 C THR A 109 -18.012 -5.019 57.553 1.00101.45 C
ANISOU 471 C THR A 109 16425 14019 8103 -20 -252 2555 C
ATOM 472 O THR A 109 -18.234 -5.484 58.675 1.00 98.87 O
ANISOU 472 O THR A 109 16324 13730 7513 -74 -214 2676 O
ATOM 473 CB THR A 109 -15.942 -6.015 56.514 1.00105.63 C
ANISOU 473 CB THR A 109 16945 14495 8694 580 -479 2870 C
ATOM 474 OG1 THR A 109 -15.389 -4.723 56.788 1.00108.79 O
ANISOU 474 OG1 THR A 109 16989 15254 9092 517 -642 2720 O
ATOM 475 CG2 THR A 109 -15.399 -6.507 55.184 1.00101.30 C
ANISOU 475 CG2 THR A 109 16377 13757 8356 827 -490 2931 C
ATOM 476 N TYR A 110 -18.242 -3.736 57.258 1.00103.54 N
ANISOU 476 N TYR A 110 16393 14433 8515 -159 -273 2302 N
ATOM 477 CA TYR A 110 -18.866 -2.852 58.239 1.00103.36 C
ANISOU 477 CA TYR A 110 16326 14601 8345 -378 -224 2147 C
ATOM 478 C TYR A 110 -20.359 -3.116 58.376 1.00101.21 C
ANISOU 478 C TYR A 110 16181 14204 8069 -613 19 2078 C
ATOM 479 O TYR A 110 -20.968 -2.683 59.358 1.00104.66 O
ANISOU 479 O TYR A 110 16656 14787 8323 -769 98 2005 O
ATOM 480 CB TYR A 110 -18.616 -1.387 57.863 1.00101.92 C
ANISOU 480 CB TYR A 110 15849 14583 8292 -430 -308 1902 C
ATOM 481 CG TYR A 110 -19.456 -0.370 58.616 1.00103.30 C
ANISOU 481 CG TYR A 110 16008 14885 8356 -640 -204 1695 C
ATOM 482 CD1 TYR A 110 -19.031 0.154 59.830 1.00107.79 C
ANISOU 482 CD1 TYR A 110 16630 15681 8646 -698 -295 1683 C
ATOM 483 CD2 TYR A 110 -20.667 0.077 58.102 1.00102.71 C
ANISOU 483 CD2 TYR A 110 15868 14722 8436 -765 -11 1516 C
ATOM 484 CE1 TYR A 110 -19.797 1.089 60.517 1.00110.63 C
ANISOU 484 CE1 TYR A 110 17019 16134 8883 -865 -181 1488 C
ATOM 485 CE2 TYR A 110 -21.440 1.006 58.778 1.00106.06 C
ANISOU 485 CE2 TYR A 110 16289 15269 8740 -897 106 1337 C
ATOM 486 CZ TYR A 110 -21.001 1.513 59.981 1.00111.47 C
ANISOU 486 CZ TYR A 110 17068 16138 9149 -942 27 1317 C
ATOM 487 OH TYR A 110 -21.772 2.439 60.649 1.00111.69 O
ANISOU 487 OH TYR A 110 17135 16264 9038 -1050 162 1133 O
ATOM 488 N THR A 111 -20.961 -3.816 57.420 1.00 98.42 N
ANISOU 488 N THR A 111 15892 13612 7892 -655 142 2103 N
ATOM 489 CA THR A 111 -22.379 -4.147 57.492 1.00 98.08 C
ANISOU 489 CA THR A 111 15942 13502 7821 -915 370 2058 C
ATOM 490 C THR A 111 -22.607 -5.486 58.180 1.00100.60 C
ANISOU 490 C THR A 111 16641 13675 7907 -986 454 2290 C
ATOM 491 O THR A 111 -23.476 -5.602 59.050 1.00104.13 O
ANISOU 491 O THR A 111 17195 14212 8159 -1199 591 2293 O
ATOM 492 CB THR A 111 -22.990 -4.184 56.087 1.00 96.82 C
ANISOU 492 CB THR A 111 15654 13192 7943 -988 461 1957 C
ATOM 493 OG1 THR A 111 -22.180 -5.010 55.241 1.00 96.94 O
ANISOU 493 OG1 THR A 111 15792 12968 8071 -808 375 2096 O
ATOM 494 CG2 THR A 111 -23.075 -2.796 55.499 1.00 92.97 C
ANISOU 494 CG2 THR A 111 14817 12852 7654 -961 429 1715 C
ATOM 495 N LEU A 112 -21.834 -6.500 57.788 1.00100.79 N
ANISOU 495 N LEU A 112 16894 13470 7933 -797 384 2489 N
ATOM 496 CA LEU A 112 -22.032 -7.855 58.297 1.00102.52 C
ANISOU 496 CA LEU A 112 17554 13472 7928 -847 479 2721 C
ATOM 497 C LEU A 112 -21.640 -7.958 59.767 1.00107.19 C
ANISOU 497 C LEU A 112 18299 14225 8202 -786 418 2858 C
ATOM 498 O LEU A 112 -22.420 -8.434 60.606 1.00105.24 O
ANISOU 498 O LEU A 112 18284 13968 7734 -1008 557 2924 O
ATOM 499 CB LEU A 112 -21.218 -8.836 57.453 1.00100.44 C
ANISOU 499 CB LEU A 112 17523 12902 7737 -590 425 2895 C
ATOM 500 CG LEU A 112 -21.931 -9.479 56.267 1.00102.88 C
ANISOU 500 CG LEU A 112 17972 12907 8209 -761 571 2862 C
ATOM 501 CD1 LEU A 112 -22.936 -10.485 56.791 1.00106.11 C
ANISOU 501 CD1 LEU A 112 18790 13138 8390 -1083 768 2970 C
ATOM 502 CD2 LEU A 112 -22.615 -8.448 55.365 1.00102.76 C
ANISOU 502 CD2 LEU A 112 17537 13033 8473 -939 605 2593 C
ATOM 503 N MET A 113 -20.422 -7.520 60.090 1.00107.56 N
ANISOU 503 N MET A 113 18211 14450 8207 -501 208 2908 N
ATOM 504 CA MET A 113 -19.935 -7.584 61.460 1.00106.70 C
ANISOU 504 CA MET A 113 18223 14535 7783 -427 121 3046 C
ATOM 505 C MET A 113 -20.637 -6.561 62.343 1.00104.15 C
ANISOU 505 C MET A 113 17732 14484 7357 -681 172 2853 C
ATOM 506 O MET A 113 -20.972 -6.854 63.495 1.00110.00 O
ANISOU 506 O MET A 113 18677 15301 7818 -791 232 2941 O
ATOM 507 CB MET A 113 -18.421 -7.368 61.471 1.00107.62 C
ANISOU 507 CB MET A 113 18191 14831 7870 -73 -129 3154 C
ATOM 508 CG MET A 113 -17.630 -8.471 60.766 1.00109.57 C
ANISOU 508 CG MET A 113 18644 14837 8150 263 -171 3390 C
ATOM 509 SD MET A 113 -15.855 -8.149 60.701 1.00113.65 S
ANISOU 509 SD MET A 113 18886 15670 8624 694 -462 3522 S
ATOM 510 CE MET A 113 -15.211 -9.810 60.473 1.00112.82 C
ANISOU 510 CE MET A 113 19226 15260 8379 1121 -430 3891 C
ATOM 511 N GLY A 114 -20.878 -5.363 61.820 1.00100.37 N
ANISOU 511 N GLY A 114 16913 14139 7084 -763 164 2591 N
ATOM 512 CA GLY A 114 -21.467 -4.292 62.588 1.00104.80 C
ANISOU 512 CA GLY A 114 17335 14942 7543 -946 219 2394 C
ATOM 513 C GLY A 114 -20.470 -3.362 63.242 1.00110.48 C
ANISOU 513 C GLY A 114 17917 15928 8134 -848 15 2338 C
ATOM 514 O GLY A 114 -20.864 -2.288 63.721 1.00111.96 O
ANISOU 514 O GLY A 114 17994 16288 8257 -984 54 2134 O
ATOM 515 N GLU A 115 -19.197 -3.739 63.285 1.00114.91 N
ANISOU 515 N GLU A 115 18489 16545 8627 -620 -194 2518 N
ATOM 516 CA GLU A 115 -18.142 -2.911 63.847 1.00111.56 C
ANISOU 516 CA GLU A 115 17908 16423 8055 -560 -414 2485 C
ATOM 517 C GLU A 115 -17.187 -2.487 62.740 1.00105.45 C
ANISOU 517 C GLU A 115 16867 15683 7515 -401 -579 2443 C
ATOM 518 O GLU A 115 -16.846 -3.285 61.861 1.00103.47 O
ANISOU 518 O GLU A 115 16629 15258 7428 -202 -592 2582 O
ATOM 519 CB GLU A 115 -17.378 -3.657 64.954 1.00111.31 C
ANISOU 519 CB GLU A 115 18064 16546 7684 -428 -541 2756 C
ATOM 520 CG GLU A 115 -16.047 -3.007 65.334 1.00115.21 C
ANISOU 520 CG GLU A 115 18355 17398 8023 -334 -813 2783 C
ATOM 521 CD GLU A 115 -15.452 -3.549 66.619 1.00123.42 C
ANISOU 521 CD GLU A 115 19557 18665 8673 -250 -931 3021 C
ATOM 522 OE1 GLU A 115 -14.532 -2.900 67.165 1.00125.26 O
ANISOU 522 OE1 GLU A 115 19627 19259 8708 -265 -1143 3019 O
ATOM 523 OE2 GLU A 115 -15.902 -4.616 67.087 1.00127.97 O
ANISOU 523 OE2 GLU A 115 20433 19070 9119 -189 -814 3215 O
ATOM 524 N TRP A 116 -16.774 -1.221 62.781 1.00102.11 N
ANISOU 524 N TRP A 116 16231 15475 7092 -502 -693 2245 N
ATOM 525 CA TRP A 116 -15.743 -0.705 61.886 1.00102.58 C
ANISOU 525 CA TRP A 116 16024 15638 7312 -395 -873 2207 C
ATOM 526 C TRP A 116 -14.371 -1.116 62.421 1.00107.03 C
ANISOU 526 C TRP A 116 16531 16499 7637 -214 -1114 2449 C
ATOM 527 O TRP A 116 -13.890 -0.568 63.420 1.00106.14 O
ANISOU 527 O TRP A 116 16397 16690 7241 -331 -1245 2437 O
ATOM 528 CB TRP A 116 -15.876 0.812 61.751 1.00 97.54 C
ANISOU 528 CB TRP A 116 15237 15095 6729 -613 -886 1903 C
ATOM 529 CG TRP A 116 -14.865 1.442 60.816 1.00 97.53 C
ANISOU 529 CG TRP A 116 14970 15205 6883 -565 -1062 1844 C
ATOM 530 CD1 TRP A 116 -13.716 2.076 61.175 1.00100.32 C
ANISOU 530 CD1 TRP A 116 15179 15889 7049 -628 -1290 1849 C
ATOM 531 CD2 TRP A 116 -14.917 1.496 59.379 1.00 95.43 C
ANISOU 531 CD2 TRP A 116 14549 14745 6966 -474 -1024 1776 C
ATOM 532 NE1 TRP A 116 -13.051 2.527 60.063 1.00 96.50 N
ANISOU 532 NE1 TRP A 116 14457 15436 6774 -590 -1390 1790 N
ATOM 533 CE2 TRP A 116 -13.761 2.178 58.946 1.00 94.92 C
ANISOU 533 CE2 TRP A 116 14250 14904 6910 -479 -1229 1745 C
ATOM 534 CE3 TRP A 116 -15.826 1.032 58.417 1.00 94.47 C
ANISOU 534 CE3 TRP A 116 14459 14305 7131 -413 -839 1741 C
ATOM 535 CZ2 TRP A 116 -13.483 2.404 57.597 1.00 93.35 C
ANISOU 535 CZ2 TRP A 116 13859 14604 7004 -403 -1248 1683 C
ATOM 536 CZ3 TRP A 116 -15.548 1.259 57.071 1.00 89.45 C
ANISOU 536 CZ3 TRP A 116 13636 13566 6786 -333 -865 1676 C
ATOM 537 CH2 TRP A 116 -14.392 1.945 56.679 1.00 90.63 C
ANISOU 537 CH2 TRP A 116 13564 13925 6945 -320 -1063 1646 C
ATOM 538 N LYS A 117 -13.739 -2.082 61.757 1.00107.49 N
ANISOU 538 N LYS A 117 16566 16489 7787 83 -1169 2673 N
ATOM 539 CA LYS A 117 -12.498 -2.675 62.228 1.00108.92 C
ANISOU 539 CA LYS A 117 16699 16961 7726 342 -1371 2955 C
ATOM 540 C LYS A 117 -11.258 -2.144 61.512 1.00110.86 C
ANISOU 540 C LYS A 117 16582 17501 8040 454 -1584 2963 C
ATOM 541 O LYS A 117 -10.140 -2.544 61.859 1.00111.37 O
ANISOU 541 O LYS A 117 16531 17899 7887 684 -1768 3203 O
ATOM 542 CB LYS A 117 -12.573 -4.199 62.089 1.00108.04 C
ANISOU 542 CB LYS A 117 16862 16589 7601 655 -1275 3240 C
ATOM 543 N MET A 118 -11.419 -1.258 60.528 1.00109.52 N
ANISOU 543 N MET A 118 16222 17246 8146 304 -1562 2719 N
ATOM 544 CA MET A 118 -10.280 -0.648 59.857 1.00111.56 C
ANISOU 544 CA MET A 118 16132 17801 8455 346 -1757 2705 C
ATOM 545 C MET A 118 -9.918 0.659 60.565 1.00113.36 C
ANISOU 545 C MET A 118 16226 18372 8472 -3 -1902 2523 C
ATOM 546 O MET A 118 -10.458 0.983 61.626 1.00115.60 O
ANISOU 546 O MET A 118 16698 18675 8551 -216 -1859 2439 O
ATOM 547 CB MET A 118 -10.574 -0.448 58.369 1.00109.85 C
ANISOU 547 CB MET A 118 15808 17300 8630 378 -1659 2560 C
ATOM 548 CG MET A 118 -10.609 -1.742 57.561 1.00113.30 C
ANISOU 548 CG MET A 118 16357 17458 9235 736 -1559 2762 C
ATOM 549 SD MET A 118 -11.993 -2.818 57.994 1.00118.32 S
ANISOU 549 SD MET A 118 17446 17638 9872 736 -1300 2820 S
ATOM 550 CE MET A 118 -13.383 -1.761 57.600 1.00110.06 C
ANISOU 550 CE MET A 118 16398 16351 9069 347 -1121 2449 C
ATOM 551 N GLY A 119 -8.995 1.432 59.983 1.00113.32 N
ANISOU 551 N GLY A 119 15918 18643 8497 -85 -2069 2457 N
ATOM 552 CA GLY A 119 -8.481 2.599 60.645 1.00114.89 C
ANISOU 552 CA GLY A 119 16015 19195 8444 -439 -2230 2313 C
ATOM 553 C GLY A 119 -9.464 3.759 60.633 1.00113.07 C
ANISOU 553 C GLY A 119 15964 18685 8312 -790 -2084 1959 C
ATOM 554 O GLY A 119 -10.568 3.667 60.085 1.00115.73 O
ANISOU 554 O GLY A 119 16455 18594 8923 -745 -1861 1833 O
ATOM 555 N PRO A 120 -9.069 4.871 61.263 1.00106.29 N
ANISOU 555 N PRO A 120 15103 18084 7200 -1144 -2206 1801 N
ATOM 556 CA PRO A 120 -9.852 6.106 61.122 1.00103.00 C
ANISOU 556 CA PRO A 120 14873 17402 6861 -1449 -2071 1459 C
ATOM 557 C PRO A 120 -9.562 6.862 59.839 1.00104.54 C
ANISOU 557 C PRO A 120 14902 17508 7310 -1528 -2089 1305 C
ATOM 558 O PRO A 120 -10.368 7.722 59.455 1.00104.78 O
ANISOU 558 O PRO A 120 15105 17221 7486 -1671 -1930 1043 O
ATOM 559 CB PRO A 120 -9.435 6.943 62.343 1.00 99.62 C
ANISOU 559 CB PRO A 120 14565 17280 6007 -1807 -2203 1366 C
ATOM 560 CG PRO A 120 -8.325 6.183 63.013 1.00103.56 C
ANISOU 560 CG PRO A 120 14840 18157 6352 -1653 -2394 1630 C
ATOM 561 CD PRO A 120 -7.893 5.065 62.122 1.00104.68 C
ANISOU 561 CD PRO A 120 14740 18355 6679 -1262 -2439 1901 C
ATOM 562 N VAL A 121 -8.430 6.595 59.182 1.00104.11 N
ANISOU 562 N VAL A 121 14522 17743 7291 -1428 -2272 1466 N
ATOM 563 CA VAL A 121 -8.182 7.207 57.882 1.00101.91 C
ANISOU 563 CA VAL A 121 14083 17366 7274 -1481 -2275 1339 C
ATOM 564 C VAL A 121 -9.176 6.676 56.857 1.00 97.36 C
ANISOU 564 C VAL A 121 13566 16315 7110 -1206 -2050 1306 C
ATOM 565 O VAL A 121 -9.769 7.446 56.094 1.00 95.66 O
ANISOU 565 O VAL A 121 13427 15808 7111 -1312 -1927 1081 O
ATOM 566 CB VAL A 121 -6.721 6.980 57.448 1.00105.21 C
ANISOU 566 CB VAL A 121 14107 18260 7607 -1422 -2517 1541 C
ATOM 567 CG1 VAL A 121 -6.378 5.495 57.425 1.00110.28 C
ANISOU 567 CG1 VAL A 121 14599 19020 8281 -959 -2544 1877 C
ATOM 568 CG2 VAL A 121 -6.470 7.603 56.095 1.00101.78 C
ANISOU 568 CG2 VAL A 121 13511 17726 7436 -1489 -2511 1413 C
ATOM 569 N LEU A 122 -9.414 5.359 56.860 1.00 96.91 N
ANISOU 569 N LEU A 122 13511 16169 7142 -863 -1986 1530 N
ATOM 570 CA LEU A 122 -10.353 4.762 55.918 1.00 94.05 C
ANISOU 570 CA LEU A 122 13221 15380 7135 -643 -1779 1512 C
ATOM 571 C LEU A 122 -11.791 5.175 56.207 1.00 95.49 C
ANISOU 571 C LEU A 122 13678 15218 7387 -773 -1552 1300 C
ATOM 572 O LEU A 122 -12.594 5.288 55.275 1.00 99.85 O
ANISOU 572 O LEU A 122 14252 15458 8228 -726 -1392 1178 O
ATOM 573 CB LEU A 122 -10.219 3.242 55.940 1.00 94.41 C
ANISOU 573 CB LEU A 122 13272 15403 7198 -281 -1764 1808 C
ATOM 574 CG LEU A 122 -8.865 2.682 55.482 1.00 98.08 C
ANISOU 574 CG LEU A 122 13456 16188 7621 -34 -1949 2048 C
ATOM 575 CD1 LEU A 122 -8.900 1.160 55.451 1.00100.88 C
ANISOU 575 CD1 LEU A 122 13922 16411 7997 366 -1881 2326 C
ATOM 576 CD2 LEU A 122 -8.459 3.226 54.118 1.00 97.48 C
ANISOU 576 CD2 LEU A 122 13149 16088 7802 -46 -1976 1943 C
ATOM 577 N CYS A 123 -12.131 5.407 57.478 1.00 95.53 N
ANISOU 577 N CYS A 123 13878 15303 7115 -927 -1532 1260 N
ATOM 578 CA CYS A 123 -13.466 5.885 57.832 1.00 96.52 C
ANISOU 578 CA CYS A 123 14249 15162 7263 -1038 -1309 1059 C
ATOM 579 C CYS A 123 -13.785 7.204 57.134 1.00 93.58 C
ANISOU 579 C CYS A 123 13897 14634 7024 -1202 -1241 778 C
ATOM 580 O CYS A 123 -14.954 7.502 56.863 1.00 95.11 O
ANISOU 580 O CYS A 123 14214 14560 7362 -1181 -1026 627 O
ATOM 581 CB CYS A 123 -13.565 6.003 59.364 1.00104.47 C
ANISOU 581 CB CYS A 123 15454 16339 7900 -1186 -1325 1066 C
ATOM 582 SG CYS A 123 -14.958 6.939 60.081 1.00110.24 S
ANISOU 582 SG CYS A 123 16496 16862 8527 -1363 -1079 790 S
ATOM 583 N HIS A 124 -12.764 7.997 56.822 1.00 90.55 N
ANISOU 583 N HIS A 124 13396 14429 6579 -1362 -1417 715 N
ATOM 584 CA HIS A 124 -12.952 9.206 56.036 1.00 90.30 C
ANISOU 584 CA HIS A 124 13410 14223 6676 -1507 -1360 469 C
ATOM 585 C HIS A 124 -12.922 8.940 54.530 1.00 95.82 C
ANISOU 585 C HIS A 124 13898 14765 7744 -1330 -1335 496 C
ATOM 586 O HIS A 124 -13.604 9.630 53.763 1.00 93.65 O
ANISOU 586 O HIS A 124 13691 14230 7661 -1336 -1196 314 O
ATOM 587 CB HIS A 124 -11.864 10.230 56.389 1.00 88.70 C
ANISOU 587 CB HIS A 124 13218 14280 6203 -1830 -1557 380 C
ATOM 588 CG HIS A 124 -12.053 10.889 57.714 1.00 95.58 C
ANISOU 588 CG HIS A 124 14383 15221 6712 -2074 -1544 259 C
ATOM 589 ND1 HIS A 124 -12.612 12.140 57.849 1.00 96.75 N
ANISOU 589 ND1 HIS A 124 14845 15147 6768 -2268 -1415 -16 N
ATOM 590 CD2 HIS A 124 -11.732 10.483 58.965 1.00 99.02 C
ANISOU 590 CD2 HIS A 124 14871 15921 6831 -2147 -1641 376 C
ATOM 591 CE1 HIS A 124 -12.634 12.473 59.128 1.00 99.15 C
ANISOU 591 CE1 HIS A 124 15393 15565 6714 -2461 -1427 -73 C
ATOM 592 NE2 HIS A 124 -12.106 11.484 59.827 1.00 97.92 N
ANISOU 592 NE2 HIS A 124 15070 15716 6419 -2404 -1570 162 N
ATOM 593 N LEU A 125 -12.142 7.952 54.089 1.00 94.76 N
ANISOU 593 N LEU A 125 13521 14786 7697 -1149 -1460 724 N
ATOM 594 CA LEU A 125 -11.751 7.908 52.686 1.00 90.17 C
ANISOU 594 CA LEU A 125 12725 14136 7398 -1041 -1489 738 C
ATOM 595 C LEU A 125 -12.722 7.095 51.843 1.00 88.01 C
ANISOU 595 C LEU A 125 12458 13544 7439 -792 -1305 775 C
ATOM 596 O LEU A 125 -12.962 7.420 50.678 1.00 84.80 O
ANISOU 596 O LEU A 125 11977 12954 7288 -755 -1242 678 O
ATOM 597 CB LEU A 125 -10.329 7.371 52.569 1.00 89.65 C
ANISOU 597 CB LEU A 125 12386 14437 7240 -964 -1715 958 C
ATOM 598 CG LEU A 125 -9.261 8.412 52.228 1.00 88.31 C
ANISOU 598 CG LEU A 125 12057 14528 6969 -1223 -1890 873 C
ATOM 599 CD1 LEU A 125 -7.909 7.747 52.183 1.00 94.64 C
ANISOU 599 CD1 LEU A 125 12539 15768 7652 -1101 -2102 1128 C
ATOM 600 CD2 LEU A 125 -9.578 9.005 50.883 1.00 90.83 C
ANISOU 600 CD2 LEU A 125 12346 14575 7591 -1232 -1798 713 C
ATOM 601 N VAL A 126 -13.286 6.037 52.400 1.00 88.94 N
ANISOU 601 N VAL A 126 12675 13595 7523 -644 -1218 915 N
ATOM 602 CA VAL A 126 -14.222 5.206 51.652 1.00 87.19 C
ANISOU 602 CA VAL A 126 12484 13088 7556 -469 -1045 955 C
ATOM 603 C VAL A 126 -15.517 5.950 51.334 1.00 88.84 C
ANISOU 603 C VAL A 126 12794 13064 7898 -560 -846 731 C
ATOM 604 O VAL A 126 -16.027 5.811 50.214 1.00 87.77 O
ANISOU 604 O VAL A 126 12587 12737 8025 -477 -750 691 O
ATOM 605 CB VAL A 126 -14.501 3.897 52.396 1.00 88.06 C
ANISOU 605 CB VAL A 126 12725 13182 7552 -336 -996 1165 C
ATOM 606 CG1 VAL A 126 -15.484 3.112 51.625 1.00 88.14 C
ANISOU 606 CG1 VAL A 126 12798 12902 7791 -233 -816 1187 C
ATOM 607 CG2 VAL A 126 -13.219 3.121 52.530 1.00 91.38 C
ANISOU 607 CG2 VAL A 126 13039 13824 7858 -160 -1178 1409 C
ATOM 608 N PRO A 127 -16.096 6.740 52.246 1.00 90.16 N
ANISOU 608 N PRO A 127 13124 13249 7882 -709 -769 585 N
ATOM 609 CA PRO A 127 -17.224 7.595 51.821 1.00 89.08 C
ANISOU 609 CA PRO A 127 13060 12925 7863 -740 -581 373 C
ATOM 610 C PRO A 127 -16.829 8.652 50.799 1.00 83.85 C
ANISOU 610 C PRO A 127 12323 12192 7346 -783 -628 220 C
ATOM 611 O PRO A 127 -17.640 9.014 49.933 1.00 80.97 O
ANISOU 611 O PRO A 127 11936 11649 7179 -714 -489 111 O
ATOM 612 CB PRO A 127 -17.700 8.228 53.140 1.00 86.91 C
ANISOU 612 CB PRO A 127 13005 12717 7300 -864 -505 266 C
ATOM 613 CG PRO A 127 -16.563 8.069 54.097 1.00 86.46 C
ANISOU 613 CG PRO A 127 12974 12896 6980 -969 -706 373 C
ATOM 614 CD PRO A 127 -15.935 6.758 53.714 1.00 86.49 C
ANISOU 614 CD PRO A 127 12810 12963 7090 -815 -814 622 C
ATOM 615 N TYR A 128 -15.603 9.164 50.881 1.00 81.59 N
ANISOU 615 N TYR A 128 11992 12063 6944 -910 -821 216 N
ATOM 616 CA TYR A 128 -15.114 10.091 49.869 1.00 81.53 C
ANISOU 616 CA TYR A 128 11918 11997 7063 -981 -878 92 C
ATOM 617 C TYR A 128 -14.912 9.388 48.530 1.00 87.48 C
ANISOU 617 C TYR A 128 12439 12679 8121 -810 -899 196 C
ATOM 618 O TYR A 128 -15.350 9.886 47.489 1.00 93.70 O
ANISOU 618 O TYR A 128 13200 13286 9117 -771 -814 84 O
ATOM 619 CB TYR A 128 -13.819 10.717 50.356 1.00 84.03 C
ANISOU 619 CB TYR A 128 12231 12558 7140 -1212 -1088 83 C
ATOM 620 CG TYR A 128 -13.158 11.656 49.403 1.00 87.51 C
ANISOU 620 CG TYR A 128 12613 12977 7659 -1347 -1168 -27 C
ATOM 621 CD1 TYR A 128 -13.788 12.829 49.003 1.00 90.28 C
ANISOU 621 CD1 TYR A 128 13177 13078 8048 -1424 -1037 -252 C
ATOM 622 CD2 TYR A 128 -11.881 11.399 48.930 1.00 91.82 C
ANISOU 622 CD2 TYR A 128 12904 13772 8212 -1394 -1368 100 C
ATOM 623 CE1 TYR A 128 -13.180 13.707 48.141 1.00 89.59 C
ANISOU 623 CE1 TYR A 128 13079 12949 8012 -1569 -1104 -351 C
ATOM 624 CE2 TYR A 128 -11.261 12.275 48.063 1.00 93.99 C
ANISOU 624 CE2 TYR A 128 13125 14048 8540 -1555 -1438 1 C
ATOM 625 CZ TYR A 128 -11.916 13.425 47.676 1.00 90.85 C
ANISOU 625 CZ TYR A 128 12973 13363 8183 -1658 -1307 -227 C
ATOM 626 OH TYR A 128 -11.300 14.300 46.827 1.00 92.32 O
ANISOU 626 OH TYR A 128 13147 13529 8403 -1837 -1371 -321 O
ATOM 627 N ALA A 129 -14.251 8.226 48.536 1.00 87.34 N
ANISOU 627 N ALA A 129 12273 12797 8116 -688 -1003 415 N
ATOM 628 CA ALA A 129 -14.069 7.464 47.306 1.00 86.36 C
ANISOU 628 CA ALA A 129 11974 12585 8255 -505 -1005 520 C
ATOM 629 C ALA A 129 -15.386 6.979 46.714 1.00 86.92 C
ANISOU 629 C ALA A 129 12100 12389 8537 -392 -803 489 C
ATOM 630 O ALA A 129 -15.421 6.645 45.525 1.00 91.87 O
ANISOU 630 O ALA A 129 12616 12895 9397 -287 -779 510 O
ATOM 631 CB ALA A 129 -13.161 6.260 47.549 1.00 87.84 C
ANISOU 631 CB ALA A 129 12056 12951 8369 -346 -1129 774 C
ATOM 632 N GLN A 130 -16.458 6.897 47.513 1.00 84.70 N
ANISOU 632 N GLN A 130 11976 12047 8161 -425 -660 448 N
ATOM 633 CA GLN A 130 -17.755 6.547 46.943 1.00 84.94 C
ANISOU 633 CA GLN A 130 12020 11892 8360 -363 -468 411 C
ATOM 634 C GLN A 130 -18.420 7.765 46.311 1.00 84.12 C
ANISOU 634 C GLN A 130 11909 11691 8361 -394 -369 202 C
ATOM 635 O GLN A 130 -18.918 7.698 45.179 1.00 80.50 O
ANISOU 635 O GLN A 130 11351 11112 8122 -324 -296 172 O
ATOM 636 CB GLN A 130 -18.682 5.936 47.998 1.00 82.80 C
ANISOU 636 CB GLN A 130 11890 11637 7933 -390 -340 466 C
ATOM 637 CG GLN A 130 -18.515 4.443 48.117 1.00 86.12 C
ANISOU 637 CG GLN A 130 12347 12031 8345 -315 -356 685 C
ATOM 638 CD GLN A 130 -19.816 3.666 48.217 1.00 91.47 C
ANISOU 638 CD GLN A 130 13110 12614 9032 -352 -167 723 C
ATOM 639 OE1 GLN A 130 -20.869 4.112 47.757 1.00 93.28 O
ANISOU 639 OE1 GLN A 130 13283 12803 9358 -396 -25 600 O
ATOM 640 NE2 GLN A 130 -19.740 2.478 48.821 1.00 94.01 N
ANISOU 640 NE2 GLN A 130 13571 12917 9231 -338 -164 907 N
ATOM 641 N GLY A 131 -18.456 8.885 47.035 1.00 83.85 N
ANISOU 641 N GLY A 131 12009 11699 8150 -489 -356 58 N
ATOM 642 CA GLY A 131 -19.013 10.088 46.450 1.00 83.08 C
ANISOU 642 CA GLY A 131 11961 11484 8121 -479 -255 -132 C
ATOM 643 C GLY A 131 -18.228 10.547 45.243 1.00 78.29 C
ANISOU 643 C GLY A 131 11244 10811 7690 -484 -362 -169 C
ATOM 644 O GLY A 131 -18.798 11.066 44.289 1.00 78.28 O
ANISOU 644 O GLY A 131 11213 10680 7850 -409 -269 -262 O
ATOM 645 N LEU A 132 -16.920 10.328 45.254 1.00 78.53 N
ANISOU 645 N LEU A 132 11195 10962 7681 -563 -556 -81 N
ATOM 646 CA LEU A 132 -16.093 10.724 44.127 1.00 77.78 C
ANISOU 646 CA LEU A 132 10973 10845 7733 -586 -661 -102 C
ATOM 647 C LEU A 132 -16.504 9.978 42.861 1.00 76.55 C
ANISOU 647 C LEU A 132 10651 10571 7865 -420 -602 -35 C
ATOM 648 O LEU A 132 -16.509 10.547 41.764 1.00 73.19 O
ANISOU 648 O LEU A 132 10169 10040 7601 -402 -587 -116 O
ATOM 649 CB LEU A 132 -14.627 10.467 44.479 1.00 75.79 C
ANISOU 649 CB LEU A 132 10616 10830 7350 -686 -877 15 C
ATOM 650 CG LEU A 132 -13.611 10.755 43.400 1.00 76.66 C
ANISOU 650 CG LEU A 132 10553 10999 7577 -723 -1002 27 C
ATOM 651 CD1 LEU A 132 -13.496 12.232 43.282 1.00 75.70 C
ANISOU 651 CD1 LEU A 132 10585 10807 7369 -931 -1003 -169 C
ATOM 652 CD2 LEU A 132 -12.298 10.124 43.784 1.00 81.16 C
ANISOU 652 CD2 LEU A 132 10947 11876 8014 -741 -1194 206 C
ATOM 653 N ALA A 133 -16.893 8.714 43.003 1.00 74.90 N
ANISOU 653 N ALA A 133 10394 10363 7700 -315 -557 108 N
ATOM 654 CA ALA A 133 -17.219 7.901 41.843 1.00 70.28 C
ANISOU 654 CA ALA A 133 9691 9662 7351 -195 -507 178 C
ATOM 655 C ALA A 133 -18.526 8.339 41.194 1.00 73.24 C
ANISOU 655 C ALA A 133 10068 9906 7855 -166 -338 57 C
ATOM 656 O ALA A 133 -18.598 8.488 39.970 1.00 77.11 O
ANISOU 656 O ALA A 133 10457 10305 8538 -117 -326 23 O
ATOM 657 CB ALA A 133 -17.284 6.435 42.250 1.00 72.01 C
ANISOU 657 CB ALA A 133 9936 9890 7536 -122 -495 363 C
ATOM 658 N VAL A 134 -19.583 8.534 41.987 1.00 73.10 N
ANISOU 658 N VAL A 134 10148 9907 7719 -184 -202 3 N
ATOM 659 CA VAL A 134 -20.864 8.880 41.379 1.00 74.41 C
ANISOU 659 CA VAL A 134 10270 10021 7983 -124 -37 -84 C
ATOM 660 C VAL A 134 -20.797 10.240 40.689 1.00 78.61 C
ANISOU 660 C VAL A 134 10819 10476 8575 -83 -29 -238 C
ATOM 661 O VAL A 134 -21.501 10.472 39.696 1.00 83.74 O
ANISOU 661 O VAL A 134 11375 11073 9369 2 56 -281 O
ATOM 662 CB VAL A 134 -21.984 8.825 42.426 1.00 75.75 C
ANISOU 662 CB VAL A 134 10518 10282 7982 -133 117 -98 C
ATOM 663 CG1 VAL A 134 -21.544 9.554 43.666 1.00 85.33 C
ANISOU 663 CG1 VAL A 134 11910 11546 8964 -184 83 -163 C
ATOM 664 CG2 VAL A 134 -23.282 9.431 41.867 1.00 73.86 C
ANISOU 664 CG2 VAL A 134 10204 10062 7796 -37 291 -193 C
ATOM 665 N GLN A 135 -19.938 11.150 41.168 1.00 75.16 N
ANISOU 665 N GLN A 135 10516 10032 8011 -158 -120 -316 N
ATOM 666 CA GLN A 135 -19.786 12.420 40.465 1.00 73.49 C
ANISOU 666 CA GLN A 135 10377 9706 7838 -146 -114 -456 C
ATOM 667 C GLN A 135 -19.011 12.258 39.158 1.00 72.45 C
ANISOU 667 C GLN A 135 10089 9523 7916 -152 -226 -417 C
ATOM 668 O GLN A 135 -19.395 12.845 38.138 1.00 72.40 O
ANISOU 668 O GLN A 135 10060 9409 8040 -74 -167 -489 O
ATOM 669 CB GLN A 135 -19.121 13.463 41.354 1.00 77.75 C
ANISOU 669 CB GLN A 135 11157 10239 8146 -283 -170 -562 C
ATOM 670 CG GLN A 135 -19.561 13.456 42.794 1.00 88.66 C
ANISOU 670 CG GLN A 135 12701 11698 9287 -312 -100 -578 C
ATOM 671 CD GLN A 135 -20.725 14.372 43.067 1.00 97.10 C
ANISOU 671 CD GLN A 135 13961 12680 10253 -178 107 -713 C
ATOM 672 OE1 GLN A 135 -21.888 14.007 42.856 1.00 97.68 O
ANISOU 672 OE1 GLN A 135 13921 12792 10402 -10 260 -685 O
ATOM 673 NE2 GLN A 135 -20.424 15.570 43.567 1.00100.63 N
ANISOU 673 NE2 GLN A 135 14712 13025 10498 -255 120 -856 N
ATOM 674 N VAL A 136 -17.916 11.479 39.153 1.00 71.38 N
ANISOU 674 N VAL A 136 9843 9476 7802 -219 -381 -297 N
ATOM 675 CA VAL A 136 -17.199 11.290 37.888 1.00 67.99 C
ANISOU 675 CA VAL A 136 9255 9015 7562 -199 -469 -255 C
ATOM 676 C VAL A 136 -18.089 10.559 36.899 1.00 72.26 C
ANISOU 676 C VAL A 136 9676 9470 8308 -68 -368 -213 C
ATOM 677 O VAL A 136 -18.053 10.832 35.696 1.00 79.08 O
ANISOU 677 O VAL A 136 10458 10252 9335 -27 -367 -246 O
ATOM 678 CB VAL A 136 -15.850 10.554 38.058 1.00 64.80 C
ANISOU 678 CB VAL A 136 8736 8764 7120 -242 -640 -115 C
ATOM 679 CG1 VAL A 136 -14.854 11.348 38.829 1.00 63.35 C
ANISOU 679 CG1 VAL A 136 8622 8722 6725 -420 -766 -154 C
ATOM 680 CG2 VAL A 136 -16.036 9.248 38.706 1.00 75.96 C
ANISOU 680 CG2 VAL A 136 10131 10236 8493 -163 -627 33 C
ATOM 681 N SER A 137 -18.906 9.626 37.386 1.00 70.71 N
ANISOU 681 N SER A 137 9477 9299 8089 -29 -282 -138 N
ATOM 682 CA SER A 137 -19.842 8.946 36.502 1.00 67.81 C
ANISOU 682 CA SER A 137 9013 8877 7876 34 -181 -105 C
ATOM 683 C SER A 137 -20.835 9.931 35.901 1.00 70.50 C
ANISOU 683 C SER A 137 9332 9185 8271 95 -65 -229 C
ATOM 684 O SER A 137 -21.032 9.970 34.685 1.00 71.53 O
ANISOU 684 O SER A 137 9358 9258 8562 142 -53 -243 O
ATOM 685 CB SER A 137 -20.571 7.845 37.267 1.00 72.08 C
ANISOU 685 CB SER A 137 9589 9469 8331 5 -102 -7 C
ATOM 686 OG SER A 137 -19.721 6.730 37.475 1.00 78.28 O
ANISOU 686 OG SER A 137 10403 10242 9099 1 -194 136 O
ATOM 687 N THR A 138 -21.458 10.754 36.746 1.00 80.42 N
ANISOU 687 N THR A 138 10699 10482 9374 119 26 -316 N
ATOM 688 CA THR A 138 -22.469 11.691 36.270 1.00 77.81 C
ANISOU 688 CA THR A 138 10366 10141 9057 243 160 -417 C
ATOM 689 C THR A 138 -21.867 12.747 35.348 1.00 75.32 C
ANISOU 689 C THR A 138 10103 9689 8825 279 105 -506 C
ATOM 690 O THR A 138 -22.469 13.117 34.330 1.00 68.88 O
ANISOU 690 O THR A 138 9209 8845 8119 392 170 -537 O
ATOM 691 CB THR A 138 -23.159 12.336 37.464 1.00 71.50 C
ANISOU 691 CB THR A 138 9716 9408 8043 296 281 -485 C
ATOM 692 OG1 THR A 138 -23.856 11.319 38.194 1.00 69.92 O
ANISOU 692 OG1 THR A 138 9442 9355 7771 252 348 -394 O
ATOM 693 CG2 THR A 138 -24.146 13.403 36.997 1.00 70.45 C
ANISOU 693 CG2 THR A 138 9607 9269 7892 492 431 -581 C
ATOM 694 N ILE A 139 -20.667 13.230 35.672 1.00 76.06 N
ANISOU 694 N ILE A 139 10325 9721 8854 167 -18 -541 N
ATOM 695 CA ILE A 139 -19.976 14.128 34.748 1.00 74.16 C
ANISOU 695 CA ILE A 139 10136 9357 8685 145 -82 -611 C
ATOM 696 C ILE A 139 -19.615 13.402 33.444 1.00 67.20 C
ANISOU 696 C ILE A 139 9036 8468 8028 154 -153 -531 C
ATOM 697 O ILE A 139 -19.816 13.943 32.351 1.00 66.22 O
ANISOU 697 O ILE A 139 8887 8257 8016 224 -124 -576 O
ATOM 698 CB ILE A 139 -18.749 14.766 35.435 1.00 66.99 C
ANISOU 698 CB ILE A 139 9399 8436 7618 -42 -205 -658 C
ATOM 699 CG1 ILE A 139 -19.210 15.859 36.394 1.00 68.67 C
ANISOU 699 CG1 ILE A 139 9913 8576 7604 -39 -103 -785 C
ATOM 700 CG2 ILE A 139 -17.795 15.358 34.420 1.00 61.95 C
ANISOU 700 CG2 ILE A 139 8755 7722 7061 -136 -305 -690 C
ATOM 701 CD1 ILE A 139 -18.223 16.183 37.463 1.00 71.01 C
ANISOU 701 CD1 ILE A 139 10378 8920 7683 -264 -214 -814 C
ATOM 702 N THR A 140 -19.124 12.161 33.528 1.00 61.37 N
ANISOU 702 N THR A 140 8165 7809 7345 107 -233 -409 N
ATOM 703 CA THR A 140 -18.706 11.445 32.321 1.00 59.84 C
ANISOU 703 CA THR A 140 7809 7589 7339 128 -290 -336 C
ATOM 704 C THR A 140 -19.889 11.109 31.409 1.00 62.42 C
ANISOU 704 C THR A 140 8036 7886 7794 220 -178 -334 C
ATOM 705 O THR A 140 -19.770 11.189 30.182 1.00 64.93 O
ANISOU 705 O THR A 140 8271 8145 8256 252 -195 -341 O
ATOM 706 CB THR A 140 -17.950 10.166 32.679 1.00 58.68 C
ANISOU 706 CB THR A 140 7597 7513 7185 103 -377 -196 C
ATOM 707 OG1 THR A 140 -16.780 10.488 33.451 1.00 60.70 O
ANISOU 707 OG1 THR A 140 7894 7863 7306 18 -499 -181 O
ATOM 708 CG2 THR A 140 -17.545 9.416 31.413 1.00 58.65 C
ANISOU 708 CG2 THR A 140 7469 7459 7355 156 -412 -125 C
ATOM 709 N LEU A 141 -21.032 10.725 31.974 1.00 63.83 N
ANISOU 709 N LEU A 141 8207 8137 7907 246 -66 -318 N
ATOM 710 CA LEU A 141 -22.177 10.396 31.126 1.00 65.98 C
ANISOU 710 CA LEU A 141 8350 8452 8267 294 32 -307 C
ATOM 711 C LEU A 141 -22.732 11.643 30.450 1.00 65.96 C
ANISOU 711 C LEU A 141 8340 8433 8288 421 98 -404 C
ATOM 712 O LEU A 141 -23.164 11.592 29.291 1.00 61.63 O
ANISOU 712 O LEU A 141 7670 7892 7856 465 118 -398 O
ATOM 713 CB LEU A 141 -23.267 9.691 31.942 1.00 65.36 C
ANISOU 713 CB LEU A 141 8243 8511 8078 257 139 -257 C
ATOM 714 CG LEU A 141 -22.881 8.301 32.463 1.00 66.79 C
ANISOU 714 CG LEU A 141 8466 8680 8231 135 95 -142 C
ATOM 715 CD1 LEU A 141 -23.781 7.871 33.626 1.00 67.10 C
ANISOU 715 CD1 LEU A 141 8537 8853 8105 75 196 -106 C
ATOM 716 CD2 LEU A 141 -22.902 7.282 31.337 1.00 65.80 C
ANISOU 716 CD2 LEU A 141 8275 8492 8235 75 79 -74 C
ATOM 717 N THR A 142 -22.710 12.773 31.163 1.00 64.84 N
ANISOU 717 N THR A 142 8360 8258 8017 486 134 -491 N
ATOM 718 CA THR A 142 -23.208 14.031 30.617 1.00 61.97 C
ANISOU 718 CA THR A 142 8067 7840 7638 647 214 -578 C
ATOM 719 C THR A 142 -22.350 14.503 29.454 1.00 60.93 C
ANISOU 719 C THR A 142 7954 7559 7638 623 122 -605 C
ATOM 720 O THR A 142 -22.868 15.057 28.478 1.00 61.54 O
ANISOU 720 O THR A 142 7995 7610 7776 753 175 -629 O
ATOM 721 CB THR A 142 -23.244 15.086 31.725 1.00 63.53 C
ANISOU 721 CB THR A 142 8521 7982 7635 706 280 -669 C
ATOM 722 OG1 THR A 142 -24.187 14.690 32.728 1.00 74.05 O
ANISOU 722 OG1 THR A 142 9816 9480 8839 758 391 -642 O
ATOM 723 CG2 THR A 142 -23.636 16.465 31.179 1.00 59.37 C
ANISOU 723 CG2 THR A 142 8158 7336 7062 900 373 -760 C
ATOM 724 N VAL A 143 -21.033 14.304 29.551 1.00 60.53 N
ANISOU 724 N VAL A 143 7947 7440 7613 465 -15 -593 N
ATOM 725 CA VAL A 143 -20.130 14.600 28.444 1.00 57.18 C
ANISOU 725 CA VAL A 143 7502 6917 7307 412 -107 -602 C
ATOM 726 C VAL A 143 -20.386 13.664 27.262 1.00 59.52 C
ANISOU 726 C VAL A 143 7579 7250 7784 443 -117 -528 C
ATOM 727 O VAL A 143 -20.296 14.078 26.098 1.00 56.86 O
ANISOU 727 O VAL A 143 7209 6846 7548 482 -127 -548 O
ATOM 728 CB VAL A 143 -18.668 14.506 28.913 1.00 55.58 C
ANISOU 728 CB VAL A 143 7343 6719 7057 233 -249 -585 C
ATOM 729 CG1 VAL A 143 -17.721 14.613 27.725 1.00 53.88 C
ANISOU 729 CG1 VAL A 143 7048 6460 6964 172 -341 -571 C
ATOM 730 CG2 VAL A 143 -18.368 15.587 29.915 1.00 60.74 C
ANISOU 730 CG2 VAL A 143 8248 7322 7510 150 -247 -677 C
ATOM 731 N ILE A 144 -20.646 12.379 27.527 1.00 55.77 N
ANISOU 731 N ILE A 144 6987 6866 7336 405 -117 -441 N
ATOM 732 CA ILE A 144 -20.883 11.462 26.420 1.00 50.75 C
ANISOU 732 CA ILE A 144 6203 6240 6841 401 -120 -380 C
ATOM 733 C ILE A 144 -22.098 11.915 25.631 1.00 51.86 C
ANISOU 733 C ILE A 144 6260 6434 7012 500 -24 -412 C
ATOM 734 O ILE A 144 -22.088 11.908 24.397 1.00 60.77 O
ANISOU 734 O ILE A 144 7308 7530 8253 517 -42 -409 O
ATOM 735 CB ILE A 144 -21.056 10.022 26.916 1.00 53.66 C
ANISOU 735 CB ILE A 144 6536 6661 7190 325 -114 -284 C
ATOM 736 CG1 ILE A 144 -19.759 9.454 27.470 1.00 55.48 C
ANISOU 736 CG1 ILE A 144 6827 6855 7396 279 -216 -222 C
ATOM 737 CG2 ILE A 144 -21.553 9.132 25.781 1.00 51.28 C
ANISOU 737 CG2 ILE A 144 6135 6356 6992 291 -88 -239 C
ATOM 738 CD1 ILE A 144 -19.901 7.981 27.931 1.00 56.38 C
ANISOU 738 CD1 ILE A 144 6971 6976 7473 234 -198 -114 C
ATOM 739 N ALA A 145 -23.151 12.350 26.327 1.00 55.80 N
ANISOU 739 N ALA A 145 6768 7041 7393 584 82 -437 N
ATOM 740 CA ALA A 145 -24.413 12.656 25.659 1.00 58.35 C
ANISOU 740 CA ALA A 145 6959 7501 7712 706 180 -437 C
ATOM 741 C ALA A 145 -24.300 13.911 24.810 1.00 56.74 C
ANISOU 741 C ALA A 145 6823 7195 7539 860 187 -499 C
ATOM 742 O ALA A 145 -24.853 13.975 23.705 1.00 51.99 O
ANISOU 742 O ALA A 145 6091 6661 7002 930 207 -479 O
ATOM 743 CB ALA A 145 -25.535 12.816 26.686 1.00 58.20 C
ANISOU 743 CB ALA A 145 6915 7669 7530 791 304 -435 C
ATOM 744 N LEU A 146 -23.608 14.929 25.333 1.00 52.10 N
ANISOU 744 N LEU A 146 6465 6446 6884 899 174 -571 N
ATOM 745 CA LEU A 146 -23.426 16.177 24.599 1.00 46.93 C
ANISOU 745 CA LEU A 146 5957 5645 6230 1023 189 -632 C
ATOM 746 C LEU A 146 -22.512 15.987 23.389 1.00 49.30 C
ANISOU 746 C LEU A 146 6203 5841 6687 912 79 -618 C
ATOM 747 O LEU A 146 -22.784 16.510 22.303 1.00 50.09 O
ANISOU 747 O LEU A 146 6287 5907 6839 1018 100 -622 O
ATOM 748 CB LEU A 146 -22.855 17.237 25.525 1.00 47.79 C
ANISOU 748 CB LEU A 146 6379 5586 6193 1021 203 -718 C
ATOM 749 CG LEU A 146 -23.649 17.832 26.690 1.00 54.14 C
ANISOU 749 CG LEU A 146 7345 6425 6801 1176 335 -761 C
ATOM 750 CD1 LEU A 146 -22.699 18.772 27.395 1.00 57.67 C
ANISOU 750 CD1 LEU A 146 8145 6652 7116 1069 304 -855 C
ATOM 751 CD2 LEU A 146 -24.912 18.593 26.255 1.00 52.83 C
ANISOU 751 CD2 LEU A 146 7185 6325 6562 1502 489 -761 C
ATOM 752 N ASP A 147 -21.429 15.237 23.551 1.00 51.80 N
ANISOU 752 N ASP A 147 6488 6125 7067 721 -31 -592 N
ATOM 753 CA ASP A 147 -20.519 15.025 22.436 1.00 48.30 C
ANISOU 753 CA ASP A 147 5983 5611 6756 635 -123 -573 C
ATOM 754 C ASP A 147 -21.226 14.323 21.282 1.00 51.19 C
ANISOU 754 C ASP A 147 6156 6055 7237 682 -101 -522 C
ATOM 755 O ASP A 147 -21.077 14.713 20.118 1.00 54.68 O
ANISOU 755 O ASP A 147 6580 6440 7756 714 -118 -531 O
ATOM 756 CB ASP A 147 -19.300 14.233 22.908 1.00 56.07 C
ANISOU 756 CB ASP A 147 6939 6606 7759 475 -229 -531 C
ATOM 757 CG ASP A 147 -18.404 13.816 21.764 1.00 71.42 C
ANISOU 757 CG ASP A 147 8784 8523 9830 419 -307 -493 C
ATOM 758 OD1 ASP A 147 -17.550 14.628 21.360 1.00 77.15 O
ANISOU 758 OD1 ASP A 147 9579 9184 10551 358 -358 -529 O
ATOM 759 OD2 ASP A 147 -18.564 12.679 21.257 1.00 80.29 O
ANISOU 759 OD2 ASP A 147 9779 9686 11040 424 -309 -429 O
ATOM 760 N ARG A 148 -21.995 13.274 21.585 1.00 51.15 N
ANISOU 760 N ARG A 148 6021 6186 7226 658 -65 -469 N
ATOM 761 CA ARG A 148 -22.771 12.602 20.546 1.00 54.16 C
ANISOU 761 CA ARG A 148 6235 6668 7675 651 -41 -425 C
ATOM 762 C ARG A 148 -23.734 13.567 19.863 1.00 51.99 C
ANISOU 762 C ARG A 148 5909 6473 7371 821 27 -446 C
ATOM 763 O ARG A 148 -23.821 13.600 18.631 1.00 50.03 O
ANISOU 763 O ARG A 148 5583 6228 7197 835 7 -435 O
ATOM 764 CB ARG A 148 -23.534 11.423 21.136 1.00 60.38 C
ANISOU 764 CB ARG A 148 6932 7600 8411 551 0 -369 C
ATOM 765 CG ARG A 148 -22.636 10.293 21.495 1.00 61.50 C
ANISOU 765 CG ARG A 148 7138 7645 8585 414 -61 -325 C
ATOM 766 CD ARG A 148 -22.894 9.155 20.577 1.00 64.52 C
ANISOU 766 CD ARG A 148 7461 8034 9020 299 -62 -278 C
ATOM 767 NE ARG A 148 -21.705 8.327 20.476 1.00 64.71 N
ANISOU 767 NE ARG A 148 7587 7901 9100 253 -124 -240 N
ATOM 768 CZ ARG A 148 -21.638 7.252 19.712 1.00 66.11 C
ANISOU 768 CZ ARG A 148 7797 8010 9311 167 -123 -201 C
ATOM 769 NH1 ARG A 148 -22.701 6.892 19.003 1.00 60.55 N
ANISOU 769 NH1 ARG A 148 7024 7397 8587 62 -76 -201 N
ATOM 770 NH2 ARG A 148 -20.516 6.549 19.658 1.00 72.54 N
ANISOU 770 NH2 ARG A 148 8720 8686 10156 190 -163 -157 N
ATOM 771 N TYR A 149 -24.470 14.360 20.647 1.00 43.27 N
ANISOU 771 N TYR A 149 4856 5443 6140 975 115 -469 N
ATOM 772 CA TYR A 149 -25.400 15.308 20.053 1.00 42.30 C
ANISOU 772 CA TYR A 149 4698 5413 5960 1205 195 -470 C
ATOM 773 C TYR A 149 -24.681 16.253 19.093 1.00 52.64 C
ANISOU 773 C TYR A 149 6157 6513 7331 1272 155 -509 C
ATOM 774 O TYR A 149 -25.210 16.568 18.017 1.00 54.29 O
ANISOU 774 O TYR A 149 6277 6791 7559 1391 172 -481 O
ATOM 775 CB TYR A 149 -26.126 16.066 21.160 1.00 45.93 C
ANISOU 775 CB TYR A 149 5251 5948 6252 1401 311 -492 C
ATOM 776 CG TYR A 149 -27.001 17.184 20.694 1.00 51.64 C
ANISOU 776 CG TYR A 149 5997 6745 6880 1717 414 -486 C
ATOM 777 CD1 TYR A 149 -27.979 16.972 19.733 1.00 58.22 C
ANISOU 777 CD1 TYR A 149 6566 7842 7714 1816 439 -413 C
ATOM 778 CD2 TYR A 149 -26.862 18.448 21.215 1.00 53.24 C
ANISOU 778 CD2 TYR A 149 6505 6760 6964 1922 490 -548 C
ATOM 779 CE1 TYR A 149 -28.791 17.997 19.290 1.00 56.06 C
ANISOU 779 CE1 TYR A 149 6300 7670 7332 2157 536 -385 C
ATOM 780 CE2 TYR A 149 -27.671 19.471 20.791 1.00 61.88 C
ANISOU 780 CE2 TYR A 149 7663 7902 7947 2266 602 -530 C
ATOM 781 CZ TYR A 149 -28.635 19.241 19.827 1.00 62.88 C
ANISOU 781 CZ TYR A 149 7491 8318 8081 2405 624 -440 C
ATOM 782 OH TYR A 149 -29.433 20.272 19.389 1.00 69.55 O
ANISOU 782 OH TYR A 149 8392 9237 8797 2796 737 -402 O
ATOM 783 N ARG A 150 -23.447 16.669 19.437 1.00 51.18 N
ANISOU 783 N ARG A 150 6187 6094 7164 1168 94 -564 N
ATOM 784 CA ARG A 150 -22.711 17.598 18.579 1.00 47.36 C
ANISOU 784 CA ARG A 150 5868 5412 6713 1183 59 -600 C
ATOM 785 C ARG A 150 -22.216 16.920 17.294 1.00 44.96 C
ANISOU 785 C ARG A 150 5406 5115 6562 1064 -24 -563 C
ATOM 786 O ARG A 150 -22.224 17.540 16.218 1.00 38.67 O
ANISOU 786 O ARG A 150 4645 4255 5793 1141 -22 -563 O
ATOM 787 CB ARG A 150 -21.542 18.213 19.344 1.00 44.85 C
ANISOU 787 CB ARG A 150 5808 4898 6335 1047 15 -666 C
ATOM 788 CG ARG A 150 -21.903 18.906 20.671 1.00 52.07 C
ANISOU 788 CG ARG A 150 6941 5768 7074 1134 98 -719 C
ATOM 789 CD ARG A 150 -23.127 19.804 20.584 1.00 56.03 C
ANISOU 789 CD ARG A 150 7547 6282 7461 1450 241 -724 C
ATOM 790 NE ARG A 150 -22.993 20.882 19.608 1.00 62.43 N
ANISOU 790 NE ARG A 150 8561 6908 8252 1563 266 -743 N
ATOM 791 CZ ARG A 150 -24.005 21.656 19.210 1.00 66.80 C
ANISOU 791 CZ ARG A 150 9193 7475 8713 1888 385 -722 C
ATOM 792 NH1 ARG A 150 -25.223 21.473 19.708 1.00 64.55 N
ANISOU 792 NH1 ARG A 150 8760 7420 8345 2128 490 -680 N
ATOM 793 NH2 ARG A 150 -23.810 22.614 18.309 1.00 64.47 N
ANISOU 793 NH2 ARG A 150 9119 6984 8391 1987 406 -731 N
ATOM 794 N CYS A 151 -21.768 15.652 17.383 1.00 39.68 N
ANISOU 794 N CYS A 151 4592 4507 5977 892 -89 -529 N
ATOM 795 CA CYS A 151 -21.334 14.950 16.180 1.00 42.67 C
ANISOU 795 CA CYS A 151 4851 4882 6479 801 -149 -496 C
ATOM 796 C CYS A 151 -22.488 14.718 15.229 1.00 47.32 C
ANISOU 796 C CYS A 151 5283 5618 7080 879 -108 -460 C
ATOM 797 O CYS A 151 -22.281 14.624 14.014 1.00 51.42 O
ANISOU 797 O CYS A 151 5752 6113 7672 855 -141 -449 O
ATOM 798 CB CYS A 151 -20.721 13.602 16.517 1.00 47.16 C
ANISOU 798 CB CYS A 151 5349 5470 7101 649 -200 -459 C
ATOM 799 SG CYS A 151 -19.197 13.663 17.373 1.00 52.87 S
ANISOU 799 SG CYS A 151 6179 6100 7809 549 -275 -469 S
ATOM 800 N ILE A 152 -23.702 14.594 15.767 1.00 43.15 N
ANISOU 800 N ILE A 152 4656 5276 6462 960 -38 -437 N
ATOM 801 CA ILE A 152 -24.846 14.260 14.940 1.00 46.86 C
ANISOU 801 CA ILE A 152 4925 5971 6910 995 -8 -388 C
ATOM 802 C ILE A 152 -25.391 15.519 14.225 1.00 56.58 C
ANISOU 802 C ILE A 152 6174 7236 8089 1241 35 -382 C
ATOM 803 O ILE A 152 -25.913 15.419 13.105 1.00 63.96 O
ANISOU 803 O ILE A 152 6966 8304 9032 1264 23 -342 O
ATOM 804 CB ILE A 152 -25.890 13.509 15.805 1.00 47.96 C
ANISOU 804 CB ILE A 152 4916 6354 6952 942 47 -350 C
ATOM 805 CG1 ILE A 152 -25.624 12.000 15.807 1.00 54.78 C
ANISOU 805 CG1 ILE A 152 5739 7212 7862 670 3 -327 C
ATOM 806 CG2 ILE A 152 -27.301 13.647 15.277 1.00 47.12 C
ANISOU 806 CG2 ILE A 152 4582 6575 6745 1044 104 -294 C
ATOM 807 CD1 ILE A 152 -24.450 11.509 16.621 1.00 57.85 C
ANISOU 807 CD1 ILE A 152 6294 7383 8304 573 -39 -347 C
ATOM 808 N VAL A 153 -25.226 16.725 14.791 1.00 50.70 N
ANISOU 808 N VAL A 153 5638 6351 7274 1427 86 -420 N
ATOM 809 CA VAL A 153 -25.680 17.902 14.044 1.00 55.15 C
ANISOU 809 CA VAL A 153 6281 6900 7773 1686 137 -405 C
ATOM 810 C VAL A 153 -24.617 18.354 13.043 1.00 49.85 C
ANISOU 810 C VAL A 153 5767 5980 7194 1610 70 -433 C
ATOM 811 O VAL A 153 -24.940 18.779 11.925 1.00 49.55 O
ANISOU 811 O VAL A 153 5699 5974 7153 1729 72 -396 O
ATOM 812 CB VAL A 153 -26.137 19.064 14.970 1.00 47.48 C
ANISOU 812 CB VAL A 153 5522 5873 6644 1962 250 -426 C
ATOM 813 CG1 VAL A 153 -27.275 18.608 15.871 1.00 47.79 C
ANISOU 813 CG1 VAL A 153 5362 6219 6578 2056 329 -386 C
ATOM 814 CG2 VAL A 153 -25.010 19.662 15.757 1.00 38.73 C
ANISOU 814 CG2 VAL A 153 4750 4442 5525 1864 237 -513 C
ATOM 815 N TYR A 154 -23.345 18.259 13.407 1.00 48.20 N
ANISOU 815 N TYR A 154 5706 5554 7052 1409 8 -488 N
ATOM 816 CA TYR A 154 -22.283 18.626 12.483 1.00 48.09 C
ANISOU 816 CA TYR A 154 5809 5351 7111 1303 -53 -508 C
ATOM 817 C TYR A 154 -22.012 17.531 11.470 1.00 48.90 C
ANISOU 817 C TYR A 154 5696 5542 7341 1150 -124 -475 C
ATOM 818 O TYR A 154 -21.151 17.727 10.607 1.00 55.75 O
ANISOU 818 O TYR A 154 6623 6290 8270 1065 -170 -483 O
ATOM 819 CB TYR A 154 -20.996 18.955 13.244 1.00 45.49 C
ANISOU 819 CB TYR A 154 5685 4825 6773 1128 -94 -568 C
ATOM 820 CG TYR A 154 -20.995 20.280 13.999 1.00 49.93 C
ANISOU 820 CG TYR A 154 6577 5210 7186 1226 -27 -621 C
ATOM 821 CD1 TYR A 154 -21.573 20.390 15.253 1.00 48.13 C
ANISOU 821 CD1 TYR A 154 6415 5020 6852 1322 38 -642 C
ATOM 822 CD2 TYR A 154 -20.367 21.396 13.472 1.00 54.59 C
ANISOU 822 CD2 TYR A 154 7446 5577 7720 1199 -22 -652 C
ATOM 823 CE1 TYR A 154 -21.561 21.559 15.935 1.00 53.56 C
ANISOU 823 CE1 TYR A 154 7448 5520 7382 1411 111 -698 C
ATOM 824 CE2 TYR A 154 -20.341 22.579 14.156 1.00 61.09 C
ANISOU 824 CE2 TYR A 154 8639 6194 8377 1260 49 -708 C
ATOM 825 CZ TYR A 154 -20.946 22.664 15.390 1.00 65.38 C
ANISOU 825 CZ TYR A 154 9259 6767 8815 1376 119 -734 C
ATOM 826 OH TYR A 154 -20.919 23.864 16.083 1.00 74.70 O
ANISOU 826 OH TYR A 154 10868 7711 9804 1442 204 -799 O
ATOM 827 N HIS A 155 -22.734 16.399 11.564 1.00 49.50 N
ANISOU 827 N HIS A 155 5552 5821 7435 1101 -124 -439 N
ATOM 828 CA HIS A 155 -22.607 15.247 10.650 1.00 46.30 C
ANISOU 828 CA HIS A 155 4990 5484 7116 945 -175 -413 C
ATOM 829 C HIS A 155 -21.182 14.719 10.636 1.00 41.09 C
ANISOU 829 C HIS A 155 4401 4663 6548 783 -234 -435 C
ATOM 830 O HIS A 155 -20.661 14.295 9.602 1.00 52.87 O
ANISOU 830 O HIS A 155 5862 6118 8109 708 -268 -427 O
ATOM 831 CB HIS A 155 -23.067 15.586 9.225 1.00 45.09 C
ANISOU 831 CB HIS A 155 4770 5398 6965 1017 -180 -384 C
ATOM 832 CG HIS A 155 -24.465 16.116 9.150 1.00 44.75 C
ANISOU 832 CG HIS A 155 4618 5577 6807 1218 -123 -337 C
ATOM 833 ND1 HIS A 155 -25.576 15.300 9.215 1.00 44.73 N
ANISOU 833 ND1 HIS A 155 4386 5867 6743 1169 -109 -292 N
ATOM 834 CD2 HIS A 155 -24.934 17.380 9.031 1.00 39.55 C
ANISOU 834 CD2 HIS A 155 4053 4914 6061 1479 -70 -319 C
ATOM 835 CE1 HIS A 155 -26.668 16.036 9.112 1.00 42.31 C
ANISOU 835 CE1 HIS A 155 3982 5778 6317 1403 -55 -240 C
ATOM 836 NE2 HIS A 155 -26.307 17.302 9.011 1.00 45.20 N
ANISOU 836 NE2 HIS A 155 4557 5951 6667 1624 -25 -253 N
ATOM 837 N LEU A 156 -20.540 14.770 11.788 1.00 40.43 N
ANISOU 837 N LEU A 156 4406 4508 6448 743 -243 -457 N
ATOM 838 CA LEU A 156 -19.142 14.414 11.921 1.00 40.46 C
ANISOU 838 CA LEU A 156 4452 4417 6504 624 -300 -462 C
ATOM 839 C LEU A 156 -18.973 13.111 12.695 1.00 42.78 C
ANISOU 839 C LEU A 156 4689 4758 6806 549 -310 -431 C
ATOM 840 O LEU A 156 -19.870 12.641 13.402 1.00 43.89 O
ANISOU 840 O LEU A 156 4795 4982 6900 556 -273 -419 O
ATOM 841 CB LEU A 156 -18.376 15.538 12.616 1.00 37.08 C
ANISOU 841 CB LEU A 156 4183 3889 6016 607 -315 -501 C
ATOM 842 CG LEU A 156 -18.319 16.815 11.802 1.00 41.11 C
ANISOU 842 CG LEU A 156 4825 4294 6500 654 -301 -527 C
ATOM 843 CD1 LEU A 156 -17.514 17.834 12.585 1.00 45.19 C
ANISOU 843 CD1 LEU A 156 5550 4697 6924 569 -315 -573 C
ATOM 844 CD2 LEU A 156 -17.690 16.519 10.436 1.00 36.12 C
ANISOU 844 CD2 LEU A 156 4116 3654 5955 593 -337 -505 C
ATOM 845 N GLU A 157 -17.790 12.534 12.556 1.00 42.39 N
ANISOU 845 N GLU A 157 4637 4669 6800 488 -353 -410 N
ATOM 846 CA GLU A 157 -17.453 11.351 13.317 1.00 43.35 C
ANISOU 846 CA GLU A 157 4751 4810 6910 457 -359 -367 C
ATOM 847 C GLU A 157 -16.614 11.673 14.549 1.00 56.16 C
ANISOU 847 C GLU A 157 6412 6452 8474 440 -399 -361 C
ATOM 848 O GLU A 157 -16.538 10.839 15.462 1.00 64.41 O
ANISOU 848 O GLU A 157 7466 7525 9480 438 -399 -321 O
ATOM 849 CB GLU A 157 -16.763 10.336 12.401 1.00 34.59 C
ANISOU 849 CB GLU A 157 3624 3663 5854 453 -363 -328 C
ATOM 850 CG GLU A 157 -17.741 9.633 11.439 1.00 46.55 C
ANISOU 850 CG GLU A 157 5136 5163 7387 419 -319 -331 C
ATOM 851 CD GLU A 157 -18.896 8.887 12.170 1.00 65.53 C
ANISOU 851 CD GLU A 157 7559 7614 9727 355 -277 -318 C
ATOM 852 OE1 GLU A 157 -18.687 8.433 13.328 1.00 72.07 O
ANISOU 852 OE1 GLU A 157 8437 8436 10512 355 -274 -290 O
ATOM 853 OE2 GLU A 157 -20.011 8.756 11.587 1.00 64.42 O
ANISOU 853 OE2 GLU A 157 7372 7543 9563 290 -249 -330 O
ATOM 854 N SER A 158 -16.019 12.872 14.608 1.00 52.26 N
ANISOU 854 N SER A 158 5961 5945 7950 408 -433 -399 N
ATOM 855 CA SER A 158 -15.502 13.448 15.850 1.00 48.31 C
ANISOU 855 CA SER A 158 5528 5474 7353 349 -468 -415 C
ATOM 856 C SER A 158 -15.699 14.966 15.851 1.00 56.06 C
ANISOU 856 C SER A 158 6655 6374 8272 318 -454 -488 C
ATOM 857 O SER A 158 -15.500 15.647 14.834 1.00 57.54 O
ANISOU 857 O SER A 158 6877 6498 8487 303 -453 -509 O
ATOM 858 CB SER A 158 -14.004 13.113 16.112 1.00 48.31 C
ANISOU 858 CB SER A 158 5455 5576 7323 280 -543 -362 C
ATOM 859 OG SER A 158 -13.310 12.493 15.032 1.00 48.43 O
ANISOU 859 OG SER A 158 5365 5625 7412 315 -553 -312 O
ATOM 860 N LYS A 159 -16.145 15.483 16.993 1.00 58.21 N
ANISOU 860 N LYS A 159 7048 6628 8442 321 -430 -527 N
ATOM 861 CA LYS A 159 -16.020 16.894 17.304 1.00 50.67 C
ANISOU 861 CA LYS A 159 6310 5568 7374 266 -418 -597 C
ATOM 862 C LYS A 159 -14.890 17.109 18.300 1.00 51.79 C
ANISOU 862 C LYS A 159 6508 5768 7402 79 -493 -606 C
ATOM 863 O LYS A 159 -13.975 17.892 18.033 1.00 62.62 O
ANISOU 863 O LYS A 159 7967 7116 8708 -88 -539 -631 O
ATOM 864 CB LYS A 159 -17.344 17.458 17.849 1.00 52.09 C
ANISOU 864 CB LYS A 159 6627 5683 7482 422 -320 -641 C
ATOM 865 CG LYS A 159 -17.564 18.975 17.573 1.00 63.18 C
ANISOU 865 CG LYS A 159 8312 6908 8786 469 -262 -707 C
ATOM 866 CD LYS A 159 -18.215 19.711 18.780 1.00 71.37 C
ANISOU 866 CD LYS A 159 9586 7871 9660 555 -181 -765 C
ATOM 867 CE LYS A 159 -18.774 21.107 18.418 1.00 70.52 C
ANISOU 867 CE LYS A 159 9793 7560 9440 710 -80 -817 C
ATOM 868 NZ LYS A 159 -19.662 21.690 19.491 1.00 61.45 N
ANISOU 868 NZ LYS A 159 8860 6358 8131 890 34 -861 N
ATOM 869 N ILE A 160 -14.901 16.382 19.421 1.00 48.44 N
ANISOU 869 N ILE A 160 6024 5445 6937 79 -512 -576 N
ATOM 870 CA ILE A 160 -13.865 16.515 20.449 1.00 53.44 C
ANISOU 870 CA ILE A 160 6683 6184 7436 -97 -594 -571 C
ATOM 871 C ILE A 160 -12.655 15.651 20.121 1.00 55.76 C
ANISOU 871 C ILE A 160 6745 6667 7773 -154 -685 -477 C
ATOM 872 O ILE A 160 -12.785 14.457 19.824 1.00 57.50 O
ANISOU 872 O ILE A 160 6808 6941 8100 -14 -675 -401 O
ATOM 873 CB ILE A 160 -14.403 16.148 21.837 1.00 49.36 C
ANISOU 873 CB ILE A 160 6215 5705 6834 -56 -573 -572 C
ATOM 874 CG1 ILE A 160 -15.400 17.208 22.334 1.00 55.31 C
ANISOU 874 CG1 ILE A 160 7228 6300 7487 -3 -477 -669 C
ATOM 875 CG2 ILE A 160 -13.253 16.063 22.791 1.00 49.27 C
ANISOU 875 CG2 ILE A 160 6174 5857 6690 -233 -676 -541 C
ATOM 876 CD1 ILE A 160 -16.075 16.822 23.624 1.00 56.60 C
ANISOU 876 CD1 ILE A 160 7428 6511 7568 61 -435 -669 C
ATOM 877 N SER A 161 -11.473 16.241 20.252 1.00 59.52 N
ANISOU 877 N SER A 161 7216 7261 8136 -363 -768 -476 N
ATOM 878 CA SER A 161 -10.219 15.552 19.983 1.00 59.24 C
ANISOU 878 CA SER A 161 6933 7475 8101 -403 -853 -374 C
ATOM 879 C SER A 161 -9.855 14.544 21.076 1.00 59.30 C
ANISOU 879 C SER A 161 6812 7676 8045 -335 -903 -282 C
ATOM 880 O SER A 161 -10.169 14.718 22.255 1.00 70.22 O
ANISOU 880 O SER A 161 8308 9054 9320 -387 -912 -311 O
ATOM 881 CB SER A 161 -9.087 16.565 19.862 1.00 66.45 C
ANISOU 881 CB SER A 161 7858 8518 8871 -691 -929 -395 C
ATOM 882 N LYS A 162 -9.122 13.508 20.673 1.00 45.59 N
ANISOU 882 N LYS A 162 4851 6115 6355 -207 -932 -164 N
ATOM 883 CA LYS A 162 -8.605 12.533 21.621 1.00 51.65 C
ANISOU 883 CA LYS A 162 5497 7087 7039 -107 -982 -49 C
ATOM 884 C LYS A 162 -7.703 13.154 22.669 1.00 55.60 C
ANISOU 884 C LYS A 162 5953 7847 7325 -331 -1093 -35 C
ATOM 885 O LYS A 162 -7.468 12.527 23.701 1.00 73.73 O
ANISOU 885 O LYS A 162 8195 10297 9521 -268 -1136 46 O
ATOM 886 CB LYS A 162 -7.813 11.418 20.915 1.00 58.71 C
ANISOU 886 CB LYS A 162 6183 8140 7985 103 -983 87 C
ATOM 887 CG LYS A 162 -8.596 10.574 19.919 1.00 59.60 C
ANISOU 887 CG LYS A 162 6357 8012 8276 315 -877 87 C
ATOM 888 CD LYS A 162 -7.834 9.304 19.557 1.00 61.08 C
ANISOU 888 CD LYS A 162 6415 8328 8463 568 -861 232 C
ATOM 889 CE LYS A 162 -8.592 8.479 18.520 1.00 63.65 C
ANISOU 889 CE LYS A 162 6855 8392 8937 732 -751 218 C
ATOM 890 NZ LYS A 162 -7.750 7.376 17.959 1.00 64.46 N
ANISOU 890 NZ LYS A 162 6880 8588 9023 990 -716 347 N
ATOM 891 N ARG A 163 -7.170 14.346 22.449 1.00 51.64 N
ANISOU 891 N ARG A 163 5485 7407 6727 -611 -1141 -105 N
ATOM 892 CA ARG A 163 -6.323 14.920 23.484 1.00 60.22 C
ANISOU 892 CA ARG A 163 6545 8761 7574 -880 -1253 -96 C
ATOM 893 C ARG A 163 -7.068 15.901 24.381 1.00 64.43 C
ANISOU 893 C ARG A 163 7406 9076 8000 -1071 -1231 -237 C
ATOM 894 O ARG A 163 -6.683 16.058 25.543 1.00 64.81 O
ANISOU 894 O ARG A 163 7475 9297 7852 -1230 -1307 -227 O
ATOM 895 CB ARG A 163 -5.075 15.572 22.860 1.00 69.16 C
ANISOU 895 CB ARG A 163 7510 10175 8593 -1140 -1334 -69 C
ATOM 896 CG ARG A 163 -3.835 14.612 22.762 1.00 77.98 C
ANISOU 896 CG ARG A 163 8224 11757 9648 -1007 -1412 120 C
ATOM 897 CD ARG A 163 -4.156 13.212 22.115 1.00 80.27 C
ANISOU 897 CD ARG A 163 8400 11956 10142 -554 -1326 222 C
ATOM 898 NE ARG A 163 -3.286 12.126 22.599 1.00 84.73 N
ANISOU 898 NE ARG A 163 8695 12891 10607 -325 -1379 409 N
ATOM 899 CZ ARG A 163 -3.275 10.874 22.129 1.00 80.11 C
ANISOU 899 CZ ARG A 163 8025 12284 10128 65 -1309 525 C
ATOM 900 NH1 ARG A 163 -2.444 9.974 22.649 1.00 77.88 N
ANISOU 900 NH1 ARG A 163 7530 12344 9717 296 -1354 705 N
ATOM 901 NH2 ARG A 163 -4.080 10.514 21.136 1.00 72.19 N
ANISOU 901 NH2 ARG A 163 7168 10923 9337 231 -1192 466 N
ATOM 902 N ILE A 164 -8.148 16.526 23.899 1.00 68.12 N
ANISOU 902 N ILE A 164 8132 9178 8574 -1030 -1122 -359 N
ATOM 903 CA ILE A 164 -9.028 17.258 24.812 1.00 71.41 C
ANISOU 903 CA ILE A 164 8870 9371 8893 -1096 -1067 -478 C
ATOM 904 C ILE A 164 -9.801 16.294 25.719 1.00 72.52 C
ANISOU 904 C ILE A 164 8986 9496 9074 -867 -1028 -434 C
ATOM 905 O ILE A 164 -10.043 16.597 26.897 1.00 67.58 O
ANISOU 905 O ILE A 164 8522 8861 8293 -954 -1032 -481 O
ATOM 906 CB ILE A 164 -9.978 18.184 24.025 1.00 68.29 C
ANISOU 906 CB ILE A 164 8747 8622 8579 -1053 -949 -598 C
ATOM 907 CG1 ILE A 164 -9.226 19.418 23.516 1.00 62.33 C
ANISOU 907 CG1 ILE A 164 8153 7837 7693 -1368 -984 -665 C
ATOM 908 CG2 ILE A 164 -11.170 18.611 24.881 1.00 62.59 C
ANISOU 908 CG2 ILE A 164 8315 7668 7798 -958 -849 -693 C
ATOM 909 CD1 ILE A 164 -8.546 20.220 24.601 1.00 63.96 C
ANISOU 909 CD1 ILE A 164 8548 8142 7613 -1726 -1059 -721 C
ATOM 910 N SER A 165 -10.181 15.115 25.200 1.00 65.07 N
ANISOU 910 N SER A 165 7864 8543 8315 -596 -987 -346 N
ATOM 911 CA SER A 165 -10.876 14.125 26.013 1.00 57.27 C
ANISOU 911 CA SER A 165 6869 7542 7350 -412 -947 -293 C
ATOM 912 C SER A 165 -10.075 13.722 27.246 1.00 60.52 C
ANISOU 912 C SER A 165 7201 8213 7581 -487 -1049 -209 C
ATOM 913 O SER A 165 -10.668 13.413 28.287 1.00 62.76 O
ANISOU 913 O SER A 165 7583 8465 7797 -440 -1020 -210 O
ATOM 914 CB SER A 165 -11.205 12.892 25.180 1.00 63.40 C
ANISOU 914 CB SER A 165 7500 8274 8316 -167 -895 -204 C
ATOM 915 OG SER A 165 -10.024 12.196 24.826 1.00 71.12 O
ANISOU 915 OG SER A 165 8261 9473 9289 -118 -972 -80 O
ATOM 916 N PHE A 166 -8.740 13.699 27.169 1.00 64.83 N
ANISOU 916 N PHE A 166 7552 9051 8028 -599 -1167 -126 N
ATOM 917 CA PHE A 166 -7.993 13.412 28.398 1.00 67.57 C
ANISOU 917 CA PHE A 166 7814 9691 8168 -679 -1274 -40 C
ATOM 918 C PHE A 166 -8.061 14.584 29.366 1.00 62.49 C
ANISOU 918 C PHE A 166 7398 9029 7315 -982 -1307 -165 C
ATOM 919 O PHE A 166 -8.114 14.378 30.580 1.00 67.02 O
ANISOU 919 O PHE A 166 8027 9699 7740 -1012 -1341 -143 O
ATOM 920 CB PHE A 166 -6.539 13.046 28.101 1.00 63.77 C
ANISOU 920 CB PHE A 166 7019 9608 7603 -698 -1393 103 C
ATOM 921 CG PHE A 166 -6.398 11.874 27.194 1.00 66.11 C
ANISOU 921 CG PHE A 166 7134 9915 8071 -371 -1346 229 C
ATOM 922 CD1 PHE A 166 -7.088 10.703 27.443 1.00 66.70 C
ANISOU 922 CD1 PHE A 166 7269 9836 8239 -81 -1270 299 C
ATOM 923 CD2 PHE A 166 -5.601 11.954 26.064 1.00 69.11 C
ANISOU 923 CD2 PHE A 166 7317 10439 8502 -366 -1366 272 C
ATOM 924 CE1 PHE A 166 -6.969 9.612 26.596 1.00 66.94 C
ANISOU 924 CE1 PHE A 166 7205 9829 8400 210 -1213 406 C
ATOM 925 CE2 PHE A 166 -5.476 10.878 25.202 1.00 67.47 C
ANISOU 925 CE2 PHE A 166 6984 10216 8434 -49 -1307 379 C
ATOM 926 CZ PHE A 166 -6.160 9.702 25.472 1.00 71.13 C
ANISOU 926 CZ PHE A 166 7549 10497 8980 240 -1229 444 C
ATOM 927 N LEU A 167 -8.120 15.808 28.848 1.00 59.67 N
ANISOU 927 N LEU A 167 7222 8518 6933 -1201 -1283 -299 N
ATOM 928 CA LEU A 167 -8.186 16.989 29.705 1.00 63.72 C
ANISOU 928 CA LEU A 167 8036 8956 7220 -1500 -1295 -432 C
ATOM 929 C LEU A 167 -9.550 17.121 30.386 1.00 65.98 C
ANISOU 929 C LEU A 167 8607 8938 7524 -1351 -1164 -529 C
ATOM 930 O LEU A 167 -9.627 17.553 31.543 1.00 61.80 O
ANISOU 930 O LEU A 167 8276 8420 6787 -1501 -1178 -589 O
ATOM 931 CB LEU A 167 -7.853 18.228 28.872 1.00 66.58 C
ANISOU 931 CB LEU A 167 8564 9199 7536 -1762 -1289 -539 C
ATOM 932 CG LEU A 167 -8.386 19.619 29.204 1.00 70.17 C
ANISOU 932 CG LEU A 167 9487 9341 7833 -1976 -1214 -720 C
ATOM 933 CD1 LEU A 167 -7.922 20.082 30.581 1.00 75.47 C
ANISOU 933 CD1 LEU A 167 10327 10158 8192 -2285 -1294 -764 C
ATOM 934 CD2 LEU A 167 -7.913 20.578 28.127 1.00 63.66 C
ANISOU 934 CD2 LEU A 167 8775 8419 6992 -2198 -1212 -780 C
ATOM 935 N ILE A 168 -10.636 16.752 29.687 1.00 71.35 N
ANISOU 935 N ILE A 168 9300 9377 8432 -1064 -1035 -542 N
ATOM 936 CA ILE A 168 -11.963 16.730 30.306 1.00 67.51 C
ANISOU 936 CA ILE A 168 9007 8683 7959 -891 -905 -606 C
ATOM 937 C ILE A 168 -12.055 15.612 31.346 1.00 68.36 C
ANISOU 937 C ILE A 168 8989 8955 8028 -787 -933 -502 C
ATOM 938 O ILE A 168 -12.704 15.774 32.388 1.00 74.81 O
ANISOU 938 O ILE A 168 9984 9715 8724 -781 -875 -553 O
ATOM 939 CB ILE A 168 -13.071 16.595 29.242 1.00 58.90 C
ANISOU 939 CB ILE A 168 7912 7371 7097 -638 -773 -628 C
ATOM 940 CG1 ILE A 168 -12.940 17.677 28.166 1.00 57.66 C
ANISOU 940 CG1 ILE A 168 7887 7050 6970 -720 -747 -713 C
ATOM 941 CG2 ILE A 168 -14.455 16.684 29.890 1.00 57.86 C
ANISOU 941 CG2 ILE A 168 7952 7089 6942 -470 -631 -689 C
ATOM 942 CD1 ILE A 168 -14.031 17.624 27.064 1.00 54.13 C
ANISOU 942 CD1 ILE A 168 7426 6416 6725 -468 -625 -729 C
ATOM 943 N ILE A 169 -11.406 14.472 31.093 1.00 62.94 N
ANISOU 943 N ILE A 169 8021 8467 7425 -688 -1010 -351 N
ATOM 944 CA ILE A 169 -11.353 13.418 32.095 1.00 65.39 C
ANISOU 944 CA ILE A 169 8247 8931 7666 -592 -1043 -235 C
ATOM 945 C ILE A 169 -10.579 13.862 33.334 1.00 71.48 C
ANISOU 945 C ILE A 169 9073 9923 8165 -820 -1156 -236 C
ATOM 946 O ILE A 169 -10.889 13.432 34.453 1.00 75.18 O
ANISOU 946 O ILE A 169 9605 10441 8520 -785 -1150 -202 O
ATOM 947 CB ILE A 169 -10.773 12.139 31.472 1.00 62.88 C
ANISOU 947 CB ILE A 169 7670 8749 7474 -400 -1086 -68 C
ATOM 948 CG1 ILE A 169 -11.837 11.508 30.553 1.00 58.92 C
ANISOU 948 CG1 ILE A 169 7181 8002 7203 -188 -954 -73 C
ATOM 949 CG2 ILE A 169 -10.287 11.182 32.570 1.00 62.25 C
ANISOU 949 CG2 ILE A 169 7511 8890 7253 -328 -1158 79 C
ATOM 950 CD1 ILE A 169 -11.390 10.265 29.756 1.00 56.41 C
ANISOU 950 CD1 ILE A 169 6690 7732 7012 12 -963 71 C
ATOM 951 N GLY A 170 -9.592 14.740 33.177 1.00 68.32 N
ANISOU 951 N GLY A 170 8661 9666 7632 -1086 -1259 -276 N
ATOM 952 CA GLY A 170 -8.887 15.276 34.333 1.00 64.35 C
ANISOU 952 CA GLY A 170 8234 9383 6833 -1370 -1371 -293 C
ATOM 953 C GLY A 170 -9.749 16.196 35.180 1.00 68.97 C
ANISOU 953 C GLY A 170 9203 9726 7276 -1490 -1279 -461 C
ATOM 954 O GLY A 170 -9.918 15.956 36.378 1.00 74.15 O
ANISOU 954 O GLY A 170 9938 10463 7774 -1508 -1292 -446 O
ATOM 955 N LEU A 171 -10.294 17.253 34.565 1.00 71.75 N
ANISOU 955 N LEU A 171 9814 9780 7669 -1550 -1176 -615 N
ATOM 956 CA LEU A 171 -11.247 18.130 35.241 1.00 75.82 C
ANISOU 956 CA LEU A 171 10730 10021 8058 -1574 -1046 -773 C
ATOM 957 C LEU A 171 -12.302 17.345 35.996 1.00 76.05 C
ANISOU 957 C LEU A 171 10758 10002 8137 -1307 -945 -738 C
ATOM 958 O LEU A 171 -12.686 17.726 37.105 1.00 85.12 O
ANISOU 958 O LEU A 171 12150 11107 9086 -1371 -899 -812 O
ATOM 959 CB LEU A 171 -11.957 19.034 34.234 1.00 83.01 C
ANISOU 959 CB LEU A 171 11867 10592 9082 -1493 -909 -895 C
ATOM 960 CG LEU A 171 -11.574 20.483 33.954 1.00 86.91 C
ANISOU 960 CG LEU A 171 12714 10904 9402 -1778 -900 -1038 C
ATOM 961 CD1 LEU A 171 -10.339 20.545 33.081 1.00 85.90 C
ANISOU 961 CD1 LEU A 171 12369 10970 9300 -2017 -1042 -977 C
ATOM 962 CD2 LEU A 171 -12.746 21.168 33.275 1.00 85.83 C
ANISOU 962 CD2 LEU A 171 12848 10391 9371 -1532 -708 -1140 C
ATOM 963 N ALA A 172 -12.810 16.262 35.396 1.00 68.35 N
ANISOU 963 N ALA A 172 9535 9027 7409 -1025 -899 -630 N
ATOM 964 CA ALA A 172 -13.903 15.519 36.018 1.00 68.18 C
ANISOU 964 CA ALA A 172 9520 8956 7428 -804 -787 -597 C
ATOM 965 C ALA A 172 -13.475 14.935 37.357 1.00 71.70 C
ANISOU 965 C ALA A 172 9941 9617 7683 -884 -872 -517 C
ATOM 966 O ALA A 172 -14.177 15.086 38.362 1.00 76.61 O
ANISOU 966 O ALA A 172 10750 10190 8168 -870 -789 -570 O
ATOM 967 CB ALA A 172 -14.394 14.414 35.090 1.00 62.22 C
ANISOU 967 CB ALA A 172 8524 8177 6941 -561 -739 -491 C
ATOM 968 N TRP A 173 -12.317 14.266 37.389 1.00 67.09 N
ANISOU 968 N TRP A 173 9124 9297 7071 -949 -1032 -378 N
ATOM 969 CA TRP A 173 -11.762 13.803 38.655 1.00 65.09 C
ANISOU 969 CA TRP A 173 8842 9290 6599 -1034 -1135 -289 C
ATOM 970 C TRP A 173 -11.371 14.970 39.549 1.00 72.74 C
ANISOU 970 C TRP A 173 10053 10311 7275 -1349 -1189 -416 C
ATOM 971 O TRP A 173 -11.561 14.916 40.767 1.00 82.52 O
ANISOU 971 O TRP A 173 11423 11615 8314 -1405 -1190 -422 O
ATOM 972 CB TRP A 173 -10.568 12.900 38.389 1.00 71.39 C
ANISOU 972 CB TRP A 173 9322 10390 7412 -990 -1290 -99 C
ATOM 973 CG TRP A 173 -10.999 11.560 37.888 1.00 75.44 C
ANISOU 973 CG TRP A 173 9690 10835 8139 -675 -1225 39 C
ATOM 974 CD1 TRP A 173 -11.188 11.191 36.594 1.00 69.34 C
ANISOU 974 CD1 TRP A 173 8806 9926 7614 -515 -1168 60 C
ATOM 975 CD2 TRP A 173 -11.332 10.417 38.685 1.00 74.66 C
ANISOU 975 CD2 TRP A 173 9591 10775 8000 -506 -1199 170 C
ATOM 976 NE1 TRP A 173 -11.609 9.890 36.533 1.00 65.76 N
ANISOU 976 NE1 TRP A 173 8303 9415 7266 -275 -1108 189 N
ATOM 977 CE2 TRP A 173 -11.705 9.392 37.803 1.00 68.87 C
ANISOU 977 CE2 TRP A 173 8773 9907 7488 -265 -1123 261 C
ATOM 978 CE3 TRP A 173 -11.351 10.166 40.060 1.00 77.50 C
ANISOU 978 CE3 TRP A 173 10043 11262 8141 -550 -1231 219 C
ATOM 979 CZ2 TRP A 173 -12.090 8.129 38.245 1.00 73.15 C
ANISOU 979 CZ2 TRP A 173 9347 10414 8032 -82 -1072 399 C
ATOM 980 CZ3 TRP A 173 -11.734 8.917 40.498 1.00 79.79 C
ANISOU 980 CZ3 TRP A 173 10339 11533 8446 -348 -1183 364 C
ATOM 981 CH2 TRP A 173 -12.098 7.909 39.590 1.00 77.77 C
ANISOU 981 CH2 TRP A 173 10025 11118 8406 -123 -1101 452 C
ATOM 982 N GLY A 174 -10.832 16.039 38.964 1.00 75.25 N
ANISOU 982 N GLY A 174 10463 10587 7542 -1577 -1230 -522 N
ATOM 983 CA GLY A 174 -10.472 17.201 39.763 1.00 75.38 C
ANISOU 983 CA GLY A 174 10781 10610 7250 -1925 -1271 -659 C
ATOM 984 C GLY A 174 -11.684 17.907 40.336 1.00 77.97 C
ANISOU 984 C GLY A 174 11514 10610 7500 -1860 -1085 -824 C
ATOM 985 O GLY A 174 -11.774 18.120 41.547 1.00 84.73 O
ANISOU 985 O GLY A 174 12572 11511 8109 -1981 -1085 -871 O
ATOM 986 N ILE A 175 -12.644 18.266 39.473 1.00 73.10 N
ANISOU 986 N ILE A 175 11013 9683 7080 -1644 -919 -906 N
ATOM 987 CA ILE A 175 -13.859 18.938 39.941 1.00 75.05 C
ANISOU 987 CA ILE A 175 11620 9646 7248 -1507 -718 -1047 C
ATOM 988 C ILE A 175 -14.628 18.053 40.920 1.00 75.47 C
ANISOU 988 C ILE A 175 11603 9788 7286 -1312 -650 -978 C
ATOM 989 O ILE A 175 -15.226 18.544 41.880 1.00 79.66 O
ANISOU 989 O ILE A 175 12428 10225 7615 -1311 -542 -1076 O
ATOM 990 CB ILE A 175 -14.736 19.372 38.749 1.00 74.81 C
ANISOU 990 CB ILE A 175 11654 9337 7435 -1261 -561 -1108 C
ATOM 991 CG1 ILE A 175 -14.099 20.562 38.028 1.00 80.61 C
ANISOU 991 CG1 ILE A 175 12626 9909 8094 -1490 -591 -1217 C
ATOM 992 CG2 ILE A 175 -16.148 19.759 39.189 1.00 71.95 C
ANISOU 992 CG2 ILE A 175 11547 8766 7024 -996 -336 -1200 C
ATOM 993 CD1 ILE A 175 -14.697 20.834 36.649 1.00 80.11 C
ANISOU 993 CD1 ILE A 175 12538 9630 8270 -1257 -484 -1234 C
ATOM 994 N SER A 176 -14.620 16.745 40.717 1.00 75.08 N
ANISOU 994 N SER A 176 11194 9908 7424 -1152 -701 -810 N
ATOM 995 CA SER A 176 -15.402 15.926 41.632 1.00 79.54 C
ANISOU 995 CA SER A 176 11730 10535 7957 -994 -622 -745 C
ATOM 996 C SER A 176 -14.649 15.597 42.914 1.00 85.09 C
ANISOU 996 C SER A 176 12446 11476 8410 -1182 -754 -682 C
ATOM 997 O SER A 176 -15.288 15.349 43.941 1.00 89.60 O
ANISOU 997 O SER A 176 13131 12063 8851 -1125 -674 -683 O
ATOM 998 CB SER A 176 -15.870 14.642 40.945 1.00 75.90 C
ANISOU 998 CB SER A 176 10961 10109 7767 -754 -591 -598 C
ATOM 999 OG SER A 176 -14.816 13.720 40.843 1.00 82.13 O
ANISOU 999 OG SER A 176 11503 11107 8596 -798 -760 -438 O
ATOM 1000 N ALA A 177 -13.316 15.605 42.898 1.00 82.09 N
ANISOU 1000 N ALA A 177 11940 11314 7937 -1405 -954 -619 N
ATOM 1001 CA ALA A 177 -12.594 15.452 44.157 1.00 76.69 C
ANISOU 1001 CA ALA A 177 11282 10892 6966 -1605 -1088 -566 C
ATOM 1002 C ALA A 177 -12.787 16.657 45.076 1.00 78.97 C
ANISOU 1002 C ALA A 177 11983 11069 6952 -1841 -1034 -754 C
ATOM 1003 O ALA A 177 -12.627 16.521 46.295 1.00 80.31 O
ANISOU 1003 O ALA A 177 12245 11396 6873 -1958 -1083 -736 O
ATOM 1004 CB ALA A 177 -11.106 15.201 43.894 1.00 72.12 C
ANISOU 1004 CB ALA A 177 10426 10646 6330 -1784 -1317 -440 C
ATOM 1005 N LEU A 178 -13.138 17.825 44.521 1.00 80.16 N
ANISOU 1005 N LEU A 178 12418 10937 7101 -1901 -926 -933 N
ATOM 1006 CA LEU A 178 -13.496 18.981 45.345 1.00 81.20 C
ANISOU 1006 CA LEU A 178 13032 10880 6940 -2065 -825 -1126 C
ATOM 1007 C LEU A 178 -14.955 18.931 45.786 1.00 87.34 C
ANISOU 1007 C LEU A 178 13987 11452 7748 -1747 -585 -1184 C
ATOM 1008 O LEU A 178 -15.272 19.298 46.923 1.00 95.03 O
ANISOU 1008 O LEU A 178 15254 12398 8455 -1814 -516 -1269 O
ATOM 1009 CB LEU A 178 -13.230 20.286 44.593 1.00 76.61 C
ANISOU 1009 CB LEU A 178 12751 10055 6304 -2254 -795 -1287 C
ATOM 1010 CG LEU A 178 -11.880 20.963 44.811 1.00 83.14 C
ANISOU 1010 CG LEU A 178 13685 11049 6855 -2753 -990 -1329 C
ATOM 1011 CD1 LEU A 178 -11.928 21.795 46.063 1.00 85.95 C
ANISOU 1011 CD1 LEU A 178 14523 11323 6812 -3015 -952 -1482 C
ATOM 1012 CD2 LEU A 178 -10.742 19.942 44.898 1.00 88.16 C
ANISOU 1012 CD2 LEU A 178 13823 12160 7512 -2876 -1236 -1123 C
ATOM 1013 N LEU A 179 -15.855 18.479 44.909 1.00 85.51 N
ANISOU 1013 N LEU A 179 13571 11105 7815 -1410 -455 -1138 N
ATOM 1014 CA LEU A 179 -17.278 18.470 45.228 1.00 88.17 C
ANISOU 1014 CA LEU A 179 14025 11305 8169 -1108 -220 -1184 C
ATOM 1015 C LEU A 179 -17.642 17.437 46.293 1.00 89.78 C
ANISOU 1015 C LEU A 179 14093 11713 8308 -1043 -212 -1072 C
ATOM 1016 O LEU A 179 -18.693 17.571 46.930 1.00 87.90 O
ANISOU 1016 O LEU A 179 14013 11416 7970 -875 -25 -1126 O
ATOM 1017 CB LEU A 179 -18.096 18.223 43.955 1.00 86.69 C
ANISOU 1017 CB LEU A 179 13631 11008 8300 -808 -106 -1148 C
ATOM 1018 CG LEU A 179 -18.292 19.404 42.995 1.00 86.79 C
ANISOU 1018 CG LEU A 179 13875 10750 8351 -745 -12 -1280 C
ATOM 1019 CD1 LEU A 179 -18.748 18.925 41.626 1.00 86.60 C
ANISOU 1019 CD1 LEU A 179 13539 10705 8660 -518 21 -1200 C
ATOM 1020 CD2 LEU A 179 -19.300 20.395 43.567 1.00 88.21 C
ANISOU 1020 CD2 LEU A 179 14469 10725 8322 -568 221 -1429 C
ATOM 1021 N ALA A 180 -16.805 16.419 46.506 1.00 88.80 N
ANISOU 1021 N ALA A 180 13689 11834 8217 -1154 -400 -910 N
ATOM 1022 CA ALA A 180 -17.098 15.343 47.447 1.00 86.05 C
ANISOU 1022 CA ALA A 180 13221 11664 7811 -1087 -399 -779 C
ATOM 1023 C ALA A 180 -16.215 15.377 48.690 1.00 88.86 C
ANISOU 1023 C ALA A 180 13689 12218 7854 -1344 -549 -759 C
ATOM 1024 O ALA A 180 -16.221 14.415 49.462 1.00 93.97 O
ANISOU 1024 O ALA A 180 14224 13042 8439 -1309 -588 -622 O
ATOM 1025 CB ALA A 180 -16.973 13.978 46.758 1.00 82.97 C
ANISOU 1025 CB ALA A 180 12453 11383 7687 -946 -469 -579 C
ATOM 1026 N SER A 181 -15.466 16.456 48.913 1.00 89.77 N
ANISOU 1026 N SER A 181 14044 12316 7750 -1621 -633 -889 N
ATOM 1027 CA SER A 181 -14.627 16.578 50.105 1.00 89.63 C
ANISOU 1027 CA SER A 181 14142 12519 7394 -1913 -783 -881 C
ATOM 1028 C SER A 181 -15.431 16.794 51.389 1.00 93.42 C
ANISOU 1028 C SER A 181 14930 12946 7621 -1891 -637 -965 C
ATOM 1029 O SER A 181 -14.987 16.347 52.454 1.00103.18 O
ANISOU 1029 O SER A 181 16153 14417 8635 -2027 -747 -884 O
ATOM 1030 CB SER A 181 -13.612 17.706 49.930 1.00 89.08 C
ANISOU 1030 CB SER A 181 14262 12453 7133 -2279 -913 -1005 C
ATOM 1031 OG SER A 181 -14.168 18.766 49.180 1.00 89.21 O
ANISOU 1031 OG SER A 181 14558 12120 7217 -2232 -753 -1185 O
ATOM 1032 N PRO A 182 -16.586 17.477 51.363 1.00 91.68 N
ANISOU 1032 N PRO A 182 14987 12448 7398 -1711 -389 -1119 N
ATOM 1033 CA PRO A 182 -17.479 17.413 52.534 1.00 94.32 C
ANISOU 1033 CA PRO A 182 15528 12778 7530 -1609 -225 -1158 C
ATOM 1034 C PRO A 182 -17.764 15.995 53.009 1.00 94.70 C
ANISOU 1034 C PRO A 182 15267 13049 7664 -1474 -247 -953 C
ATOM 1035 O PRO A 182 -17.864 15.748 54.219 1.00 96.86 O
ANISOU 1035 O PRO A 182 15660 13450 7694 -1541 -238 -930 O
ATOM 1036 CB PRO A 182 -18.741 18.115 52.023 1.00 93.17 C
ANISOU 1036 CB PRO A 182 15574 12352 7476 -1317 53 -1294 C
ATOM 1037 CG PRO A 182 -18.193 19.172 51.139 1.00 93.77 C
ANISOU 1037 CG PRO A 182 15833 12220 7574 -1441 12 -1422 C
ATOM 1038 CD PRO A 182 -17.015 18.540 50.434 1.00 92.00 C
ANISOU 1038 CD PRO A 182 15243 12183 7531 -1625 -250 -1280 C
ATOM 1039 N LEU A 183 -17.880 15.048 52.078 1.00 88.89 N
ANISOU 1039 N LEU A 183 14171 12350 7254 -1298 -274 -802 N
ATOM 1040 CA LEU A 183 -18.055 13.653 52.460 1.00 87.24 C
ANISOU 1040 CA LEU A 183 13719 12316 7112 -1197 -301 -597 C
ATOM 1041 C LEU A 183 -16.851 13.114 53.241 1.00 87.28 C
ANISOU 1041 C LEU A 183 13654 12582 6928 -1393 -539 -461 C
ATOM 1042 O LEU A 183 -16.989 12.145 54.002 1.00 88.65 O
ANISOU 1042 O LEU A 183 13763 12896 7024 -1342 -549 -312 O
ATOM 1043 CB LEU A 183 -18.316 12.808 51.208 1.00 83.65 C
ANISOU 1043 CB LEU A 183 12949 11813 7021 -1004 -288 -476 C
ATOM 1044 CG LEU A 183 -19.681 12.957 50.524 1.00 86.32 C
ANISOU 1044 CG LEU A 183 13266 11988 7543 -780 -51 -546 C
ATOM 1045 CD1 LEU A 183 -19.658 12.407 49.101 1.00 85.17 C
ANISOU 1045 CD1 LEU A 183 12845 11781 7735 -666 -83 -464 C
ATOM 1046 CD2 LEU A 183 -20.765 12.262 51.332 1.00 84.75 C
ANISOU 1046 CD2 LEU A 183 13070 11870 7263 -678 114 -481 C
ATOM 1047 N ALA A 184 -15.673 13.718 53.076 1.00 82.42 N
ANISOU 1047 N ALA A 184 13046 12059 6212 -1623 -730 -498 N
ATOM 1048 CA ALA A 184 -14.451 13.191 53.675 1.00 82.90 C
ANISOU 1048 CA ALA A 184 12962 12443 6094 -1790 -975 -342 C
ATOM 1049 C ALA A 184 -14.111 13.837 54.998 1.00 92.12 C
ANISOU 1049 C ALA A 184 14404 13746 6853 -2064 -1034 -430 C
ATOM 1050 O ALA A 184 -13.488 13.193 55.852 1.00 98.78 O
ANISOU 1050 O ALA A 184 15154 14878 7501 -2138 -1184 -277 O
ATOM 1051 CB ALA A 184 -13.259 13.386 52.737 1.00 85.25 C
ANISOU 1051 CB ALA A 184 13040 12867 6486 -1911 -1172 -300 C
ATOM 1052 N ILE A 185 -14.498 15.092 55.186 1.00 92.28 N
ANISOU 1052 N ILE A 185 14785 13559 6720 -2208 -917 -669 N
ATOM 1053 CA ILE A 185 -14.156 15.829 56.387 1.00 94.71 C
ANISOU 1053 CA ILE A 185 15420 13957 6610 -2510 -965 -784 C
ATOM 1054 C ILE A 185 -15.229 15.691 57.455 1.00 93.58 C
ANISOU 1054 C ILE A 185 15513 13732 6312 -2377 -766 -828 C
ATOM 1055 O ILE A 185 -14.915 15.525 58.634 1.00 93.03 O
ANISOU 1055 O ILE A 185 15547 13866 5935 -2539 -847 -789 O
ATOM 1056 CB ILE A 185 -13.892 17.301 56.022 1.00 95.10 C
ANISOU 1056 CB ILE A 185 15808 13799 6527 -2770 -944 -1024 C
ATOM 1057 CG1 ILE A 185 -12.758 17.329 55.000 1.00 94.27 C
ANISOU 1057 CG1 ILE A 185 15418 13841 6559 -2930 -1156 -952 C
ATOM 1058 CG2 ILE A 185 -13.581 18.118 57.278 1.00 94.36 C
ANISOU 1058 CG2 ILE A 185 16129 13760 5963 -3121 -977 -1168 C
ATOM 1059 CD1 ILE A 185 -12.477 18.655 54.425 1.00 92.75 C
ANISOU 1059 CD1 ILE A 185 15525 13430 6285 -3184 -1137 -1160 C
ATOM 1060 N PHE A 186 -16.498 15.712 57.064 1.00 93.00 N
ANISOU 1060 N PHE A 186 15499 13403 6434 -2080 -508 -893 N
ATOM 1061 CA PHE A 186 -17.573 15.593 58.037 1.00 96.79 C
ANISOU 1061 CA PHE A 186 16174 13841 6762 -1941 -297 -930 C
ATOM 1062 C PHE A 186 -17.902 14.142 58.369 1.00 98.86 C
ANISOU 1062 C PHE A 186 16144 14286 7133 -1773 -303 -697 C
ATOM 1063 O PHE A 186 -19.064 13.814 58.634 1.00 99.27 O
ANISOU 1063 O PHE A 186 16221 14277 7221 -1568 -84 -692 O
ATOM 1064 CB PHE A 186 -18.802 16.354 57.544 1.00 96.62 C
ANISOU 1064 CB PHE A 186 16351 13521 6841 -1696 -5 -1102 C
ATOM 1065 CG PHE A 186 -18.531 17.812 57.305 1.00 97.49 C
ANISOU 1065 CG PHE A 186 16849 13395 6796 -1843 30 -1334 C
ATOM 1066 CD1 PHE A 186 -18.657 18.729 58.336 1.00 95.53 C
ANISOU 1066 CD1 PHE A 186 17083 13053 6160 -1983 127 -1512 C
ATOM 1067 CD2 PHE A 186 -18.109 18.260 56.059 1.00 93.90 C
ANISOU 1067 CD2 PHE A 186 16316 12800 6560 -1861 -35 -1373 C
ATOM 1068 CE1 PHE A 186 -18.398 20.069 58.125 1.00 95.70 C
ANISOU 1068 CE1 PHE A 186 17541 12814 6007 -2139 171 -1728 C
ATOM 1069 CE2 PHE A 186 -17.844 19.600 55.839 1.00 94.10 C
ANISOU 1069 CE2 PHE A 186 16751 12582 6420 -2022 3 -1581 C
ATOM 1070 CZ PHE A 186 -17.988 20.507 56.876 1.00 97.97 C
ANISOU 1070 CZ PHE A 186 17759 12950 6514 -2165 108 -1760 C
ATOM 1071 N ARG A 187 -16.904 13.262 58.344 1.00 95.02 N
ANISOU 1071 N ARG A 187 15389 14031 6682 -1851 -541 -495 N
ATOM 1072 CA ARG A 187 -16.991 11.937 58.934 1.00 90.78 C
ANISOU 1072 CA ARG A 187 14684 13672 6135 -1746 -576 -266 C
ATOM 1073 C ARG A 187 -16.312 11.969 60.297 1.00 96.15 C
ANISOU 1073 C ARG A 187 15515 14599 6419 -1969 -718 -229 C
ATOM 1074 O ARG A 187 -15.334 12.695 60.500 1.00102.64 O
ANISOU 1074 O ARG A 187 16416 15548 7036 -2232 -894 -301 O
ATOM 1075 CB ARG A 187 -16.322 10.887 58.045 1.00 88.40 C
ANISOU 1075 CB ARG A 187 14026 13461 6100 -1627 -733 -46 C
ATOM 1076 CG ARG A 187 -17.198 10.300 56.970 1.00 85.38 C
ANISOU 1076 CG ARG A 187 13481 12879 6082 -1379 -575 -4 C
ATOM 1077 CD ARG A 187 -18.007 9.090 57.434 1.00 87.17 C
ANISOU 1077 CD ARG A 187 13676 13117 6328 -1232 -455 159 C
ATOM 1078 NE ARG A 187 -19.172 8.919 56.564 1.00 90.25 N
ANISOU 1078 NE ARG A 187 13991 13313 6987 -1070 -244 116 N
ATOM 1079 CZ ARG A 187 -19.981 7.866 56.552 1.00 93.82 C
ANISOU 1079 CZ ARG A 187 14379 13740 7529 -966 -120 247 C
ATOM 1080 NH1 ARG A 187 -19.774 6.837 57.366 1.00 89.91 N
ANISOU 1080 NH1 ARG A 187 13920 13356 6887 -980 -173 437 N
ATOM 1081 NH2 ARG A 187 -21.004 7.848 55.708 1.00 98.15 N
ANISOU 1081 NH2 ARG A 187 14836 14161 8296 -862 58 193 N
ATOM 1082 N GLU A 188 -16.835 11.186 61.237 1.00 94.83 N
ANISOU 1082 N GLU A 188 15392 14518 6122 -1891 -643 -113 N
ATOM 1083 CA GLU A 188 -16.265 11.151 62.575 1.00102.78 C
ANISOU 1083 CA GLU A 188 16543 15771 6738 -2087 -771 -63 C
ATOM 1084 C GLU A 188 -15.933 9.718 62.976 1.00103.61 C
ANISOU 1084 C GLU A 188 16448 16084 6835 -1966 -883 236 C
ATOM 1085 O GLU A 188 -16.693 8.783 62.694 1.00 98.65 O
ANISOU 1085 O GLU A 188 15729 15342 6411 -1745 -746 357 O
ATOM 1086 CB GLU A 188 -17.207 11.795 63.611 1.00109.32 C
ANISOU 1086 CB GLU A 188 17733 16505 7300 -2141 -555 -240 C
ATOM 1087 CG GLU A 188 -18.607 11.196 63.677 1.00110.08 C
ANISOU 1087 CG GLU A 188 17826 16469 7529 -1891 -280 -207 C
ATOM 1088 CD GLU A 188 -19.106 11.028 65.106 1.00112.39 C
ANISOU 1088 CD GLU A 188 18346 16873 7483 -1944 -177 -197 C
ATOM 1089 OE1 GLU A 188 -18.326 10.535 65.952 1.00114.12 O
ANISOU 1089 OE1 GLU A 188 18569 17325 7468 -2080 -366 -54 O
ATOM 1090 OE2 GLU A 188 -20.273 11.390 65.380 1.00112.42 O
ANISOU 1090 OE2 GLU A 188 18515 16758 7442 -1836 94 -324 O
ATOM 1091 N TYR A 189 -14.785 9.559 63.635 1.00103.63 N
ANISOU 1091 N TYR A 189 16397 16402 6575 -2121 -1133 359 N
ATOM 1092 CA TYR A 189 -14.327 8.275 64.156 1.00102.79 C
ANISOU 1092 CA TYR A 189 16147 16525 6385 -1993 -1258 658 C
ATOM 1093 C TYR A 189 -14.368 8.343 65.677 1.00104.56 C
ANISOU 1093 C TYR A 189 16604 16934 6191 -2152 -1274 666 C
ATOM 1094 O TYR A 189 -13.535 9.022 66.287 1.00105.34 O
ANISOU 1094 O TYR A 189 16748 17258 6020 -2397 -1445 603 O
ATOM 1095 CB TYR A 189 -12.910 7.967 63.667 1.00 99.55 C
ANISOU 1095 CB TYR A 189 15436 16401 5986 -1988 -1543 835 C
ATOM 1096 CG TYR A 189 -12.397 6.580 64.019 1.00 99.63 C
ANISOU 1096 CG TYR A 189 15294 16626 5936 -1761 -1662 1173 C
ATOM 1097 CD1 TYR A 189 -12.850 5.471 63.328 1.00101.60 C
ANISOU 1097 CD1 TYR A 189 15461 16665 6477 -1449 -1552 1336 C
ATOM 1098 CD2 TYR A 189 -11.442 6.381 65.022 1.00 99.01 C
ANISOU 1098 CD2 TYR A 189 15174 16960 5486 -1855 -1883 1334 C
ATOM 1099 CE1 TYR A 189 -12.390 4.200 63.620 1.00101.03 C
ANISOU 1099 CE1 TYR A 189 15320 16734 6332 -1213 -1639 1647 C
ATOM 1100 CE2 TYR A 189 -10.965 5.105 65.319 1.00 96.06 C
ANISOU 1100 CE2 TYR A 189 14680 16765 5055 -1585 -1979 1659 C
ATOM 1101 CZ TYR A 189 -11.455 4.020 64.606 1.00103.74 C
ANISOU 1101 CZ TYR A 189 15626 17475 6316 -1258 -1849 1814 C
ATOM 1102 OH TYR A 189 -11.025 2.738 64.853 1.00107.08 O
ANISOU 1102 OH TYR A 189 16006 18015 6663 -965 -1918 2139 O
ATOM 1103 N SER A 190 -15.321 7.652 66.296 1.00104.23 N
ANISOU 1103 N SER A 190 16695 16791 6115 -2024 -1092 737 N
ATOM 1104 CA SER A 190 -15.310 7.585 67.754 1.00115.28 C
ANISOU 1104 CA SER A 190 18305 18388 7110 -2158 -1116 778 C
ATOM 1105 C SER A 190 -16.179 6.422 68.221 1.00116.29 C
ANISOU 1105 C SER A 190 18493 18433 7257 -1968 -951 956 C
ATOM 1106 O SER A 190 -16.841 5.746 67.426 1.00112.44 O
ANISOU 1106 O SER A 190 17910 17730 7083 -1770 -808 1024 O
ATOM 1107 CB SER A 190 -15.762 8.905 68.391 1.00118.37 C
ANISOU 1107 CB SER A 190 18965 18668 7342 -2357 -987 469 C
ATOM 1108 OG SER A 190 -15.293 9.014 69.731 1.00118.83 O
ANISOU 1108 OG SER A 190 19105 18909 7137 -2473 -1080 487 O
ATOM 1109 N LEU A 191 -16.175 6.214 69.539 1.00117.30 N
ANISOU 1109 N LEU A 191 18778 18716 7073 -2038 -964 1019 N
ATOM 1110 CA LEU A 191 -16.802 5.063 70.171 1.00113.02 C
ANISOU 1110 CA LEU A 191 18329 18158 6454 -1910 -848 1225 C
ATOM 1111 C LEU A 191 -18.278 5.341 70.431 1.00112.63 C
ANISOU 1111 C LEU A 191 18487 17916 6391 -1943 -526 1059 C
ATOM 1112 O LEU A 191 -18.652 6.453 70.819 1.00107.58 O
ANISOU 1112 O LEU A 191 17983 17230 5664 -2055 -420 800 O
ATOM 1113 CB LEU A 191 -16.085 4.720 71.484 1.00112.17 C
ANISOU 1113 CB LEU A 191 18246 18287 6086 -1921 -1001 1363 C
ATOM 1114 CG LEU A 191 -14.634 4.195 71.509 1.00113.89 C
ANISOU 1114 CG LEU A 191 18241 18771 6260 -1822 -1306 1592 C
ATOM 1115 CD1 LEU A 191 -14.494 2.865 70.765 1.00112.73 C
ANISOU 1115 CD1 LEU A 191 17991 18575 6267 -1550 -1334 1892 C
ATOM 1116 CD2 LEU A 191 -13.603 5.220 70.994 1.00116.23 C
ANISOU 1116 CD2 LEU A 191 18346 19211 6607 -1969 -1506 1446 C
ATOM 1117 N ILE A 192 -19.114 4.334 70.161 1.00116.78 N
ANISOU 1117 N ILE A 192 18990 18295 7085 -1798 -356 1199 N
ATOM 1118 CA ILE A 192 -20.500 4.270 70.622 1.00114.59 C
ANISOU 1118 CA ILE A 192 18860 17923 6755 -1814 -54 1124 C
ATOM 1119 C ILE A 192 -20.773 2.828 71.029 1.00117.71 C
ANISOU 1119 C ILE A 192 19309 18319 7095 -1750 -12 1410 C
ATOM 1120 O ILE A 192 -20.451 1.897 70.284 1.00120.24 O
ANISOU 1120 O ILE A 192 19517 18540 7629 -1620 -86 1602 O
ATOM 1121 CB ILE A 192 -21.513 4.748 69.555 1.00110.08 C
ANISOU 1121 CB ILE A 192 18177 17142 6507 -1739 172 939 C
ATOM 1122 CG1 ILE A 192 -22.862 5.067 70.201 1.00109.08 C
ANISOU 1122 CG1 ILE A 192 18191 17022 6232 -1770 478 810 C
ATOM 1123 CG2 ILE A 192 -21.716 3.725 68.420 1.00106.68 C
ANISOU 1123 CG2 ILE A 192 17551 16553 6428 -1604 193 1102 C
ATOM 1124 CD1 ILE A 192 -24.010 5.074 69.217 1.00110.05 C
ANISOU 1124 CD1 ILE A 192 18154 17010 6651 -1665 717 733 C
ATOM 1125 N GLU A 193 -21.315 2.629 72.227 1.00120.65 N
ANISOU 1125 N GLU A 193 19858 18777 7208 -1818 108 1437 N
ATOM 1126 CA GLU A 193 -21.671 1.293 72.692 1.00120.68 C
ANISOU 1126 CA GLU A 193 19946 18750 7158 -1773 177 1694 C
ATOM 1127 C GLU A 193 -23.191 1.177 72.730 1.00120.66 C
ANISOU 1127 C GLU A 193 19988 18670 7186 -1840 505 1618 C
ATOM 1128 O GLU A 193 -23.852 1.875 73.510 1.00117.40 O
ANISOU 1128 O GLU A 193 19635 18342 6628 -1897 661 1448 O
ATOM 1129 CB GLU A 193 -21.062 0.984 74.063 1.00120.54 C
ANISOU 1129 CB GLU A 193 20035 18895 6869 -1764 49 1819 C
ATOM 1130 CG GLU A 193 -19.924 -0.053 74.023 1.00122.06 C
ANISOU 1130 CG GLU A 193 20204 19131 7042 -1609 -192 2120 C
ATOM 1131 CD GLU A 193 -18.537 0.567 73.843 1.00124.44 C
ANISOU 1131 CD GLU A 193 20346 19613 7322 -1568 -490 2095 C
ATOM 1132 OE1 GLU A 193 -18.413 1.806 73.950 1.00123.82 O
ANISOU 1132 OE1 GLU A 193 20223 19614 7208 -1706 -520 1839 O
ATOM 1133 OE2 GLU A 193 -17.564 -0.183 73.598 1.00128.67 O
ANISOU 1133 OE2 GLU A 193 20806 20214 7870 -1392 -686 2332 O
ATOM 1134 N ILE A 194 -23.735 0.315 71.859 1.00124.37 N
ANISOU 1134 N ILE A 194 20420 18993 7842 -1831 612 1742 N
ATOM 1135 CA ILE A 194 -25.159 -0.004 71.885 1.00125.68 C
ANISOU 1135 CA ILE A 194 20583 19135 8034 -1920 912 1717 C
ATOM 1136 C ILE A 194 -25.536 -0.585 73.240 1.00133.83 C
ANISOU 1136 C ILE A 194 21761 20253 8836 -1974 996 1829 C
ATOM 1137 O ILE A 194 -26.513 -0.163 73.870 1.00139.77 O
ANISOU 1137 O ILE A 194 22509 21119 9477 -2038 1211 1705 O
ATOM 1138 CB ILE A 194 -25.509 -0.976 70.744 1.00123.28 C
ANISOU 1138 CB ILE A 194 20199 18638 8002 -1915 968 1853 C
ATOM 1139 CG1 ILE A 194 -24.692 -0.644 69.491 1.00117.69 C
ANISOU 1139 CG1 ILE A 194 19296 17792 7628 -1761 786 1793 C
ATOM 1140 CG2 ILE A 194 -26.993 -0.902 70.444 1.00123.67 C
ANISOU 1140 CG2 ILE A 194 20137 18732 8121 -2031 1269 1751 C
ATOM 1141 CD1 ILE A 194 -24.739 -1.709 68.445 1.00116.00 C
ANISOU 1141 CD1 ILE A 194 19051 17359 7666 -1726 787 1953 C
ATOM 1142 N ILE A 195 -24.772 -1.570 73.703 1.00135.82 N
ANISOU 1142 N ILE A 195 22145 20459 9002 -1924 835 2074 N
ATOM 1143 CA ILE A 195 -24.900 -2.129 75.050 1.00137.79 C
ANISOU 1143 CA ILE A 195 22555 20790 9008 -1955 869 2199 C
ATOM 1144 C ILE A 195 -23.451 -2.240 75.536 1.00134.10 C
ANISOU 1144 C ILE A 195 22147 20391 8412 -1820 570 2330 C
ATOM 1145 O ILE A 195 -22.555 -1.796 74.799 1.00134.07 O
ANISOU 1145 O ILE A 195 22031 20390 8518 -1733 377 2292 O
ATOM 1146 CB ILE A 195 -25.662 -3.466 75.023 1.00139.07 C
ANISOU 1146 CB ILE A 195 22825 20812 9204 -2034 1029 2404 C
ATOM 1147 CG1 ILE A 195 -24.925 -4.447 74.128 1.00137.17 C
ANISOU 1147 CG1 ILE A 195 22646 20350 9121 -1923 885 2618 C
ATOM 1148 CG2 ILE A 195 -27.116 -3.266 74.552 1.00138.56 C
ANISOU 1148 CG2 ILE A 195 22633 20764 9251 -2191 1318 2265 C
ATOM 1149 CD1 ILE A 195 -25.341 -5.860 74.294 1.00139.56 C
ANISOU 1149 CD1 ILE A 195 23146 20473 9407 -1977 986 2851 C
ATOM 1150 N PRO A 196 -23.119 -2.811 76.806 1.00128.00 N
ANISOU 1150 N PRO A 196 21531 19715 7387 -1790 511 2494 N
ATOM 1151 CA PRO A 196 -21.722 -2.893 77.269 1.00127.97 C
ANISOU 1151 CA PRO A 196 21539 19842 7243 -1641 222 2628 C
ATOM 1152 C PRO A 196 -20.829 -3.965 76.620 1.00131.45 C
ANISOU 1152 C PRO A 196 21997 20174 7774 -1429 57 2910 C
ATOM 1153 O PRO A 196 -20.092 -4.677 77.303 1.00135.69 O
ANISOU 1153 O PRO A 196 22629 20791 8137 -1274 -74 3139 O
ATOM 1154 CB PRO A 196 -21.875 -3.172 78.768 1.00126.70 C
ANISOU 1154 CB PRO A 196 21538 19813 6788 -1677 261 2705 C
ATOM 1155 CG PRO A 196 -23.276 -2.836 79.114 1.00124.47 C
ANISOU 1155 CG PRO A 196 21292 19512 6488 -1859 552 2536 C
ATOM 1156 CD PRO A 196 -24.062 -3.132 77.899 1.00125.85 C
ANISOU 1156 CD PRO A 196 21390 19494 6932 -1905 714 2513 C
ATOM 1157 N ASP A 197 -20.915 -4.090 75.292 1.00133.28 N
ANISOU 1157 N ASP A 197 22145 20225 8271 -1398 77 2898 N
ATOM 1158 CA ASP A 197 -19.912 -4.797 74.503 1.00137.50 C
ANISOU 1158 CA ASP A 197 22656 20676 8910 -1163 -104 3113 C
ATOM 1159 C ASP A 197 -18.598 -4.035 74.597 1.00136.37 C
ANISOU 1159 C ASP A 197 22327 20800 8686 -1047 -389 3080 C
ATOM 1160 O ASP A 197 -18.572 -2.826 74.353 1.00132.20 O
ANISOU 1160 O ASP A 197 21640 20379 8211 -1185 -428 2822 O
ATOM 1161 CB ASP A 197 -20.380 -4.907 73.050 1.00136.55 C
ANISOU 1161 CB ASP A 197 22482 20309 9093 -1192 -7 3056 C
ATOM 1162 CG ASP A 197 -20.852 -6.291 72.703 1.00139.53 C
ANISOU 1162 CG ASP A 197 23068 20391 9555 -1146 133 3269 C
ATOM 1163 OD1 ASP A 197 -21.718 -6.827 73.433 1.00142.25 O
ANISOU 1163 OD1 ASP A 197 23575 20678 9796 -1286 315 3311 O
ATOM 1164 OD2 ASP A 197 -20.340 -6.844 71.706 1.00136.46 O
ANISOU 1164 OD2 ASP A 197 22690 19825 9334 -976 60 3392 O
ATOM 1165 N PHE A 198 -17.509 -4.728 74.965 1.00139.25 N
ANISOU 1165 N PHE A 198 22710 21286 8912 -793 -581 3337 N
ATOM 1166 CA PHE A 198 -16.361 -3.996 75.492 1.00139.73 C
ANISOU 1166 CA PHE A 198 22606 21675 8809 -737 -837 3296 C
ATOM 1167 C PHE A 198 -15.541 -3.337 74.389 1.00138.58 C
ANISOU 1167 C PHE A 198 22197 21608 8850 -691 -1019 3207 C
ATOM 1168 O PHE A 198 -14.741 -2.439 74.669 1.00141.55 O
ANISOU 1168 O PHE A 198 22394 22245 9144 -761 -1210 3082 O
ATOM 1169 CB PHE A 198 -15.504 -4.881 76.404 1.00137.23 C
ANISOU 1169 CB PHE A 198 22393 21510 8237 -472 -975 3588 C
ATOM 1170 CG PHE A 198 -15.748 -4.583 77.843 1.00138.45 C
ANISOU 1170 CG PHE A 198 22658 21829 8118 -618 -948 3527 C
ATOM 1171 CD1 PHE A 198 -16.931 -3.974 78.215 1.00137.03 C
ANISOU 1171 CD1 PHE A 198 22550 21569 7947 -918 -735 3292 C
ATOM 1172 CD2 PHE A 198 -14.797 -4.839 78.826 1.00144.01 C
ANISOU 1172 CD2 PHE A 198 23399 22772 8548 -455 -1136 3685 C
ATOM 1173 CE1 PHE A 198 -17.200 -3.659 79.534 1.00141.06 C
ANISOU 1173 CE1 PHE A 198 23169 22223 8204 -1052 -695 3223 C
ATOM 1174 CE2 PHE A 198 -15.057 -4.525 80.159 1.00143.52 C
ANISOU 1174 CE2 PHE A 198 23444 22859 8229 -611 -1107 3617 C
ATOM 1175 CZ PHE A 198 -16.267 -3.933 80.507 1.00142.44 C
ANISOU 1175 CZ PHE A 198 23380 22631 8111 -911 -883 3385 C
ATOM 1176 N GLU A 199 -15.747 -3.724 73.131 1.00134.60 N
ANISOU 1176 N GLU A 199 21662 20880 8599 -610 -958 3252 N
ATOM 1177 CA GLU A 199 -15.144 -3.016 72.005 1.00133.66 C
ANISOU 1177 CA GLU A 199 21280 20823 8682 -607 -1097 3137 C
ATOM 1178 C GLU A 199 -16.141 -2.926 70.857 1.00130.79 C
ANISOU 1178 C GLU A 199 20947 20160 8589 -730 -904 3009 C
ATOM 1179 O GLU A 199 -16.518 -3.952 70.277 1.00131.67 O
ANISOU 1179 O GLU A 199 21212 19999 8816 -606 -791 3176 O
ATOM 1180 CB GLU A 199 -13.857 -3.709 71.527 1.00134.17 C
ANISOU 1180 CB GLU A 199 21223 20989 8766 -258 -1312 3396 C
ATOM 1181 CG GLU A 199 -12.732 -3.797 72.559 1.00136.28 C
ANISOU 1181 CG GLU A 199 21441 21558 8780 -120 -1534 3520 C
ATOM 1182 CD GLU A 199 -12.071 -2.457 72.890 1.00135.19 C
ANISOU 1182 CD GLU A 199 21030 21755 8582 -351 -1714 3287 C
ATOM 1183 OE1 GLU A 199 -12.768 -1.421 72.985 1.00132.32 O
ANISOU 1183 OE1 GLU A 199 20663 21370 8241 -666 -1614 3003 O
ATOM 1184 OE2 GLU A 199 -10.834 -2.445 73.075 1.00136.48 O
ANISOU 1184 OE2 GLU A 199 20997 22194 8667 -227 -1952 3386 O
ATOM 1185 N ILE A 200 -16.565 -1.706 70.534 1.00127.34 N
ANISOU 1185 N ILE A 200 20392 19749 8241 -968 -857 2707 N
ATOM 1186 CA ILE A 200 -17.301 -1.444 69.301 1.00122.88 C
ANISOU 1186 CA ILE A 200 19718 18904 8068 -989 -694 2524 C
ATOM 1187 C ILE A 200 -17.117 0.031 68.948 1.00114.66 C
ANISOU 1187 C ILE A 200 18475 17972 7117 -1139 -755 2220 C
ATOM 1188 O ILE A 200 -17.063 0.896 69.831 1.00120.16 O
ANISOU 1188 O ILE A 200 19231 18864 7561 -1324 -790 2078 O
ATOM 1189 CB ILE A 200 -18.789 -1.846 69.436 1.00121.88 C
ANISOU 1189 CB ILE A 200 19782 18539 7987 -1114 -390 2471 C
ATOM 1190 CG1 ILE A 200 -19.520 -1.797 68.094 1.00116.05 C
ANISOU 1190 CG1 ILE A 200 18915 17536 7643 -1109 -234 2338 C
ATOM 1191 CG2 ILE A 200 -19.524 -1.012 70.478 1.00123.19 C
ANISOU 1191 CG2 ILE A 200 20048 18842 7918 -1343 -265 2278 C
ATOM 1192 CD1 ILE A 200 -20.912 -2.394 68.192 1.00118.87 C
ANISOU 1192 CD1 ILE A 200 19434 17718 8014 -1242 48 2344 C
ATOM 1193 N VAL A 201 -16.967 0.304 67.651 1.00105.23 N
ANISOU 1193 N VAL A 201 17077 16642 6263 -1063 -770 2128 N
ATOM 1194 CA VAL A 201 -16.700 1.641 67.113 1.00106.60 C
ANISOU 1194 CA VAL A 201 17077 16875 6553 -1185 -833 1861 C
ATOM 1195 C VAL A 201 -17.448 1.781 65.795 1.00 98.01 C
ANISOU 1195 C VAL A 201 15881 15497 5863 -1136 -669 1721 C
ATOM 1196 O VAL A 201 -17.395 0.885 64.947 1.00 96.85 O
ANISOU 1196 O VAL A 201 15671 15190 5939 -964 -657 1871 O
ATOM 1197 CB VAL A 201 -15.191 1.899 66.888 1.00105.97 C
ANISOU 1197 CB VAL A 201 16788 17065 6412 -1135 -1134 1943 C
ATOM 1198 CG1 VAL A 201 -14.485 0.633 66.417 1.00107.41 C
ANISOU 1198 CG1 VAL A 201 16884 17251 6675 -836 -1241 2257 C
ATOM 1199 CG2 VAL A 201 -14.983 3.010 65.855 1.00100.26 C
ANISOU 1199 CG2 VAL A 201 15878 16291 5925 -1225 -1168 1701 C
ATOM 1200 N ALA A 202 -18.144 2.892 65.618 1.00 95.44 N
ANISOU 1200 N ALA A 202 15554 15101 5607 -1273 -536 1441 N
ATOM 1201 CA ALA A 202 -18.869 3.131 64.381 1.00100.28 C
ANISOU 1201 CA ALA A 202 16046 15480 6574 -1222 -385 1304 C
ATOM 1202 C ALA A 202 -18.259 4.310 63.630 1.00102.04 C
ANISOU 1202 C ALA A 202 16126 15717 6927 -1265 -497 1107 C
ATOM 1203 O ALA A 202 -17.386 5.028 64.132 1.00102.68 O
ANISOU 1203 O ALA A 202 16224 15989 6802 -1384 -670 1048 O
ATOM 1204 CB ALA A 202 -20.361 3.366 64.653 1.00100.20 C
ANISOU 1204 CB ALA A 202 16146 15370 6556 -1294 -94 1163 C
ATOM 1205 N CYS A 203 -18.724 4.492 62.397 1.00103.67 N
ANISOU 1205 N CYS A 203 16200 15726 7464 -1190 -399 1010 N
ATOM 1206 CA CYS A 203 -18.241 5.552 61.520 1.00106.26 C
ANISOU 1206 CA CYS A 203 16405 16020 7949 -1221 -480 830 C
ATOM 1207 C CYS A 203 -19.462 6.233 60.915 1.00105.14 C
ANISOU 1207 C CYS A 203 16277 15684 7988 -1204 -239 618 C
ATOM 1208 O CYS A 203 -20.219 5.604 60.168 1.00103.17 O
ANISOU 1208 O CYS A 203 15932 15297 7972 -1100 -105 669 O
ATOM 1209 CB CYS A 203 -17.310 4.981 60.446 1.00108.45 C
ANISOU 1209 CB CYS A 203 16462 16286 8458 -1090 -650 975 C
ATOM 1210 SG CYS A 203 -16.639 6.156 59.236 1.00112.35 S
ANISOU 1210 SG CYS A 203 16781 16745 9161 -1138 -758 786 S
ATOM 1211 N THR A 204 -19.658 7.509 61.249 1.00106.46 N
ANISOU 1211 N THR A 204 16580 15850 8021 -1304 -179 386 N
ATOM 1212 CA THR A 204 -20.848 8.256 60.862 1.00106.08 C
ANISOU 1212 CA THR A 204 16580 15654 8072 -1241 70 189 C
ATOM 1213 C THR A 204 -20.471 9.684 60.479 1.00105.53 C
ANISOU 1213 C THR A 204 16607 15500 7990 -1302 37 -43 C
ATOM 1214 O THR A 204 -19.342 10.137 60.692 1.00105.07 O
ANISOU 1214 O THR A 204 16602 15524 7797 -1457 -171 -67 O
ATOM 1215 CB THR A 204 -21.887 8.280 61.992 1.00106.84 C
ANISOU 1215 CB THR A 204 16860 15816 7919 -1255 284 149 C
ATOM 1216 OG1 THR A 204 -22.842 9.321 61.746 1.00108.70 O
ANISOU 1216 OG1 THR A 204 17174 15956 8171 -1171 508 -70 O
ATOM 1217 CG2 THR A 204 -21.208 8.525 63.335 1.00106.30 C
ANISOU 1217 CG2 THR A 204 17011 15903 7475 -1416 166 149 C
ATOM 1218 N GLU A 205 -21.445 10.396 59.918 1.00103.53 N
ANISOU 1218 N GLU A 205 16385 15098 7855 -1185 250 -208 N
ATOM 1219 CA GLU A 205 -21.268 11.782 59.512 1.00104.15 C
ANISOU 1219 CA GLU A 205 16624 15036 7914 -1209 269 -435 C
ATOM 1220 C GLU A 205 -21.537 12.721 60.684 1.00107.97 C
ANISOU 1220 C GLU A 205 17473 15522 8029 -1291 382 -606 C
ATOM 1221 O GLU A 205 -22.442 12.487 61.489 1.00108.97 O
ANISOU 1221 O GLU A 205 17684 15717 8002 -1215 568 -598 O
ATOM 1222 CB GLU A 205 -22.204 12.122 58.350 1.00101.92 C
ANISOU 1222 CB GLU A 205 16226 14592 7908 -996 455 -519 C
ATOM 1223 CG GLU A 205 -22.083 11.194 57.160 1.00100.66 C
ANISOU 1223 CG GLU A 205 15731 14412 8102 -919 374 -365 C
ATOM 1224 CD GLU A 205 -23.394 11.029 56.419 1.00102.63 C
ANISOU 1224 CD GLU A 205 15825 14617 8551 -720 602 -375 C
ATOM 1225 OE1 GLU A 205 -24.448 11.376 56.996 1.00105.55 O
ANISOU 1225 OE1 GLU A 205 16297 15038 8769 -626 827 -450 O
ATOM 1226 OE2 GLU A 205 -23.371 10.548 55.264 1.00100.68 O
ANISOU 1226 OE2 GLU A 205 15345 14312 8595 -658 557 -302 O
ATOM 1227 N LYS A 206 -20.749 13.792 60.772 1.00106.65 N
ANISOU 1227 N LYS A 206 17543 15281 7700 -1464 276 -764 N
ATOM 1228 CA LYS A 206 -20.934 14.805 61.807 1.00105.02 C
ANISOU 1228 CA LYS A 206 17760 15024 7118 -1563 387 -955 C
ATOM 1229 C LYS A 206 -20.671 16.178 61.202 1.00108.04 C
ANISOU 1229 C LYS A 206 18413 15164 7475 -1618 411 -1180 C
ATOM 1230 O LYS A 206 -19.529 16.501 60.856 1.00109.34 O
ANISOU 1230 O LYS A 206 18580 15335 7629 -1863 182 -1196 O
ATOM 1231 CB LYS A 206 -20.022 14.549 63.006 1.00103.80 C
ANISOU 1231 CB LYS A 206 17720 15084 6636 -1846 186 -889 C
ATOM 1232 CG LYS A 206 -20.130 15.613 64.109 1.00111.53 C
ANISOU 1232 CG LYS A 206 19184 16004 7188 -1997 287 -1099 C
ATOM 1233 CD LYS A 206 -21.586 15.999 64.419 1.00112.22 C
ANISOU 1233 CD LYS A 206 19473 15956 7211 -1718 647 -1220 C
ATOM 1234 CE LYS A 206 -22.369 14.875 65.096 1.00111.09 C
ANISOU 1234 CE LYS A 206 19138 16014 7059 -1582 757 -1046 C
ATOM 1235 NZ LYS A 206 -22.135 14.820 66.572 1.00111.78 N
ANISOU 1235 NZ LYS A 206 19467 16255 6750 -1769 723 -1044 N
ATOM 1236 N TRP A 207 -21.729 16.990 61.099 1.00105.97 N
ANISOU 1236 N TRP A 207 18388 14701 7173 -1388 696 -1346 N
ATOM 1237 CA TRP A 207 -21.883 18.346 60.590 1.00103.05 C
ANISOU 1237 CA TRP A 207 18370 14037 6747 -1326 825 -1570 C
ATOM 1238 C TRP A 207 -21.774 19.370 61.718 1.00104.76 C
ANISOU 1238 C TRP A 207 19100 14139 6566 -1472 899 -1755 C
ATOM 1239 O TRP A 207 -22.258 19.120 62.827 1.00100.47 O
ANISOU 1239 O TRP A 207 18617 13716 5842 -1426 1000 -1733 O
ATOM 1240 CB TRP A 207 -23.221 18.480 59.864 1.00100.02 C
ANISOU 1240 CB TRP A 207 17885 13547 6571 -899 1113 -1593 C
ATOM 1241 CG TRP A 207 -23.172 17.740 58.559 1.00100.96 C
ANISOU 1241 CG TRP A 207 17529 13710 7122 -803 1012 -1443 C
ATOM 1242 CD1 TRP A 207 -23.683 16.499 58.292 1.00101.73 C
ANISOU 1242 CD1 TRP A 207 17190 14006 7458 -682 1018 -1246 C
ATOM 1243 CD2 TRP A 207 -22.520 18.173 57.354 1.00100.21 C
ANISOU 1243 CD2 TRP A 207 17378 13451 7247 -856 883 -1479 C
ATOM 1244 NE1 TRP A 207 -23.411 16.147 56.986 1.00 98.15 N
ANISOU 1244 NE1 TRP A 207 16426 13509 7357 -642 907 -1166 N
ATOM 1245 CE2 TRP A 207 -22.699 17.157 56.392 1.00 95.46 C
ANISOU 1245 CE2 TRP A 207 16293 12959 7018 -736 823 -1303 C
ATOM 1246 CE3 TRP A 207 -21.820 19.332 56.991 1.00 99.82 C
ANISOU 1246 CE3 TRP A 207 17667 13164 7096 -1013 823 -1646 C
ATOM 1247 CZ2 TRP A 207 -22.204 17.264 55.096 1.00 88.89 C
ANISOU 1247 CZ2 TRP A 207 15289 12019 6466 -741 706 -1289 C
ATOM 1248 CZ3 TRP A 207 -21.331 19.436 55.704 1.00 93.02 C
ANISOU 1248 CZ3 TRP A 207 16624 12205 6516 -1030 706 -1624 C
ATOM 1249 CH2 TRP A 207 -21.521 18.407 54.773 1.00 90.28 C
ANISOU 1249 CH2 TRP A 207 15773 11984 6545 -883 648 -1447 C
ATOM 1250 N PRO A 208 -21.165 20.544 61.411 1.00110.52 N
ANISOU 1250 N PRO A 208 20080 14614 7299 -1616 840 -1901 N
ATOM 1251 CA PRO A 208 -20.507 21.365 62.443 1.00113.37 C
ANISOU 1251 CA PRO A 208 20746 14900 7431 -1901 759 -1999 C
ATOM 1252 C PRO A 208 -21.251 21.538 63.762 1.00124.67 C
ANISOU 1252 C PRO A 208 22396 16345 8628 -1781 948 -2050 C
ATOM 1253 O PRO A 208 -20.642 21.442 64.834 1.00129.70 O
ANISOU 1253 O PRO A 208 23100 17121 9059 -2055 811 -2030 O
ATOM 1254 CB PRO A 208 -20.338 22.716 61.738 1.00113.29 C
ANISOU 1254 CB PRO A 208 21043 14517 7485 -1915 820 -2159 C
ATOM 1255 CG PRO A 208 -20.222 22.371 60.320 1.00110.69 C
ANISOU 1255 CG PRO A 208 20455 14178 7424 -1829 758 -2102 C
ATOM 1256 CD PRO A 208 -21.153 21.216 60.101 1.00109.24 C
ANISOU 1256 CD PRO A 208 19963 14200 7345 -1513 877 -1980 C
ATOM 1257 N GLY A 209 -22.553 21.801 63.711 1.00127.11 N
ANISOU 1257 N GLY A 209 22797 16540 8958 -1370 1259 -2108 N
ATOM 1258 CA GLY A 209 -23.291 22.036 64.931 1.00128.59 C
ANISOU 1258 CA GLY A 209 23189 16749 8921 -1235 1453 -2161 C
ATOM 1259 C GLY A 209 -23.647 20.758 65.666 1.00128.04 C
ANISOU 1259 C GLY A 209 22839 17036 8773 -1214 1449 -2004 C
ATOM 1260 O GLY A 209 -23.736 19.673 65.093 1.00125.06 O
ANISOU 1260 O GLY A 209 22111 16860 8546 -1172 1391 -1849 O
ATOM 1261 N GLU A 210 -23.852 20.898 66.977 1.00135.99 N
ANISOU 1261 N GLU A 210 24032 18108 9530 -1257 1518 -2039 N
ATOM 1262 CA GLU A 210 -24.325 19.768 67.769 1.00138.05 C
ANISOU 1262 CA GLU A 210 24071 18688 9695 -1213 1556 -1891 C
ATOM 1263 C GLU A 210 -25.765 19.410 67.420 1.00138.86 C
ANISOU 1263 C GLU A 210 23991 18882 9889 -793 1862 -1848 C
ATOM 1264 O GLU A 210 -26.178 18.258 67.594 1.00137.90 O
ANISOU 1264 O GLU A 210 23585 19033 9779 -761 1886 -1681 O
ATOM 1265 CB GLU A 210 -24.184 20.081 69.260 1.00137.66 C
ANISOU 1265 CB GLU A 210 24281 18680 9345 -1364 1558 -1949 C
ATOM 1266 CG GLU A 210 -22.766 20.448 69.651 1.00138.80 C
ANISOU 1266 CG GLU A 210 24576 18784 9379 -1803 1258 -1982 C
ATOM 1267 CD GLU A 210 -21.753 19.452 69.118 1.00137.52 C
ANISOU 1267 CD GLU A 210 24059 18842 9352 -2044 947 -1801 C
ATOM 1268 OE1 GLU A 210 -21.792 18.284 69.554 1.00137.31 O
ANISOU 1268 OE1 GLU A 210 23780 19098 9294 -2053 878 -1619 O
ATOM 1269 OE2 GLU A 210 -20.933 19.830 68.250 1.00135.66 O
ANISOU 1269 OE2 GLU A 210 23796 18498 9250 -2210 780 -1829 O
ATOM 1270 N GLU A 211 -26.533 20.381 66.922 1.00140.43 N
ANISOU 1270 N GLU A 211 24339 18870 10149 -474 2096 -1980 N
ATOM 1271 CA GLU A 211 -27.887 20.140 66.443 1.00139.82 C
ANISOU 1271 CA GLU A 211 24030 18919 10177 -56 2381 -1932 C
ATOM 1272 C GLU A 211 -28.145 20.876 65.130 1.00141.09 C
ANISOU 1272 C GLU A 211 24197 18851 10561 195 2466 -2004 C
ATOM 1273 O GLU A 211 -29.300 20.955 64.693 1.00143.37 O
ANISOU 1273 O GLU A 211 24315 19225 10933 586 2716 -1984 O
ATOM 1274 CB GLU A 211 -28.911 20.553 67.522 1.00143.76 C
ANISOU 1274 CB GLU A 211 24665 19501 10456 185 2652 -1992 C
ATOM 1275 CG GLU A 211 -30.347 20.058 67.323 1.00141.92 C
ANISOU 1275 CG GLU A 211 24094 19553 10276 561 2937 -1897 C
ATOM 1276 CD GLU A 211 -30.454 18.549 67.210 1.00137.29 C
ANISOU 1276 CD GLU A 211 23106 19302 9757 425 2872 -1685 C
ATOM 1277 OE1 GLU A 211 -29.595 17.838 67.773 1.00136.53 O
ANISOU 1277 OE1 GLU A 211 23030 19265 9579 77 2647 -1605 O
ATOM 1278 OE2 GLU A 211 -31.405 18.074 66.553 1.00135.12 O
ANISOU 1278 OE2 GLU A 211 22492 19235 9614 662 3043 -1586 O
ATOM 1279 N LYS A 212 -27.105 21.403 64.479 1.00139.82 N
ANISOU 1279 N LYS A 212 24198 18430 10498 -23 2260 -2073 N
ATOM 1280 CA LYS A 212 -27.257 22.212 63.273 1.00137.32 C
ANISOU 1280 CA LYS A 212 23944 17853 10377 191 2327 -2147 C
ATOM 1281 C LYS A 212 -27.218 21.300 62.050 1.00131.49 C
ANISOU 1281 C LYS A 212 22812 17252 9897 220 2244 -2019 C
ATOM 1282 O LYS A 212 -26.150 20.817 61.652 1.00132.85 O
ANISOU 1282 O LYS A 212 22903 17427 10146 -110 1977 -1969 O
ATOM 1283 CB LYS A 212 -26.176 23.288 63.199 1.00137.33 C
ANISOU 1283 CB LYS A 212 24340 17503 10338 -88 2162 -2282 C
ATOM 1284 CG LYS A 212 -26.082 24.165 64.445 1.00140.60 C
ANISOU 1284 CG LYS A 212 25187 17761 10473 -187 2222 -2404 C
ATOM 1285 CD LYS A 212 -27.453 24.644 64.897 1.00142.96 C
ANISOU 1285 CD LYS A 212 25588 18054 10678 276 2562 -2446 C
ATOM 1286 CE LYS A 212 -27.660 24.394 66.384 1.00144.98 C
ANISOU 1286 CE LYS A 212 25941 18487 10659 192 2617 -2453 C
ATOM 1287 NZ LYS A 212 -29.061 24.669 66.812 1.00146.93 N
ANISOU 1287 NZ LYS A 212 26189 18820 10817 655 2951 -2466 N
ATOM 1288 N SER A 213 -28.382 21.082 61.450 1.00123.08 N
ANISOU 1288 N SER A 213 21487 16320 8957 615 2473 -1958 N
ATOM 1289 CA SER A 213 -28.544 20.157 60.340 1.00113.20 C
ANISOU 1289 CA SER A 213 19848 15230 7934 676 2440 -1824 C
ATOM 1290 C SER A 213 -28.447 20.832 58.977 1.00110.70 C
ANISOU 1290 C SER A 213 19540 14676 7844 839 2433 -1880 C
ATOM 1291 O SER A 213 -28.476 20.135 57.959 1.00111.07 O
ANISOU 1291 O SER A 213 19172 14831 8199 856 2341 -1755 O
ATOM 1292 CB SER A 213 -29.894 19.439 60.480 1.00106.42 C
ANISOU 1292 CB SER A 213 18636 14724 7073 975 2688 -1698 C
ATOM 1293 OG SER A 213 -30.820 20.241 61.204 1.00100.24 O
ANISOU 1293 OG SER A 213 17983 13959 6146 1264 2930 -1777 O
ATOM 1294 N ILE A 214 -28.299 22.159 58.932 1.00111.64 N
ANISOU 1294 N ILE A 214 20017 14469 7934 919 2472 -2027 N
ATOM 1295 CA ILE A 214 -28.500 22.886 57.680 1.00111.08 C
ANISOU 1295 CA ILE A 214 19956 14182 8066 1166 2527 -2063 C
ATOM 1296 C ILE A 214 -27.357 22.637 56.699 1.00114.71 C
ANISOU 1296 C ILE A 214 20374 14516 8696 863 2266 -2057 C
ATOM 1297 O ILE A 214 -27.596 22.399 55.508 1.00119.58 O
ANISOU 1297 O ILE A 214 20747 15155 9532 1035 2280 -2001 O
ATOM 1298 CB ILE A 214 -28.703 24.385 57.954 1.00113.06 C
ANISOU 1298 CB ILE A 214 20651 14092 8214 1340 2658 -2196 C
ATOM 1299 CG1 ILE A 214 -27.723 24.880 59.022 1.00117.27 C
ANISOU 1299 CG1 ILE A 214 21606 14432 8519 939 2517 -2304 C
ATOM 1300 CG2 ILE A 214 -30.142 24.643 58.357 1.00114.42 C
ANISOU 1300 CG2 ILE A 214 20737 14421 8315 1815 2962 -2167 C
ATOM 1301 CD1 ILE A 214 -26.734 25.921 58.530 1.00115.71 C
ANISOU 1301 CD1 ILE A 214 21785 13833 8347 700 2376 -2405 C
ATOM 1302 N TYR A 215 -26.104 22.695 57.164 1.00115.95 N
ANISOU 1302 N TYR A 215 20737 14568 8749 406 2020 -2106 N
ATOM 1303 CA TYR A 215 -24.982 22.450 56.257 1.00115.64 C
ANISOU 1303 CA TYR A 215 20619 14461 8859 99 1758 -2089 C
ATOM 1304 C TYR A 215 -25.121 21.102 55.553 1.00111.36 C
ANISOU 1304 C TYR A 215 19418 14208 8687 129 1635 -1873 C
ATOM 1305 O TYR A 215 -24.797 20.973 54.367 1.00110.30 O
ANISOU 1305 O TYR A 215 19040 14019 8849 124 1517 -1818 O
ATOM 1306 CB TYR A 215 -23.651 22.510 57.012 1.00115.56 C
ANISOU 1306 CB TYR A 215 20780 14438 8691 -414 1487 -2120 C
ATOM 1307 CG TYR A 215 -23.119 23.902 57.296 1.00113.06 C
ANISOU 1307 CG TYR A 215 20903 13793 8262 -577 1470 -2263 C
ATOM 1308 CD1 TYR A 215 -22.724 24.743 56.259 1.00108.27 C
ANISOU 1308 CD1 TYR A 215 20439 12905 7794 -603 1434 -2322 C
ATOM 1309 CD2 TYR A 215 -22.974 24.361 58.610 1.00111.77 C
ANISOU 1309 CD2 TYR A 215 21030 13597 7841 -736 1487 -2328 C
ATOM 1310 CE1 TYR A 215 -22.223 26.013 56.516 1.00107.87 C
ANISOU 1310 CE1 TYR A 215 20825 12538 7622 -791 1429 -2432 C
ATOM 1311 CE2 TYR A 215 -22.470 25.627 58.877 1.00111.49 C
ANISOU 1311 CE2 TYR A 215 21434 13246 7682 -922 1479 -2448 C
ATOM 1312 CZ TYR A 215 -22.097 26.449 57.824 1.00111.86 C
ANISOU 1312 CZ TYR A 215 21631 13007 7864 -956 1454 -2494 C
ATOM 1313 OH TYR A 215 -21.599 27.711 58.071 1.00115.90 O
ANISOU 1313 OH TYR A 215 22613 13188 8237 -1168 1459 -2593 O
ATOM 1314 N GLY A 216 -25.620 20.092 56.261 1.00109.85 N
ANISOU 1314 N GLY A 216 18940 14310 8487 154 1665 -1743 N
ATOM 1315 CA GLY A 216 -25.717 18.758 55.706 1.00109.19 C
ANISOU 1315 CA GLY A 216 18285 14475 8729 133 1545 -1531 C
ATOM 1316 C GLY A 216 -26.896 18.516 54.795 1.00107.90 C
ANISOU 1316 C GLY A 216 17789 14412 8795 489 1730 -1459 C
ATOM 1317 O GLY A 216 -26.926 17.485 54.118 1.00102.89 O
ANISOU 1317 O GLY A 216 16718 13932 8445 443 1622 -1300 O
ATOM 1318 N THR A 217 -27.871 19.423 54.761 1.00106.65 N
ANISOU 1318 N THR A 217 17833 14189 8501 846 2008 -1565 N
ATOM 1319 CA THR A 217 -29.015 19.244 53.876 1.00100.54 C
ANISOU 1319 CA THR A 217 16710 13576 7916 1196 2181 -1485 C
ATOM 1320 C THR A 217 -28.887 20.029 52.581 1.00100.49 C
ANISOU 1320 C THR A 217 16760 13336 8085 1362 2175 -1548 C
ATOM 1321 O THR A 217 -29.247 19.514 51.518 1.00100.27 O
ANISOU 1321 O THR A 217 16324 13434 8341 1456 2146 -1438 O
ATOM 1322 CB THR A 217 -30.320 19.648 54.566 1.00 96.40 C
ANISOU 1322 CB THR A 217 16272 13223 7132 1567 2516 -1519 C
ATOM 1323 OG1 THR A 217 -30.314 21.061 54.785 1.00 98.85 O
ANISOU 1323 OG1 THR A 217 17140 13231 7186 1784 2676 -1711 O
ATOM 1324 CG2 THR A 217 -30.504 18.898 55.885 1.00 92.28 C
ANISOU 1324 CG2 THR A 217 15710 12940 6411 1402 2542 -1458 C
ATOM 1325 N VAL A 218 -28.392 21.268 52.636 1.00 98.67 N
ANISOU 1325 N VAL A 218 17053 12761 7675 1383 2206 -1723 N
ATOM 1326 CA VAL A 218 -28.217 22.018 51.394 1.00 96.52 C
ANISOU 1326 CA VAL A 218 16871 12243 7559 1519 2195 -1777 C
ATOM 1327 C VAL A 218 -27.201 21.318 50.502 1.00 92.96 C
ANISOU 1327 C VAL A 218 16105 11783 7432 1185 1888 -1686 C
ATOM 1328 O VAL A 218 -27.370 21.249 49.281 1.00 92.89 O
ANISOU 1328 O VAL A 218 15844 11766 7684 1314 1864 -1629 O
ATOM 1329 CB VAL A 218 -27.833 23.481 51.687 1.00 94.92 C
ANISOU 1329 CB VAL A 218 17373 11633 7061 1557 2293 -1986 C
ATOM 1330 CG1 VAL A 218 -28.541 23.965 52.938 1.00 94.94 C
ANISOU 1330 CG1 VAL A 218 17580 11666 6827 1720 2483 -2025 C
ATOM 1331 CG2 VAL A 218 -26.322 23.669 51.806 1.00 93.55 C
ANISOU 1331 CG2 VAL A 218 17454 11238 6852 1041 2014 -2062 C
ATOM 1332 N TYR A 219 -26.144 20.767 51.099 1.00 92.53 N
ANISOU 1332 N TYR A 219 16048 11757 7353 771 1654 -1662 N
ATOM 1333 CA TYR A 219 -25.257 19.897 50.347 1.00 91.16 C
ANISOU 1333 CA TYR A 219 15509 11651 7475 505 1381 -1541 C
ATOM 1334 C TYR A 219 -26.026 18.707 49.810 1.00 93.55 C
ANISOU 1334 C TYR A 219 15276 12227 8041 642 1404 -1363 C
ATOM 1335 O TYR A 219 -25.864 18.332 48.647 1.00 98.51 O
ANISOU 1335 O TYR A 219 15621 12853 8955 646 1305 -1288 O
ATOM 1336 CB TYR A 219 -24.104 19.442 51.234 1.00 93.44 C
ANISOU 1336 CB TYR A 219 15861 12001 7641 100 1151 -1517 C
ATOM 1337 CG TYR A 219 -23.071 18.594 50.541 1.00 92.48 C
ANISOU 1337 CG TYR A 219 15400 11961 7777 -146 873 -1388 C
ATOM 1338 CD1 TYR A 219 -23.221 17.215 50.445 1.00 94.72 C
ANISOU 1338 CD1 TYR A 219 15256 12478 8257 -150 799 -1200 C
ATOM 1339 CD2 TYR A 219 -21.931 19.166 50.006 1.00 91.63 C
ANISOU 1339 CD2 TYR A 219 15424 11701 7689 -379 694 -1450 C
ATOM 1340 CE1 TYR A 219 -22.266 16.431 49.817 1.00 94.94 C
ANISOU 1340 CE1 TYR A 219 15010 12567 8497 -327 563 -1077 C
ATOM 1341 CE2 TYR A 219 -20.973 18.396 49.377 1.00 93.02 C
ANISOU 1341 CE2 TYR A 219 15274 11988 8082 -568 453 -1322 C
ATOM 1342 CZ TYR A 219 -21.140 17.033 49.289 1.00 94.69 C
ANISOU 1342 CZ TYR A 219 15078 12414 8486 -517 393 -1137 C
ATOM 1343 OH TYR A 219 -20.180 16.276 48.664 1.00 95.61 O
ANISOU 1343 OH TYR A 219 14909 12624 8794 -656 173 -1008 O
ATOM 1344 N SER A 220 -26.886 18.113 50.636 1.00 91.61 N
ANISOU 1344 N SER A 220 14905 12220 7683 736 1541 -1296 N
ATOM 1345 CA SER A 220 -27.743 17.026 50.189 1.00 90.65 C
ANISOU 1345 CA SER A 220 14315 12372 7757 831 1592 -1134 C
ATOM 1346 C SER A 220 -28.927 17.504 49.373 1.00 95.68 C
ANISOU 1346 C SER A 220 14812 13085 8457 1203 1810 -1144 C
ATOM 1347 O SER A 220 -29.811 16.699 49.067 1.00102.25 O
ANISOU 1347 O SER A 220 15260 14198 9394 1279 1886 -1018 O
ATOM 1348 CB SER A 220 -28.268 16.222 51.372 1.00 92.93 C
ANISOU 1348 CB SER A 220 14522 12913 7875 766 1670 -1051 C
ATOM 1349 OG SER A 220 -29.191 15.252 50.910 1.00 92.20 O
ANISOU 1349 OG SER A 220 14008 13087 7935 829 1744 -904 O
ATOM 1350 N LEU A 221 -28.992 18.783 49.055 1.00 94.69 N
ANISOU 1350 N LEU A 221 15002 12736 8239 1431 1919 -1282 N
ATOM 1351 CA LEU A 221 -30.001 19.281 48.133 1.00 91.53 C
ANISOU 1351 CA LEU A 221 14465 12404 7908 1819 2103 -1274 C
ATOM 1352 C LEU A 221 -29.396 19.898 46.889 1.00 89.00 C
ANISOU 1352 C LEU A 221 14230 11811 7776 1838 1995 -1324 C
ATOM 1353 O LEU A 221 -29.897 19.658 45.793 1.00 89.35 O
ANISOU 1353 O LEU A 221 13947 11974 8029 1987 2007 -1242 O
ATOM 1354 CB LEU A 221 -30.923 20.301 48.825 1.00 91.29 C
ANISOU 1354 CB LEU A 221 14744 12384 7559 2211 2405 -1372 C
ATOM 1355 CG LEU A 221 -31.895 19.600 49.783 1.00 88.54 C
ANISOU 1355 CG LEU A 221 14159 12427 7055 2279 2563 -1284 C
ATOM 1356 CD1 LEU A 221 -32.802 20.558 50.515 1.00 84.19 C
ANISOU 1356 CD1 LEU A 221 13899 11922 6169 2696 2877 -1371 C
ATOM 1357 CD2 LEU A 221 -32.700 18.540 49.026 1.00 87.07 C
ANISOU 1357 CD2 LEU A 221 13362 12630 7089 2291 2561 -1105 C
ATOM 1358 N SER A 222 -28.318 20.671 47.028 1.00 90.58 N
ANISOU 1358 N SER A 222 14858 11665 7892 1658 1885 -1452 N
ATOM 1359 CA SER A 222 -27.635 21.204 45.853 1.00 86.07 C
ANISOU 1359 CA SER A 222 14368 10838 7495 1613 1765 -1492 C
ATOM 1360 C SER A 222 -27.002 20.083 45.045 1.00 89.88 C
ANISOU 1360 C SER A 222 14411 11436 8304 1344 1521 -1362 C
ATOM 1361 O SER A 222 -27.164 20.009 43.824 1.00 92.69 O
ANISOU 1361 O SER A 222 14539 11792 8886 1448 1494 -1310 O
ATOM 1362 CB SER A 222 -26.569 22.214 46.267 1.00 82.04 C
ANISOU 1362 CB SER A 222 14416 9969 6785 1393 1692 -1653 C
ATOM 1363 OG SER A 222 -27.027 23.048 47.308 1.00 85.63 O
ANISOU 1363 OG SER A 222 15328 10316 6892 1562 1902 -1775 O
ATOM 1364 N SER A 223 -26.266 19.197 45.715 1.00 91.67 N
ANISOU 1364 N SER A 223 14533 11758 8541 1014 1345 -1303 N
ATOM 1365 CA SER A 223 -25.623 18.108 44.994 1.00 92.80 C
ANISOU 1365 CA SER A 223 14306 11990 8964 795 1129 -1174 C
ATOM 1366 C SER A 223 -26.660 17.197 44.343 1.00 91.62 C
ANISOU 1366 C SER A 223 13721 12085 9004 953 1208 -1040 C
ATOM 1367 O SER A 223 -26.484 16.759 43.201 1.00 87.54 O
ANISOU 1367 O SER A 223 12955 11568 8737 925 1111 -973 O
ATOM 1368 CB SER A 223 -24.703 17.334 45.940 1.00 89.24 C
ANISOU 1368 CB SER A 223 13850 11615 8441 473 950 -1119 C
ATOM 1369 OG SER A 223 -23.724 18.200 46.494 1.00 84.53 O
ANISOU 1369 OG SER A 223 13634 10837 7646 280 861 -1241 O
ATOM 1370 N LEU A 224 -27.765 16.928 45.039 1.00 93.92 N
ANISOU 1370 N LEU A 224 13922 12604 9158 1105 1391 -1004 N
ATOM 1371 CA LEU A 224 -28.861 16.204 44.405 1.00 91.53 C
ANISOU 1371 CA LEU A 224 13216 12576 8985 1236 1487 -886 C
ATOM 1372 C LEU A 224 -29.459 17.008 43.254 1.00 92.27 C
ANISOU 1372 C LEU A 224 13252 12641 9164 1536 1592 -920 C
ATOM 1373 O LEU A 224 -29.962 16.429 42.284 1.00 93.77 O
ANISOU 1373 O LEU A 224 13092 12999 9537 1564 1581 -824 O
ATOM 1374 CB LEU A 224 -29.931 15.860 45.445 1.00 91.04 C
ANISOU 1374 CB LEU A 224 13071 12806 8713 1325 1677 -841 C
ATOM 1375 CG LEU A 224 -30.553 14.464 45.374 1.00 87.90 C
ANISOU 1375 CG LEU A 224 12278 12715 8405 1169 1672 -679 C
ATOM 1376 CD1 LEU A 224 -31.266 14.130 46.677 1.00 91.02 C
ANISOU 1376 CD1 LEU A 224 12680 13352 8550 1161 1822 -645 C
ATOM 1377 CD2 LEU A 224 -31.515 14.370 44.213 1.00 82.91 C
ANISOU 1377 CD2 LEU A 224 11303 12294 7904 1334 1758 -615 C
ATOM 1378 N LEU A 225 -29.403 18.337 43.332 1.00 90.01 N
ANISOU 1378 N LEU A 225 13333 12136 8730 1755 1693 -1052 N
ATOM 1379 CA LEU A 225 -29.916 19.169 42.244 1.00 85.70 C
ANISOU 1379 CA LEU A 225 12786 11532 8243 2075 1795 -1077 C
ATOM 1380 C LEU A 225 -28.889 19.276 41.122 1.00 83.78 C
ANISOU 1380 C LEU A 225 12566 11034 8233 1902 1593 -1094 C
ATOM 1381 O LEU A 225 -29.090 18.754 40.022 1.00 84.85 O
ANISOU 1381 O LEU A 225 12367 11280 8591 1906 1530 -1005 O
ATOM 1382 CB LEU A 225 -30.287 20.556 42.776 1.00 86.43 C
ANISOU 1382 CB LEU A 225 13333 11452 8054 2410 2008 -1207 C
ATOM 1383 CG LEU A 225 -31.129 21.449 41.866 1.00 88.51 C
ANISOU 1383 CG LEU A 225 13613 11719 8297 2866 2186 -1209 C
ATOM 1384 CD1 LEU A 225 -32.608 21.070 41.967 1.00 85.54 C
ANISOU 1384 CD1 LEU A 225 12841 11818 7841 3185 2391 -1094 C
ATOM 1385 CD2 LEU A 225 -30.906 22.930 42.180 1.00 89.97 C
ANISOU 1385 CD2 LEU A 225 14431 11517 8235 3097 2323 -1366 C
ATOM 1386 N ILE A 226 -27.765 19.935 41.405 1.00 82.64 N
ANISOU 1386 N ILE A 226 12814 10567 8018 1721 1487 -1206 N
ATOM 1387 CA ILE A 226 -26.749 20.217 40.398 1.00 79.26 C
ANISOU 1387 CA ILE A 226 12451 9900 7763 1556 1314 -1233 C
ATOM 1388 C ILE A 226 -26.156 18.941 39.794 1.00 79.57 C
ANISOU 1388 C ILE A 226 12090 10069 8075 1285 1102 -1112 C
ATOM 1389 O ILE A 226 -25.588 18.993 38.695 1.00 79.26 O
ANISOU 1389 O ILE A 226 11976 9916 8223 1217 986 -1101 O
ATOM 1390 CB ILE A 226 -25.643 21.122 41.019 1.00 78.96 C
ANISOU 1390 CB ILE A 226 12914 9552 7537 1339 1242 -1374 C
ATOM 1391 CG1 ILE A 226 -26.236 22.363 41.730 1.00 75.25 C
ANISOU 1391 CG1 ILE A 226 12934 8907 6751 1605 1475 -1505 C
ATOM 1392 CG2 ILE A 226 -24.604 21.554 39.975 1.00 73.48 C
ANISOU 1392 CG2 ILE A 226 12310 8626 6982 1157 1081 -1408 C
ATOM 1393 CD1 ILE A 226 -27.220 23.178 40.892 1.00 74.05 C
ANISOU 1393 CD1 ILE A 226 12855 8691 6591 2061 1681 -1515 C
ATOM 1394 N LEU A 227 -26.303 17.781 40.465 1.00 80.71 N
ANISOU 1394 N LEU A 227 11995 10439 8232 1144 1062 -1016 N
ATOM 1395 CA LEU A 227 -25.654 16.543 40.029 1.00 75.29 C
ANISOU 1395 CA LEU A 227 11018 9829 7760 896 872 -901 C
ATOM 1396 C LEU A 227 -26.571 15.332 39.921 1.00 73.56 C
ANISOU 1396 C LEU A 227 10439 9883 7629 910 925 -768 C
ATOM 1397 O LEU A 227 -26.079 14.204 39.797 1.00 76.05 O
ANISOU 1397 O LEU A 227 10586 10242 8068 705 792 -668 O
ATOM 1398 CB LEU A 227 -24.490 16.194 40.943 1.00 79.59 C
ANISOU 1398 CB LEU A 227 11696 10324 8220 614 709 -898 C
ATOM 1399 CG LEU A 227 -23.284 17.100 40.746 1.00 85.44 C
ANISOU 1399 CG LEU A 227 12701 10839 8925 469 582 -997 C
ATOM 1400 CD1 LEU A 227 -22.989 17.861 42.029 1.00 85.12 C
ANISOU 1400 CD1 LEU A 227 13034 10721 8585 380 614 -1106 C
ATOM 1401 CD2 LEU A 227 -22.062 16.298 40.258 1.00 86.76 C
ANISOU 1401 CD2 LEU A 227 12678 11028 9259 232 351 -906 C
ATOM 1402 N TYR A 228 -27.871 15.510 39.966 1.00 74.04 N
ANISOU 1402 N TYR A 228 10387 10138 7606 1137 1119 -756 N
ATOM 1403 CA TYR A 228 -28.734 14.400 39.575 1.00 76.36 C
ANISOU 1403 CA TYR A 228 10312 10709 7992 1096 1155 -628 C
ATOM 1404 C TYR A 228 -29.910 14.792 38.693 1.00 84.70 C
ANISOU 1404 C TYR A 228 11150 11963 9071 1356 1300 -609 C
ATOM 1405 O TYR A 228 -30.143 14.097 37.706 1.00 82.90 O
ANISOU 1405 O TYR A 228 10648 11841 9008 1272 1245 -528 O
ATOM 1406 CB TYR A 228 -29.273 13.681 40.839 1.00 73.65 C
ANISOU 1406 CB TYR A 228 9931 10580 7473 1000 1238 -569 C
ATOM 1407 CG TYR A 228 -30.094 12.464 40.528 1.00 74.60 C
ANISOU 1407 CG TYR A 228 9717 10977 7652 871 1269 -435 C
ATOM 1408 CD1 TYR A 228 -29.514 11.284 40.072 1.00 74.68 C
ANISOU 1408 CD1 TYR A 228 9633 10917 7824 605 1116 -344 C
ATOM 1409 CD2 TYR A 228 -31.459 12.507 40.657 1.00 78.02 C
ANISOU 1409 CD2 TYR A 228 9939 11751 7954 1013 1461 -397 C
ATOM 1410 CE1 TYR A 228 -30.286 10.171 39.772 1.00 79.29 C
ANISOU 1410 CE1 TYR A 228 9973 11723 8430 443 1154 -229 C
ATOM 1411 CE2 TYR A 228 -32.240 11.409 40.359 1.00 84.65 C
ANISOU 1411 CE2 TYR A 228 10474 12875 8814 834 1490 -275 C
ATOM 1412 CZ TYR A 228 -31.656 10.238 39.918 1.00 81.18 C
ANISOU 1412 CZ TYR A 228 9997 12319 8530 527 1336 -197 C
ATOM 1413 OH TYR A 228 -32.438 9.138 39.626 1.00 77.18 O
ANISOU 1413 OH TYR A 228 9251 12063 8011 302 1372 -84 O
ATOM 1414 N VAL A 229 -30.606 15.904 38.939 1.00 87.66 N
ANISOU 1414 N VAL A 229 11650 12382 9274 1682 1480 -677 N
ATOM 1415 CA VAL A 229 -31.719 16.261 38.061 1.00 83.63 C
ANISOU 1415 CA VAL A 229 10897 12111 8769 1971 1614 -634 C
ATOM 1416 C VAL A 229 -31.244 17.219 36.979 1.00 83.65 C
ANISOU 1416 C VAL A 229 11058 11844 8883 2137 1567 -699 C
ATOM 1417 O VAL A 229 -31.831 17.287 35.891 1.00 83.66 O
ANISOU 1417 O VAL A 229 10821 11993 8972 2289 1593 -644 O
ATOM 1418 CB VAL A 229 -32.905 16.850 38.846 1.00 80.11 C
ANISOU 1418 CB VAL A 229 10446 11938 8055 2304 1864 -636 C
ATOM 1419 CG1 VAL A 229 -33.352 15.861 39.905 1.00 80.43 C
ANISOU 1419 CG1 VAL A 229 10324 12256 7979 2098 1908 -565 C
ATOM 1420 CG2 VAL A 229 -32.537 18.186 39.453 1.00 80.97 C
ANISOU 1420 CG2 VAL A 229 11038 11740 7988 2552 1959 -775 C
ATOM 1421 N LEU A 230 -30.173 17.965 37.263 1.00 82.00 N
ANISOU 1421 N LEU A 230 11253 11252 8650 2085 1494 -814 N
ATOM 1422 CA LEU A 230 -29.576 18.784 36.208 1.00 79.23 C
ANISOU 1422 CA LEU A 230 11074 10620 8410 2162 1428 -872 C
ATOM 1423 C LEU A 230 -28.911 17.913 35.151 1.00 78.90 C
ANISOU 1423 C LEU A 230 10783 10551 8643 1893 1226 -807 C
ATOM 1424 O LEU A 230 -29.285 18.015 33.966 1.00 75.86 O
ANISOU 1424 O LEU A 230 10219 10226 8379 2021 1229 -765 O
ATOM 1425 CB LEU A 230 -28.623 19.814 36.814 1.00 79.79 C
ANISOU 1425 CB LEU A 230 11660 10312 8345 2118 1408 -1012 C
ATOM 1426 CG LEU A 230 -28.420 20.967 35.831 1.00 83.53 C
ANISOU 1426 CG LEU A 230 12383 10518 8836 2311 1435 -1076 C
ATOM 1427 CD1 LEU A 230 -29.646 21.874 35.848 1.00 88.18 C
ANISOU 1427 CD1 LEU A 230 13081 11192 9232 2806 1691 -1083 C
ATOM 1428 CD2 LEU A 230 -27.134 21.763 36.054 1.00 83.04 C
ANISOU 1428 CD2 LEU A 230 12788 10057 8707 2090 1334 -1203 C
ATOM 1429 N PRO A 231 -27.966 17.017 35.484 1.00 83.73 N
ANISOU 1429 N PRO A 231 11366 11097 9350 1549 1057 -784 N
ATOM 1430 CA PRO A 231 -27.317 16.249 34.413 1.00 79.14 C
ANISOU 1430 CA PRO A 231 10586 10470 9013 1349 887 -724 C
ATOM 1431 C PRO A 231 -28.234 15.230 33.774 1.00 79.87 C
ANISOU 1431 C PRO A 231 10295 10848 9205 1331 914 -609 C
ATOM 1432 O PRO A 231 -28.049 14.928 32.593 1.00 84.22 O
ANISOU 1432 O PRO A 231 10696 11373 9932 1280 831 -574 O
ATOM 1433 CB PRO A 231 -26.122 15.583 35.112 1.00 74.99 C
ANISOU 1433 CB PRO A 231 10153 9834 8507 1048 726 -716 C
ATOM 1434 CG PRO A 231 -25.952 16.315 36.377 1.00 82.07 C
ANISOU 1434 CG PRO A 231 11355 10651 9177 1071 786 -803 C
ATOM 1435 CD PRO A 231 -27.347 16.703 36.782 1.00 84.50 C
ANISOU 1435 CD PRO A 231 11633 11144 9329 1347 1005 -808 C
ATOM 1436 N LEU A 232 -29.211 14.680 34.497 1.00 80.78 N
ANISOU 1436 N LEU A 232 10252 11244 9196 1342 1027 -550 N
ATOM 1437 CA LEU A 232 -30.192 13.832 33.826 1.00 71.99 C
ANISOU 1437 CA LEU A 232 8778 10439 8135 1297 1065 -446 C
ATOM 1438 C LEU A 232 -31.179 14.652 33.032 1.00 74.10 C
ANISOU 1438 C LEU A 232 8897 10894 8362 1609 1188 -441 C
ATOM 1439 O LEU A 232 -31.847 14.102 32.149 1.00 73.58 O
ANISOU 1439 O LEU A 232 8525 11072 8361 1562 1186 -361 O
ATOM 1440 CB LEU A 232 -30.955 12.953 34.816 1.00 72.37 C
ANISOU 1440 CB LEU A 232 8687 10770 8039 1166 1150 -372 C
ATOM 1441 CG LEU A 232 -30.213 11.759 35.437 1.00 71.01 C
ANISOU 1441 CG LEU A 232 8589 10486 7905 833 1034 -324 C
ATOM 1442 CD1 LEU A 232 -31.085 11.136 36.485 1.00 78.65 C
ANISOU 1442 CD1 LEU A 232 9464 11734 8687 742 1152 -260 C
ATOM 1443 CD2 LEU A 232 -29.843 10.701 34.421 1.00 63.28 C
ANISOU 1443 CD2 LEU A 232 7488 9443 7111 600 907 -255 C
ATOM 1444 N GLY A 233 -31.297 15.946 33.341 1.00 78.18 N
ANISOU 1444 N GLY A 233 9645 11310 8751 1929 1299 -520 N
ATOM 1445 CA GLY A 233 -32.033 16.838 32.461 1.00 72.25 C
ANISOU 1445 CA GLY A 233 8817 10667 7968 2280 1402 -511 C
ATOM 1446 C GLY A 233 -31.320 17.030 31.137 1.00 67.74 C
ANISOU 1446 C GLY A 233 8275 9863 7602 2230 1265 -527 C
ATOM 1447 O GLY A 233 -31.907 16.828 30.072 1.00 71.92 O
ANISOU 1447 O GLY A 233 8525 10600 8203 2289 1260 -455 O
ATOM 1448 N ILE A 234 -30.031 17.390 31.193 1.00 63.03 N
ANISOU 1448 N ILE A 234 8000 8861 7086 2094 1147 -616 N
ATOM 1449 CA ILE A 234 -29.237 17.594 29.977 1.00 61.17 C
ANISOU 1449 CA ILE A 234 7811 8397 7035 2024 1017 -633 C
ATOM 1450 C ILE A 234 -29.198 16.325 29.124 1.00 61.14 C
ANISOU 1450 C ILE A 234 7472 8539 7221 1770 895 -545 C
ATOM 1451 O ILE A 234 -29.493 16.358 27.924 1.00 60.94 O
ANISOU 1451 O ILE A 234 7280 8585 7291 1836 875 -506 O
ATOM 1452 CB ILE A 234 -27.812 18.051 30.329 1.00 57.01 C
ANISOU 1452 CB ILE A 234 7645 7483 6533 1847 904 -732 C
ATOM 1453 CG1 ILE A 234 -27.777 19.481 30.843 1.00 59.20 C
ANISOU 1453 CG1 ILE A 234 8339 7539 6617 2078 1020 -835 C
ATOM 1454 CG2 ILE A 234 -26.931 17.925 29.092 1.00 53.82 C
ANISOU 1454 CG2 ILE A 234 7203 6912 6335 1697 752 -726 C
ATOM 1455 CD1 ILE A 234 -26.381 19.895 31.346 1.00 57.88 C
ANISOU 1455 CD1 ILE A 234 8526 7042 6422 1822 904 -934 C
ATOM 1456 N ILE A 235 -28.788 15.200 29.723 1.00 61.50 N
ANISOU 1456 N ILE A 235 7455 8604 7307 1476 814 -513 N
ATOM 1457 CA ILE A 235 -28.681 13.936 28.991 1.00 60.88 C
ANISOU 1457 CA ILE A 235 7147 8605 7381 1223 711 -435 C
ATOM 1458 C ILE A 235 -30.000 13.598 28.298 1.00 59.19 C
ANISOU 1458 C ILE A 235 6606 8748 7134 1282 793 -356 C
ATOM 1459 O ILE A 235 -30.036 13.289 27.099 1.00 57.92 O
ANISOU 1459 O ILE A 235 6298 8617 7093 1219 730 -323 O
ATOM 1460 CB ILE A 235 -28.236 12.803 29.934 1.00 59.26 C
ANISOU 1460 CB ILE A 235 6972 8383 7162 956 654 -398 C
ATOM 1461 CG1 ILE A 235 -26.808 13.022 30.413 1.00 60.88 C
ANISOU 1461 CG1 ILE A 235 7438 8286 7406 871 538 -454 C
ATOM 1462 CG2 ILE A 235 -28.298 11.482 29.242 1.00 59.81 C
ANISOU 1462 CG2 ILE A 235 6864 8522 7338 717 587 -315 C
ATOM 1463 CD1 ILE A 235 -26.473 12.181 31.649 1.00 59.05 C
ANISOU 1463 CD1 ILE A 235 7278 8067 7092 697 511 -416 C
ATOM 1464 N SER A 236 -31.102 13.664 29.039 1.00 62.26 N
ANISOU 1464 N SER A 236 6867 9447 7343 1396 934 -321 N
ATOM 1465 CA SER A 236 -32.416 13.407 28.453 1.00 70.28 C
ANISOU 1465 CA SER A 236 7527 10894 8283 1449 1017 -233 C
ATOM 1466 C SER A 236 -32.673 14.296 27.233 1.00 67.49 C
ANISOU 1466 C SER A 236 7100 10569 7973 1718 1026 -233 C
ATOM 1467 O SER A 236 -33.149 13.821 26.190 1.00 59.91 O
ANISOU 1467 O SER A 236 5878 9823 7062 1623 986 -168 O
ATOM 1468 CB SER A 236 -33.501 13.614 29.507 1.00 67.79 C
ANISOU 1468 CB SER A 236 7095 10927 7734 1608 1189 -199 C
ATOM 1469 OG SER A 236 -34.757 13.262 28.976 1.00 77.03 O
ANISOU 1469 OG SER A 236 7870 12592 8806 1611 1260 -97 O
ATOM 1470 N PHE A 237 -32.361 15.591 27.351 1.00 61.95 N
ANISOU 1470 N PHE A 237 6660 9645 7235 2043 1080 -305 N
ATOM 1471 CA PHE A 237 -32.566 16.527 26.250 1.00 65.07 C
ANISOU 1471 CA PHE A 237 7052 10023 7650 2334 1101 -300 C
ATOM 1472 C PHE A 237 -31.744 16.125 25.033 1.00 68.73 C
ANISOU 1472 C PHE A 237 7509 10275 8332 2111 935 -307 C
ATOM 1473 O PHE A 237 -32.255 16.081 23.908 1.00 75.23 O
ANISOU 1473 O PHE A 237 8106 11289 9188 2165 917 -247 O
ATOM 1474 CB PHE A 237 -32.224 17.941 26.738 1.00 73.06 C
ANISOU 1474 CB PHE A 237 8463 10737 8560 2670 1193 -389 C
ATOM 1475 CG PHE A 237 -31.795 18.910 25.657 1.00 72.52 C
ANISOU 1475 CG PHE A 237 8586 10409 8560 2864 1164 -419 C
ATOM 1476 CD1 PHE A 237 -32.732 19.712 25.007 1.00 71.32 C
ANISOU 1476 CD1 PHE A 237 8346 10459 8292 3277 1283 -357 C
ATOM 1477 CD2 PHE A 237 -30.444 19.070 25.345 1.00 68.18 C
ANISOU 1477 CD2 PHE A 237 8317 9427 8160 2650 1028 -502 C
ATOM 1478 CE1 PHE A 237 -32.332 20.624 24.040 1.00 70.60 C
ANISOU 1478 CE1 PHE A 237 8477 10103 8246 3461 1264 -379 C
ATOM 1479 CE2 PHE A 237 -30.042 19.972 24.376 1.00 69.47 C
ANISOU 1479 CE2 PHE A 237 8678 9351 8368 2798 1009 -528 C
ATOM 1480 CZ PHE A 237 -30.985 20.751 23.724 1.00 70.07 C
ANISOU 1480 CZ PHE A 237 8702 9587 8336 3201 1127 -469 C
ATOM 1481 N SER A 238 -30.469 15.800 25.242 1.00 68.01 N
ANISOU 1481 N SER A 238 7645 9821 8375 1862 813 -373 N
ATOM 1482 CA SER A 238 -29.601 15.461 24.123 1.00 65.74 C
ANISOU 1482 CA SER A 238 7368 9328 8281 1680 669 -381 C
ATOM 1483 C SER A 238 -30.114 14.231 23.381 1.00 65.48 C
ANISOU 1483 C SER A 238 7023 9547 8311 1445 618 -299 C
ATOM 1484 O SER A 238 -30.389 14.291 22.182 1.00 70.66 O
ANISOU 1484 O SER A 238 7535 10291 9021 1480 588 -267 O
ATOM 1485 CB SER A 238 -28.180 15.262 24.634 1.00 67.36 C
ANISOU 1485 CB SER A 238 7831 9183 8580 1471 560 -447 C
ATOM 1486 OG SER A 238 -27.780 16.426 25.326 1.00 65.99 O
ANISOU 1486 OG SER A 238 7962 8802 8310 1639 610 -527 O
ATOM 1487 N TYR A 239 -30.286 13.110 24.085 1.00 63.02 N
ANISOU 1487 N TYR A 239 6627 9352 7967 1191 613 -264 N
ATOM 1488 CA TYR A 239 -30.748 11.888 23.427 1.00 58.22 C
ANISOU 1488 CA TYR A 239 5794 8943 7385 910 571 -194 C
ATOM 1489 C TYR A 239 -32.143 12.037 22.826 1.00 61.12 C
ANISOU 1489 C TYR A 239 5831 9765 7628 1005 648 -122 C
ATOM 1490 O TYR A 239 -32.525 11.255 21.950 1.00 55.91 O
ANISOU 1490 O TYR A 239 4987 9274 6981 780 601 -72 O
ATOM 1491 CB TYR A 239 -30.732 10.718 24.417 1.00 57.41 C
ANISOU 1491 CB TYR A 239 5721 8864 7227 626 574 -164 C
ATOM 1492 CG TYR A 239 -29.351 10.269 24.749 1.00 60.69 C
ANISOU 1492 CG TYR A 239 6405 8889 7764 497 474 -202 C
ATOM 1493 CD1 TYR A 239 -28.385 10.227 23.764 1.00 56.34 C
ANISOU 1493 CD1 TYR A 239 5947 8084 7377 466 369 -228 C
ATOM 1494 CD2 TYR A 239 -28.990 9.924 26.051 1.00 63.66 C
ANISOU 1494 CD2 TYR A 239 6930 9181 8075 426 486 -203 C
ATOM 1495 CE1 TYR A 239 -27.104 9.836 24.043 1.00 57.10 C
ANISOU 1495 CE1 TYR A 239 6248 7883 7563 382 281 -246 C
ATOM 1496 CE2 TYR A 239 -27.696 9.528 26.339 1.00 61.24 C
ANISOU 1496 CE2 TYR A 239 6840 8568 7859 339 388 -219 C
ATOM 1497 CZ TYR A 239 -26.759 9.493 25.317 1.00 57.41 C
ANISOU 1497 CZ TYR A 239 6416 7867 7532 327 288 -237 C
ATOM 1498 OH TYR A 239 -25.463 9.116 25.527 1.00 57.90 O
ANISOU 1498 OH TYR A 239 6648 7684 7668 271 194 -237 O
ATOM 1499 N THR A 240 -32.945 12.979 23.327 1.00 65.08 N
ANISOU 1499 N THR A 240 6251 10498 7978 1330 773 -107 N
ATOM 1500 CA THR A 240 -34.268 13.202 22.751 1.00 59.43 C
ANISOU 1500 CA THR A 240 5182 10280 7118 1479 850 -18 C
ATOM 1501 C THR A 240 -34.132 13.868 21.389 1.00 59.00 C
ANISOU 1501 C THR A 240 5106 10162 7148 1662 796 -14 C
ATOM 1502 O THR A 240 -34.739 13.428 20.405 1.00 56.49 O
ANISOU 1502 O THR A 240 4513 10142 6807 1540 757 54 O
ATOM 1503 CB THR A 240 -35.131 14.033 23.719 1.00 57.74 C
ANISOU 1503 CB THR A 240 4903 10337 6697 1839 1019 8 C
ATOM 1504 OG1 THR A 240 -35.538 13.214 24.819 1.00 67.20 O
ANISOU 1504 OG1 THR A 240 6015 11734 7783 1609 1073 34 O
ATOM 1505 CG2 THR A 240 -36.363 14.579 23.070 1.00 56.60 C
ANISOU 1505 CG2 THR A 240 4416 10696 6393 2134 1107 108 C
ATOM 1506 N ARG A 241 -33.291 14.904 21.308 1.00 60.73 N
ANISOU 1506 N ARG A 241 5636 9984 7453 1915 788 -89 N
ATOM 1507 CA ARG A 241 -32.978 15.516 20.020 1.00 60.80 C
ANISOU 1507 CA ARG A 241 5689 9856 7555 2054 728 -92 C
ATOM 1508 C ARG A 241 -32.267 14.527 19.101 1.00 62.25 C
ANISOU 1508 C ARG A 241 5855 9883 7916 1675 579 -106 C
ATOM 1509 O ARG A 241 -32.692 14.306 17.965 1.00 62.30 O
ANISOU 1509 O ARG A 241 5656 10088 7929 1624 535 -53 O
ATOM 1510 CB ARG A 241 -32.132 16.775 20.232 1.00 58.31 C
ANISOU 1510 CB ARG A 241 5771 9109 7274 2328 754 -177 C
ATOM 1511 CG ARG A 241 -32.924 18.017 20.696 1.00 70.55 C
ANISOU 1511 CG ARG A 241 7395 10785 8624 2815 921 -156 C
ATOM 1512 CD ARG A 241 -32.107 19.323 20.556 1.00 69.05 C
ANISOU 1512 CD ARG A 241 7656 10131 8450 3059 942 -237 C
ATOM 1513 NE ARG A 241 -32.933 20.495 20.246 1.00 70.32 N
ANISOU 1513 NE ARG A 241 7906 10367 8445 3454 1048 -173 N
ATOM 1514 CZ ARG A 241 -32.521 21.760 20.348 1.00 75.25 C
ANISOU 1514 CZ ARG A 241 8979 10611 9003 3652 1097 -222 C
ATOM 1515 NH1 ARG A 241 -31.286 22.032 20.754 1.00 74.41 N
ANISOU 1515 NH1 ARG A 241 9241 10063 8970 3555 1075 -352 N
ATOM 1516 NH2 ARG A 241 -33.347 22.763 20.061 1.00 76.93 N
ANISOU 1516 NH2 ARG A 241 9290 10892 9049 3934 1169 -137 N
ATOM 1517 N ILE A 242 -31.184 13.912 19.588 1.00 62.86 N
ANISOU 1517 N ILE A 242 6149 9617 8117 1421 506 -171 N
ATOM 1518 CA ILE A 242 -30.429 12.937 18.804 1.00 52.99 C
ANISOU 1518 CA ILE A 242 4928 8189 7018 1104 384 -182 C
ATOM 1519 C ILE A 242 -31.359 11.912 18.181 1.00 60.23 C
ANISOU 1519 C ILE A 242 5560 9457 7867 857 373 -109 C
ATOM 1520 O ILE A 242 -31.204 11.526 17.015 1.00 64.84 O
ANISOU 1520 O ILE A 242 6097 10019 8521 718 300 -101 O
ATOM 1521 CB ILE A 242 -29.379 12.234 19.685 1.00 45.46 C
ANISOU 1521 CB ILE A 242 4194 6935 6142 893 335 -228 C
ATOM 1522 CG1 ILE A 242 -28.290 13.170 20.165 1.00 44.08 C
ANISOU 1522 CG1 ILE A 242 4299 6421 6029 1051 316 -303 C
ATOM 1523 CG2 ILE A 242 -28.746 11.106 18.954 1.00 43.82 C
ANISOU 1523 CG2 ILE A 242 4017 6584 6050 605 241 -222 C
ATOM 1524 CD1 ILE A 242 -27.213 12.402 20.867 1.00 45.23 C
ANISOU 1524 CD1 ILE A 242 4608 6334 6242 842 248 -326 C
ATOM 1525 N TRP A 243 -32.337 11.448 18.952 1.00 60.48 N
ANISOU 1525 N TRP A 243 5409 9830 7742 768 448 -56 N
ATOM 1526 CA TRP A 243 -33.163 10.344 18.493 1.00 61.49 C
ANISOU 1526 CA TRP A 243 5301 10291 7773 430 434 9 C
ATOM 1527 C TRP A 243 -33.990 10.746 17.276 1.00 65.63 C
ANISOU 1527 C TRP A 243 5543 11168 8227 525 423 68 C
ATOM 1528 O TRP A 243 -33.950 10.068 16.245 1.00 69.90 O
ANISOU 1528 O TRP A 243 6039 11721 8797 263 344 76 O
ATOM 1529 CB TRP A 243 -34.048 9.851 19.632 1.00 66.85 C
ANISOU 1529 CB TRP A 243 5834 11295 8270 304 525 60 C
ATOM 1530 CG TRP A 243 -35.090 8.914 19.164 1.00 77.84 C
ANISOU 1530 CG TRP A 243 6946 13124 9506 -46 525 137 C
ATOM 1531 CD1 TRP A 243 -34.961 7.568 18.986 1.00 80.18 C
ANISOU 1531 CD1 TRP A 243 7340 13336 9789 -518 476 139 C
ATOM 1532 CD2 TRP A 243 -36.433 9.247 18.787 1.00 77.49 C
ANISOU 1532 CD2 TRP A 243 6487 13691 9263 29 580 230 C
ATOM 1533 NE1 TRP A 243 -36.144 7.040 18.528 1.00 80.11 N
ANISOU 1533 NE1 TRP A 243 7019 13841 9580 -798 492 217 N
ATOM 1534 CE2 TRP A 243 -37.064 8.050 18.401 1.00 79.44 C
ANISOU 1534 CE2 TRP A 243 6580 14226 9379 -468 549 280 C
ATOM 1535 CE3 TRP A 243 -37.164 10.442 18.746 1.00 78.84 C
ANISOU 1535 CE3 TRP A 243 6417 14208 9331 482 658 284 C
ATOM 1536 CZ2 TRP A 243 -38.396 8.010 17.976 1.00 79.59 C
ANISOU 1536 CZ2 TRP A 243 6270 14802 9167 -550 557 376 C
ATOM 1537 CZ3 TRP A 243 -38.486 10.400 18.320 1.00 78.43 C
ANISOU 1537 CZ3 TRP A 243 6109 14629 9061 432 655 386 C
ATOM 1538 CH2 TRP A 243 -39.085 9.194 17.940 1.00 75.63 C
ANISOU 1538 CH2 TRP A 243 5636 14520 8579 -81 595 428 C
ATOM 1539 N SER A 244 -34.740 11.848 17.366 1.00 64.33 N
ANISOU 1539 N SER A 244 5202 11291 7950 915 505 115 N
ATOM 1540 CA SER A 244 -35.476 12.318 16.193 1.00 65.62 C
ANISOU 1540 CA SER A 244 5099 11800 8035 1067 491 188 C
ATOM 1541 C SER A 244 -34.531 12.545 15.011 1.00 63.54 C
ANISOU 1541 C SER A 244 5031 11158 7954 1074 387 135 C
ATOM 1542 O SER A 244 -34.765 12.036 13.905 1.00 58.11 O
ANISOU 1542 O SER A 244 4198 10626 7256 862 312 166 O
ATOM 1543 CB SER A 244 -36.261 13.590 16.527 1.00 61.05 C
ANISOU 1543 CB SER A 244 4479 11407 7309 1545 593 245 C
ATOM 1544 OG SER A 244 -35.554 14.401 17.442 1.00 62.87 O
ANISOU 1544 OG SER A 244 4966 11316 7605 1859 672 172 O
ATOM 1545 N LYS A 245 -33.440 13.281 15.241 1.00 59.79 N
ANISOU 1545 N LYS A 245 4892 10194 7630 1283 381 53 N
ATOM 1546 CA LYS A 245 -32.381 13.413 14.249 1.00 63.56 C
ANISOU 1546 CA LYS A 245 5578 10286 8286 1243 285 -4 C
ATOM 1547 C LYS A 245 -32.098 12.082 13.539 1.00 64.08 C
ANISOU 1547 C LYS A 245 5619 10312 8417 803 191 -14 C
ATOM 1548 O LYS A 245 -32.336 11.954 12.326 1.00 62.65 O
ANISOU 1548 O LYS A 245 5316 10260 8227 728 136 15 O
ATOM 1549 CB LYS A 245 -31.117 13.974 14.920 1.00 57.22 C
ANISOU 1549 CB LYS A 245 5143 8980 7618 1352 283 -97 C
ATOM 1550 CG LYS A 245 -31.156 15.483 15.186 1.00 54.43 C
ANISOU 1550 CG LYS A 245 4939 8534 7209 1786 363 -106 C
ATOM 1551 CD LYS A 245 -31.034 16.267 13.883 1.00 62.51 C
ANISOU 1551 CD LYS A 245 5996 9489 8265 1972 332 -87 C
ATOM 1552 CE LYS A 245 -31.362 17.757 14.052 1.00 66.67 C
ANISOU 1552 CE LYS A 245 6678 9977 8677 2440 438 -70 C
ATOM 1553 NZ LYS A 245 -31.747 18.379 12.737 1.00 62.05 N
ANISOU 1553 NZ LYS A 245 6057 9464 8054 2593 417 -1 N
ATOM 1554 N LEU A 246 -31.651 11.062 14.296 1.00 54.14 N
ANISOU 1554 N LEU A 246 4490 8885 7195 515 181 -50 N
ATOM 1555 CA LEU A 246 -31.276 9.781 13.689 1.00 54.34 C
ANISOU 1555 CA LEU A 246 4591 8787 7267 126 112 -66 C
ATOM 1556 C LEU A 246 -32.436 9.059 13.015 1.00 58.79 C
ANISOU 1556 C LEU A 246 4890 9784 7665 -152 105 -2 C
ATOM 1557 O LEU A 246 -32.185 8.192 12.171 1.00 64.08 O
ANISOU 1557 O LEU A 246 5643 10351 8352 -446 47 -20 O
ATOM 1558 CB LEU A 246 -30.653 8.836 14.724 1.00 53.51 C
ANISOU 1558 CB LEU A 246 4704 8430 7196 -85 121 -97 C
ATOM 1559 CG LEU A 246 -29.181 9.052 15.108 1.00 60.24 C
ANISOU 1559 CG LEU A 246 5853 8813 8221 36 87 -161 C
ATOM 1560 CD1 LEU A 246 -28.563 7.778 15.669 1.00 63.82 C
ANISOU 1560 CD1 LEU A 246 6515 9042 8692 -220 77 -168 C
ATOM 1561 CD2 LEU A 246 -28.334 9.593 13.933 1.00 59.85 C
ANISOU 1561 CD2 LEU A 246 5889 8541 8310 155 23 -198 C
ATOM 1562 N LYS A 247 -33.689 9.384 13.361 1.00 54.02 N
ANISOU 1562 N LYS A 247 3972 9678 6876 -76 165 75 N
ATOM 1563 CA LYS A 247 -34.846 8.644 12.864 1.00 60.20 C
ANISOU 1563 CA LYS A 247 4463 10956 7455 -402 156 147 C
ATOM 1564 C LYS A 247 -35.414 9.230 11.570 1.00 69.49 C
ANISOU 1564 C LYS A 247 5386 12451 8565 -274 110 203 C
ATOM 1565 O LYS A 247 -35.846 8.479 10.688 1.00 74.02 O
ANISOU 1565 O LYS A 247 5915 13175 9036 -616 50 222 O
ATOM 1566 CB LYS A 247 -35.940 8.605 13.938 1.00 69.00 C
ANISOU 1566 CB LYS A 247 5316 12531 8369 -414 248 220 C
ATOM 1567 CG LYS A 247 -36.954 7.465 13.791 1.00 77.08 C
ANISOU 1567 CG LYS A 247 6192 13930 9164 -907 237 277 C
ATOM 1568 CD LYS A 247 -36.327 6.131 14.185 1.00 79.64 C
ANISOU 1568 CD LYS A 247 6791 13941 9527 -1378 228 220 C
ATOM 1569 CE LYS A 247 -37.313 4.974 14.070 1.00 77.58 C
ANISOU 1569 CE LYS A 247 6486 13980 9010 -1896 223 267 C
ATOM 1570 NZ LYS A 247 -36.569 3.683 14.055 1.00 77.22 N
ANISOU 1570 NZ LYS A 247 6788 13547 9005 -2366 209 206 N
ATOM 1571 N ASN A 248 -35.417 10.558 11.431 1.00 71.12 N
ANISOU 1571 N ASN A 248 5573 12639 8809 215 135 225 N
ATOM 1572 CA ASN A 248 -36.054 11.229 10.304 1.00 71.38 C
ANISOU 1572 CA ASN A 248 5527 12846 8747 393 100 290 C
ATOM 1573 C ASN A 248 -35.075 12.098 9.527 1.00 71.58 C
ANISOU 1573 C ASN A 248 5727 12512 8957 678 63 245 C
ATOM 1574 O ASN A 248 -35.458 13.119 8.946 1.00 72.59 O
ANISOU 1574 O ASN A 248 5860 12694 9025 997 73 300 O
ATOM 1575 CB ASN A 248 -37.244 12.058 10.778 1.00 70.87 C
ANISOU 1575 CB ASN A 248 5322 13129 8476 706 177 387 C
ATOM 1576 CG ASN A 248 -38.397 11.195 11.211 1.00 79.58 C
ANISOU 1576 CG ASN A 248 6211 14683 9344 394 193 454 C
ATOM 1577 OD1 ASN A 248 -38.487 10.795 12.373 1.00 80.57 O
ANISOU 1577 OD1 ASN A 248 6321 14850 9441 299 254 442 O
ATOM 1578 ND2 ASN A 248 -39.278 10.876 10.270 1.00 81.40 N
ANISOU 1578 ND2 ASN A 248 6282 15262 9386 212 136 525 N
ATOM 1579 N HIS A 249 -33.811 11.704 9.509 1.00 67.48 N
ANISOU 1579 N HIS A 249 5420 11578 8643 551 22 148 N
ATOM 1580 CA HIS A 249 -32.826 12.386 8.692 1.00 71.56 C
ANISOU 1580 CA HIS A 249 6165 11705 9321 737 -23 100 C
ATOM 1581 C HIS A 249 -32.817 11.778 7.295 1.00 68.47 C
ANISOU 1581 C HIS A 249 5719 11376 8921 474 -112 104 C
ATOM 1582 O HIS A 249 -33.109 10.593 7.110 1.00 72.52 O
ANISOU 1582 O HIS A 249 6174 12017 9362 61 -145 97 O
ATOM 1583 CB HIS A 249 -31.433 12.283 9.323 1.00 73.69 C
ANISOU 1583 CB HIS A 249 6798 11410 9789 706 -26 -5 C
ATOM 1584 CG HIS A 249 -30.640 11.105 8.843 1.00 73.99 C
ANISOU 1584 CG HIS A 249 6999 11186 9926 337 -91 -64 C
ATOM 1585 ND1 HIS A 249 -31.159 9.829 8.791 1.00 72.40 N
ANISOU 1585 ND1 HIS A 249 6722 11162 9626 -49 -105 -52 N
ATOM 1586 CD2 HIS A 249 -29.369 11.014 8.379 1.00 71.69 C
ANISOU 1586 CD2 HIS A 249 6963 10476 9800 307 -134 -131 C
ATOM 1587 CE1 HIS A 249 -30.244 9.005 8.310 1.00 73.19 C
ANISOU 1587 CE1 HIS A 249 7059 10925 9826 -270 -145 -112 C
ATOM 1588 NE2 HIS A 249 -29.147 9.699 8.056 1.00 69.62 N
ANISOU 1588 NE2 HIS A 249 6783 10132 9537 -44 -164 -156 N
ATOM 1589 N VAL A 250 -32.503 12.609 6.310 1.00 61.33 N
ANISOU 1589 N VAL A 250 4861 10373 8068 703 -145 114 N
ATOM 1590 CA VAL A 250 -32.126 12.160 4.977 1.00 58.50 C
ANISOU 1590 CA VAL A 250 4553 9928 7747 491 -227 92 C
ATOM 1591 C VAL A 250 -30.638 12.418 4.828 1.00 53.54 C
ANISOU 1591 C VAL A 250 4276 8729 7337 557 -240 0 C
ATOM 1592 O VAL A 250 -30.151 13.468 5.253 1.00 60.01 O
ANISOU 1592 O VAL A 250 5235 9335 8232 872 -202 -11 O
ATOM 1593 CB VAL A 250 -32.912 12.895 3.876 1.00 60.83 C
ANISOU 1593 CB VAL A 250 4649 10552 7910 683 -256 187 C
ATOM 1594 CG1 VAL A 250 -32.751 14.402 4.029 1.00 66.17 C
ANISOU 1594 CG1 VAL A 250 5472 11049 8619 1173 -198 218 C
ATOM 1595 CG2 VAL A 250 -32.431 12.450 2.513 1.00 56.02 C
ANISOU 1595 CG2 VAL A 250 4091 9853 7341 466 -342 156 C
ATOM 1596 N ALA A1000 -29.905 11.461 4.257 1.00 48.22 N
ANISOU 1596 N ALA A1000 3761 7819 6742 255 -286 -64 N
ATOM 1597 CA ALA A1000 -28.482 11.704 4.034 1.00 46.68 C
ANISOU 1597 CA ALA A1000 3849 7155 6732 327 -296 -136 C
ATOM 1598 C ALA A1000 -28.273 12.816 2.994 1.00 54.64 C
ANISOU 1598 C ALA A1000 4872 8125 7764 569 -320 -110 C
ATOM 1599 O ALA A1000 -28.992 12.913 1.986 1.00 57.85 O
ANISOU 1599 O ALA A1000 5115 8804 8063 561 -355 -55 O
ATOM 1600 CB ALA A1000 -27.770 10.424 3.601 1.00 40.63 C
ANISOU 1600 CB ALA A1000 3253 6167 6019 4 -321 -198 C
ATOM 1601 N LYS A1001 -27.295 13.679 3.260 1.00 45.48 N
ANISOU 1601 N LYS A1001 3916 6640 6723 771 -300 -145 N
ATOM 1602 CA LYS A1001 -26.913 14.745 2.347 1.00 34.26 C
ANISOU 1602 CA LYS A1001 2587 5105 5327 974 -312 -128 C
ATOM 1603 C LYS A1001 -25.516 14.481 1.793 1.00 35.93 C
ANISOU 1603 C LYS A1001 3004 4970 5678 838 -340 -196 C
ATOM 1604 O LYS A1001 -24.574 14.238 2.557 1.00 32.03 O
ANISOU 1604 O LYS A1001 2651 4237 5283 776 -326 -251 O
ATOM 1605 CB LYS A1001 -26.958 16.084 3.065 1.00 40.32 C
ANISOU 1605 CB LYS A1001 3460 5787 6072 1306 -254 -107 C
ATOM 1606 CG LYS A1001 -28.370 16.564 3.363 1.00 50.32 C
ANISOU 1606 CG LYS A1001 4518 7432 7171 1545 -210 -16 C
ATOM 1607 CD LYS A1001 -28.374 17.646 4.427 1.00 53.23 C
ANISOU 1607 CD LYS A1001 5051 7668 7507 1851 -125 -16 C
ATOM 1608 CE LYS A1001 -27.156 18.555 4.285 1.00 54.75 C
ANISOU 1608 CE LYS A1001 5594 7418 7792 1922 -118 -73 C
ATOM 1609 NZ LYS A1001 -27.094 19.258 2.980 1.00 57.23 N
ANISOU 1609 NZ LYS A1001 5978 7692 8076 2049 -138 -25 N
ATOM 1610 N ALA A1002 -25.390 14.503 0.464 1.00 39.14 N
ANISOU 1610 N ALA A1002 3408 5387 6075 795 -376 -183 N
ATOM 1611 CA ALA A1002 -24.116 14.286 -0.213 1.00 31.53 C
ANISOU 1611 CA ALA A1002 2612 4147 5220 687 -392 -237 C
ATOM 1612 C ALA A1002 -23.722 15.516 -1.018 1.00 40.63 C
ANISOU 1612 C ALA A1002 3869 5191 6376 865 -394 -211 C
ATOM 1613 O ALA A1002 -24.562 16.154 -1.679 1.00 32.42 O
ANISOU 1613 O ALA A1002 2748 4334 5235 1013 -404 -143 O
ATOM 1614 CB ALA A1002 -24.157 13.052 -1.127 1.00 31.95 C
ANISOU 1614 CB ALA A1002 2631 4260 5248 432 -420 -259 C
ATOM 1615 N LEU A1003 -22.434 15.841 -0.937 1.00 29.93 N
ANISOU 1615 N LEU A1003 2694 3558 5121 845 -383 -255 N
ATOM 1616 CA LEU A1003 -21.806 16.865 -1.762 1.00 31.86 C
ANISOU 1616 CA LEU A1003 3082 3654 5369 929 -381 -240 C
ATOM 1617 C LEU A1003 -20.910 16.139 -2.745 1.00 30.70 C
ANISOU 1617 C LEU A1003 2954 3430 5281 749 -399 -273 C
ATOM 1618 O LEU A1003 -20.109 15.294 -2.326 1.00 30.70 O
ANISOU 1618 O LEU A1003 2968 3342 5356 617 -391 -321 O
ATOM 1619 CB LEU A1003 -20.977 17.849 -0.918 1.00 30.46 C
ANISOU 1619 CB LEU A1003 3102 3248 5223 997 -350 -264 C
ATOM 1620 CG LEU A1003 -20.196 18.938 -1.653 1.00 37.72 C
ANISOU 1620 CG LEU A1003 4223 3982 6128 1023 -339 -254 C
ATOM 1621 CD1 LEU A1003 -21.169 19.873 -2.323 1.00 44.49 C
ANISOU 1621 CD1 LEU A1003 5129 4905 6870 1250 -325 -180 C
ATOM 1622 CD2 LEU A1003 -19.280 19.755 -0.772 1.00 34.05 C
ANISOU 1622 CD2 LEU A1003 3969 3301 5669 991 -314 -290 C
ATOM 1623 N ILE A1004 -21.047 16.440 -4.041 1.00 30.09 N
ANISOU 1623 N ILE A1004 2881 3396 5154 764 -416 -242 N
ATOM 1624 CA ILE A1004 -20.084 15.968 -5.044 1.00 29.99 C
ANISOU 1624 CA ILE A1004 2922 3288 5183 625 -416 -272 C
ATOM 1625 C ILE A1004 -19.401 17.177 -5.662 1.00 31.64 C
ANISOU 1625 C ILE A1004 3278 3359 5384 695 -404 -246 C
ATOM 1626 O ILE A1004 -20.054 18.019 -6.297 1.00 36.47 O
ANISOU 1626 O ILE A1004 3923 4024 5911 826 -414 -187 O
ATOM 1627 CB ILE A1004 -20.712 15.079 -6.128 1.00 32.27 C
ANISOU 1627 CB ILE A1004 3119 3739 5405 514 -442 -269 C
ATOM 1628 CG1 ILE A1004 -21.270 13.795 -5.516 1.00 32.69 C
ANISOU 1628 CG1 ILE A1004 3084 3892 5443 375 -445 -302 C
ATOM 1629 CG2 ILE A1004 -19.663 14.671 -7.104 1.00 30.86 C
ANISOU 1629 CG2 ILE A1004 3029 3440 5258 406 -423 -304 C
ATOM 1630 CD1 ILE A1004 -22.173 13.027 -6.484 1.00 33.76 C
ANISOU 1630 CD1 ILE A1004 3138 4231 5458 225 -478 -296 C
ATOM 1631 N VAL A1005 -18.085 17.261 -5.469 1.00 31.45 N
ANISOU 1631 N VAL A1005 3344 3178 5428 605 -381 -281 N
ATOM 1632 CA VAL A1005 -17.262 18.304 -6.058 1.00 32.55 C
ANISOU 1632 CA VAL A1005 3634 3189 5545 592 -364 -262 C
ATOM 1633 C VAL A1005 -16.282 17.620 -6.975 1.00 35.54 C
ANISOU 1633 C VAL A1005 3978 3572 5955 457 -350 -283 C
ATOM 1634 O VAL A1005 -15.494 16.786 -6.514 1.00 35.74 O
ANISOU 1634 O VAL A1005 3940 3599 6042 378 -333 -320 O
ATOM 1635 CB VAL A1005 -16.514 19.140 -5.004 1.00 34.09 C
ANISOU 1635 CB VAL A1005 3963 3240 5750 567 -346 -277 C
ATOM 1636 CG1 VAL A1005 -15.716 20.282 -5.709 1.00 31.26 C
ANISOU 1636 CG1 VAL A1005 3799 2749 5331 500 -325 -253 C
ATOM 1637 CG2 VAL A1005 -17.481 19.717 -3.979 1.00 30.18 C
ANISOU 1637 CG2 VAL A1005 3525 2729 5213 723 -342 -266 C
ATOM 1638 N TYR A1006 -16.307 17.985 -8.260 1.00 38.87 N
ANISOU 1638 N TYR A1006 4449 4000 6320 454 -348 -253 N
ATOM 1639 CA TYR A1006 -15.365 17.450 -9.246 1.00 40.69 C
ANISOU 1639 CA TYR A1006 4664 4239 6558 343 -319 -270 C
ATOM 1640 C TYR A1006 -14.659 18.569 -10.004 1.00 39.82 C
ANISOU 1640 C TYR A1006 4687 4049 6394 298 -299 -233 C
ATOM 1641 O TYR A1006 -15.191 19.673 -10.143 1.00 36.74 O
ANISOU 1641 O TYR A1006 4432 3591 5937 376 -311 -186 O
ATOM 1642 CB TYR A1006 -16.058 16.543 -10.278 1.00 32.35 C
ANISOU 1642 CB TYR A1006 3546 3288 5459 330 -331 -279 C
ATOM 1643 CG TYR A1006 -17.169 17.277 -10.966 1.00 40.48 C
ANISOU 1643 CG TYR A1006 4599 4389 6394 420 -373 -221 C
ATOM 1644 CD1 TYR A1006 -18.387 17.449 -10.335 1.00 41.56 C
ANISOU 1644 CD1 TYR A1006 4669 4623 6498 532 -412 -191 C
ATOM 1645 CD2 TYR A1006 -16.995 17.840 -12.211 1.00 42.97 C
ANISOU 1645 CD2 TYR A1006 4992 4697 6636 414 -370 -182 C
ATOM 1646 CE1 TYR A1006 -19.396 18.133 -10.924 1.00 37.93 C
ANISOU 1646 CE1 TYR A1006 4204 4276 5931 661 -447 -118 C
ATOM 1647 CE2 TYR A1006 -18.016 18.520 -12.816 1.00 47.77 C
ANISOU 1647 CE2 TYR A1006 5620 5391 7141 532 -410 -111 C
ATOM 1648 CZ TYR A1006 -19.216 18.665 -12.166 1.00 43.84 C
ANISOU 1648 CZ TYR A1006 5037 5013 6606 670 -449 -74 C
ATOM 1649 OH TYR A1006 -20.258 19.365 -12.748 1.00 51.93 O
ANISOU 1649 OH TYR A1006 6054 6175 7503 838 -486 19 O
ATOM 1650 N GLY A1007 -13.470 18.250 -10.518 1.00 37.58 N
ANISOU 1650 N GLY A1007 4377 3783 6120 184 -257 -246 N
ATOM 1651 CA GLY A1007 -12.771 19.075 -11.502 1.00 38.33 C
ANISOU 1651 CA GLY A1007 4575 3843 6145 99 -229 -210 C
ATOM 1652 C GLY A1007 -12.604 18.326 -12.819 1.00 41.94 C
ANISOU 1652 C GLY A1007 4981 4382 6573 79 -199 -217 C
ATOM 1653 O GLY A1007 -12.084 17.212 -12.835 1.00 39.66 O
ANISOU 1653 O GLY A1007 4584 4163 6321 67 -162 -256 O
ATOM 1654 N SER A1008 -13.058 18.950 -13.919 1.00 40.60 N
ANISOU 1654 N SER A1008 4915 4194 6319 93 -209 -174 N
ATOM 1655 CA SER A1008 -13.170 18.248 -15.197 1.00 38.78 C
ANISOU 1655 CA SER A1008 4655 4042 6036 80 -192 -184 C
ATOM 1656 C SER A1008 -12.910 19.198 -16.359 1.00 43.33 C
ANISOU 1656 C SER A1008 5362 4589 6512 34 -176 -126 C
ATOM 1657 O SER A1008 -13.622 20.183 -16.531 1.00 50.57 O
ANISOU 1657 O SER A1008 6405 5446 7365 106 -215 -65 O
ATOM 1658 CB SER A1008 -14.548 17.593 -15.328 1.00 44.76 C
ANISOU 1658 CB SER A1008 5361 4874 6772 158 -250 -196 C
ATOM 1659 OG SER A1008 -14.698 16.888 -16.552 1.00 46.12 O
ANISOU 1659 OG SER A1008 5534 5121 6868 109 -239 -215 O
ATOM 1660 N THR A1009 -11.916 18.878 -17.191 1.00 55.77 N
ANISOU 1660 N THR A1009 6920 6215 8056 -63 -110 -137 N
ATOM 1661 CA THR A1009 -11.538 19.748 -18.303 1.00 56.08 C
ANISOU 1661 CA THR A1009 7086 6233 7989 -137 -83 -80 C
ATOM 1662 C THR A1009 -12.229 19.356 -19.599 1.00 48.54 C
ANISOU 1662 C THR A1009 6157 5339 6946 -97 -98 -73 C
ATOM 1663 O THR A1009 -12.596 20.217 -20.394 1.00 51.66 O
ANISOU 1663 O THR A1009 6684 5702 7241 -85 -119 -5 O
ATOM 1664 CB THR A1009 -10.012 19.745 -18.516 1.00 52.11 C
ANISOU 1664 CB THR A1009 6532 5796 7470 -285 5 -82 C
ATOM 1665 OG1 THR A1009 -9.367 20.388 -17.416 1.00 56.88 O
ANISOU 1665 OG1 THR A1009 7136 6368 8108 -376 5 -71 O
ATOM 1666 CG2 THR A1009 -9.661 20.536 -19.714 1.00 46.75 C
ANISOU 1666 CG2 THR A1009 5985 5108 6669 -383 40 -25 C
ATOM 1667 N THR A1010 -12.409 18.075 -19.850 1.00 44.65 N
ANISOU 1667 N THR A1010 5570 4928 6467 -85 -85 -140 N
ATOM 1668 CA THR A1010 -13.087 17.651 -21.062 1.00 46.36 C
ANISOU 1668 CA THR A1010 5825 5216 6575 -89 -105 -143 C
ATOM 1669 C THR A1010 -14.330 16.844 -20.756 1.00 47.53 C
ANISOU 1669 C THR A1010 5909 5431 6720 -51 -179 -179 C
ATOM 1670 O THR A1010 -14.864 16.187 -21.657 1.00 54.41 O
ANISOU 1670 O THR A1010 6800 6387 7487 -104 -196 -205 O
ATOM 1671 CB THR A1010 -12.151 16.834 -21.953 1.00 51.90 C
ANISOU 1671 CB THR A1010 6535 5958 7227 -159 -4 -194 C
ATOM 1672 OG1 THR A1010 -12.059 15.509 -21.429 1.00 54.36 O
ANISOU 1672 OG1 THR A1010 6792 6271 7591 -136 35 -279 O
ATOM 1673 CG2 THR A1010 -10.753 17.491 -22.030 1.00 47.71 C
ANISOU 1673 CG2 THR A1010 6002 5424 6702 -220 82 -159 C
ATOM 1674 N GLY A1011 -14.771 16.844 -19.495 1.00 46.37 N
ANISOU 1674 N GLY A1011 5690 5261 6666 10 -220 -185 N
ATOM 1675 CA GLY A1011 -16.047 16.299 -19.106 1.00 44.98 C
ANISOU 1675 CA GLY A1011 5436 5184 6470 32 -297 -198 C
ATOM 1676 C GLY A1011 -16.049 14.858 -18.647 1.00 47.51 C
ANISOU 1676 C GLY A1011 5722 5504 6824 -46 -267 -292 C
ATOM 1677 O GLY A1011 -17.139 14.327 -18.382 1.00 51.49 O
ANISOU 1677 O GLY A1011 6167 6111 7284 -84 -330 -305 O
ATOM 1678 N ASN A1012 -14.888 14.199 -18.543 1.00 42.86 N
ANISOU 1678 N ASN A1012 5175 4818 6290 -66 -169 -349 N
ATOM 1679 CA ASN A1012 -14.906 12.790 -18.167 1.00 43.08 C
ANISOU 1679 CA ASN A1012 5238 4808 6321 -111 -125 -431 C
ATOM 1680 C ASN A1012 -15.264 12.605 -16.693 1.00 42.86 C
ANISOU 1680 C ASN A1012 5131 4757 6397 -69 -159 -436 C
ATOM 1681 O ASN A1012 -16.186 11.842 -16.361 1.00 44.77 O
ANISOU 1681 O ASN A1012 5377 5036 6599 -142 -195 -470 O
ATOM 1682 CB ASN A1012 -13.570 12.137 -18.494 1.00 43.24 C
ANISOU 1682 CB ASN A1012 5334 4749 6345 -77 4 -473 C
ATOM 1683 CG ASN A1012 -13.431 11.852 -19.959 1.00 48.11 C
ANISOU 1683 CG ASN A1012 6070 5385 6825 -140 52 -497 C
ATOM 1684 OD1 ASN A1012 -14.431 11.625 -20.650 1.00 56.18 O
ANISOU 1684 OD1 ASN A1012 7151 6463 7733 -250 -8 -514 O
ATOM 1685 ND2 ASN A1012 -12.202 11.881 -20.457 1.00 47.55 N
ANISOU 1685 ND2 ASN A1012 6020 5301 6744 -80 161 -494 N
ATOM 1686 N THR A1013 -14.534 13.283 -15.794 1.00 39.13 N
ANISOU 1686 N THR A1013 4594 4237 6038 19 -145 -404 N
ATOM 1687 CA THR A1013 -14.891 13.282 -14.374 1.00 38.03 C
ANISOU 1687 CA THR A1013 4381 4081 5988 63 -182 -402 C
ATOM 1688 C THR A1013 -16.279 13.862 -14.136 1.00 40.44 C
ANISOU 1688 C THR A1013 4626 4479 6260 74 -279 -363 C
ATOM 1689 O THR A1013 -16.987 13.419 -13.230 1.00 42.21 O
ANISOU 1689 O THR A1013 4794 4737 6505 69 -309 -377 O
ATOM 1690 CB THR A1013 -13.885 14.083 -13.574 1.00 40.21 C
ANISOU 1690 CB THR A1013 4612 4310 6355 122 -161 -370 C
ATOM 1691 OG1 THR A1013 -12.572 13.692 -13.966 1.00 43.14 O
ANISOU 1691 OG1 THR A1013 4991 4675 6724 125 -72 -382 O
ATOM 1692 CG2 THR A1013 -14.070 13.787 -12.103 1.00 40.80 C
ANISOU 1692 CG2 THR A1013 4629 4361 6511 161 -181 -383 C
ATOM 1693 N GLU A1014 -16.681 14.858 -14.925 1.00 44.99 N
ANISOU 1693 N GLU A1014 5211 5114 6769 107 -320 -303 N
ATOM 1694 CA GLU A1014 -18.039 15.369 -14.815 1.00 47.47 C
ANISOU 1694 CA GLU A1014 5450 5568 7017 169 -403 -246 C
ATOM 1695 C GLU A1014 -19.055 14.279 -15.123 1.00 51.32 C
ANISOU 1695 C GLU A1014 5873 6220 7407 45 -444 -278 C
ATOM 1696 O GLU A1014 -20.031 14.109 -14.381 1.00 56.61 O
ANISOU 1696 O GLU A1014 6432 7020 8059 51 -491 -263 O
ATOM 1697 CB GLU A1014 -18.224 16.563 -15.744 1.00 44.46 C
ANISOU 1697 CB GLU A1014 5123 5218 6552 256 -430 -163 C
ATOM 1698 CG GLU A1014 -19.594 17.188 -15.736 1.00 42.66 C
ANISOU 1698 CG GLU A1014 4812 5170 6225 390 -505 -77 C
ATOM 1699 CD GLU A1014 -19.620 18.412 -16.605 1.00 59.52 C
ANISOU 1699 CD GLU A1014 7055 7289 8271 517 -515 18 C
ATOM 1700 OE1 GLU A1014 -20.046 19.483 -16.119 1.00 65.16 O
ANISOU 1700 OE1 GLU A1014 7819 7976 8962 717 -522 96 O
ATOM 1701 OE2 GLU A1014 -19.170 18.315 -17.777 1.00 68.50 O
ANISOU 1701 OE2 GLU A1014 8260 8418 9349 425 -502 15 O
ATOM 1702 N TYR A1015 -18.834 13.517 -16.210 1.00 49.97 N
ANISOU 1702 N TYR A1015 5782 6054 7152 -93 -420 -324 N
ATOM 1703 CA TYR A1015 -19.696 12.371 -16.499 1.00 43.68 C
ANISOU 1703 CA TYR A1015 4980 5385 6233 -282 -449 -372 C
ATOM 1704 C TYR A1015 -19.653 11.357 -15.371 1.00 45.97 C
ANISOU 1704 C TYR A1015 5297 5585 6586 -351 -412 -436 C
ATOM 1705 O TYR A1015 -20.686 10.806 -14.988 1.00 47.63 O
ANISOU 1705 O TYR A1015 5439 5942 6716 -478 -461 -442 O
ATOM 1706 CB TYR A1015 -19.317 11.702 -17.823 1.00 43.41 C
ANISOU 1706 CB TYR A1015 5096 5315 6084 -423 -409 -426 C
ATOM 1707 CG TYR A1015 -20.025 10.383 -18.040 1.00 45.97 C
ANISOU 1707 CG TYR A1015 5499 5705 6263 -672 -418 -499 C
ATOM 1708 CD1 TYR A1015 -21.299 10.323 -18.584 1.00 45.26 C
ANISOU 1708 CD1 TYR A1015 5306 5896 5993 -835 -520 -468 C
ATOM 1709 CD2 TYR A1015 -19.421 9.188 -17.659 1.00 56.12 C
ANISOU 1709 CD2 TYR A1015 6976 6779 7568 -750 -321 -593 C
ATOM 1710 CE1 TYR A1015 -21.938 9.104 -18.754 1.00 46.32 C
ANISOU 1710 CE1 TYR A1015 5539 6096 5965 -1131 -529 -540 C
ATOM 1711 CE2 TYR A1015 -20.058 7.954 -17.814 1.00 53.29 C
ANISOU 1711 CE2 TYR A1015 6767 6430 7051 -1011 -315 -667 C
ATOM 1712 CZ TYR A1015 -21.308 7.912 -18.361 1.00 49.30 C
ANISOU 1712 CZ TYR A1015 6169 6201 6363 -1232 -421 -646 C
ATOM 1713 OH TYR A1015 -21.900 6.670 -18.502 1.00 48.52 O
ANISOU 1713 OH TYR A1015 6250 6106 6079 -1552 -413 -726 O
ATOM 1714 N THR A1016 -18.473 11.099 -14.815 1.00 48.43 N
ANISOU 1714 N THR A1016 5699 5682 7021 -273 -325 -475 N
ATOM 1715 CA THR A1016 -18.413 10.152 -13.709 1.00 41.60 C
ANISOU 1715 CA THR A1016 4877 4723 6206 -308 -287 -522 C
ATOM 1716 C THR A1016 -19.229 10.649 -12.523 1.00 39.21 C
ANISOU 1716 C THR A1016 4411 4530 5956 -257 -353 -476 C
ATOM 1717 O THR A1016 -19.951 9.875 -11.889 1.00 41.47 O
ANISOU 1717 O THR A1016 4689 4870 6199 -374 -367 -499 O
ATOM 1718 CB THR A1016 -16.959 9.879 -13.326 1.00 40.58 C
ANISOU 1718 CB THR A1016 4839 4397 6183 -186 -187 -546 C
ATOM 1719 OG1 THR A1016 -16.260 9.413 -14.492 1.00 42.13 O
ANISOU 1719 OG1 THR A1016 5181 4520 6305 -208 -111 -583 O
ATOM 1720 CG2 THR A1016 -16.897 8.789 -12.253 1.00 42.79 C
ANISOU 1720 CG2 THR A1016 5202 4570 6488 -203 -141 -586 C
ATOM 1721 N ALA A1017 -19.176 11.947 -12.255 1.00 37.03 N
ANISOU 1721 N ALA A1017 4029 4291 5749 -94 -388 -411 N
ATOM 1722 CA ALA A1017 -19.859 12.516 -11.101 1.00 35.90 C
ANISOU 1722 CA ALA A1017 3761 4230 5648 1 -430 -368 C
ATOM 1723 C ALA A1017 -21.381 12.463 -11.259 1.00 41.63 C
ANISOU 1723 C ALA A1017 4345 5233 6241 -62 -503 -327 C
ATOM 1724 O ALA A1017 -22.105 12.244 -10.281 1.00 49.79 O
ANISOU 1724 O ALA A1017 5277 6373 7267 -73 -521 -317 O
ATOM 1725 CB ALA A1017 -19.375 13.957 -10.895 1.00 35.48 C
ANISOU 1725 CB ALA A1017 3707 4108 5665 188 -431 -313 C
ATOM 1726 N GLU A1018 -21.880 12.698 -12.475 1.00 39.81 N
ANISOU 1726 N GLU A1018 4083 5158 5885 -102 -548 -292 N
ATOM 1727 CA GLU A1018 -23.299 12.589 -12.781 1.00 40.79 C
ANISOU 1727 CA GLU A1018 4034 5622 5842 -184 -626 -240 C
ATOM 1728 C GLU A1018 -23.822 11.178 -12.586 1.00 45.75 C
ANISOU 1728 C GLU A1018 4672 6333 6377 -481 -629 -306 C
ATOM 1729 O GLU A1018 -25.028 10.986 -12.391 1.00 48.85 O
ANISOU 1729 O GLU A1018 4883 7042 6637 -586 -690 -264 O
ATOM 1730 CB GLU A1018 -23.542 12.988 -14.236 1.00 46.16 C
ANISOU 1730 CB GLU A1018 4705 6442 6391 -196 -672 -194 C
ATOM 1731 CG GLU A1018 -24.066 14.389 -14.490 1.00 55.23 C
ANISOU 1731 CG GLU A1018 5743 7750 7492 75 -718 -69 C
ATOM 1732 CD GLU A1018 -24.046 14.751 -15.970 1.00 66.37 C
ANISOU 1732 CD GLU A1018 7195 9238 8784 68 -752 -27 C
ATOM 1733 OE1 GLU A1018 -23.187 14.199 -16.702 1.00 69.67 O
ANISOU 1733 OE1 GLU A1018 7778 9470 9222 -88 -712 -105 O
ATOM 1734 OE2 GLU A1018 -24.885 15.581 -16.400 1.00 71.65 O
ANISOU 1734 OE2 GLU A1018 7737 10162 9326 239 -812 92 O
ATOM 1735 N THR A1019 -22.946 10.190 -12.703 1.00 45.13 N
ANISOU 1735 N THR A1019 4816 5992 6338 -621 -559 -402 N
ATOM 1736 CA THR A1019 -23.299 8.783 -12.689 1.00 42.62 C
ANISOU 1736 CA THR A1019 4624 5667 5903 -924 -540 -476 C
ATOM 1737 C THR A1019 -23.338 8.268 -11.264 1.00 45.33 C
ANISOU 1737 C THR A1019 4978 5924 6323 -935 -504 -495 C
ATOM 1738 O THR A1019 -24.238 7.506 -10.884 1.00 49.99 O
ANISOU 1738 O THR A1019 5542 6665 6788 -1174 -526 -507 O
ATOM 1739 CB THR A1019 -22.286 8.005 -13.540 1.00 42.92 C
ANISOU 1739 CB THR A1019 4953 5429 5924 -1007 -457 -563 C
ATOM 1740 OG1 THR A1019 -22.112 8.689 -14.775 1.00 52.79 O
ANISOU 1740 OG1 THR A1019 6181 6747 7131 -947 -484 -535 O
ATOM 1741 CG2 THR A1019 -22.762 6.594 -13.860 1.00 42.08 C
ANISOU 1741 CG2 THR A1019 5057 5303 5628 -1354 -434 -642 C
ATOM 1742 N ILE A1020 -22.346 8.684 -10.486 1.00 44.53 N
ANISOU 1742 N ILE A1020 4915 5595 6409 -701 -451 -495 N
ATOM 1743 CA ILE A1020 -22.378 8.499 -9.048 1.00 43.67 C
ANISOU 1743 CA ILE A1020 4774 5433 6385 -651 -430 -493 C
ATOM 1744 C ILE A1020 -23.636 9.134 -8.491 1.00 48.93 C
ANISOU 1744 C ILE A1020 5179 6417 6997 -629 -502 -421 C
ATOM 1745 O ILE A1020 -24.380 8.531 -7.701 1.00 48.65 O
ANISOU 1745 O ILE A1020 5089 6500 6897 -773 -507 -421 O
ATOM 1746 CB ILE A1020 -21.113 9.106 -8.427 1.00 35.90 C
ANISOU 1746 CB ILE A1020 3830 4222 5589 -398 -382 -489 C
ATOM 1747 CG1 ILE A1020 -19.899 8.264 -8.822 1.00 37.69 C
ANISOU 1747 CG1 ILE A1020 4289 4189 5842 -406 -294 -547 C
ATOM 1748 CG2 ILE A1020 -21.269 9.262 -6.934 1.00 34.86 C
ANISOU 1748 CG2 ILE A1020 3618 4091 5536 -315 -381 -468 C
ATOM 1749 CD1 ILE A1020 -18.539 8.903 -8.504 1.00 34.67 C
ANISOU 1749 CD1 ILE A1020 3906 3660 5607 -184 -252 -532 C
ATOM 1750 N ALA A1021 -23.918 10.347 -8.951 1.00 46.95 N
ANISOU 1750 N ALA A1021 4774 6320 6746 -441 -550 -351 N
ATOM 1751 CA ALA A1021 -24.947 11.137 -8.316 1.00 39.37 C
ANISOU 1751 CA ALA A1021 3578 5637 5744 -302 -594 -268 C
ATOM 1752 C ALA A1021 -26.314 10.563 -8.613 1.00 41.23 C
ANISOU 1752 C ALA A1021 3631 6263 5772 -531 -653 -234 C
ATOM 1753 O ALA A1021 -27.228 10.702 -7.797 1.00 45.74 O
ANISOU 1753 O ALA A1021 4004 7093 6284 -501 -669 -180 O
ATOM 1754 CB ALA A1021 -24.827 12.590 -8.764 1.00 37.09 C
ANISOU 1754 CB ALA A1021 3240 5366 5486 -7 -612 -194 C
ATOM 1755 N ARG A1022 -26.466 9.886 -9.753 1.00 40.02 N
ANISOU 1755 N ARG A1022 3541 6180 5486 -783 -682 -265 N
ATOM 1756 CA ARG A1022 -27.767 9.318 -10.077 1.00 41.42 C
ANISOU 1756 CA ARG A1022 3537 6775 5427 -1067 -749 -232 C
ATOM 1757 C ARG A1022 -28.057 8.093 -9.232 1.00 50.84 C
ANISOU 1757 C ARG A1022 4812 7940 6563 -1379 -716 -292 C
ATOM 1758 O ARG A1022 -29.225 7.781 -8.992 1.00 48.35 O
ANISOU 1758 O ARG A1022 4285 8019 6067 -1589 -763 -246 O
ATOM 1759 CB ARG A1022 -27.852 8.991 -11.568 1.00 44.94 C
ANISOU 1759 CB ARG A1022 4049 7308 5717 -1276 -795 -251 C
ATOM 1760 CG ARG A1022 -29.231 8.536 -12.068 1.00 53.46 C
ANISOU 1760 CG ARG A1022 4904 8899 6508 -1599 -886 -202 C
ATOM 1761 CD ARG A1022 -30.365 9.330 -11.386 1.00 69.76 C
ANISOU 1761 CD ARG A1022 6567 11436 8503 -1405 -938 -67 C
ATOM 1762 NE ARG A1022 -30.104 10.774 -11.364 1.00 73.85 N
ANISOU 1762 NE ARG A1022 6990 11919 9151 -905 -932 24 N
ATOM 1763 CZ ARG A1022 -30.881 11.682 -10.783 1.00 65.09 C
ANISOU 1763 CZ ARG A1022 5602 11125 8005 -601 -947 146 C
ATOM 1764 NH1 ARG A1022 -31.995 11.319 -10.161 1.00 56.63 N
ANISOU 1764 NH1 ARG A1022 4251 10490 6775 -737 -973 202 N
ATOM 1765 NH2 ARG A1022 -30.528 12.957 -10.829 1.00 68.16 N
ANISOU 1765 NH2 ARG A1022 6013 11387 8496 -161 -924 214 N
ATOM 1766 N GLU A1023 -27.009 7.414 -8.740 1.00 54.22 N
ANISOU 1766 N GLU A1023 5543 7931 7129 -1401 -631 -383 N
ATOM 1767 CA GLU A1023 -27.182 6.238 -7.888 1.00 46.42 C
ANISOU 1767 CA GLU A1023 4703 6850 6086 -1669 -585 -436 C
ATOM 1768 C GLU A1023 -27.418 6.628 -6.435 1.00 43.73 C
ANISOU 1768 C GLU A1023 4202 6568 5845 -1496 -568 -390 C
ATOM 1769 O GLU A1023 -28.221 5.996 -5.735 1.00 45.77 O
ANISOU 1769 O GLU A1023 4398 7007 5984 -1730 -568 -380 O
ATOM 1770 CB GLU A1023 -25.968 5.308 -7.987 1.00 45.15 C
ANISOU 1770 CB GLU A1023 4953 6203 5999 -1717 -490 -536 C
ATOM 1771 CG GLU A1023 -25.615 4.757 -9.403 1.00 51.35 C
ANISOU 1771 CG GLU A1023 5977 6863 6670 -1891 -475 -601 C
ATOM 1772 CD GLU A1023 -26.819 4.324 -10.275 1.00 54.53 C
ANISOU 1772 CD GLU A1023 6306 7619 6793 -2291 -552 -599 C
ATOM 1773 OE1 GLU A1023 -27.006 4.908 -11.372 1.00 57.78 O
ANISOU 1773 OE1 GLU A1023 6593 8219 7142 -2263 -615 -571 O
ATOM 1774 OE2 GLU A1023 -27.556 3.395 -9.887 1.00 56.15 O
ANISOU 1774 OE2 GLU A1023 6588 7924 6823 -2654 -550 -622 O
ATOM 1775 N LEU A1024 -26.726 7.657 -5.959 1.00 42.60 N
ANISOU 1775 N LEU A1024 4011 6275 5900 -1115 -550 -363 N
ATOM 1776 CA LEU A1024 -27.018 8.157 -4.621 1.00 43.82 C
ANISOU 1776 CA LEU A1024 4015 6508 6126 -937 -536 -318 C
ATOM 1777 C LEU A1024 -28.401 8.810 -4.553 1.00 42.47 C
ANISOU 1777 C LEU A1024 3491 6834 5810 -892 -592 -220 C
ATOM 1778 O LEU A1024 -29.069 8.741 -3.520 1.00 39.69 O
ANISOU 1778 O LEU A1024 2996 6670 5415 -904 -578 -186 O
ATOM 1779 CB LEU A1024 -25.926 9.135 -4.176 1.00 45.34 C
ANISOU 1779 CB LEU A1024 4277 6418 6531 -579 -504 -320 C
ATOM 1780 CG LEU A1024 -24.459 8.677 -4.049 1.00 42.16 C
ANISOU 1780 CG LEU A1024 4152 5592 6276 -544 -445 -390 C
ATOM 1781 CD1 LEU A1024 -23.599 9.884 -3.685 1.00 35.09 C
ANISOU 1781 CD1 LEU A1024 3248 4546 5538 -233 -436 -372 C
ATOM 1782 CD2 LEU A1024 -24.203 7.527 -3.052 1.00 36.19 C
ANISOU 1782 CD2 LEU A1024 3559 4664 5527 -688 -391 -432 C
ATOM 1783 N ALA A1025 -28.857 9.453 -5.624 1.00 39.98 N
ANISOU 1783 N ALA A1025 3022 6765 5402 -817 -651 -162 N
ATOM 1784 CA ALA A1025 -30.220 9.967 -5.581 1.00 41.04 C
ANISOU 1784 CA ALA A1025 2797 7436 5361 -758 -700 -50 C
ATOM 1785 C ALA A1025 -31.212 8.824 -5.542 1.00 55.71 C
ANISOU 1785 C ALA A1025 4533 9636 6997 -1206 -730 -50 C
ATOM 1786 O ALA A1025 -32.184 8.867 -4.785 1.00 57.59 O
ANISOU 1786 O ALA A1025 4508 10252 7121 -1222 -732 19 O
ATOM 1787 CB ALA A1025 -30.513 10.870 -6.764 1.00 41.59 C
ANISOU 1787 CB ALA A1025 2730 7721 5351 -567 -759 30 C
ATOM 1788 N ASP A1026 -30.962 7.777 -6.329 1.00 53.40 N
ANISOU 1788 N ASP A1026 4455 9210 6623 -1588 -745 -131 N
ATOM 1789 CA ASP A1026 -31.821 6.603 -6.332 1.00 53.06 C
ANISOU 1789 CA ASP A1026 4385 9433 6341 -2096 -767 -148 C
ATOM 1790 C ASP A1026 -31.811 5.871 -4.995 1.00 51.40 C
ANISOU 1790 C ASP A1026 4288 9076 6164 -2240 -697 -185 C
ATOM 1791 O ASP A1026 -32.680 5.024 -4.764 1.00 55.88 O
ANISOU 1791 O ASP A1026 4879 9831 6522 -2564 -680 -170 O
ATOM 1792 CB ASP A1026 -31.403 5.663 -7.469 1.00 62.96 C
ANISOU 1792 CB ASP A1026 5953 10470 7499 -2455 -776 -244 C
ATOM 1793 CG ASP A1026 -31.836 6.174 -8.856 1.00 77.41 C
ANISOU 1793 CG ASP A1026 7627 12596 9188 -2438 -858 -189 C
ATOM 1794 OD1 ASP A1026 -32.499 7.238 -8.928 1.00 84.07 O
ANISOU 1794 OD1 ASP A1026 8141 13798 10003 -2121 -898 -64 O
ATOM 1795 OD2 ASP A1026 -31.513 5.510 -9.873 1.00 76.31 O
ANISOU 1795 OD2 ASP A1026 7742 12297 8956 -2705 -865 -265 O
ATOM 1796 N ALA A1027 -30.865 6.197 -4.115 1.00 52.11 N
ANISOU 1796 N ALA A1027 4540 8759 6500 -1927 -628 -217 N
ATOM 1797 CA ALA A1027 -30.689 5.573 -2.810 1.00 49.51 C
ANISOU 1797 CA ALA A1027 4349 8238 6225 -2004 -559 -249 C
ATOM 1798 C ALA A1027 -31.279 6.415 -1.689 1.00 55.69 C
ANISOU 1798 C ALA A1027 4825 9292 7041 -1732 -549 -165 C
ATOM 1799 O ALA A1027 -31.060 6.114 -0.507 1.00 60.19 O
ANISOU 1799 O ALA A1027 5490 9696 7682 -1716 -490 -183 O
ATOM 1800 CB ALA A1027 -29.199 5.330 -2.543 1.00 42.95 C
ANISOU 1800 CB ALA A1027 3896 6804 5618 -1834 -491 -332 C
ATOM 1801 N GLY A1028 -31.987 7.482 -2.040 1.00 49.10 N
ANISOU 1801 N GLY A1028 3650 8856 6149 -1484 -595 -70 N
ATOM 1802 CA GLY A1028 -32.603 8.355 -1.073 1.00 42.81 C
ANISOU 1802 CA GLY A1028 2577 8336 5352 -1173 -569 16 C
ATOM 1803 C GLY A1028 -31.718 9.446 -0.524 1.00 43.64 C
ANISOU 1803 C GLY A1028 2802 8092 5689 -696 -523 5 C
ATOM 1804 O GLY A1028 -32.100 10.069 0.467 1.00 53.14 O
ANISOU 1804 O GLY A1028 3866 9428 6898 -447 -479 55 O
ATOM 1805 N TYR A1029 -30.543 9.678 -1.097 1.00 39.98 N
ANISOU 1805 N TYR A1029 2601 7195 5396 -582 -525 -59 N
ATOM 1806 CA TYR A1029 -29.749 10.848 -0.731 1.00 45.68 C
ANISOU 1806 CA TYR A1029 3425 7637 6295 -167 -492 -59 C
ATOM 1807 C TYR A1029 -30.305 12.116 -1.376 1.00 46.22 C
ANISOU 1807 C TYR A1029 3311 7958 6294 164 -515 36 C
ATOM 1808 O TYR A1029 -30.898 12.086 -2.462 1.00 48.93 O
ANISOU 1808 O TYR A1029 3503 8588 6501 84 -572 87 O
ATOM 1809 CB TYR A1029 -28.282 10.697 -1.162 1.00 40.00 C
ANISOU 1809 CB TYR A1029 3021 6420 5756 -174 -484 -147 C
ATOM 1810 CG TYR A1029 -27.517 9.657 -0.406 1.00 42.53 C
ANISOU 1810 CG TYR A1029 3564 6433 6164 -363 -444 -225 C
ATOM 1811 CD1 TYR A1029 -27.882 8.333 -0.460 1.00 47.17 C
ANISOU 1811 CD1 TYR A1029 4211 7071 6640 -728 -442 -255 C
ATOM 1812 CD2 TYR A1029 -26.419 10.002 0.356 1.00 51.02 C
ANISOU 1812 CD2 TYR A1029 4808 7171 7407 -182 -407 -262 C
ATOM 1813 CE1 TYR A1029 -27.179 7.377 0.239 1.00 58.96 C
ANISOU 1813 CE1 TYR A1029 5949 8259 8194 -859 -393 -312 C
ATOM 1814 CE2 TYR A1029 -25.695 9.048 1.057 1.00 52.21 C
ANISOU 1814 CE2 TYR A1029 5151 7065 7620 -313 -371 -315 C
ATOM 1815 CZ TYR A1029 -26.080 7.746 0.997 1.00 60.68 C
ANISOU 1815 CZ TYR A1029 6301 8167 8587 -624 -359 -336 C
ATOM 1816 OH TYR A1029 -25.370 6.799 1.700 1.00 69.14 O
ANISOU 1816 OH TYR A1029 7603 8966 9701 -713 -312 -373 O
ATOM 1817 N GLU A1030 -30.109 13.241 -0.693 1.00 44.67 N
ANISOU 1817 N GLU A1030 3156 7646 6171 542 -465 63 N
ATOM 1818 CA GLU A1030 -30.292 14.553 -1.307 1.00 41.87 C
ANISOU 1818 CA GLU A1030 2773 7359 5777 914 -464 142 C
ATOM 1819 C GLU A1030 -28.927 14.983 -1.854 1.00 44.08 C
ANISOU 1819 C GLU A1030 3366 7155 6226 963 -466 73 C
ATOM 1820 O GLU A1030 -28.054 15.430 -1.106 1.00 43.95 O
ANISOU 1820 O GLU A1030 3566 6791 6342 1075 -419 20 O
ATOM 1821 CB GLU A1030 -30.860 15.529 -0.290 1.00 40.76 C
ANISOU 1821 CB GLU A1030 2567 7338 5583 1291 -392 207 C
ATOM 1822 CG GLU A1030 -31.119 16.919 -0.806 1.00 57.76 C
ANISOU 1822 CG GLU A1030 4819 9466 7663 1678 -358 292 C
ATOM 1823 CD GLU A1030 -31.470 17.901 0.322 1.00 67.59 C
ANISOU 1823 CD GLU A1030 6199 10623 8861 1991 -252 319 C
ATOM 1824 OE1 GLU A1030 -31.634 19.105 0.031 1.00 66.78 O
ANISOU 1824 OE1 GLU A1030 6265 10426 8684 2298 -203 378 O
ATOM 1825 OE2 GLU A1030 -31.580 17.467 1.497 1.00 68.69 O
ANISOU 1825 OE2 GLU A1030 6293 10784 9022 1923 -213 281 O
ATOM 1826 N VAL A1031 -28.724 14.817 -3.186 1.00 48.59 N
ANISOU 1826 N VAL A1031 3955 7731 6775 847 -521 76 N
ATOM 1827 CA VAL A1031 -27.399 14.973 -3.783 1.00 46.66 C
ANISOU 1827 CA VAL A1031 3980 7072 6677 814 -520 6 C
ATOM 1828 C VAL A1031 -27.195 16.413 -4.232 1.00 41.91 C
ANISOU 1828 C VAL A1031 3491 6362 6069 1150 -503 67 C
ATOM 1829 O VAL A1031 -28.124 17.093 -4.668 1.00 47.02 O
ANISOU 1829 O VAL A1031 4001 7292 6572 1375 -513 172 O
ATOM 1830 CB VAL A1031 -27.153 14.004 -4.965 1.00 36.80 C
ANISOU 1830 CB VAL A1031 2749 5830 5404 507 -570 -36 C
ATOM 1831 CG1 VAL A1031 -25.669 13.859 -5.154 1.00 35.34 C
ANISOU 1831 CG1 VAL A1031 2829 5214 5384 445 -543 -123 C
ATOM 1832 CG2 VAL A1031 -27.764 12.634 -4.728 1.00 47.87 C
ANISOU 1832 CG2 VAL A1031 4041 7429 6720 165 -589 -68 C
ATOM 1833 N ASP A1032 -25.939 16.854 -4.168 1.00 37.30 N
ANISOU 1833 N ASP A1032 3172 5377 5624 1172 -474 6 N
ATOM 1834 CA ASP A1032 -25.527 18.228 -4.467 1.00 45.27 C
ANISOU 1834 CA ASP A1032 4384 6186 6630 1433 -443 45 C
ATOM 1835 C ASP A1032 -24.253 18.170 -5.326 1.00 34.35 C
ANISOU 1835 C ASP A1032 3185 4521 5344 1268 -455 -11 C
ATOM 1836 O ASP A1032 -23.167 18.001 -4.790 1.00 32.86 O
ANISOU 1836 O ASP A1032 3135 4073 5278 1149 -432 -87 O
ATOM 1837 CB ASP A1032 -25.298 18.954 -3.135 1.00 47.35 C
ANISOU 1837 CB ASP A1032 4801 6259 6930 1604 -376 25 C
ATOM 1838 CG ASP A1032 -25.370 20.469 -3.225 1.00 50.46 C
ANISOU 1838 CG ASP A1032 5419 6513 7240 1933 -323 89 C
ATOM 1839 OD1 ASP A1032 -25.000 21.058 -4.264 1.00 54.17 O
ANISOU 1839 OD1 ASP A1032 6030 6868 7685 1976 -332 122 O
ATOM 1840 OD2 ASP A1032 -25.758 21.073 -2.196 1.00 51.62 O
ANISOU 1840 OD2 ASP A1032 5642 6635 7337 2147 -261 104 O
ATOM 1841 N SER A1033 -24.379 18.316 -6.650 1.00 46.94 N
ANISOU 1841 N SER A1033 4765 6199 6871 1266 -489 34 N
ATOM 1842 CA SER A1033 -23.219 18.391 -7.558 1.00 44.32 C
ANISOU 1842 CA SER A1033 4606 5629 6606 1140 -489 -6 C
ATOM 1843 C SER A1033 -22.754 19.835 -7.764 1.00 41.42 C
ANISOU 1843 C SER A1033 4484 5039 6213 1339 -450 40 C
ATOM 1844 O SER A1033 -23.549 20.702 -8.133 1.00 45.31 O
ANISOU 1844 O SER A1033 5000 5636 6579 1590 -447 138 O
ATOM 1845 CB SER A1033 -23.537 17.792 -8.931 1.00 40.18 C
ANISOU 1845 CB SER A1033 3975 5289 6003 1009 -541 14 C
ATOM 1846 OG SER A1033 -23.302 16.408 -9.004 1.00 37.78 O
ANISOU 1846 OG SER A1033 3601 5012 5743 729 -555 -67 O
ATOM 1847 N ARG A1034 -21.461 20.083 -7.563 1.00 37.23 N
ANISOU 1847 N ARG A1034 4148 4217 5780 1221 -418 -21 N
ATOM 1848 CA ARG A1034 -20.875 21.382 -7.865 1.00 36.72 C
ANISOU 1848 CA ARG A1034 4363 3916 5672 1314 -379 12 C
ATOM 1849 C ARG A1034 -19.576 21.188 -8.630 1.00 35.94 C
ANISOU 1849 C ARG A1034 4345 3674 5636 1080 -376 -33 C
ATOM 1850 O ARG A1034 -18.686 20.459 -8.184 1.00 37.32 O
ANISOU 1850 O ARG A1034 4465 3799 5917 888 -372 -108 O
ATOM 1851 CB ARG A1034 -20.586 22.195 -6.610 1.00 35.51 C
ANISOU 1851 CB ARG A1034 4413 3555 5524 1394 -327 -11 C
ATOM 1852 CG ARG A1034 -21.393 21.817 -5.417 1.00 37.55 C
ANISOU 1852 CG ARG A1034 4531 3945 5790 1499 -322 -23 C
ATOM 1853 CD ARG A1034 -22.047 23.053 -4.858 1.00 40.78 C
ANISOU 1853 CD ARG A1034 5150 4269 6077 1806 -261 36 C
ATOM 1854 NE ARG A1034 -22.860 22.736 -3.697 1.00 48.32 N
ANISOU 1854 NE ARG A1034 5961 5375 7022 1927 -244 30 N
ATOM 1855 CZ ARG A1034 -22.628 23.180 -2.469 1.00 45.53 C
ANISOU 1855 CZ ARG A1034 5779 4851 6668 1967 -193 -16 C
ATOM 1856 NH1 ARG A1034 -21.595 24.002 -2.233 1.00 37.16 N
ANISOU 1856 NH1 ARG A1034 5056 3459 5604 1869 -158 -61 N
ATOM 1857 NH2 ARG A1034 -23.445 22.801 -1.482 1.00 47.28 N
ANISOU 1857 NH2 ARG A1034 5838 5252 6874 2078 -176 -15 N
ATOM 1858 N ASP A1035 -19.456 21.863 -9.764 1.00 41.44 N
ANISOU 1858 N ASP A1035 5173 4320 6252 1117 -372 23 N
ATOM 1859 CA ASP A1035 -18.162 21.924 -10.425 1.00 43.36 C
ANISOU 1859 CA ASP A1035 5523 4422 6531 907 -351 -9 C
ATOM 1860 C ASP A1035 -17.177 22.665 -9.523 1.00 36.17 C
ANISOU 1860 C ASP A1035 4818 3282 5642 811 -307 -44 C
ATOM 1861 O ASP A1035 -17.529 23.662 -8.881 1.00 37.36 O
ANISOU 1861 O ASP A1035 5180 3293 5722 950 -279 -16 O
ATOM 1862 CB ASP A1035 -18.318 22.604 -11.792 1.00 44.06 C
ANISOU 1862 CB ASP A1035 5737 4500 6504 972 -351 70 C
ATOM 1863 CG ASP A1035 -17.063 22.560 -12.604 1.00 59.68 C
ANISOU 1863 CG ASP A1035 7785 6388 8502 746 -326 43 C
ATOM 1864 OD1 ASP A1035 -15.991 22.819 -12.025 1.00 63.57 O
ANISOU 1864 OD1 ASP A1035 8374 6740 9041 588 -290 -1 O
ATOM 1865 OD2 ASP A1035 -17.138 22.272 -13.822 1.00 71.12 O
ANISOU 1865 OD2 ASP A1035 9184 7934 9904 716 -341 69 O
ATOM 1866 N ALA A1036 -15.949 22.145 -9.426 1.00 35.01 N
ANISOU 1866 N ALA A1036 4611 3117 5575 575 -298 -103 N
ATOM 1867 CA ALA A1036 -14.955 22.805 -8.575 1.00 36.10 C
ANISOU 1867 CA ALA A1036 4908 3099 5708 428 -269 -133 C
ATOM 1868 C ALA A1036 -14.728 24.254 -9.007 1.00 41.91 C
ANISOU 1868 C ALA A1036 5990 3625 6309 409 -230 -84 C
ATOM 1869 O ALA A1036 -14.494 25.128 -8.161 1.00 38.25 O
ANISOU 1869 O ALA A1036 5768 2983 5781 366 -203 -96 O
ATOM 1870 CB ALA A1036 -13.639 22.035 -8.575 1.00 34.94 C
ANISOU 1870 CB ALA A1036 4600 3041 5635 196 -265 -178 C
ATOM 1871 N ALA A1037 -14.839 24.520 -10.315 1.00 38.27 N
ANISOU 1871 N ALA A1037 5590 3166 5783 438 -224 -28 N
ATOM 1872 CA ALA A1037 -14.725 25.848 -10.879 1.00 40.06 C
ANISOU 1872 CA ALA A1037 6178 3181 5862 441 -181 35 C
ATOM 1873 C ALA A1037 -15.633 26.872 -10.219 1.00 45.38 C
ANISOU 1873 C ALA A1037 7148 3667 6429 692 -150 75 C
ATOM 1874 O ALA A1037 -15.343 28.076 -10.270 1.00 50.17 O
ANISOU 1874 O ALA A1037 8157 4011 6894 656 -94 108 O
ATOM 1875 CB ALA A1037 -15.038 25.771 -12.358 1.00 41.08 C
ANISOU 1875 CB ALA A1037 6274 3392 5941 512 -190 99 C
ATOM 1876 N SER A1038 -16.715 26.440 -9.590 1.00 48.28 N
ANISOU 1876 N SER A1038 7350 4155 6838 945 -172 77 N
ATOM 1877 CA SER A1038 -17.738 27.376 -9.166 1.00 55.23 C
ANISOU 1877 CA SER A1038 8482 4910 7591 1273 -129 140 C
ATOM 1878 C SER A1038 -17.782 27.602 -7.657 1.00 52.14 C
ANISOU 1878 C SER A1038 8198 4406 7207 1297 -98 80 C
ATOM 1879 O SER A1038 -18.590 28.429 -7.205 1.00 50.10 O
ANISOU 1879 O SER A1038 8191 4021 6825 1593 -40 127 O
ATOM 1880 CB SER A1038 -19.097 26.898 -9.665 1.00 59.50 C
ANISOU 1880 CB SER A1038 8764 5725 8118 1588 -168 215 C
ATOM 1881 OG SER A1038 -19.398 25.660 -9.062 1.00 58.79 O
ANISOU 1881 OG SER A1038 8289 5886 8164 1534 -220 154 O
ATOM 1882 N VAL A1039 -16.920 26.937 -6.882 1.00 48.26 N
ANISOU 1882 N VAL A1039 7547 3955 6834 1015 -126 -15 N
ATOM 1883 CA VAL A1039 -16.952 26.989 -5.422 1.00 43.91 C
ANISOU 1883 CA VAL A1039 7049 3340 6295 1015 -110 -77 C
ATOM 1884 C VAL A1039 -15.726 27.717 -4.844 1.00 48.78 C
ANISOU 1884 C VAL A1039 7970 3723 6842 693 -81 -135 C
ATOM 1885 O VAL A1039 -14.762 28.051 -5.533 1.00 47.41 O
ANISOU 1885 O VAL A1039 7909 3478 6626 430 -79 -131 O
ATOM 1886 CB VAL A1039 -17.059 25.590 -4.801 1.00 44.11 C
ANISOU 1886 CB VAL A1039 6644 3631 6486 966 -169 -130 C
ATOM 1887 CG1 VAL A1039 -18.415 24.949 -5.127 1.00 51.09 C
ANISOU 1887 CG1 VAL A1039 7264 4754 7394 1248 -193 -78 C
ATOM 1888 CG2 VAL A1039 -15.887 24.734 -5.249 1.00 35.95 C
ANISOU 1888 CG2 VAL A1039 5390 2709 5562 657 -214 -171 C
ATOM 1889 N GLU A1040 -15.803 27.985 -3.549 1.00 48.73 N
ANISOU 1889 N GLU A1040 8099 3616 6800 700 -58 -187 N
ATOM 1890 CA GLU A1040 -14.695 28.450 -2.737 1.00 42.17 C
ANISOU 1890 CA GLU A1040 7481 2641 5902 354 -51 -257 C
ATOM 1891 C GLU A1040 -14.570 27.462 -1.587 1.00 47.87 C
ANISOU 1891 C GLU A1040 7879 3561 6749 293 -103 -319 C
ATOM 1892 O GLU A1040 -15.502 26.710 -1.289 1.00 58.62 O
ANISOU 1892 O GLU A1040 8984 5081 8207 548 -118 -310 O
ATOM 1893 CB GLU A1040 -14.918 29.883 -2.237 1.00 44.68 C
ANISOU 1893 CB GLU A1040 8387 2589 6001 415 41 -261 C
ATOM 1894 CG GLU A1040 -15.093 30.890 -3.355 1.00 59.21 C
ANISOU 1894 CG GLU A1040 10533 4270 7693 500 102 -181 C
ATOM 1895 CD GLU A1040 -13.784 31.549 -3.767 1.00 65.84 C
ANISOU 1895 CD GLU A1040 11611 4988 8416 48 109 -198 C
ATOM 1896 OE1 GLU A1040 -12.980 31.852 -2.863 1.00 69.77 O
ANISOU 1896 OE1 GLU A1040 12222 5453 8834 -273 106 -266 O
ATOM 1897 OE2 GLU A1040 -13.560 31.763 -4.981 1.00 63.82 O
ANISOU 1897 OE2 GLU A1040 11416 4702 8130 2 115 -138 O
ATOM 1898 N ALA A1041 -13.400 27.420 -0.961 1.00 40.67 N
ANISOU 1898 N ALA A1041 6959 2674 5820 -63 -134 -374 N
ATOM 1899 CA ALA A1041 -13.145 26.284 -0.096 1.00 42.03 C
ANISOU 1899 CA ALA A1041 6759 3088 6124 -120 -195 -412 C
ATOM 1900 C ALA A1041 -13.702 26.466 1.316 1.00 44.62 C
ANISOU 1900 C ALA A1041 7213 3335 6407 -12 -176 -459 C
ATOM 1901 O ALA A1041 -13.913 25.476 2.015 1.00 50.71 O
ANISOU 1901 O ALA A1041 7684 4292 7292 54 -215 -475 O
ATOM 1902 CB ALA A1041 -11.649 25.999 -0.054 1.00 50.01 C
ANISOU 1902 CB ALA A1041 7616 4254 7132 -507 -245 -428 C
ATOM 1903 N GLY A1042 -14.000 27.688 1.740 1.00 44.57 N
ANISOU 1903 N GLY A1042 7670 3040 6226 27 -106 -478 N
ATOM 1904 CA GLY A1042 -14.366 27.898 3.126 1.00 39.91 C
ANISOU 1904 CA GLY A1042 7229 2368 5567 89 -80 -533 C
ATOM 1905 C GLY A1042 -15.740 27.340 3.427 1.00 40.23 C
ANISOU 1905 C GLY A1042 7077 2515 5692 505 -54 -507 C
ATOM 1906 O GLY A1042 -16.727 27.685 2.767 1.00 47.14 O
ANISOU 1906 O GLY A1042 8034 3339 6539 829 1 -448 O
ATOM 1907 N GLY A1043 -15.814 26.495 4.453 1.00 41.40 N
ANISOU 1907 N GLY A1043 6969 2837 5924 493 -93 -542 N
ATOM 1908 CA GLY A1043 -17.051 25.877 4.889 1.00 37.34 C
ANISOU 1908 CA GLY A1043 6244 2468 5475 819 -71 -520 C
ATOM 1909 C GLY A1043 -17.723 24.959 3.888 1.00 35.93 C
ANISOU 1909 C GLY A1043 5697 2522 5434 988 -102 -455 C
ATOM 1910 O GLY A1043 -18.885 24.583 4.098 1.00 36.65 O
ANISOU 1910 O GLY A1043 5630 2756 5540 1256 -77 -423 O
ATOM 1911 N LEU A1044 -17.022 24.571 2.816 1.00 35.58 N
ANISOU 1911 N LEU A1044 5508 2541 5470 819 -155 -434 N
ATOM 1912 CA LEU A1044 -17.668 23.899 1.694 1.00 36.58 C
ANISOU 1912 CA LEU A1044 5374 2843 5682 962 -176 -375 C
ATOM 1913 C LEU A1044 -18.282 22.578 2.138 1.00 38.18 C
ANISOU 1913 C LEU A1044 5217 3295 5995 1020 -210 -375 C
ATOM 1914 O LEU A1044 -19.369 22.200 1.687 1.00 39.62 O
ANISOU 1914 O LEU A1044 5233 3638 6183 1212 -205 -328 O
ATOM 1915 CB LEU A1044 -16.651 23.705 0.557 1.00 38.02 C
ANISOU 1915 CB LEU A1044 5495 3034 5915 741 -216 -365 C
ATOM 1916 CG LEU A1044 -17.034 23.056 -0.790 1.00 40.06 C
ANISOU 1916 CG LEU A1044 5534 3444 6243 813 -241 -315 C
ATOM 1917 CD1 LEU A1044 -18.125 23.823 -1.559 1.00 34.32 C
ANISOU 1917 CD1 LEU A1044 4940 2682 5417 1090 -202 -245 C
ATOM 1918 CD2 LEU A1044 -15.811 22.846 -1.685 1.00 40.03 C
ANISOU 1918 CD2 LEU A1044 5484 3446 6279 567 -268 -319 C
ATOM 1919 N PHE A1045 -17.629 21.888 3.061 1.00 38.60 N
ANISOU 1919 N PHE A1045 5160 3396 6110 847 -244 -422 N
ATOM 1920 CA PHE A1045 -18.070 20.549 3.425 1.00 37.55 C
ANISOU 1920 CA PHE A1045 4728 3467 6073 859 -272 -419 C
ATOM 1921 C PHE A1045 -19.135 20.552 4.507 1.00 40.57 C
ANISOU 1921 C PHE A1045 5097 3911 6405 1031 -235 -421 C
ATOM 1922 O PHE A1045 -19.728 19.499 4.762 1.00 46.78 O
ANISOU 1922 O PHE A1045 5653 4878 7243 1045 -249 -410 O
ATOM 1923 CB PHE A1045 -16.873 19.697 3.881 1.00 31.55 C
ANISOU 1923 CB PHE A1045 3850 2747 5391 634 -320 -449 C
ATOM 1924 CG PHE A1045 -15.903 19.380 2.778 1.00 35.20 C
ANISOU 1924 CG PHE A1045 4240 3229 5904 496 -347 -435 C
ATOM 1925 CD1 PHE A1045 -16.075 19.905 1.504 1.00 31.86 C
ANISOU 1925 CD1 PHE A1045 3883 2761 5460 537 -334 -409 C
ATOM 1926 CD2 PHE A1045 -14.847 18.540 2.997 1.00 37.01 C
ANISOU 1926 CD2 PHE A1045 4331 3541 6189 355 -379 -439 C
ATOM 1927 CE1 PHE A1045 -15.222 19.619 0.490 1.00 30.67 C
ANISOU 1927 CE1 PHE A1045 3668 2640 5346 418 -348 -397 C
ATOM 1928 CE2 PHE A1045 -13.958 18.261 1.955 1.00 44.42 C
ANISOU 1928 CE2 PHE A1045 5197 4524 7158 262 -386 -421 C
ATOM 1929 CZ PHE A1045 -14.159 18.797 0.702 1.00 36.31 C
ANISOU 1929 CZ PHE A1045 4239 3444 6112 284 -370 -405 C
ATOM 1930 N GLU A1046 -19.398 21.710 5.116 1.00 34.25 N
ANISOU 1930 N GLU A1046 4564 2963 5488 1156 -177 -434 N
ATOM 1931 CA GLU A1046 -20.217 21.791 6.312 1.00 33.11 C
ANISOU 1931 CA GLU A1046 4439 2863 5277 1312 -128 -444 C
ATOM 1932 C GLU A1046 -21.662 21.415 6.022 1.00 43.21 C
ANISOU 1932 C GLU A1046 5500 4383 6535 1556 -98 -381 C
ATOM 1933 O GLU A1046 -22.280 21.899 5.062 1.00 40.32 O
ANISOU 1933 O GLU A1046 5144 4061 6116 1738 -75 -322 O
ATOM 1934 CB GLU A1046 -20.147 23.193 6.892 1.00 41.87 C
ANISOU 1934 CB GLU A1046 5949 3726 6235 1409 -55 -474 C
ATOM 1935 CG GLU A1046 -18.759 23.608 7.356 1.00 46.86 C
ANISOU 1935 CG GLU A1046 6801 4161 6842 1108 -88 -541 C
ATOM 1936 CD GLU A1046 -18.800 24.899 8.164 1.00 71.12 C
ANISOU 1936 CD GLU A1046 10316 6976 9729 1170 -6 -587 C
ATOM 1937 OE1 GLU A1046 -18.082 25.860 7.806 1.00 75.71 O
ANISOU 1937 OE1 GLU A1046 11230 7323 10213 1028 8 -609 O
ATOM 1938 OE2 GLU A1046 -19.574 24.958 9.154 1.00 83.44 O
ANISOU 1938 OE2 GLU A1046 11918 8564 11223 1356 54 -600 O
ATOM 1939 N GLY A1047 -22.207 20.543 6.872 1.00 41.24 N
ANISOU 1939 N GLY A1047 5045 4317 6308 1547 -98 -383 N
ATOM 1940 CA GLY A1047 -23.563 20.075 6.726 1.00 38.62 C
ANISOU 1940 CA GLY A1047 4462 4279 5932 1712 -74 -321 C
ATOM 1941 C GLY A1047 -23.709 18.727 6.040 1.00 51.04 C
ANISOU 1941 C GLY A1047 5741 6056 7595 1523 -142 -301 C
ATOM 1942 O GLY A1047 -24.805 18.149 6.075 1.00 58.03 O
ANISOU 1942 O GLY A1047 6394 7225 8429 1569 -132 -254 O
ATOM 1943 N PHE A1048 -22.656 18.198 5.427 1.00 30.84 N
ANISOU 1943 N PHE A1048 3196 3377 5146 1303 -202 -332 N
ATOM 1944 CA PHE A1048 -22.800 17.007 4.601 1.00 45.37 C
ANISOU 1944 CA PHE A1048 4832 5364 7041 1145 -249 -316 C
ATOM 1945 C PHE A1048 -22.383 15.746 5.358 1.00 38.14 C
ANISOU 1945 C PHE A1048 3850 4450 6191 945 -269 -349 C
ATOM 1946 O PHE A1048 -21.415 15.753 6.130 1.00 39.25 O
ANISOU 1946 O PHE A1048 4101 4433 6379 881 -275 -386 O
ATOM 1947 CB PHE A1048 -22.003 17.156 3.300 1.00 29.46 C
ANISOU 1947 CB PHE A1048 2882 3233 5080 1071 -285 -319 C
ATOM 1948 CG PHE A1048 -22.491 18.259 2.427 1.00 34.81 C
ANISOU 1948 CG PHE A1048 3629 3919 5679 1263 -267 -271 C
ATOM 1949 CD1 PHE A1048 -23.595 18.071 1.593 1.00 40.34 C
ANISOU 1949 CD1 PHE A1048 4151 4871 6307 1349 -278 -208 C
ATOM 1950 CD2 PHE A1048 -21.884 19.501 2.446 1.00 35.63 C
ANISOU 1950 CD2 PHE A1048 3992 3793 5752 1352 -239 -281 C
ATOM 1951 CE1 PHE A1048 -24.078 19.109 0.766 1.00 40.89 C
ANISOU 1951 CE1 PHE A1048 4285 4970 6283 1571 -261 -143 C
ATOM 1952 CE2 PHE A1048 -22.367 20.550 1.622 1.00 33.97 C
ANISOU 1952 CE2 PHE A1048 3898 3562 5447 1562 -211 -223 C
ATOM 1953 CZ PHE A1048 -23.456 20.340 0.783 1.00 32.88 C
ANISOU 1953 CZ PHE A1048 3564 3684 5246 1693 -223 -149 C
ATOM 1954 N ASP A1049 -23.144 14.667 5.136 1.00 32.46 N
ANISOU 1954 N ASP A1049 2961 3923 5450 840 -277 -328 N
ATOM 1955 CA ASP A1049 -22.791 13.337 5.639 1.00 34.44 C
ANISOU 1955 CA ASP A1049 3198 4147 5742 644 -287 -349 C
ATOM 1956 C ASP A1049 -21.661 12.718 4.841 1.00 34.10 C
ANISOU 1956 C ASP A1049 3235 3941 5781 525 -313 -372 C
ATOM 1957 O ASP A1049 -20.816 12.019 5.410 1.00 45.14 O
ANISOU 1957 O ASP A1049 4703 5222 7227 452 -313 -389 O
ATOM 1958 CB ASP A1049 -24.008 12.399 5.607 1.00 35.05 C
ANISOU 1958 CB ASP A1049 3116 4470 5730 523 -278 -320 C
ATOM 1959 CG ASP A1049 -25.234 13.006 6.297 1.00 54.35 C
ANISOU 1959 CG ASP A1049 5424 7160 8066 667 -241 -279 C
ATOM 1960 OD1 ASP A1049 -25.115 13.409 7.477 1.00 60.03 O
ANISOU 1960 OD1 ASP A1049 6205 7820 8785 765 -207 -292 O
ATOM 1961 OD2 ASP A1049 -26.305 13.103 5.654 1.00 61.28 O
ANISOU 1961 OD2 ASP A1049 6127 8313 8844 693 -243 -229 O
ATOM 1962 N LEU A1050 -21.619 13.002 3.539 1.00 28.61 N
ANISOU 1962 N LEU A1050 2532 3251 5089 532 -330 -366 N
ATOM 1963 CA LEU A1050 -20.709 12.380 2.600 1.00 37.29 C
ANISOU 1963 CA LEU A1050 3693 4235 6241 433 -341 -384 C
ATOM 1964 C LEU A1050 -20.254 13.419 1.584 1.00 38.23 C
ANISOU 1964 C LEU A1050 3851 4296 6377 513 -355 -378 C
ATOM 1965 O LEU A1050 -21.074 14.080 0.941 1.00 41.80 O
ANISOU 1965 O LEU A1050 4254 4858 6771 592 -363 -350 O
ATOM 1966 CB LEU A1050 -21.383 11.193 1.899 1.00 35.26 C
ANISOU 1966 CB LEU A1050 3398 4075 5926 273 -340 -384 C
ATOM 1967 CG LEU A1050 -20.676 10.430 0.773 1.00 37.20 C
ANISOU 1967 CG LEU A1050 3737 4211 6188 176 -333 -406 C
ATOM 1968 CD1 LEU A1050 -19.420 9.733 1.252 1.00 31.02 C
ANISOU 1968 CD1 LEU A1050 3078 3242 5467 183 -302 -422 C
ATOM 1969 CD2 LEU A1050 -21.609 9.413 0.214 1.00 36.15 C
ANISOU 1969 CD2 LEU A1050 3597 4189 5950 -14 -331 -412 C
ATOM 1970 N VAL A1051 -18.947 13.543 1.436 1.00 39.01 N
ANISOU 1970 N VAL A1051 4034 4250 6539 494 -355 -395 N
ATOM 1971 CA VAL A1051 -18.328 14.334 0.386 1.00 37.89 C
ANISOU 1971 CA VAL A1051 3945 4045 6406 515 -362 -390 C
ATOM 1972 C VAL A1051 -17.614 13.364 -0.555 1.00 34.34 C
ANISOU 1972 C VAL A1051 3497 3567 5984 426 -351 -401 C
ATOM 1973 O VAL A1051 -16.810 12.529 -0.121 1.00 34.75 O
ANISOU 1973 O VAL A1051 3563 3571 6068 393 -332 -410 O
ATOM 1974 CB VAL A1051 -17.354 15.363 0.986 1.00 30.60 C
ANISOU 1974 CB VAL A1051 3117 3012 5497 533 -364 -397 C
ATOM 1975 CG1 VAL A1051 -16.766 16.301 -0.065 1.00 35.60 C
ANISOU 1975 CG1 VAL A1051 3834 3577 6115 522 -364 -387 C
ATOM 1976 CG2 VAL A1051 -18.054 16.132 2.032 1.00 28.97 C
ANISOU 1976 CG2 VAL A1051 2959 2803 5246 624 -357 -398 C
ATOM 1977 N LEU A1052 -17.905 13.456 -1.832 1.00 32.05 N
ANISOU 1977 N LEU A1052 3205 3310 5663 410 -355 -394 N
ATOM 1978 CA LEU A1052 -17.069 12.802 -2.827 1.00 33.86 C
ANISOU 1978 CA LEU A1052 3472 3490 5904 351 -331 -408 C
ATOM 1979 C LEU A1052 -16.339 13.884 -3.613 1.00 29.06 C
ANISOU 1979 C LEU A1052 2899 2843 5300 375 -333 -392 C
ATOM 1980 O LEU A1052 -16.967 14.847 -4.059 1.00 31.75 O
ANISOU 1980 O LEU A1052 3258 3206 5601 421 -354 -369 O
ATOM 1981 CB LEU A1052 -17.910 11.913 -3.747 1.00 34.80 C
ANISOU 1981 CB LEU A1052 3591 3675 5958 266 -328 -420 C
ATOM 1982 CG LEU A1052 -18.868 10.923 -3.070 1.00 35.52 C
ANISOU 1982 CG LEU A1052 3665 3829 6003 180 -328 -432 C
ATOM 1983 CD1 LEU A1052 -19.657 10.176 -4.093 1.00 34.90 C
ANISOU 1983 CD1 LEU A1052 3604 3833 5823 36 -333 -446 C
ATOM 1984 CD2 LEU A1052 -18.101 9.938 -2.252 1.00 41.54 C
ANISOU 1984 CD2 LEU A1052 4512 4470 6801 171 -285 -449 C
ATOM 1985 N LEU A1053 -15.023 13.749 -3.740 1.00 27.61 N
ANISOU 1985 N LEU A1053 2727 2617 5145 351 -305 -393 N
ATOM 1986 CA LEU A1053 -14.196 14.649 -4.545 1.00 37.71 C
ANISOU 1986 CA LEU A1053 4037 3880 6410 324 -298 -376 C
ATOM 1987 C LEU A1053 -13.621 13.925 -5.760 1.00 36.94 C
ANISOU 1987 C LEU A1053 3937 3801 6296 303 -254 -381 C
ATOM 1988 O LEU A1053 -12.797 13.020 -5.591 1.00 38.77 O
ANISOU 1988 O LEU A1053 4140 4049 6540 324 -211 -384 O
ATOM 1989 CB LEU A1053 -13.041 15.200 -3.728 1.00 40.69 C
ANISOU 1989 CB LEU A1053 4402 4259 6800 282 -299 -365 C
ATOM 1990 CG LEU A1053 -13.381 15.791 -2.395 1.00 37.80 C
ANISOU 1990 CG LEU A1053 4067 3861 6435 289 -331 -370 C
ATOM 1991 CD1 LEU A1053 -12.043 16.094 -1.774 1.00 41.68 C
ANISOU 1991 CD1 LEU A1053 4526 4400 6912 197 -334 -358 C
ATOM 1992 CD2 LEU A1053 -14.155 17.036 -2.660 1.00 46.73 C
ANISOU 1992 CD2 LEU A1053 5322 4914 7518 317 -344 -364 C
ATOM 1993 N GLY A1054 -14.002 14.368 -6.961 1.00 35.63 N
ANISOU 1993 N GLY A1054 3814 3638 6087 284 -259 -373 N
ATOM 1994 CA GLY A1054 -13.492 13.818 -8.219 1.00 37.95 C
ANISOU 1994 CA GLY A1054 4128 3947 6346 259 -212 -381 C
ATOM 1995 C GLY A1054 -12.532 14.759 -8.941 1.00 36.85 C
ANISOU 1995 C GLY A1054 4001 3820 6181 217 -192 -351 C
ATOM 1996 O GLY A1054 -12.806 15.951 -9.098 1.00 35.71 O
ANISOU 1996 O GLY A1054 3915 3643 6012 193 -225 -324 O
ATOM 1997 N CYS A1055 -11.418 14.202 -9.400 1.00 39.03 N
ANISOU 1997 N CYS A1055 4239 4145 6444 216 -127 -349 N
ATOM 1998 CA CYS A1055 -10.384 15.009 -10.044 1.00 40.30 C
ANISOU 1998 CA CYS A1055 4383 4366 6565 145 -98 -315 C
ATOM 1999 C CYS A1055 -9.650 14.176 -11.082 1.00 42.86 C
ANISOU 1999 C CYS A1055 4684 4757 6842 183 -12 -318 C
ATOM 2000 O CYS A1055 -9.228 13.051 -10.779 1.00 49.44 O
ANISOU 2000 O CYS A1055 5482 5621 7682 287 44 -331 O
ATOM 2001 CB CYS A1055 -9.374 15.537 -9.016 1.00 41.53 C
ANISOU 2001 CB CYS A1055 4451 4600 6730 85 -106 -286 C
ATOM 2002 SG CYS A1055 -8.447 17.023 -9.567 1.00 52.56 S
ANISOU 2002 SG CYS A1055 5879 6048 8042 -110 -101 -240 S
ATOM 2003 N SER A1056 -9.461 14.741 -12.283 1.00 38.54 N
ANISOU 2003 N SER A1056 4182 4228 6233 119 9 -303 N
ATOM 2004 CA SER A1056 -8.584 14.149 -13.292 1.00 39.60 C
ANISOU 2004 CA SER A1056 4293 4451 6304 152 105 -299 C
ATOM 2005 C SER A1056 -7.119 14.573 -13.093 1.00 45.36 C
ANISOU 2005 C SER A1056 4871 5363 7000 107 154 -245 C
ATOM 2006 O SER A1056 -6.818 15.618 -12.493 1.00 42.56 O
ANISOU 2006 O SER A1056 4478 5045 6648 -27 103 -212 O
ATOM 2007 CB SER A1056 -9.062 14.529 -14.680 1.00 40.14 C
ANISOU 2007 CB SER A1056 4470 4479 6304 93 107 -303 C
ATOM 2008 OG SER A1056 -9.271 15.928 -14.794 1.00 44.93 O
ANISOU 2008 OG SER A1056 5123 5054 6894 -19 47 -262 O
ATOM 2009 N THR A1057 -6.204 13.734 -13.578 1.00 41.65 N
ANISOU 2009 N THR A1057 4324 5025 6476 217 260 -233 N
ATOM 2010 CA THR A1057 -4.782 13.917 -13.319 1.00 44.05 C
ANISOU 2010 CA THR A1057 4422 5590 6724 206 314 -167 C
ATOM 2011 C THR A1057 -4.122 14.481 -14.558 1.00 47.35 C
ANISOU 2011 C THR A1057 4815 6133 7043 101 377 -134 C
ATOM 2012 O THR A1057 -4.444 14.072 -15.668 1.00 52.03 O
ANISOU 2012 O THR A1057 5526 6646 7597 162 433 -166 O
ATOM 2013 CB THR A1057 -4.091 12.618 -12.936 1.00 44.75 C
ANISOU 2013 CB THR A1057 4411 5800 6791 456 408 -149 C
ATOM 2014 OG1 THR A1057 -4.830 12.001 -11.889 1.00 55.19 O
ANISOU 2014 OG1 THR A1057 5807 6965 8196 548 356 -183 O
ATOM 2015 CG2 THR A1057 -2.700 12.920 -12.446 1.00 42.18 C
ANISOU 2015 CG2 THR A1057 3812 5816 6397 440 437 -60 C
ATOM 2016 N TRP A1058 -3.200 15.419 -14.353 1.00 45.09 N
ANISOU 2016 N TRP A1058 4384 6051 6697 -85 367 -72 N
ATOM 2017 CA TRP A1058 -2.566 16.189 -15.421 1.00 46.02 C
ANISOU 2017 CA TRP A1058 4484 6297 6703 -259 416 -31 C
ATOM 2018 C TRP A1058 -1.070 16.347 -15.117 1.00 51.12 C
ANISOU 2018 C TRP A1058 4841 7340 7242 -345 471 52 C
ATOM 2019 O TRP A1058 -0.448 15.585 -14.371 1.00 51.34 O
ANISOU 2019 O TRP A1058 4665 7576 7267 -178 501 85 O
ATOM 2020 CB TRP A1058 -3.336 17.514 -15.556 1.00 45.72 C
ANISOU 2020 CB TRP A1058 4662 6037 6674 -493 322 -41 C
ATOM 2021 CG TRP A1058 -4.736 17.305 -15.989 1.00 44.83 C
ANISOU 2021 CG TRP A1058 4767 5637 6630 -379 277 -99 C
ATOM 2022 CD1 TRP A1058 -5.779 16.980 -15.213 1.00 44.82 C
ANISOU 2022 CD1 TRP A1058 4841 5459 6730 -273 204 -145 C
ATOM 2023 CD2 TRP A1058 -5.237 17.359 -17.334 1.00 52.04 C
ANISOU 2023 CD2 TRP A1058 5824 6457 7492 -370 303 -110 C
ATOM 2024 NE1 TRP A1058 -6.921 16.844 -15.964 1.00 45.32 N
ANISOU 2024 NE1 TRP A1058 5065 5352 6802 -209 177 -179 N
ATOM 2025 CE2 TRP A1058 -6.610 17.071 -17.275 1.00 52.32 C
ANISOU 2025 CE2 TRP A1058 6001 6284 7595 -265 233 -159 C
ATOM 2026 CE3 TRP A1058 -4.661 17.645 -18.582 1.00 48.71 C
ANISOU 2026 CE3 TRP A1058 5417 6132 6958 -453 378 -78 C
ATOM 2027 CZ2 TRP A1058 -7.405 17.051 -18.409 1.00 49.43 C
ANISOU 2027 CZ2 TRP A1058 5777 5825 7181 -244 225 -173 C
ATOM 2028 CZ3 TRP A1058 -5.442 17.639 -19.672 1.00 48.38 C
ANISOU 2028 CZ3 TRP A1058 5540 5961 6880 -422 374 -97 C
ATOM 2029 CH2 TRP A1058 -6.789 17.328 -19.595 1.00 47.26 C
ANISOU 2029 CH2 TRP A1058 5526 5632 6800 -319 295 -143 C
ATOM 2030 N GLY A1059 -0.442 17.337 -15.716 1.00 54.95 N
ANISOU 2030 N GLY A1059 5296 7969 7614 -613 487 100 N
ATOM 2031 CA GLY A1059 0.950 17.570 -15.408 1.00 52.80 C
ANISOU 2031 CA GLY A1059 4720 8132 7210 -756 528 188 C
ATOM 2032 C GLY A1059 1.900 16.923 -16.404 1.00 58.26 C
ANISOU 2032 C GLY A1059 5207 9146 7783 -606 677 242 C
ATOM 2033 O GLY A1059 1.549 16.012 -17.163 1.00 62.78 O
ANISOU 2033 O GLY A1059 5871 9596 8385 -322 762 203 O
ATOM 2034 N ASP A1060 3.137 17.406 -16.378 1.00 60.40 N
ANISOU 2034 N ASP A1060 5198 9856 7895 -815 715 336 N
ATOM 2035 CA ASP A1060 4.183 16.988 -17.303 1.00 65.48 C
ANISOU 2035 CA ASP A1060 5598 10896 8387 -713 866 409 C
ATOM 2036 C ASP A1060 5.402 16.536 -16.506 1.00 67.65 C
ANISOU 2036 C ASP A1060 5439 11717 8548 -615 905 516 C
ATOM 2037 O ASP A1060 6.177 17.368 -16.021 1.00 76.31 O
ANISOU 2037 O ASP A1060 6319 13157 9518 -971 852 589 O
ATOM 2038 CB ASP A1060 4.560 18.126 -18.240 1.00 71.70 C
ANISOU 2038 CB ASP A1060 6432 11774 9037 -1106 886 444 C
ATOM 2039 CG ASP A1060 5.856 17.878 -18.921 1.00 79.85 C
ANISOU 2039 CG ASP A1060 7121 13345 9874 -1082 1033 544 C
ATOM 2040 OD1 ASP A1060 5.998 16.767 -19.468 1.00 87.49 O
ANISOU 2040 OD1 ASP A1060 8018 14385 10839 -668 1162 544 O
ATOM 2041 OD2 ASP A1060 6.727 18.773 -18.893 1.00 80.84 O
ANISOU 2041 OD2 ASP A1060 7057 13826 9831 -1477 1025 625 O
ATOM 2042 N ASP A1061 5.584 15.223 -16.406 1.00 65.94 N
ANISOU 2042 N ASP A1061 5112 11594 8350 -138 1003 532 N
ATOM 2043 CA ASP A1061 6.675 14.595 -15.660 1.00 66.52 C
ANISOU 2043 CA ASP A1061 4777 12188 8308 84 1055 650 C
ATOM 2044 C ASP A1061 6.576 14.884 -14.171 1.00 65.84 C
ANISOU 2044 C ASP A1061 4610 12126 8279 -60 900 661 C
ATOM 2045 O ASP A1061 7.595 15.008 -13.474 1.00 68.76 O
ANISOU 2045 O ASP A1061 4714 12903 8508 -134 856 755 O
ATOM 2046 CB ASP A1061 8.045 14.994 -16.196 1.00 68.49 C
ANISOU 2046 CB ASP A1061 4681 13020 8322 -69 1134 770 C
ATOM 2047 CG ASP A1061 8.846 13.795 -16.629 1.00 74.93 C
ANISOU 2047 CG ASP A1061 5403 14042 9026 436 1277 830 C
ATOM 2048 OD1 ASP A1061 8.241 12.707 -16.762 1.00 71.75 O
ANISOU 2048 OD1 ASP A1061 5179 13363 8721 877 1371 779 O
ATOM 2049 OD2 ASP A1061 10.075 13.930 -16.824 1.00 85.42 O
ANISOU 2049 OD2 ASP A1061 6509 15796 10152 391 1294 930 O
ATOM 2050 N SER A1062 5.325 14.988 -13.725 1.00 60.06 N
ANISOU 2050 N SER A1062 4236 10845 7740 -97 791 545 N
ATOM 2051 CA SER A1062 4.913 15.297 -12.366 1.00 59.74 C
ANISOU 2051 CA SER A1062 4233 10681 7783 -233 641 521 C
ATOM 2052 C SER A1062 3.394 15.226 -12.337 1.00 55.14 C
ANISOU 2052 C SER A1062 4079 9466 7407 -178 575 387 C
ATOM 2053 O SER A1062 2.739 15.448 -13.354 1.00 68.41 O
ANISOU 2053 O SER A1062 6009 10852 9133 -220 603 321 O
ATOM 2054 CB SER A1062 5.369 16.679 -11.948 1.00 65.92 C
ANISOU 2054 CB SER A1062 4928 11662 8458 -773 535 552 C
ATOM 2055 OG SER A1062 4.440 17.622 -12.443 1.00 67.29 O
ANISOU 2055 OG SER A1062 5483 11375 8709 -1051 478 457 O
ATOM 2056 N ILE A1063 2.829 14.933 -11.170 1.00 48.41 N
ANISOU 2056 N ILE A1063 3295 8437 6661 -91 486 355 N
ATOM 2057 CA ILE A1063 1.371 14.949 -11.013 1.00 52.03 C
ANISOU 2057 CA ILE A1063 4117 8358 7294 -74 413 239 C
ATOM 2058 C ILE A1063 0.890 16.370 -10.730 1.00 49.76 C
ANISOU 2058 C ILE A1063 3998 7889 7021 -482 294 198 C
ATOM 2059 O ILE A1063 1.438 17.059 -9.869 1.00 60.23 O
ANISOU 2059 O ILE A1063 5200 9413 8271 -734 222 236 O
ATOM 2060 CB ILE A1063 0.912 13.978 -9.912 1.00 52.36 C
ANISOU 2060 CB ILE A1063 4186 8278 7432 203 383 222 C
ATOM 2061 CG1 ILE A1063 1.193 12.549 -10.345 1.00 56.76 C
ANISOU 2061 CG1 ILE A1063 4713 8889 7965 633 522 249 C
ATOM 2062 CG2 ILE A1063 -0.590 14.138 -9.631 1.00 46.45 C
ANISOU 2062 CG2 ILE A1063 3765 7045 6840 159 297 113 C
ATOM 2063 CD1 ILE A1063 1.046 11.531 -9.252 1.00 61.21 C
ANISOU 2063 CD1 ILE A1063 5279 9408 8571 921 518 266 C
ATOM 2064 N GLU A1064 -0.097 16.816 -11.499 1.00 47.96 N
ANISOU 2064 N GLU A1064 4064 7297 6860 -544 282 126 N
ATOM 2065 CA GLU A1064 -0.829 18.057 -11.299 1.00 49.21 C
ANISOU 2065 CA GLU A1064 4480 7179 7040 -824 188 82 C
ATOM 2066 C GLU A1064 -2.301 17.706 -11.214 1.00 45.27 C
ANISOU 2066 C GLU A1064 4230 6280 6692 -630 146 1 C
ATOM 2067 O GLU A1064 -2.776 16.781 -11.887 1.00 45.46 O
ANISOU 2067 O GLU A1064 4294 6207 6771 -390 200 -28 O
ATOM 2068 CB GLU A1064 -0.669 19.065 -12.445 1.00 46.85 C
ANISOU 2068 CB GLU A1064 4315 6845 6642 -1075 217 97 C
ATOM 2069 CG GLU A1064 0.601 19.893 -12.443 1.00 53.66 C
ANISOU 2069 CG GLU A1064 5015 8052 7323 -1430 231 172 C
ATOM 2070 CD GLU A1064 0.871 20.581 -13.809 1.00 67.27 C
ANISOU 2070 CD GLU A1064 6844 9782 8935 -1624 297 199 C
ATOM 2071 OE1 GLU A1064 -0.067 20.721 -14.639 1.00 68.25 O
ANISOU 2071 OE1 GLU A1064 7234 9575 9122 -1529 304 156 O
ATOM 2072 OE2 GLU A1064 2.034 20.969 -14.063 1.00 66.18 O
ANISOU 2072 OE2 GLU A1064 6506 10011 8628 -1878 342 272 O
ATOM 2073 N LEU A1065 -3.024 18.464 -10.412 1.00 43.19 N
ANISOU 2073 N LEU A1065 4143 5799 6469 -748 56 -34 N
ATOM 2074 CA LEU A1065 -4.456 18.278 -10.382 1.00 43.33 C
ANISOU 2074 CA LEU A1065 4372 5491 6600 -586 17 -96 C
ATOM 2075 C LEU A1065 -5.067 18.993 -11.564 1.00 41.24 C
ANISOU 2075 C LEU A1065 4322 5042 6305 -647 26 -103 C
ATOM 2076 O LEU A1065 -4.445 19.849 -12.194 1.00 46.79 O
ANISOU 2076 O LEU A1065 5072 5805 6901 -856 51 -66 O
ATOM 2077 CB LEU A1065 -5.047 18.801 -9.062 1.00 46.29 C
ANISOU 2077 CB LEU A1065 4853 5719 7017 -641 -68 -125 C
ATOM 2078 CG LEU A1065 -4.361 18.259 -7.796 1.00 47.65 C
ANISOU 2078 CG LEU A1065 4817 6095 7193 -623 -91 -107 C
ATOM 2079 CD1 LEU A1065 -4.999 18.867 -6.598 1.00 52.93 C
ANISOU 2079 CD1 LEU A1065 5630 6596 7884 -694 -167 -142 C
ATOM 2080 CD2 LEU A1065 -4.340 16.751 -7.694 1.00 39.46 C
ANISOU 2080 CD2 LEU A1065 3622 5145 6227 -334 -47 -104 C
ATOM 2081 N GLN A1066 -6.290 18.594 -11.879 1.00 42.26 N
ANISOU 2081 N GLN A1066 4574 4971 6510 -469 7 -144 N
ATOM 2082 CA GLN A1066 -7.166 19.355 -12.756 1.00 40.62 C
ANISOU 2082 CA GLN A1066 4587 4574 6272 -487 -12 -143 C
ATOM 2083 C GLN A1066 -7.203 20.820 -12.324 1.00 40.89 C
ANISOU 2083 C GLN A1066 4825 4473 6237 -668 -49 -119 C
ATOM 2084 O GLN A1066 -7.105 21.134 -11.141 1.00 43.24 O
ANISOU 2084 O GLN A1066 5136 4748 6546 -730 -86 -131 O
ATOM 2085 CB GLN A1066 -8.554 18.707 -12.728 1.00 43.59 C
ANISOU 2085 CB GLN A1066 5016 4818 6729 -283 -51 -183 C
ATOM 2086 CG GLN A1066 -9.454 19.037 -13.887 1.00 41.23 C
ANISOU 2086 CG GLN A1066 4861 4419 6384 -238 -63 -172 C
ATOM 2087 CD GLN A1066 -9.917 20.468 -13.805 1.00 42.71 C
ANISOU 2087 CD GLN A1066 5264 4452 6511 -291 -100 -131 C
ATOM 2088 OE1 GLN A1066 -10.081 21.007 -12.699 1.00 42.63 O
ANISOU 2088 OE1 GLN A1066 5320 4359 6519 -303 -132 -136 O
ATOM 2089 NE2 GLN A1066 -10.095 21.115 -14.966 1.00 42.74 N
ANISOU 2089 NE2 GLN A1066 5412 4404 6424 -317 -87 -88 N
ATOM 2090 N ASP A1067 -7.328 21.732 -13.290 1.00 45.28 N
ANISOU 2090 N ASP A1067 5580 4925 6701 -757 -33 -84 N
ATOM 2091 CA ASP A1067 -6.966 23.121 -13.016 1.00 51.16 C
ANISOU 2091 CA ASP A1067 6559 5550 7328 -990 -37 -54 C
ATOM 2092 C ASP A1067 -7.930 23.806 -12.051 1.00 55.70 C
ANISOU 2092 C ASP A1067 7366 5882 7914 -907 -86 -72 C
ATOM 2093 O ASP A1067 -7.504 24.638 -11.243 1.00 55.20 O
ANISOU 2093 O ASP A1067 7459 5741 7772 -1101 -92 -74 O
ATOM 2094 CB ASP A1067 -6.873 23.905 -14.322 1.00 64.19 C
ANISOU 2094 CB ASP A1067 8407 7124 8860 -1093 4 -3 C
ATOM 2095 CG ASP A1067 -5.599 23.605 -15.089 1.00 75.81 C
ANISOU 2095 CG ASP A1067 9685 8854 10264 -1277 69 25 C
ATOM 2096 OD1 ASP A1067 -5.523 22.534 -15.745 1.00 79.16 O
ANISOU 2096 OD1 ASP A1067 9896 9435 10747 -1123 102 13 O
ATOM 2097 OD2 ASP A1067 -4.672 24.441 -15.018 1.00 76.42 O
ANISOU 2097 OD2 ASP A1067 9836 8989 10210 -1586 94 59 O
ATOM 2098 N ASP A1068 -9.234 23.506 -12.124 1.00 56.34 N
ANISOU 2098 N ASP A1068 7485 5856 8066 -631 -116 -81 N
ATOM 2099 CA ASP A1068 -10.159 24.181 -11.210 1.00 48.02 C
ANISOU 2099 CA ASP A1068 6641 4602 7002 -512 -146 -88 C
ATOM 2100 C ASP A1068 -10.050 23.661 -9.787 1.00 46.87 C
ANISOU 2100 C ASP A1068 6351 4518 6940 -510 -175 -140 C
ATOM 2101 O ASP A1068 -10.440 24.366 -8.849 1.00 47.95 O
ANISOU 2101 O ASP A1068 6684 4498 7038 -493 -185 -153 O
ATOM 2102 CB ASP A1068 -11.592 24.065 -11.713 1.00 48.18 C
ANISOU 2102 CB ASP A1068 6703 4561 7043 -217 -168 -64 C
ATOM 2103 CG ASP A1068 -11.731 24.533 -13.176 1.00 62.86 C
ANISOU 2103 CG ASP A1068 8695 6382 8806 -202 -146 -1 C
ATOM 2104 OD1 ASP A1068 -11.179 25.625 -13.518 1.00 57.71 O
ANISOU 2104 OD1 ASP A1068 8314 5585 8029 -360 -108 38 O
ATOM 2105 OD2 ASP A1068 -12.369 23.789 -13.975 1.00 63.66 O
ANISOU 2105 OD2 ASP A1068 8644 6603 8942 -59 -167 7 O
ATOM 2106 N PHE A1069 -9.495 22.464 -9.607 1.00 47.25 N
ANISOU 2106 N PHE A1069 6088 4782 7081 -516 -180 -166 N
ATOM 2107 CA PHE A1069 -9.344 21.873 -8.287 1.00 41.47 C
ANISOU 2107 CA PHE A1069 5208 4128 6420 -501 -208 -204 C
ATOM 2108 C PHE A1069 -8.150 22.403 -7.517 1.00 43.61 C
ANISOU 2108 C PHE A1069 5481 4478 6612 -769 -211 -202 C
ATOM 2109 O PHE A1069 -8.093 22.214 -6.300 1.00 50.00 O
ANISOU 2109 O PHE A1069 6235 5317 7447 -777 -242 -229 O
ATOM 2110 CB PHE A1069 -9.192 20.373 -8.410 1.00 37.13 C
ANISOU 2110 CB PHE A1069 4373 3763 5973 -381 -201 -219 C
ATOM 2111 CG PHE A1069 -9.667 19.622 -7.232 1.00 38.02 C
ANISOU 2111 CG PHE A1069 4385 3889 6170 -259 -233 -252 C
ATOM 2112 CD1 PHE A1069 -8.821 19.351 -6.172 1.00 46.22 C
ANISOU 2112 CD1 PHE A1069 5298 5049 7213 -341 -244 -256 C
ATOM 2113 CD2 PHE A1069 -10.960 19.139 -7.194 1.00 38.38 C
ANISOU 2113 CD2 PHE A1069 4445 3864 6275 -72 -252 -272 C
ATOM 2114 CE1 PHE A1069 -9.263 18.621 -5.095 1.00 43.14 C
ANISOU 2114 CE1 PHE A1069 4830 4668 6894 -224 -270 -280 C
ATOM 2115 CE2 PHE A1069 -11.398 18.427 -6.133 1.00 36.10 C
ANISOU 2115 CE2 PHE A1069 4072 3595 6050 16 -274 -298 C
ATOM 2116 CZ PHE A1069 -10.556 18.166 -5.084 1.00 43.30 C
ANISOU 2116 CZ PHE A1069 4890 4588 6975 -52 -281 -304 C
ATOM 2117 N ILE A1070 -7.182 23.012 -8.189 1.00 41.76 N
ANISOU 2117 N ILE A1070 5290 4310 6268 -1009 -180 -169 N
ATOM 2118 CA ILE A1070 -5.986 23.469 -7.479 1.00 45.08 C
ANISOU 2118 CA ILE A1070 5670 4878 6580 -1321 -190 -161 C
ATOM 2119 C ILE A1070 -6.327 24.371 -6.314 1.00 46.69 C
ANISOU 2119 C ILE A1070 6146 4880 6715 -1425 -222 -196 C
ATOM 2120 O ILE A1070 -5.832 24.115 -5.198 1.00 52.42 O
ANISOU 2120 O ILE A1070 6736 5748 7432 -1523 -260 -213 O
ATOM 2121 CB ILE A1070 -5.008 24.145 -8.471 1.00 47.07 C
ANISOU 2121 CB ILE A1070 5969 5226 6688 -1608 -146 -114 C
ATOM 2122 CG1 ILE A1070 -4.477 23.120 -9.465 1.00 49.43 C
ANISOU 2122 CG1 ILE A1070 5952 5787 7041 -1499 -103 -81 C
ATOM 2123 CG2 ILE A1070 -3.925 24.746 -7.702 1.00 43.80 C
ANISOU 2123 CG2 ILE A1070 5546 4968 6127 -1977 -165 -104 C
ATOM 2124 CD1 ILE A1070 -3.909 23.781 -10.687 1.00 44.56 C
ANISOU 2124 CD1 ILE A1070 5428 5204 6299 -1704 -49 -35 C
ATOM 2125 N PRO A1071 -7.138 25.414 -6.452 1.00 46.61 N
ANISOU 2125 N PRO A1071 6529 4545 6637 -1393 -204 -203 N
ATOM 2126 CA PRO A1071 -7.398 26.278 -5.300 1.00 49.86 C
ANISOU 2126 CA PRO A1071 7243 4747 6953 -1485 -215 -242 C
ATOM 2127 C PRO A1071 -8.110 25.573 -4.164 1.00 47.22 C
ANISOU 2127 C PRO A1071 6773 4427 6740 -1247 -252 -284 C
ATOM 2128 O PRO A1071 -7.848 25.871 -2.996 1.00 48.48 O
ANISOU 2128 O PRO A1071 7014 4571 6834 -1390 -276 -321 O
ATOM 2129 CB PRO A1071 -8.250 27.387 -5.905 1.00 42.23 C
ANISOU 2129 CB PRO A1071 6727 3426 5892 -1382 -166 -225 C
ATOM 2130 CG PRO A1071 -7.895 27.381 -7.300 1.00 42.69 C
ANISOU 2130 CG PRO A1071 6735 3553 5934 -1436 -138 -172 C
ATOM 2131 CD PRO A1071 -7.738 25.982 -7.675 1.00 42.03 C
ANISOU 2131 CD PRO A1071 6180 3771 6018 -1291 -163 -168 C
ATOM 2132 N LEU A1072 -9.000 24.637 -4.480 1.00 45.54 N
ANISOU 2132 N LEU A1072 6365 4256 6684 -916 -258 -280 N
ATOM 2133 CA LEU A1072 -9.681 23.873 -3.442 1.00 41.45 C
ANISOU 2133 CA LEU A1072 5702 3775 6273 -711 -288 -313 C
ATOM 2134 C LEU A1072 -8.696 23.008 -2.674 1.00 41.23 C
ANISOU 2134 C LEU A1072 5371 4010 6284 -840 -325 -321 C
ATOM 2135 O LEU A1072 -8.757 22.925 -1.447 1.00 53.81 O
ANISOU 2135 O LEU A1072 6961 5611 7874 -850 -354 -350 O
ATOM 2136 CB LEU A1072 -10.794 23.037 -4.079 1.00 39.17 C
ANISOU 2136 CB LEU A1072 5271 3503 6109 -397 -285 -300 C
ATOM 2137 CG LEU A1072 -11.647 22.168 -3.161 1.00 39.85 C
ANISOU 2137 CG LEU A1072 5207 3639 6297 -192 -308 -327 C
ATOM 2138 CD1 LEU A1072 -12.055 22.902 -1.890 1.00 44.04 C
ANISOU 2138 CD1 LEU A1072 5944 4026 6762 -178 -308 -358 C
ATOM 2139 CD2 LEU A1072 -12.865 21.731 -3.913 1.00 40.39 C
ANISOU 2139 CD2 LEU A1072 5222 3706 6420 52 -302 -308 C
ATOM 2140 N PHE A1073 -7.757 22.388 -3.385 1.00 47.25 N
ANISOU 2140 N PHE A1073 5885 5004 7065 -923 -319 -285 N
ATOM 2141 CA PHE A1073 -6.693 21.614 -2.752 1.00 42.09 C
ANISOU 2141 CA PHE A1073 4931 4647 6413 -1014 -345 -267 C
ATOM 2142 C PHE A1073 -5.766 22.511 -1.925 1.00 42.58 C
ANISOU 2142 C PHE A1073 5074 4790 6313 -1359 -377 -268 C
ATOM 2143 O PHE A1073 -5.317 22.122 -0.844 1.00 42.56 O
ANISOU 2143 O PHE A1073 4916 4960 6294 -1408 -421 -267 O
ATOM 2144 CB PHE A1073 -5.917 20.863 -3.845 1.00 41.08 C
ANISOU 2144 CB PHE A1073 4551 4751 6308 -987 -307 -219 C
ATOM 2145 CG PHE A1073 -4.858 19.923 -3.318 1.00 45.84 C
ANISOU 2145 CG PHE A1073 4819 5694 6905 -981 -316 -177 C
ATOM 2146 CD1 PHE A1073 -3.552 20.372 -3.081 1.00 47.82 C
ANISOU 2146 CD1 PHE A1073 4931 6230 7009 -1266 -331 -130 C
ATOM 2147 CD2 PHE A1073 -5.151 18.588 -3.076 1.00 36.98 C
ANISOU 2147 CD2 PHE A1073 3527 4627 5896 -695 -304 -173 C
ATOM 2148 CE1 PHE A1073 -2.570 19.504 -2.577 1.00 42.67 C
ANISOU 2148 CE1 PHE A1073 3936 5949 6327 -1216 -339 -69 C
ATOM 2149 CE2 PHE A1073 -4.180 17.745 -2.603 1.00 37.24 C
ANISOU 2149 CE2 PHE A1073 3284 4963 5902 -637 -300 -117 C
ATOM 2150 CZ PHE A1073 -2.888 18.206 -2.337 1.00 43.71 C
ANISOU 2150 CZ PHE A1073 3927 6104 6577 -875 -320 -60 C
ATOM 2151 N ASP A1074 -5.465 23.720 -2.403 1.00 41.57 N
ANISOU 2151 N ASP A1074 5210 4541 6042 -1625 -358 -268 N
ATOM 2152 CA ASP A1074 -4.541 24.562 -1.647 1.00 44.59 C
ANISOU 2152 CA ASP A1074 5694 5015 6235 -2025 -390 -273 C
ATOM 2153 C ASP A1074 -5.157 25.096 -0.366 1.00 46.67 C
ANISOU 2153 C ASP A1074 6230 5052 6451 -2039 -416 -336 C
ATOM 2154 O ASP A1074 -4.421 25.570 0.509 1.00 47.45 O
ANISOU 2154 O ASP A1074 6376 5260 6393 -2363 -456 -350 O
ATOM 2155 CB ASP A1074 -4.066 25.729 -2.502 1.00 45.96 C
ANISOU 2155 CB ASP A1074 6140 5086 6237 -2348 -352 -258 C
ATOM 2156 CG ASP A1074 -3.234 25.282 -3.690 1.00 60.47 C
ANISOU 2156 CG ASP A1074 7687 7211 8079 -2404 -322 -191 C
ATOM 2157 OD1 ASP A1074 -2.345 24.418 -3.515 1.00 61.52 O
ANISOU 2157 OD1 ASP A1074 7401 7749 8225 -2416 -343 -146 O
ATOM 2158 OD2 ASP A1074 -3.470 25.811 -4.798 1.00 71.86 O
ANISOU 2158 OD2 ASP A1074 9332 8479 9494 -2417 -270 -176 O
ATOM 2159 N SER A1075 -6.487 25.041 -0.263 1.00 43.12 N
ANISOU 2159 N SER A1075 5956 4317 6112 -1706 -391 -371 N
ATOM 2160 CA SER A1075 -7.257 25.595 0.841 1.00 43.73 C
ANISOU 2160 CA SER A1075 6328 4146 6140 -1647 -390 -430 C
ATOM 2161 C SER A1075 -8.070 24.516 1.527 1.00 47.75 C
ANISOU 2161 C SER A1075 6610 4713 6819 -1310 -410 -442 C
ATOM 2162 O SER A1075 -8.988 24.828 2.305 1.00 43.61 O
ANISOU 2162 O SER A1075 6297 3988 6286 -1158 -393 -484 O
ATOM 2163 CB SER A1075 -8.193 26.701 0.351 1.00 41.53 C
ANISOU 2163 CB SER A1075 6519 3472 5790 -1537 -321 -447 C
ATOM 2164 OG SER A1075 -7.501 27.892 0.052 1.00 43.10 O
ANISOU 2164 OG SER A1075 7067 3532 5778 -1898 -294 -450 O
ATOM 2165 N LEU A1076 -7.751 23.253 1.246 1.00 44.47 N
ANISOU 2165 N LEU A1076 5792 4565 6539 -1187 -434 -402 N
ATOM 2166 CA LEU A1076 -8.553 22.140 1.720 1.00 41.32 C
ANISOU 2166 CA LEU A1076 5205 4203 6293 -883 -443 -407 C
ATOM 2167 C LEU A1076 -8.718 22.139 3.232 1.00 41.72 C
ANISOU 2167 C LEU A1076 5300 4247 6306 -900 -475 -443 C
ATOM 2168 O LEU A1076 -9.649 21.511 3.733 1.00 39.04 O
ANISOU 2168 O LEU A1076 4912 3861 6062 -659 -470 -456 O
ATOM 2169 CB LEU A1076 -7.911 20.848 1.251 1.00 41.92 C
ANISOU 2169 CB LEU A1076 4910 4551 6465 -803 -452 -357 C
ATOM 2170 CG LEU A1076 -8.801 19.639 1.131 1.00 40.77 C
ANISOU 2170 CG LEU A1076 4625 4395 6471 -498 -436 -355 C
ATOM 2171 CD1 LEU A1076 -9.988 20.034 0.295 1.00 41.03 C
ANISOU 2171 CD1 LEU A1076 4834 4213 6542 -353 -401 -373 C
ATOM 2172 CD2 LEU A1076 -7.973 18.562 0.450 1.00 41.50 C
ANISOU 2172 CD2 LEU A1076 4447 4711 6610 -445 -421 -305 C
ATOM 2173 N GLU A1077 -7.847 22.834 3.970 1.00 46.78 N
ANISOU 2173 N GLU A1077 6038 4947 6790 -1206 -510 -458 N
ATOM 2174 CA GLU A1077 -7.953 22.905 5.423 1.00 45.07 C
ANISOU 2174 CA GLU A1077 5890 4726 6510 -1253 -543 -496 C
ATOM 2175 C GLU A1077 -9.036 23.868 5.903 1.00 48.40 C
ANISOU 2175 C GLU A1077 6723 4800 6865 -1166 -492 -563 C
ATOM 2176 O GLU A1077 -9.379 23.838 7.085 1.00 57.07 O
ANISOU 2176 O GLU A1077 7890 5866 7928 -1131 -502 -600 O
ATOM 2177 CB GLU A1077 -6.608 23.306 6.029 1.00 41.14 C
ANISOU 2177 CB GLU A1077 5344 4454 5834 -1647 -605 -487 C
ATOM 2178 CG GLU A1077 -6.240 24.793 5.872 1.00 42.97 C
ANISOU 2178 CG GLU A1077 5972 4501 5853 -2007 -586 -529 C
ATOM 2179 CD GLU A1077 -5.697 25.138 4.501 1.00 56.78 C
ANISOU 2179 CD GLU A1077 7710 6283 7579 -2143 -558 -488 C
ATOM 2180 OE1 GLU A1077 -5.187 26.274 4.351 1.00 66.88 O
ANISOU 2180 OE1 GLU A1077 9294 7458 8659 -2504 -547 -510 O
ATOM 2181 OE2 GLU A1077 -5.756 24.281 3.583 1.00 54.09 O
ANISOU 2181 OE2 GLU A1077 7085 6067 7400 -1915 -543 -436 O
ATOM 2182 N GLU A1078 -9.595 24.712 5.043 1.00 40.20 N
ANISOU 2182 N GLU A1078 5971 3508 5794 -1101 -429 -571 N
ATOM 2183 CA GLU A1078 -10.713 25.562 5.447 1.00 41.87 C
ANISOU 2183 CA GLU A1078 6571 3403 5934 -919 -360 -616 C
ATOM 2184 C GLU A1078 -12.092 24.971 5.087 1.00 42.39 C
ANISOU 2184 C GLU A1078 6518 3438 6152 -490 -319 -591 C
ATOM 2185 O GLU A1078 -13.106 25.670 5.205 1.00 49.07 O
ANISOU 2185 O GLU A1078 7647 4065 6934 -269 -249 -604 O
ATOM 2186 CB GLU A1078 -10.569 26.964 4.823 1.00 41.23 C
ANISOU 2186 CB GLU A1078 6950 3038 5677 -1075 -301 -629 C
ATOM 2187 CG GLU A1078 -9.260 27.661 5.086 1.00 50.60 C
ANISOU 2187 CG GLU A1078 8300 4255 6672 -1566 -335 -653 C
ATOM 2188 CD GLU A1078 -9.063 27.996 6.569 1.00 75.62 C
ANISOU 2188 CD GLU A1078 11651 7388 9693 -1750 -355 -721 C
ATOM 2189 OE1 GLU A1078 -7.891 28.112 7.007 1.00 81.40 O
ANISOU 2189 OE1 GLU A1078 12320 8314 10294 -2171 -422 -730 O
ATOM 2190 OE2 GLU A1078 -10.081 28.143 7.296 1.00 81.27 O
ANISOU 2190 OE2 GLU A1078 12560 7913 10407 -1478 -303 -761 O
ATOM 2191 N THR A1079 -12.162 23.723 4.644 1.00 36.81 N
ANISOU 2191 N THR A1079 5416 2954 5616 -369 -355 -551 N
ATOM 2192 CA THR A1079 -13.395 23.201 4.075 1.00 35.25 C
ANISOU 2192 CA THR A1079 5105 2759 5529 -44 -324 -523 C
ATOM 2193 C THR A1079 -14.301 22.502 5.092 1.00 49.91 C
ANISOU 2193 C THR A1079 6835 4687 7441 150 -321 -536 C
ATOM 2194 O THR A1079 -15.477 22.255 4.782 1.00 39.25 O
ANISOU 2194 O THR A1079 5425 3353 6135 403 -288 -512 O
ATOM 2195 CB THR A1079 -13.092 22.230 2.904 1.00 37.54 C
ANISOU 2195 CB THR A1079 5097 3221 5947 -35 -352 -478 C
ATOM 2196 OG1 THR A1079 -12.454 21.021 3.371 1.00 33.40 O
ANISOU 2196 OG1 THR A1079 4275 2907 5508 -100 -398 -472 O
ATOM 2197 CG2 THR A1079 -12.254 22.921 1.818 1.00 35.03 C
ANISOU 2197 CG2 THR A1079 4891 2852 5567 -217 -345 -458 C
ATOM 2198 N GLY A1080 -13.805 22.189 6.290 1.00 49.76 N
ANISOU 2198 N GLY A1080 6766 4739 7402 27 -354 -564 N
ATOM 2199 CA GLY A1080 -14.577 21.405 7.229 1.00 33.92 C
ANISOU 2199 CA GLY A1080 4620 2820 5448 183 -352 -569 C
ATOM 2200 C GLY A1080 -14.372 19.908 7.123 1.00 46.16 C
ANISOU 2200 C GLY A1080 5830 4577 7133 194 -395 -534 C
ATOM 2201 O GLY A1080 -15.313 19.147 7.380 1.00 40.05 O
ANISOU 2201 O GLY A1080 4934 3867 6417 353 -378 -523 O
ATOM 2202 N ALA A1081 -13.152 19.451 6.782 1.00 43.27 N
ANISOU 2202 N ALA A1081 5320 4325 6794 29 -441 -511 N
ATOM 2203 CA ALA A1081 -12.895 18.057 6.429 1.00 32.87 C
ANISOU 2203 CA ALA A1081 3741 3164 5586 81 -459 -470 C
ATOM 2204 C ALA A1081 -12.573 17.157 7.627 1.00 38.79 C
ANISOU 2204 C ALA A1081 4366 4034 6340 78 -489 -455 C
ATOM 2205 O ALA A1081 -12.853 15.943 7.572 1.00 38.08 O
ANISOU 2205 O ALA A1081 4139 4005 6324 186 -479 -426 O
ATOM 2206 CB ALA A1081 -11.761 17.976 5.398 1.00 32.56 C
ANISOU 2206 CB ALA A1081 3604 3211 5555 -31 -473 -438 C
ATOM 2207 N GLN A1082 -12.007 17.684 8.712 1.00 34.20 N
ANISOU 2207 N GLN A1082 3853 3480 5663 -51 -523 -471 N
ATOM 2208 CA GLN A1082 -11.740 16.814 9.859 1.00 41.44 C
ANISOU 2208 CA GLN A1082 4651 4523 6572 -35 -554 -445 C
ATOM 2209 C GLN A1082 -13.029 16.221 10.460 1.00 41.41 C
ANISOU 2209 C GLN A1082 4666 4456 6613 130 -516 -457 C
ATOM 2210 O GLN A1082 -14.006 16.927 10.725 1.00 50.99 O
ANISOU 2210 O GLN A1082 6027 5554 7794 186 -478 -501 O
ATOM 2211 CB GLN A1082 -10.951 17.596 10.892 1.00 36.54 C
ANISOU 2211 CB GLN A1082 4112 3959 5811 -235 -604 -464 C
ATOM 2212 CG GLN A1082 -10.755 17.007 12.273 1.00 36.45 C
ANISOU 2212 CG GLN A1082 4031 4068 5749 -236 -643 -444 C
ATOM 2213 CD GLN A1082 -10.001 18.012 13.136 1.00 49.22 C
ANISOU 2213 CD GLN A1082 5768 5737 7195 -490 -696 -476 C
ATOM 2214 OE1 GLN A1082 -8.796 17.858 13.400 1.00 54.16 O
ANISOU 2214 OE1 GLN A1082 6237 6602 7738 -646 -766 -426 O
ATOM 2215 NE2 GLN A1082 -10.697 19.105 13.516 1.00 53.78 N
ANISOU 2215 NE2 GLN A1082 6641 6100 7692 -539 -658 -559 N
ATOM 2216 N GLY A1083 -13.028 14.909 10.668 1.00 37.78 N
ANISOU 2216 N GLY A1083 4067 4079 6208 214 -516 -411 N
ATOM 2217 CA GLY A1083 -14.207 14.174 11.083 1.00 42.83 C
ANISOU 2217 CA GLY A1083 4709 4685 6881 325 -477 -412 C
ATOM 2218 C GLY A1083 -15.214 13.896 9.983 1.00 45.26 C
ANISOU 2218 C GLY A1083 5002 4941 7253 403 -431 -418 C
ATOM 2219 O GLY A1083 -16.159 13.132 10.210 1.00 35.81 O
ANISOU 2219 O GLY A1083 3780 3759 6067 451 -400 -410 O
ATOM 2220 N ARG A1084 -15.049 14.492 8.804 1.00 48.52 N
ANISOU 2220 N ARG A1084 5430 5314 7690 391 -429 -429 N
ATOM 2221 CA ARG A1084 -16.002 14.338 7.711 1.00 38.62 C
ANISOU 2221 CA ARG A1084 4157 4042 6475 453 -396 -431 C
ATOM 2222 C ARG A1084 -15.726 13.050 6.966 1.00 32.11 C
ANISOU 2222 C ARG A1084 3255 3244 5702 448 -387 -403 C
ATOM 2223 O ARG A1084 -14.566 12.728 6.713 1.00 35.89 O
ANISOU 2223 O ARG A1084 3701 3740 6195 427 -399 -380 O
ATOM 2224 CB ARG A1084 -15.887 15.524 6.746 1.00 29.26 C
ANISOU 2224 CB ARG A1084 3049 2792 5275 450 -395 -447 C
ATOM 2225 CG ARG A1084 -16.929 15.560 5.659 1.00 28.21 C
ANISOU 2225 CG ARG A1084 2895 2670 5155 530 -370 -440 C
ATOM 2226 CD ARG A1084 -18.180 16.250 6.166 1.00 27.71 C
ANISOU 2226 CD ARG A1084 2881 2621 5028 654 -339 -445 C
ATOM 2227 NE ARG A1084 -17.817 17.437 6.907 1.00 31.24 N
ANISOU 2227 NE ARG A1084 3506 2958 5407 665 -330 -472 N
ATOM 2228 CZ ARG A1084 -18.675 18.151 7.614 1.00 31.34 C
ANISOU 2228 CZ ARG A1084 3619 2951 5339 796 -286 -482 C
ATOM 2229 NH1 ARG A1084 -19.939 17.772 7.676 1.00 31.17 N
ANISOU 2229 NH1 ARG A1084 3478 3066 5298 929 -254 -456 N
ATOM 2230 NH2 ARG A1084 -18.266 19.232 8.267 1.00 32.53 N
ANISOU 2230 NH2 ARG A1084 3996 2959 5404 784 -269 -517 N
ATOM 2231 N LYS A1085 -16.789 12.312 6.588 1.00 35.25 N
ANISOU 2231 N LYS A1085 3629 3659 6104 461 -359 -401 N
ATOM 2232 CA LYS A1085 -16.653 11.095 5.766 1.00 35.19 C
ANISOU 2232 CA LYS A1085 3621 3634 6115 434 -337 -387 C
ATOM 2233 C LYS A1085 -16.490 11.453 4.281 1.00 38.41 C
ANISOU 2233 C LYS A1085 4023 4028 6544 428 -335 -396 C
ATOM 2234 O LYS A1085 -17.389 12.061 3.684 1.00 38.09 O
ANISOU 2234 O LYS A1085 3963 4023 6485 431 -340 -407 O
ATOM 2235 CB LYS A1085 -17.867 10.189 5.936 1.00 28.58 C
ANISOU 2235 CB LYS A1085 2791 2830 5238 380 -310 -387 C
ATOM 2236 CG LYS A1085 -18.102 9.615 7.348 1.00 31.15 C
ANISOU 2236 CG LYS A1085 3141 3165 5529 367 -299 -371 C
ATOM 2237 CD LYS A1085 -19.543 9.126 7.474 1.00 31.56 C
ANISOU 2237 CD LYS A1085 3168 3309 5516 274 -275 -372 C
ATOM 2238 CE LYS A1085 -20.166 9.659 8.753 1.00 45.83 C
ANISOU 2238 CE LYS A1085 4924 5204 7285 309 -273 -369 C
ATOM 2239 NZ LYS A1085 -21.307 10.647 8.544 1.00 52.50 N
ANISOU 2239 NZ LYS A1085 5657 6202 8087 364 -268 -375 N
ATOM 2240 N VAL A1086 -15.364 11.056 3.667 1.00 31.61 N
ANISOU 2240 N VAL A1086 3170 3137 5703 439 -323 -382 N
ATOM 2241 CA VAL A1086 -15.079 11.425 2.284 1.00 30.51 C
ANISOU 2241 CA VAL A1086 3029 2990 5575 429 -317 -389 C
ATOM 2242 C VAL A1086 -14.791 10.188 1.419 1.00 31.01 C
ANISOU 2242 C VAL A1086 3144 3012 5627 436 -268 -386 C
ATOM 2243 O VAL A1086 -14.617 9.078 1.903 1.00 26.87 O
ANISOU 2243 O VAL A1086 2682 2444 5082 466 -233 -372 O
ATOM 2244 CB VAL A1086 -13.904 12.406 2.213 1.00 34.16 C
ANISOU 2244 CB VAL A1086 3458 3477 6043 422 -337 -377 C
ATOM 2245 CG1 VAL A1086 -14.212 13.667 2.969 1.00 29.68 C
ANISOU 2245 CG1 VAL A1086 2922 2899 5456 395 -372 -392 C
ATOM 2246 CG2 VAL A1086 -12.672 11.737 2.766 1.00 33.07 C
ANISOU 2246 CG2 VAL A1086 3270 3396 5899 459 -328 -339 C
ATOM 2247 N ALA A1087 -14.749 10.401 0.109 1.00 35.32 N
ANISOU 2247 N ALA A1087 3699 3553 6168 415 -256 -398 N
ATOM 2248 CA ALA A1087 -14.188 9.436 -0.835 1.00 36.46 C
ANISOU 2248 CA ALA A1087 3918 3648 6287 440 -197 -399 C
ATOM 2249 C ALA A1087 -13.780 10.210 -2.077 1.00 39.70 C
ANISOU 2249 C ALA A1087 4295 4090 6701 427 -199 -403 C
ATOM 2250 O ALA A1087 -14.159 11.366 -2.261 1.00 47.34 O
ANISOU 2250 O ALA A1087 5216 5091 7680 389 -245 -405 O
ATOM 2251 CB ALA A1087 -15.170 8.316 -1.199 1.00 28.25 C
ANISOU 2251 CB ALA A1087 3006 2540 5187 361 -165 -428 C
ATOM 2252 N CYS A1088 -13.014 9.553 -2.935 1.00 39.50 N
ANISOU 2252 N CYS A1088 4319 4043 6648 475 -136 -399 N
ATOM 2253 CA CYS A1088 -12.360 10.211 -4.053 1.00 38.04 C
ANISOU 2253 CA CYS A1088 4093 3904 6455 470 -124 -393 C
ATOM 2254 C CYS A1088 -12.480 9.361 -5.305 1.00 36.47 C
ANISOU 2254 C CYS A1088 4015 3643 6198 470 -60 -421 C
ATOM 2255 O CYS A1088 -12.319 8.130 -5.266 1.00 32.87 O
ANISOU 2255 O CYS A1088 3688 3106 5697 535 10 -430 O
ATOM 2256 CB CYS A1088 -10.879 10.453 -3.772 1.00 42.21 C
ANISOU 2256 CB CYS A1088 4513 4538 6985 543 -100 -345 C
ATOM 2257 SG CYS A1088 -10.549 11.314 -2.281 1.00 53.05 S
ANISOU 2257 SG CYS A1088 5774 5995 8388 506 -172 -316 S
ATOM 2258 N PHE A1089 -12.753 10.024 -6.418 1.00 29.30 N
ANISOU 2258 N PHE A1089 3102 2759 5271 401 -77 -433 N
ATOM 2259 CA PHE A1089 -12.705 9.372 -7.714 1.00 36.26 C
ANISOU 2259 CA PHE A1089 4098 3597 6081 388 -16 -461 C
ATOM 2260 C PHE A1089 -11.893 10.219 -8.663 1.00 36.29 C
ANISOU 2260 C PHE A1089 4034 3675 6078 396 -1 -438 C
ATOM 2261 O PHE A1089 -11.570 11.382 -8.399 1.00 30.79 O
ANISOU 2261 O PHE A1089 3228 3047 5422 369 -48 -405 O
ATOM 2262 CB PHE A1089 -14.095 9.105 -8.318 1.00 31.61 C
ANISOU 2262 CB PHE A1089 3595 2984 5430 250 -53 -502 C
ATOM 2263 CG PHE A1089 -14.967 10.286 -8.370 1.00 31.48 C
ANISOU 2263 CG PHE A1089 3467 3061 5432 191 -146 -483 C
ATOM 2264 CD1 PHE A1089 -15.479 10.836 -7.192 1.00 30.38 C
ANISOU 2264 CD1 PHE A1089 3239 2958 5347 210 -202 -462 C
ATOM 2265 CD2 PHE A1089 -15.297 10.854 -9.583 1.00 32.67 C
ANISOU 2265 CD2 PHE A1089 3619 3264 5530 142 -169 -478 C
ATOM 2266 CE1 PHE A1089 -16.305 11.973 -7.216 1.00 30.91 C
ANISOU 2266 CE1 PHE A1089 3231 3105 5409 213 -269 -434 C
ATOM 2267 CE2 PHE A1089 -16.129 12.007 -9.630 1.00 36.96 C
ANISOU 2267 CE2 PHE A1089 4078 3896 6069 143 -246 -440 C
ATOM 2268 CZ PHE A1089 -16.636 12.561 -8.442 1.00 32.36 C
ANISOU 2268 CZ PHE A1089 3420 3340 5534 194 -290 -417 C
ATOM 2269 N GLY A1090 -11.553 9.616 -9.780 1.00 39.58 N
ANISOU 2269 N GLY A1090 4548 4067 6425 418 75 -458 N
ATOM 2270 CA GLY A1090 -10.936 10.432 -10.790 1.00 39.21 C
ANISOU 2270 CA GLY A1090 4444 4098 6356 397 89 -436 C
ATOM 2271 C GLY A1090 -10.803 9.683 -12.077 1.00 35.40 C
ANISOU 2271 C GLY A1090 4100 3574 5777 412 173 -471 C
ATOM 2272 O GLY A1090 -10.819 8.457 -12.094 1.00 37.07 O
ANISOU 2272 O GLY A1090 4465 3687 5932 476 248 -507 O
ATOM 2273 N CYS A1091 -10.696 10.427 -13.161 1.00 38.47 N
ANISOU 2273 N CYS A1091 4471 4017 6128 347 167 -461 N
ATOM 2274 CA CYS A1091 -10.379 9.852 -14.447 1.00 45.89 C
ANISOU 2274 CA CYS A1091 5533 4939 6964 364 258 -490 C
ATOM 2275 C CYS A1091 -8.877 9.938 -14.717 1.00 46.12 C
ANISOU 2275 C CYS A1091 5467 5086 6972 487 361 -445 C
ATOM 2276 O CYS A1091 -8.216 10.934 -14.394 1.00 43.83 O
ANISOU 2276 O CYS A1091 5001 4927 6726 457 331 -387 O
ATOM 2277 CB CYS A1091 -11.184 10.565 -15.532 1.00 53.91 C
ANISOU 2277 CB CYS A1091 6583 5972 7928 222 192 -497 C
ATOM 2278 SG CYS A1091 -12.963 10.200 -15.430 1.00 55.79 S
ANISOU 2278 SG CYS A1091 6905 6165 8129 84 88 -540 S
ATOM 2279 N GLY A1092 -8.340 8.869 -15.294 1.00 44.80 N
ANISOU 2279 N GLY A1092 5428 4882 6711 621 493 -470 N
ATOM 2280 CA GLY A1092 -6.968 8.877 -15.730 1.00 44.00 C
ANISOU 2280 CA GLY A1092 5223 4940 6554 764 609 -421 C
ATOM 2281 C GLY A1092 -6.700 8.042 -16.960 1.00 48.15 C
ANISOU 2281 C GLY A1092 5945 5409 6941 860 748 -463 C
ATOM 2282 O GLY A1092 -7.588 7.749 -17.770 1.00 47.77 O
ANISOU 2282 O GLY A1092 6108 5214 6828 741 735 -534 O
ATOM 2283 N ASP A1093 -5.438 7.657 -17.088 1.00 48.08 N
ANISOU 2283 N ASP A1093 5859 5547 6864 1084 888 -414 N
ATOM 2284 CA ASP A1093 -4.945 6.934 -18.245 1.00 47.03 C
ANISOU 2284 CA ASP A1093 5897 5395 6578 1230 1053 -441 C
ATOM 2285 C ASP A1093 -3.815 6.071 -17.743 1.00 50.90 C
ANISOU 2285 C ASP A1093 6348 5991 7002 1581 1208 -381 C
ATOM 2286 O ASP A1093 -2.824 6.594 -17.227 1.00 57.71 O
ANISOU 2286 O ASP A1093 6889 7147 7890 1666 1211 -282 O
ATOM 2287 CB ASP A1093 -4.452 7.886 -19.315 1.00 53.02 C
ANISOU 2287 CB ASP A1093 6512 6341 7292 1117 1064 -410 C
ATOM 2288 CG ASP A1093 -4.415 7.261 -20.662 1.00 60.47 C
ANISOU 2288 CG ASP A1093 7697 7201 8079 1177 1197 -468 C
ATOM 2289 OD1 ASP A1093 -3.628 6.311 -20.853 1.00 59.30 O
ANISOU 2289 OD1 ASP A1093 7647 7071 7815 1462 1376 -462 O
ATOM 2290 OD2 ASP A1093 -5.198 7.718 -21.523 1.00 70.78 O
ANISOU 2290 OD2 ASP A1093 9107 8424 9362 953 1123 -516 O
ATOM 2291 N SER A1094 -3.972 4.758 -17.867 1.00 49.85 N
ANISOU 2291 N SER A1094 6552 5627 6761 1780 1336 -434 N
ATOM 2292 CA SER A1094 -2.977 3.876 -17.289 1.00 52.70 C
ANISOU 2292 CA SER A1094 6915 6064 7044 2175 1489 -362 C
ATOM 2293 C SER A1094 -1.652 3.892 -18.047 1.00 52.04 C
ANISOU 2293 C SER A1094 6668 6276 6830 2436 1658 -287 C
ATOM 2294 O SER A1094 -0.684 3.287 -17.571 1.00 62.29 O
ANISOU 2294 O SER A1094 7884 7736 8046 2810 1789 -196 O
ATOM 2295 CB SER A1094 -3.562 2.483 -17.230 1.00 56.95 C
ANISOU 2295 CB SER A1094 7937 6223 7477 2307 1591 -441 C
ATOM 2296 OG SER A1094 -4.304 2.294 -18.412 1.00 61.66 O
ANISOU 2296 OG SER A1094 8838 6607 7983 2105 1612 -555 O
ATOM 2297 N SER A1095 -1.597 4.538 -19.215 1.00 50.14 N
ANISOU 2297 N SER A1095 6378 6124 6549 2266 1666 -314 N
ATOM 2298 CA SER A1095 -0.325 4.772 -19.892 1.00 57.64 C
ANISOU 2298 CA SER A1095 7091 7429 7382 2455 1808 -229 C
ATOM 2299 C SER A1095 0.656 5.499 -18.989 1.00 65.84 C
ANISOU 2299 C SER A1095 7642 8898 8477 2491 1754 -90 C
ATOM 2300 O SER A1095 1.850 5.180 -18.958 1.00 66.45 O
ANISOU 2300 O SER A1095 7509 9308 8430 2811 1901 17 O
ATOM 2301 CB SER A1095 -0.552 5.594 -21.154 1.00 57.90 C
ANISOU 2301 CB SER A1095 7115 7495 7389 2173 1778 -273 C
ATOM 2302 OG SER A1095 -1.401 4.892 -22.030 1.00 73.51 O
ANISOU 2302 OG SER A1095 9531 9120 9280 2129 1829 -398 O
ATOM 2303 N TRP A1096 0.161 6.468 -18.234 1.00 59.15 N
ANISOU 2303 N TRP A1096 6615 8067 7793 2167 1547 -85 N
ATOM 2304 CA TRP A1096 1.022 7.335 -17.465 1.00 50.04 C
ANISOU 2304 CA TRP A1096 5023 7316 6673 2089 1474 32 C
ATOM 2305 C TRP A1096 1.654 6.575 -16.313 1.00 52.82 C
ANISOU 2305 C TRP A1096 5249 7824 6997 2422 1523 120 C
ATOM 2306 O TRP A1096 1.102 5.588 -15.814 1.00 58.65 O
ANISOU 2306 O TRP A1096 6270 8261 7753 2618 1550 76 O
ATOM 2307 CB TRP A1096 0.218 8.540 -16.977 1.00 49.34 C
ANISOU 2307 CB TRP A1096 4873 7129 6745 1662 1253 -3 C
ATOM 2308 CG TRP A1096 -0.216 9.430 -18.121 1.00 49.85 C
ANISOU 2308 CG TRP A1096 5014 7118 6807 1366 1211 -52 C
ATOM 2309 CD1 TRP A1096 -1.276 9.235 -18.969 1.00 54.76 C
ANISOU 2309 CD1 TRP A1096 5956 7410 7440 1277 1196 -156 C
ATOM 2310 CD2 TRP A1096 0.422 10.635 -18.552 1.00 51.71 C
ANISOU 2310 CD2 TRP A1096 5015 7631 7003 1114 1181 11 C
ATOM 2311 NE1 TRP A1096 -1.340 10.255 -19.903 1.00 58.76 N
ANISOU 2311 NE1 TRP A1096 6434 7971 7922 1021 1157 -155 N
ATOM 2312 CE2 TRP A1096 -0.310 11.128 -19.666 1.00 53.99 C
ANISOU 2312 CE2 TRP A1096 5512 7713 7287 914 1153 -56 C
ATOM 2313 CE3 TRP A1096 1.539 11.357 -18.103 1.00 61.70 C
ANISOU 2313 CE3 TRP A1096 5919 9313 8212 1010 1173 121 C
ATOM 2314 CZ2 TRP A1096 0.041 12.296 -20.332 1.00 54.84 C
ANISOU 2314 CZ2 TRP A1096 5514 7978 7344 641 1127 -13 C
ATOM 2315 CZ3 TRP A1096 1.890 12.540 -18.776 1.00 64.37 C
ANISOU 2315 CZ3 TRP A1096 6153 9814 8491 688 1147 155 C
ATOM 2316 CH2 TRP A1096 1.140 12.988 -19.873 1.00 59.34 C
ANISOU 2316 CH2 TRP A1096 5765 8922 7859 521 1129 89 C
ATOM 2317 N GLU A1097 2.848 7.029 -15.920 1.00 56.81 N
ANISOU 2317 N GLU A1097 5327 8826 7431 2476 1538 254 N
ATOM 2318 CA GLU A1097 3.555 6.537 -14.744 1.00 58.47 C
ANISOU 2318 CA GLU A1097 5318 9298 7600 2757 1553 369 C
ATOM 2319 C GLU A1097 2.613 6.300 -13.566 1.00 58.45 C
ANISOU 2319 C GLU A1097 5498 8964 7747 2692 1416 316 C
ATOM 2320 O GLU A1097 2.415 5.153 -13.141 1.00 57.02 O
ANISOU 2320 O GLU A1097 5587 8543 7534 2971 1472 305 O
ATOM 2321 CB GLU A1097 4.652 7.524 -14.346 1.00 58.15 C
ANISOU 2321 CB GLU A1097 4792 9805 7497 2542 1469 491 C
ATOM 2322 CG GLU A1097 5.720 6.940 -13.435 1.00 70.63 C
ANISOU 2322 CG GLU A1097 6230 11655 8952 2735 1441 611 C
ATOM 2323 CD GLU A1097 7.063 7.626 -13.602 1.00 87.18 C
ANISOU 2323 CD GLU A1097 7925 14315 10886 2595 1427 735 C
ATOM 2324 OE1 GLU A1097 7.858 7.616 -12.635 1.00 96.03 O
ANISOU 2324 OE1 GLU A1097 8834 15736 11916 2604 1346 841 O
ATOM 2325 OE2 GLU A1097 7.324 8.173 -14.702 1.00 90.19 O
ANISOU 2325 OE2 GLU A1097 8210 14848 11210 2462 1499 730 O
ATOM 2326 N TYR A1098 2.006 7.367 -13.043 1.00 49.41 N
ANISOU 2326 N TYR A1098 4275 7754 6744 2272 1219 273 N
ATOM 2327 CA TYR A1098 1.141 7.271 -11.862 1.00 45.79 C
ANISOU 2327 CA TYR A1098 3943 7036 6420 2189 1084 231 C
ATOM 2328 C TYR A1098 -0.318 7.362 -12.312 1.00 44.41 C
ANISOU 2328 C TYR A1098 4129 6380 6363 1961 1013 84 C
ATOM 2329 O TYR A1098 -0.883 8.449 -12.448 1.00 46.83 O
ANISOU 2329 O TYR A1098 4409 6627 6759 1609 884 37 O
ATOM 2330 CB TYR A1098 1.503 8.363 -10.857 1.00 45.31 C
ANISOU 2330 CB TYR A1098 3550 7262 6404 1913 926 292 C
ATOM 2331 CG TYR A1098 2.879 8.221 -10.256 1.00 47.18 C
ANISOU 2331 CG TYR A1098 3397 8028 6503 2114 972 448 C
ATOM 2332 CD1 TYR A1098 3.192 7.127 -9.467 1.00 53.95 C
ANISOU 2332 CD1 TYR A1098 4342 8860 7298 2429 1004 499 C
ATOM 2333 CD2 TYR A1098 3.857 9.179 -10.451 1.00 51.04 C
ANISOU 2333 CD2 TYR A1098 3514 8986 6894 1891 948 531 C
ATOM 2334 CE1 TYR A1098 4.437 6.973 -8.908 1.00 57.56 C
ANISOU 2334 CE1 TYR A1098 4567 9705 7597 2512 990 622 C
ATOM 2335 CE2 TYR A1098 5.138 9.028 -9.888 1.00 59.85 C
ANISOU 2335 CE2 TYR A1098 4397 10501 7843 1951 932 649 C
ATOM 2336 CZ TYR A1098 5.410 7.920 -9.115 1.00 65.24 C
ANISOU 2336 CZ TYR A1098 5187 11134 8467 2281 953 698 C
ATOM 2337 OH TYR A1098 6.642 7.731 -8.533 1.00 76.55 O
ANISOU 2337 OH TYR A1098 6394 12975 9718 2370 937 830 O
ATOM 2338 N PHE A1099 -0.934 6.209 -12.548 1.00 45.44 N
ANISOU 2338 N PHE A1099 4615 6179 6471 2161 1101 18 N
ATOM 2339 CA PHE A1099 -2.324 6.173 -13.003 1.00 45.29 C
ANISOU 2339 CA PHE A1099 4921 5762 6527 1938 1037 -112 C
ATOM 2340 C PHE A1099 -3.237 6.829 -11.975 1.00 45.29 C
ANISOU 2340 C PHE A1099 4879 5654 6676 1677 852 -141 C
ATOM 2341 O PHE A1099 -3.269 6.418 -10.804 1.00 49.57 O
ANISOU 2341 O PHE A1099 5406 6177 7252 1779 820 -110 O
ATOM 2342 CB PHE A1099 -2.736 4.722 -13.278 1.00 43.72 C
ANISOU 2342 CB PHE A1099 5130 5245 6237 2173 1172 -170 C
ATOM 2343 CG PHE A1099 -4.214 4.516 -13.500 1.00 49.43 C
ANISOU 2343 CG PHE A1099 6173 5600 7009 1921 1094 -294 C
ATOM 2344 CD1 PHE A1099 -4.928 5.310 -14.389 1.00 47.26 C
ANISOU 2344 CD1 PHE A1099 5905 5280 6770 1620 1008 -361 C
ATOM 2345 CD2 PHE A1099 -4.892 3.489 -12.818 1.00 48.50 C
ANISOU 2345 CD2 PHE A1099 6352 5200 6875 1984 1111 -333 C
ATOM 2346 CE1 PHE A1099 -6.299 5.108 -14.575 1.00 46.19 C
ANISOU 2346 CE1 PHE A1099 6017 4881 6653 1391 930 -458 C
ATOM 2347 CE2 PHE A1099 -6.241 3.274 -12.999 1.00 45.26 C
ANISOU 2347 CE2 PHE A1099 6203 4514 6480 1718 1039 -438 C
ATOM 2348 CZ PHE A1099 -6.951 4.091 -13.887 1.00 50.32 C
ANISOU 2348 CZ PHE A1099 6799 5166 7153 1423 944 -498 C
ATOM 2349 N CYS A1100 -3.946 7.873 -12.411 1.00 43.27 N
ANISOU 2349 N CYS A1100 4608 5340 6493 1366 737 -192 N
ATOM 2350 CA CYS A1100 -4.865 8.642 -11.565 1.00 44.59 C
ANISOU 2350 CA CYS A1100 4748 5411 6784 1133 574 -220 C
ATOM 2351 C CYS A1100 -4.169 9.119 -10.305 1.00 46.12 C
ANISOU 2351 C CYS A1100 4688 5822 7012 1137 512 -142 C
ATOM 2352 O CYS A1100 -4.588 8.823 -9.189 1.00 56.34 O
ANISOU 2352 O CYS A1100 6010 7033 8363 1165 455 -145 O
ATOM 2353 CB CYS A1100 -6.099 7.829 -11.189 1.00 47.65 C
ANISOU 2353 CB CYS A1100 5396 5503 7207 1129 546 -294 C
ATOM 2354 SG CYS A1100 -7.354 7.867 -12.417 1.00 45.58 S
ANISOU 2354 SG CYS A1100 5366 5031 6922 935 519 -390 S
ATOM 2355 N GLY A1101 -3.068 9.837 -10.504 1.00 46.65 N
ANISOU 2355 N GLY A1101 4507 6194 7025 1089 526 -71 N
ATOM 2356 CA GLY A1101 -2.267 10.250 -9.370 1.00 43.59 C
ANISOU 2356 CA GLY A1101 3859 6075 6627 1065 471 10 C
ATOM 2357 C GLY A1101 -2.999 11.228 -8.478 1.00 45.78 C
ANISOU 2357 C GLY A1101 4153 6242 6998 802 319 -25 C
ATOM 2358 O GLY A1101 -2.847 11.193 -7.256 1.00 50.55 O
ANISOU 2358 O GLY A1101 4663 6924 7620 817 261 8 O
ATOM 2359 N ALA A1102 -3.825 12.096 -9.084 1.00 44.06 N
ANISOU 2359 N ALA A1102 4074 5838 6828 585 260 -87 N
ATOM 2360 CA ALA A1102 -4.548 13.138 -8.357 1.00 44.03 C
ANISOU 2360 CA ALA A1102 4128 5713 6890 366 137 -117 C
ATOM 2361 C ALA A1102 -5.401 12.566 -7.234 1.00 46.17 C
ANISOU 2361 C ALA A1102 4483 5819 7241 456 86 -151 C
ATOM 2362 O ALA A1102 -5.539 13.194 -6.175 1.00 45.55 O
ANISOU 2362 O ALA A1102 4373 5746 7187 345 3 -148 O
ATOM 2363 CB ALA A1102 -5.420 13.931 -9.325 1.00 37.65 C
ANISOU 2363 CB ALA A1102 3495 4711 6100 220 108 -167 C
ATOM 2364 N VAL A1103 -5.960 11.373 -7.440 1.00 41.14 N
ANISOU 2364 N VAL A1103 3975 5032 6623 639 141 -184 N
ATOM 2365 CA VAL A1103 -6.756 10.718 -6.407 1.00 35.88 C
ANISOU 2365 CA VAL A1103 3402 4219 6012 708 106 -210 C
ATOM 2366 C VAL A1103 -5.925 10.497 -5.152 1.00 39.65 C
ANISOU 2366 C VAL A1103 3722 4870 6472 797 93 -144 C
ATOM 2367 O VAL A1103 -6.275 10.980 -4.067 1.00 37.09 O
ANISOU 2367 O VAL A1103 3374 4531 6189 701 7 -149 O
ATOM 2368 CB VAL A1103 -7.336 9.404 -6.943 1.00 36.03 C
ANISOU 2368 CB VAL A1103 3623 4055 6010 851 186 -251 C
ATOM 2369 CG1 VAL A1103 -7.878 8.567 -5.788 1.00 41.83 C
ANISOU 2369 CG1 VAL A1103 4448 4674 6770 929 172 -258 C
ATOM 2370 CG2 VAL A1103 -8.414 9.717 -7.977 1.00 32.40 C
ANISOU 2370 CG2 VAL A1103 3304 3445 5560 709 161 -319 C
ATOM 2371 N ASP A1104 -4.800 9.779 -5.297 1.00 39.77 N
ANISOU 2371 N ASP A1104 3626 5077 6408 996 183 -74 N
ATOM 2372 CA ASP A1104 -3.819 9.605 -4.221 1.00 41.59 C
ANISOU 2372 CA ASP A1104 3651 5567 6586 1102 172 16 C
ATOM 2373 C ASP A1104 -3.444 10.922 -3.536 1.00 42.75 C
ANISOU 2373 C ASP A1104 3614 5903 6726 834 59 37 C
ATOM 2374 O ASP A1104 -3.317 10.986 -2.311 1.00 46.52 O
ANISOU 2374 O ASP A1104 4013 6466 7197 815 -7 67 O
ATOM 2375 CB ASP A1104 -2.553 8.964 -4.788 1.00 49.52 C
ANISOU 2375 CB ASP A1104 4505 6836 7473 1347 291 106 C
ATOM 2376 CG ASP A1104 -2.758 7.527 -5.227 1.00 60.90 C
ANISOU 2376 CG ASP A1104 6179 8081 8880 1662 424 98 C
ATOM 2377 OD1 ASP A1104 -2.911 6.658 -4.337 1.00 66.62 O
ANISOU 2377 OD1 ASP A1104 7002 8715 9595 1848 440 125 O
ATOM 2378 OD2 ASP A1104 -2.748 7.270 -6.459 1.00 55.70 O
ANISOU 2378 OD2 ASP A1104 5632 7346 8185 1717 519 65 O
ATOM 2379 N ALA A1105 -3.211 11.970 -4.320 1.00 44.48 N
ANISOU 2379 N ALA A1105 3790 6190 6922 614 42 23 N
ATOM 2380 CA ALA A1105 -2.833 13.260 -3.761 1.00 36.90 C
ANISOU 2380 CA ALA A1105 2728 5373 5920 315 -51 35 C
ATOM 2381 C ALA A1105 -3.923 13.787 -2.832 1.00 39.00 C
ANISOU 2381 C ALA A1105 3171 5383 6265 194 -144 -34 C
ATOM 2382 O ALA A1105 -3.648 14.182 -1.689 1.00 40.34 O
ANISOU 2382 O ALA A1105 3270 5661 6397 84 -214 -15 O
ATOM 2383 CB ALA A1105 -2.553 14.240 -4.907 1.00 37.83 C
ANISOU 2383 CB ALA A1105 2857 5528 5990 98 -35 26 C
ATOM 2384 N ILE A1106 -5.173 13.784 -3.316 1.00 39.23 N
ANISOU 2384 N ILE A1106 3422 5100 6385 219 -141 -110 N
ATOM 2385 CA ILE A1106 -6.319 14.205 -2.516 1.00 40.87 C
ANISOU 2385 CA ILE A1106 3788 5085 6656 159 -210 -168 C
ATOM 2386 C ILE A1106 -6.536 13.271 -1.327 1.00 44.79 C
ANISOU 2386 C ILE A1106 4258 5577 7182 307 -223 -157 C
ATOM 2387 O ILE A1106 -6.725 13.732 -0.193 1.00 40.57 O
ANISOU 2387 O ILE A1106 3735 5037 6644 222 -287 -166 O
ATOM 2388 CB ILE A1106 -7.577 14.273 -3.389 1.00 39.59 C
ANISOU 2388 CB ILE A1106 3812 4676 6556 185 -198 -228 C
ATOM 2389 CG1 ILE A1106 -7.332 15.194 -4.574 1.00 37.57 C
ANISOU 2389 CG1 ILE A1106 3598 4421 6257 53 -183 -226 C
ATOM 2390 CG2 ILE A1106 -8.798 14.682 -2.552 1.00 33.56 C
ANISOU 2390 CG2 ILE A1106 3177 3736 5839 163 -256 -273 C
ATOM 2391 CD1 ILE A1106 -8.383 15.042 -5.596 1.00 43.98 C
ANISOU 2391 CD1 ILE A1106 4545 5063 7104 114 -165 -264 C
ATOM 2392 N GLU A1107 -6.524 11.948 -1.555 1.00 31.61 N
ANISOU 2392 N GLU A1107 2593 3891 5527 529 -154 -139 N
ATOM 2393 CA GLU A1107 -6.764 11.041 -0.423 1.00 34.70 C
ANISOU 2393 CA GLU A1107 3006 4249 5931 667 -159 -122 C
ATOM 2394 C GLU A1107 -5.772 11.306 0.701 1.00 35.61 C
ANISOU 2394 C GLU A1107 2936 4616 5980 642 -209 -53 C
ATOM 2395 O GLU A1107 -6.146 11.285 1.875 1.00 42.64 O
ANISOU 2395 O GLU A1107 3852 5469 6880 625 -262 -58 O
ATOM 2396 CB GLU A1107 -6.714 9.552 -0.833 1.00 31.37 C
ANISOU 2396 CB GLU A1107 2669 3757 5492 915 -59 -100 C
ATOM 2397 CG GLU A1107 -7.618 9.138 -1.973 1.00 41.33 C
ANISOU 2397 CG GLU A1107 4125 4796 6783 913 -7 -168 C
ATOM 2398 CD GLU A1107 -7.825 7.630 -2.057 1.00 58.98 C
ANISOU 2398 CD GLU A1107 6547 6883 8979 1106 87 -165 C
ATOM 2399 OE1 GLU A1107 -8.845 7.145 -1.509 1.00 69.80 O
ANISOU 2399 OE1 GLU A1107 8071 8077 10371 1064 69 -203 O
ATOM 2400 OE2 GLU A1107 -6.993 6.927 -2.674 1.00 63.66 O
ANISOU 2400 OE2 GLU A1107 7159 7529 9501 1297 188 -124 O
ATOM 2401 N GLU A1108 -4.514 11.597 0.358 1.00 36.18 N
ANISOU 2401 N GLU A1108 2806 4976 5965 616 -197 15 N
ATOM 2402 CA GLU A1108 -3.483 11.834 1.366 1.00 36.61 C
ANISOU 2402 CA GLU A1108 2641 5351 5919 565 -252 94 C
ATOM 2403 C GLU A1108 -3.701 13.149 2.088 1.00 41.00 C
ANISOU 2403 C GLU A1108 3234 5890 6456 245 -355 45 C
ATOM 2404 O GLU A1108 -3.371 13.278 3.271 1.00 39.82 O
ANISOU 2404 O GLU A1108 3000 5886 6242 180 -421 77 O
ATOM 2405 CB GLU A1108 -2.093 11.843 0.718 1.00 43.25 C
ANISOU 2405 CB GLU A1108 3222 6568 6643 594 -208 187 C
ATOM 2406 CG GLU A1108 -0.936 12.231 1.643 1.00 38.79 C
ANISOU 2406 CG GLU A1108 2372 6434 5934 478 -278 282 C
ATOM 2407 CD GLU A1108 -0.736 11.253 2.803 1.00 55.61 C
ANISOU 2407 CD GLU A1108 4424 8679 8028 732 -290 361 C
ATOM 2408 OE1 GLU A1108 -1.144 10.061 2.713 1.00 52.07 O
ANISOU 2408 OE1 GLU A1108 4108 8042 7634 1065 -209 373 O
ATOM 2409 OE2 GLU A1108 -0.166 11.687 3.827 1.00 61.68 O
ANISOU 2409 OE2 GLU A1108 5021 9722 8692 582 -381 412 O
ATOM 2410 N LYS A1109 -4.210 14.159 1.391 1.00 38.64 N
ANISOU 2410 N LYS A1109 3081 5415 6186 45 -364 -26 N
ATOM 2411 CA LYS A1109 -4.413 15.415 2.084 1.00 35.66 C
ANISOU 2411 CA LYS A1109 2811 4976 5761 -237 -442 -73 C
ATOM 2412 C LYS A1109 -5.580 15.288 3.032 1.00 38.48 C
ANISOU 2412 C LYS A1109 3342 5086 6194 -164 -470 -132 C
ATOM 2413 O LYS A1109 -5.473 15.654 4.204 1.00 42.82 O
ANISOU 2413 O LYS A1109 3899 5688 6682 -274 -530 -136 O
ATOM 2414 CB LYS A1109 -4.630 16.553 1.098 1.00 41.95 C
ANISOU 2414 CB LYS A1109 3765 5630 6544 -439 -431 -121 C
ATOM 2415 CG LYS A1109 -4.773 17.865 1.801 1.00 46.39 C
ANISOU 2415 CG LYS A1109 4509 6095 7023 -721 -490 -168 C
ATOM 2416 CD LYS A1109 -4.272 19.035 0.996 1.00 49.15 C
ANISOU 2416 CD LYS A1109 4957 6450 7268 -1005 -483 -172 C
ATOM 2417 CE LYS A1109 -4.042 20.194 1.935 1.00 50.94 C
ANISOU 2417 CE LYS A1109 5355 6650 7350 -1327 -541 -205 C
ATOM 2418 NZ LYS A1109 -3.681 21.417 1.168 1.00 60.33 N
ANISOU 2418 NZ LYS A1109 6738 7769 8416 -1634 -524 -217 N
ATOM 2419 N LEU A1110 -6.703 14.742 2.539 1.00 41.46 N
ANISOU 2419 N LEU A1110 3852 5218 6683 8 -426 -175 N
ATOM 2420 CA LEU A1110 -7.855 14.489 3.395 1.00 31.63 C
ANISOU 2420 CA LEU A1110 2736 3785 5498 88 -441 -220 C
ATOM 2421 C LEU A1110 -7.460 13.664 4.610 1.00 34.40 C
ANISOU 2421 C LEU A1110 2983 4269 5820 181 -463 -171 C
ATOM 2422 O LEU A1110 -7.896 13.943 5.736 1.00 39.53 O
ANISOU 2422 O LEU A1110 3698 4870 6453 130 -506 -196 O
ATOM 2423 CB LEU A1110 -8.959 13.789 2.610 1.00 30.01 C
ANISOU 2423 CB LEU A1110 2627 3391 5384 238 -389 -252 C
ATOM 2424 CG LEU A1110 -9.576 14.525 1.420 1.00 32.38 C
ANISOU 2424 CG LEU A1110 3036 3560 5707 183 -372 -292 C
ATOM 2425 CD1 LEU A1110 -10.529 13.605 0.665 1.00 30.27 C
ANISOU 2425 CD1 LEU A1110 2820 3182 5499 312 -329 -312 C
ATOM 2426 CD2 LEU A1110 -10.272 15.789 1.828 1.00 30.56 C
ANISOU 2426 CD2 LEU A1110 2955 3204 5452 82 -406 -335 C
ATOM 2427 N LYS A1111 -6.606 12.671 4.419 1.00 34.11 N
ANISOU 2427 N LYS A1111 2794 4407 5760 336 -429 -95 N
ATOM 2428 CA LYS A1111 -6.164 11.885 5.564 1.00 40.04 C
ANISOU 2428 CA LYS A1111 3452 5300 6461 458 -448 -28 C
ATOM 2429 C LYS A1111 -5.301 12.728 6.523 1.00 44.41 C
ANISOU 2429 C LYS A1111 3870 6105 6897 260 -535 4 C
ATOM 2430 O LYS A1111 -5.459 12.644 7.742 1.00 39.01 O
ANISOU 2430 O LYS A1111 3202 5442 6178 249 -583 11 O
ATOM 2431 CB LYS A1111 -5.440 10.640 5.051 1.00 40.80 C
ANISOU 2431 CB LYS A1111 3451 5518 6533 724 -371 59 C
ATOM 2432 CG LYS A1111 -4.880 9.710 6.115 1.00 49.96 C
ANISOU 2432 CG LYS A1111 4525 6838 7619 922 -375 157 C
ATOM 2433 CD LYS A1111 -4.411 8.390 5.456 1.00 57.27 C
ANISOU 2433 CD LYS A1111 5461 7781 8517 1252 -263 234 C
ATOM 2434 CE LYS A1111 -5.533 7.739 4.626 1.00 45.53 C
ANISOU 2434 CE LYS A1111 4253 5922 7123 1313 -181 152 C
ATOM 2435 NZ LYS A1111 -5.088 6.517 3.947 1.00 47.91 N
ANISOU 2435 NZ LYS A1111 4641 6191 7373 1612 -58 211 N
ATOM 2436 N ASN A1112 -4.408 13.572 5.997 1.00 48.32 N
ANISOU 2436 N ASN A1112 4248 6800 7311 66 -557 21 N
ATOM 2437 CA ASN A1112 -3.602 14.426 6.866 1.00 42.24 C
ANISOU 2437 CA ASN A1112 3372 6282 6395 -197 -645 43 C
ATOM 2438 C ASN A1112 -4.477 15.373 7.672 1.00 46.38 C
ANISOU 2438 C ASN A1112 4144 6559 6918 -396 -692 -57 C
ATOM 2439 O ASN A1112 -4.194 15.641 8.844 1.00 46.02 O
ANISOU 2439 O ASN A1112 4079 6639 6769 -525 -761 -48 O
ATOM 2440 CB ASN A1112 -2.601 15.238 6.042 1.00 44.38 C
ANISOU 2440 CB ASN A1112 3513 6788 6563 -434 -651 70 C
ATOM 2441 CG ASN A1112 -1.474 14.397 5.477 1.00 59.73 C
ANISOU 2441 CG ASN A1112 5146 9100 8448 -248 -608 192 C
ATOM 2442 OD1 ASN A1112 -0.505 14.944 4.959 1.00 69.02 O
ANISOU 2442 OD1 ASN A1112 6145 10572 9506 -440 -616 238 O
ATOM 2443 ND2 ASN A1112 -1.596 13.067 5.555 1.00 60.07 N
ANISOU 2443 ND2 ASN A1112 5143 9128 8553 130 -551 249 N
ATOM 2444 N LEU A1113 -5.535 15.905 7.050 1.00 43.67 N
ANISOU 2444 N LEU A1113 4040 5883 6669 -408 -652 -146 N
ATOM 2445 CA LEU A1113 -6.509 16.790 7.674 1.00 40.31 C
ANISOU 2445 CA LEU A1113 3882 5195 6240 -515 -667 -237 C
ATOM 2446 C LEU A1113 -7.462 16.075 8.626 1.00 47.67 C
ANISOU 2446 C LEU A1113 4871 6002 7238 -325 -661 -254 C
ATOM 2447 O LEU A1113 -8.402 16.705 9.127 1.00 48.23 O
ANISOU 2447 O LEU A1113 5152 5864 7308 -354 -655 -325 O
ATOM 2448 CB LEU A1113 -7.333 17.504 6.600 1.00 35.56 C
ANISOU 2448 CB LEU A1113 3488 4324 5701 -519 -615 -300 C
ATOM 2449 CG LEU A1113 -6.618 18.527 5.721 1.00 38.74 C
ANISOU 2449 CG LEU A1113 3942 4761 6016 -758 -614 -302 C
ATOM 2450 CD1 LEU A1113 -7.566 19.006 4.630 1.00 43.23 C
ANISOU 2450 CD1 LEU A1113 4712 5056 6659 -676 -557 -345 C
ATOM 2451 CD2 LEU A1113 -6.096 19.656 6.546 1.00 38.55 C
ANISOU 2451 CD2 LEU A1113 4060 4768 5819 -1077 -665 -332 C
ATOM 2452 N GLY A1114 -7.269 14.787 8.871 1.00 44.74 N
ANISOU 2452 N GLY A1114 4341 5748 6909 -122 -651 -186 N
ATOM 2453 CA GLY A1114 -8.070 14.122 9.871 1.00 36.54 C
ANISOU 2453 CA GLY A1114 3367 4612 5904 11 -647 -194 C
ATOM 2454 C GLY A1114 -9.479 13.849 9.410 1.00 39.14 C
ANISOU 2454 C GLY A1114 3843 4681 6348 135 -586 -250 C
ATOM 2455 O GLY A1114 -10.417 13.922 10.208 1.00 45.11 O
ANISOU 2455 O GLY A1114 4709 5322 7108 154 -582 -289 O
ATOM 2456 N ALA A1115 -9.654 13.545 8.139 1.00 42.77 N
ANISOU 2456 N ALA A1115 4294 5076 6882 209 -538 -250 N
ATOM 2457 CA ALA A1115 -10.952 13.192 7.599 1.00 41.09 C
ANISOU 2457 CA ALA A1115 4183 4677 6752 303 -488 -291 C
ATOM 2458 C ALA A1115 -11.055 11.671 7.582 1.00 42.21 C
ANISOU 2458 C ALA A1115 4297 4815 6926 457 -447 -246 C
ATOM 2459 O ALA A1115 -10.049 10.968 7.668 1.00 42.60 O
ANISOU 2459 O ALA A1115 4256 4987 6943 540 -441 -179 O
ATOM 2460 CB ALA A1115 -11.134 13.805 6.205 1.00 29.32 C
ANISOU 2460 CB ALA A1115 2730 3114 5296 268 -465 -320 C
ATOM 2461 N GLU A1116 -12.290 11.165 7.540 1.00 48.80 N
ANISOU 2461 N GLU A1116 5223 5520 7799 494 -412 -277 N
ATOM 2462 CA GLU A1116 -12.561 9.732 7.686 1.00 46.24 C
ANISOU 2462 CA GLU A1116 4951 5144 7475 590 -366 -244 C
ATOM 2463 C GLU A1116 -12.850 9.180 6.300 1.00 39.73 C
ANISOU 2463 C GLU A1116 4180 4236 6679 611 -313 -259 C
ATOM 2464 O GLU A1116 -13.951 9.351 5.770 1.00 40.80 O
ANISOU 2464 O GLU A1116 4360 4309 6834 543 -304 -306 O
ATOM 2465 CB GLU A1116 -13.717 9.479 8.651 1.00 40.07 C
ANISOU 2465 CB GLU A1116 4239 4306 6678 559 -361 -263 C
ATOM 2466 CG GLU A1116 -14.172 8.021 8.746 1.00 48.57 C
ANISOU 2466 CG GLU A1116 5428 5296 7731 598 -305 -236 C
ATOM 2467 CD GLU A1116 -13.162 7.104 9.426 1.00 66.02 C
ANISOU 2467 CD GLU A1116 7670 7523 9890 727 -291 -157 C
ATOM 2468 OE1 GLU A1116 -13.256 5.873 9.220 1.00 58.05 O
ANISOU 2468 OE1 GLU A1116 6812 6400 8844 791 -225 -127 O
ATOM 2469 OE2 GLU A1116 -12.283 7.604 10.168 1.00 79.53 O
ANISOU 2469 OE2 GLU A1116 9275 9366 11577 763 -342 -121 O
ATOM 2470 N ILE A1117 -11.850 8.528 5.709 1.00 41.95 N
ANISOU 2470 N ILE A1117 4452 4543 6944 714 -275 -215 N
ATOM 2471 CA ILE A1117 -11.950 8.028 4.337 1.00 39.28 C
ANISOU 2471 CA ILE A1117 4187 4124 6613 737 -216 -234 C
ATOM 2472 C ILE A1117 -12.696 6.694 4.325 1.00 41.03 C
ANISOU 2472 C ILE A1117 4603 4190 6796 754 -152 -240 C
ATOM 2473 O ILE A1117 -12.480 5.789 5.146 1.00 41.18 O
ANISOU 2473 O ILE A1117 4715 4163 6767 845 -121 -193 O
ATOM 2474 CB ILE A1117 -10.550 7.926 3.698 1.00 34.70 C
ANISOU 2474 CB ILE A1117 3523 3651 6009 858 -184 -182 C
ATOM 2475 CG1 ILE A1117 -9.972 9.311 3.485 1.00 34.05 C
ANISOU 2475 CG1 ILE A1117 3280 3714 5943 753 -245 -189 C
ATOM 2476 CG2 ILE A1117 -10.598 7.297 2.392 1.00 28.85 C
ANISOU 2476 CG2 ILE A1117 2890 2814 5256 904 -110 -201 C
ATOM 2477 CD1 ILE A1117 -8.578 9.273 2.897 1.00 46.92 C
ANISOU 2477 CD1 ILE A1117 4780 5520 7528 840 -215 -128 C
ATOM 2478 N VAL A1118 -13.578 6.564 3.355 1.00 41.99 N
ANISOU 2478 N VAL A1118 4806 4231 6917 648 -132 -293 N
ATOM 2479 CA VAL A1118 -14.708 5.662 3.464 1.00 38.18 C
ANISOU 2479 CA VAL A1118 4488 3638 6380 538 -100 -319 C
ATOM 2480 C VAL A1118 -14.682 4.578 2.404 1.00 41.40 C
ANISOU 2480 C VAL A1118 5113 3901 6717 531 -18 -336 C
ATOM 2481 O VAL A1118 -15.259 3.502 2.626 1.00 42.50 O
ANISOU 2481 O VAL A1118 5471 3906 6770 452 34 -343 O
ATOM 2482 CB VAL A1118 -16.017 6.488 3.400 1.00 33.41 C
ANISOU 2482 CB VAL A1118 3780 3121 5795 374 -158 -363 C
ATOM 2483 CG1 VAL A1118 -16.954 6.033 2.298 1.00 35.18 C
ANISOU 2483 CG1 VAL A1118 4087 3319 5959 223 -138 -404 C
ATOM 2484 CG2 VAL A1118 -16.675 6.606 4.781 1.00 29.53 C
ANISOU 2484 CG2 VAL A1118 3246 2681 5294 335 -186 -351 C
ATOM 2485 N GLN A1119 -14.004 4.820 1.284 1.00 38.52 N
ANISOU 2485 N GLN A1119 4722 3548 6366 601 5 -345 N
ATOM 2486 CA GLN A1119 -13.659 3.827 0.280 1.00 43.01 C
ANISOU 2486 CA GLN A1119 5516 3973 6854 655 102 -357 C
ATOM 2487 C GLN A1119 -12.276 4.164 -0.231 1.00 38.93 C
ANISOU 2487 C GLN A1119 4887 3542 6361 865 134 -316 C
ATOM 2488 O GLN A1119 -11.810 5.297 -0.089 1.00 41.05 O
ANISOU 2488 O GLN A1119 4906 3984 6706 874 64 -297 O
ATOM 2489 CB GLN A1119 -14.623 3.825 -0.910 1.00 53.56 C
ANISOU 2489 CB GLN A1119 6927 5275 8147 447 98 -428 C
ATOM 2490 CG GLN A1119 -15.895 3.073 -0.688 1.00 53.80 C
ANISOU 2490 CG GLN A1119 7130 5227 8086 215 101 -464 C
ATOM 2491 CD GLN A1119 -15.718 1.608 -0.891 1.00 52.90 C
ANISOU 2491 CD GLN A1119 7397 4869 7835 219 217 -474 C
ATOM 2492 OE1 GLN A1119 -15.393 1.152 -1.985 1.00 66.66 O
ANISOU 2492 OE1 GLN A1119 9321 6500 9505 238 288 -507 O
ATOM 2493 NE2 GLN A1119 -15.915 0.855 0.159 1.00 42.63 N
ANISOU 2493 NE2 GLN A1119 6256 3461 6480 207 249 -446 N
ATOM 2494 N ASP A1120 -11.620 3.172 -0.832 1.00 44.20 N
ANISOU 2494 N ASP A1120 5760 4092 6941 1027 248 -300 N
ATOM 2495 CA ASP A1120 -10.450 3.480 -1.630 1.00 40.43 C
ANISOU 2495 CA ASP A1120 5167 3730 6463 1202 292 -268 C
ATOM 2496 C ASP A1120 -10.929 4.134 -2.909 1.00 32.50 C
ANISOU 2496 C ASP A1120 4124 2742 5482 1026 265 -337 C
ATOM 2497 O ASP A1120 -12.002 3.822 -3.425 1.00 37.75 O
ANISOU 2497 O ASP A1120 4953 3281 6109 837 261 -405 O
ATOM 2498 CB ASP A1120 -9.614 2.228 -1.922 1.00 48.13 C
ANISOU 2498 CB ASP A1120 6387 4585 7316 1480 443 -223 C
ATOM 2499 CG ASP A1120 -8.140 2.559 -2.228 1.00 70.50 C
ANISOU 2499 CG ASP A1120 8998 7652 10137 1742 487 -142 C
ATOM 2500 OD1 ASP A1120 -7.392 2.879 -1.278 1.00 75.69 O
ANISOU 2500 OD1 ASP A1120 9427 8518 10813 1869 444 -56 O
ATOM 2501 OD2 ASP A1120 -7.726 2.514 -3.414 1.00 79.78 O
ANISOU 2501 OD2 ASP A1120 10211 8836 11267 1805 562 -161 O
ATOM 2502 N GLY A1121 -10.134 5.069 -3.402 1.00 34.21 N
ANISOU 2502 N GLY A1121 4115 3139 5743 1070 242 -313 N
ATOM 2503 CA GLY A1121 -10.561 5.898 -4.512 1.00 37.76 C
ANISOU 2503 CA GLY A1121 4503 3624 6219 907 201 -364 C
ATOM 2504 C GLY A1121 -10.916 5.109 -5.756 1.00 38.07 C
ANISOU 2504 C GLY A1121 4784 3514 6165 874 283 -420 C
ATOM 2505 O GLY A1121 -10.446 4.004 -5.992 1.00 36.50 O
ANISOU 2505 O GLY A1121 4803 3193 5873 1029 402 -415 O
ATOM 2506 N LEU A1122 -11.760 5.715 -6.577 1.00 44.08 N
ANISOU 2506 N LEU A1122 5525 4289 6936 677 223 -471 N
ATOM 2507 CA LEU A1122 -12.164 5.134 -7.848 1.00 41.27 C
ANISOU 2507 CA LEU A1122 5377 3826 6476 592 280 -530 C
ATOM 2508 C LEU A1122 -11.306 5.748 -8.952 1.00 47.86 C
ANISOU 2508 C LEU A1122 6115 4763 7308 664 314 -517 C
ATOM 2509 O LEU A1122 -11.266 6.979 -9.112 1.00 46.52 O
ANISOU 2509 O LEU A1122 5730 4735 7210 600 234 -494 O
ATOM 2510 CB LEU A1122 -13.650 5.382 -8.096 1.00 35.72 C
ANISOU 2510 CB LEU A1122 4686 3133 5753 327 186 -579 C
ATOM 2511 CG LEU A1122 -14.257 5.107 -9.465 1.00 36.83 C
ANISOU 2511 CG LEU A1122 4974 3240 5778 164 199 -637 C
ATOM 2512 CD1 LEU A1122 -14.410 3.601 -9.746 1.00 37.02 C
ANISOU 2512 CD1 LEU A1122 5370 3050 5647 107 307 -694 C
ATOM 2513 CD2 LEU A1122 -15.599 5.896 -9.575 1.00 35.43 C
ANISOU 2513 CD2 LEU A1122 4638 3217 5605 -48 68 -642 C
ATOM 2514 N ARG A1123 -10.616 4.893 -9.701 1.00 44.49 N
ANISOU 2514 N ARG A1123 5873 4252 6779 803 446 -528 N
ATOM 2515 CA ARG A1123 -9.752 5.323 -10.794 1.00 40.43 C
ANISOU 2515 CA ARG A1123 5282 3843 6235 883 503 -514 C
ATOM 2516 C ARG A1123 -10.270 4.739 -12.100 1.00 40.05 C
ANISOU 2516 C ARG A1123 5497 3659 6060 780 563 -590 C
ATOM 2517 O ARG A1123 -10.119 3.538 -12.335 1.00 40.38 O
ANISOU 2517 O ARG A1123 5841 3521 5979 880 688 -624 O
ATOM 2518 CB ARG A1123 -8.320 4.874 -10.544 1.00 42.49 C
ANISOU 2518 CB ARG A1123 5497 4188 6461 1188 625 -444 C
ATOM 2519 CG ARG A1123 -7.859 5.076 -9.139 1.00 37.07 C
ANISOU 2519 CG ARG A1123 4615 3618 5852 1292 577 -370 C
ATOM 2520 CD ARG A1123 -6.496 4.447 -8.957 1.00 40.00 C
ANISOU 2520 CD ARG A1123 4946 4106 6146 1627 707 -287 C
ATOM 2521 NE ARG A1123 -6.151 4.377 -7.545 1.00 49.73 N
ANISOU 2521 NE ARG A1123 6043 5433 7421 1738 665 -214 N
ATOM 2522 CZ ARG A1123 -5.276 5.166 -6.935 1.00 49.22 C
ANISOU 2522 CZ ARG A1123 5641 5666 7393 1772 609 -130 C
ATOM 2523 NH1 ARG A1123 -4.618 6.099 -7.618 1.00 43.11 N
ANISOU 2523 NH1 ARG A1123 4636 5125 6620 1693 595 -107 N
ATOM 2524 NH2 ARG A1123 -5.060 5.013 -5.634 1.00 57.83 N
ANISOU 2524 NH2 ARG A1123 6639 6830 8503 1858 565 -69 N
ATOM 2525 N ILE A1124 -10.846 5.576 -12.960 1.00 38.41 N
ANISOU 2525 N ILE A1124 5204 3530 5860 591 481 -614 N
ATOM 2526 CA ILE A1124 -11.362 5.140 -14.251 1.00 41.02 C
ANISOU 2526 CA ILE A1124 5756 3774 6054 458 518 -684 C
ATOM 2527 C ILE A1124 -10.247 5.178 -15.280 1.00 46.13 C
ANISOU 2527 C ILE A1124 6420 4470 6639 616 637 -672 C
ATOM 2528 O ILE A1124 -9.506 6.161 -15.359 1.00 45.87 O
ANISOU 2528 O ILE A1124 6129 4618 6681 681 616 -610 O
ATOM 2529 CB ILE A1124 -12.526 6.029 -14.714 1.00 40.22 C
ANISOU 2529 CB ILE A1124 5538 3776 5967 207 371 -697 C
ATOM 2530 CG1 ILE A1124 -13.670 5.968 -13.736 1.00 39.72 C
ANISOU 2530 CG1 ILE A1124 5436 3713 5941 63 267 -702 C
ATOM 2531 CG2 ILE A1124 -12.952 5.686 -16.154 1.00 43.19 C
ANISOU 2531 CG2 ILE A1124 6109 4117 6184 60 399 -758 C
ATOM 2532 CD1 ILE A1124 -13.887 7.317 -13.170 1.00 45.32 C
ANISOU 2532 CD1 ILE A1124 5852 4582 6784 69 149 -639 C
ATOM 2533 N ASP A1125 -10.154 4.130 -16.104 1.00 49.49 N
ANISOU 2533 N ASP A1125 7166 4735 6902 654 766 -734 N
ATOM 2534 CA ASP A1125 -9.211 4.079 -17.216 1.00 48.29 C
ANISOU 2534 CA ASP A1125 7066 4627 6656 801 896 -733 C
ATOM 2535 C ASP A1125 -9.946 4.388 -18.511 1.00 47.39 C
ANISOU 2535 C ASP A1125 7043 4514 6450 557 848 -794 C
ATOM 2536 O ASP A1125 -10.908 3.702 -18.855 1.00 61.28 O
ANISOU 2536 O ASP A1125 9071 6123 8091 358 832 -874 O
ATOM 2537 CB ASP A1125 -8.572 2.705 -17.269 1.00 50.95 C
ANISOU 2537 CB ASP A1125 7740 4772 6847 1053 1095 -759 C
ATOM 2538 CG ASP A1125 -7.340 2.660 -18.097 1.00 62.59 C
ANISOU 2538 CG ASP A1125 9196 6349 8236 1315 1255 -726 C
ATOM 2539 OD1 ASP A1125 -6.994 3.681 -18.718 1.00 63.85 O
ANISOU 2539 OD1 ASP A1125 9090 6728 8443 1252 1209 -691 O
ATOM 2540 OD2 ASP A1125 -6.718 1.571 -18.109 1.00 71.42 O
ANISOU 2540 OD2 ASP A1125 10589 7326 9222 1597 1439 -731 O
ATOM 2541 N GLY A1126 -9.524 5.437 -19.209 1.00 48.03 N
ANISOU 2541 N GLY A1126 6903 4781 6567 544 817 -750 N
ATOM 2542 CA GLY A1126 -10.129 5.805 -20.474 1.00 46.97 C
ANISOU 2542 CA GLY A1126 6838 4675 6335 342 771 -790 C
ATOM 2543 C GLY A1126 -11.491 6.468 -20.418 1.00 53.46 C
ANISOU 2543 C GLY A1126 7564 5556 7192 76 581 -791 C
ATOM 2544 O GLY A1126 -11.764 7.320 -19.563 1.00 67.10 O
ANISOU 2544 O GLY A1126 9051 7379 9066 62 466 -730 O
ATOM 2545 N ASP A1127 -12.351 6.087 -21.353 1.00 57.31 N
ANISOU 2545 N ASP A1127 8245 6008 7524 -130 553 -856 N
ATOM 2546 CA ASP A1127 -13.659 6.710 -21.497 1.00 51.20 C
ANISOU 2546 CA ASP A1127 7353 5363 6736 -365 378 -840 C
ATOM 2547 C ASP A1127 -14.588 6.193 -20.404 1.00 56.47 C
ANISOU 2547 C ASP A1127 8030 5994 7431 -477 304 -859 C
ATOM 2548 O ASP A1127 -14.856 4.982 -20.352 1.00 48.88 O
ANISOU 2548 O ASP A1127 7351 4876 6346 -579 370 -939 O
ATOM 2549 CB ASP A1127 -14.233 6.420 -22.877 1.00 52.71 C
ANISOU 2549 CB ASP A1127 7730 5581 6718 -567 369 -896 C
ATOM 2550 CG ASP A1127 -15.576 7.109 -23.128 1.00 64.75 C
ANISOU 2550 CG ASP A1127 9091 7315 8196 -782 182 -857 C
ATOM 2551 OD1 ASP A1127 -15.720 8.315 -22.847 1.00 67.87 O
ANISOU 2551 OD1 ASP A1127 9218 7855 8714 -702 84 -762 O
ATOM 2552 OD2 ASP A1127 -16.498 6.434 -23.628 1.00 70.78 O
ANISOU 2552 OD2 ASP A1127 10009 8111 8774 -1034 139 -916 O
ATOM 2553 N PRO A1128 -15.090 7.063 -19.518 1.00 54.29 N
ANISOU 2553 N PRO A1128 7485 5846 7296 -466 180 -790 N
ATOM 2554 CA PRO A1128 -15.885 6.577 -18.380 1.00 46.47 C
ANISOU 2554 CA PRO A1128 6483 4837 6335 -552 125 -801 C
ATOM 2555 C PRO A1128 -17.206 5.979 -18.795 1.00 52.68 C
ANISOU 2555 C PRO A1128 7375 5701 6940 -855 51 -848 C
ATOM 2556 O PRO A1128 -17.785 5.203 -18.026 1.00 59.86 O
ANISOU 2556 O PRO A1128 8373 6558 7812 -983 45 -881 O
ATOM 2557 CB PRO A1128 -16.083 7.837 -17.523 1.00 43.14 C
ANISOU 2557 CB PRO A1128 5748 4560 6084 -450 18 -710 C
ATOM 2558 CG PRO A1128 -15.925 8.982 -18.473 1.00 45.44 C
ANISOU 2558 CG PRO A1128 5924 4970 6371 -412 -24 -655 C
ATOM 2559 CD PRO A1128 -14.997 8.536 -19.563 1.00 47.85 C
ANISOU 2559 CD PRO A1128 6405 5185 6591 -383 95 -698 C
ATOM 2560 N ARG A1129 -17.711 6.345 -19.974 1.00 55.24 N
ANISOU 2560 N ARG A1129 7680 6175 7133 -993 -11 -845 N
ATOM 2561 CA ARG A1129 -18.907 5.724 -20.526 1.00 49.65 C
ANISOU 2561 CA ARG A1129 7072 5590 6204 -1325 -82 -890 C
ATOM 2562 C ARG A1129 -18.702 4.243 -20.773 1.00 46.98 C
ANISOU 2562 C ARG A1129 7153 5000 5696 -1489 43 -1009 C
ATOM 2563 O ARG A1129 -19.643 3.453 -20.636 1.00 53.14 O
ANISOU 2563 O ARG A1129 8067 5813 6311 -1798 4 -1058 O
ATOM 2564 CB ARG A1129 -19.291 6.425 -21.822 1.00 50.02 C
ANISOU 2564 CB ARG A1129 7026 5848 6130 -1403 -163 -855 C
ATOM 2565 CG ARG A1129 -20.091 7.669 -21.621 1.00 50.38 C
ANISOU 2565 CG ARG A1129 6714 6194 6236 -1338 -314 -735 C
ATOM 2566 CD ARG A1129 -20.239 8.453 -22.887 1.00 52.37 C
ANISOU 2566 CD ARG A1129 6897 6617 6384 -1335 -374 -680 C
ATOM 2567 NE ARG A1129 -20.455 9.857 -22.539 1.00 64.07 N
ANISOU 2567 NE ARG A1129 8099 8254 7990 -1108 -459 -551 N
ATOM 2568 CZ ARG A1129 -19.494 10.677 -22.107 1.00 66.42 C
ANISOU 2568 CZ ARG A1129 8357 8396 8483 -850 -402 -509 C
ATOM 2569 NH1 ARG A1129 -18.241 10.247 -21.983 1.00 61.24 N
ANISOU 2569 NH1 ARG A1129 7859 7486 7924 -774 -268 -574 N
ATOM 2570 NH2 ARG A1129 -19.782 11.939 -21.810 1.00 66.20 N
ANISOU 2570 NH2 ARG A1129 8144 8480 8528 -669 -473 -397 N
ATOM 2571 N ALA A1130 -17.481 3.850 -21.123 1.00 48.36 N
ANISOU 2571 N ALA A1130 7556 4929 5889 -1288 202 -1052 N
ATOM 2572 CA ALA A1130 -17.093 2.448 -21.279 1.00 49.19 C
ANISOU 2572 CA ALA A1130 8124 4730 5835 -1343 363 -1158 C
ATOM 2573 C ALA A1130 -16.784 1.750 -19.958 1.00 47.96 C
ANISOU 2573 C ALA A1130 8086 4368 5769 -1217 440 -1161 C
ATOM 2574 O ALA A1130 -16.463 0.561 -19.982 1.00 54.40 O
ANISOU 2574 O ALA A1130 9332 4896 6442 -1226 587 -1238 O
ATOM 2575 CB ALA A1130 -15.873 2.345 -22.198 1.00 49.63 C
ANISOU 2575 CB ALA A1130 8360 4640 5856 -1110 521 -1185 C
ATOM 2576 N ALA A1131 -16.861 2.474 -18.831 1.00 51.14 N
ANISOU 2576 N ALA A1131 8145 4899 6386 -1087 353 -1076 N
ATOM 2577 CA ALA A1131 -16.575 2.005 -17.477 1.00 44.38 C
ANISOU 2577 CA ALA A1131 7327 3897 5637 -948 402 -1058 C
ATOM 2578 C ALA A1131 -17.774 2.170 -16.557 1.00 48.93 C
ANISOU 2578 C ALA A1131 7714 4636 6241 -1169 263 -1029 C
ATOM 2579 O ALA A1131 -17.623 2.018 -15.333 1.00 44.79 O
ANISOU 2579 O ALA A1131 7143 4043 5831 -1053 276 -997 O
ATOM 2580 CB ALA A1131 -15.393 2.764 -16.860 1.00 43.43 C
ANISOU 2580 CB ALA A1131 6954 3802 5747 -564 438 -976 C
ATOM 2581 N ARG A1132 -18.954 2.482 -17.120 1.00 48.63 N
ANISOU 2581 N ARG A1132 7548 4845 6085 -1472 131 -1031 N
ATOM 2582 CA ARG A1132 -20.136 2.781 -16.323 1.00 45.47 C
ANISOU 2582 CA ARG A1132 6893 4689 5696 -1655 -4 -985 C
ATOM 2583 C ARG A1132 -20.375 1.725 -15.250 1.00 51.72 C
ANISOU 2583 C ARG A1132 7906 5305 6442 -1778 52 -1019 C
ATOM 2584 O ARG A1132 -20.748 2.067 -14.123 1.00 43.76 O
ANISOU 2584 O ARG A1132 6668 4407 5552 -1732 -7 -962 O
ATOM 2585 CB ARG A1132 -21.358 2.928 -17.235 1.00 46.35 C
ANISOU 2585 CB ARG A1132 6904 5105 5602 -1997 -128 -987 C
ATOM 2586 CG ARG A1132 -22.419 3.890 -16.694 1.00 54.85 C
ANISOU 2586 CG ARG A1132 7535 6573 6732 -2021 -286 -886 C
ATOM 2587 CD ARG A1132 -23.784 3.802 -17.366 1.00 53.94 C
ANISOU 2587 CD ARG A1132 7299 6831 6366 -2395 -411 -874 C
ATOM 2588 NE ARG A1132 -24.691 2.903 -16.647 1.00 62.02 N
ANISOU 2588 NE ARG A1132 8387 7938 7240 -2739 -430 -901 N
ATOM 2589 CZ ARG A1132 -25.088 1.702 -17.085 1.00 75.80 C
ANISOU 2589 CZ ARG A1132 10476 9605 8721 -3165 -397 -995 C
ATOM 2590 NH1 ARG A1132 -24.675 1.228 -18.264 1.00 76.28 N
ANISOU 2590 NH1 ARG A1132 10858 9494 8631 -3284 -339 -1078 N
ATOM 2591 NH2 ARG A1132 -25.915 0.968 -16.341 1.00 79.10 N
ANISOU 2591 NH2 ARG A1132 10939 10113 9002 -3497 -414 -1008 N
ATOM 2592 N ASP A1133 -20.130 0.435 -15.573 1.00 59.57 N
ANISOU 2592 N ASP A1133 9382 5998 7252 -1922 180 -1111 N
ATOM 2593 CA ASP A1133 -20.297 -0.651 -14.595 1.00 57.43 C
ANISOU 2593 CA ASP A1133 9410 5501 6908 -2040 255 -1142 C
ATOM 2594 C ASP A1133 -19.391 -0.461 -13.374 1.00 57.72 C
ANISOU 2594 C ASP A1133 9351 5401 7179 -1644 313 -1079 C
ATOM 2595 O ASP A1133 -19.823 -0.632 -12.230 1.00 54.40 O
ANISOU 2595 O ASP A1133 8867 5001 6801 -1700 283 -1047 O
ATOM 2596 CB ASP A1133 -20.009 -2.010 -15.246 1.00 66.42 C
ANISOU 2596 CB ASP A1133 11169 6274 7795 -2195 412 -1250 C
ATOM 2597 CG ASP A1133 -20.919 -2.319 -16.463 1.00 81.28 C
ANISOU 2597 CG ASP A1133 13165 8315 9401 -2620 354 -1304 C
ATOM 2598 OD1 ASP A1133 -22.132 -2.012 -16.410 1.00 84.95 O
ANISOU 2598 OD1 ASP A1133 13357 9133 9786 -2957 202 -1275 O
ATOM 2599 OD2 ASP A1133 -20.420 -2.894 -17.470 1.00 79.51 O
ANISOU 2599 OD2 ASP A1133 13269 7914 9027 -2579 466 -1348 O
ATOM 2600 N ASP A1134 -18.127 -0.113 -13.596 1.00 59.31 N
ANISOU 2600 N ASP A1134 9527 5493 7516 -1255 396 -1055 N
ATOM 2601 CA ASP A1134 -17.214 0.076 -12.481 1.00 47.85 C
ANISOU 2601 CA ASP A1134 7960 3963 6259 -895 443 -988 C
ATOM 2602 C ASP A1134 -17.647 1.247 -11.611 1.00 51.71 C
ANISOU 2602 C ASP A1134 7970 4734 6942 -860 295 -910 C
ATOM 2603 O ASP A1134 -17.472 1.225 -10.385 1.00 56.24 O
ANISOU 2603 O ASP A1134 8469 5277 7622 -734 295 -865 O
ATOM 2604 CB ASP A1134 -15.790 0.276 -13.017 1.00 50.95 C
ANISOU 2604 CB ASP A1134 8369 4268 6721 -522 555 -969 C
ATOM 2605 CG ASP A1134 -15.200 -1.006 -13.646 1.00 71.36 C
ANISOU 2605 CG ASP A1134 11482 6526 9105 -447 746 -1035 C
ATOM 2606 OD1 ASP A1134 -15.453 -2.127 -13.122 1.00 70.94 O
ANISOU 2606 OD1 ASP A1134 11817 6219 8917 -533 829 -1069 O
ATOM 2607 OD2 ASP A1134 -14.474 -0.891 -14.665 1.00 76.13 O
ANISOU 2607 OD2 ASP A1134 12142 7114 9671 -294 826 -1052 O
ATOM 2608 N ILE A1135 -18.224 2.271 -12.226 1.00 46.82 N
ANISOU 2608 N ILE A1135 7053 4383 6354 -956 174 -890 N
ATOM 2609 CA ILE A1135 -18.590 3.463 -11.487 1.00 39.91 C
ANISOU 2609 CA ILE A1135 5771 3749 5643 -873 53 -814 C
ATOM 2610 C ILE A1135 -19.809 3.191 -10.618 1.00 39.98 C
ANISOU 2610 C ILE A1135 5712 3884 5595 -1106 -18 -806 C
ATOM 2611 O ILE A1135 -19.823 3.493 -9.417 1.00 42.17 O
ANISOU 2611 O ILE A1135 5836 4193 5992 -993 -42 -760 O
ATOM 2612 CB ILE A1135 -18.848 4.624 -12.462 1.00 43.02 C
ANISOU 2612 CB ILE A1135 5919 4371 6056 -869 -38 -784 C
ATOM 2613 CG1 ILE A1135 -17.578 4.957 -13.254 1.00 46.41 C
ANISOU 2613 CG1 ILE A1135 6395 4694 6543 -648 39 -784 C
ATOM 2614 CG2 ILE A1135 -19.407 5.823 -11.702 1.00 39.35 C
ANISOU 2614 CG2 ILE A1135 5100 4135 5717 -788 -151 -706 C
ATOM 2615 CD1 ILE A1135 -17.813 5.879 -14.441 1.00 41.78 C
ANISOU 2615 CD1 ILE A1135 5669 4282 5924 -684 -28 -763 C
ATOM 2616 N VAL A1136 -20.857 2.628 -11.222 1.00 40.92 N
ANISOU 2616 N VAL A1136 5932 4105 5509 -1455 -55 -847 N
ATOM 2617 CA VAL A1136 -22.088 2.345 -10.492 1.00 41.83 C
ANISOU 2617 CA VAL A1136 5955 4410 5530 -1728 -123 -832 C
ATOM 2618 C VAL A1136 -21.810 1.381 -9.351 1.00 41.87 C
ANISOU 2618 C VAL A1136 6210 4160 5538 -1732 -34 -849 C
ATOM 2619 O VAL A1136 -22.291 1.575 -8.228 1.00 42.76 O
ANISOU 2619 O VAL A1136 6145 4392 5711 -1735 -75 -803 O
ATOM 2620 CB VAL A1136 -23.154 1.829 -11.473 1.00 46.27 C
ANISOU 2620 CB VAL A1136 6601 5152 5827 -2150 -174 -875 C
ATOM 2621 CG1 VAL A1136 -24.348 1.231 -10.761 1.00 43.67 C
ANISOU 2621 CG1 VAL A1136 6247 5005 5341 -2509 -218 -869 C
ATOM 2622 CG2 VAL A1136 -23.566 2.990 -12.398 1.00 44.12 C
ANISOU 2622 CG2 VAL A1136 5988 5213 5564 -2095 -288 -822 C
ATOM 2623 N GLY A1137 -20.967 0.379 -9.598 1.00 41.71 N
ANISOU 2623 N GLY A1137 6613 3781 5452 -1682 100 -906 N
ATOM 2624 CA GLY A1137 -20.413 -0.436 -8.552 1.00 41.61 C
ANISOU 2624 CA GLY A1137 6860 3488 5463 -1561 203 -901 C
ATOM 2625 C GLY A1137 -19.781 0.318 -7.413 1.00 40.79 C
ANISOU 2625 C GLY A1137 6474 3430 5595 -1216 181 -824 C
ATOM 2626 O GLY A1137 -20.128 0.083 -6.257 1.00 53.25 O
ANISOU 2626 O GLY A1137 8032 5009 7191 -1256 171 -794 O
ATOM 2627 N TRP A1138 -18.833 1.208 -7.715 1.00 44.37 N
ANISOU 2627 N TRP A1138 6724 3922 6212 -902 175 -792 N
ATOM 2628 CA TRP A1138 -18.176 2.002 -6.673 1.00 39.54 C
ANISOU 2628 CA TRP A1138 5850 3372 5802 -612 147 -723 C
ATOM 2629 C TRP A1138 -19.192 2.722 -5.821 1.00 38.98 C
ANISOU 2629 C TRP A1138 5481 3543 5788 -723 33 -686 C
ATOM 2630 O TRP A1138 -19.144 2.670 -4.590 1.00 39.57 O
ANISOU 2630 O TRP A1138 5510 3600 5926 -648 33 -651 O
ATOM 2631 CB TRP A1138 -17.234 3.025 -7.301 1.00 38.64 C
ANISOU 2631 CB TRP A1138 5531 3335 5815 -370 135 -697 C
ATOM 2632 CG TRP A1138 -16.425 3.815 -6.290 1.00 39.24 C
ANISOU 2632 CG TRP A1138 5376 3470 6065 -113 112 -632 C
ATOM 2633 CD1 TRP A1138 -15.368 3.361 -5.578 1.00 35.67 C
ANISOU 2633 CD1 TRP A1138 5005 2897 5650 113 188 -597 C
ATOM 2634 CD2 TRP A1138 -16.609 5.196 -5.895 1.00 36.99 C
ANISOU 2634 CD2 TRP A1138 4764 3385 5906 -66 8 -591 C
ATOM 2635 NE1 TRP A1138 -14.874 4.353 -4.774 1.00 36.06 N
ANISOU 2635 NE1 TRP A1138 4781 3082 5838 256 127 -542 N
ATOM 2636 CE2 TRP A1138 -15.614 5.488 -4.952 1.00 32.35 C
ANISOU 2636 CE2 TRP A1138 4088 2780 5423 143 23 -545 C
ATOM 2637 CE3 TRP A1138 -17.498 6.208 -6.274 1.00 36.55 C
ANISOU 2637 CE3 TRP A1138 4506 3519 5862 -164 -88 -584 C
ATOM 2638 CZ2 TRP A1138 -15.476 6.737 -4.378 1.00 33.14 C
ANISOU 2638 CZ2 TRP A1138 3945 3014 5632 211 -51 -508 C
ATOM 2639 CZ3 TRP A1138 -17.373 7.434 -5.701 1.00 35.12 C
ANISOU 2639 CZ3 TRP A1138 4106 3446 5792 -47 -149 -540 C
ATOM 2640 CH2 TRP A1138 -16.374 7.696 -4.752 1.00 39.27 C
ANISOU 2640 CH2 TRP A1138 4586 3920 6416 118 -130 -511 C
ATOM 2641 N ALA A1139 -20.119 3.408 -6.490 1.00 43.16 N
ANISOU 2641 N ALA A1139 5803 4318 6277 -881 -59 -687 N
ATOM 2642 CA ALA A1139 -21.138 4.204 -5.823 1.00 41.77 C
ANISOU 2642 CA ALA A1139 5319 4420 6132 -936 -158 -641 C
ATOM 2643 C ALA A1139 -21.985 3.347 -4.893 1.00 43.52 C
ANISOU 2643 C ALA A1139 5622 4666 6248 -1163 -149 -644 C
ATOM 2644 O ALA A1139 -22.326 3.787 -3.782 1.00 39.07 O
ANISOU 2644 O ALA A1139 4872 4218 5754 -1094 -182 -600 O
ATOM 2645 CB ALA A1139 -22.008 4.903 -6.873 1.00 42.37 C
ANISOU 2645 CB ALA A1139 5197 4771 6129 -1052 -244 -629 C
ATOM 2646 N HIS A1140 -22.321 2.111 -5.321 1.00 39.45 N
ANISOU 2646 N HIS A1140 5415 4029 5547 -1451 -96 -697 N
ATOM 2647 CA HIS A1140 -23.041 1.211 -4.424 1.00 40.28 C
ANISOU 2647 CA HIS A1140 5656 4120 5528 -1704 -73 -699 C
ATOM 2648 C HIS A1140 -22.212 0.874 -3.202 1.00 39.73 C
ANISOU 2648 C HIS A1140 5722 3805 5570 -1476 -2 -674 C
ATOM 2649 O HIS A1140 -22.759 0.759 -2.106 1.00 45.54 O
ANISOU 2649 O HIS A1140 6385 4623 6294 -1555 -16 -642 O
ATOM 2650 CB HIS A1140 -23.461 -0.069 -5.125 1.00 41.75 C
ANISOU 2650 CB HIS A1140 6229 4168 5465 -2085 -17 -766 C
ATOM 2651 CG HIS A1140 -24.433 0.124 -6.253 1.00 50.07 C
ANISOU 2651 CG HIS A1140 7148 5519 6356 -2393 -99 -787 C
ATOM 2652 ND1 HIS A1140 -25.101 1.312 -6.483 1.00 46.77 N
ANISOU 2652 ND1 HIS A1140 6266 5512 5993 -2332 -218 -729 N
ATOM 2653 CD2 HIS A1140 -24.832 -0.729 -7.233 1.00 47.36 C
ANISOU 2653 CD2 HIS A1140 7095 5127 5772 -2759 -78 -855 C
ATOM 2654 CE1 HIS A1140 -25.890 1.172 -7.536 1.00 44.23 C
ANISOU 2654 CE1 HIS A1140 5913 5420 5474 -2641 -275 -749 C
ATOM 2655 NE2 HIS A1140 -25.751 -0.058 -8.002 1.00 49.38 N
ANISOU 2655 NE2 HIS A1140 7015 5805 5942 -2931 -197 -831 N
ATOM 2656 N ASP A1141 -20.893 0.748 -3.360 1.00 42.13 N
ANISOU 2656 N ASP A1141 6194 3845 5968 -1182 72 -678 N
ATOM 2657 CA ASP A1141 -20.012 0.428 -2.233 1.00 38.84 C
ANISOU 2657 CA ASP A1141 5885 3234 5638 -932 135 -638 C
ATOM 2658 C ASP A1141 -19.904 1.585 -1.252 1.00 39.53 C
ANISOU 2658 C ASP A1141 5597 3518 5906 -732 55 -581 C
ATOM 2659 O ASP A1141 -19.807 1.368 -0.044 1.00 44.12 O
ANISOU 2659 O ASP A1141 6195 4055 6515 -667 69 -544 O
ATOM 2660 CB ASP A1141 -18.621 0.047 -2.738 1.00 43.59 C
ANISOU 2660 CB ASP A1141 6711 3584 6269 -643 234 -641 C
ATOM 2661 CG ASP A1141 -18.614 -1.266 -3.499 1.00 57.76 C
ANISOU 2661 CG ASP A1141 8990 5099 7859 -790 351 -698 C
ATOM 2662 OD1 ASP A1141 -19.522 -2.088 -3.239 1.00 56.69 O
ANISOU 2662 OD1 ASP A1141 9088 4893 7557 -1113 368 -725 O
ATOM 2663 OD2 ASP A1141 -17.702 -1.473 -4.343 1.00 64.74 O
ANISOU 2663 OD2 ASP A1141 10036 5835 8729 -594 432 -715 O
ATOM 2664 N VAL A1142 -19.903 2.817 -1.753 1.00 41.08 N
ANISOU 2664 N VAL A1142 5490 3911 6206 -636 -21 -573 N
ATOM 2665 CA VAL A1142 -19.826 3.984 -0.878 1.00 41.09 C
ANISOU 2665 CA VAL A1142 5194 4070 6350 -462 -87 -529 C
ATOM 2666 C VAL A1142 -21.085 4.079 -0.023 1.00 41.12 C
ANISOU 2666 C VAL A1142 5059 4266 6299 -628 -132 -511 C
ATOM 2667 O VAL A1142 -21.015 4.207 1.214 1.00 35.61 O
ANISOU 2667 O VAL A1142 4306 3572 5652 -543 -133 -481 O
ATOM 2668 CB VAL A1142 -19.589 5.258 -1.717 1.00 34.16 C
ANISOU 2668 CB VAL A1142 4100 3320 5559 -341 -144 -525 C
ATOM 2669 CG1 VAL A1142 -20.049 6.507 -0.968 1.00 33.90 C
ANISOU 2669 CG1 VAL A1142 3802 3475 5604 -249 -214 -489 C
ATOM 2670 CG2 VAL A1142 -18.116 5.379 -2.085 1.00 32.93 C
ANISOU 2670 CG2 VAL A1142 4009 3017 5486 -125 -99 -520 C
ATOM 2671 N ARG A1143 -22.249 3.975 -0.683 1.00 39.70 N
ANISOU 2671 N ARG A1143 4815 4278 5993 -877 -166 -525 N
ATOM 2672 CA ARG A1143 -23.555 3.924 -0.033 1.00 38.09 C
ANISOU 2672 CA ARG A1143 4459 4325 5687 -1077 -199 -501 C
ATOM 2673 C ARG A1143 -23.607 2.881 1.088 1.00 45.11 C
ANISOU 2673 C ARG A1143 5551 5073 6514 -1199 -141 -497 C
ATOM 2674 O ARG A1143 -24.089 3.171 2.193 1.00 43.11 O
ANISOU 2674 O ARG A1143 5146 4959 6275 -1178 -154 -461 O
ATOM 2675 CB ARG A1143 -24.625 3.641 -1.093 1.00 39.94 C
ANISOU 2675 CB ARG A1143 4645 4785 5744 -1380 -236 -516 C
ATOM 2676 CG ARG A1143 -26.052 3.876 -0.649 1.00 39.65 C
ANISOU 2676 CG ARG A1143 4332 5149 5586 -1560 -286 -470 C
ATOM 2677 CD ARG A1143 -26.654 2.624 0.042 1.00 40.88 C
ANISOU 2677 CD ARG A1143 4668 5289 5574 -1910 -241 -480 C
ATOM 2678 NE ARG A1143 -27.793 2.191 -0.725 1.00 42.13 N
ANISOU 2678 NE ARG A1143 4756 5749 5502 -2301 -281 -481 N
ATOM 2679 CZ ARG A1143 -29.001 1.989 -0.247 1.00 43.22 C
ANISOU 2679 CZ ARG A1143 4700 6252 5470 -2576 -304 -440 C
ATOM 2680 NH1 ARG A1143 -29.935 1.597 -1.091 1.00 44.49 N
ANISOU 2680 NH1 ARG A1143 4791 6713 5400 -2957 -350 -440 N
ATOM 2681 NH2 ARG A1143 -29.271 2.137 1.060 1.00 49.23 N
ANISOU 2681 NH2 ARG A1143 5339 7097 6268 -2495 -281 -396 N
ATOM 2682 N GLY A1144 -23.129 1.657 0.817 1.00 39.33 N
ANISOU 2682 N GLY A1144 5193 4053 5696 -1316 -65 -531 N
ATOM 2683 CA GLY A1144 -23.118 0.626 1.845 1.00 39.95 C
ANISOU 2683 CA GLY A1144 5530 3952 5698 -1415 3 -519 C
ATOM 2684 C GLY A1144 -22.270 0.994 3.046 1.00 48.39 C
ANISOU 2684 C GLY A1144 6543 4926 6918 -1098 13 -473 C
ATOM 2685 O GLY A1144 -22.678 0.788 4.192 1.00 52.00 O
ANISOU 2685 O GLY A1144 6986 5427 7344 -1157 20 -441 O
ATOM 2686 N ALA A1145 -21.076 1.553 2.799 1.00 50.30 N
ANISOU 2686 N ALA A1145 6741 5064 7307 -780 11 -467 N
ATOM 2687 CA ALA A1145 -20.214 2.063 3.876 1.00 40.23 C
ANISOU 2687 CA ALA A1145 5362 3760 6162 -498 1 -421 C
ATOM 2688 C ALA A1145 -20.888 3.152 4.702 1.00 41.63 C
ANISOU 2688 C ALA A1145 5223 4192 6402 -483 -71 -403 C
ATOM 2689 O ALA A1145 -20.695 3.205 5.919 1.00 42.00 O
ANISOU 2689 O ALA A1145 5249 4232 6478 -395 -70 -369 O
ATOM 2690 CB ALA A1145 -18.911 2.617 3.307 1.00 35.81 C
ANISOU 2690 CB ALA A1145 4751 3134 5720 -223 -1 -416 C
ATOM 2691 N ILE A1146 -21.642 4.058 4.062 1.00 37.76 N
ANISOU 2691 N ILE A1146 4497 3926 5923 -536 -128 -419 N
ATOM 2692 CA ILE A1146 -22.339 5.092 4.839 1.00 37.23 C
ANISOU 2692 CA ILE A1146 4165 4092 5887 -477 -174 -396 C
ATOM 2693 C ILE A1146 -23.432 4.455 5.684 1.00 41.52 C
ANISOU 2693 C ILE A1146 4704 4767 6306 -689 -153 -377 C
ATOM 2694 O ILE A1146 -23.676 4.874 6.827 1.00 50.29 O
ANISOU 2694 O ILE A1146 5706 5970 7433 -611 -155 -352 O
ATOM 2695 CB ILE A1146 -22.910 6.210 3.930 1.00 38.08 C
ANISOU 2695 CB ILE A1146 4046 4412 6009 -431 -226 -399 C
ATOM 2696 CG1 ILE A1146 -21.814 6.864 3.065 1.00 35.65 C
ANISOU 2696 CG1 ILE A1146 3762 3973 5812 -252 -242 -415 C
ATOM 2697 CG2 ILE A1146 -23.497 7.333 4.752 1.00 37.94 C
ANISOU 2697 CG2 ILE A1146 3812 4592 6012 -291 -250 -372 C
ATOM 2698 CD1 ILE A1146 -20.607 7.331 3.854 1.00 33.19 C
ANISOU 2698 CD1 ILE A1146 3479 3517 5613 -49 -239 -407 C
ATOM 2699 N ASP A 257 -24.081 3.409 5.156 1.00 39.83 N
ANISOU 2699 N ASP A 257 4629 4559 5944 -983 -126 -391 N
ATOM 2700 CA ASP A 257 -25.089 2.699 5.924 1.00 40.63 C
ANISOU 2700 CA ASP A 257 4750 4790 5896 -1248 -100 -369 C
ATOM 2701 C ASP A 257 -24.490 2.051 7.167 1.00 48.06 C
ANISOU 2701 C ASP A 257 5906 5504 6852 -1187 -48 -347 C
ATOM 2702 O ASP A 257 -25.176 1.922 8.191 1.00 54.41 O
ANISOU 2702 O ASP A 257 6645 6446 7584 -1291 -33 -316 O
ATOM 2703 CB ASP A 257 -25.775 1.667 5.032 1.00 41.31 C
ANISOU 2703 CB ASP A 257 5004 4898 5794 -1628 -81 -395 C
ATOM 2704 CG ASP A 257 -26.884 2.259 4.171 1.00 54.73 C
ANISOU 2704 CG ASP A 257 6396 6994 7406 -1776 -144 -389 C
ATOM 2705 OD1 ASP A 257 -27.186 3.479 4.280 1.00 63.26 O
ANISOU 2705 OD1 ASP A 257 7143 8327 8567 -1548 -192 -357 O
ATOM 2706 OD2 ASP A 257 -27.468 1.482 3.377 1.00 60.62 O
ANISOU 2706 OD2 ASP A 257 7255 7802 7974 -2126 -142 -412 O
ATOM 2707 N HIS A 258 -23.214 1.651 7.108 1.00 49.01 N
ANISOU 2707 N HIS A 258 6267 5306 7049 -1002 -16 -351 N
ATOM 2708 CA HIS A 258 -22.575 1.073 8.288 1.00 44.57 C
ANISOU 2708 CA HIS A 258 5895 4552 6489 -895 28 -310 C
ATOM 2709 C HIS A 258 -22.177 2.142 9.305 1.00 42.62 C
ANISOU 2709 C HIS A 258 5410 4416 6369 -642 -19 -285 C
ATOM 2710 O HIS A 258 -22.307 1.928 10.514 1.00 41.65 O
ANISOU 2710 O HIS A 258 5316 4300 6210 -645 -2 -249 O
ATOM 2711 CB HIS A 258 -21.369 0.223 7.885 1.00 46.53 C
ANISOU 2711 CB HIS A 258 6475 4466 6739 -749 88 -304 C
ATOM 2712 CG HIS A 258 -21.696 -1.217 7.620 1.00 52.66 C
ANISOU 2712 CG HIS A 258 7663 5017 7329 -998 176 -310 C
ATOM 2713 ND1 HIS A 258 -22.059 -1.686 6.375 1.00 56.26 N
ANISOU 2713 ND1 HIS A 258 8277 5414 7685 -1213 200 -365 N
ATOM 2714 CD2 HIS A 258 -21.707 -2.296 8.443 1.00 57.67 C
ANISOU 2714 CD2 HIS A 258 8629 5448 7835 -1080 251 -270 C
ATOM 2715 CE1 HIS A 258 -22.284 -2.987 6.441 1.00 55.85 C
ANISOU 2715 CE1 HIS A 258 8657 5120 7444 -1436 290 -365 C
ATOM 2716 NE2 HIS A 258 -22.075 -3.384 7.684 1.00 58.52 N
ANISOU 2716 NE2 HIS A 258 9117 5356 7762 -1352 326 -305 N
ATOM 2717 N TYR A 259 -21.700 3.306 8.876 1.00 40.93 N
ANISOU 2717 N TYR A 259 4986 4281 6284 -442 -73 -303 N
ATOM 2718 CA TYR A 259 -21.471 4.328 9.886 1.00 40.18 C
ANISOU 2718 CA TYR A 259 4713 4287 6267 -265 -111 -289 C
ATOM 2719 C TYR A 259 -22.793 4.732 10.539 1.00 48.34 C
ANISOU 2719 C TYR A 259 5572 5566 7228 -378 -111 -285 C
ATOM 2720 O TYR A 259 -22.859 4.879 11.763 1.00 57.53 O
ANISOU 2720 O TYR A 259 6714 6768 8376 -330 -103 -263 O
ATOM 2721 CB TYR A 259 -20.744 5.549 9.305 1.00 35.98 C
ANISOU 2721 CB TYR A 259 4036 3778 5857 -71 -162 -311 C
ATOM 2722 CG TYR A 259 -19.308 5.301 8.946 1.00 36.44 C
ANISOU 2722 CG TYR A 259 4204 3663 5977 74 -161 -299 C
ATOM 2723 CD1 TYR A 259 -18.980 4.730 7.717 1.00 40.99 C
ANISOU 2723 CD1 TYR A 259 4893 4134 6549 51 -133 -313 C
ATOM 2724 CD2 TYR A 259 -18.266 5.652 9.802 1.00 34.03 C
ANISOU 2724 CD2 TYR A 259 3877 3335 5717 235 -185 -269 C
ATOM 2725 CE1 TYR A 259 -17.678 4.491 7.360 1.00 40.37 C
ANISOU 2725 CE1 TYR A 259 4894 3936 6509 214 -117 -292 C
ATOM 2726 CE2 TYR A 259 -16.924 5.433 9.434 1.00 35.58 C
ANISOU 2726 CE2 TYR A 259 4123 3449 5948 379 -183 -241 C
ATOM 2727 CZ TYR A 259 -16.648 4.840 8.208 1.00 44.30 C
ANISOU 2727 CZ TYR A 259 5330 4455 7048 384 -142 -249 C
ATOM 2728 OH TYR A 259 -15.358 4.559 7.791 1.00 53.86 O
ANISOU 2728 OH TYR A 259 6579 5613 8272 555 -121 -213 O
ATOM 2729 N HIS A 260 -23.864 4.880 9.744 1.00 41.74 N
ANISOU 2729 N HIS A 260 4602 4930 6327 -524 -117 -298 N
ATOM 2730 CA HIS A 260 -25.155 5.258 10.313 1.00 39.93 C
ANISOU 2730 CA HIS A 260 4163 5004 6003 -604 -108 -277 C
ATOM 2731 C HIS A 260 -25.668 4.206 11.288 1.00 46.18 C
ANISOU 2731 C HIS A 260 5067 5809 6669 -821 -58 -248 C
ATOM 2732 O HIS A 260 -26.176 4.543 12.368 1.00 46.31 O
ANISOU 2732 O HIS A 260 4969 5981 6644 -785 -38 -225 O
ATOM 2733 CB HIS A 260 -26.177 5.490 9.205 1.00 40.90 C
ANISOU 2733 CB HIS A 260 4101 5390 6048 -726 -128 -277 C
ATOM 2734 CG HIS A 260 -27.474 6.068 9.693 1.00 41.87 C
ANISOU 2734 CG HIS A 260 3945 5901 6064 -731 -116 -239 C
ATOM 2735 ND1 HIS A 260 -28.705 5.557 9.331 1.00 48.03 N
ANISOU 2735 ND1 HIS A 260 4575 7005 6669 -1005 -110 -208 N
ATOM 2736 CD2 HIS A 260 -27.732 7.115 10.511 1.00 42.45 C
ANISOU 2736 CD2 HIS A 260 3862 6110 6156 -488 -101 -222 C
ATOM 2737 CE1 HIS A 260 -29.663 6.265 9.904 1.00 46.08 C
ANISOU 2737 CE1 HIS A 260 4054 7112 6343 -902 -90 -162 C
ATOM 2738 NE2 HIS A 260 -29.098 7.203 10.643 1.00 44.27 N
ANISOU 2738 NE2 HIS A 260 3840 6750 6229 -574 -77 -173 N
ATOM 2739 N GLN A 261 -25.540 2.922 10.921 1.00 47.40 N
ANISOU 2739 N GLN A 261 5480 5784 6744 -1050 -27 -249 N
ATOM 2740 CA GLN A 261 -26.034 1.836 11.759 1.00 44.22 C
ANISOU 2740 CA GLN A 261 5251 5358 6194 -1300 30 -218 C
ATOM 2741 C GLN A 261 -25.217 1.696 13.034 1.00 50.45 C
ANISOU 2741 C GLN A 261 6182 5952 7034 -1119 50 -187 C
ATOM 2742 O GLN A 261 -25.774 1.414 14.108 1.00 52.55 O
ANISOU 2742 O GLN A 261 6449 6312 7204 -1227 84 -153 O
ATOM 2743 CB GLN A 261 -25.982 0.549 10.977 1.00 44.62 C
ANISOU 2743 CB GLN A 261 5627 5196 6130 -1570 69 -232 C
ATOM 2744 CG GLN A 261 -25.580 -0.620 11.811 1.00 48.33 C
ANISOU 2744 CG GLN A 261 6470 5380 6512 -1655 138 -198 C
ATOM 2745 CD GLN A 261 -25.840 -1.891 11.130 1.00 54.40 C
ANISOU 2745 CD GLN A 261 7600 5962 7106 -1987 196 -214 C
ATOM 2746 OE1 GLN A 261 -26.023 -1.928 9.915 1.00 51.16 O
ANISOU 2746 OE1 GLN A 261 7194 5577 6669 -2111 179 -259 O
ATOM 2747 NE2 GLN A 261 -25.873 -2.965 11.901 1.00 68.07 N
ANISOU 2747 NE2 GLN A 261 9678 7490 8696 -2152 270 -177 N
ATOM 2748 N ARG A 262 -23.882 1.830 12.908 1.00 50.69 N
ANISOU 2748 N ARG A 262 6332 5733 7193 -858 30 -191 N
ATOM 2749 CA ARG A 262 -22.971 1.885 14.045 1.00 45.15 C
ANISOU 2749 CA ARG A 262 5708 4904 6543 -645 27 -154 C
ATOM 2750 C ARG A 262 -23.326 3.032 14.968 1.00 45.34 C
ANISOU 2750 C ARG A 262 5474 5150 6604 -533 -4 -159 C
ATOM 2751 O ARG A 262 -23.050 2.978 16.171 1.00 50.23 O
ANISOU 2751 O ARG A 262 6142 5744 7200 -464 3 -126 O
ATOM 2752 CB ARG A 262 -21.543 2.057 13.535 1.00 49.84 C
ANISOU 2752 CB ARG A 262 6371 5309 7256 -389 -2 -155 C
ATOM 2753 CG ARG A 262 -20.440 1.604 14.454 1.00 58.60 C
ANISOU 2753 CG ARG A 262 7642 6259 8366 -202 5 -93 C
ATOM 2754 CD ARG A 262 -19.135 1.409 13.641 1.00 65.55 C
ANISOU 2754 CD ARG A 262 8616 6980 9311 8 2 -78 C
ATOM 2755 NE ARG A 262 -19.197 0.296 12.675 1.00 68.11 N
ANISOU 2755 NE ARG A 262 9219 7101 9559 -85 74 -82 N
ATOM 2756 CZ ARG A 262 -18.912 0.382 11.368 1.00 60.59 C
ANISOU 2756 CZ ARG A 262 8270 6101 8652 -60 78 -123 C
ATOM 2757 NH1 ARG A 262 -18.519 1.522 10.832 1.00 44.88 N
ANISOU 2757 NH1 ARG A 262 6012 4251 6789 55 13 -157 N
ATOM 2758 NH2 ARG A 262 -19.000 -0.691 10.587 1.00 65.94 N
ANISOU 2758 NH2 ARG A 262 9256 6570 9228 -160 156 -132 N
ATOM 2759 N ARG A 263 -23.944 4.074 14.427 1.00 42.93 N
ANISOU 2759 N ARG A 263 4918 5057 6338 -499 -31 -196 N
ATOM 2760 CA ARG A 263 -24.315 5.205 15.251 1.00 43.91 C
ANISOU 2760 CA ARG A 263 4848 5364 6472 -360 -39 -204 C
ATOM 2761 C ARG A 263 -25.544 4.866 16.080 1.00 48.23 C
ANISOU 2761 C ARG A 263 5318 6135 6874 -528 16 -175 C
ATOM 2762 O ARG A 263 -25.487 4.878 17.310 1.00 52.26 O
ANISOU 2762 O ARG A 263 5864 6648 7345 -486 38 -155 O
ATOM 2763 CB ARG A 263 -24.557 6.418 14.364 1.00 42.58 C
ANISOU 2763 CB ARG A 263 4486 5324 6368 -225 -69 -241 C
ATOM 2764 CG ARG A 263 -24.624 7.674 15.101 1.00 42.54 C
ANISOU 2764 CG ARG A 263 4377 5409 6378 -22 -69 -257 C
ATOM 2765 CD ARG A 263 -23.263 8.299 15.105 1.00 51.19 C
ANISOU 2765 CD ARG A 263 5571 6294 7585 139 -119 -285 C
ATOM 2766 NE ARG A 263 -23.244 9.492 14.268 1.00 48.27 N
ANISOU 2766 NE ARG A 263 5124 5949 7269 277 -140 -318 N
ATOM 2767 CZ ARG A 263 -22.236 10.352 14.223 1.00 46.95 C
ANISOU 2767 CZ ARG A 263 5024 5645 7168 395 -178 -347 C
ATOM 2768 NH1 ARG A 263 -21.162 10.141 14.988 1.00 54.84 N
ANISOU 2768 NH1 ARG A 263 6126 6524 8188 393 -209 -344 N
ATOM 2769 NH2 ARG A 263 -22.310 11.408 13.415 1.00 38.14 N
ANISOU 2769 NH2 ARG A 263 3876 4536 6080 503 -186 -372 N
ATOM 2770 N GLN A 264 -26.656 4.509 15.411 1.00 45.60 N
ANISOU 2770 N GLN A 264 4872 6015 6439 -744 39 -166 N
ATOM 2771 CA GLN A 264 -27.869 4.061 16.098 1.00 50.50 C
ANISOU 2771 CA GLN A 264 5396 6904 6889 -965 96 -127 C
ATOM 2772 C GLN A 264 -27.571 3.012 17.168 1.00 53.25 C
ANISOU 2772 C GLN A 264 5997 7070 7164 -1105 136 -93 C
ATOM 2773 O GLN A 264 -27.998 3.146 18.320 1.00 53.85 O
ANISOU 2773 O GLN A 264 6012 7282 7165 -1098 176 -66 O
ATOM 2774 CB GLN A 264 -28.876 3.507 15.090 1.00 50.09 C
ANISOU 2774 CB GLN A 264 5244 7077 6710 -1267 102 -116 C
ATOM 2775 CG GLN A 264 -29.221 4.472 13.991 1.00 50.64 C
ANISOU 2775 CG GLN A 264 5062 7351 6826 -1127 59 -132 C
ATOM 2776 CD GLN A 264 -30.239 3.928 13.024 1.00 56.47 C
ANISOU 2776 CD GLN A 264 5674 8370 7411 -1448 53 -113 C
ATOM 2777 OE1 GLN A 264 -30.494 2.724 12.989 1.00 67.86 O
ANISOU 2777 OE1 GLN A 264 7295 9763 8724 -1816 77 -105 O
ATOM 2778 NE2 GLN A 264 -30.834 4.808 12.231 1.00 57.18 N
ANISOU 2778 NE2 GLN A 264 5476 8761 7490 -1323 22 -101 N
ATOM 2779 N LYS A 265 -26.829 1.964 16.813 1.00 51.67 N
ANISOU 2779 N LYS A 265 6107 6554 6971 -1208 137 -87 N
ATOM 2780 CA LYS A 265 -26.565 0.916 17.789 1.00 51.94 C
ANISOU 2780 CA LYS A 265 6426 6396 6912 -1320 184 -39 C
ATOM 2781 C LYS A 265 -25.847 1.468 19.010 1.00 57.22 C
ANISOU 2781 C LYS A 265 7087 7005 7649 -1051 168 -22 C
ATOM 2782 O LYS A 265 -26.249 1.200 20.145 1.00 62.59 O
ANISOU 2782 O LYS A 265 7800 7759 8224 -1130 210 17 O
ATOM 2783 CB LYS A 265 -25.771 -0.213 17.146 1.00 52.09 C
ANISOU 2783 CB LYS A 265 6819 6051 6920 -1386 200 -30 C
ATOM 2784 CG LYS A 265 -26.639 -1.080 16.259 1.00 53.73 C
ANISOU 2784 CG LYS A 265 7144 6294 6976 -1772 239 -42 C
ATOM 2785 CD LYS A 265 -26.089 -2.448 16.080 1.00 58.17 C
ANISOU 2785 CD LYS A 265 8195 6467 7440 -1897 298 -19 C
ATOM 2786 CE LYS A 265 -26.889 -3.162 15.012 1.00 62.93 C
ANISOU 2786 CE LYS A 265 8928 7095 7887 -2301 328 -53 C
ATOM 2787 NZ LYS A 265 -28.314 -3.341 15.441 1.00 63.43 N
ANISOU 2787 NZ LYS A 265 8833 7510 7757 -2711 353 -34 N
ATOM 2788 N THR A 266 -24.798 2.267 18.803 1.00 57.55 N
ANISOU 2788 N THR A 266 7081 6937 7848 -757 106 -49 N
ATOM 2789 CA THR A 266 -24.072 2.799 19.953 1.00 54.95 C
ANISOU 2789 CA THR A 266 6752 6571 7555 -544 80 -35 C
ATOM 2790 C THR A 266 -24.888 3.846 20.713 1.00 56.80 C
ANISOU 2790 C THR A 266 6753 7073 7754 -495 96 -61 C
ATOM 2791 O THR A 266 -24.780 3.936 21.936 1.00 62.59 O
ANISOU 2791 O THR A 266 7526 7825 8432 -445 109 -40 O
ATOM 2792 CB THR A 266 -22.727 3.370 19.509 1.00 50.40 C
ANISOU 2792 CB THR A 266 6180 5847 7122 -298 9 -55 C
ATOM 2793 OG1 THR A 266 -21.910 2.307 19.016 1.00 59.24 O
ANISOU 2793 OG1 THR A 266 7535 6729 8245 -290 14 -13 O
ATOM 2794 CG2 THR A 266 -22.008 3.994 20.676 1.00 51.62 C
ANISOU 2794 CG2 THR A 266 6316 6011 7285 -129 -30 -45 C
ATOM 2795 N THR A 267 -25.704 4.642 20.017 1.00 53.55 N
ANISOU 2795 N THR A 267 6115 6876 7357 -483 103 -101 N
ATOM 2796 CA THR A 267 -26.574 5.586 20.705 1.00 51.02 C
ANISOU 2796 CA THR A 267 5595 6821 6971 -394 144 -115 C
ATOM 2797 C THR A 267 -27.542 4.859 21.628 1.00 56.04 C
ANISOU 2797 C THR A 267 6216 7639 7437 -600 220 -65 C
ATOM 2798 O THR A 267 -27.805 5.320 22.742 1.00 55.29 O
ANISOU 2798 O THR A 267 6078 7656 7274 -510 260 -62 O
ATOM 2799 CB THR A 267 -27.366 6.444 19.705 1.00 49.05 C
ANISOU 2799 CB THR A 267 5107 6796 6735 -320 150 -141 C
ATOM 2800 OG1 THR A 267 -26.480 7.287 18.972 1.00 55.21 O
ANISOU 2800 OG1 THR A 267 5914 7407 7657 -119 89 -188 O
ATOM 2801 CG2 THR A 267 -28.354 7.341 20.426 1.00 48.52 C
ANISOU 2801 CG2 THR A 267 4846 7025 6563 -185 219 -139 C
ATOM 2802 N LYS A 268 -28.099 3.725 21.182 1.00 53.28 N
ANISOU 2802 N LYS A 268 5922 7325 6996 -900 247 -27 N
ATOM 2803 CA LYS A 268 -29.096 3.075 22.012 1.00 56.07 C
ANISOU 2803 CA LYS A 268 6250 7891 7163 -1144 324 24 C
ATOM 2804 C LYS A 268 -28.467 2.329 23.176 1.00 62.44 C
ANISOU 2804 C LYS A 268 7335 8466 7925 -1182 340 64 C
ATOM 2805 O LYS A 268 -29.134 2.134 24.197 1.00 65.53 O
ANISOU 2805 O LYS A 268 7695 9030 8174 -1292 405 102 O
ATOM 2806 CB LYS A 268 -29.977 2.134 21.184 1.00 63.18 C
ANISOU 2806 CB LYS A 268 7134 8936 7937 -1520 350 51 C
ATOM 2807 CG LYS A 268 -30.709 2.809 20.000 1.00 76.37 C
ANISOU 2807 CG LYS A 268 8497 10905 9617 -1505 327 29 C
ATOM 2808 CD LYS A 268 -31.086 4.293 20.254 1.00 83.05 C
ANISOU 2808 CD LYS A 268 9034 12018 10502 -1153 339 13 C
ATOM 2809 CE LYS A 268 -31.448 5.043 18.946 1.00 81.00 C
ANISOU 2809 CE LYS A 268 8541 11945 10289 -1036 300 -4 C
ATOM 2810 NZ LYS A 268 -32.112 6.375 19.173 1.00 77.63 N
ANISOU 2810 NZ LYS A 268 7828 11837 9830 -708 342 4 N
ATOM 2811 N MET A 269 -27.199 1.920 23.058 1.00 63.28 N
ANISOU 2811 N MET A 269 7699 8213 8133 -1074 287 68 N
ATOM 2812 CA MET A 269 -26.515 1.330 24.204 1.00 60.34 C
ANISOU 2812 CA MET A 269 7571 7646 7710 -1039 293 122 C
ATOM 2813 C MET A 269 -26.181 2.410 25.228 1.00 62.80 C
ANISOU 2813 C MET A 269 7761 8045 8055 -790 270 98 C
ATOM 2814 O MET A 269 -26.380 2.223 26.435 1.00 68.68 O
ANISOU 2814 O MET A 269 8564 8844 8686 -825 309 135 O
ATOM 2815 CB MET A 269 -25.282 0.555 23.730 1.00 54.87 C
ANISOU 2815 CB MET A 269 7168 6594 7086 -958 252 151 C
ATOM 2816 CG MET A 269 -24.187 0.329 24.748 1.00 61.89 C
ANISOU 2816 CG MET A 269 8241 7304 7970 -766 222 209 C
ATOM 2817 SD MET A 269 -22.574 -0.137 24.021 1.00 66.48 S
ANISOU 2817 SD MET A 269 9030 7572 8659 -525 162 244 S
ATOM 2818 CE MET A 269 -21.851 1.433 23.512 1.00 54.30 C
ANISOU 2818 CE MET A 269 7177 6151 7304 -276 62 161 C
ATOM 2819 N LEU A 270 -25.752 3.574 24.768 1.00 60.25 N
ANISOU 2819 N LEU A 270 7286 7744 7864 -564 215 32 N
ATOM 2820 CA LEU A 270 -25.472 4.636 25.711 1.00 60.16 C
ANISOU 2820 CA LEU A 270 7211 7796 7852 -366 200 -3 C
ATOM 2821 C LEU A 270 -26.723 5.045 26.488 1.00 65.85 C
ANISOU 2821 C LEU A 270 7781 8804 8436 -406 293 -9 C
ATOM 2822 O LEU A 270 -26.621 5.363 27.683 1.00 66.38 O
ANISOU 2822 O LEU A 270 7896 8902 8425 -334 313 -9 O
ATOM 2823 CB LEU A 270 -24.854 5.821 24.983 1.00 58.66 C
ANISOU 2823 CB LEU A 270 6930 7559 7799 -159 137 -76 C
ATOM 2824 CG LEU A 270 -23.463 5.509 24.411 1.00 57.33 C
ANISOU 2824 CG LEU A 270 6887 7148 7746 -94 47 -63 C
ATOM 2825 CD1 LEU A 270 -22.887 6.749 23.765 1.00 51.88 C
ANISOU 2825 CD1 LEU A 270 6110 6436 7166 68 -10 -133 C
ATOM 2826 CD2 LEU A 270 -22.533 4.944 25.465 1.00 56.72 C
ANISOU 2826 CD2 LEU A 270 6978 6958 7614 -64 11 -2 C
ATOM 2827 N VAL A 271 -27.903 5.012 25.846 1.00 67.39 N
ANISOU 2827 N VAL A 271 7785 9243 8579 -522 353 -6 N
ATOM 2828 CA VAL A 271 -29.146 5.378 26.530 1.00 61.67 C
ANISOU 2828 CA VAL A 271 6869 8862 7700 -538 454 6 C
ATOM 2829 C VAL A 271 -29.514 4.327 27.570 1.00 65.12 C
ANISOU 2829 C VAL A 271 7419 9345 7979 -779 513 75 C
ATOM 2830 O VAL A 271 -30.071 4.649 28.624 1.00 71.28 O
ANISOU 2830 O VAL A 271 8132 10319 8632 -739 588 84 O
ATOM 2831 CB VAL A 271 -30.299 5.588 25.528 1.00 60.07 C
ANISOU 2831 CB VAL A 271 6387 8980 7456 -598 496 12 C
ATOM 2832 CG1 VAL A 271 -31.671 5.664 26.275 1.00 58.08 C
ANISOU 2832 CG1 VAL A 271 5908 9162 6997 -664 615 57 C
ATOM 2833 CG2 VAL A 271 -30.062 6.832 24.650 1.00 54.33 C
ANISOU 2833 CG2 VAL A 271 5551 8237 6855 -305 458 -49 C
ATOM 2834 N CYS A 272 -29.215 3.055 27.290 1.00 65.29 N
ANISOU 2834 N CYS A 272 7644 9175 7988 -1026 491 126 N
ATOM 2835 CA CYS A 272 -29.454 2.002 28.277 1.00 66.51 C
ANISOU 2835 CA CYS A 272 7982 9309 7981 -1260 547 200 C
ATOM 2836 C CYS A 272 -28.563 2.165 29.491 1.00 67.30 C
ANISOU 2836 C CYS A 272 8258 9232 8081 -1080 521 211 C
ATOM 2837 O CYS A 272 -28.985 1.837 30.609 1.00 65.99 O
ANISOU 2837 O CYS A 272 8146 9167 7760 -1182 586 257 O
ATOM 2838 CB CYS A 272 -29.203 0.618 27.687 1.00 68.48 C
ANISOU 2838 CB CYS A 272 8506 9312 8201 -1531 538 252 C
ATOM 2839 SG CYS A 272 -30.461 0.078 26.595 1.00 78.86 S
ANISOU 2839 SG CYS A 272 9675 10882 9408 -1907 586 259 S
ATOM 2840 N VAL A 273 -27.324 2.629 29.280 1.00 65.03 N
ANISOU 2840 N VAL A 273 8057 8705 7946 -838 424 177 N
ATOM 2841 CA VAL A 273 -26.399 2.833 30.388 1.00 63.41 C
ANISOU 2841 CA VAL A 273 7994 8374 7724 -680 379 191 C
ATOM 2842 C VAL A 273 -26.915 3.926 31.318 1.00 64.23 C
ANISOU 2842 C VAL A 273 7953 8700 7751 -561 427 137 C
ATOM 2843 O VAL A 273 -26.830 3.802 32.541 1.00 71.40 O
ANISOU 2843 O VAL A 273 8963 9627 8538 -566 449 168 O
ATOM 2844 CB VAL A 273 -24.984 3.148 29.856 1.00 63.10 C
ANISOU 2844 CB VAL A 273 8027 8105 7843 -477 260 170 C
ATOM 2845 CG1 VAL A 273 -24.083 3.705 30.982 1.00 61.95 C
ANISOU 2845 CG1 VAL A 273 7948 7929 7662 -316 200 168 C
ATOM 2846 CG2 VAL A 273 -24.370 1.910 29.264 1.00 62.85 C
ANISOU 2846 CG2 VAL A 273 8208 7834 7837 -548 235 245 C
ATOM 2847 N VAL A 274 -27.472 5.002 30.763 1.00 63.76 N
ANISOU 2847 N VAL A 274 7679 8807 7739 -436 455 61 N
ATOM 2848 CA VAL A 274 -27.924 6.088 31.618 1.00 67.54 C
ANISOU 2848 CA VAL A 274 8075 9460 8126 -273 520 6 C
ATOM 2849 C VAL A 274 -29.207 5.690 32.310 1.00 69.97 C
ANISOU 2849 C VAL A 274 8273 10065 8249 -413 650 54 C
ATOM 2850 O VAL A 274 -29.405 6.004 33.485 1.00 73.20 O
ANISOU 2850 O VAL A 274 8722 10566 8525 -356 711 49 O
ATOM 2851 CB VAL A 274 -28.092 7.422 30.851 1.00 65.37 C
ANISOU 2851 CB VAL A 274 7660 9244 7934 -42 526 -82 C
ATOM 2852 CG1 VAL A 274 -26.859 7.767 30.026 1.00 65.01 C
ANISOU 2852 CG1 VAL A 274 7708 8929 8065 46 400 -124 C
ATOM 2853 CG2 VAL A 274 -29.284 7.392 29.988 1.00 65.97 C
ANISOU 2853 CG2 VAL A 274 7491 9584 7989 -83 599 -64 C
ATOM 2854 N VAL A 275 -30.087 4.967 31.615 1.00 70.50 N
ANISOU 2854 N VAL A 275 8203 10305 8280 -627 696 105 N
ATOM 2855 CA VAL A 275 -31.349 4.588 32.239 1.00 70.74 C
ANISOU 2855 CA VAL A 275 8088 10683 8107 -803 822 160 C
ATOM 2856 C VAL A 275 -31.099 3.619 33.383 1.00 70.51 C
ANISOU 2856 C VAL A 275 8294 10541 7956 -997 839 228 C
ATOM 2857 O VAL A 275 -31.636 3.796 34.482 1.00 72.35 O
ANISOU 2857 O VAL A 275 8491 10971 8027 -989 930 244 O
ATOM 2858 CB VAL A 275 -32.329 4.033 31.190 1.00 68.00 C
ANISOU 2858 CB VAL A 275 7530 10586 7721 -1045 856 202 C
ATOM 2859 CG1 VAL A 275 -33.432 3.219 31.850 1.00 65.98 C
ANISOU 2859 CG1 VAL A 275 7188 10650 7231 -1365 967 284 C
ATOM 2860 CG2 VAL A 275 -32.933 5.200 30.422 1.00 65.09 C
ANISOU 2860 CG2 VAL A 275 6860 10480 7392 -792 883 154 C
ATOM 2861 N VAL A 276 -30.226 2.628 33.172 1.00 71.21 N
ANISOU 2861 N VAL A 276 8648 10301 8109 -1132 756 274 N
ATOM 2862 CA VAL A 276 -29.822 1.730 34.259 1.00 73.85 C
ANISOU 2862 CA VAL A 276 9257 10477 8325 -1258 763 351 C
ATOM 2863 C VAL A 276 -29.055 2.481 35.351 1.00 72.21 C
ANISOU 2863 C VAL A 276 9132 10192 8112 -1005 724 319 C
ATOM 2864 O VAL A 276 -29.016 2.038 36.502 1.00 72.03 O
ANISOU 2864 O VAL A 276 9260 10164 7943 -1075 757 376 O
ATOM 2865 CB VAL A 276 -29.013 0.546 33.682 1.00 67.94 C
ANISOU 2865 CB VAL A 276 8802 9377 7637 -1388 693 415 C
ATOM 2866 CG1 VAL A 276 -28.450 -0.301 34.767 1.00 67.16 C
ANISOU 2866 CG1 VAL A 276 9015 9083 7418 -1437 692 507 C
ATOM 2867 CG2 VAL A 276 -29.898 -0.310 32.817 1.00 65.31 C
ANISOU 2867 CG2 VAL A 276 8453 9124 7237 -1723 751 448 C
ATOM 2868 N PHE A 277 -28.473 3.635 35.033 1.00 71.75 N
ANISOU 2868 N PHE A 277 8991 10084 8186 -735 659 226 N
ATOM 2869 CA PHE A 277 -27.825 4.445 36.057 1.00 70.60 C
ANISOU 2869 CA PHE A 277 8931 9894 8000 -543 626 181 C
ATOM 2870 C PHE A 277 -28.852 5.201 36.891 1.00 70.82 C
ANISOU 2870 C PHE A 277 8832 10208 7868 -480 759 138 C
ATOM 2871 O PHE A 277 -28.822 5.146 38.123 1.00 73.90 O
ANISOU 2871 O PHE A 277 9336 10634 8107 -493 793 157 O
ATOM 2872 CB PHE A 277 -26.848 5.423 35.401 1.00 69.81 C
ANISOU 2872 CB PHE A 277 8824 9636 8066 -329 517 94 C
ATOM 2873 CG PHE A 277 -26.026 6.212 36.376 1.00 69.06 C
ANISOU 2873 CG PHE A 277 8853 9474 7911 -193 462 45 C
ATOM 2874 CD1 PHE A 277 -26.467 7.428 36.860 1.00 69.87 C
ANISOU 2874 CD1 PHE A 277 8923 9694 7931 -51 534 -53 C
ATOM 2875 CD2 PHE A 277 -24.816 5.736 36.796 1.00 71.60 C
ANISOU 2875 CD2 PHE A 277 9339 9631 8236 -204 343 100 C
ATOM 2876 CE1 PHE A 277 -25.713 8.141 37.736 1.00 69.29 C
ANISOU 2876 CE1 PHE A 277 9004 9547 7776 25 483 -108 C
ATOM 2877 CE2 PHE A 277 -24.057 6.447 37.673 1.00 74.57 C
ANISOU 2877 CE2 PHE A 277 9814 9990 8531 -125 279 58 C
ATOM 2878 CZ PHE A 277 -24.507 7.648 38.148 1.00 73.32 C
ANISOU 2878 CZ PHE A 277 9649 9923 8287 -37 348 -54 C
ATOM 2879 N ALA A 278 -29.765 5.913 36.221 1.00 70.20 N
ANISOU 2879 N ALA A 278 8519 10348 7806 -387 839 86 N
ATOM 2880 CA ALA A 278 -30.753 6.756 36.889 1.00 72.69 C
ANISOU 2880 CA ALA A 278 8699 10958 7963 -243 983 47 C
ATOM 2881 C ALA A 278 -31.802 5.947 37.648 1.00 78.36 C
ANISOU 2881 C ALA A 278 9330 11967 8478 -461 1108 135 C
ATOM 2882 O ALA A 278 -32.249 6.379 38.712 1.00 78.84 O
ANISOU 2882 O ALA A 278 9391 12196 8367 -370 1214 120 O
ATOM 2883 CB ALA A 278 -31.449 7.650 35.873 1.00 68.94 C
ANISOU 2883 CB ALA A 278 7987 10662 7545 -50 1038 -4 C
ATOM 2884 N VAL A 279 -32.225 4.793 37.128 1.00 79.03 N
ANISOU 2884 N VAL A 279 9355 12117 8554 -764 1108 223 N
ATOM 2885 CA VAL A 279 -33.170 3.972 37.885 1.00 79.65 C
ANISOU 2885 CA VAL A 279 9383 12466 8414 -1034 1226 312 C
ATOM 2886 C VAL A 279 -32.496 3.369 39.115 1.00 77.00 C
ANISOU 2886 C VAL A 279 9354 11916 7987 -1124 1201 358 C
ATOM 2887 O VAL A 279 -33.109 3.250 40.178 1.00 79.45 O
ANISOU 2887 O VAL A 279 9653 12439 8094 -1199 1311 395 O
ATOM 2888 CB VAL A 279 -33.803 2.886 36.989 1.00 76.42 C
ANISOU 2888 CB VAL A 279 8879 12171 7985 -1397 1233 390 C
ATOM 2889 CG1 VAL A 279 -34.689 1.963 37.813 1.00 73.07 C
ANISOU 2889 CG1 VAL A 279 8451 12001 7310 -1744 1350 489 C
ATOM 2890 CG2 VAL A 279 -34.622 3.538 35.874 1.00 71.47 C
ANISOU 2890 CG2 VAL A 279 7895 11859 7401 -1305 1267 358 C
ATOM 2891 N CYS A 280 -31.222 2.998 39.006 1.00 78.10 N
ANISOU 2891 N CYS A 280 9758 11660 8258 -1098 1059 365 N
ATOM 2892 CA CYS A 280 -30.575 2.363 40.152 1.00 81.04 C
ANISOU 2892 CA CYS A 280 10414 11856 8523 -1167 1029 432 C
ATOM 2893 C CYS A 280 -30.302 3.353 41.287 1.00 83.29 C
ANISOU 2893 C CYS A 280 10735 12193 8720 -940 1043 366 C
ATOM 2894 O CYS A 280 -30.302 2.957 42.454 1.00 89.46 O
ANISOU 2894 O CYS A 280 11664 12998 9329 -1022 1081 422 O
ATOM 2895 CB CYS A 280 -29.291 1.660 39.704 1.00 74.69 C
ANISOU 2895 CB CYS A 280 9860 10664 7855 -1163 879 479 C
ATOM 2896 SG CYS A 280 -29.609 0.071 38.885 1.00 76.62 S
ANISOU 2896 SG CYS A 280 10253 10774 8084 -1508 900 591 S
ATOM 2897 N TRP A 281 -30.073 4.627 40.976 1.00 79.06 N
ANISOU 2897 N TRP A 281 10102 11659 8277 -672 1021 247 N
ATOM 2898 CA TRP A 281 -29.873 5.671 41.974 1.00 77.85 C
ANISOU 2898 CA TRP A 281 10024 11538 8016 -471 1050 163 C
ATOM 2899 C TRP A 281 -31.176 6.308 42.434 1.00 79.47 C
ANISOU 2899 C TRP A 281 10052 12092 8051 -381 1243 127 C
ATOM 2900 O TRP A 281 -31.167 7.136 43.357 1.00 80.45 O
ANISOU 2900 O TRP A 281 10272 12256 8040 -216 1303 56 O
ATOM 2901 CB TRP A 281 -28.966 6.766 41.411 1.00 79.91 C
ANISOU 2901 CB TRP A 281 10331 11602 8429 -246 942 51 C
ATOM 2902 CG TRP A 281 -27.549 6.375 41.358 1.00 79.25 C
ANISOU 2902 CG TRP A 281 10427 11240 8445 -284 760 81 C
ATOM 2903 CD1 TRP A 281 -26.849 5.971 40.270 1.00 78.38 C
ANISOU 2903 CD1 TRP A 281 10300 10952 8529 -305 642 109 C
ATOM 2904 CD2 TRP A 281 -26.644 6.350 42.453 1.00 78.43 C
ANISOU 2904 CD2 TRP A 281 10528 11043 8228 -292 677 98 C
ATOM 2905 NE1 TRP A 281 -25.554 5.690 40.618 1.00 78.38 N
ANISOU 2905 NE1 TRP A 281 10465 10774 8543 -301 496 151 N
ATOM 2906 CE2 TRP A 281 -25.402 5.918 41.959 1.00 76.39 C
ANISOU 2906 CE2 TRP A 281 10342 10581 8100 -301 507 148 C
ATOM 2907 CE3 TRP A 281 -26.762 6.650 43.809 1.00 78.79 C
ANISOU 2907 CE3 TRP A 281 10697 11181 8058 -288 731 81 C
ATOM 2908 CZ2 TRP A 281 -24.284 5.782 42.774 1.00 74.23 C
ANISOU 2908 CZ2 TRP A 281 10228 10234 7741 -302 382 192 C
ATOM 2909 CZ3 TRP A 281 -25.652 6.509 44.610 1.00 78.06 C
ANISOU 2909 CZ3 TRP A 281 10789 10986 7886 -315 600 115 C
ATOM 2910 CH2 TRP A 281 -24.431 6.073 44.090 1.00 74.78 C
ANISOU 2910 CH2 TRP A 281 10410 10405 7598 -320 424 176 C
ATOM 2911 N LEU A 282 -32.289 5.957 41.790 1.00 79.12 N
ANISOU 2911 N LEU A 282 9749 12322 7990 -481 1344 175 N
ATOM 2912 CA LEU A 282 -33.565 6.576 42.138 1.00 76.41 C
ANISOU 2912 CA LEU A 282 9177 12385 7470 -354 1536 158 C
ATOM 2913 C LEU A 282 -33.969 6.263 43.573 1.00 83.61 C
ANISOU 2913 C LEU A 282 10172 13462 8134 -449 1648 202 C
ATOM 2914 O LEU A 282 -34.323 7.205 44.307 1.00 81.00 O
ANISOU 2914 O LEU A 282 9846 13272 7658 -203 1768 134 O
ATOM 2915 CB LEU A 282 -34.631 6.155 41.124 1.00 71.88 C
ANISOU 2915 CB LEU A 282 8271 12133 6908 -489 1601 222 C
ATOM 2916 CG LEU A 282 -35.998 6.805 41.302 1.00 74.25 C
ANISOU 2916 CG LEU A 282 8253 12940 7018 -319 1801 228 C
ATOM 2917 CD1 LEU A 282 -35.923 8.362 41.367 1.00 72.51 C
ANISOU 2917 CD1 LEU A 282 8066 12687 6799 165 1864 109 C
ATOM 2918 CD2 LEU A 282 -36.891 6.330 40.177 1.00 73.73 C
ANISOU 2918 CD2 LEU A 282 7844 13200 6969 -495 1822 301 C
ATOM 2919 N PRO A 283 -33.935 4.980 44.057 1.00 87.79 N
ANISOU 2919 N PRO A 283 10807 13965 8584 -790 1627 316 N
ATOM 2920 CA PRO A 283 -34.276 4.730 45.467 1.00 86.67 C
ANISOU 2920 CA PRO A 283 10766 13971 8195 -875 1734 359 C
ATOM 2921 C PRO A 283 -33.440 5.550 46.431 1.00 88.70 C
ANISOU 2921 C PRO A 283 11275 14023 8403 -642 1694 270 C
ATOM 2922 O PRO A 283 -33.974 6.401 47.150 1.00 90.67 O
ANISOU 2922 O PRO A 283 11491 14472 8486 -442 1834 205 O
ATOM 2923 CB PRO A 283 -33.999 3.234 45.634 1.00 84.49 C
ANISOU 2923 CB PRO A 283 10668 13543 7890 -1256 1668 492 C
ATOM 2924 CG PRO A 283 -34.224 2.672 44.287 1.00 85.27 C
ANISOU 2924 CG PRO A 283 10630 13631 8139 -1425 1621 528 C
ATOM 2925 CD PRO A 283 -33.752 3.716 43.318 1.00 83.71 C
ANISOU 2925 CD PRO A 283 10332 13311 8164 -1113 1538 413 C
ATOM 2926 N LEU A 284 -32.125 5.313 46.431 1.00 88.79 N
ANISOU 2926 N LEU A 284 11539 13656 8540 -664 1507 268 N
ATOM 2927 CA LEU A 284 -31.249 5.951 47.410 1.00 89.45 C
ANISOU 2927 CA LEU A 284 11872 13571 8543 -525 1444 199 C
ATOM 2928 C LEU A 284 -31.479 7.457 47.479 1.00 87.21 C
ANISOU 2928 C LEU A 284 11568 13350 8216 -218 1531 45 C
ATOM 2929 O LEU A 284 -31.494 8.039 48.570 1.00 83.86 O
ANISOU 2929 O LEU A 284 11301 12968 7595 -123 1603 -14 O
ATOM 2930 CB LEU A 284 -29.784 5.660 47.082 1.00 84.88 C
ANISOU 2930 CB LEU A 284 11480 12641 8129 -550 1217 216 C
ATOM 2931 CG LEU A 284 -28.858 6.139 48.195 1.00 84.09 C
ANISOU 2931 CG LEU A 284 11626 12425 7899 -485 1135 172 C
ATOM 2932 CD1 LEU A 284 -28.845 5.126 49.310 1.00 90.52 C
ANISOU 2932 CD1 LEU A 284 12587 13282 8524 -666 1145 301 C
ATOM 2933 CD2 LEU A 284 -27.477 6.388 47.669 1.00 81.47 C
ANISOU 2933 CD2 LEU A 284 11389 11836 7729 -428 925 144 C
ATOM 2934 N HIS A 285 -31.657 8.104 46.314 1.00 83.90 N
ANISOU 2934 N HIS A 285 10994 12920 7963 -54 1531 -20 N
ATOM 2935 CA HIS A 285 -31.798 9.560 46.284 1.00 86.24 C
ANISOU 2935 CA HIS A 285 11342 13211 8216 265 1615 -163 C
ATOM 2936 C HIS A 285 -33.189 9.998 46.726 1.00 85.50 C
ANISOU 2936 C HIS A 285 11083 13493 7912 440 1865 -169 C
ATOM 2937 O HIS A 285 -33.348 11.071 47.324 1.00 81.05 O
ANISOU 2937 O HIS A 285 10673 12932 7189 700 1982 -274 O
ATOM 2938 CB HIS A 285 -31.497 10.094 44.884 1.00 87.20 C
ANISOU 2938 CB HIS A 285 11377 13184 8571 395 1534 -216 C
ATOM 2939 CG HIS A 285 -30.050 10.094 44.528 1.00 89.26 C
ANISOU 2939 CG HIS A 285 11827 13089 9000 313 1312 -247 C
ATOM 2940 ND1 HIS A 285 -29.593 9.824 43.259 1.00 88.50 N
ANISOU 2940 ND1 HIS A 285 11624 12857 9145 269 1187 -225 N
ATOM 2941 CD2 HIS A 285 -28.951 10.338 45.278 1.00 87.74 C
ANISOU 2941 CD2 HIS A 285 11904 12687 8747 262 1193 -292 C
ATOM 2942 CE1 HIS A 285 -28.271 9.894 43.243 1.00 87.54 C
ANISOU 2942 CE1 HIS A 285 11684 12469 9107 210 1008 -250 C
ATOM 2943 NE2 HIS A 285 -27.857 10.205 44.458 1.00 84.44 N
ANISOU 2943 NE2 HIS A 285 11510 12043 8530 195 1002 -287 N
ATOM 2944 N ALA A 286 -34.208 9.205 46.385 1.00 87.26 N
ANISOU 2944 N ALA A 286 10995 14048 8113 305 1956 -56 N
ATOM 2945 CA ALA A 286 -35.536 9.375 46.959 1.00 84.97 C
ANISOU 2945 CA ALA A 286 10498 14205 7581 411 2193 -23 C
ATOM 2946 C ALA A 286 -35.450 9.390 48.475 1.00 90.41 C
ANISOU 2946 C ALA A 286 11418 14903 8029 386 2270 -38 C
ATOM 2947 O ALA A 286 -35.867 10.350 49.132 1.00 89.62 O
ANISOU 2947 O ALA A 286 11398 14914 7738 677 2434 -120 O
ATOM 2948 CB ALA A 286 -36.462 8.254 46.488 1.00 82.99 C
ANISOU 2948 CB ALA A 286 9904 14312 7318 121 2239 122 C
ATOM 2949 N PHE A 287 -34.898 8.322 49.041 1.00 92.53 N
ANISOU 2949 N PHE A 287 11824 15044 8291 53 2158 44 N
ATOM 2950 CA PHE A 287 -34.464 8.302 50.429 1.00 96.27 C
ANISOU 2950 CA PHE A 287 12582 15427 8570 3 2165 28 C
ATOM 2951 C PHE A 287 -33.721 9.580 50.801 1.00 96.89 C
ANISOU 2951 C PHE A 287 12953 15247 8614 274 2136 -133 C
ATOM 2952 O PHE A 287 -34.218 10.378 51.598 1.00100.07 O
ANISOU 2952 O PHE A 287 13452 15780 8791 487 2309 -211 O
ATOM 2953 CB PHE A 287 -33.573 7.089 50.669 1.00 98.50 C
ANISOU 2953 CB PHE A 287 13028 15477 8920 -331 1979 135 C
ATOM 2954 CG PHE A 287 -33.684 6.524 52.037 1.00101.88 C
ANISOU 2954 CG PHE A 287 13610 16000 9100 -494 2040 204 C
ATOM 2955 CD1 PHE A 287 -34.896 6.024 52.488 1.00105.50 C
ANISOU 2955 CD1 PHE A 287 13881 16841 9362 -622 2235 291 C
ATOM 2956 CD2 PHE A 287 -32.582 6.469 52.865 1.00100.80 C
ANISOU 2956 CD2 PHE A 287 13787 15603 8908 -538 1899 194 C
ATOM 2957 CE1 PHE A 287 -35.013 5.492 53.742 1.00108.39 C
ANISOU 2957 CE1 PHE A 287 14398 17296 9489 -785 2297 360 C
ATOM 2958 CE2 PHE A 287 -32.685 5.930 54.124 1.00109.25 C
ANISOU 2958 CE2 PHE A 287 15007 16765 9739 -686 1952 268 C
ATOM 2959 CZ PHE A 287 -33.907 5.438 54.565 1.00112.29 C
ANISOU 2959 CZ PHE A 287 15229 17499 9937 -809 2156 349 C
ATOM 2960 N GLN A 288 -32.544 9.794 50.207 1.00 98.46 N
ANISOU 2960 N GLN A 288 13308 15088 9015 260 1927 -186 N
ATOM 2961 CA GLN A 288 -31.707 10.935 50.577 1.00 99.31 C
ANISOU 2961 CA GLN A 288 13733 14932 9067 421 1873 -337 C
ATOM 2962 C GLN A 288 -32.497 12.241 50.620 1.00 98.36 C
ANISOU 2962 C GLN A 288 13660 14908 8803 780 2089 -463 C
ATOM 2963 O GLN A 288 -32.321 13.044 51.538 1.00 95.41 O
ANISOU 2963 O GLN A 288 13590 14447 8215 896 2162 -572 O
ATOM 2964 CB GLN A 288 -30.519 11.050 49.614 1.00 95.64 C
ANISOU 2964 CB GLN A 288 13333 14149 8857 366 1641 -368 C
ATOM 2965 CG GLN A 288 -29.417 10.047 49.912 1.00 96.41 C
ANISOU 2965 CG GLN A 288 13518 14098 9015 91 1423 -270 C
ATOM 2966 CD GLN A 288 -28.220 10.155 48.979 1.00 98.97 C
ANISOU 2966 CD GLN A 288 13874 14161 9568 53 1204 -290 C
ATOM 2967 OE1 GLN A 288 -28.184 10.989 48.069 1.00 99.34 O
ANISOU 2967 OE1 GLN A 288 13894 14110 9742 202 1206 -383 O
ATOM 2968 NE2 GLN A 288 -27.228 9.298 49.203 1.00101.10 N
ANISOU 2968 NE2 GLN A 288 14203 14333 9877 -131 1020 -190 N
ATOM 2969 N LEU A 289 -33.382 12.467 49.647 1.00 97.23 N
ANISOU 2969 N LEU A 289 13239 14952 8752 973 2202 -444 N
ATOM 2970 CA LEU A 289 -34.161 13.704 49.653 1.00 96.11 C
ANISOU 2970 CA LEU A 289 13149 14913 8456 1383 2425 -543 C
ATOM 2971 C LEU A 289 -35.212 13.689 50.752 1.00100.23 C
ANISOU 2971 C LEU A 289 13615 15792 8674 1498 2670 -515 C
ATOM 2972 O LEU A 289 -35.430 14.701 51.431 1.00100.23 O
ANISOU 2972 O LEU A 289 13879 15756 8446 1786 2836 -626 O
ATOM 2973 CB LEU A 289 -34.838 13.925 48.302 1.00 91.77 C
ANISOU 2973 CB LEU A 289 12284 14517 8066 1585 2476 -508 C
ATOM 2974 CG LEU A 289 -35.957 14.980 48.366 1.00 85.94 C
ANISOU 2974 CG LEU A 289 11505 14027 7120 2059 2755 -552 C
ATOM 2975 CD1 LEU A 289 -35.367 16.384 48.432 1.00 82.73 C
ANISOU 2975 CD1 LEU A 289 11567 13226 6642 2353 2786 -724 C
ATOM 2976 CD2 LEU A 289 -36.994 14.856 47.246 1.00 79.90 C
ANISOU 2976 CD2 LEU A 289 10279 13640 6440 2225 2841 -450 C
ATOM 2977 N ALA A 290 -35.886 12.552 50.926 1.00103.57 N
ANISOU 2977 N ALA A 290 13717 16561 9073 1268 2705 -366 N
ATOM 2978 CA ALA A 290 -36.963 12.461 51.906 1.00106.20 C
ANISOU 2978 CA ALA A 290 13934 17304 9112 1350 2947 -319 C
ATOM 2979 C ALA A 290 -36.425 12.510 53.332 1.00108.29 C
ANISOU 2979 C ALA A 290 14571 17410 9163 1252 2950 -376 C
ATOM 2980 O ALA A 290 -36.812 13.378 54.120 1.00110.63 O
ANISOU 2980 O ALA A 290 15061 17769 9203 1535 3145 -468 O
ATOM 2981 CB ALA A 290 -37.773 11.182 51.681 1.00106.97 C
ANISOU 2981 CB ALA A 290 13608 17811 9226 1049 2971 -140 C
ATOM 2982 N VAL A 291 -35.528 11.591 53.686 1.00108.76 N
ANISOU 2982 N VAL A 291 14752 17267 9304 871 2740 -320 N
ATOM 2983 CA VAL A 291 -35.085 11.483 55.074 1.00116.44 C
ANISOU 2983 CA VAL A 291 16032 18158 10052 743 2735 -343 C
ATOM 2984 C VAL A 291 -33.924 12.434 55.354 1.00113.61 C
ANISOU 2984 C VAL A 291 16107 17383 9676 821 2609 -504 C
ATOM 2985 O VAL A 291 -33.112 12.193 56.255 1.00109.23 O
ANISOU 2985 O VAL A 291 15813 16674 9015 617 2487 -512 O
ATOM 2986 CB VAL A 291 -34.719 10.028 55.431 1.00119.77 C
ANISOU 2986 CB VAL A 291 16399 18592 10515 321 2587 -185 C
ATOM 2987 CG1 VAL A 291 -35.938 9.129 55.284 1.00121.24 C
ANISOU 2987 CG1 VAL A 291 16210 19206 10650 185 2738 -35 C
ATOM 2988 CG2 VAL A 291 -33.586 9.521 54.564 1.00118.29 C
ANISOU 2988 CG2 VAL A 291 16245 18074 10624 135 2306 -151 C
ATOM 2989 N ASP A 292 -33.832 13.518 54.585 1.00116.75 N
ANISOU 2989 N ASP A 292 16593 17608 10158 1096 2634 -627 N
ATOM 2990 CA ASP A 292 -32.968 14.643 54.918 1.00121.06 C
ANISOU 2990 CA ASP A 292 17595 17798 10605 1191 2583 -802 C
ATOM 2991 C ASP A 292 -33.739 15.954 54.976 1.00120.61 C
ANISOU 2991 C ASP A 292 17718 17757 10350 1631 2851 -935 C
ATOM 2992 O ASP A 292 -33.133 17.001 55.245 1.00122.46 O
ANISOU 2992 O ASP A 292 18399 17672 10460 1723 2848 -1096 O
ATOM 2993 CB ASP A 292 -31.800 14.770 53.923 1.00123.79 C
ANISOU 2993 CB ASP A 292 18003 17805 11226 1058 2321 -836 C
ATOM 2994 CG ASP A 292 -30.727 13.698 54.123 1.00125.02 C
ANISOU 2994 CG ASP A 292 18131 17871 11499 667 2048 -734 C
ATOM 2995 OD1 ASP A 292 -30.656 13.118 55.228 1.00126.74 O
ANISOU 2995 OD1 ASP A 292 18426 18193 11537 499 2043 -677 O
ATOM 2996 OD2 ASP A 292 -29.947 13.444 53.177 1.00122.68 O
ANISOU 2996 OD2 ASP A 292 17745 17408 11461 552 1845 -704 O
ATOM 2997 N ILE A 293 -35.047 15.932 54.688 1.00117.49 N
ANISOU 2997 N ILE A 293 16999 17733 9909 1908 3084 -864 N
ATOM 2998 CA ILE A 293 -35.966 16.993 55.107 1.00114.50 C
ANISOU 2998 CA ILE A 293 16775 17481 9247 2370 3397 -952 C
ATOM 2999 C ILE A 293 -36.819 16.567 56.305 1.00116.69 C
ANISOU 2999 C ILE A 293 16957 18144 9234 2383 3604 -890 C
ATOM 3000 O ILE A 293 -37.440 17.429 56.950 1.00115.74 O
ANISOU 3000 O ILE A 293 16998 18032 8946 2659 3791 -968 O
ATOM 3001 CB ILE A 293 -36.886 17.464 53.950 1.00107.13 C
ANISOU 3001 CB ILE A 293 15544 16752 8409 2770 3547 -914 C
ATOM 3002 CG1 ILE A 293 -37.559 16.287 53.238 1.00104.96 C
ANISOU 3002 CG1 ILE A 293 14649 16904 8326 2588 3501 -720 C
ATOM 3003 CG2 ILE A 293 -36.131 18.322 52.951 1.00103.69 C
ANISOU 3003 CG2 ILE A 293 15362 15883 8154 2885 3425 -1022 C
ATOM 3004 CD1 ILE A 293 -38.517 16.710 52.145 1.00103.49 C
ANISOU 3004 CD1 ILE A 293 14114 16966 8240 2936 3615 -663 C
ATOM 3005 N ASP A 294 -36.851 15.271 56.629 1.00116.30 N
ANISOU 3005 N ASP A 294 16625 18318 9244 1998 3500 -743 N
ATOM 3006 CA ASP A 294 -37.640 14.715 57.726 1.00115.60 C
ANISOU 3006 CA ASP A 294 16415 18617 8892 1936 3679 -660 C
ATOM 3007 C ASP A 294 -36.878 14.771 59.051 1.00116.34 C
ANISOU 3007 C ASP A 294 16955 18478 8770 1748 3622 -742 C
ATOM 3008 O ASP A 294 -37.349 15.386 60.013 1.00120.95 O
ANISOU 3008 O ASP A 294 17750 19138 9069 1949 3829 -820 O
ATOM 3009 CB ASP A 294 -38.055 13.278 57.368 1.00116.89 C
ANISOU 3009 CB ASP A 294 16098 19108 9205 1579 3597 -457 C
ATOM 3010 CG ASP A 294 -38.203 12.373 58.583 1.00121.23 C
ANISOU 3010 CG ASP A 294 16661 19852 9549 1273 3629 -364 C
ATOM 3011 OD1 ASP A 294 -39.008 12.696 59.484 1.00125.15 O
ANISOU 3011 OD1 ASP A 294 17173 20644 9735 1461 3885 -377 O
ATOM 3012 OD2 ASP A 294 -37.528 11.320 58.624 1.00120.35 O
ANISOU 3012 OD2 ASP A 294 16551 19602 9574 860 3409 -269 O
ATOM 3013 N SER A 295 -35.704 14.134 59.110 1.00113.50 N
ANISOU 3013 N SER A 295 16724 17833 8567 1353 3325 -717 N
ATOM 3014 CA SER A 295 -34.866 14.112 60.313 1.00112.97 C
ANISOU 3014 CA SER A 295 17051 17570 8301 1135 3225 -775 C
ATOM 3015 C SER A 295 -35.580 13.429 61.478 1.00121.15 C
ANISOU 3015 C SER A 295 18007 18952 9072 1030 3384 -677 C
ATOM 3016 O SER A 295 -35.453 13.838 62.636 1.00125.01 O
ANISOU 3016 O SER A 295 18834 19402 9262 1048 3467 -762 O
ATOM 3017 CB SER A 295 -34.414 15.521 60.707 1.00111.05 C
ANISOU 3017 CB SER A 295 17320 17014 7860 1357 3288 -995 C
ATOM 3018 OG SER A 295 -33.011 15.669 60.572 1.00110.69 O
ANISOU 3018 OG SER A 295 17546 16585 7925 1100 2996 -1063 O
ATOM 3019 N GLN A 296 -36.344 12.379 61.168 1.00123.61 N
ANISOU 3019 N GLN A 296 17883 19609 9474 894 3429 -498 N
ATOM 3020 CA GLN A 296 -37.033 11.580 62.189 1.00128.05 C
ANISOU 3020 CA GLN A 296 18336 20523 9796 727 3569 -377 C
ATOM 3021 C GLN A 296 -37.173 10.164 61.626 1.00126.39 C
ANISOU 3021 C GLN A 296 17772 20461 9790 368 3444 -173 C
ATOM 3022 O GLN A 296 -38.162 9.839 60.966 1.00124.47 O
ANISOU 3022 O GLN A 296 17129 20560 9604 398 3573 -82 O
ATOM 3023 CB GLN A 296 -38.382 12.176 62.570 1.00128.95 C
ANISOU 3023 CB GLN A 296 18303 21053 9640 1077 3931 -402 C
ATOM 3024 CG GLN A 296 -38.327 13.178 63.719 1.00130.46 C
ANISOU 3024 CG GLN A 296 18910 21064 9596 1258 4045 -570 C
ATOM 3025 CD GLN A 296 -37.932 12.539 65.042 1.00132.73 C
ANISOU 3025 CD GLN A 296 19431 21374 9628 958 4008 -525 C
ATOM 3026 OE1 GLN A 296 -38.562 11.583 65.496 1.00133.86 O
ANISOU 3026 OE1 GLN A 296 19336 21820 9705 743 4078 -369 O
ATOM 3027 NE2 GLN A 296 -36.883 13.065 65.665 1.00132.31 N
ANISOU 3027 NE2 GLN A 296 19855 20978 9437 914 3884 -656 N
ATOM 3028 N VAL A 297 -36.169 9.331 61.901 1.00124.19 N
ANISOU 3028 N VAL A 297 17663 19930 9593 29 3195 -98 N
ATOM 3029 CA VAL A 297 -36.111 7.978 61.363 1.00116.84 C
ANISOU 3029 CA VAL A 297 16516 19028 8848 -312 3058 88 C
ATOM 3030 C VAL A 297 -35.479 7.034 62.383 1.00114.17 C
ANISOU 3030 C VAL A 297 16417 18588 8375 -626 2934 201 C
ATOM 3031 O VAL A 297 -34.414 6.455 62.134 1.00110.25 O
ANISOU 3031 O VAL A 297 16055 17792 8044 -798 2678 263 O
ATOM 3032 CB VAL A 297 -35.348 7.955 60.021 1.00108.01 C
ANISOU 3032 CB VAL A 297 15332 17610 8097 -315 2831 74 C
ATOM 3033 CG1 VAL A 297 -36.310 8.211 58.851 1.00103.12 C
ANISOU 3033 CG1 VAL A 297 14332 17224 7624 -151 2961 72 C
ATOM 3034 CG2 VAL A 297 -34.198 8.983 60.029 1.00103.58 C
ANISOU 3034 CG2 VAL A 297 15092 16673 7592 -148 2674 -93 C
ATOM 3035 N LEU A 298 -36.130 6.866 63.538 1.00118.43 N
ANISOU 3035 N LEU A 298 17009 19393 8597 -682 3119 241 N
ATOM 3036 CA LEU A 298 -35.696 5.895 64.534 1.00122.11 C
ANISOU 3036 CA LEU A 298 17685 19810 8900 -982 3032 375 C
ATOM 3037 C LEU A 298 -36.278 4.503 64.276 1.00125.63 C
ANISOU 3037 C LEU A 298 17934 20424 9376 -1318 3059 586 C
ATOM 3038 O LEU A 298 -36.272 3.651 65.176 1.00128.47 O
ANISOU 3038 O LEU A 298 18447 20829 9536 -1568 3067 719 O
ATOM 3039 CB LEU A 298 -36.048 6.377 65.946 1.00121.76 C
ANISOU 3039 CB LEU A 298 17840 19946 8478 -906 3213 314 C
ATOM 3040 CG LEU A 298 -35.372 5.680 67.139 1.00120.45 C
ANISOU 3040 CG LEU A 298 17984 19678 8103 -1150 3097 413 C
ATOM 3041 CD1 LEU A 298 -33.894 6.041 67.243 1.00119.64 C
ANISOU 3041 CD1 LEU A 298 18186 19194 8078 -1128 2810 342 C
ATOM 3042 CD2 LEU A 298 -36.109 5.954 68.452 1.00120.62 C
ANISOU 3042 CD2 LEU A 298 18110 19991 7730 -1116 3344 387 C
ATOM 3043 N ASP A 299 -36.776 4.252 63.067 1.00119.64 N
ANISOU 3043 N ASP A 299 16867 19749 8840 -1349 3074 622 N
ATOM 3044 CA ASP A 299 -37.162 2.902 62.657 1.00120.37 C
ANISOU 3044 CA ASP A 299 16837 19918 8981 -1721 3061 813 C
ATOM 3045 C ASP A 299 -35.958 2.088 62.187 1.00117.71 C
ANISOU 3045 C ASP A 299 16728 19132 8863 -1877 2778 899 C
ATOM 3046 O ASP A 299 -36.088 1.245 61.299 1.00116.12 O
ANISOU 3046 O ASP A 299 16426 18872 8821 -2086 2726 1002 O
ATOM 3047 CB ASP A 299 -38.230 2.982 61.568 1.00123.29 C
ANISOU 3047 CB ASP A 299 16778 20605 9460 -1713 3197 815 C
ATOM 3048 CG ASP A 299 -37.813 3.872 60.409 1.00123.80 C
ANISOU 3048 CG ASP A 299 16734 20483 9823 -1408 3090 677 C
ATOM 3049 OD1 ASP A 299 -37.130 4.889 60.663 1.00125.12 O
ANISOU 3049 OD1 ASP A 299 17092 20436 10013 -1108 3031 528 O
ATOM 3050 OD2 ASP A 299 -38.161 3.557 59.249 1.00122.56 O
ANISOU 3050 OD2 ASP A 299 16320 20389 9859 -1492 3066 716 O
ATOM 3051 N LEU A 300 -34.785 2.307 62.795 1.00118.24 N
ANISOU 3051 N LEU A 300 17109 18903 8913 -1781 2600 867 N
ATOM 3052 CA LEU A 300 -33.499 1.837 62.280 1.00117.33 C
ANISOU 3052 CA LEU A 300 17174 18390 9015 -1804 2322 923 C
ATOM 3053 C LEU A 300 -33.378 0.318 62.193 1.00119.07 C
ANISOU 3053 C LEU A 300 17527 18480 9233 -2109 2260 1142 C
ATOM 3054 O LEU A 300 -32.438 -0.170 61.552 1.00116.29 O
ANISOU 3054 O LEU A 300 17288 17817 9078 -2102 2058 1205 O
ATOM 3055 CB LEU A 300 -32.364 2.398 63.141 1.00115.00 C
ANISOU 3055 CB LEU A 300 17158 17918 8617 -1663 2164 860 C
ATOM 3056 CG LEU A 300 -32.403 3.907 63.419 1.00110.01 C
ANISOU 3056 CG LEU A 300 16521 17360 7917 -1396 2233 636 C
ATOM 3057 CD1 LEU A 300 -31.827 4.224 64.803 1.00107.86 C
ANISOU 3057 CD1 LEU A 300 16550 17076 7354 -1393 2190 607 C
ATOM 3058 CD2 LEU A 300 -31.675 4.694 62.333 1.00101.90 C
ANISOU 3058 CD2 LEU A 300 15432 16111 7176 -1206 2078 505 C
ATOM 3059 N LYS A 301 -34.272 -0.442 62.834 1.00123.31 N
ANISOU 3059 N LYS A 301 18085 19235 9532 -2373 2434 1264 N
ATOM 3060 CA LYS A 301 -34.352 -1.869 62.538 1.00123.18 C
ANISOU 3060 CA LYS A 301 18206 19082 9513 -2697 2412 1462 C
ATOM 3061 C LYS A 301 -34.892 -2.096 61.130 1.00126.33 C
ANISOU 3061 C LYS A 301 18351 19505 10144 -2800 2439 1450 C
ATOM 3062 O LYS A 301 -34.507 -3.064 60.460 1.00128.05 O
ANISOU 3062 O LYS A 301 18725 19448 10480 -2964 2338 1565 O
ATOM 3063 CB LYS A 301 -35.209 -2.575 63.591 1.00118.45 C
ANISOU 3063 CB LYS A 301 17709 18725 8573 -2997 2602 1591 C
ATOM 3064 CG LYS A 301 -34.658 -2.414 64.999 1.00114.46 C
ANISOU 3064 CG LYS A 301 17477 18190 7822 -2907 2569 1614 C
ATOM 3065 CD LYS A 301 -35.590 -2.978 66.055 1.00113.45 C
ANISOU 3065 CD LYS A 301 17350 18246 7511 -3082 2723 1694 C
ATOM 3066 CE LYS A 301 -35.113 -2.606 67.463 1.00113.11 C
ANISOU 3066 CE LYS A 301 17526 18212 7238 -2943 2698 1681 C
ATOM 3067 NZ LYS A 301 -35.932 -3.236 68.550 1.00115.87 N
ANISOU 3067 NZ LYS A 301 17915 18714 7395 -3121 2839 1777 N
ATOM 3068 N GLU A 302 -35.762 -1.204 60.661 1.00125.77 N
ANISOU 3068 N GLU A 302 17905 19757 10124 -2684 2577 1316 N
ATOM 3069 CA GLU A 302 -36.122 -1.130 59.252 1.00120.43 C
ANISOU 3069 CA GLU A 302 16951 19113 9694 -2693 2568 1273 C
ATOM 3070 C GLU A 302 -35.197 -0.179 58.492 1.00118.50 C
ANISOU 3070 C GLU A 302 16665 18618 9740 -2329 2395 1125 C
ATOM 3071 O GLU A 302 -34.691 -0.535 57.425 1.00121.35 O
ANISOU 3071 O GLU A 302 17034 18729 10346 -2349 2255 1142 O
ATOM 3072 CB GLU A 302 -37.585 -0.690 59.097 1.00117.09 C
ANISOU 3072 CB GLU A 302 16113 19225 9149 -2742 2811 1230 C
ATOM 3073 CG GLU A 302 -38.596 -1.833 58.985 1.00115.50 C
ANISOU 3073 CG GLU A 302 15819 19250 8814 -3200 2931 1380 C
ATOM 3074 CD GLU A 302 -39.202 -2.238 60.320 1.00122.69 C
ANISOU 3074 CD GLU A 302 16805 20309 9504 -3326 3040 1447 C
ATOM 3075 OE1 GLU A 302 -38.893 -1.597 61.349 1.00124.30 O
ANISOU 3075 OE1 GLU A 302 17132 20540 9557 -3101 3078 1394 O
ATOM 3076 OE2 GLU A 302 -39.996 -3.203 60.340 1.00127.16 O
ANISOU 3076 OE2 GLU A 302 17318 20963 10034 -3668 3084 1547 O
ATOM 3077 N TYR A 303 -34.940 1.012 59.049 1.00114.16 N
ANISOU 3077 N TYR A 303 16110 18118 9146 -2016 2405 980 N
ATOM 3078 CA TYR A 303 -34.222 2.057 58.314 1.00110.11 C
ANISOU 3078 CA TYR A 303 15544 17416 8875 -1699 2275 824 C
ATOM 3079 C TYR A 303 -32.852 1.585 57.842 1.00108.00 C
ANISOU 3079 C TYR A 303 15493 16728 8813 -1700 2010 873 C
ATOM 3080 O TYR A 303 -32.517 1.726 56.660 1.00111.02 O
ANISOU 3080 O TYR A 303 15762 16960 9461 -1620 1909 831 O
ATOM 3081 CB TYR A 303 -34.076 3.315 59.174 1.00106.96 C
ANISOU 3081 CB TYR A 303 15226 17084 8329 -1420 2329 669 C
ATOM 3082 CG TYR A 303 -33.046 4.303 58.665 1.00104.40 C
ANISOU 3082 CG TYR A 303 14984 16485 8200 -1162 2158 522 C
ATOM 3083 CD1 TYR A 303 -31.696 4.157 58.968 1.00102.65 C
ANISOU 3083 CD1 TYR A 303 15023 15965 8013 -1175 1926 542 C
ATOM 3084 CD2 TYR A 303 -33.424 5.391 57.891 1.00107.61 C
ANISOU 3084 CD2 TYR A 303 15206 16953 8727 -908 2232 372 C
ATOM 3085 CE1 TYR A 303 -30.757 5.051 58.508 1.00103.74 C
ANISOU 3085 CE1 TYR A 303 15222 15893 8301 -994 1771 413 C
ATOM 3086 CE2 TYR A 303 -32.486 6.298 57.429 1.00107.91 C
ANISOU 3086 CE2 TYR A 303 15353 16727 8919 -712 2083 239 C
ATOM 3087 CZ TYR A 303 -31.155 6.120 57.740 1.00107.45 C
ANISOU 3087 CZ TYR A 303 15541 16394 8891 -781 1851 257 C
ATOM 3088 OH TYR A 303 -30.214 7.013 57.285 1.00108.88 O
ANISOU 3088 OH TYR A 303 15817 16352 9201 -638 1701 131 O
ATOM 3089 N LYS A 304 -32.024 1.072 58.758 1.00102.68 N
ANISOU 3089 N LYS A 304 15120 15887 8007 -1759 1898 965 N
ATOM 3090 CA LYS A 304 -30.694 0.612 58.366 1.00 99.60 C
ANISOU 3090 CA LYS A 304 14913 15154 7778 -1715 1654 1035 C
ATOM 3091 C LYS A 304 -30.784 -0.385 57.221 1.00102.96 C
ANISOU 3091 C LYS A 304 15301 15424 8394 -1863 1622 1141 C
ATOM 3092 O LYS A 304 -29.975 -0.342 56.286 1.00102.00 O
ANISOU 3092 O LYS A 304 15164 15079 8511 -1743 1464 1122 O
ATOM 3093 CB LYS A 304 -29.959 -0.006 59.556 1.00 97.98 C
ANISOU 3093 CB LYS A 304 15021 14855 7353 -1773 1562 1168 C
ATOM 3094 N LEU A 305 -31.788 -1.269 57.256 1.00105.99 N
ANISOU 3094 N LEU A 305 15674 15937 8659 -2145 1779 1247 N
ATOM 3095 CA LEU A 305 -32.017 -2.184 56.140 1.00101.97 C
ANISOU 3095 CA LEU A 305 15153 15294 8297 -2337 1773 1330 C
ATOM 3096 C LEU A 305 -32.518 -1.445 54.902 1.00101.83 C
ANISOU 3096 C LEU A 305 14782 15401 8507 -2248 1804 1192 C
ATOM 3097 O LEU A 305 -32.176 -1.816 53.774 1.00101.66 O
ANISOU 3097 O LEU A 305 14753 15174 8698 -2265 1711 1207 O
ATOM 3098 CB LEU A 305 -33.012 -3.266 56.545 1.00102.29 C
ANISOU 3098 CB LEU A 305 15290 15469 8105 -2725 1942 1472 C
ATOM 3099 CG LEU A 305 -33.338 -4.269 55.447 1.00 98.94 C
ANISOU 3099 CG LEU A 305 14911 14907 7776 -3000 1954 1555 C
ATOM 3100 CD1 LEU A 305 -32.072 -5.049 55.090 1.00 96.06 C
ANISOU 3100 CD1 LEU A 305 14908 14062 7527 -2906 1771 1658 C
ATOM 3101 CD2 LEU A 305 -34.497 -5.184 55.868 1.00 99.12 C
ANISOU 3101 CD2 LEU A 305 14993 15142 7526 -3452 2147 1674 C
ATOM 3102 N ILE A 306 -33.335 -0.403 55.089 1.00100.56 N
ANISOU 3102 N ILE A 306 14342 15577 8291 -2131 1941 1065 N
ATOM 3103 CA ILE A 306 -33.818 0.369 53.946 1.00 98.78 C
ANISOU 3103 CA ILE A 306 13784 15488 8259 -1996 1974 945 C
ATOM 3104 C ILE A 306 -32.660 1.059 53.239 1.00 99.01 C
ANISOU 3104 C ILE A 306 13853 15216 8551 -1714 1780 843 C
ATOM 3105 O ILE A 306 -32.610 1.109 52.004 1.00 96.11 O
ANISOU 3105 O ILE A 306 13341 14767 8408 -1684 1723 810 O
ATOM 3106 CB ILE A 306 -34.885 1.389 54.385 1.00 95.03 C
ANISOU 3106 CB ILE A 306 13037 15436 7633 -1852 2176 842 C
ATOM 3107 CG1 ILE A 306 -36.072 0.687 55.013 1.00 97.28 C
ANISOU 3107 CG1 ILE A 306 13229 16086 7648 -2155 2377 953 C
ATOM 3108 CG2 ILE A 306 -35.388 2.173 53.183 1.00 93.37 C
ANISOU 3108 CG2 ILE A 306 12493 15375 7607 -1674 2212 739 C
ATOM 3109 CD1 ILE A 306 -36.981 1.631 55.738 1.00 99.26 C
ANISOU 3109 CD1 ILE A 306 13269 16755 7691 -1969 2584 874 C
ATOM 3110 N PHE A 307 -31.716 1.614 54.004 1.00 98.34 N
ANISOU 3110 N PHE A 307 13957 14985 8424 -1528 1675 793 N
ATOM 3111 CA PHE A 307 -30.608 2.310 53.364 1.00 94.87 C
ANISOU 3111 CA PHE A 307 13541 14304 8202 -1302 1492 698 C
ATOM 3112 C PHE A 307 -29.606 1.340 52.751 1.00 97.40 C
ANISOU 3112 C PHE A 307 14012 14318 8679 -1369 1309 816 C
ATOM 3113 O PHE A 307 -28.950 1.686 51.761 1.00101.73 O
ANISOU 3113 O PHE A 307 14491 14706 9457 -1237 1186 759 O
ATOM 3114 CB PHE A 307 -29.896 3.245 54.339 1.00 93.03 C
ANISOU 3114 CB PHE A 307 13461 14042 7846 -1127 1429 603 C
ATOM 3115 CG PHE A 307 -28.882 4.132 53.669 1.00 98.00 C
ANISOU 3115 CG PHE A 307 14088 14481 8666 -934 1264 486 C
ATOM 3116 CD1 PHE A 307 -29.256 5.370 53.161 1.00101.78 C
ANISOU 3116 CD1 PHE A 307 14434 15019 9218 -748 1337 316 C
ATOM 3117 CD2 PHE A 307 -27.564 3.717 53.508 1.00 98.17 C
ANISOU 3117 CD2 PHE A 307 14242 14278 8780 -932 1043 557 C
ATOM 3118 CE1 PHE A 307 -28.336 6.193 52.521 1.00100.25 C
ANISOU 3118 CE1 PHE A 307 14266 14640 9184 -609 1192 210 C
ATOM 3119 CE2 PHE A 307 -26.632 4.531 52.863 1.00 97.32 C
ANISOU 3119 CE2 PHE A 307 14109 14036 8833 -791 893 455 C
ATOM 3120 CZ PHE A 307 -27.022 5.775 52.371 1.00 97.89 C
ANISOU 3120 CZ PHE A 307 14074 14145 8976 -653 967 277 C
ATOM 3121 N THR A 308 -29.463 0.130 53.301 1.00 92.08 N
ANISOU 3121 N THR A 308 13563 13553 7872 -1551 1299 986 N
ATOM 3122 CA THR A 308 -28.547 -0.821 52.676 1.00 91.67 C
ANISOU 3122 CA THR A 308 13685 13197 7947 -1563 1152 1108 C
ATOM 3123 C THR A 308 -29.129 -1.377 51.380 1.00 92.31 C
ANISOU 3123 C THR A 308 13660 13220 8193 -1705 1205 1123 C
ATOM 3124 O THR A 308 -28.476 -1.331 50.334 1.00 93.68 O
ANISOU 3124 O THR A 308 13797 13209 8590 -1588 1090 1097 O
ATOM 3125 CB THR A 308 -28.193 -1.960 53.629 1.00 96.74 C
ANISOU 3125 CB THR A 308 14658 13722 8376 -1677 1134 1297 C
ATOM 3126 OG1 THR A 308 -29.389 -2.590 54.085 1.00107.49 O
ANISOU 3126 OG1 THR A 308 16058 15237 9546 -1962 1325 1363 O
ATOM 3127 CG2 THR A 308 -27.440 -1.460 54.812 1.00 95.52 C
ANISOU 3127 CG2 THR A 308 14611 13620 8064 -1530 1043 1295 C
ATOM 3128 N VAL A 309 -30.357 -1.907 51.427 1.00 96.20 N
ANISOU 3128 N VAL A 309 14100 13893 8560 -1981 1379 1165 N
ATOM 3129 CA VAL A 309 -30.952 -2.488 50.223 1.00 97.68 C
ANISOU 3129 CA VAL A 309 14199 14054 8862 -2180 1426 1184 C
ATOM 3130 C VAL A 309 -31.112 -1.433 49.139 1.00 97.62 C
ANISOU 3130 C VAL A 309 13852 14154 9085 -2000 1403 1028 C
ATOM 3131 O VAL A 309 -30.996 -1.738 47.944 1.00 97.56 O
ANISOU 3131 O VAL A 309 13806 14008 9256 -2040 1351 1024 O
ATOM 3132 CB VAL A 309 -32.297 -3.180 50.531 1.00 97.73 C
ANISOU 3132 CB VAL A 309 14174 14314 8646 -2563 1619 1257 C
ATOM 3133 CG1 VAL A 309 -33.320 -2.185 51.007 1.00 98.49 C
ANISOU 3133 CG1 VAL A 309 13927 14859 8636 -2518 1765 1157 C
ATOM 3134 CG2 VAL A 309 -32.817 -3.889 49.283 1.00 97.43 C
ANISOU 3134 CG2 VAL A 309 14094 14231 8694 -2828 1649 1286 C
ATOM 3135 N PHE A 310 -31.375 -0.181 49.524 1.00 95.22 N
ANISOU 3135 N PHE A 310 13333 14080 8768 -1792 1447 898 N
ATOM 3136 CA PHE A 310 -31.314 0.898 48.546 1.00 91.63 C
ANISOU 3136 CA PHE A 310 12630 13658 8526 -1562 1408 756 C
ATOM 3137 C PHE A 310 -29.892 1.070 48.027 1.00 90.61 C
ANISOU 3137 C PHE A 310 12634 13191 8602 -1370 1203 731 C
ATOM 3138 O PHE A 310 -29.676 1.260 46.824 1.00 88.82 O
ANISOU 3138 O PHE A 310 12291 12866 8590 -1302 1138 683 O
ATOM 3139 CB PHE A 310 -31.834 2.201 49.154 1.00 89.07 C
ANISOU 3139 CB PHE A 310 12137 13599 8105 -1351 1514 628 C
ATOM 3140 CG PHE A 310 -33.334 2.295 49.179 1.00 91.21 C
ANISOU 3140 CG PHE A 310 12136 14286 8234 -1453 1724 629 C
ATOM 3141 CD1 PHE A 310 -34.112 1.224 48.750 1.00 89.83 C
ANISOU 3141 CD1 PHE A 310 11880 14245 8007 -1789 1794 742 C
ATOM 3142 CD2 PHE A 310 -33.969 3.458 49.617 1.00 92.22 C
ANISOU 3142 CD2 PHE A 310 12096 14687 8255 -1215 1859 523 C
ATOM 3143 CE1 PHE A 310 -35.506 1.303 48.764 1.00 92.70 C
ANISOU 3143 CE1 PHE A 310 11939 15072 8212 -1911 1983 757 C
ATOM 3144 CE2 PHE A 310 -35.358 3.554 49.628 1.00 91.33 C
ANISOU 3144 CE2 PHE A 310 11688 15024 7991 -1268 2062 542 C
ATOM 3145 CZ PHE A 310 -36.131 2.476 49.197 1.00 93.66 C
ANISOU 3145 CZ PHE A 310 11841 15513 8234 -1627 2118 664 C
ATOM 3146 N HIS A 311 -28.908 0.968 48.918 1.00 91.64 N
ANISOU 3146 N HIS A 311 12995 13174 8651 -1290 1098 776 N
ATOM 3147 CA HIS A 311 -27.522 1.131 48.512 1.00 90.48 C
ANISOU 3147 CA HIS A 311 12938 12781 8659 -1113 902 770 C
ATOM 3148 C HIS A 311 -27.048 -0.008 47.616 1.00 89.62 C
ANISOU 3148 C HIS A 311 12947 12429 8677 -1181 829 889 C
ATOM 3149 O HIS A 311 -26.192 0.210 46.751 1.00 93.99 O
ANISOU 3149 O HIS A 311 13462 12829 9421 -1033 702 860 O
ATOM 3150 CB HIS A 311 -26.638 1.245 49.749 1.00 90.34 C
ANISOU 3150 CB HIS A 311 13111 12737 8477 -1032 808 810 C
ATOM 3151 CG HIS A 311 -25.185 1.412 49.437 1.00 89.73 C
ANISOU 3151 CG HIS A 311 13088 12492 8513 -865 601 823 C
ATOM 3152 ND1 HIS A 311 -24.323 0.344 49.312 1.00 89.97 N
ANISOU 3152 ND1 HIS A 311 13288 12343 8555 -841 494 986 N
ATOM 3153 CD2 HIS A 311 -24.442 2.523 49.231 1.00 87.19 C
ANISOU 3153 CD2 HIS A 311 12677 12177 8275 -717 490 700 C
ATOM 3154 CE1 HIS A 311 -23.111 0.790 49.043 1.00 88.60 C
ANISOU 3154 CE1 HIS A 311 13075 12120 8469 -672 322 970 C
ATOM 3155 NE2 HIS A 311 -23.157 2.109 48.988 1.00 87.30 N
ANISOU 3155 NE2 HIS A 311 12756 12065 8348 -626 312 795 N
ATOM 3156 N ILE A 312 -27.571 -1.222 47.802 1.00 82.49 N
ANISOU 3156 N ILE A 312 12216 11475 7650 -1408 915 1022 N
ATOM 3157 CA ILE A 312 -27.158 -2.339 46.952 1.00 85.12 C
ANISOU 3157 CA ILE A 312 12738 11534 8070 -1472 869 1131 C
ATOM 3158 C ILE A 312 -27.620 -2.123 45.508 1.00 82.10 C
ANISOU 3158 C ILE A 312 12146 11155 7895 -1520 891 1041 C
ATOM 3159 O ILE A 312 -26.873 -2.380 44.553 1.00 78.20 O
ANISOU 3159 O ILE A 312 11706 10439 7567 -1414 795 1054 O
ATOM 3160 CB ILE A 312 -27.692 -3.670 47.515 1.00 90.22 C
ANISOU 3160 CB ILE A 312 13684 12100 8496 -1746 977 1289 C
ATOM 3161 CG1 ILE A 312 -27.289 -3.848 48.980 1.00 88.80 C
ANISOU 3161 CG1 ILE A 312 13706 11939 8094 -1692 960 1384 C
ATOM 3162 CG2 ILE A 312 -27.209 -4.850 46.659 1.00 89.06 C
ANISOU 3162 CG2 ILE A 312 13825 11607 8406 -1790 944 1402 C
ATOM 3163 CD1 ILE A 312 -27.914 -5.041 49.641 1.00 87.82 C
ANISOU 3163 CD1 ILE A 312 13885 11758 7725 -1979 1084 1534 C
ATOM 3164 N ILE A 313 -28.869 -1.681 45.332 1.00 83.20 N
ANISOU 3164 N ILE A 313 12036 11571 8004 -1672 1021 961 N
ATOM 3165 CA ILE A 313 -29.397 -1.360 44.008 1.00 81.28 C
ANISOU 3165 CA ILE A 313 11550 11401 7932 -1708 1042 877 C
ATOM 3166 C ILE A 313 -28.466 -0.404 43.284 1.00 80.99 C
ANISOU 3166 C ILE A 313 11390 11253 8129 -1402 906 772 C
ATOM 3167 O ILE A 313 -28.068 -0.640 42.138 1.00 89.83 O
ANISOU 3167 O ILE A 313 12510 12202 9421 -1377 838 766 O
ATOM 3168 CB ILE A 313 -30.809 -0.758 44.132 1.00 82.86 C
ANISOU 3168 CB ILE A 313 11438 12010 8034 -1822 1197 810 C
ATOM 3169 CG1 ILE A 313 -31.797 -1.784 44.672 1.00 81.30 C
ANISOU 3169 CG1 ILE A 313 11331 11963 7596 -2198 1336 920 C
ATOM 3170 CG2 ILE A 313 -31.291 -0.193 42.798 1.00 77.43 C
ANISOU 3170 CG2 ILE A 313 10454 11447 7519 -1784 1201 719 C
ATOM 3171 CD1 ILE A 313 -33.103 -1.146 45.021 1.00 81.63 C
ANISOU 3171 CD1 ILE A 313 11039 12479 7499 -2265 1494 873 C
ATOM 3172 N ALA A 314 -28.115 0.700 43.939 1.00 78.53 N
ANISOU 3172 N ALA A 314 10993 11036 7807 -1187 870 685 N
ATOM 3173 CA ALA A 314 -27.251 1.682 43.296 1.00 82.54 C
ANISOU 3173 CA ALA A 314 11403 11452 8506 -942 748 581 C
ATOM 3174 C ALA A 314 -25.903 1.082 42.913 1.00 82.02 C
ANISOU 3174 C ALA A 314 11512 11107 8543 -855 591 659 C
ATOM 3175 O ALA A 314 -25.336 1.454 41.882 1.00 80.25 O
ANISOU 3175 O ALA A 314 11198 10783 8511 -738 505 606 O
ATOM 3176 CB ALA A 314 -27.066 2.896 44.207 1.00 86.26 C
ANISOU 3176 CB ALA A 314 11840 12043 8892 -777 743 479 C
ATOM 3177 N MET A 315 -25.383 0.146 43.714 1.00 83.23 N
ANISOU 3177 N MET A 315 11914 11150 8560 -892 558 796 N
ATOM 3178 CA MET A 315 -24.123 -0.500 43.374 1.00 82.38 C
ANISOU 3178 CA MET A 315 11971 10812 8519 -759 426 897 C
ATOM 3179 C MET A 315 -24.230 -1.388 42.148 1.00 86.24 C
ANISOU 3179 C MET A 315 12536 11104 9126 -829 451 945 C
ATOM 3180 O MET A 315 -23.196 -1.847 41.648 1.00 85.36 O
ANISOU 3180 O MET A 315 12539 10803 9090 -672 356 1017 O
ATOM 3181 CB MET A 315 -23.609 -1.326 44.549 1.00 78.82 C
ANISOU 3181 CB MET A 315 11786 10301 7860 -745 400 1053 C
ATOM 3182 CG MET A 315 -23.120 -0.491 45.686 1.00 85.67 C
ANISOU 3182 CG MET A 315 12607 11334 8608 -645 328 1018 C
ATOM 3183 SD MET A 315 -22.279 0.998 45.120 1.00 93.45 S
ANISOU 3183 SD MET A 315 13343 12400 9765 -467 190 857 S
ATOM 3184 CE MET A 315 -23.464 2.251 45.586 1.00 92.81 C
ANISOU 3184 CE MET A 315 13114 12525 9625 -551 321 674 C
ATOM 3185 N CYS A 316 -25.444 -1.654 41.665 1.00 84.63 N
ANISOU 3185 N CYS A 316 12274 10964 8917 -1064 579 913 N
ATOM 3186 CA CYS A 316 -25.585 -2.465 40.467 1.00 84.31 C
ANISOU 3186 CA CYS A 316 12327 10739 8967 -1174 603 944 C
ATOM 3187 C CYS A 316 -25.270 -1.660 39.215 1.00 80.13 C
ANISOU 3187 C CYS A 316 11560 10211 8676 -1031 531 828 C
ATOM 3188 O CYS A 316 -24.867 -2.232 38.198 1.00 77.73 O
ANISOU 3188 O CYS A 316 11357 9702 8474 -1014 503 856 O
ATOM 3189 CB CYS A 316 -26.984 -3.078 40.425 1.00 87.19 C
ANISOU 3189 CB CYS A 316 12714 11214 9201 -1534 756 960 C
ATOM 3190 SG CYS A 316 -27.273 -4.253 41.810 1.00 86.91 S
ANISOU 3190 SG CYS A 316 13048 11111 8861 -1748 848 1122 S
ATOM 3191 N SER A 317 -25.384 -0.333 39.295 1.00 78.67 N
ANISOU 3191 N SER A 317 11097 10229 8565 -911 506 703 N
ATOM 3192 CA SER A 317 -24.896 0.548 38.247 1.00 72.67 C
ANISOU 3192 CA SER A 317 10146 9451 8014 -744 424 600 C
ATOM 3193 C SER A 317 -23.395 0.428 38.020 1.00 77.61 C
ANISOU 3193 C SER A 317 10873 9890 8725 -535 282 648 C
ATOM 3194 O SER A 317 -22.898 0.935 37.008 1.00 80.44 O
ANISOU 3194 O SER A 317 11107 10201 9255 -423 215 585 O
ATOM 3195 CB SER A 317 -25.217 1.991 38.587 1.00 71.71 C
ANISOU 3195 CB SER A 317 9803 9541 7904 -640 435 468 C
ATOM 3196 OG SER A 317 -24.207 2.545 39.431 1.00 73.09 O
ANISOU 3196 OG SER A 317 10041 9697 8031 -487 335 460 O
ATOM 3197 N THR A 318 -22.649 -0.194 38.928 1.00 79.44 N
ANISOU 3197 N THR A 318 11306 10047 8830 -466 234 767 N
ATOM 3198 CA THR A 318 -21.249 -0.438 38.607 1.00 82.47 C
ANISOU 3198 CA THR A 318 11755 10304 9274 -249 108 841 C
ATOM 3199 C THR A 318 -21.106 -1.652 37.693 1.00 84.45 C
ANISOU 3199 C THR A 318 12212 10309 9566 -247 145 935 C
ATOM 3200 O THR A 318 -20.651 -1.525 36.549 1.00 93.86 O
ANISOU 3200 O THR A 318 13325 11421 10918 -151 104 898 O
ATOM 3201 CB THR A 318 -20.419 -0.620 39.872 1.00 87.86 C
ANISOU 3201 CB THR A 318 12554 11041 9787 -133 32 949 C
ATOM 3202 OG1 THR A 318 -20.381 -2.010 40.205 1.00 96.73 O
ANISOU 3202 OG1 THR A 318 13986 11990 10777 -138 84 1116 O
ATOM 3203 CG2 THR A 318 -21.009 0.197 41.031 1.00 83.84 C
ANISOU 3203 CG2 THR A 318 11968 10736 9153 -234 61 872 C
ATOM 3204 N PHE A 319 -21.531 -2.835 38.155 1.00 75.85 N
ANISOU 3204 N PHE A 319 11421 9080 8319 -368 235 1052 N
ATOM 3205 CA PHE A 319 -21.266 -4.033 37.359 1.00 79.69 C
ANISOU 3205 CA PHE A 319 12197 9278 8804 -344 277 1149 C
ATOM 3206 C PHE A 319 -22.097 -4.107 36.078 1.00 75.71 C
ANISOU 3206 C PHE A 319 11642 8708 8418 -550 350 1051 C
ATOM 3207 O PHE A 319 -21.695 -4.824 35.151 1.00 72.67 O
ANISOU 3207 O PHE A 319 11449 8086 8075 -489 364 1092 O
ATOM 3208 CB PHE A 319 -21.453 -5.313 38.197 1.00 84.22 C
ANISOU 3208 CB PHE A 319 13184 9670 9144 -428 363 1308 C
ATOM 3209 CG PHE A 319 -22.884 -5.696 38.458 1.00 85.90 C
ANISOU 3209 CG PHE A 319 13489 9910 9239 -822 501 1281 C
ATOM 3210 CD1 PHE A 319 -23.645 -6.326 37.490 1.00 85.89 C
ANISOU 3210 CD1 PHE A 319 13623 9767 9246 -1083 597 1252 C
ATOM 3211 CD2 PHE A 319 -23.453 -5.482 39.706 1.00 84.78 C
ANISOU 3211 CD2 PHE A 319 13311 9957 8946 -951 537 1295 C
ATOM 3212 CE1 PHE A 319 -24.959 -6.690 37.752 1.00 84.95 C
ANISOU 3212 CE1 PHE A 319 13559 9736 8983 -1487 719 1239 C
ATOM 3213 CE2 PHE A 319 -24.768 -5.857 39.971 1.00 78.60 C
ANISOU 3213 CE2 PHE A 319 12586 9250 8027 -1325 671 1284 C
ATOM 3214 CZ PHE A 319 -25.518 -6.451 38.996 1.00 76.35 C
ANISOU 3214 CZ PHE A 319 12398 8863 7748 -1602 759 1259 C
ATOM 3215 N ALA A 320 -23.216 -3.370 35.987 1.00 73.64 N
ANISOU 3215 N ALA A 320 11121 8665 8192 -769 398 928 N
ATOM 3216 CA ALA A 320 -24.111 -3.502 34.832 1.00 71.32 C
ANISOU 3216 CA ALA A 320 10762 8367 7968 -996 466 854 C
ATOM 3217 C ALA A 320 -23.453 -3.062 33.531 1.00 70.62 C
ANISOU 3217 C ALA A 320 10540 8204 8089 -820 391 785 C
ATOM 3218 O ALA A 320 -23.706 -3.661 32.482 1.00 66.94 O
ANISOU 3218 O ALA A 320 10190 7591 7654 -945 433 777 O
ATOM 3219 CB ALA A 320 -25.396 -2.704 35.038 1.00 68.66 C
ANISOU 3219 CB ALA A 320 10121 8356 7611 -1199 529 755 C
ATOM 3220 N ASN A 321 -22.614 -2.018 33.579 1.00 76.70 N
ANISOU 3220 N ASN A 321 11082 9077 8984 -561 282 733 N
ATOM 3221 CA ASN A 321 -22.096 -1.403 32.355 1.00 74.15 C
ANISOU 3221 CA ASN A 321 10583 8735 8857 -425 215 654 C
ATOM 3222 C ASN A 321 -21.329 -2.357 31.443 1.00 74.66 C
ANISOU 3222 C ASN A 321 10879 8530 8958 -320 210 726 C
ATOM 3223 O ASN A 321 -21.543 -2.301 30.220 1.00 76.10 O
ANISOU 3223 O ASN A 321 11002 8660 9252 -375 223 660 O
ATOM 3224 CB ASN A 321 -21.234 -0.192 32.719 1.00 76.31 C
ANISOU 3224 CB ASN A 321 10631 9155 9209 -205 101 602 C
ATOM 3225 CG ASN A 321 -22.057 1.033 33.016 1.00 76.49 C
ANISOU 3225 CG ASN A 321 10406 9405 9250 -278 121 479 C
ATOM 3226 OD1 ASN A 321 -23.275 1.010 32.888 1.00 81.09 O
ANISOU 3226 OD1 ASN A 321 10927 10084 9799 -460 216 439 O
ATOM 3227 ND2 ASN A 321 -21.399 2.109 33.428 1.00 73.38 N
ANISOU 3227 ND2 ASN A 321 9882 9114 8884 -138 37 423 N
ATOM 3228 N PRO A 322 -20.422 -3.219 31.924 1.00 76.14 N
ANISOU 3228 N PRO A 322 11336 8549 9046 -142 197 862 N
ATOM 3229 CA PRO A 322 -19.771 -4.148 30.981 1.00 71.02 C
ANISOU 3229 CA PRO A 322 10942 7630 8412 -9 223 930 C
ATOM 3230 C PRO A 322 -20.734 -5.141 30.349 1.00 70.19 C
ANISOU 3230 C PRO A 322 11131 7309 8228 -298 348 924 C
ATOM 3231 O PRO A 322 -20.530 -5.516 29.190 1.00 72.51 O
ANISOU 3231 O PRO A 322 11538 7429 8584 -273 373 903 O
ATOM 3232 CB PRO A 322 -18.706 -4.846 31.841 1.00 64.01 C
ANISOU 3232 CB PRO A 322 10287 6647 7386 274 198 1098 C
ATOM 3233 CG PRO A 322 -18.431 -3.865 32.938 1.00 67.78 C
ANISOU 3233 CG PRO A 322 10484 7414 7855 337 98 1084 C
ATOM 3234 CD PRO A 322 -19.773 -3.269 33.249 1.00 75.31 C
ANISOU 3234 CD PRO A 322 11289 8510 8815 15 148 964 C
ATOM 3235 N LEU A 323 -21.791 -5.552 31.055 1.00 71.02 N
ANISOU 3235 N LEU A 323 11362 7440 8184 -602 430 938 N
ATOM 3236 CA LEU A 323 -22.764 -6.474 30.465 1.00 73.45 C
ANISOU 3236 CA LEU A 323 11945 7582 8382 -960 546 929 C
ATOM 3237 C LEU A 323 -23.536 -5.831 29.312 1.00 76.16 C
ANISOU 3237 C LEU A 323 11988 8092 8856 -1164 540 789 C
ATOM 3238 O LEU A 323 -23.756 -6.475 28.277 1.00 79.78 O
ANISOU 3238 O LEU A 323 12651 8367 9293 -1322 591 768 O
ATOM 3239 CB LEU A 323 -23.727 -6.981 31.538 1.00 68.69 C
ANISOU 3239 CB LEU A 323 11497 7034 7568 -1273 632 981 C
ATOM 3240 CG LEU A 323 -23.034 -7.672 32.711 1.00 69.10 C
ANISOU 3240 CG LEU A 323 11878 6915 7462 -1084 644 1134 C
ATOM 3241 CD1 LEU A 323 -24.043 -7.982 33.784 1.00 72.71 C
ANISOU 3241 CD1 LEU A 323 12423 7480 7722 -1411 725 1171 C
ATOM 3242 CD2 LEU A 323 -22.321 -8.938 32.243 1.00 65.80 C
ANISOU 3242 CD2 LEU A 323 11998 6063 6941 -945 707 1246 C
ATOM 3243 N LEU A 324 -23.958 -4.563 29.471 1.00 70.69 N
ANISOU 3243 N LEU A 324 10838 7743 8279 -1154 482 695 N
ATOM 3244 CA LEU A 324 -24.631 -3.860 28.377 1.00 64.97 C
ANISOU 3244 CA LEU A 324 9810 7201 7675 -1279 470 577 C
ATOM 3245 C LEU A 324 -23.739 -3.749 27.150 1.00 66.55 C
ANISOU 3245 C LEU A 324 10017 7233 8035 -1068 413 543 C
ATOM 3246 O LEU A 324 -24.206 -3.931 26.021 1.00 67.23 O
ANISOU 3246 O LEU A 324 10104 7294 8147 -1240 437 488 O
ATOM 3247 CB LEU A 324 -25.076 -2.473 28.814 1.00 67.01 C
ANISOU 3247 CB LEU A 324 9633 7814 8015 -1206 428 497 C
ATOM 3248 CG LEU A 324 -26.191 -2.381 29.874 1.00 72.74 C
ANISOU 3248 CG LEU A 324 10258 8797 8583 -1421 501 510 C
ATOM 3249 CD1 LEU A 324 -26.610 -0.924 30.085 1.00 72.71 C
ANISOU 3249 CD1 LEU A 324 9846 9120 8662 -1286 476 419 C
ATOM 3250 CD2 LEU A 324 -27.408 -3.239 29.532 1.00 66.43 C
ANISOU 3250 CD2 LEU A 324 9548 8071 7621 -1849 601 528 C
ATOM 3251 N TYR A 325 -22.451 -3.454 27.344 1.00 70.95 N
ANISOU 3251 N TYR A 325 10568 7706 8684 -709 337 578 N
ATOM 3252 CA TYR A 325 -21.555 -3.354 26.196 1.00 65.85 C
ANISOU 3252 CA TYR A 325 9913 6932 8176 -500 291 555 C
ATOM 3253 C TYR A 325 -21.475 -4.685 25.473 1.00 71.81 C
ANISOU 3253 C TYR A 325 11092 7361 8833 -579 377 607 C
ATOM 3254 O TYR A 325 -21.614 -4.746 24.245 1.00 69.31 O
ANISOU 3254 O TYR A 325 10781 6975 8579 -655 391 543 O
ATOM 3255 CB TYR A 325 -20.158 -2.899 26.620 1.00 57.16 C
ANISOU 3255 CB TYR A 325 8724 5850 7145 -126 198 607 C
ATOM 3256 CG TYR A 325 -20.136 -1.623 27.408 1.00 57.22 C
ANISOU 3256 CG TYR A 325 8396 6135 7210 -69 117 553 C
ATOM 3257 CD1 TYR A 325 -21.171 -0.688 27.302 1.00 61.47 C
ANISOU 3257 CD1 TYR A 325 8673 6880 7801 -243 124 442 C
ATOM 3258 CD2 TYR A 325 -19.079 -1.343 28.277 1.00 60.40 C
ANISOU 3258 CD2 TYR A 325 8757 6605 7588 166 38 620 C
ATOM 3259 CE1 TYR A 325 -21.151 0.503 28.045 1.00 63.22 C
ANISOU 3259 CE1 TYR A 325 8655 7314 8050 -172 69 387 C
ATOM 3260 CE2 TYR A 325 -19.047 -0.158 29.017 1.00 63.53 C
ANISOU 3260 CE2 TYR A 325 8898 7233 8008 183 -32 560 C
ATOM 3261 CZ TYR A 325 -20.088 0.752 28.895 1.00 62.98 C
ANISOU 3261 CZ TYR A 325 8630 7309 7990 19 -8 439 C
ATOM 3262 OH TYR A 325 -20.048 1.908 29.618 1.00 63.88 O
ANISOU 3262 OH TYR A 325 8563 7605 8102 54 -58 375 O
ATOM 3263 N GLY A 326 -21.274 -5.768 26.226 1.00 74.52 N
ANISOU 3263 N GLY A 326 11830 7484 9000 -567 444 723 N
ATOM 3264 CA GLY A 326 -21.131 -7.073 25.599 1.00 74.76 C
ANISOU 3264 CA GLY A 326 12361 7143 8902 -614 545 778 C
ATOM 3265 C GLY A 326 -22.414 -7.548 24.946 1.00 71.52 C
ANISOU 3265 C GLY A 326 12088 6693 8393 -1095 626 706 C
ATOM 3266 O GLY A 326 -22.393 -8.164 23.875 1.00 64.56 O
ANISOU 3266 O GLY A 326 11471 5582 7477 -1180 681 678 O
ATOM 3267 N TRP A 327 -23.550 -7.253 25.569 1.00 71.00 N
ANISOU 3267 N TRP A 327 11832 6882 8262 -1426 636 675 N
ATOM 3268 CA TRP A 327 -24.805 -7.754 25.034 1.00 75.49 C
ANISOU 3268 CA TRP A 327 12505 7486 8693 -1929 710 625 C
ATOM 3269 C TRP A 327 -25.243 -6.956 23.809 1.00 74.87 C
ANISOU 3269 C TRP A 327 12052 7635 8760 -2019 654 504 C
ATOM 3270 O TRP A 327 -25.604 -7.536 22.781 1.00 77.96 O
ANISOU 3270 O TRP A 327 12645 7900 9078 -2273 698 464 O
ATOM 3271 CB TRP A 327 -25.868 -7.750 26.142 1.00 79.59 C
ANISOU 3271 CB TRP A 327 12925 8254 9063 -2244 749 652 C
ATOM 3272 CG TRP A 327 -27.252 -8.106 25.681 1.00 91.80 C
ANISOU 3272 CG TRP A 327 14457 9976 10448 -2799 812 606 C
ATOM 3273 CD1 TRP A 327 -27.642 -9.246 25.032 1.00 93.44 C
ANISOU 3273 CD1 TRP A 327 15114 9929 10459 -3180 899 612 C
ATOM 3274 CD2 TRP A 327 -28.437 -7.311 25.844 1.00 97.09 C
ANISOU 3274 CD2 TRP A 327 14634 11147 11108 -3043 797 555 C
ATOM 3275 NE1 TRP A 327 -28.995 -9.202 24.774 1.00 95.04 N
ANISOU 3275 NE1 TRP A 327 15100 10482 10529 -3689 924 568 N
ATOM 3276 CE2 TRP A 327 -29.505 -8.027 25.264 1.00 96.72 C
ANISOU 3276 CE2 TRP A 327 14715 11180 10855 -3588 865 540 C
ATOM 3277 CE3 TRP A 327 -28.697 -6.062 26.423 1.00 94.62 C
ANISOU 3277 CE3 TRP A 327 13803 11230 10919 -2846 742 523 C
ATOM 3278 CZ2 TRP A 327 -30.810 -7.533 25.247 1.00 95.72 C
ANISOU 3278 CZ2 TRP A 327 14153 11574 10643 -3919 871 510 C
ATOM 3279 CZ3 TRP A 327 -29.992 -5.575 26.405 1.00 89.74 C
ANISOU 3279 CZ3 TRP A 327 12798 11080 10221 -3130 764 490 C
ATOM 3280 CH2 TRP A 327 -31.029 -6.306 25.820 1.00 92.11 C
ANISOU 3280 CH2 TRP A 327 13173 11507 10317 -3651 824 491 C
ATOM 3281 N MET A 328 -25.130 -5.634 23.871 1.00 72.12 N
ANISOU 3281 N MET A 328 11203 7594 8607 -1794 560 449 N
ATOM 3282 CA MET A 328 -25.826 -4.736 22.966 1.00 66.98 C
ANISOU 3282 CA MET A 328 10146 7245 8060 -1903 514 349 C
ATOM 3283 C MET A 328 -24.927 -4.048 21.958 1.00 70.55 C
ANISOU 3283 C MET A 328 10446 7637 8724 -1587 438 293 C
ATOM 3284 O MET A 328 -25.404 -3.169 21.229 1.00 72.92 O
ANISOU 3284 O MET A 328 10400 8184 9122 -1614 392 217 O
ATOM 3285 CB MET A 328 -26.532 -3.664 23.779 1.00 67.84 C
ANISOU 3285 CB MET A 328 9820 7759 8199 -1892 486 326 C
ATOM 3286 CG MET A 328 -27.981 -3.453 23.499 1.00 66.78 C
ANISOU 3286 CG MET A 328 9419 7995 7961 -2245 520 291 C
ATOM 3287 SD MET A 328 -28.374 -2.147 24.645 1.00 63.75 S
ANISOU 3287 SD MET A 328 8607 7990 7626 -2035 502 280 S
ATOM 3288 CE MET A 328 -27.533 -2.802 26.087 1.00 65.34 C
ANISOU 3288 CE MET A 328 9158 7913 7757 -1910 524 368 C
ATOM 3289 N ASN A 329 -23.641 -4.390 21.921 1.00 74.56 N
ANISOU 3289 N ASN A 329 11186 7855 9289 -1272 425 339 N
ATOM 3290 CA ASN A 329 -22.660 -3.717 21.071 1.00 65.99 C
ANISOU 3290 CA ASN A 329 9940 6741 8392 -957 354 299 C
ATOM 3291 C ASN A 329 -21.699 -4.776 20.571 1.00 66.26 C
ANISOU 3291 C ASN A 329 10398 6404 8375 -796 407 357 C
ATOM 3292 O ASN A 329 -20.957 -5.366 21.367 1.00 66.01 O
ANISOU 3292 O ASN A 329 10611 6201 8270 -589 433 457 O
ATOM 3293 CB ASN A 329 -21.910 -2.630 21.830 1.00 70.05 C
ANISOU 3293 CB ASN A 329 10158 7420 9037 -641 266 307 C
ATOM 3294 CG ASN A 329 -20.886 -1.927 20.972 1.00 72.72 C
ANISOU 3294 CG ASN A 329 10331 7754 9546 -364 195 272 C
ATOM 3295 OD1 ASN A 329 -19.795 -2.449 20.744 1.00 62.55 O
ANISOU 3295 OD1 ASN A 329 9229 6275 8261 -132 199 331 O
ATOM 3296 ND2 ASN A 329 -21.234 -0.731 20.482 1.00 77.13 N
ANISOU 3296 ND2 ASN A 329 10543 8534 10229 -374 137 183 N
ATOM 3297 N SER A 330 -21.715 -5.009 19.257 1.00 70.25 N
ANISOU 3297 N SER A 330 10995 6796 8902 -867 429 300 N
ATOM 3298 CA SER A 330 -21.040 -6.172 18.700 1.00 69.61 C
ANISOU 3298 CA SER A 330 11399 6331 8717 -767 517 347 C
ATOM 3299 C SER A 330 -19.535 -5.981 18.605 1.00 66.25 C
ANISOU 3299 C SER A 330 10948 5826 8399 -270 486 405 C
ATOM 3300 O SER A 330 -18.793 -6.968 18.662 1.00 66.33 O
ANISOU 3300 O SER A 330 11367 5541 8294 -54 568 494 O
ATOM 3301 CB SER A 330 -21.616 -6.512 17.329 1.00 75.17 C
ANISOU 3301 CB SER A 330 12237 6947 9379 -1043 558 259 C
ATOM 3302 OG SER A 330 -20.694 -7.287 16.578 1.00 84.75 O
ANISOU 3302 OG SER A 330 13838 7817 10548 -819 630 284 O
ATOM 3303 N ASN A 331 -19.058 -4.740 18.475 1.00 62.49 N
ANISOU 3303 N ASN A 331 10011 5618 8116 -79 378 366 N
ATOM 3304 CA ASN A 331 -17.615 -4.515 18.535 1.00 63.67 C
ANISOU 3304 CA ASN A 331 10082 5773 8338 355 339 436 C
ATOM 3305 C ASN A 331 -17.076 -4.642 19.953 1.00 68.25 C
ANISOU 3305 C ASN A 331 10680 6404 8849 551 315 550 C
ATOM 3306 O ASN A 331 -15.879 -4.881 20.131 1.00 75.27 O
ANISOU 3306 O ASN A 331 11616 7266 9716 914 311 651 O
ATOM 3307 CB ASN A 331 -17.251 -3.148 17.953 1.00 65.67 C
ANISOU 3307 CB ASN A 331 9872 6292 8787 444 232 359 C
ATOM 3308 CG ASN A 331 -17.365 -3.110 16.438 1.00 71.00 C
ANISOU 3308 CG ASN A 331 10557 6896 9523 375 257 277 C
ATOM 3309 OD1 ASN A 331 -16.886 -4.009 15.747 1.00 64.76 O
ANISOU 3309 OD1 ASN A 331 10082 5864 8659 490 340 307 O
ATOM 3310 ND2 ASN A 331 -18.021 -2.071 15.916 1.00 76.45 N
ANISOU 3310 ND2 ASN A 331 10927 7792 10330 200 191 176 N
ATOM 3311 N TYR A 332 -17.925 -4.501 20.967 1.00 63.25 N
ANISOU 3311 N TYR A 332 9999 5871 8164 327 303 546 N
ATOM 3312 CA TYR A 332 -17.492 -4.847 22.313 1.00 59.48 C
ANISOU 3312 CA TYR A 332 9626 5394 7578 483 298 664 C
ATOM 3313 C TYR A 332 -17.535 -6.356 22.519 1.00 65.47 C
ANISOU 3313 C TYR A 332 10944 5802 8130 487 426 766 C
ATOM 3314 O TYR A 332 -16.542 -6.960 22.943 1.00 65.97 O
ANISOU 3314 O TYR A 332 11214 5748 8102 832 450 899 O
ATOM 3315 CB TYR A 332 -18.347 -4.111 23.361 1.00 63.70 C
ANISOU 3315 CB TYR A 332 9916 6169 8119 262 247 623 C
ATOM 3316 CG TYR A 332 -17.697 -2.822 23.822 1.00 61.29 C
ANISOU 3316 CG TYR A 332 9199 6153 7935 438 123 600 C
ATOM 3317 CD1 TYR A 332 -16.595 -2.853 24.667 1.00 62.12 C
ANISOU 3317 CD1 TYR A 332 9290 6325 7989 720 69 710 C
ATOM 3318 CD2 TYR A 332 -18.151 -1.584 23.382 1.00 57.08 C
ANISOU 3318 CD2 TYR A 332 8316 5827 7543 322 63 475 C
ATOM 3319 CE1 TYR A 332 -15.973 -1.704 25.070 1.00 61.97 C
ANISOU 3319 CE1 TYR A 332 8927 6572 8046 824 -46 685 C
ATOM 3320 CE2 TYR A 332 -17.527 -0.415 23.791 1.00 55.36 C
ANISOU 3320 CE2 TYR A 332 7798 5830 7406 453 -40 449 C
ATOM 3321 CZ TYR A 332 -16.439 -0.493 24.632 1.00 60.66 C
ANISOU 3321 CZ TYR A 332 8470 6563 8015 676 -96 549 C
ATOM 3322 OH TYR A 332 -15.798 0.639 25.049 1.00 71.02 O
ANISOU 3322 OH TYR A 332 9510 8102 9372 749 -201 521 O
ATOM 3323 N ARG A 333 -18.679 -6.973 22.219 1.00 70.98 N
ANISOU 3323 N ARG A 333 11900 6340 8728 101 511 713 N
ATOM 3324 CA ARG A 333 -18.822 -8.425 22.292 1.00 69.19 C
ANISOU 3324 CA ARG A 333 12287 5726 8276 29 650 793 C
ATOM 3325 C ARG A 333 -17.596 -9.140 21.745 1.00 70.76 C
ANISOU 3325 C ARG A 333 12809 5652 8425 460 714 882 C
ATOM 3326 O ARG A 333 -16.986 -9.967 22.427 1.00 74.60 O
ANISOU 3326 O ARG A 333 13653 5937 8754 727 779 1026 O
ATOM 3327 CB ARG A 333 -20.080 -8.833 21.523 1.00 67.38 C
ANISOU 3327 CB ARG A 333 12239 5396 7966 -475 719 689 C
ATOM 3328 CG ARG A 333 -20.336 -10.306 21.405 1.00 67.57 C
ANISOU 3328 CG ARG A 333 12956 4985 7731 -650 872 743 C
ATOM 3329 CD ARG A 333 -21.796 -10.601 21.676 1.00 68.77 C
ANISOU 3329 CD ARG A 333 13196 5198 7737 -1248 913 692 C
ATOM 3330 NE ARG A 333 -22.677 -9.490 21.325 1.00 69.79 N
ANISOU 3330 NE ARG A 333 12743 5758 8016 -1517 815 572 N
ATOM 3331 CZ ARG A 333 -23.088 -9.235 20.088 1.00 77.20 C
ANISOU 3331 CZ ARG A 333 13554 6766 9011 -1709 799 465 C
ATOM 3332 NH1 ARG A 333 -23.897 -8.203 19.844 1.00 76.43 N
ANISOU 3332 NH1 ARG A 333 12925 7084 9032 -1904 713 378 N
ATOM 3333 NH2 ARG A 333 -22.669 -10.008 19.089 1.00 79.21 N
ANISOU 3333 NH2 ARG A 333 14231 6675 9190 -1678 874 450 N
ATOM 3334 N LYS A 334 -17.193 -8.793 20.523 1.00 75.37 N
ANISOU 3334 N LYS A 334 13255 6251 9131 569 700 809 N
ATOM 3335 CA LYS A 334 -16.027 -9.427 19.916 1.00 76.97 C
ANISOU 3335 CA LYS A 334 13733 6232 9279 1007 775 892 C
ATOM 3336 C LYS A 334 -14.737 -9.078 20.662 1.00 74.12 C
ANISOU 3336 C LYS A 334 13123 6085 8954 1510 704 1029 C
ATOM 3337 O LYS A 334 -13.846 -9.924 20.794 1.00 74.49 O
ANISOU 3337 O LYS A 334 13389 6054 8860 1861 773 1132 O
ATOM 3338 CB LYS A 334 -15.945 -9.032 18.437 1.00 75.92 C
ANISOU 3338 CB LYS A 334 13459 6115 9272 976 772 774 C
ATOM 3339 CG LYS A 334 -17.193 -9.442 17.634 1.00 77.41 C
ANISOU 3339 CG LYS A 334 13904 6120 9390 466 837 647 C
ATOM 3340 CD LYS A 334 -17.194 -8.882 16.209 1.00 76.65 C
ANISOU 3340 CD LYS A 334 13591 6104 9427 407 808 525 C
ATOM 3341 CE LYS A 334 -18.433 -9.324 15.430 1.00 74.69 C
ANISOU 3341 CE LYS A 334 13558 5746 9073 -120 858 406 C
ATOM 3342 NZ LYS A 334 -18.349 -8.990 13.973 1.00 71.86 N
ANISOU 3342 NZ LYS A 334 13074 5431 8800 -146 845 301 N
ATOM 3343 N ALA A 335 -14.622 -7.850 21.179 1.00 67.57 N
ANISOU 3343 N ALA A 335 11727 5659 8288 1491 552 994 N
ATOM 3344 CA ALA A 335 -13.386 -7.445 21.849 1.00 65.12 C
ANISOU 3344 CA ALA A 335 11140 5611 7990 1906 467 1118 C
ATOM 3345 C ALA A 335 -13.192 -8.175 23.182 1.00 70.98 C
ANISOU 3345 C ALA A 335 12144 6282 8544 2064 495 1278 C
ATOM 3346 O ALA A 335 -12.067 -8.563 23.522 1.00 69.06 O
ANISOU 3346 O ALA A 335 11951 6091 8199 2515 502 1440 O
ATOM 3347 CB ALA A 335 -13.373 -5.930 22.052 1.00 57.75 C
ANISOU 3347 CB ALA A 335 9602 5093 7249 1779 304 1025 C
ATOM 3348 N PHE A 336 -14.269 -8.366 23.956 1.00 75.76 N
ANISOU 3348 N PHE A 336 12901 6800 9083 1710 512 1247 N
ATOM 3349 CA PHE A 336 -14.166 -9.163 25.179 1.00 75.51 C
ANISOU 3349 CA PHE A 336 13189 6653 8849 1833 556 1403 C
ATOM 3350 C PHE A 336 -13.755 -10.596 24.869 1.00 75.11 C
ANISOU 3350 C PHE A 336 13725 6221 8594 2081 716 1509 C
ATOM 3351 O PHE A 336 -12.896 -11.164 25.553 1.00 83.31 O
ANISOU 3351 O PHE A 336 14825 7334 9495 2424 728 1634 O
ATOM 3352 CB PHE A 336 -15.490 -9.167 25.952 1.00 76.28 C
ANISOU 3352 CB PHE A 336 13364 6722 8898 1359 567 1339 C
ATOM 3353 CG PHE A 336 -15.894 -7.825 26.503 1.00 71.96 C
ANISOU 3353 CG PHE A 336 12258 6577 8506 1154 427 1237 C
ATOM 3354 CD1 PHE A 336 -14.944 -6.926 26.958 1.00 73.11 C
ANISOU 3354 CD1 PHE A 336 11986 7056 8735 1420 294 1273 C
ATOM 3355 CD2 PHE A 336 -17.234 -7.471 26.558 1.00 66.13 C
ANISOU 3355 CD2 PHE A 336 11430 5893 7804 691 437 1109 C
ATOM 3356 CE1 PHE A 336 -15.316 -5.696 27.465 1.00 74.07 C
ANISOU 3356 CE1 PHE A 336 11675 7497 8972 1227 182 1171 C
ATOM 3357 CE2 PHE A 336 -17.617 -6.250 27.053 1.00 73.18 C
ANISOU 3357 CE2 PHE A 336 11860 7127 8817 551 332 1019 C
ATOM 3358 CZ PHE A 336 -16.654 -5.353 27.515 1.00 75.92 C
ANISOU 3358 CZ PHE A 336 11856 7746 9246 820 208 1044 C
ATOM 3359 N LEU A 337 -14.363 -11.206 23.845 1.00 75.29 N
ANISOU 3359 N LEU A 337 14026 5993 8589 1823 823 1382 N
ATOM 3360 CA LEU A 337 -14.017 -12.585 23.510 1.00 82.93 C
ANISOU 3360 CA LEU A 337 15425 6737 9349 1959 966 1387 C
ATOM 3361 C LEU A 337 -12.669 -12.697 22.809 1.00 82.77 C
ANISOU 3361 C LEU A 337 15253 6857 9340 2434 981 1422 C
ATOM 3362 O LEU A 337 -12.118 -13.798 22.730 1.00 82.28 O
ANISOU 3362 O LEU A 337 15526 6657 9078 2675 1103 1465 O
ATOM 3363 CB LEU A 337 -15.111 -13.231 22.653 1.00 83.48 C
ANISOU 3363 CB LEU A 337 15856 6525 9338 1504 1070 1240 C
ATOM 3364 CG LEU A 337 -16.193 -13.972 23.453 1.00 86.20 C
ANISOU 3364 CG LEU A 337 16589 6669 9493 1106 1138 1237 C
ATOM 3365 CD1 LEU A 337 -17.143 -12.974 24.152 1.00 82.17 C
ANISOU 3365 CD1 LEU A 337 15807 6309 9106 739 1041 1234 C
ATOM 3366 CD2 LEU A 337 -16.961 -14.984 22.589 1.00 83.94 C
ANISOU 3366 CD2 LEU A 337 16744 6121 9028 749 1263 1108 C
ATOM 3367 N SER A 338 -12.119 -11.589 22.312 1.00 80.24 N
ANISOU 3367 N SER A 338 14443 6818 9226 2571 869 1405 N
ATOM 3368 CA SER A 338 -10.766 -11.605 21.775 1.00 80.60 C
ANISOU 3368 CA SER A 338 14274 7082 9270 3006 873 1456 C
ATOM 3369 C SER A 338 -9.697 -11.425 22.854 1.00 86.97 C
ANISOU 3369 C SER A 338 14816 8210 10017 3389 797 1622 C
ATOM 3370 O SER A 338 -8.510 -11.595 22.559 1.00 91.23 O
ANISOU 3370 O SER A 338 15198 8966 10499 3757 817 1688 O
ATOM 3371 CB SER A 338 -10.620 -10.526 20.702 1.00 75.14 C
ANISOU 3371 CB SER A 338 13172 6574 8803 2950 791 1358 C
ATOM 3372 OG SER A 338 -9.471 -10.756 19.910 1.00 82.42 O
ANISOU 3372 OG SER A 338 13985 7645 9687 3285 837 1382 O
ATOM 3373 N ALA A 339 -10.083 -11.088 24.089 1.00 84.62 N
ANISOU 3373 N ALA A 339 14460 7978 9713 3297 711 1694 N
ATOM 3374 CA ALA A 339 -9.158 -11.052 25.218 1.00 82.40 C
ANISOU 3374 CA ALA A 339 13981 7997 9332 3624 641 1857 C
ATOM 3375 C ALA A 339 -9.174 -12.356 26.009 1.00 83.91 C
ANISOU 3375 C ALA A 339 14648 7958 9275 3747 763 1951 C
ATOM 3376 O ALA A 339 -8.113 -12.857 26.404 1.00 88.43 O
ANISOU 3376 O ALA A 339 15193 8705 9700 4142 792 2073 O
ATOM 3377 CB ALA A 339 -9.487 -9.877 26.147 1.00 77.14 C
ANISOU 3377 CB ALA A 339 12963 7573 8773 3476 467 1892 C
ATOM 3378 N PHE A 340 -10.364 -12.924 26.246 1.00 88.81 N
ANISOU 3378 N PHE A 340 15709 8205 9830 3404 843 1894 N
ATOM 3379 CA PHE A 340 -10.492 -14.255 26.840 1.00 96.52 C
ANISOU 3379 CA PHE A 340 17216 8902 10556 3467 983 1953 C
ATOM 3380 C PHE A 340 -10.019 -15.376 25.908 1.00100.78 C
ANISOU 3380 C PHE A 340 18127 9224 10939 3680 1158 1917 C
ATOM 3381 O PHE A 340 -10.107 -16.538 26.313 1.00101.25 O
ANISOU 3381 O PHE A 340 18683 9023 10766 3750 1293 1955 O
ATOM 3382 CB PHE A 340 -11.941 -14.517 27.264 1.00 99.63 C
ANISOU 3382 CB PHE A 340 17960 8986 10907 2966 1021 1886 C
ATOM 3383 CG PHE A 340 -12.329 -13.860 28.566 1.00106.83 C
ANISOU 3383 CG PHE A 340 18689 10059 11843 2838 903 1975 C
ATOM 3384 CD1 PHE A 340 -11.560 -12.842 29.111 1.00107.83 C
ANISOU 3384 CD1 PHE A 340 18308 10591 12070 3086 742 2072 C
ATOM 3385 CD2 PHE A 340 -13.461 -14.276 29.253 1.00110.30 C
ANISOU 3385 CD2 PHE A 340 19466 10267 12175 2446 955 1960 C
ATOM 3386 CE1 PHE A 340 -11.922 -12.248 30.309 1.00105.83 C
ANISOU 3386 CE1 PHE A 340 17918 10490 11801 2966 636 2153 C
ATOM 3387 CE2 PHE A 340 -13.824 -13.685 30.449 1.00106.89 C
ANISOU 3387 CE2 PHE A 340 18884 9990 11738 2324 859 2047 C
ATOM 3388 CZ PHE A 340 -13.055 -12.671 30.976 1.00104.05 C
ANISOU 3388 CZ PHE A 340 18049 10015 11470 2596 701 2144 C
ATOM 3389 N ARG A 341 -9.537 -15.025 24.704 1.00100.61 N
ANISOU 3389 N ARG A 341 17892 9309 11027 3778 1162 1846 N
ATOM 3390 CA ARG A 341 -8.946 -15.972 23.762 1.00100.09 C
ANISOU 3390 CA ARG A 341 18133 9095 10803 4029 1326 1824 C
ATOM 3391 C ARG A 341 -7.436 -15.824 23.608 1.00101.64 C
ANISOU 3391 C ARG A 341 17990 9660 10969 4552 1319 1937 C
ATOM 3392 O ARG A 341 -6.814 -16.681 22.975 1.00104.15 O
ANISOU 3392 O ARG A 341 18582 9883 11109 4839 1474 1953 O
ATOM 3393 CB ARG A 341 -9.582 -15.810 22.380 1.00 92.60 C
ANISOU 3393 CB ARG A 341 17253 7972 9958 3717 1361 1653 C
ATOM 3394 CG ARG A 341 -10.750 -16.702 22.042 1.00 86.24 C
ANISOU 3394 CG ARG A 341 17027 6729 9011 3317 1485 1536 C
ATOM 3395 CD ARG A 341 -11.243 -16.256 20.672 1.00 85.47 C
ANISOU 3395 CD ARG A 341 16834 6586 9054 3029 1474 1381 C
ATOM 3396 NE ARG A 341 -10.180 -15.526 19.969 1.00 88.34 N
ANISOU 3396 NE ARG A 341 16739 7260 9567 3357 1415 1406 N
ATOM 3397 CZ ARG A 341 -10.367 -14.777 18.889 1.00 89.97 C
ANISOU 3397 CZ ARG A 341 16680 7544 9959 3186 1358 1298 C
ATOM 3398 NH1 ARG A 341 -9.345 -14.137 18.323 1.00 90.39 N
ANISOU 3398 NH1 ARG A 341 16320 7896 10127 3483 1308 1329 N
ATOM 3399 NH2 ARG A 341 -11.579 -14.662 18.386 1.00 86.14 N
ANISOU 3399 NH2 ARG A 341 16333 6864 9533 2703 1351 1161 N
ATOM 3400 N CYS A 342 -6.838 -14.741 24.115 1.00 99.35 N
ANISOU 3400 N CYS A 342 17112 9806 10829 4662 1147 2013 N
ATOM 3401 CA CYS A 342 -5.389 -14.637 24.245 1.00 99.77 C
ANISOU 3401 CA CYS A 342 16822 10279 10807 5129 1130 2146 C
ATOM 3402 C CYS A 342 -4.946 -14.841 25.686 1.00105.27 C
ANISOU 3402 C CYS A 342 17467 11164 11365 5352 1083 2310 C
ATOM 3403 O CYS A 342 -3.863 -14.385 26.070 1.00107.90 O
ANISOU 3403 O CYS A 342 17359 11961 11676 5636 1000 2426 O
ATOM 3404 CB CYS A 342 -4.873 -13.303 23.710 1.00 97.33 C
ANISOU 3404 CB CYS A 342 15872 10388 10720 5088 973 2115 C
ATOM 3405 SG CYS A 342 -5.154 -13.056 21.939 1.00100.58 S
ANISOU 3405 SG CYS A 342 16296 10641 11277 4903 1030 1942 S
ATOM 3406 N GLU A 343 -5.769 -15.520 26.483 1.00109.84 N
ANISOU 3406 N GLU A 343 18486 11409 11838 5205 1136 2321 N
ATOM 3407 CA GLU A 343 -5.436 -15.886 27.852 1.00114.14 C
ANISOU 3407 CA GLU A 343 19078 12066 12223 5414 1115 2477 C
ATOM 3408 C GLU A 343 -6.159 -17.172 28.248 1.00115.49 C
ANISOU 3408 C GLU A 343 19953 11743 12185 5349 1281 2471 C
ATOM 3409 O GLU A 343 -7.071 -17.158 29.079 1.00113.35 O
ANISOU 3409 O GLU A 343 19848 11299 11922 5048 1236 2466 O
ATOM 3410 CB GLU A 343 -5.800 -14.758 28.823 1.00113.51 C
ANISOU 3410 CB GLU A 343 18586 12247 12296 5172 900 2508 C
ATOM 3411 CG GLU A 343 -4.915 -14.701 30.059 1.00117.14 C
ANISOU 3411 CG GLU A 343 18793 13091 12624 5478 814 2691 C
ATOM 3412 CD GLU A 343 -3.925 -13.556 30.011 1.00116.13 C
ANISOU 3412 CD GLU A 343 17974 13553 12599 5593 644 2737 C
ATOM 3413 OE1 GLU A 343 -4.365 -12.398 29.849 1.00110.85 O
ANISOU 3413 OE1 GLU A 343 16965 13017 12136 5279 494 2651 O
ATOM 3414 OE2 GLU A 343 -2.709 -13.818 30.133 1.00118.98 O
ANISOU 3414 OE2 GLU A 343 18139 14253 12815 5988 670 2858 O
TER 3415 GLU A 343
HETATM 3416 C13 H46 A1201 -24.514 10.788 46.368 1.00 84.26 C
ANISOU 3416 C13 H46 A1201 12071 11673 8271 -58 587 -353 C
HETATM 3417 C17 H46 A1201 -22.994 8.364 47.529 1.00 83.83 C
ANISOU 3417 C17 H46 A1201 12033 11687 8131 -330 311 -27 C
HETATM 3418 C20 H46 A1201 -22.088 9.165 50.146 1.00 80.41 C
ANISOU 3418 C20 H46 A1201 11985 11400 7169 -482 222 -89 C
HETATM 3419 C21 H46 A1201 -22.337 10.155 49.125 1.00 79.97 C
ANISOU 3419 C21 H46 A1201 11890 11231 7264 -394 277 -234 C
HETATM 3420 C24 H46 A1201 -22.759 4.744 51.795 1.00 83.53 C
ANISOU 3420 C24 H46 A1201 12428 11946 7364 -632 275 520 C
HETATM 3421 C26 H46 A1201 -20.636 5.451 52.145 1.00 82.78 C
ANISOU 3421 C26 H46 A1201 12374 11906 7174 -609 -49 518 C
HETATM 3422 C28 H46 A1201 -21.529 3.629 53.114 1.00 91.15 C
ANISOU 3422 C28 H46 A1201 13589 12976 8069 -658 91 763 C
HETATM 3423 C01 H46 A1201 -24.814 11.630 43.927 1.00 75.36 C
ANISOU 3423 C01 H46 A1201 10727 10390 7518 139 608 -446 C
HETATM 3424 C02 H46 A1201 -24.981 11.839 45.315 1.00 83.23 C
ANISOU 3424 C02 H46 A1201 11904 11461 8258 112 674 -475 C
HETATM 3425 C03 H46 A1201 -25.539 13.016 45.757 1.00 83.43 C
ANISOU 3425 C03 H46 A1201 12113 11473 8115 257 823 -613 C
HETATM 3426 C04 H46 A1201 -25.931 14.027 44.802 1.00 82.42 C
ANISOU 3426 C04 H46 A1201 11999 11247 8070 453 909 -714 C
HETATM 3427 C05 H46 A1201 -25.791 13.794 43.416 1.00 74.92 C
ANISOU 3427 C05 H46 A1201 10843 10243 7381 473 835 -674 C
HETATM 3428 C06 H46 A1201 -25.219 12.592 42.972 1.00 72.24 C
ANISOU 3428 C06 H46 A1201 10311 9922 7215 305 683 -545 C
HETATM 3429 C07 H46 A1201 -24.584 13.266 48.064 1.00 77.44 C
ANISOU 3429 C07 H46 A1201 11766 10726 6930 37 742 -662 C
HETATM 3430 C08 H46 A1201 -24.721 13.658 49.405 1.00 82.45 C
ANISOU 3430 C08 H46 A1201 12647 11409 7271 8 818 -724 C
HETATM 3431 C09 H46 A1201 -25.979 14.040 49.981 1.00 90.87 C
ANISOU 3431 C09 H46 A1201 13780 12577 8171 194 1069 -779 C
HETATM 3432 C11 H46 A1201 -26.957 13.789 47.759 1.00 79.73 C
ANISOU 3432 C11 H46 A1201 11918 11196 7180 431 1149 -715 C
HETATM 3433 C12 H46 A1201 -25.702 13.309 47.259 1.00 79.09 C
ANISOU 3433 C12 H46 A1201 11796 10989 7267 232 904 -661 C
HETATM 3434 C16 H46 A1201 -22.773 9.735 47.824 1.00 81.93 C
ANISOU 3434 C16 H46 A1201 11929 11419 7781 -307 315 -194 C
HETATM 3435 C18 H46 A1201 -22.711 7.394 48.539 1.00 84.83 C
ANISOU 3435 C18 H46 A1201 12241 11887 8103 -417 263 114 C
HETATM 3436 C19 H46 A1201 -22.310 7.824 49.786 1.00 79.01 C
ANISOU 3436 C19 H46 A1201 11674 11230 7117 -475 224 83 C
HETATM 3437 C23 H46 A1201 -23.301 6.037 51.138 1.00 80.66 C
ANISOU 3437 C23 H46 A1201 11966 11572 7108 -573 364 311 C
HETATM 3438 C27 H46 A1201 -20.851 6.777 51.358 1.00 79.36 C
ANISOU 3438 C27 H46 A1201 11871 11412 6872 -590 -8 302 C
HETATM 3439 C29 H46 A1201 -22.677 3.478 54.150 1.00 97.49 C
ANISOU 3439 C29 H46 A1201 14506 13869 8667 -759 278 756 C
HETATM 3440 C32 H46 A1201 -24.352 2.043 55.437 1.00 98.80 C
ANISOU 3440 C32 H46 A1201 14861 14127 8551 -954 557 929 C
HETATM 3441 C33 H46 A1201 -25.374 1.021 54.760 1.00 94.73 C
ANISOU 3441 C33 H46 A1201 14314 13545 8135 -1070 711 1018 C
HETATM 3442 C34 H46 A1201 -22.721 0.994 53.717 1.00 89.32 C
ANISOU 3442 C34 H46 A1201 13612 12633 7693 -783 294 1107 C
HETATM 3443 C35 H46 A1201 -23.475 1.139 52.353 1.00 85.20 C
ANISOU 3443 C35 H46 A1201 12916 12022 7435 -802 395 1009 C
HETATM 3444 C36 H46 A1201 -20.374 3.441 54.159 1.00 88.32 C
ANISOU 3444 C36 H46 A1201 13340 12737 7479 -654 -89 878 C
HETATM 3445 C37 H46 A1201 -20.057 4.422 55.149 1.00 88.89 C
ANISOU 3445 C37 H46 A1201 13488 12961 7326 -732 -142 767 C
HETATM 3446 C38 H46 A1201 -18.938 4.162 56.052 1.00 92.13 C
ANISOU 3446 C38 H46 A1201 13966 13532 7509 -743 -331 897 C
HETATM 3447 C39 H46 A1201 -18.168 2.957 56.002 1.00 94.79 C
ANISOU 3447 C39 H46 A1201 14297 13880 7838 -623 -450 1144 C
HETATM 3448 C40 H46 A1201 -18.517 2.009 54.984 1.00 91.72 C
ANISOU 3448 C40 H46 A1201 13877 13289 7682 -516 -373 1243 C
HETATM 3449 C41 H46 A1201 -19.642 2.238 54.105 1.00 85.12 C
ANISOU 3449 C41 H46 A1201 12980 12294 7066 -563 -194 1105 C
HETATM 3450 F42 H46 A1201 -22.855 5.913 48.434 1.00 90.97 F
ANISOU 3450 F42 H46 A1201 12983 12652 8930 -458 265 300 F
HETATM 3451 N10 H46 A1201 -27.082 14.110 49.128 1.00 86.14 N
ANISOU 3451 N10 H46 A1201 12972 12055 7702 417 1234 -770 N
HETATM 3452 N14 H46 A1201 -23.070 10.848 46.809 1.00 80.11 N
ANISOU 3452 N14 H46 A1201 11677 11081 7680 -194 379 -342 N
HETATM 3453 N22 H46 A1201 -22.105 6.682 50.635 1.00 78.61 N
ANISOU 3453 N22 H46 A1201 11685 11248 6934 -539 182 256 N
HETATM 3454 N25 H46 A1201 -21.770 4.961 52.682 1.00 86.42 N
ANISOU 3454 N25 H46 A1201 12903 12384 7548 -649 129 548 N
HETATM 3455 N30 H46 A1201 -23.206 2.168 54.477 1.00 96.43 N
ANISOU 3455 N30 H46 A1201 14478 13703 8459 -830 365 934 N
HETATM 3456 O15 H46 A1201 -25.295 9.910 46.775 1.00 85.45 O
ANISOU 3456 O15 H46 A1201 12134 11960 8374 -88 682 -256 O
HETATM 3457 O31 H46 A1201 -23.079 4.504 54.770 1.00 99.49 O
ANISOU 3457 O31 H46 A1201 14792 14223 8785 -784 354 601 O
HETATM 3458 N1 FMN A1202 -3.784 10.353 -16.379 1.00 48.80 N
ANISOU 3458 N1 FMN A1202 5280 6207 7056 845 758 -230 N
HETATM 3459 C2 FMN A1202 -3.199 9.712 -15.304 1.00 46.22 C
ANISOU 3459 C2 FMN A1202 4842 5979 6742 1041 792 -187 C
HETATM 3460 O2 FMN A1202 -3.721 8.736 -14.779 1.00 46.18 O
ANISOU 3460 O2 FMN A1202 5004 5785 6759 1184 808 -226 O
HETATM 3461 N3 FMN A1202 -1.995 10.149 -14.813 1.00 46.13 N
ANISOU 3461 N3 FMN A1202 4530 6304 6695 1067 811 -89 N
HETATM 3462 C4 FMN A1202 -1.392 11.251 -15.373 1.00 52.42 C
ANISOU 3462 C4 FMN A1202 5156 7318 7443 856 797 -43 C
HETATM 3463 O4 FMN A1202 -0.318 11.660 -14.938 1.00 63.57 O
ANISOU 3463 O4 FMN A1202 6287 9070 8798 826 808 46 O
HETATM 3464 C4A FMN A1202 -1.979 11.896 -16.444 1.00 50.30 C
ANISOU 3464 C4A FMN A1202 5036 6906 7168 663 772 -89 C
HETATM 3465 N5 FMN A1202 -1.331 12.972 -16.996 1.00 50.65 N
ANISOU 3465 N5 FMN A1202 4946 7154 7145 446 770 -36 N
HETATM 3466 C5A FMN A1202 -1.879 13.637 -18.062 1.00 51.49 C
ANISOU 3466 C5A FMN A1202 5213 7120 7230 271 748 -67 C
HETATM 3467 C6 FMN A1202 -1.215 14.741 -18.599 1.00 56.87 C
ANISOU 3467 C6 FMN A1202 5796 7986 7827 32 752 -7 C
HETATM 3468 C7 FMN A1202 -1.760 15.387 -19.702 1.00 54.22 C
ANISOU 3468 C7 FMN A1202 5646 7501 7454 -120 736 -27 C
HETATM 3469 C7M FMN A1202 -1.089 16.560 -20.345 1.00 52.40 C
ANISOU 3469 C7M FMN A1202 5367 7429 7112 -393 751 39 C
HETATM 3470 C8 FMN A1202 -2.966 14.933 -20.205 1.00 52.30 C
ANISOU 3470 C8 FMN A1202 5644 6969 7257 -34 703 -104 C
HETATM 3471 C8M FMN A1202 -3.569 15.620 -21.374 1.00 51.92 C
ANISOU 3471 C8M FMN A1202 5781 6796 7152 -176 676 -111 C
HETATM 3472 C9 FMN A1202 -3.630 13.861 -19.650 1.00 52.57 C
ANISOU 3472 C9 FMN A1202 5759 6849 7368 161 691 -167 C
HETATM 3473 C9A FMN A1202 -3.088 13.198 -18.575 1.00 48.65 C
ANISOU 3473 C9A FMN A1202 5117 6456 6912 317 719 -151 C
HETATM 3474 N10 FMN A1202 -3.744 12.114 -18.028 1.00 47.39 N
ANISOU 3474 N10 FMN A1202 5076 6120 6811 497 717 -209 N
HETATM 3475 C10 FMN A1202 -3.178 11.449 -16.959 1.00 49.67 C
ANISOU 3475 C10 FMN A1202 5239 6509 7126 674 750 -180 C
HETATM 3476 C1' FMN A1202 -5.051 11.635 -18.599 1.00 47.20 C
ANISOU 3476 C1' FMN A1202 5318 5819 6795 484 680 -296 C
HETATM 3477 C2' FMN A1202 -6.251 12.485 -18.160 1.00 49.04 C
ANISOU 3477 C2' FMN A1202 5608 5904 7122 304 516 -311 C
HETATM 3478 O2' FMN A1202 -6.406 12.392 -16.763 1.00 51.72 O
ANISOU 3478 O2' FMN A1202 5870 6219 7561 340 453 -305 O
HETATM 3479 C3' FMN A1202 -7.527 11.978 -18.848 1.00 49.69 C
ANISOU 3479 C3' FMN A1202 5907 5801 7172 274 479 -383 C
HETATM 3480 O3' FMN A1202 -7.551 12.272 -20.223 1.00 49.22 O
ANISOU 3480 O3' FMN A1202 5932 5760 7009 201 511 -385 O
HETATM 3481 C4' FMN A1202 -8.839 12.403 -18.188 1.00 45.46 C
ANISOU 3481 C4' FMN A1202 5405 5153 6716 182 333 -396 C
HETATM 3482 O4' FMN A1202 -9.900 11.834 -18.887 1.00 45.19 O
ANISOU 3482 O4' FMN A1202 5529 5028 6614 135 307 -452 O
HETATM 3483 C5' FMN A1202 -9.172 13.876 -18.186 1.00 46.22 C
ANISOU 3483 C5' FMN A1202 5459 5265 6839 60 234 -340 C
HETATM 3484 O5' FMN A1202 -10.266 13.979 -17.295 1.00 42.11 O
ANISOU 3484 O5' FMN A1202 4946 4664 6388 57 130 -351 O
HETATM 3485 P FMN A1202 -11.353 15.153 -17.474 1.00 45.03 P
ANISOU 3485 P FMN A1202 5364 5001 6746 -3 19 -310 P
HETATM 3486 O1P FMN A1202 -12.531 14.983 -16.550 1.00 51.91 O
ANISOU 3486 O1P FMN A1202 6217 5838 7669 34 -67 -324 O
HETATM 3487 O2P FMN A1202 -10.742 16.498 -17.137 1.00 53.01 O
ANISOU 3487 O2P FMN A1202 6364 6004 7773 -55 6 -246 O
HETATM 3488 O3P FMN A1202 -11.815 15.098 -18.916 1.00 50.27 O
ANISOU 3488 O3P FMN A1202 6121 5687 7293 -44 19 -311 O
CONECT 582 1210
CONECT 1210 582
CONECT 3416 3424 3452 3456
CONECT 3417 3434 3435
CONECT 3418 3419 3436
CONECT 3419 3418 3434
CONECT 3420 3437 3454
CONECT 3421 3438 3454
CONECT 3422 3439 3444 3454
CONECT 3423 3424 3428
CONECT 3424 3416 3423 3425
CONECT 3425 3424 3426 3433
CONECT 3426 3425 3427
CONECT 3427 3426 3428
CONECT 3428 3423 3427
CONECT 3429 3430 3433
CONECT 3430 3429 3431
CONECT 3431 3430 3451
CONECT 3432 3433 3451
CONECT 3433 3425 3429 3432
CONECT 3434 3417 3419 3452
CONECT 3435 3417 3436 3450
CONECT 3436 3418 3435 3453
CONECT 3437 3420 3453
CONECT 3438 3421 3453
CONECT 3439 3422 3455 3457
CONECT 3440 3441 3455
CONECT 3441 3440
CONECT 3442 3443 3455
CONECT 3443 3442
CONECT 3444 3422 3445 3449
CONECT 3445 3444 3446
CONECT 3446 3445 3447
CONECT 3447 3446 3448
CONECT 3448 3447 3449
CONECT 3449 3444 3448
CONECT 3450 3435
CONECT 3451 3431 3432
CONECT 3452 3416 3434
CONECT 3453 3436 3437 3438
CONECT 3454 3420 3421 3422
CONECT 3455 3439 3440 3442
CONECT 3456 3416
CONECT 3457 3439
CONECT 3458 3459 3475
CONECT 3459 3458 3460 3461
CONECT 3460 3459
CONECT 3461 3459 3462
CONECT 3462 3461 3463 3464
CONECT 3463 3462
CONECT 3464 3462 3465 3475
CONECT 3465 3464 3466
CONECT 3466 3465 3467 3473
CONECT 3467 3466 3468
CONECT 3468 3467 3469 3470
CONECT 3469 3468
CONECT 3470 3468 3471 3472
CONECT 3471 3470
CONECT 3472 3470 3473
CONECT 3473 3466 3472 3474
CONECT 3474 3473 3475 3476
CONECT 3475 3458 3464 3474
CONECT 3476 3474 3477
CONECT 3477 3476 3478 3479
CONECT 3478 3477
CONECT 3479 3477 3480 3481
CONECT 3480 3479
CONECT 3481 3479 3482 3483
CONECT 3482 3481
CONECT 3483 3481 3484
CONECT 3484 3483 3485
CONECT 3485 3484 3486 3487 3488
CONECT 3486 3485
CONECT 3487 3485
CONECT 3488 3485
MASTER 476 0 2 17 14 0 0 6 3487 1 75 52
END