HEADER MEMBRANE PROTEIN 11-OCT-21 7PYR
TITLE CRYSTAL STRUCTURE OF THE ADENOSINE A2A RECEPTOR (A2A-PSB1-BRIL) IN
TITLE 2 COMPLEX WITH PRELADENANT CONJUGATE PSB-2115
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE
COMPND 3 RECEPTOR A2A;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: CYTOCHROME B-562;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: ADORA2A, ADORA2, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS GPCR, MEMBRANE PROTEIN, A2A, G PROTEIN-COUPLED RECEPTOR, ADENOSINE
KEYWDS 2 RECEPTOR, PRELADENANT
EXPDTA X-RAY DIFFRACTION
AUTHOR T.CLAFF,T.A.KLAPSCHINSKI,U.K.TIRUTTANI SUBHRAMANYAM,V.J.VAASSEN,
AUTHOR 2 J.G.SCHLEGEL,C.VIELMUTH,J.H.VOSS,J.LABAHN,C.E.MULLER
REVDAT 3 25-MAY-22 7PYR 1 JRNL
REVDAT 2 06-APR-22 7PYR 1 JRNL
REVDAT 1 02-MAR-22 7PYR 0
JRNL AUTH T.CLAFF,T.A.KLAPSCHINSKI,U.K.TIRUTTANI SUBHRAMANYAM,
JRNL AUTH 2 V.J.VAASSEN,J.G.SCHLEGEL,C.VIELMUTH,J.H.VOSS,J.LABAHN,
JRNL AUTH 3 C.E.MULLER
JRNL TITL SINGLE STABILIZING POINT MUTATION ENABLES HIGH-RESOLUTION
JRNL TITL 2 CO-CRYSTAL STRUCTURES OF THE ADENOSINE A 2A RECEPTOR WITH
JRNL TITL 3 PRELADENANT CONJUGATES.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 61 15545 2022
JRNL REFN ESSN 1521-3773
JRNL PMID 35174942
JRNL DOI 10.1002/ANIE.202115545
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 15571
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1561
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 45.0300 - 5.7800 0.99 1398 155 0.2189 0.2753
REMARK 3 2 5.7800 - 4.5900 1.00 1322 148 0.1944 0.2349
REMARK 3 3 4.5900 - 4.0100 1.00 1288 143 0.1580 0.2033
REMARK 3 4 4.0100 - 3.6400 0.99 1316 145 0.1588 0.2042
REMARK 3 5 3.6400 - 3.3800 0.99 1279 142 0.1934 0.3097
REMARK 3 6 3.3800 - 3.1800 0.98 1254 141 0.1940 0.2836
REMARK 3 7 3.1800 - 3.0200 0.98 1249 142 0.2076 0.2739
REMARK 3 8 3.0200 - 2.8900 0.97 1246 138 0.2041 0.2819
REMARK 3 9 2.8900 - 2.7800 0.97 1236 134 0.2100 0.2521
REMARK 3 10 2.7800 - 2.6800 0.96 1230 141 0.2299 0.2602
REMARK 3 11 2.6800 - 2.6000 0.95 1192 132 0.2357 0.2973
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) : 0.289
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 3621
REMARK 3 ANGLE : 0.612 4799
REMARK 3 CHIRALITY : 0.041 527
REMARK 3 PLANARITY : 0.003 559
REMARK 3 DIHEDRAL : 12.550 1409
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -2 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5227 -3.8536 20.8846
REMARK 3 T TENSOR
REMARK 3 T11: 0.2497 T22: 0.3144
REMARK 3 T33: 0.2220 T12: -0.0262
REMARK 3 T13: 0.0017 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 1.7036 L22: 0.7206
REMARK 3 L33: 1.7448 L12: -0.3566
REMARK 3 L13: 0.3408 L23: 0.1319
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: -0.0147 S13: 0.0122
REMARK 3 S21: -0.0463 S22: 0.0741 S23: 0.0772
REMARK 3 S31: -0.0588 S32: -0.0596 S33: -0.0004
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 258 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7515 -39.0542 18.8599
REMARK 3 T TENSOR
REMARK 3 T11: 0.6400 T22: 0.4919
REMARK 3 T33: 0.8309 T12: 0.1052
REMARK 3 T13: -0.0213 T23: -0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 1.0606 L22: 0.7877
REMARK 3 L33: 0.3569 L12: -0.5110
REMARK 3 L13: 0.1913 L23: -0.4759
REMARK 3 S TENSOR
REMARK 3 S11: 0.0843 S12: 0.0040 S13: -0.6849
REMARK 3 S21: -0.3216 S22: 0.0213 S23: -0.2558
REMARK 3 S31: 0.4028 S32: 0.1828 S33: 0.0008
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 259 THROUGH 2435 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4462 -4.2189 14.2155
REMARK 3 T TENSOR
REMARK 3 T11: 0.3388 T22: 0.4880
REMARK 3 T33: 0.2766 T12: -0.0056
REMARK 3 T13: 0.0171 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 2.1840 L22: 3.1986
REMARK 3 L33: 1.8217 L12: 0.1963
REMARK 3 L13: 0.3030 L23: 0.1128
REMARK 3 S TENSOR
REMARK 3 S11: -0.0813 S12: -0.1302 S13: -0.1460
REMARK 3 S21: 0.0749 S22: 0.1038 S23: 0.1351
REMARK 3 S31: -0.0117 S32: -0.1911 S33: 0.0001
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 7PYR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1292118642.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-21
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 : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL (SI-111 AND SI
REMARK 200 -113 REFLECTION)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15875
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 45.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
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: PHASER
REMARK 200 STARTING MODEL: A2A MODEL WITH PSB-2113 LIGAND
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% (V/V) PEG-400 (POLYETHYLENE GLYCOL
REMARK 280 400, AVERAGE MOLECULAR WEIGHT 400), 10-30 MM SODIUM THIOCYANATE,
REMARK 280 100 MM SODIUM CITRATE PH 5.2, AND 2% (V/V) 2,5-HEXANEDIOL,
REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 70.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.65500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.05500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.65500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.05500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.20000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.65500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.05500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.20000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.65500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.05500
REMARK 290 SMTRY3 8 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 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 MET A -24
REMARK 465 LYS A -23
REMARK 465 THR A -22
REMARK 465 ILE A -21
REMARK 465 ILE A -20
REMARK 465 ALA A -19
REMARK 465 LEU A -18
REMARK 465 SER A -17
REMARK 465 TYR A -16
REMARK 465 ILE A -15
REMARK 465 PHE A -14
REMARK 465 CYS A -13
REMARK 465 LEU A -12
REMARK 465 VAL A -11
REMARK 465 PHE A -10
REMARK 465 ALA A -9
REMARK 465 ASP A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ALA A 1043
REMARK 465 THR A 1044
REMARK 465 PRO A 1045
REMARK 465 PRO A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 PRO A 1056
REMARK 465 HIS A 306
REMARK 465 VAL A 307
REMARK 465 LEU A 308
REMARK 465 ARG A 309
REMARK 465 GLN A 310
REMARK 465 GLN A 311
REMARK 465 GLU A 312
REMARK 465 PRO A 313
REMARK 465 PHE A 314
REMARK 465 LYS A 315
REMARK 465 ALA A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 199 NE CZ NH1 NH2
REMARK 470 GLU A1008 CD OE1 OE2
REMARK 470 LYS A1042 CG CD CE NZ
REMARK 470 GLU A1057 CG CD OE1 OE2
REMARK 470 MET A1058 CG SD CE
REMARK 470 LYS A1059 CG CD CE NZ
REMARK 470 PHE A1061 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 38 69.79 -102.67
REMARK 500 CYS A 166 97.98 -70.00
REMARK 500 TYR A1101 -58.81 -141.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 8IM A 2404
REMARK 610 OLA A 2405
REMARK 610 OLA A 2406
REMARK 610 OLA A 2408
REMARK 610 OLA A 2409
REMARK 610 OLA A 2410
REMARK 610 OLA A 2411
REMARK 610 OLA A 2412
REMARK 610 OLA A 2413
REMARK 610 OLA A 2414
REMARK 610 OLA A 2416
REMARK 610 OLA A 2417
REMARK 610 OLA A 2418
REMARK 610 OLA A 2419
REMARK 610 OLA A 2420
REMARK 610 OLA A 2421
REMARK 610 OLA A 2422
REMARK 610 OLA A 2423
REMARK 610 OLA A 2424
REMARK 610 OLA A 2425
REMARK 610 OLA A 2426
REMARK 610 OLA A 2428
REMARK 610 OLA A 2429
REMARK 610 OLC A 2431
REMARK 610 OLC A 2432
REMARK 610 OLC A 2433
DBREF 7PYR A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 7PYR A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 7PYR A 219 316 UNP P29274 AA2AR_HUMAN 219 316
SEQADV 7PYR MET A -24 UNP P29274 INITIATING METHIONINE
SEQADV 7PYR LYS A -23 UNP P29274 EXPRESSION TAG
SEQADV 7PYR THR A -22 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ILE A -21 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ILE A -20 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ALA A -19 UNP P29274 EXPRESSION TAG
SEQADV 7PYR LEU A -18 UNP P29274 EXPRESSION TAG
SEQADV 7PYR SER A -17 UNP P29274 EXPRESSION TAG
SEQADV 7PYR TYR A -16 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ILE A -15 UNP P29274 EXPRESSION TAG
SEQADV 7PYR PHE A -14 UNP P29274 EXPRESSION TAG
SEQADV 7PYR CYS A -13 UNP P29274 EXPRESSION TAG
SEQADV 7PYR LEU A -12 UNP P29274 EXPRESSION TAG
SEQADV 7PYR VAL A -11 UNP P29274 EXPRESSION TAG
SEQADV 7PYR PHE A -10 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ALA A -9 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ASP A -8 UNP P29274 EXPRESSION TAG
SEQADV 7PYR TYR A -7 UNP P29274 EXPRESSION TAG
SEQADV 7PYR LYS A -6 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ASP A -5 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ASP A -4 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ASP A -3 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ASP A -2 UNP P29274 EXPRESSION TAG
SEQADV 7PYR GLY A -1 UNP P29274 EXPRESSION TAG
SEQADV 7PYR ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 7PYR PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 7PYR LYS A 91 UNP P29274 SER 91 ENGINEERED MUTATION
SEQADV 7PYR TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 7PYR ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 7PYR LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 7PYR HIS A 317 UNP P29274 EXPRESSION TAG
SEQADV 7PYR HIS A 318 UNP P29274 EXPRESSION TAG
SEQADV 7PYR HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 7PYR HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 7PYR HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 7PYR HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 7PYR HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 7PYR HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 7PYR HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 7PYR HIS A 326 UNP P29274 EXPRESSION TAG
SEQRES 1 A 447 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU
SEQRES 2 A 447 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO
SEQRES 3 A 447 PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU LEU
SEQRES 4 A 447 ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL
SEQRES 5 A 447 CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL
SEQRES 6 A 447 THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE
SEQRES 7 A 447 ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE
SEQRES 8 A 447 SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE
SEQRES 9 A 447 ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER LYS ILE
SEQRES 10 A 447 PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA
SEQRES 11 A 447 ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY
SEQRES 12 A 447 THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL LEU
SEQRES 13 A 447 SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN
SEQRES 14 A 447 ASN CYS GLY GLN PRO LYS GLU GLY LYS ASN HIS SER GLN
SEQRES 15 A 447 GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP
SEQRES 16 A 447 VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE
SEQRES 17 A 447 ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL
SEQRES 18 A 447 TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU ALA
SEQRES 19 A 447 ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU
SEQRES 20 A 447 LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS
SEQRES 21 A 447 ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA
SEQRES 22 A 447 GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO
SEQRES 23 A 447 ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP
SEQRES 24 A 447 ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA
SEQRES 25 A 447 ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU
SEQRES 26 A 447 GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR
SEQRES 27 A 447 LEU GLU ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS
SEQRES 28 A 447 ALA ALA LYS SER LEU ALA ILE ILE VAL GLY LEU PHE ALA
SEQRES 29 A 447 LEU CYS TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR
SEQRES 30 A 447 PHE PHE CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU
SEQRES 31 A 447 MET TYR LEU ALA ILE VAL LEU SER HIS THR ASN SER VAL
SEQRES 32 A 447 VAL ASN PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE
SEQRES 33 A 447 ARG GLN THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU
SEQRES 34 A 447 ARG GLN GLN GLU PRO PHE LYS ALA HIS HIS HIS HIS HIS
SEQRES 35 A 447 HIS HIS HIS HIS HIS
HET CLR A2401 28
HET CLR A2402 28
HET CLR A2403 28
HET 8IM A2404 50
HET OLA A2405 9
HET OLA A2406 11
HET OLA A2407 20
HET OLA A2408 19
HET OLA A2409 13
HET OLA A2410 7
HET OLA A2411 16
HET OLA A2412 12
HET OLA A2413 13
HET OLA A2414 12
HET OLA A2415 20
HET OLA A2416 9
HET OLA A2417 11
HET OLA A2418 16
HET OLA A2419 15
HET OLA A2420 15
HET OLA A2421 14
HET OLA A2422 9
HET OLA A2423 11
HET OLA A2424 11
HET OLA A2425 15
HET OLA A2426 14
HET OLA A2427 20
HET OLA A2428 14
HET OLA A2429 12
HET OLC A2430 25
HET OLC A2431 19
HET OLC A2432 21
HET OLC A2433 19
HET PEG A2434 7
HET PEG A2435 7
HETNAM CLR CHOLESTEROL
HETNAM 8IM 2-[2-[2-[2-[2-[2-[4-[4-[2-[7-AZANYL-4-(FURAN-2-YL)-3,5,
HETNAM 2 8IM 6,8,10,11-HEXAZATRICYCLO[7.3.0.0^{2,6}]DODECA-1(9),2,
HETNAM 3 8IM 4,7,11-PENTAEN-10-YL]ETHYL]PIPERAZIN-1-
HETNAM 4 8IM YL]PHENOXY]ETHANOYLAMINO]ETHOXY]ETHOXY]ETHOXY]ETHOXY]-
HETNAM 5 8IM ~{N}-[5-[2,2-BIS(FLUORANYL)-4,6,10,12-TETRAMETHYL-1,3-
HETNAM 6 8IM DIAZA-2$L^{4}-BORATRICYCLO[7.3.0.0^{3,7}]DODECA-4,6,9,
HETNAM 7 8IM 11-TETRAEN-8-YL]PENTYL]ETHANAMIDE
HETNAM OLA OLEIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 CLR 3(C27 H46 O)
FORMUL 5 8IM C52 H68 B F2 N13 O8
FORMUL 6 OLA 25(C18 H34 O2)
FORMUL 31 OLC 4(C21 H40 O4)
FORMUL 35 PEG 2(C4 H10 O3)
FORMUL 37 HOH *201(H2 O)
HELIX 1 AA1 PRO A 1 ASN A 34 1 34
HELIX 2 AA2 SER A 35 GLN A 38 5 4
HELIX 3 AA3 ASN A 39 LEU A 58 1 20
HELIX 4 AA4 LEU A 58 SER A 67 1 10
HELIX 5 AA5 CYS A 74 ILE A 108 1 35
HELIX 6 AA6 ARG A 111 VAL A 116 1 6
HELIX 7 AA7 THR A 117 LEU A 137 1 21
HELIX 8 AA8 THR A 138 GLY A 142 5 5
HELIX 9 AA9 LYS A 150 GLN A 157 1 8
HELIX 10 AB1 LEU A 167 VAL A 172 1 6
HELIX 11 AB2 PRO A 173 TYR A 179 1 7
HELIX 12 AB3 VAL A 186 LYS A 1019 1 42
HELIX 13 AB4 ASN A 1022 LYS A 1042 1 21
HELIX 14 AB5 MET A 1058 GLU A 1081 1 24
HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11
HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9
HELIX 17 AB8 TYR A 1101 CYS A 259 1 47
HELIX 18 AB9 PRO A 266 THR A 279 1 14
HELIX 19 AC1 THR A 279 ILE A 292 1 14
HELIX 20 AC2 ILE A 292 SER A 305 1 14
SHEET 1 AA1 2 CYS A 71 ALA A 73 0
SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72
SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03
CRYST1 39.310 180.110 140.400 90.00 90.00 90.00 C 2 2 21 8
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 0.025439 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005552 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007123 0.00000
ATOM 1 N ASP A -2 17.956 27.637 3.390 1.00104.35 N
ANISOU 1 N ASP A -2 15576 10581 13492 -1426 -727 3045 N
ATOM 2 CA ASP A -2 18.050 27.262 1.984 1.00 93.09 C
ANISOU 2 CA ASP A -2 14099 9388 11882 -1442 -646 3224 C
ATOM 3 C ASP A -2 18.228 25.756 1.821 1.00 86.15 C
ANISOU 3 C ASP A -2 13041 8855 10838 -1442 -565 3132 C
ATOM 4 O ASP A -2 18.737 25.287 0.803 1.00106.53 O
ANISOU 4 O ASP A -2 15555 11654 13267 -1529 -480 3263 O
ATOM 5 CB ASP A -2 19.203 28.004 1.304 1.00 92.59 C
ANISOU 5 CB ASP A -2 14034 9302 11843 -1636 -555 3369 C
ATOM 6 CG ASP A -2 18.916 29.480 1.115 1.00 94.60 C
ANISOU 6 CG ASP A -2 14455 9263 12226 -1601 -612 3477 C
ATOM 7 OD1 ASP A -2 17.812 29.927 1.494 1.00110.06 O
ANISOU 7 OD1 ASP A -2 16525 11042 14251 -1412 -723 3433 O
ATOM 8 OD2 ASP A -2 19.792 30.195 0.585 1.00103.54 O
ANISOU 8 OD2 ASP A -2 15604 10345 13392 -1757 -546 3605 O
ATOM 9 N GLY A -1 17.812 25.001 2.836 1.00 87.80 N
ANISOU 9 N GLY A -1 13157 9129 11075 -1328 -581 2883 N
ATOM 10 CA GLY A -1 17.827 23.557 2.732 1.00 71.43 C
ANISOU 10 CA GLY A -1 10910 7372 8857 -1287 -509 2761 C
ATOM 11 C GLY A -1 16.622 23.033 1.972 1.00 80.67 C
ANISOU 11 C GLY A -1 12072 8694 9887 -1088 -538 2784 C
ATOM 12 O GLY A -1 15.549 23.636 1.964 1.00 76.34 O
ANISOU 12 O GLY A -1 11627 8004 9375 -928 -631 2809 O
ATOM 13 N ALA A 0 16.819 21.892 1.314 1.00 61.58 N
ANISOU 13 N ALA A 0 9525 6569 7304 -1096 -463 2769 N
ATOM 14 CA ALA A 0 15.737 21.254 0.581 1.00 61.16 C
ANISOU 14 CA ALA A 0 9441 6689 7107 -921 -489 2768 C
ATOM 15 C ALA A 0 14.573 20.949 1.524 1.00 61.26 C
ANISOU 15 C ALA A 0 9434 6654 7186 -732 -564 2574 C
ATOM 16 O ALA A 0 14.779 20.733 2.723 1.00 63.01 O
ANISOU 16 O ALA A 0 9610 6812 7518 -747 -562 2402 O
ATOM 17 CB ALA A 0 16.228 19.970 -0.084 1.00 63.65 C
ANISOU 17 CB ALA A 0 9610 7321 7253 -967 -396 2734 C
ATOM 18 N PRO A 1 13.342 20.945 1.014 1.00 58.53 N
ANISOU 18 N PRO A 1 9119 6348 6773 -552 -632 2600 N
ATOM 19 CA PRO A 1 12.173 20.692 1.871 1.00 55.00 C
ANISOU 19 CA PRO A 1 8643 5871 6384 -369 -703 2426 C
ATOM 20 C PRO A 1 12.327 19.397 2.646 1.00 53.83 C
ANISOU 20 C PRO A 1 8338 5889 6225 -382 -648 2214 C
ATOM 21 O PRO A 1 12.702 18.361 2.076 1.00 65.81 O
ANISOU 21 O PRO A 1 9752 7632 7620 -434 -582 2197 O
ATOM 22 CB PRO A 1 11.013 20.609 0.869 1.00 48.04 C
ANISOU 22 CB PRO A 1 7775 5101 5378 -204 -761 2506 C
ATOM 23 CG PRO A 1 11.462 21.444 -0.279 1.00 52.16 C
ANISOU 23 CG PRO A 1 8409 5572 5838 -276 -757 2755 C
ATOM 24 CD PRO A 1 12.953 21.259 -0.372 1.00 50.22 C
ANISOU 24 CD PRO A 1 8128 5368 5584 -504 -652 2801 C
ATOM 25 N PRO A 2 12.054 19.417 3.953 1.00 72.22 N
ANISOU 25 N PRO A 2 10650 8113 8677 -330 -676 2049 N
ATOM 26 CA PRO A 2 12.290 18.214 4.768 1.00 60.09 C
ANISOU 26 CA PRO A 2 8973 6720 7137 -353 -622 1861 C
ATOM 27 C PRO A 2 11.430 17.029 4.369 1.00 52.75 C
ANISOU 27 C PRO A 2 7933 6017 6091 -248 -619 1787 C
ATOM 28 O PRO A 2 11.855 15.882 4.553 1.00 54.75 O
ANISOU 28 O PRO A 2 8073 6430 6298 -303 -556 1686 O
ATOM 29 CB PRO A 2 11.969 18.691 6.193 1.00 46.78 C
ANISOU 29 CB PRO A 2 7313 4862 5600 -289 -668 1722 C
ATOM 30 CG PRO A 2 11.057 19.864 6.006 1.00 64.68 C
ANISOU 30 CG PRO A 2 9709 6950 7919 -158 -764 1804 C
ATOM 31 CD PRO A 2 11.525 20.537 4.750 1.00 52.87 C
ANISOU 31 CD PRO A 2 8309 5410 6370 -241 -760 2025 C
ATOM 32 N ILE A 3 10.239 17.269 3.816 1.00 51.51 N
ANISOU 32 N ILE A 3 7807 5878 5888 -98 -690 1832 N
ATOM 33 CA ILE A 3 9.335 16.175 3.486 1.00 58.02 C
ANISOU 33 CA ILE A 3 8521 6910 6612 1 -698 1750 C
ATOM 34 C ILE A 3 9.869 15.318 2.343 1.00 60.51 C
ANISOU 34 C ILE A 3 8778 7433 6779 -80 -641 1805 C
ATOM 35 O ILE A 3 9.447 14.166 2.190 1.00 53.80 O
ANISOU 35 O ILE A 3 7820 6765 5857 -45 -630 1704 O
ATOM 36 CB ILE A 3 7.936 16.729 3.154 1.00 48.16 C
ANISOU 36 CB ILE A 3 7314 5635 5350 184 -796 1788 C
ATOM 37 CG1 ILE A 3 6.881 15.623 3.233 1.00 55.00 C
ANISOU 37 CG1 ILE A 3 8049 6691 6158 288 -814 1656 C
ATOM 38 CG2 ILE A 3 7.931 17.364 1.779 1.00 54.44 C
ANISOU 38 CG2 ILE A 3 8199 6440 6047 192 -823 1987 C
ATOM 39 CD1 ILE A 3 5.487 16.086 2.875 1.00 58.12 C
ANISOU 39 CD1 ILE A 3 8461 7095 6529 471 -910 1684 C
ATOM 40 N MET A 4 10.796 15.844 1.539 1.00 46.39 N
ANISOU 40 N MET A 4 7056 5626 4943 -190 -604 1961 N
ATOM 41 CA MET A 4 11.341 15.069 0.428 1.00 43.67 C
ANISOU 41 CA MET A 4 6653 5494 4444 -259 -546 2012 C
ATOM 42 C MET A 4 12.212 13.925 0.933 1.00 53.34 C
ANISOU 42 C MET A 4 7766 6833 5668 -359 -464 1873 C
ATOM 43 O MET A 4 11.950 12.752 0.645 1.00 41.15 O
ANISOU 43 O MET A 4 6125 5471 4038 -326 -449 1774 O
ATOM 44 CB MET A 4 12.131 15.982 -0.508 1.00 66.64 C
ANISOU 44 CB MET A 4 9659 8359 7301 -356 -520 2225 C
ATOM 45 CG MET A 4 11.285 17.044 -1.181 1.00 45.42 C
ANISOU 45 CG MET A 4 7089 5575 4592 -249 -603 2384 C
ATOM 46 SD MET A 4 12.199 17.915 -2.458 1.00 53.71 S
ANISOU 46 SD MET A 4 8241 6622 5546 -370 -562 2656 S
ATOM 47 CE MET A 4 12.685 16.548 -3.507 1.00 59.47 C
ANISOU 47 CE MET A 4 8837 7694 6063 -416 -482 2624 C
ATOM 48 N GLY A 5 13.266 14.251 1.685 1.00 54.04 N
ANISOU 48 N GLY A 5 7867 6812 5853 -480 -414 1862 N
ATOM 49 CA GLY A 5 14.061 13.209 2.310 1.00 37.81 C
ANISOU 49 CA GLY A 5 5706 4850 3810 -557 -345 1724 C
ATOM 50 C GLY A 5 13.271 12.407 3.323 1.00 43.81 C
ANISOU 50 C GLY A 5 6395 5620 4629 -463 -372 1543 C
ATOM 51 O GLY A 5 13.583 11.241 3.580 1.00 44.10 O
ANISOU 51 O GLY A 5 6335 5781 4638 -485 -328 1425 O
ATOM 52 N SER A 6 12.240 13.016 3.911 1.00 45.39 N
ANISOU 52 N SER A 6 6643 5693 4911 -354 -445 1521 N
ATOM 53 CA SER A 6 11.370 12.288 4.827 1.00 44.23 C
ANISOU 53 CA SER A 6 6422 5573 4809 -260 -469 1363 C
ATOM 54 C SER A 6 10.582 11.211 4.095 1.00 34.46 C
ANISOU 54 C SER A 6 5105 4525 3464 -192 -482 1318 C
ATOM 55 O SER A 6 10.385 10.111 4.623 1.00 37.29 O
ANISOU 55 O SER A 6 5370 4970 3828 -182 -463 1187 O
ATOM 56 CB SER A 6 10.427 13.261 5.535 1.00 47.75 C
ANISOU 56 CB SER A 6 6933 5857 5355 -148 -543 1356 C
ATOM 57 OG SER A 6 9.469 12.576 6.322 1.00 73.52 O
ANISOU 57 OG SER A 6 10116 9173 8646 -50 -566 1218 O
ATOM 58 N SER A 7 10.132 11.506 2.873 1.00 39.40 N
ANISOU 58 N SER A 7 5767 5216 3989 -147 -518 1428 N
ATOM 59 CA SER A 7 9.336 10.539 2.124 1.00 37.54 C
ANISOU 59 CA SER A 7 5455 5161 3646 -80 -543 1378 C
ATOM 60 C SER A 7 10.149 9.299 1.779 1.00 35.85 C
ANISOU 60 C SER A 7 5162 5102 3358 -166 -475 1308 C
ATOM 61 O SER A 7 9.632 8.177 1.835 1.00 33.68 O
ANISOU 61 O SER A 7 4801 4937 3059 -134 -483 1189 O
ATOM 62 CB SER A 7 8.781 11.191 0.860 1.00 37.05 C
ANISOU 62 CB SER A 7 5454 5143 3481 -12 -598 1518 C
ATOM 63 OG SER A 7 7.973 12.306 1.189 1.00 51.44 O
ANISOU 63 OG SER A 7 7351 6817 5376 87 -669 1576 O
ATOM 64 N VAL A 8 11.420 9.478 1.419 1.00 34.92 N
ANISOU 64 N VAL A 8 5069 4992 3205 -276 -410 1379 N
ATOM 65 CA VAL A 8 12.281 8.332 1.141 1.00 34.21 C
ANISOU 65 CA VAL A 8 4904 5048 3046 -347 -343 1304 C
ATOM 66 C VAL A 8 12.465 7.494 2.400 1.00 37.90 C
ANISOU 66 C VAL A 8 5304 5482 3614 -366 -316 1150 C
ATOM 67 O VAL A 8 12.283 6.271 2.388 1.00 32.62 O
ANISOU 67 O VAL A 8 4559 4921 2915 -349 -310 1035 O
ATOM 68 CB VAL A 8 13.630 8.800 0.568 1.00 35.10 C
ANISOU 68 CB VAL A 8 5048 5184 3105 -461 -274 1418 C
ATOM 69 CG1 VAL A 8 14.625 7.651 0.535 1.00 34.31 C
ANISOU 69 CG1 VAL A 8 4862 5218 2956 -527 -201 1321 C
ATOM 70 CG2 VAL A 8 13.435 9.380 -0.825 1.00 36.78 C
ANISOU 70 CG2 VAL A 8 5315 5476 3185 -440 -293 1572 C
ATOM 71 N TYR A 9 12.817 8.145 3.511 1.00 34.77 N
ANISOU 71 N TYR A 9 4939 4933 3340 -399 -305 1146 N
ATOM 72 CA TYR A 9 13.029 7.420 4.759 1.00 34.97 C
ANISOU 72 CA TYR A 9 4905 4930 3453 -412 -280 1012 C
ATOM 73 C TYR A 9 11.763 6.701 5.208 1.00 35.32 C
ANISOU 73 C TYR A 9 4897 5001 3523 -317 -326 910 C
ATOM 74 O TYR A 9 11.820 5.546 5.645 1.00 29.04 O
ANISOU 74 O TYR A 9 4030 4268 2736 -325 -303 800 O
ATOM 75 CB TYR A 9 13.524 8.379 5.843 1.00 30.84 C
ANISOU 75 CB TYR A 9 4430 4241 3049 -452 -273 1026 C
ATOM 76 CG TYR A 9 13.445 7.817 7.243 1.00 29.56 C
ANISOU 76 CG TYR A 9 4217 4039 2977 -435 -264 895 C
ATOM 77 CD1 TYR A 9 14.293 6.797 7.653 1.00 36.50 C
ANISOU 77 CD1 TYR A 9 5027 4990 3850 -490 -209 811 C
ATOM 78 CD2 TYR A 9 12.525 8.312 8.157 1.00 41.78 C
ANISOU 78 CD2 TYR A 9 5784 5484 4608 -355 -312 857 C
ATOM 79 CE1 TYR A 9 14.222 6.282 8.932 1.00 35.92 C
ANISOU 79 CE1 TYR A 9 4911 4885 3850 -471 -201 705 C
ATOM 80 CE2 TYR A 9 12.447 7.805 9.438 1.00 32.65 C
ANISOU 80 CE2 TYR A 9 4578 4308 3520 -338 -300 746 C
ATOM 81 CZ TYR A 9 13.298 6.791 9.821 1.00 31.36 C
ANISOU 81 CZ TYR A 9 4353 4215 3348 -398 -244 676 C
ATOM 82 OH TYR A 9 13.222 6.285 11.098 1.00 41.17 O
ANISOU 82 OH TYR A 9 5550 5442 4650 -377 -233 578 O
ATOM 83 N ILE A 10 10.608 7.363 5.098 1.00 30.67 N
ANISOU 83 N ILE A 10 4340 4366 2947 -227 -392 948 N
ATOM 84 CA ILE A 10 9.351 6.733 5.496 1.00 31.17 C
ANISOU 84 CA ILE A 10 4340 4471 3033 -141 -436 857 C
ATOM 85 C ILE A 10 9.046 5.536 4.604 1.00 30.00 C
ANISOU 85 C ILE A 10 4125 4484 2791 -140 -442 806 C
ATOM 86 O ILE A 10 8.626 4.476 5.084 1.00 35.81 O
ANISOU 86 O ILE A 10 4786 5267 3552 -134 -440 698 O
ATOM 87 CB ILE A 10 8.209 7.767 5.479 1.00 35.51 C
ANISOU 87 CB ILE A 10 4932 4952 3607 -35 -509 913 C
ATOM 88 CG1 ILE A 10 8.385 8.764 6.626 1.00 32.65 C
ANISOU 88 CG1 ILE A 10 4625 4423 3358 -23 -509 917 C
ATOM 89 CG2 ILE A 10 6.853 7.082 5.569 1.00 30.81 C
ANISOU 89 CG2 ILE A 10 4253 4446 3006 51 -557 833 C
ATOM 90 CD1 ILE A 10 7.313 9.823 6.688 1.00 50.34 C
ANISOU 90 CD1 ILE A 10 6913 6582 5631 97 -582 961 C
ATOM 91 N THR A 11 9.265 5.680 3.296 1.00 36.41 N
ANISOU 91 N THR A 11 4964 5379 3490 -147 -450 883 N
ATOM 92 CA THR A 11 8.971 4.590 2.372 1.00 33.32 C
ANISOU 92 CA THR A 11 4515 5146 3000 -138 -465 824 C
ATOM 93 C THR A 11 9.888 3.394 2.611 1.00 30.12 C
ANISOU 93 C THR A 11 4059 4791 2593 -210 -403 724 C
ATOM 94 O THR A 11 9.441 2.242 2.563 1.00 29.70 O
ANISOU 94 O THR A 11 3942 4810 2532 -199 -420 617 O
ATOM 95 CB THR A 11 9.090 5.085 0.930 1.00 32.41 C
ANISOU 95 CB THR A 11 4444 5121 2749 -124 -483 933 C
ATOM 96 OG1 THR A 11 8.273 6.249 0.761 1.00 34.73 O
ANISOU 96 OG1 THR A 11 4795 5350 3051 -48 -544 1035 O
ATOM 97 CG2 THR A 11 8.635 4.015 -0.048 1.00 32.69 C
ANISOU 97 CG2 THR A 11 4419 5326 2676 -98 -514 857 C
ATOM 98 N VAL A 12 11.170 3.647 2.877 1.00 29.92 N
ANISOU 98 N VAL A 12 4061 4724 2581 -283 -337 757 N
ATOM 99 CA VAL A 12 12.101 2.552 3.131 1.00 29.15 C
ANISOU 99 CA VAL A 12 3916 4676 2483 -337 -281 664 C
ATOM 100 C VAL A 12 11.744 1.835 4.429 1.00 27.96 C
ANISOU 100 C VAL A 12 3721 4458 2445 -329 -280 558 C
ATOM 101 O VAL A 12 11.825 0.604 4.516 1.00 27.82 O
ANISOU 101 O VAL A 12 3653 4491 2426 -337 -270 457 O
ATOM 102 CB VAL A 12 13.548 3.080 3.140 1.00 30.39 C
ANISOU 102 CB VAL A 12 4100 4816 2628 -416 -212 729 C
ATOM 103 CG1 VAL A 12 14.518 1.997 3.583 1.00 28.57 C
ANISOU 103 CG1 VAL A 12 3816 4629 2411 -457 -156 628 C
ATOM 104 CG2 VAL A 12 13.926 3.597 1.760 1.00 30.68 C
ANISOU 104 CG2 VAL A 12 4171 4952 2536 -432 -202 837 C
ATOM 105 N GLU A 13 11.323 2.586 5.450 1.00 30.22 N
ANISOU 105 N GLU A 13 4028 4628 2828 -310 -293 580 N
ATOM 106 CA GLU A 13 10.928 1.970 6.714 1.00 26.67 C
ANISOU 106 CA GLU A 13 3532 4126 2473 -298 -290 492 C
ATOM 107 C GLU A 13 9.703 1.082 6.542 1.00 33.81 C
ANISOU 107 C GLU A 13 4380 5094 3374 -254 -336 424 C
ATOM 108 O GLU A 13 9.640 -0.017 7.105 1.00 32.49 O
ANISOU 108 O GLU A 13 4163 4936 3246 -271 -322 339 O
ATOM 109 CB GLU A 13 10.654 3.047 7.761 1.00 29.21 C
ANISOU 109 CB GLU A 13 3888 4329 2882 -272 -299 526 C
ATOM 110 CG GLU A 13 11.894 3.757 8.250 1.00 39.11 C
ANISOU 110 CG GLU A 13 5186 5506 4169 -331 -254 564 C
ATOM 111 CD GLU A 13 12.567 3.030 9.394 1.00 47.95 C
ANISOU 111 CD GLU A 13 6265 6608 5345 -364 -210 482 C
ATOM 112 OE1 GLU A 13 12.573 3.579 10.516 1.00 35.78 O
ANISOU 112 OE1 GLU A 13 4736 4981 3879 -353 -208 468 O
ATOM 113 OE2 GLU A 13 13.080 1.910 9.175 1.00 27.54 O
ANISOU 113 OE2 GLU A 13 3639 4098 2727 -393 -180 429 O
ATOM 114 N LEU A 14 8.713 1.545 5.777 1.00 27.41 N
ANISOU 114 N LEU A 14 3573 4323 2518 -200 -395 464 N
ATOM 115 CA LEU A 14 7.521 0.733 5.563 1.00 29.26 C
ANISOU 115 CA LEU A 14 3740 4627 2749 -167 -446 397 C
ATOM 116 C LEU A 14 7.851 -0.529 4.775 1.00 27.58 C
ANISOU 116 C LEU A 14 3496 4507 2474 -205 -443 322 C
ATOM 117 O LEU A 14 7.290 -1.597 5.042 1.00 29.10 O
ANISOU 117 O LEU A 14 3630 4721 2704 -217 -460 234 O
ATOM 118 CB LEU A 14 6.443 1.557 4.859 1.00 28.53 C
ANISOU 118 CB LEU A 14 3655 4572 2613 -92 -515 457 C
ATOM 119 CG LEU A 14 5.889 2.730 5.673 1.00 34.79 C
ANISOU 119 CG LEU A 14 4473 5271 3475 -31 -532 511 C
ATOM 120 CD1 LEU A 14 4.814 3.472 4.895 1.00 39.88 C
ANISOU 120 CD1 LEU A 14 5122 5960 4069 59 -607 568 C
ATOM 121 CD2 LEU A 14 5.353 2.254 7.017 1.00 27.88 C
ANISOU 121 CD2 LEU A 14 3534 4360 2698 -26 -517 437 C
ATOM 122 N ALA A 15 8.766 -0.429 3.809 1.00 28.03 N
ANISOU 122 N ALA A 15 3592 4620 2438 -225 -422 354 N
ATOM 123 CA ALA A 15 9.193 -1.613 3.072 1.00 30.41 C
ANISOU 123 CA ALA A 15 3868 5011 2675 -250 -417 269 C
ATOM 124 C ALA A 15 9.858 -2.625 3.996 1.00 31.55 C
ANISOU 124 C ALA A 15 3990 5101 2896 -293 -370 185 C
ATOM 125 O ALA A 15 9.612 -3.832 3.889 1.00 29.79 O
ANISOU 125 O ALA A 15 3730 4904 2683 -302 -389 85 O
ATOM 126 CB ALA A 15 10.141 -1.214 1.940 1.00 28.93 C
ANISOU 126 CB ALA A 15 3722 4907 2364 -258 -391 328 C
ATOM 127 N ILE A 16 10.700 -2.149 4.915 1.00 26.60 N
ANISOU 127 N ILE A 16 3387 4393 2326 -318 -313 224 N
ATOM 128 CA ILE A 16 11.358 -3.044 5.861 1.00 29.48 C
ANISOU 128 CA ILE A 16 3733 4709 2760 -348 -271 155 C
ATOM 129 C ILE A 16 10.338 -3.675 6.802 1.00 25.32 C
ANISOU 129 C ILE A 16 3165 4128 2328 -342 -296 104 C
ATOM 130 O ILE A 16 10.428 -4.864 7.129 1.00 33.39 O
ANISOU 130 O ILE A 16 4162 5137 3387 -361 -290 27 O
ATOM 131 CB ILE A 16 12.451 -2.282 6.632 1.00 30.06 C
ANISOU 131 CB ILE A 16 3835 4720 2866 -375 -213 209 C
ATOM 132 CG1 ILE A 16 13.568 -1.849 5.681 1.00 29.10 C
ANISOU 132 CG1 ILE A 16 3739 4668 2651 -399 -178 256 C
ATOM 133 CG2 ILE A 16 13.017 -3.132 7.760 1.00 24.53 C
ANISOU 133 CG2 ILE A 16 3112 3968 2239 -392 -176 145 C
ATOM 134 CD1 ILE A 16 14.607 -0.980 6.335 1.00 25.72 C
ANISOU 134 CD1 ILE A 16 3333 4184 2255 -440 -128 316 C
ATOM 135 N ALA A 17 9.351 -2.895 7.248 1.00 28.16 N
ANISOU 135 N ALA A 17 3516 4456 2727 -314 -324 150 N
ATOM 136 CA ALA A 17 8.355 -3.425 8.173 1.00 26.26 C
ANISOU 136 CA ALA A 17 3224 4183 2569 -311 -340 113 C
ATOM 137 C ALA A 17 7.541 -4.542 7.532 1.00 25.54 C
ANISOU 137 C ALA A 17 3085 4149 2468 -325 -388 40 C
ATOM 138 O ALA A 17 7.274 -5.566 8.169 1.00 29.39 O
ANISOU 138 O ALA A 17 3537 4608 3023 -357 -383 -14 O
ATOM 139 CB ALA A 17 7.440 -2.303 8.663 1.00 25.19 C
ANISOU 139 CB ALA A 17 3082 4025 2464 -263 -362 171 C
ATOM 140 N VAL A 18 7.146 -4.371 6.268 1.00 26.34 N
ANISOU 140 N VAL A 18 3186 4333 2488 -304 -437 39 N
ATOM 141 CA VAL A 18 6.384 -5.415 5.587 1.00 26.97 C
ANISOU 141 CA VAL A 18 3219 4472 2555 -320 -493 -44 C
ATOM 142 C VAL A 18 7.218 -6.684 5.455 1.00 30.42 C
ANISOU 142 C VAL A 18 3669 4892 2997 -360 -473 -131 C
ATOM 143 O VAL A 18 6.735 -7.792 5.721 1.00 27.00 O
ANISOU 143 O VAL A 18 3200 4432 2626 -398 -496 -204 O
ATOM 144 CB VAL A 18 5.888 -4.913 4.217 1.00 27.96 C
ANISOU 144 CB VAL A 18 3346 4704 2573 -279 -554 -29 C
ATOM 145 CG1 VAL A 18 5.191 -6.032 3.461 1.00 28.90 C
ANISOU 145 CG1 VAL A 18 3416 4892 2674 -300 -619 -134 C
ATOM 146 CG2 VAL A 18 4.947 -3.736 4.397 1.00 28.21 C
ANISOU 146 CG2 VAL A 18 3364 4746 2611 -226 -584 51 C
ATOM 147 N LEU A 19 8.486 -6.545 5.062 1.00 26.72 N
ANISOU 147 N LEU A 19 3251 4436 2467 -354 -431 -122 N
ATOM 148 CA LEU A 19 9.339 -7.719 4.912 1.00 30.24 C
ANISOU 148 CA LEU A 19 3709 4871 2911 -373 -413 -210 C
ATOM 149 C LEU A 19 9.645 -8.373 6.254 1.00 27.30 C
ANISOU 149 C LEU A 19 3333 4390 2650 -401 -373 -225 C
ATOM 150 O LEU A 19 9.781 -9.600 6.325 1.00 30.98 O
ANISOU 150 O LEU A 19 3798 4819 3156 -419 -383 -308 O
ATOM 151 CB LEU A 19 10.633 -7.340 4.192 1.00 26.90 C
ANISOU 151 CB LEU A 19 3324 4508 2387 -353 -371 -192 C
ATOM 152 CG LEU A 19 10.465 -6.781 2.776 1.00 28.29 C
ANISOU 152 CG LEU A 19 3508 4808 2431 -323 -404 -170 C
ATOM 153 CD1 LEU A 19 11.788 -6.267 2.224 1.00 28.03 C
ANISOU 153 CD1 LEU A 19 3508 4840 2303 -316 -346 -125 C
ATOM 154 CD2 LEU A 19 9.862 -7.825 1.845 1.00 28.73 C
ANISOU 154 CD2 LEU A 19 3541 4930 2445 -314 -472 -286 C
ATOM 155 N ALA A 20 9.748 -7.584 7.326 1.00 25.25 N
ANISOU 155 N ALA A 20 3076 4076 2440 -400 -332 -147 N
ATOM 156 CA ALA A 20 10.028 -8.164 8.636 1.00 30.78 C
ANISOU 156 CA ALA A 20 3772 4689 3233 -419 -294 -153 C
ATOM 157 C ALA A 20 8.828 -8.936 9.168 1.00 33.08 C
ANISOU 157 C ALA A 20 4019 4944 3607 -450 -326 -179 C
ATOM 158 O ALA A 20 8.989 -9.973 9.823 1.00 28.08 O
ANISOU 158 O ALA A 20 3386 4244 3039 -477 -314 -212 O
ATOM 159 CB ALA A 20 10.439 -7.071 9.622 1.00 26.63 C
ANISOU 159 CB ALA A 20 3260 4130 2729 -406 -247 -73 C
ATOM 160 N ILE A 21 7.619 -8.447 8.900 1.00 26.66 N
ANISOU 160 N ILE A 21 3165 4175 2791 -448 -368 -158 N
ATOM 161 CA ILE A 21 6.420 -9.144 9.350 1.00 26.60 C
ANISOU 161 CA ILE A 21 3097 4152 2858 -488 -398 -179 C
ATOM 162 C ILE A 21 6.221 -10.431 8.558 1.00 27.75 C
ANISOU 162 C ILE A 21 3237 4295 3013 -530 -448 -274 C
ATOM 163 O ILE A 21 5.991 -11.501 9.131 1.00 29.50 O
ANISOU 163 O ILE A 21 3444 4448 3317 -582 -449 -305 O
ATOM 164 CB ILE A 21 5.196 -8.218 9.246 1.00 25.89 C
ANISOU 164 CB ILE A 21 2953 4128 2756 -464 -433 -136 C
ATOM 165 CG1 ILE A 21 5.351 -7.034 10.200 1.00 25.24 C
ANISOU 165 CG1 ILE A 21 2881 4025 2682 -419 -387 -55 C
ATOM 166 CG2 ILE A 21 3.920 -8.983 9.556 1.00 30.66 C
ANISOU 166 CG2 ILE A 21 3476 4743 3430 -516 -467 -163 C
ATOM 167 CD1 ILE A 21 4.358 -5.928 9.957 1.00 26.73 C
ANISOU 167 CD1 ILE A 21 3036 4275 2845 -368 -423 -13 C
ATOM 168 N LEU A 22 6.314 -10.349 7.230 1.00 27.01 N
ANISOU 168 N LEU A 22 3157 4274 2833 -508 -492 -322 N
ATOM 169 CA LEU A 22 6.051 -11.518 6.394 1.00 33.24 C
ANISOU 169 CA LEU A 22 3939 5068 3622 -541 -552 -431 C
ATOM 170 C LEU A 22 7.053 -12.634 6.667 1.00 29.76 C
ANISOU 170 C LEU A 22 3550 4536 3223 -555 -527 -492 C
ATOM 171 O LEU A 22 6.673 -13.800 6.824 1.00 28.38 O
ANISOU 171 O LEU A 22 3367 4289 3127 -607 -559 -557 O
ATOM 172 CB LEU A 22 6.075 -11.121 4.918 1.00 35.03 C
ANISOU 172 CB LEU A 22 4174 5410 3725 -499 -600 -470 C
ATOM 173 CG LEU A 22 4.902 -10.279 4.416 1.00 35.74 C
ANISOU 173 CG LEU A 22 4210 5596 3772 -481 -652 -433 C
ATOM 174 CD1 LEU A 22 5.177 -9.771 3.011 1.00 29.67 C
ANISOU 174 CD1 LEU A 22 3466 4944 2862 -426 -686 -447 C
ATOM 175 CD2 LEU A 22 3.614 -11.086 4.454 1.00 29.84 C
ANISOU 175 CD2 LEU A 22 3389 4850 3099 -541 -718 -496 C
ATOM 176 N GLY A 23 8.341 -12.296 6.733 1.00 32.88 N
ANISOU 176 N GLY A 23 3995 4930 3569 -508 -471 -470 N
ATOM 177 CA GLY A 23 9.354 -13.324 6.896 1.00 27.25 C
ANISOU 177 CA GLY A 23 3328 4145 2882 -500 -452 -534 C
ATOM 178 C GLY A 23 9.274 -14.034 8.234 1.00 34.01 C
ANISOU 178 C GLY A 23 4187 4878 3859 -538 -426 -506 C
ATOM 179 O GLY A 23 9.393 -15.260 8.304 1.00 30.81 O
ANISOU 179 O GLY A 23 3806 4386 3514 -558 -449 -575 O
ATOM 180 N ASN A 24 9.069 -13.279 9.313 1.00 29.29 N
ANISOU 180 N ASN A 24 3567 4269 3294 -544 -380 -405 N
ATOM 181 CA ASN A 24 9.074 -13.873 10.642 1.00 25.89 C
ANISOU 181 CA ASN A 24 3138 3739 2959 -572 -346 -363 C
ATOM 182 C ASN A 24 7.752 -14.531 11.006 1.00 31.79 C
ANISOU 182 C ASN A 24 3839 4445 3796 -647 -381 -359 C
ATOM 183 O ASN A 24 7.739 -15.428 11.857 1.00 26.75 O
ANISOU 183 O ASN A 24 3212 3710 3241 -684 -366 -342 O
ATOM 184 CB ASN A 24 9.440 -12.820 11.683 1.00 24.91 C
ANISOU 184 CB ASN A 24 3008 3631 2826 -543 -284 -267 C
ATOM 185 CG ASN A 24 10.890 -12.421 11.601 1.00 25.22 C
ANISOU 185 CG ASN A 24 3091 3689 2804 -488 -244 -270 C
ATOM 186 OD1 ASN A 24 11.767 -13.137 12.086 1.00 24.34 O
ANISOU 186 OD1 ASN A 24 3011 3521 2718 -470 -221 -287 O
ATOM 187 ND2 ASN A 24 11.158 -11.283 10.970 1.00 26.72 N
ANISOU 187 ND2 ASN A 24 3280 3959 2915 -461 -237 -248 N
ATOM 188 N VAL A 25 6.644 -14.110 10.395 1.00 26.95 N
ANISOU 188 N VAL A 25 3170 3906 3165 -672 -425 -367 N
ATOM 189 CA VAL A 25 5.411 -14.878 10.527 1.00 27.85 C
ANISOU 189 CA VAL A 25 3227 3991 3362 -756 -468 -383 C
ATOM 190 C VAL A 25 5.576 -16.239 9.863 1.00 28.84 C
ANISOU 190 C VAL A 25 3393 4037 3530 -796 -522 -490 C
ATOM 191 O VAL A 25 5.085 -17.258 10.365 1.00 33.15 O
ANISOU 191 O VAL A 25 3929 4487 4178 -874 -537 -494 O
ATOM 192 CB VAL A 25 4.220 -14.093 9.945 1.00 30.02 C
ANISOU 192 CB VAL A 25 3424 4382 3599 -763 -510 -377 C
ATOM 193 CG1 VAL A 25 3.039 -15.013 9.695 1.00 29.42 C
ANISOU 193 CG1 VAL A 25 3285 4295 3597 -856 -573 -428 C
ATOM 194 CG2 VAL A 25 3.816 -12.974 10.892 1.00 28.29 C
ANISOU 194 CG2 VAL A 25 3160 4213 3375 -733 -460 -273 C
ATOM 195 N LEU A 26 6.295 -16.280 8.738 1.00 30.38 N
ANISOU 195 N LEU A 26 3633 4265 3645 -743 -552 -577 N
ATOM 196 CA LEU A 26 6.582 -17.549 8.079 1.00 30.05 C
ANISOU 196 CA LEU A 26 3638 4145 3635 -760 -606 -697 C
ATOM 197 C LEU A 26 7.443 -18.450 8.954 1.00 31.90 C
ANISOU 197 C LEU A 26 3939 4237 3946 -754 -569 -687 C
ATOM 198 O LEU A 26 7.300 -19.677 8.906 1.00 33.80 O
ANISOU 198 O LEU A 26 4211 4360 4272 -800 -614 -754 O
ATOM 199 CB LEU A 26 7.265 -17.295 6.735 1.00 30.26 C
ANISOU 199 CB LEU A 26 3696 4264 3538 -684 -634 -789 C
ATOM 200 CG LEU A 26 7.579 -18.508 5.856 1.00 39.64 C
ANISOU 200 CG LEU A 26 4931 5397 4732 -679 -698 -940 C
ATOM 201 CD1 LEU A 26 6.302 -19.205 5.411 1.00 45.07 C
ANISOU 201 CD1 LEU A 26 5577 6060 5486 -768 -788 -1016 C
ATOM 202 CD2 LEU A 26 8.410 -18.089 4.655 1.00 45.71 C
ANISOU 202 CD2 LEU A 26 5725 6289 5353 -587 -704 -1011 C
ATOM 203 N VAL A 27 8.334 -17.867 9.757 1.00 28.89 N
ANISOU 203 N VAL A 27 3579 3860 3537 -697 -494 -604 N
ATOM 204 CA VAL A 27 9.118 -18.662 10.697 1.00 28.84 C
ANISOU 204 CA VAL A 27 3629 3732 3598 -682 -460 -580 C
ATOM 205 C VAL A 27 8.213 -19.265 11.765 1.00 39.28 C
ANISOU 205 C VAL A 27 4928 4957 5039 -773 -455 -504 C
ATOM 206 O VAL A 27 8.283 -20.464 12.055 1.00 37.31 O
ANISOU 206 O VAL A 27 4726 4569 4880 -806 -477 -527 O
ATOM 207 CB VAL A 27 10.237 -17.808 11.322 1.00 38.94 C
ANISOU 207 CB VAL A 27 4924 5060 4814 -603 -385 -511 C
ATOM 208 CG1 VAL A 27 10.977 -18.603 12.388 1.00 27.67 C
ANISOU 208 CG1 VAL A 27 3545 3517 3451 -582 -353 -475 C
ATOM 209 CG2 VAL A 27 11.200 -17.317 10.250 1.00 27.47 C
ANISOU 209 CG2 VAL A 27 3489 3702 3246 -526 -385 -579 C
ATOM 210 N CYS A 28 7.347 -18.441 12.365 1.00 28.77 N
ANISOU 210 N CYS A 28 3525 3699 3708 -811 -425 -411 N
ATOM 211 CA CYS A 28 6.452 -18.937 13.409 1.00 39.12 C
ANISOU 211 CA CYS A 28 4799 4948 5118 -899 -410 -328 C
ATOM 212 C CYS A 28 5.466 -19.959 12.855 1.00 43.33 C
ANISOU 212 C CYS A 28 5310 5414 5738 -1005 -482 -391 C
ATOM 213 O CYS A 28 5.156 -20.955 13.519 1.00 44.74 O
ANISOU 213 O CYS A 28 5504 5473 6022 -1082 -483 -353 O
ATOM 214 CB CYS A 28 5.705 -17.773 14.063 1.00 29.81 C
ANISOU 214 CB CYS A 28 3535 3885 3906 -903 -365 -232 C
ATOM 215 SG CYS A 28 6.741 -16.665 15.057 1.00 33.35 S
ANISOU 215 SG CYS A 28 4006 4385 4281 -801 -281 -148 S
ATOM 216 N TRP A 29 4.960 -19.724 11.642 1.00 38.24 N
ANISOU 216 N TRP A 29 4633 4847 5051 -1013 -545 -485 N
ATOM 217 CA TRP A 29 4.079 -20.692 10.998 1.00 32.61 C
ANISOU 217 CA TRP A 29 3899 4077 4416 -1114 -627 -569 C
ATOM 218 C TRP A 29 4.793 -22.016 10.757 1.00 38.09 C
ANISOU 218 C TRP A 29 4693 4602 5177 -1117 -666 -656 C
ATOM 219 O TRP A 29 4.184 -23.082 10.892 1.00 34.90 O
ANISOU 219 O TRP A 29 4293 4075 4890 -1222 -711 -675 O
ATOM 220 CB TRP A 29 3.545 -20.116 9.685 1.00 33.12 C
ANISOU 220 CB TRP A 29 3912 4275 4397 -1098 -691 -662 C
ATOM 221 CG TRP A 29 2.330 -20.811 9.136 1.00 61.33 C
ANISOU 221 CG TRP A 29 7422 7838 8042 -1214 -776 -734 C
ATOM 222 CD1 TRP A 29 1.699 -21.899 9.661 1.00 71.19 C
ANISOU 222 CD1 TRP A 29 8659 8960 9430 -1340 -798 -724 C
ATOM 223 CD2 TRP A 29 1.598 -20.457 7.951 1.00 68.34 C
ANISOU 223 CD2 TRP A 29 8247 8852 8867 -1218 -853 -826 C
ATOM 224 NE1 TRP A 29 0.625 -22.249 8.880 1.00 72.73 N
ANISOU 224 NE1 TRP A 29 8783 9194 9659 -1431 -886 -811 N
ATOM 225 CE2 TRP A 29 0.540 -21.380 7.824 1.00 57.00 C
ANISOU 225 CE2 TRP A 29 6756 7361 7539 -1353 -923 -878 C
ATOM 226 CE3 TRP A 29 1.735 -19.452 6.989 1.00 72.89 C
ANISOU 226 CE3 TRP A 29 8809 9583 9304 -1124 -871 -862 C
ATOM 227 CZ2 TRP A 29 -0.375 -21.328 6.774 1.00 60.63 C
ANISOU 227 CZ2 TRP A 29 7140 7926 7969 -1390 -1014 -978 C
ATOM 228 CZ3 TRP A 29 0.825 -19.402 5.946 1.00 64.32 C
ANISOU 228 CZ3 TRP A 29 7656 8602 8183 -1153 -959 -951 C
ATOM 229 CH2 TRP A 29 -0.217 -20.335 5.848 1.00 56.16 C
ANISOU 229 CH2 TRP A 29 6562 7520 7256 -1282 -1032 -1014 C
ATOM 230 N ALA A 30 6.085 -21.972 10.422 1.00 48.23 N
ANISOU 230 N ALA A 30 6057 5876 6392 -1002 -652 -707 N
ATOM 231 CA ALA A 30 6.819 -23.210 10.176 1.00 36.82 C
ANISOU 231 CA ALA A 30 4711 4275 5006 -981 -692 -800 C
ATOM 232 C ALA A 30 7.004 -24.012 11.459 1.00 42.42 C
ANISOU 232 C ALA A 30 5468 4820 5828 -1018 -655 -700 C
ATOM 233 O ALA A 30 6.822 -25.236 11.463 1.00 44.08 O
ANISOU 233 O ALA A 30 5732 4862 6152 -1079 -708 -744 O
ATOM 234 CB ALA A 30 8.171 -22.903 9.535 1.00 33.34 C
ANISOU 234 CB ALA A 30 4327 3891 4451 -839 -677 -875 C
ATOM 235 N VAL A 31 7.360 -23.342 12.559 1.00 33.09 N
ANISOU 235 N VAL A 31 4272 3684 4619 -982 -570 -564 N
ATOM 236 CA VAL A 31 7.552 -24.042 13.827 1.00 39.21 C
ANISOU 236 CA VAL A 31 5090 4325 5483 -1007 -530 -453 C
ATOM 237 C VAL A 31 6.245 -24.665 14.297 1.00 41.53 C
ANISOU 237 C VAL A 31 5339 4544 5896 -1163 -549 -388 C
ATOM 238 O VAL A 31 6.224 -25.793 14.804 1.00 36.27 O
ANISOU 238 O VAL A 31 4734 3704 5343 -1220 -565 -354 O
ATOM 239 CB VAL A 31 8.135 -23.087 14.885 1.00 32.48 C
ANISOU 239 CB VAL A 31 4217 3565 4558 -934 -438 -330 C
ATOM 240 CG1 VAL A 31 8.170 -23.761 16.249 1.00 35.38 C
ANISOU 240 CG1 VAL A 31 4618 3819 5007 -966 -397 -200 C
ATOM 241 CG2 VAL A 31 9.526 -22.635 14.478 1.00 31.05 C
ANISOU 241 CG2 VAL A 31 4083 3439 4277 -794 -422 -392 C
ATOM 242 N TRP A 32 5.134 -23.944 14.136 1.00 40.27 N
ANISOU 242 N TRP A 32 5069 4515 5715 -1235 -548 -365 N
ATOM 243 CA TRP A 32 3.836 -24.491 14.511 1.00 46.55 C
ANISOU 243 CA TRP A 32 5799 5269 6620 -1392 -564 -307 C
ATOM 244 C TRP A 32 3.476 -25.711 13.673 1.00 47.61 C
ANISOU 244 C TRP A 32 5975 5255 6859 -1483 -663 -427 C
ATOM 245 O TRP A 32 2.773 -26.609 14.153 1.00 38.91 O
ANISOU 245 O TRP A 32 4867 4032 5886 -1618 -679 -372 O
ATOM 246 CB TRP A 32 2.759 -23.414 14.363 1.00 38.64 C
ANISOU 246 CB TRP A 32 4661 4461 5560 -1428 -552 -281 C
ATOM 247 CG TRP A 32 1.348 -23.890 14.597 1.00 43.63 C
ANISOU 247 CG TRP A 32 5197 5089 6292 -1593 -573 -238 C
ATOM 248 CD1 TRP A 32 0.545 -24.555 13.714 1.00 38.07 C
ANISOU 248 CD1 TRP A 32 4459 4346 5659 -1702 -663 -340 C
ATOM 249 CD2 TRP A 32 0.566 -23.703 15.784 1.00 51.14 C
ANISOU 249 CD2 TRP A 32 6060 6096 7276 -1669 -503 -84 C
ATOM 250 NE1 TRP A 32 -0.679 -24.807 14.282 1.00 52.03 N
ANISOU 250 NE1 TRP A 32 6120 6138 7511 -1850 -653 -255 N
ATOM 251 CE2 TRP A 32 -0.694 -24.292 15.551 1.00 48.86 C
ANISOU 251 CE2 TRP A 32 5681 5799 7082 -1830 -551 -94 C
ATOM 252 CE3 TRP A 32 0.810 -23.099 17.021 1.00 63.62 C
ANISOU 252 CE3 TRP A 32 7624 7741 8808 -1614 -405 56 C
ATOM 253 CZ2 TRP A 32 -1.705 -24.297 16.511 1.00 57.16 C
ANISOU 253 CZ2 TRP A 32 6623 6915 8182 -1941 -496 39 C
ATOM 254 CZ3 TRP A 32 -0.197 -23.104 17.971 1.00 62.31 C
ANISOU 254 CZ3 TRP A 32 7355 7639 8681 -1714 -352 182 C
ATOM 255 CH2 TRP A 32 -1.438 -23.699 17.711 1.00 71.67 C
ANISOU 255 CH2 TRP A 32 8448 8824 9961 -1876 -394 177 C
ATOM 256 N LEU A 33 3.954 -25.772 12.430 1.00 43.36 N
ANISOU 256 N LEU A 33 5480 4724 6270 -1413 -731 -590 N
ATOM 257 CA LEU A 33 3.445 -26.772 11.501 1.00 39.32 C
ANISOU 257 CA LEU A 33 4990 4106 5845 -1500 -837 -729 C
ATOM 258 C LEU A 33 4.212 -28.085 11.606 1.00 40.51 C
ANISOU 258 C LEU A 33 5278 4018 6096 -1486 -874 -778 C
ATOM 259 O LEU A 33 3.611 -29.165 11.561 1.00 42.33 O
ANISOU 259 O LEU A 33 5534 4084 6465 -1611 -939 -810 O
ATOM 260 CB LEU A 33 3.509 -26.225 10.072 1.00 57.02 C
ANISOU 260 CB LEU A 33 7208 6485 7972 -1429 -898 -890 C
ATOM 261 CG LEU A 33 2.336 -26.531 9.136 1.00 62.99 C
ANISOU 261 CG LEU A 33 7892 7273 8768 -1543 -997 -1002 C
ATOM 262 CD1 LEU A 33 1.073 -25.813 9.594 1.00 48.19 C
ANISOU 262 CD1 LEU A 33 5872 5538 6899 -1643 -967 -893 C
ATOM 263 CD2 LEU A 33 2.695 -26.142 7.714 1.00 52.92 C
ANISOU 263 CD2 LEU A 33 6625 6116 7365 -1441 -1058 -1168 C
ATOM 264 N ASN A 34 5.531 -28.012 11.745 1.00 39.64 N
ANISOU 264 N ASN A 34 5256 3884 5921 -1334 -838 -786 N
ATOM 265 CA ASN A 34 6.402 -29.174 11.639 1.00 48.20 C
ANISOU 265 CA ASN A 34 6476 4763 7077 -1277 -884 -865 C
ATOM 266 C ASN A 34 6.892 -29.579 13.023 1.00 51.27 C
ANISOU 266 C ASN A 34 6925 5026 7530 -1265 -818 -701 C
ATOM 267 O ASN A 34 7.533 -28.783 13.718 1.00 39.15 O
ANISOU 267 O ASN A 34 5373 3600 5904 -1172 -732 -600 O
ATOM 268 CB ASN A 34 7.577 -28.876 10.710 1.00 43.67 C
ANISOU 268 CB ASN A 34 5950 4267 6376 -1103 -898 -1007 C
ATOM 269 CG ASN A 34 8.543 -30.025 10.619 1.00 41.28 C
ANISOU 269 CG ASN A 34 5781 3767 6135 -1016 -942 -1095 C
ATOM 270 OD1 ASN A 34 9.746 -29.826 10.498 1.00 53.96 O
ANISOU 270 OD1 ASN A 34 7432 5418 7652 -859 -913 -1134 O
ATOM 271 ND2 ASN A 34 8.021 -31.243 10.685 1.00 52.23 N
ANISOU 271 ND2 ASN A 34 7232 4932 7681 -1118 -1014 -1127 N
ATOM 272 N SER A 35 6.598 -30.823 13.413 1.00 48.41 N
ANISOU 272 N SER A 35 6636 4433 7324 -1358 -861 -675 N
ATOM 273 CA SER A 35 7.003 -31.298 14.731 1.00 44.83 C
ANISOU 273 CA SER A 35 6248 3851 6934 -1351 -804 -506 C
ATOM 274 C SER A 35 8.519 -31.405 14.850 1.00 48.31 C
ANISOU 274 C SER A 35 6789 4255 7311 -1155 -787 -538 C
ATOM 275 O SER A 35 9.062 -31.302 15.957 1.00 43.36 O
ANISOU 275 O SER A 35 6186 3621 6667 -1099 -717 -393 O
ATOM 276 CB SER A 35 6.350 -32.648 15.026 1.00 48.50 C
ANISOU 276 CB SER A 35 6780 4060 7588 -1501 -862 -470 C
ATOM 277 OG SER A 35 6.830 -33.647 14.144 1.00 66.30 O
ANISOU 277 OG SER A 35 9151 6129 9912 -1454 -965 -647 O
ATOM 278 N ASN A 36 9.215 -31.606 13.729 1.00 48.16 N
ANISOU 278 N ASN A 36 6822 4229 7248 -1045 -850 -730 N
ATOM 279 CA ASN A 36 10.672 -31.648 13.751 1.00 41.87 C
ANISOU 279 CA ASN A 36 6100 3431 6378 -850 -832 -775 C
ATOM 280 C ASN A 36 11.282 -30.309 14.146 1.00 43.85 C
ANISOU 280 C ASN A 36 6271 3919 6472 -756 -736 -698 C
ATOM 281 O ASN A 36 12.423 -30.279 14.620 1.00 49.25 O
ANISOU 281 O ASN A 36 6998 4608 7105 -618 -699 -670 O
ATOM 282 CB ASN A 36 11.208 -32.082 12.385 1.00 45.00 C
ANISOU 282 CB ASN A 36 6549 3804 6744 -754 -916 -1007 C
ATOM 283 CG ASN A 36 10.707 -33.452 11.969 1.00 55.24 C
ANISOU 283 CG ASN A 36 7940 4847 8203 -834 -1024 -1108 C
ATOM 284 OD1 ASN A 36 10.464 -34.319 12.808 1.00 46.94 O
ANISOU 284 OD1 ASN A 36 6960 3583 7293 -906 -1036 -1002 O
ATOM 285 ND2 ASN A 36 10.549 -33.653 10.665 1.00 57.10 N
ANISOU 285 ND2 ASN A 36 8178 5102 8417 -824 -1107 -1315 N
ATOM 286 N LEU A 37 10.553 -29.209 13.965 1.00 41.20 N
ANISOU 286 N LEU A 37 5819 3773 6062 -824 -700 -666 N
ATOM 287 CA LEU A 37 11.006 -27.890 14.382 1.00 41.67 C
ANISOU 287 CA LEU A 37 5805 4040 5988 -754 -613 -587 C
ATOM 288 C LEU A 37 10.541 -27.523 15.785 1.00 42.74 C
ANISOU 288 C LEU A 37 5898 4196 6146 -819 -538 -389 C
ATOM 289 O LEU A 37 10.776 -26.394 16.226 1.00 38.75 O
ANISOU 289 O LEU A 37 5327 3857 5540 -775 -469 -321 O
ATOM 290 CB LEU A 37 10.526 -26.828 13.387 1.00 40.73 C
ANISOU 290 CB LEU A 37 5593 4116 5768 -773 -617 -663 C
ATOM 291 CG LEU A 37 11.113 -26.863 11.975 1.00 37.40 C
ANISOU 291 CG LEU A 37 5193 3747 5269 -684 -671 -850 C
ATOM 292 CD1 LEU A 37 10.415 -25.846 11.086 1.00 35.13 C
ANISOU 292 CD1 LEU A 37 4812 3644 4890 -724 -678 -893 C
ATOM 293 CD2 LEU A 37 12.609 -26.607 12.011 1.00 35.08 C
ANISOU 293 CD2 LEU A 37 4935 3513 4882 -521 -631 -875 C
ATOM 294 N GLN A 38 9.892 -28.444 16.495 1.00 39.10 N
ANISOU 294 N GLN A 38 5471 3572 5812 -924 -550 -296 N
ATOM 295 CA GLN A 38 9.350 -28.161 17.824 1.00 46.50 C
ANISOU 295 CA GLN A 38 6360 4541 6766 -994 -477 -104 C
ATOM 296 C GLN A 38 10.255 -28.759 18.900 1.00 50.07 C
ANISOU 296 C GLN A 38 6902 4884 7240 -911 -446 1 C
ATOM 297 O GLN A 38 9.920 -29.724 19.589 1.00 56.88 O
ANISOU 297 O GLN A 38 7821 5580 8212 -983 -454 103 O
ATOM 298 CB GLN A 38 7.921 -28.684 17.934 1.00 38.24 C
ANISOU 298 CB GLN A 38 5272 3423 5836 -1183 -500 -47 C
ATOM 299 CG GLN A 38 6.970 -28.043 16.946 1.00 50.50 C
ANISOU 299 CG GLN A 38 6723 5106 7360 -1260 -532 -142 C
ATOM 300 CD GLN A 38 5.591 -28.659 16.975 1.00 42.24 C
ANISOU 300 CD GLN A 38 5626 3987 6436 -1451 -565 -104 C
ATOM 301 OE1 GLN A 38 5.272 -29.460 17.854 1.00 42.06 O
ANISOU 301 OE1 GLN A 38 5635 3829 6517 -1541 -549 20 O
ATOM 302 NE2 GLN A 38 4.761 -28.289 16.006 1.00 51.91 N
ANISOU 302 NE2 GLN A 38 6767 5307 7648 -1518 -613 -207 N
ATOM 303 N ASN A 39 11.429 -28.157 19.029 1.00 53.43 N
ANISOU 303 N ASN A 39 7336 5408 7556 -757 -413 -21 N
ATOM 304 CA ASN A 39 12.377 -28.466 20.087 1.00 36.15 C
ANISOU 304 CA ASN A 39 5210 3172 5354 -654 -378 77 C
ATOM 305 C ASN A 39 12.614 -27.211 20.921 1.00 39.92 C
ANISOU 305 C ASN A 39 5604 3853 5711 -608 -295 169 C
ATOM 306 O ASN A 39 12.111 -26.129 20.610 1.00 45.00 O
ANISOU 306 O ASN A 39 6152 4658 6287 -646 -268 148 O
ATOM 307 CB ASN A 39 13.686 -29.007 19.507 1.00 36.50 C
ANISOU 307 CB ASN A 39 5342 3144 5383 -499 -424 -48 C
ATOM 308 CG ASN A 39 14.174 -28.198 18.325 1.00 42.17 C
ANISOU 308 CG ASN A 39 6011 4014 5999 -430 -435 -209 C
ATOM 309 OD1 ASN A 39 14.828 -27.169 18.489 1.00 51.61 O
ANISOU 309 OD1 ASN A 39 7147 5383 7078 -352 -384 -202 O
ATOM 310 ND2 ASN A 39 13.854 -28.660 17.122 1.00 36.19 N
ANISOU 310 ND2 ASN A 39 5275 3194 5282 -461 -504 -354 N
ATOM 311 N VAL A 40 13.388 -27.368 21.997 1.00 47.93 N
ANISOU 311 N VAL A 40 6657 4857 6698 -520 -259 270 N
ATOM 312 CA VAL A 40 13.613 -26.255 22.917 1.00 39.62 C
ANISOU 312 CA VAL A 40 5530 3986 5536 -477 -186 356 C
ATOM 313 C VAL A 40 14.348 -25.119 22.218 1.00 42.67 C
ANISOU 313 C VAL A 40 5863 4538 5812 -392 -177 238 C
ATOM 314 O VAL A 40 14.035 -23.939 22.424 1.00 39.89 O
ANISOU 314 O VAL A 40 5426 4345 5385 -412 -132 260 O
ATOM 315 CB VAL A 40 14.375 -26.739 24.164 1.00 50.52 C
ANISOU 315 CB VAL A 40 6968 5323 6903 -389 -161 476 C
ATOM 316 CG1 VAL A 40 14.752 -25.560 25.041 1.00 34.72 C
ANISOU 316 CG1 VAL A 40 4892 3520 4779 -328 -96 534 C
ATOM 317 CG2 VAL A 40 13.532 -27.739 24.942 1.00 63.48 C
ANISOU 317 CG2 VAL A 40 8655 6817 8646 -491 -158 626 C
ATOM 318 N THR A 41 15.329 -25.456 21.377 1.00 31.80 N
ANISOU 318 N THR A 41 4535 3125 4424 -296 -219 112 N
ATOM 319 CA THR A 41 16.113 -24.434 20.691 1.00 36.42 C
ANISOU 319 CA THR A 41 5068 3868 4903 -220 -207 9 C
ATOM 320 C THR A 41 15.218 -23.497 19.888 1.00 42.12 C
ANISOU 320 C THR A 41 5714 4694 5595 -310 -202 -36 C
ATOM 321 O THR A 41 15.364 -22.270 19.955 1.00 42.66 O
ANISOU 321 O THR A 41 5716 4917 5577 -297 -162 -30 O
ATOM 322 CB THR A 41 17.153 -25.094 19.783 1.00 37.81 C
ANISOU 322 CB THR A 41 5302 3988 5076 -113 -255 -126 C
ATOM 323 OG1 THR A 41 17.968 -25.984 20.555 1.00 46.49 O
ANISOU 323 OG1 THR A 41 6473 4985 6205 -16 -265 -81 O
ATOM 324 CG2 THR A 41 18.041 -24.041 19.134 1.00 35.35 C
ANISOU 324 CG2 THR A 41 4929 3855 4648 -40 -233 -215 C
ATOM 325 N ASN A 42 14.271 -24.057 19.134 1.00 30.53 N
ANISOU 325 N ASN A 42 4258 3141 4201 -403 -248 -82 N
ATOM 326 CA ASN A 42 13.407 -23.233 18.300 1.00 36.60 C
ANISOU 326 CA ASN A 42 4956 4011 4939 -479 -254 -130 C
ATOM 327 C ASN A 42 12.385 -22.438 19.099 1.00 29.35 C
ANISOU 327 C ASN A 42 3960 3177 4013 -561 -206 -15 C
ATOM 328 O ASN A 42 11.771 -21.524 18.539 1.00 39.28 O
ANISOU 328 O ASN A 42 5152 4546 5228 -600 -204 -43 O
ATOM 329 CB ASN A 42 12.694 -24.098 17.263 1.00 31.10 C
ANISOU 329 CB ASN A 42 4288 3208 4321 -551 -325 -225 C
ATOM 330 CG ASN A 42 13.608 -24.514 16.133 1.00 31.49 C
ANISOU 330 CG ASN A 42 4389 3236 4341 -460 -373 -378 C
ATOM 331 OD1 ASN A 42 14.615 -23.859 15.864 1.00 36.97 O
ANISOU 331 OD1 ASN A 42 5068 4043 4937 -360 -347 -421 O
ATOM 332 ND2 ASN A 42 13.260 -25.603 15.460 1.00 50.48 N
ANISOU 332 ND2 ASN A 42 6850 5499 6830 -495 -444 -466 N
ATOM 333 N TYR A 43 12.182 -22.752 20.380 1.00 29.67 N
ANISOU 333 N TYR A 43 4008 3178 4088 -581 -169 114 N
ATOM 334 CA TYR A 43 11.308 -21.912 21.194 1.00 39.73 C
ANISOU 334 CA TYR A 43 5200 4560 5334 -638 -117 216 C
ATOM 335 C TYR A 43 11.912 -20.524 21.378 1.00 37.77 C
ANISOU 335 C TYR A 43 4906 4472 4974 -558 -76 205 C
ATOM 336 O TYR A 43 11.189 -19.521 21.397 1.00 31.91 O
ANISOU 336 O TYR A 43 4091 3840 4194 -591 -54 221 O
ATOM 337 CB TYR A 43 11.041 -22.576 22.547 1.00 32.09 C
ANISOU 337 CB TYR A 43 4250 3530 4411 -668 -81 362 C
ATOM 338 CG TYR A 43 10.265 -23.875 22.454 1.00 50.29 C
ANISOU 338 CG TYR A 43 6595 5673 6842 -776 -117 396 C
ATOM 339 CD1 TYR A 43 9.592 -24.223 21.288 1.00 63.34 C
ANISOU 339 CD1 TYR A 43 8241 7270 8557 -858 -176 298 C
ATOM 340 CD2 TYR A 43 10.205 -24.750 23.529 1.00 41.94 C
ANISOU 340 CD2 TYR A 43 5582 4516 5838 -801 -95 529 C
ATOM 341 CE1 TYR A 43 8.887 -25.409 21.196 1.00 71.36 C
ANISOU 341 CE1 TYR A 43 9291 8126 9696 -969 -215 322 C
ATOM 342 CE2 TYR A 43 9.502 -25.937 23.448 1.00 48.35 C
ANISOU 342 CE2 TYR A 43 6435 5163 6775 -914 -129 569 C
ATOM 343 CZ TYR A 43 8.844 -26.262 22.278 1.00 72.20 C
ANISOU 343 CZ TYR A 43 9446 8121 9866 -1002 -191 460 C
ATOM 344 OH TYR A 43 8.141 -27.444 22.189 1.00 68.39 O
ANISOU 344 OH TYR A 43 9003 7464 9517 -1127 -232 491 O
ATOM 345 N PHE A 44 13.238 -20.446 21.506 1.00 30.43 N
ANISOU 345 N PHE A 44 4015 3552 3993 -451 -70 174 N
ATOM 346 CA PHE A 44 13.903 -19.148 21.511 1.00 34.27 C
ANISOU 346 CA PHE A 44 4461 4178 4383 -388 -42 146 C
ATOM 347 C PHE A 44 13.902 -18.518 20.125 1.00 25.61 C
ANISOU 347 C PHE A 44 3343 3136 3252 -395 -69 41 C
ATOM 348 O PHE A 44 13.866 -17.289 20.005 1.00 37.60 O
ANISOU 348 O PHE A 44 4814 4764 4708 -389 -48 36 O
ATOM 349 CB PHE A 44 15.336 -19.288 22.025 1.00 25.96 C
ANISOU 349 CB PHE A 44 3445 3132 3288 -280 -30 141 C
ATOM 350 CG PHE A 44 15.429 -19.843 23.415 1.00 30.41 C
ANISOU 350 CG PHE A 44 4031 3657 3867 -256 -5 251 C
ATOM 351 CD1 PHE A 44 15.152 -19.044 24.512 1.00 26.10 C
ANISOU 351 CD1 PHE A 44 3436 3208 3271 -256 41 332 C
ATOM 352 CD2 PHE A 44 15.800 -21.160 23.627 1.00 27.56 C
ANISOU 352 CD2 PHE A 44 3744 3164 3565 -226 -30 274 C
ATOM 353 CE1 PHE A 44 15.238 -19.550 25.793 1.00 35.75 C
ANISOU 353 CE1 PHE A 44 4677 4414 4491 -228 65 438 C
ATOM 354 CE2 PHE A 44 15.889 -21.671 24.906 1.00 35.05 C
ANISOU 354 CE2 PHE A 44 4718 4080 4520 -201 -7 390 C
ATOM 355 CZ PHE A 44 15.607 -20.865 25.990 1.00 39.03 C
ANISOU 355 CZ PHE A 44 5167 4699 4963 -203 43 475 C
ATOM 356 N VAL A 45 13.951 -19.338 19.073 1.00 27.02 N
ANISOU 356 N VAL A 45 3561 3239 3467 -404 -117 -44 N
ATOM 357 CA VAL A 45 13.858 -18.814 17.714 1.00 36.67 C
ANISOU 357 CA VAL A 45 4763 4524 4647 -413 -145 -139 C
ATOM 358 C VAL A 45 12.493 -18.178 17.486 1.00 31.00 C
ANISOU 358 C VAL A 45 3985 3856 3937 -498 -150 -113 C
ATOM 359 O VAL A 45 12.372 -17.153 16.803 1.00 25.27 O
ANISOU 359 O VAL A 45 3223 3230 3149 -494 -150 -142 O
ATOM 360 CB VAL A 45 14.147 -19.929 16.691 1.00 38.90 C
ANISOU 360 CB VAL A 45 5101 4717 4964 -398 -201 -246 C
ATOM 361 CG1 VAL A 45 13.888 -19.442 15.274 1.00 46.25 C
ANISOU 361 CG1 VAL A 45 6006 5724 5842 -412 -232 -340 C
ATOM 362 CG2 VAL A 45 15.579 -20.416 16.833 1.00 27.16 C
ANISOU 362 CG2 VAL A 45 3662 3205 3453 -290 -195 -283 C
ATOM 363 N VAL A 46 11.445 -18.770 18.064 1.00 28.61 N
ANISOU 363 N VAL A 46 3669 3491 3711 -575 -154 -50 N
ATOM 364 CA VAL A 46 10.113 -18.181 17.972 1.00 26.47 C
ANISOU 364 CA VAL A 46 3326 3285 3448 -651 -156 -20 C
ATOM 365 C VAL A 46 10.050 -16.878 18.758 1.00 37.49 C
ANISOU 365 C VAL A 46 4670 4794 4780 -618 -103 48 C
ATOM 366 O VAL A 46 9.487 -15.881 18.290 1.00 29.21 O
ANISOU 366 O VAL A 46 3571 3835 3691 -624 -108 34 O
ATOM 367 CB VAL A 46 9.053 -19.188 18.451 1.00 30.06 C
ANISOU 367 CB VAL A 46 3768 3652 4002 -750 -167 35 C
ATOM 368 CG1 VAL A 46 7.713 -18.500 18.643 1.00 27.57 C
ANISOU 368 CG1 VAL A 46 3357 3431 3687 -817 -155 84 C
ATOM 369 CG2 VAL A 46 8.929 -20.328 17.455 1.00 39.44 C
ANISOU 369 CG2 VAL A 46 5001 4726 5257 -795 -236 -56 C
ATOM 370 N SER A 47 10.623 -16.862 19.964 1.00 30.83 N
ANISOU 370 N SER A 47 3841 3947 3926 -576 -58 117 N
ATOM 371 CA SER A 47 10.708 -15.615 20.718 1.00 38.89 C
ANISOU 371 CA SER A 47 4821 5072 4883 -533 -14 161 C
ATOM 372 C SER A 47 11.518 -14.576 19.957 1.00 31.72 C
ANISOU 372 C SER A 47 3921 4226 3905 -478 -21 95 C
ATOM 373 O SER A 47 11.202 -13.381 19.989 1.00 33.15 O
ANISOU 373 O SER A 47 4064 4487 4044 -466 -10 104 O
ATOM 374 CB SER A 47 11.322 -15.869 22.094 1.00 26.08 C
ANISOU 374 CB SER A 47 3218 3440 3251 -489 28 234 C
ATOM 375 OG SER A 47 11.488 -14.651 22.799 1.00 29.18 O
ANISOU 375 OG SER A 47 3576 3932 3578 -442 62 255 O
ATOM 376 N LEU A 48 12.571 -15.017 19.267 1.00 40.58 N
ANISOU 376 N LEU A 48 5090 5313 5013 -442 -40 31 N
ATOM 377 CA LEU A 48 13.340 -14.116 18.417 1.00 32.93 C
ANISOU 377 CA LEU A 48 4124 4411 3978 -404 -44 -25 C
ATOM 378 C LEU A 48 12.487 -13.583 17.271 1.00 28.49 C
ANISOU 378 C LEU A 48 3536 3889 3399 -443 -75 -59 C
ATOM 379 O LEU A 48 12.571 -12.401 16.922 1.00 31.46 O
ANISOU 379 O LEU A 48 3895 4336 3723 -428 -69 -58 O
ATOM 380 CB LEU A 48 14.573 -14.843 17.881 1.00 25.73 C
ANISOU 380 CB LEU A 48 3257 3468 3051 -357 -55 -90 C
ATOM 381 CG LEU A 48 15.665 -14.022 17.200 1.00 29.26 C
ANISOU 381 CG LEU A 48 3700 3995 3422 -314 -45 -136 C
ATOM 382 CD1 LEU A 48 16.371 -13.153 18.218 1.00 31.92 C
ANISOU 382 CD1 LEU A 48 4019 4382 3728 -282 -6 -91 C
ATOM 383 CD2 LEU A 48 16.656 -14.940 16.497 1.00 38.79 C
ANISOU 383 CD2 LEU A 48 4941 5181 4617 -267 -61 -213 C
ATOM 384 N ALA A 49 11.654 -14.442 16.680 1.00 25.05 N
ANISOU 384 N ALA A 49 3100 3408 3011 -493 -114 -88 N
ATOM 385 CA ALA A 49 10.812 -14.007 15.572 1.00 31.81 C
ANISOU 385 CA ALA A 49 3926 4314 3846 -525 -153 -124 C
ATOM 386 C ALA A 49 9.678 -13.106 16.044 1.00 29.21 C
ANISOU 386 C ALA A 49 3537 4042 3520 -548 -143 -63 C
ATOM 387 O ALA A 49 9.257 -12.209 15.307 1.00 24.33 O
ANISOU 387 O ALA A 49 2896 3491 2858 -541 -163 -74 O
ATOM 388 CB ALA A 49 10.255 -15.221 14.829 1.00 24.99 C
ANISOU 388 CB ALA A 49 3073 3386 3035 -575 -206 -186 C
ATOM 389 N ALA A 50 9.173 -13.326 17.260 1.00 23.91 N
ANISOU 389 N ALA A 50 2839 3352 2894 -568 -113 3 N
ATOM 390 CA ALA A 50 8.104 -12.479 17.776 1.00 23.84 C
ANISOU 390 CA ALA A 50 2765 3412 2882 -576 -100 54 C
ATOM 391 C ALA A 50 8.582 -11.049 18.003 1.00 31.18 C
ANISOU 391 C ALA A 50 3698 4401 3748 -510 -77 68 C
ATOM 392 O ALA A 50 7.806 -10.101 17.836 1.00 27.59 O
ANISOU 392 O ALA A 50 3204 4006 3273 -496 -88 79 O
ATOM 393 CB ALA A 50 7.545 -13.067 19.072 1.00 24.23 C
ANISOU 393 CB ALA A 50 2782 3443 2981 -608 -64 126 C
ATOM 394 N ALA A 51 9.848 -10.871 18.386 1.00 26.78 N
ANISOU 394 N ALA A 51 3188 3826 3164 -467 -50 66 N
ATOM 395 CA ALA A 51 10.376 -9.523 18.570 1.00 29.82 C
ANISOU 395 CA ALA A 51 3579 4252 3498 -418 -35 73 C
ATOM 396 C ALA A 51 10.553 -8.814 17.233 1.00 37.40 C
ANISOU 396 C ALA A 51 4557 5238 4416 -414 -66 39 C
ATOM 397 O ALA A 51 10.301 -7.608 17.128 1.00 30.89 O
ANISOU 397 O ALA A 51 3726 4446 3564 -390 -70 55 O
ATOM 398 CB ALA A 51 11.699 -9.573 19.334 1.00 21.63 C
ANISOU 398 CB ALA A 51 2576 3198 2445 -383 -2 74 C
ATOM 399 N ASP A 52 10.984 -9.543 16.201 1.00 25.63 N
ANISOU 399 N ASP A 52 3091 3733 2915 -431 -88 -8 N
ATOM 400 CA ASP A 52 11.143 -8.927 14.888 1.00 24.38 C
ANISOU 400 CA ASP A 52 2946 3615 2701 -426 -114 -33 C
ATOM 401 C ASP A 52 9.796 -8.582 14.265 1.00 27.14 C
ANISOU 401 C ASP A 52 3261 4002 3050 -440 -155 -28 C
ATOM 402 O ASP A 52 9.679 -7.563 13.572 1.00 27.73 O
ANISOU 402 O ASP A 52 3341 4117 3076 -420 -172 -13 O
ATOM 403 CB ASP A 52 11.952 -9.841 13.970 1.00 23.71 C
ANISOU 403 CB ASP A 52 2891 3523 2593 -430 -126 -95 C
ATOM 404 CG ASP A 52 13.430 -9.867 14.331 1.00 40.72 C
ANISOU 404 CG ASP A 52 5074 5674 4726 -401 -88 -103 C
ATOM 405 OD1 ASP A 52 13.947 -8.829 14.801 1.00 52.69 O
ANISOU 405 OD1 ASP A 52 6589 7210 6220 -387 -61 -66 O
ATOM 406 OD2 ASP A 52 14.076 -10.921 14.146 1.00 51.55 O
ANISOU 406 OD2 ASP A 52 6464 7019 6103 -390 -90 -152 O
ATOM 407 N ILE A 53 8.771 -9.404 14.502 1.00 23.11 N
ANISOU 407 N ILE A 53 2710 3478 2591 -476 -174 -34 N
ATOM 408 CA ILE A 53 7.417 -9.026 14.104 1.00 23.57 C
ANISOU 408 CA ILE A 53 2715 3587 2652 -486 -212 -25 C
ATOM 409 C ILE A 53 7.013 -7.727 14.789 1.00 39.03 C
ANISOU 409 C ILE A 53 4652 5578 4599 -439 -194 28 C
ATOM 410 O ILE A 53 6.415 -6.839 14.168 1.00 26.61 O
ANISOU 410 O ILE A 53 3065 4052 2993 -410 -226 38 O
ATOM 411 CB ILE A 53 6.426 -10.163 14.413 1.00 24.19 C
ANISOU 411 CB ILE A 53 2742 3648 2799 -546 -228 -36 C
ATOM 412 CG1 ILE A 53 6.728 -11.383 13.545 1.00 30.66 C
ANISOU 412 CG1 ILE A 53 3591 4424 3634 -588 -263 -106 C
ATOM 413 CG2 ILE A 53 4.990 -9.700 14.198 1.00 32.73 C
ANISOU 413 CG2 ILE A 53 3748 4803 3886 -554 -262 -23 C
ATOM 414 CD1 ILE A 53 5.908 -12.601 13.895 1.00 25.45 C
ANISOU 414 CD1 ILE A 53 2895 3717 3057 -664 -280 -115 C
ATOM 415 N ALA A 54 7.352 -7.585 16.073 1.00 22.88 N
ANISOU 415 N ALA A 54 2608 3508 2577 -423 -147 60 N
ATOM 416 CA ALA A 54 7.021 -6.364 16.797 1.00 32.28 C
ANISOU 416 CA ALA A 54 3784 4725 3756 -370 -133 95 C
ATOM 417 C ALA A 54 7.830 -5.167 16.314 1.00 25.39 C
ANISOU 417 C ALA A 54 2969 3840 2839 -331 -138 99 C
ATOM 418 O ALA A 54 7.382 -4.028 16.477 1.00 24.56 O
ANISOU 418 O ALA A 54 2860 3748 2724 -282 -150 119 O
ATOM 419 CB ALA A 54 7.225 -6.568 18.299 1.00 22.49 C
ANISOU 419 CB ALA A 54 2531 3473 2541 -359 -83 119 C
ATOM 420 N VAL A 55 9.006 -5.395 15.726 1.00 23.33 N
ANISOU 420 N VAL A 55 2758 3554 2552 -350 -132 81 N
ATOM 421 CA VAL A 55 9.772 -4.294 15.149 1.00 24.22 C
ANISOU 421 CA VAL A 55 2918 3660 2622 -332 -135 96 C
ATOM 422 C VAL A 55 9.013 -3.679 13.980 1.00 22.62 C
ANISOU 422 C VAL A 55 2718 3493 2386 -317 -181 111 C
ATOM 423 O VAL A 55 8.902 -2.453 13.865 1.00 25.25 O
ANISOU 423 O VAL A 55 3075 3815 2703 -283 -195 147 O
ATOM 424 CB VAL A 55 11.172 -4.772 14.720 1.00 21.89 C
ANISOU 424 CB VAL A 55 2661 3357 2301 -358 -113 74 C
ATOM 425 CG1 VAL A 55 11.841 -3.728 13.836 1.00 22.07 C
ANISOU 425 CG1 VAL A 55 2723 3391 2272 -359 -118 99 C
ATOM 426 CG2 VAL A 55 12.030 -5.063 15.937 1.00 21.46 C
ANISOU 426 CG2 VAL A 55 2608 3273 2272 -355 -72 67 C
ATOM 427 N GLY A 56 8.477 -4.522 13.096 1.00 26.12 N
ANISOU 427 N GLY A 56 3136 3974 2815 -341 -212 83 N
ATOM 428 CA GLY A 56 7.745 -4.009 11.953 1.00 25.91 C
ANISOU 428 CA GLY A 56 3105 3995 2744 -321 -262 95 C
ATOM 429 C GLY A 56 6.375 -3.473 12.309 1.00 23.96 C
ANISOU 429 C GLY A 56 2808 3774 2522 -281 -292 115 C
ATOM 430 O GLY A 56 5.887 -2.538 11.669 1.00 36.87 O
ANISOU 430 O GLY A 56 4452 5434 4121 -237 -330 146 O
ATOM 431 N VAL A 57 5.741 -4.043 13.332 1.00 23.86 N
ANISOU 431 N VAL A 57 2739 3763 2566 -292 -275 102 N
ATOM 432 CA VAL A 57 4.389 -3.627 13.686 1.00 27.45 C
ANISOU 432 CA VAL A 57 3125 4265 3038 -252 -299 115 C
ATOM 433 C VAL A 57 4.409 -2.352 14.521 1.00 42.27 C
ANISOU 433 C VAL A 57 5023 6116 4921 -180 -283 147 C
ATOM 434 O VAL A 57 3.569 -1.464 14.337 1.00 38.91 O
ANISOU 434 O VAL A 57 4578 5720 4484 -114 -319 164 O
ATOM 435 CB VAL A 57 3.658 -4.773 14.410 1.00 34.00 C
ANISOU 435 CB VAL A 57 3877 5121 3923 -301 -284 95 C
ATOM 436 CG1 VAL A 57 2.356 -4.279 15.020 1.00 30.28 C
ANISOU 436 CG1 VAL A 57 3321 4715 3469 -256 -292 111 C
ATOM 437 CG2 VAL A 57 3.389 -5.915 13.448 1.00 24.97 C
ANISOU 437 CG2 VAL A 57 2710 3997 2782 -368 -321 53 C
ATOM 438 N LEU A 58 5.368 -2.228 15.437 1.00 25.48 N
ANISOU 438 N LEU A 58 2937 3933 2810 -185 -235 149 N
ATOM 439 CA LEU A 58 5.377 -1.123 16.388 1.00 24.09 C
ANISOU 439 CA LEU A 58 2777 3729 2645 -119 -222 161 C
ATOM 440 C LEU A 58 6.647 -0.291 16.333 1.00 23.33 C
ANISOU 440 C LEU A 58 2769 3557 2537 -118 -212 173 C
ATOM 441 O LEU A 58 6.569 0.942 16.274 1.00 24.06 O
ANISOU 441 O LEU A 58 2902 3612 2627 -64 -236 191 O
ATOM 442 CB LEU A 58 5.175 -1.657 17.815 1.00 23.43 C
ANISOU 442 CB LEU A 58 2643 3668 2593 -118 -176 148 C
ATOM 443 CG LEU A 58 3.792 -2.222 18.132 1.00 33.04 C
ANISOU 443 CG LEU A 58 3759 4969 3826 -114 -179 148 C
ATOM 444 CD1 LEU A 58 3.761 -2.767 19.547 1.00 23.85 C
ANISOU 444 CD1 LEU A 58 2552 3829 2680 -121 -124 151 C
ATOM 445 CD2 LEU A 58 2.730 -1.154 17.936 1.00 28.41 C
ANISOU 445 CD2 LEU A 58 3140 4427 3229 -27 -219 151 C
ATOM 446 N ALA A 59 7.819 -0.929 16.360 1.00 22.80 N
ANISOU 446 N ALA A 59 2731 3465 2466 -177 -179 163 N
ATOM 447 CA ALA A 59 9.061 -0.176 16.502 1.00 25.60 C
ANISOU 447 CA ALA A 59 3151 3760 2816 -187 -163 170 C
ATOM 448 C ALA A 59 9.314 0.718 15.294 1.00 27.02 C
ANISOU 448 C ALA A 59 3387 3916 2964 -190 -195 210 C
ATOM 449 O ALA A 59 9.791 1.849 15.441 1.00 25.55 O
ANISOU 449 O ALA A 59 3254 3668 2787 -178 -201 231 O
ATOM 450 CB ALA A 59 10.233 -1.131 16.722 1.00 22.05 C
ANISOU 450 CB ALA A 59 2706 3310 2363 -242 -124 149 C
ATOM 451 N ILE A 60 8.998 0.236 14.097 1.00 23.27 N
ANISOU 451 N ILE A 60 2902 3487 2451 -209 -217 221 N
ATOM 452 CA ILE A 60 9.230 1.010 12.878 1.00 30.32 C
ANISOU 452 CA ILE A 60 3847 4375 3298 -211 -244 271 C
ATOM 453 C ILE A 60 8.208 2.140 12.771 1.00 24.50 C
ANISOU 453 C ILE A 60 3125 3615 2568 -138 -291 308 C
ATOM 454 O ILE A 60 8.600 3.274 12.459 1.00 25.75 O
ANISOU 454 O ILE A 60 3351 3712 2722 -128 -305 360 O
ATOM 455 CB ILE A 60 9.230 0.105 11.634 1.00 31.44 C
ANISOU 455 CB ILE A 60 3973 4590 3383 -244 -255 262 C
ATOM 456 CG1 ILE A 60 10.505 -0.742 11.610 1.00 25.66 C
ANISOU 456 CG1 ILE A 60 3245 3867 2636 -303 -210 231 C
ATOM 457 CG2 ILE A 60 9.113 0.931 10.363 1.00 26.21 C
ANISOU 457 CG2 ILE A 60 3354 3947 2659 -228 -291 324 C
ATOM 458 CD1 ILE A 60 10.639 -1.618 10.391 1.00 38.61 C
ANISOU 458 CD1 ILE A 60 4875 5579 4214 -327 -220 206 C
ATOM 459 N PRO A 61 6.909 1.913 13.014 1.00 30.72 N
ANISOU 459 N PRO A 61 3853 4449 3371 -85 -319 287 N
ATOM 460 CA PRO A 61 6.003 3.070 13.116 1.00 29.11 C
ANISOU 460 CA PRO A 61 3661 4220 3179 5 -363 314 C
ATOM 461 C PRO A 61 6.409 4.058 14.199 1.00 33.76 C
ANISOU 461 C PRO A 61 4296 4715 3815 40 -350 308 C
ATOM 462 O PRO A 61 6.228 5.268 14.015 1.00 27.81 O
ANISOU 462 O PRO A 61 3602 3895 3070 98 -388 344 O
ATOM 463 CB PRO A 61 4.643 2.423 13.409 1.00 34.15 C
ANISOU 463 CB PRO A 61 4201 4947 3828 44 -381 277 C
ATOM 464 CG PRO A 61 4.736 1.088 12.778 1.00 25.28 C
ANISOU 464 CG PRO A 61 3035 3888 2680 -32 -372 253 C
ATOM 465 CD PRO A 61 6.154 0.645 13.013 1.00 32.92 C
ANISOU 465 CD PRO A 61 4050 4808 3652 -104 -320 244 C
ATOM 466 N PHE A 62 6.968 3.585 15.318 1.00 25.39 N
ANISOU 466 N PHE A 62 3215 3646 2785 10 -303 262 N
ATOM 467 CA PHE A 62 7.461 4.509 16.338 1.00 24.83 C
ANISOU 467 CA PHE A 62 3189 3492 2753 38 -295 244 C
ATOM 468 C PHE A 62 8.649 5.312 15.823 1.00 26.03 C
ANISOU 468 C PHE A 62 3432 3553 2907 -15 -298 284 C
ATOM 469 O PHE A 62 8.804 6.490 16.164 1.00 25.63 O
ANISOU 469 O PHE A 62 3442 3405 2889 19 -322 290 O
ATOM 470 CB PHE A 62 7.851 3.755 17.611 1.00 24.14 C
ANISOU 470 CB PHE A 62 3057 3433 2683 17 -246 189 C
ATOM 471 CG PHE A 62 6.681 3.221 18.395 1.00 26.47 C
ANISOU 471 CG PHE A 62 3266 3809 2983 73 -237 157 C
ATOM 472 CD1 PHE A 62 5.381 3.400 17.952 1.00 24.78 C
ANISOU 472 CD1 PHE A 62 3008 3645 2761 136 -274 169 C
ATOM 473 CD2 PHE A 62 6.888 2.541 19.584 1.00 23.74 C
ANISOU 473 CD2 PHE A 62 2876 3500 2643 63 -192 122 C
ATOM 474 CE1 PHE A 62 4.313 2.908 18.675 1.00 24.95 C
ANISOU 474 CE1 PHE A 62 2937 3758 2785 177 -261 144 C
ATOM 475 CE2 PHE A 62 5.820 2.049 20.313 1.00 26.86 C
ANISOU 475 CE2 PHE A 62 3188 3981 3038 105 -177 106 C
ATOM 476 CZ PHE A 62 4.533 2.235 19.857 1.00 24.54 C
ANISOU 476 CZ PHE A 62 2842 3741 2739 158 -209 116 C
ATOM 477 N ALA A 63 9.499 4.687 15.004 1.00 29.47 N
ANISOU 477 N ALA A 63 3874 4017 3308 -100 -273 310 N
ATOM 478 CA ALA A 63 10.649 5.390 14.442 1.00 30.04 C
ANISOU 478 CA ALA A 63 4016 4024 3373 -164 -268 359 C
ATOM 479 C ALA A 63 10.210 6.486 13.481 1.00 26.06 C
ANISOU 479 C ALA A 63 3578 3466 2858 -132 -316 437 C
ATOM 480 O ALA A 63 10.757 7.595 13.502 1.00 26.72 O
ANISOU 480 O ALA A 63 3735 3444 2972 -149 -330 476 O
ATOM 481 CB ALA A 63 11.575 4.399 13.737 1.00 28.50 C
ANISOU 481 CB ALA A 63 3798 3899 3130 -248 -227 365 C
ATOM 482 N ILE A 64 9.231 6.191 12.626 1.00 26.34 N
ANISOU 482 N ILE A 64 3589 3569 2849 -86 -347 462 N
ATOM 483 CA ILE A 64 8.696 7.207 11.725 1.00 27.42 C
ANISOU 483 CA ILE A 64 3787 3664 2967 -36 -400 542 C
ATOM 484 C ILE A 64 8.083 8.350 12.523 1.00 29.37 C
ANISOU 484 C ILE A 64 4075 3806 3279 55 -441 533 C
ATOM 485 O ILE A 64 8.230 9.526 12.167 1.00 39.10 O
ANISOU 485 O ILE A 64 5398 4930 4530 72 -476 599 O
ATOM 486 CB ILE A 64 7.678 6.570 10.760 1.00 32.18 C
ANISOU 486 CB ILE A 64 4338 4381 3506 5 -431 554 C
ATOM 487 CG1 ILE A 64 8.360 5.485 9.921 1.00 28.21 C
ANISOU 487 CG1 ILE A 64 3806 3974 2937 -80 -396 551 C
ATOM 488 CG2 ILE A 64 7.028 7.633 9.881 1.00 28.86 C
ANISOU 488 CG2 ILE A 64 3979 3926 3059 78 -494 639 C
ATOM 489 CD1 ILE A 64 7.407 4.644 9.097 1.00 27.31 C
ANISOU 489 CD1 ILE A 64 3631 3981 2765 -50 -428 532 C
ATOM 490 N THR A 65 7.407 8.023 13.626 1.00 27.63 N
ANISOU 490 N THR A 65 3792 3614 3092 116 -437 450 N
ATOM 491 CA THR A 65 6.772 9.046 14.451 1.00 28.31 C
ANISOU 491 CA THR A 65 3907 3618 3231 222 -476 420 C
ATOM 492 C THR A 65 7.806 9.983 15.066 1.00 28.61 C
ANISOU 492 C THR A 65 4031 3513 3326 184 -472 414 C
ATOM 493 O THR A 65 7.704 11.209 14.944 1.00 29.70 O
ANISOU 493 O THR A 65 4257 3525 3502 233 -522 448 O
ATOM 494 CB THR A 65 5.929 8.383 15.542 1.00 29.49 C
ANISOU 494 CB THR A 65 3958 3857 3391 285 -459 332 C
ATOM 495 OG1 THR A 65 4.841 7.671 14.940 1.00 33.00 O
ANISOU 495 OG1 THR A 65 4321 4424 3794 320 -474 341 O
ATOM 496 CG2 THR A 65 5.377 9.424 16.501 1.00 28.57 C
ANISOU 496 CG2 THR A 65 3866 3669 3322 401 -492 284 C
ATOM 497 N ILE A 66 8.819 9.421 15.729 1.00 27.77 N
ANISOU 497 N ILE A 66 3902 3420 3231 96 -420 368 N
ATOM 498 CA ILE A 66 9.791 10.247 16.435 1.00 28.10 C
ANISOU 498 CA ILE A 66 4008 3341 3329 56 -421 344 C
ATOM 499 C ILE A 66 10.708 11.014 15.495 1.00 28.85 C
ANISOU 499 C ILE A 66 4192 3336 3433 -35 -431 436 C
ATOM 500 O ILE A 66 11.437 11.904 15.947 1.00 32.05 O
ANISOU 500 O ILE A 66 4663 3617 3897 -74 -445 427 O
ATOM 501 CB ILE A 66 10.617 9.383 17.409 1.00 40.25 C
ANISOU 501 CB ILE A 66 5487 4941 4867 -6 -365 269 C
ATOM 502 CG1 ILE A 66 11.153 10.249 18.547 1.00 41.02 C
ANISOU 502 CG1 ILE A 66 5627 4935 5023 3 -382 201 C
ATOM 503 CG2 ILE A 66 11.754 8.677 16.678 1.00 27.26 C
ANISOU 503 CG2 ILE A 66 3828 3343 3186 -132 -320 313 C
ATOM 504 CD1 ILE A 66 11.990 9.501 19.531 1.00 32.84 C
ANISOU 504 CD1 ILE A 66 4535 3963 3981 -48 -336 130 C
ATOM 505 N SER A 67 10.688 10.706 14.198 1.00 28.94 N
ANISOU 505 N SER A 67 4206 3404 3386 -72 -425 526 N
ATOM 506 CA SER A 67 11.466 11.479 13.239 1.00 29.87 C
ANISOU 506 CA SER A 67 4407 3440 3502 -155 -432 633 C
ATOM 507 C SER A 67 10.836 12.832 12.930 1.00 31.32 C
ANISOU 507 C SER A 67 4693 3481 3727 -80 -501 698 C
ATOM 508 O SER A 67 11.536 13.727 12.443 1.00 34.60 O
ANISOU 508 O SER A 67 5196 3782 4169 -152 -512 785 O
ATOM 509 CB SER A 67 11.643 10.689 11.941 1.00 31.86 C
ANISOU 509 CB SER A 67 4626 3818 3661 -209 -401 706 C
ATOM 510 OG SER A 67 10.417 10.584 11.236 1.00 36.47 O
ANISOU 510 OG SER A 67 5200 4458 4198 -112 -442 738 O
ATOM 511 N THR A 68 9.538 13.000 13.197 1.00 34.81 N
ANISOU 511 N THR A 68 5124 3928 4176 63 -548 662 N
ATOM 512 CA THR A 68 8.857 14.253 12.895 1.00 33.04 C
ANISOU 512 CA THR A 68 4996 3569 3988 160 -622 720 C
ATOM 513 C THR A 68 9.114 15.335 13.938 1.00 33.83 C
ANISOU 513 C THR A 68 5172 3490 4190 187 -657 661 C
ATOM 514 O THR A 68 8.967 16.521 13.626 1.00 37.82 O
ANISOU 514 O THR A 68 5791 3834 4746 228 -717 724 O
ATOM 515 CB THR A 68 7.347 14.022 12.770 1.00 35.00 C
ANISOU 515 CB THR A 68 5190 3907 4201 315 -663 697 C
ATOM 516 OG1 THR A 68 6.815 13.602 14.033 1.00 37.48 O
ANISOU 516 OG1 THR A 68 5425 4276 4542 387 -652 565 O
ATOM 517 CG2 THR A 68 7.052 12.958 11.726 1.00 34.73 C
ANISOU 517 CG2 THR A 68 5081 4047 4070 286 -640 742 C
ATOM 518 N GLY A 69 9.493 14.961 15.157 1.00 33.00 N
ANISOU 518 N GLY A 69 5015 3407 4117 170 -627 540 N
ATOM 519 CA GLY A 69 9.711 15.944 16.201 1.00 38.22 C
ANISOU 519 CA GLY A 69 5743 3912 4868 203 -666 461 C
ATOM 520 C GLY A 69 8.439 16.527 16.775 1.00 44.46 C
ANISOU 520 C GLY A 69 6546 4662 5683 391 -727 392 C
ATOM 521 O GLY A 69 8.457 17.650 17.293 1.00 35.81 O
ANISOU 521 O GLY A 69 5544 3396 4667 445 -784 352 O
ATOM 522 N PHE A 70 7.337 15.784 16.709 1.00 41.66 N
ANISOU 522 N PHE A 70 6096 4466 5267 493 -717 372 N
ATOM 523 CA PHE A 70 6.039 16.282 17.141 1.00 38.30 C
ANISOU 523 CA PHE A 70 5662 4038 4853 681 -772 314 C
ATOM 524 C PHE A 70 6.033 16.568 18.640 1.00 34.89 C
ANISOU 524 C PHE A 70 5216 3577 4464 750 -775 166 C
ATOM 525 O PHE A 70 6.793 15.987 19.417 1.00 44.75 O
ANISOU 525 O PHE A 70 6418 4878 5708 663 -723 101 O
ATOM 526 CB PHE A 70 4.943 15.269 16.802 1.00 51.11 C
ANISOU 526 CB PHE A 70 7158 5867 6396 747 -751 318 C
ATOM 527 CG PHE A 70 4.909 14.078 17.722 1.00 39.10 C
ANISOU 527 CG PHE A 70 5506 4510 4839 719 -682 226 C
ATOM 528 CD1 PHE A 70 5.987 13.211 17.802 1.00 32.87 C
ANISOU 528 CD1 PHE A 70 4688 3768 4033 566 -617 230 C
ATOM 529 CD2 PHE A 70 3.794 13.823 18.502 1.00 49.54 C
ANISOU 529 CD2 PHE A 70 6734 5948 6142 849 -682 143 C
ATOM 530 CE1 PHE A 70 5.956 12.118 18.649 1.00 33.55 C
ANISOU 530 CE1 PHE A 70 4666 3995 4089 544 -558 159 C
ATOM 531 CE2 PHE A 70 3.755 12.730 19.347 1.00 32.78 C
ANISOU 531 CE2 PHE A 70 4495 3974 3985 816 -617 78 C
ATOM 532 CZ PHE A 70 4.836 11.877 19.422 1.00 35.65 C
ANISOU 532 CZ PHE A 70 4844 4365 4337 665 -557 88 C
ATOM 533 N CYS A 71 5.155 17.484 19.040 1.00 39.63 N
ANISOU 533 N CYS A 71 5858 4101 5100 919 -841 111 N
ATOM 534 CA CYS A 71 4.992 17.792 20.454 1.00 36.52 C
ANISOU 534 CA CYS A 71 5446 3699 4732 1014 -849 -41 C
ATOM 535 C CYS A 71 4.324 16.625 21.167 1.00 39.03 C
ANISOU 535 C CYS A 71 5600 4256 4972 1059 -786 -110 C
ATOM 536 O CYS A 71 3.339 16.064 20.677 1.00 35.13 O
ANISOU 536 O CYS A 71 5020 3902 4425 1120 -776 -70 O
ATOM 537 CB CYS A 71 4.162 19.062 20.632 1.00 38.39 C
ANISOU 537 CB CYS A 71 5766 3798 5021 1202 -939 -87 C
ATOM 538 SG CYS A 71 4.914 20.563 19.969 1.00 69.75 S
ANISOU 538 SG CYS A 71 9948 7448 9104 1156 -1024 -10 S
ATOM 539 N ALA A 72 4.861 16.259 22.327 1.00 38.66 N
ANISOU 539 N ALA A 72 5511 4261 4919 1026 -744 -211 N
ATOM 540 CA ALA A 72 4.309 15.158 23.101 1.00 33.86 C
ANISOU 540 CA ALA A 72 4755 3872 4238 1058 -679 -266 C
ATOM 541 C ALA A 72 4.785 15.281 24.537 1.00 36.21 C
ANISOU 541 C ALA A 72 5043 4179 4535 1081 -663 -396 C
ATOM 542 O ALA A 72 5.814 15.902 24.818 1.00 38.31 O
ANISOU 542 O ALA A 72 5402 4301 4855 1015 -689 -433 O
ATOM 543 CB ALA A 72 4.716 13.800 22.519 1.00 32.23 C
ANISOU 543 CB ALA A 72 4471 3791 3982 906 -608 -182 C
ATOM 544 N ALA A 73 4.014 14.685 25.444 1.00 39.13 N
ANISOU 544 N ALA A 73 5295 4731 4842 1172 -622 -464 N
ATOM 545 CA ALA A 73 4.465 14.536 26.819 1.00 33.62 C
ANISOU 545 CA ALA A 73 4565 4093 4116 1185 -593 -576 C
ATOM 546 C ALA A 73 5.767 13.746 26.842 1.00 32.38 C
ANISOU 546 C ALA A 73 4407 3941 3953 1003 -544 -538 C
ATOM 547 O ALA A 73 5.917 12.746 26.135 1.00 40.02 O
ANISOU 547 O ALA A 73 5327 4982 4898 895 -496 -440 O
ATOM 548 CB ALA A 73 3.396 13.834 27.659 1.00 42.48 C
ANISOU 548 CB ALA A 73 5544 5442 5155 1293 -540 -622 C
ATOM 549 N CYS A 74 6.715 14.204 27.662 1.00 40.84 N
ANISOU 549 N CYS A 74 5532 4939 5046 976 -560 -626 N
ATOM 550 CA CYS A 74 8.072 13.673 27.584 1.00 42.73 C
ANISOU 550 CA CYS A 74 5785 5158 5294 806 -530 -593 C
ATOM 551 C CYS A 74 8.134 12.191 27.944 1.00 30.34 C
ANISOU 551 C CYS A 74 4098 3784 3645 752 -445 -558 C
ATOM 552 O CYS A 74 8.991 11.467 27.426 1.00 36.12 O
ANISOU 552 O CYS A 74 4824 4522 4378 614 -412 -487 O
ATOM 553 CB CYS A 74 9.003 14.490 28.482 1.00 39.30 C
ANISOU 553 CB CYS A 74 5417 4620 4895 798 -573 -709 C
ATOM 554 SG CYS A 74 10.769 14.210 28.193 1.00 57.41 S
ANISOU 554 SG CYS A 74 7744 6847 7223 587 -559 -670 S
ATOM 555 N HIS A 75 7.239 11.717 28.812 1.00 30.42 N
ANISOU 555 N HIS A 75 4015 3954 3588 858 -410 -602 N
ATOM 556 CA HIS A 75 7.280 10.309 29.197 1.00 39.87 C
ANISOU 556 CA HIS A 75 5109 5323 4716 802 -331 -558 C
ATOM 557 C HIS A 75 6.714 9.406 28.107 1.00 28.54 C
ANISOU 557 C HIS A 75 3624 3942 3278 741 -298 -439 C
ATOM 558 O HIS A 75 7.284 8.349 27.817 1.00 27.51 O
ANISOU 558 O HIS A 75 3464 3855 3133 628 -253 -375 O
ATOM 559 CB HIS A 75 6.540 10.097 30.519 1.00 39.48 C
ANISOU 559 CB HIS A 75 4975 5436 4590 925 -299 -633 C
ATOM 560 CG HIS A 75 7.379 10.384 31.725 1.00 56.41 C
ANISOU 560 CG HIS A 75 7139 7590 6705 944 -307 -737 C
ATOM 561 ND1 HIS A 75 7.664 11.665 32.147 1.00 60.47 N
ANISOU 561 ND1 HIS A 75 7736 7986 7256 1015 -377 -854 N
ATOM 562 CD2 HIS A 75 8.013 9.555 32.588 1.00 62.13 C
ANISOU 562 CD2 HIS A 75 7815 8426 7367 903 -259 -745 C
ATOM 563 CE1 HIS A 75 8.428 11.613 33.223 1.00 60.65 C
ANISOU 563 CE1 HIS A 75 7752 8056 7235 1014 -373 -938 C
ATOM 564 NE2 HIS A 75 8.654 10.344 33.512 1.00 79.51 N
ANISOU 564 NE2 HIS A 75 10060 10590 9559 951 -302 -869 N
ATOM 565 N GLY A 76 5.596 9.798 27.494 1.00 38.16 N
ANISOU 565 N GLY A 76 4830 5158 4508 821 -325 -416 N
ATOM 566 CA GLY A 76 5.124 9.072 26.329 1.00 28.50 C
ANISOU 566 CA GLY A 76 3570 3970 3288 758 -310 -313 C
ATOM 567 C GLY A 76 6.100 9.139 25.173 1.00 36.76 C
ANISOU 567 C GLY A 76 4701 4889 4378 634 -329 -245 C
ATOM 568 O GLY A 76 6.213 8.192 24.391 1.00 42.11 O
ANISOU 568 O GLY A 76 5346 5610 5042 540 -300 -170 O
ATOM 569 N CYS A 77 6.824 10.254 25.052 1.00 28.54 N
ANISOU 569 N CYS A 77 3767 3691 3387 628 -380 -272 N
ATOM 570 CA CYS A 77 7.884 10.343 24.057 1.00 32.01 C
ANISOU 570 CA CYS A 77 4280 4022 3861 499 -390 -204 C
ATOM 571 C CYS A 77 9.040 9.405 24.389 1.00 35.67 C
ANISOU 571 C CYS A 77 4714 4536 4303 380 -337 -202 C
ATOM 572 O CYS A 77 9.722 8.919 23.480 1.00 30.90 O
ANISOU 572 O CYS A 77 4122 3918 3700 270 -319 -132 O
ATOM 573 CB CYS A 77 8.369 11.791 23.945 1.00 36.74 C
ANISOU 573 CB CYS A 77 4998 4436 4526 512 -456 -230 C
ATOM 574 SG CYS A 77 9.816 12.041 22.886 1.00 46.26 S
ANISOU 574 SG CYS A 77 6289 5513 5773 339 -461 -146 S
ATOM 575 N LEU A 78 9.271 9.133 25.678 1.00 30.95 N
ANISOU 575 N LEU A 78 4074 4006 3677 411 -312 -279 N
ATOM 576 CA LEU A 78 10.315 8.184 26.057 1.00 26.19 C
ANISOU 576 CA LEU A 78 3439 3465 3048 317 -266 -276 C
ATOM 577 C LEU A 78 9.942 6.762 25.660 1.00 32.08 C
ANISOU 577 C LEU A 78 4108 4327 3755 276 -211 -206 C
ATOM 578 O LEU A 78 10.801 5.990 25.218 1.00 27.68 O
ANISOU 578 O LEU A 78 3546 3780 3192 178 -184 -165 O
ATOM 579 CB LEU A 78 10.581 8.263 27.559 1.00 28.20 C
ANISOU 579 CB LEU A 78 3668 3775 3272 374 -258 -372 C
ATOM 580 CG LEU A 78 11.484 9.397 28.039 1.00 27.96 C
ANISOU 580 CG LEU A 78 3712 3630 3283 366 -310 -456 C
ATOM 581 CD1 LEU A 78 11.486 9.457 29.556 1.00 27.70 C
ANISOU 581 CD1 LEU A 78 3644 3679 3201 451 -307 -563 C
ATOM 582 CD2 LEU A 78 12.891 9.207 27.501 1.00 27.00 C
ANISOU 582 CD2 LEU A 78 3618 3455 3188 224 -304 -421 C
ATOM 583 N PHE A 79 8.669 6.393 25.820 1.00 31.44 N
ANISOU 583 N PHE A 79 3963 4336 3648 351 -197 -196 N
ATOM 584 CA PHE A 79 8.235 5.057 25.425 1.00 24.73 C
ANISOU 584 CA PHE A 79 3041 3582 2772 303 -153 -132 C
ATOM 585 C PHE A 79 8.373 4.859 23.921 1.00 29.41 C
ANISOU 585 C PHE A 79 3665 4124 3387 227 -168 -64 C
ATOM 586 O PHE A 79 8.763 3.779 23.463 1.00 23.71 O
ANISOU 586 O PHE A 79 2920 3436 2654 146 -138 -23 O
ATOM 587 CB PHE A 79 6.793 4.820 25.870 1.00 25.17 C
ANISOU 587 CB PHE A 79 3014 3748 2802 390 -138 -135 C
ATOM 588 CG PHE A 79 6.282 3.445 25.551 1.00 27.72 C
ANISOU 588 CG PHE A 79 3259 4164 3108 331 -96 -73 C
ATOM 589 CD1 PHE A 79 6.486 2.397 26.431 1.00 24.36 C
ANISOU 589 CD1 PHE A 79 2783 3822 2652 301 -42 -62 C
ATOM 590 CD2 PHE A 79 5.602 3.200 24.368 1.00 24.67 C
ANISOU 590 CD2 PHE A 79 2856 3780 2738 304 -116 -25 C
ATOM 591 CE1 PHE A 79 6.020 1.131 26.138 1.00 27.20 C
ANISOU 591 CE1 PHE A 79 3080 4245 3010 238 -9 -3 C
ATOM 592 CE2 PHE A 79 5.136 1.936 24.072 1.00 24.37 C
ANISOU 592 CE2 PHE A 79 2750 3816 2694 241 -85 21 C
ATOM 593 CZ PHE A 79 5.345 0.901 24.958 1.00 24.10 C
ANISOU 593 CZ PHE A 79 2669 3845 2640 204 -32 33 C
ATOM 594 N ILE A 80 8.052 5.893 23.138 1.00 24.98 N
ANISOU 594 N ILE A 80 3158 3480 2852 259 -218 -50 N
ATOM 595 CA ILE A 80 8.187 5.809 21.686 1.00 24.90 C
ANISOU 595 CA ILE A 80 3181 3430 2848 195 -236 18 C
ATOM 596 C ILE A 80 9.641 5.585 21.297 1.00 24.33 C
ANISOU 596 C ILE A 80 3154 3311 2781 85 -218 37 C
ATOM 597 O ILE A 80 9.942 4.821 20.371 1.00 30.36 O
ANISOU 597 O ILE A 80 3908 4102 3526 14 -202 83 O
ATOM 598 CB ILE A 80 7.616 7.079 21.027 1.00 31.41 C
ANISOU 598 CB ILE A 80 4068 4170 3697 261 -296 37 C
ATOM 599 CG1 ILE A 80 6.094 7.081 21.112 1.00 34.86 C
ANISOU 599 CG1 ILE A 80 4440 4685 4121 368 -313 28 C
ATOM 600 CG2 ILE A 80 8.065 7.189 19.577 1.00 40.13 C
ANISOU 600 CG2 ILE A 80 5227 5222 4800 187 -314 114 C
ATOM 601 CD1 ILE A 80 5.454 5.978 20.316 1.00 29.30 C
ANISOU 601 CD1 ILE A 80 3663 4083 3388 327 -298 75 C
ATOM 602 N ALA A 81 10.566 6.240 21.999 1.00 26.49 N
ANISOU 602 N ALA A 81 3470 3519 3075 72 -223 -6 N
ATOM 603 CA ALA A 81 11.977 6.126 21.652 1.00 41.16 C
ANISOU 603 CA ALA A 81 5358 5342 4937 -33 -208 10 C
ATOM 604 C ALA A 81 12.603 4.841 22.177 1.00 23.41 C
ANISOU 604 C ALA A 81 3050 3185 2659 -74 -158 -7 C
ATOM 605 O ALA A 81 13.502 4.290 21.533 1.00 33.25 O
ANISOU 605 O ALA A 81 4297 4444 3893 -154 -136 21 O
ATOM 606 CB ALA A 81 12.749 7.332 22.186 1.00 24.90 C
ANISOU 606 CB ALA A 81 3362 3180 2920 -42 -239 -34 C
ATOM 607 N CYS A 82 12.144 4.343 23.326 1.00 26.06 N
ANISOU 607 N CYS A 82 3336 3589 2977 -16 -138 -49 N
ATOM 608 CA CYS A 82 12.835 3.268 24.025 1.00 22.69 C
ANISOU 608 CA CYS A 82 2865 3232 2522 -44 -97 -64 C
ATOM 609 C CYS A 82 12.242 1.889 23.785 1.00 23.85 C
ANISOU 609 C CYS A 82 2958 3455 2648 -53 -63 -23 C
ATOM 610 O CYS A 82 12.878 0.895 24.150 1.00 21.82 O
ANISOU 610 O CYS A 82 2676 3240 2373 -81 -32 -21 O
ATOM 611 CB CYS A 82 12.849 3.542 25.533 1.00 22.98 C
ANISOU 611 CB CYS A 82 2884 3302 2544 22 -94 -129 C
ATOM 612 SG CYS A 82 13.882 4.935 26.008 1.00 26.82 S
ANISOU 612 SG CYS A 82 3430 3700 3060 12 -137 -200 S
ATOM 613 N PHE A 83 11.047 1.794 23.198 1.00 26.02 N
ANISOU 613 N PHE A 83 3213 3746 2927 -29 -73 7 N
ATOM 614 CA PHE A 83 10.428 0.481 23.046 1.00 22.04 C
ANISOU 614 CA PHE A 83 2653 3308 2411 -48 -46 39 C
ATOM 615 C PHE A 83 11.246 -0.422 22.132 1.00 26.24 C
ANISOU 615 C PHE A 83 3199 3829 2941 -125 -35 62 C
ATOM 616 O PHE A 83 11.241 -1.647 22.303 1.00 21.34 O
ANISOU 616 O PHE A 83 2547 3243 2317 -149 -9 74 O
ATOM 617 CB PHE A 83 8.998 0.622 22.525 1.00 22.42 C
ANISOU 617 CB PHE A 83 2668 3384 2466 -13 -66 60 C
ATOM 618 CG PHE A 83 8.288 -0.688 22.362 1.00 22.31 C
ANISOU 618 CG PHE A 83 2592 3433 2451 -46 -44 89 C
ATOM 619 CD1 PHE A 83 7.891 -1.418 23.471 1.00 22.39 C
ANISOU 619 CD1 PHE A 83 2546 3508 2453 -34 -6 94 C
ATOM 620 CD2 PHE A 83 8.030 -1.198 21.102 1.00 22.26 C
ANISOU 620 CD2 PHE A 83 2585 3422 2451 -94 -64 111 C
ATOM 621 CE1 PHE A 83 7.243 -2.629 23.324 1.00 25.77 C
ANISOU 621 CE1 PHE A 83 2920 3978 2892 -80 12 127 C
ATOM 622 CE2 PHE A 83 7.384 -2.408 20.949 1.00 22.31 C
ANISOU 622 CE2 PHE A 83 2536 3473 2466 -135 -52 128 C
ATOM 623 CZ PHE A 83 6.989 -3.125 22.061 1.00 22.42 C
ANISOU 623 CZ PHE A 83 2498 3536 2486 -133 -14 140 C
ATOM 624 N VAL A 84 11.960 0.159 21.165 1.00 24.66 N
ANISOU 624 N VAL A 84 3048 3580 2743 -162 -54 69 N
ATOM 625 CA VAL A 84 12.816 -0.646 20.301 1.00 21.29 C
ANISOU 625 CA VAL A 84 2629 3159 2302 -225 -41 80 C
ATOM 626 C VAL A 84 13.968 -1.246 21.100 1.00 37.11 C
ANISOU 626 C VAL A 84 4624 5178 4299 -239 -12 55 C
ATOM 627 O VAL A 84 14.449 -2.341 20.781 1.00 26.81 O
ANISOU 627 O VAL A 84 3308 3895 2985 -266 6 56 O
ATOM 628 CB VAL A 84 13.312 0.196 19.110 1.00 35.33 C
ANISOU 628 CB VAL A 84 4453 4900 4072 -261 -62 103 C
ATOM 629 CG1 VAL A 84 14.184 1.355 19.584 1.00 21.81 C
ANISOU 629 CG1 VAL A 84 2778 3136 2374 -270 -68 90 C
ATOM 630 CG2 VAL A 84 14.050 -0.678 18.103 1.00 25.00 C
ANISOU 630 CG2 VAL A 84 3143 3622 2735 -313 -47 110 C
ATOM 631 N LEU A 85 14.413 -0.562 22.158 1.00 30.33 N
ANISOU 631 N LEU A 85 3771 4311 3444 -214 -11 27 N
ATOM 632 CA LEU A 85 15.441 -1.128 23.024 1.00 28.52 C
ANISOU 632 CA LEU A 85 3525 4111 3200 -215 11 1 C
ATOM 633 C LEU A 85 14.921 -2.340 23.784 1.00 26.42 C
ANISOU 633 C LEU A 85 3223 3890 2924 -184 36 15 C
ATOM 634 O LEU A 85 15.690 -3.264 24.075 1.00 33.62 O
ANISOU 634 O LEU A 85 4126 4824 3825 -190 54 14 O
ATOM 635 CB LEU A 85 15.953 -0.068 23.999 1.00 21.23 C
ANISOU 635 CB LEU A 85 2612 3175 2278 -193 -2 -42 C
ATOM 636 CG LEU A 85 16.393 1.263 23.386 1.00 24.57 C
ANISOU 636 CG LEU A 85 3078 3533 2725 -231 -32 -50 C
ATOM 637 CD1 LEU A 85 16.826 2.234 24.472 1.00 23.23 C
ANISOU 637 CD1 LEU A 85 2920 3342 2566 -209 -53 -108 C
ATOM 638 CD2 LEU A 85 17.509 1.048 22.377 1.00 27.85 C
ANISOU 638 CD2 LEU A 85 3498 3950 3134 -306 -21 -31 C
ATOM 639 N VAL A 86 13.628 -2.353 24.118 1.00 26.09 N
ANISOU 639 N VAL A 86 3159 3864 2888 -151 37 33 N
ATOM 640 CA VAL A 86 13.033 -3.518 24.766 1.00 24.84 C
ANISOU 640 CA VAL A 86 2964 3748 2726 -139 65 63 C
ATOM 641 C VAL A 86 13.057 -4.715 23.825 1.00 26.01 C
ANISOU 641 C VAL A 86 3115 3875 2892 -189 68 88 C
ATOM 642 O VAL A 86 13.438 -5.826 24.214 1.00 20.81 O
ANISOU 642 O VAL A 86 2453 3220 2235 -194 87 104 O
ATOM 643 CB VAL A 86 11.600 -3.203 25.231 1.00 26.56 C
ANISOU 643 CB VAL A 86 3143 4003 2944 -101 68 78 C
ATOM 644 CG1 VAL A 86 10.920 -4.462 25.747 1.00 21.52 C
ANISOU 644 CG1 VAL A 86 2462 3408 2308 -112 100 126 C
ATOM 645 CG2 VAL A 86 11.609 -2.120 26.296 1.00 21.63 C
ANISOU 645 CG2 VAL A 86 2517 3404 2296 -35 64 39 C
ATOM 646 N LEU A 87 12.652 -4.503 22.570 1.00 29.16 N
ANISOU 646 N LEU A 87 3524 4250 3304 -219 44 88 N
ATOM 647 CA LEU A 87 12.658 -5.586 21.592 1.00 27.94 C
ANISOU 647 CA LEU A 87 3374 4079 3163 -262 39 94 C
ATOM 648 C LEU A 87 14.077 -6.048 21.290 1.00 29.92 C
ANISOU 648 C LEU A 87 3653 4317 3400 -274 46 71 C
ATOM 649 O LEU A 87 14.332 -7.252 21.173 1.00 35.60 O
ANISOU 649 O LEU A 87 4375 5022 4130 -284 52 69 O
ATOM 650 CB LEU A 87 11.957 -5.137 20.310 1.00 22.30 C
ANISOU 650 CB LEU A 87 2663 3361 2450 -282 7 93 C
ATOM 651 CG LEU A 87 10.507 -4.669 20.455 1.00 23.72 C
ANISOU 651 CG LEU A 87 2806 3566 2642 -262 -7 112 C
ATOM 652 CD1 LEU A 87 9.947 -4.198 19.118 1.00 21.45 C
ANISOU 652 CD1 LEU A 87 2525 3280 2346 -272 -46 111 C
ATOM 653 CD2 LEU A 87 9.646 -5.779 21.044 1.00 24.88 C
ANISOU 653 CD2 LEU A 87 2904 3736 2815 -278 10 134 C
ATOM 654 N THR A 88 15.011 -5.104 21.156 1.00 25.27 N
ANISOU 654 N THR A 88 3080 3730 2789 -273 44 51 N
ATOM 655 CA THR A 88 16.394 -5.472 20.879 1.00 26.80 C
ANISOU 655 CA THR A 88 3285 3935 2965 -283 53 26 C
ATOM 656 C THR A 88 16.994 -6.260 22.036 1.00 32.20 C
ANISOU 656 C THR A 88 3956 4631 3646 -249 72 22 C
ATOM 657 O THR A 88 17.722 -7.236 21.821 1.00 28.38 O
ANISOU 657 O THR A 88 3476 4149 3158 -242 78 9 O
ATOM 658 CB THR A 88 17.221 -4.219 20.590 1.00 28.78 C
ANISOU 658 CB THR A 88 3546 4192 3198 -304 49 14 C
ATOM 659 OG1 THR A 88 16.689 -3.552 19.440 1.00 42.85 O
ANISOU 659 OG1 THR A 88 5347 5959 4976 -332 31 33 O
ATOM 660 CG2 THR A 88 18.673 -4.581 20.328 1.00 32.57 C
ANISOU 660 CG2 THR A 88 4016 4704 3654 -316 63 -12 C
ATOM 661 N GLN A 89 16.685 -5.861 23.273 1.00 26.52 N
ANISOU 661 N GLN A 89 3224 3926 2925 -218 79 32 N
ATOM 662 CA GLN A 89 17.217 -6.575 24.430 1.00 23.57 C
ANISOU 662 CA GLN A 89 2840 3577 2537 -178 94 38 C
ATOM 663 C GLN A 89 16.679 -7.999 24.492 1.00 31.74 C
ANISOU 663 C GLN A 89 3879 4586 3593 -175 104 77 C
ATOM 664 O GLN A 89 17.413 -8.933 24.836 1.00 25.52 O
ANISOU 664 O GLN A 89 3100 3796 2802 -149 110 82 O
ATOM 665 CB GLN A 89 16.881 -5.822 25.716 1.00 20.67 C
ANISOU 665 CB GLN A 89 2458 3246 2152 -140 99 39 C
ATOM 666 CG GLN A 89 17.709 -6.265 26.899 1.00 20.87 C
ANISOU 666 CG GLN A 89 2472 3316 2144 -93 109 36 C
ATOM 667 CD GLN A 89 19.190 -6.040 26.666 1.00 29.89 C
ANISOU 667 CD GLN A 89 3611 4475 3270 -97 96 -11 C
ATOM 668 OE1 GLN A 89 19.586 -5.039 26.071 1.00 33.40 O
ANISOU 668 OE1 GLN A 89 4057 4911 3721 -134 82 -47 O
ATOM 669 NE2 GLN A 89 20.014 -6.976 27.122 1.00 21.05 N
ANISOU 669 NE2 GLN A 89 2485 3382 2131 -60 102 -6 N
ATOM 670 N SER A 90 15.396 -8.182 24.166 1.00 28.58 N
ANISOU 670 N SER A 90 3472 4166 3221 -202 103 106 N
ATOM 671 CA SER A 90 14.820 -9.521 24.140 1.00 21.92 C
ANISOU 671 CA SER A 90 2633 3285 2412 -220 107 143 C
ATOM 672 C SER A 90 15.549 -10.413 23.146 1.00 32.24 C
ANISOU 672 C SER A 90 3971 4546 3735 -232 91 111 C
ATOM 673 O SER A 90 15.815 -11.587 23.432 1.00 24.62 O
ANISOU 673 O SER A 90 3025 3539 2789 -219 93 128 O
ATOM 674 CB SER A 90 13.333 -9.445 23.800 1.00 23.17 C
ANISOU 674 CB SER A 90 2766 3441 2599 -259 102 168 C
ATOM 675 OG SER A 90 12.736 -10.729 23.852 1.00 28.88 O
ANISOU 675 OG SER A 90 3487 4121 3363 -293 106 207 O
ATOM 676 N LYS A 91 15.880 -9.875 21.971 1.00 21.02 N
ANISOU 676 N LYS A 91 2556 3130 2300 -250 74 65 N
ATOM 677 CA LYS A 91 16.618 -10.659 20.988 1.00 34.64 C
ANISOU 677 CA LYS A 91 4304 4832 4025 -250 61 22 C
ATOM 678 C LYS A 91 17.989 -11.058 21.522 1.00 26.34 C
ANISOU 678 C LYS A 91 3259 3796 2953 -199 72 4 C
ATOM 679 O LYS A 91 18.468 -12.167 21.261 1.00 34.80 O
ANISOU 679 O LYS A 91 4353 4832 4037 -173 63 -16 O
ATOM 680 CB LYS A 91 16.747 -9.869 19.684 1.00 22.62 C
ANISOU 680 CB LYS A 91 2780 3339 2474 -276 47 -14 C
ATOM 681 CG LYS A 91 15.413 -9.565 19.025 1.00 28.17 C
ANISOU 681 CG LYS A 91 3476 4033 3193 -316 27 -1 C
ATOM 682 CD LYS A 91 15.574 -8.693 17.797 1.00 41.93 C
ANISOU 682 CD LYS A 91 5223 5812 4896 -333 14 -22 C
ATOM 683 CE LYS A 91 16.472 -9.352 16.763 1.00 48.75 C
ANISOU 683 CE LYS A 91 6102 6692 5730 -328 9 -73 C
ATOM 684 NZ LYS A 91 16.610 -8.511 15.540 1.00 42.09 N
ANISOU 684 NZ LYS A 91 5259 5899 4833 -348 1 -79 N
ATOM 685 N ILE A 92 18.626 -10.169 22.286 1.00 21.63 N
ANISOU 685 N ILE A 92 2642 3253 2324 -178 85 7 N
ATOM 686 CA ILE A 92 19.920 -10.483 22.886 1.00 23.99 C
ANISOU 686 CA ILE A 92 2934 3584 2597 -126 91 -12 C
ATOM 687 C ILE A 92 19.800 -11.670 23.834 1.00 33.52 C
ANISOU 687 C ILE A 92 4159 4752 3823 -80 93 29 C
ATOM 688 O ILE A 92 20.629 -12.588 23.811 1.00 23.31 O
ANISOU 688 O ILE A 92 2881 3446 2529 -32 86 13 O
ATOM 689 CB ILE A 92 20.489 -9.241 23.595 1.00 21.00 C
ANISOU 689 CB ILE A 92 2524 3269 2185 -122 98 -22 C
ATOM 690 CG1 ILE A 92 21.090 -8.282 22.570 1.00 23.88 C
ANISOU 690 CG1 ILE A 92 2874 3667 2531 -165 95 -60 C
ATOM 691 CG2 ILE A 92 21.544 -9.640 24.606 1.00 22.41 C
ANISOU 691 CG2 ILE A 92 2686 3490 2336 -60 99 -30 C
ATOM 692 CD1 ILE A 92 22.318 -8.841 21.898 1.00 35.24 C
ANISOU 692 CD1 ILE A 92 4298 5145 3947 -146 98 -102 C
ATOM 693 N PHE A 93 18.767 -11.675 24.681 1.00 21.64 N
ANISOU 693 N PHE A 93 2656 3233 2334 -92 104 88 N
ATOM 694 CA PHE A 93 18.572 -12.797 25.594 1.00 33.21 C
ANISOU 694 CA PHE A 93 4141 4660 3816 -60 110 148 C
ATOM 695 C PHE A 93 18.303 -14.090 24.833 1.00 29.56 C
ANISOU 695 C PHE A 93 3720 4101 3409 -77 94 151 C
ATOM 696 O PHE A 93 18.827 -15.150 25.194 1.00 29.10 O
ANISOU 696 O PHE A 93 3695 3995 3365 -30 86 170 O
ATOM 697 CB PHE A 93 17.429 -12.496 26.564 1.00 22.76 C
ANISOU 697 CB PHE A 93 2799 3358 2490 -78 132 215 C
ATOM 698 CG PHE A 93 17.779 -11.482 27.617 1.00 33.77 C
ANISOU 698 CG PHE A 93 4163 4843 3826 -38 144 211 C
ATOM 699 CD1 PHE A 93 18.996 -11.540 28.279 1.00 34.63 C
ANISOU 699 CD1 PHE A 93 4270 4997 3892 26 139 193 C
ATOM 700 CD2 PHE A 93 16.896 -10.464 27.938 1.00 28.83 C
ANISOU 700 CD2 PHE A 93 3508 4261 3187 -56 155 214 C
ATOM 701 CE1 PHE A 93 19.320 -10.606 29.246 1.00 52.59 C
ANISOU 701 CE1 PHE A 93 6515 7357 6111 61 142 175 C
ATOM 702 CE2 PHE A 93 17.215 -9.526 28.905 1.00 26.56 C
ANISOU 702 CE2 PHE A 93 3196 4049 2844 -14 159 193 C
ATOM 703 CZ PHE A 93 18.428 -9.597 29.559 1.00 32.58 C
ANISOU 703 CZ PHE A 93 3958 4855 3566 40 151 172 C
ATOM 704 N SER A 94 17.495 -14.022 23.772 1.00 27.75 N
ANISOU 704 N SER A 94 3492 3838 3212 -139 81 127 N
ATOM 705 CA SER A 94 17.198 -15.223 22.997 1.00 23.12 C
ANISOU 705 CA SER A 94 2945 3157 2682 -160 56 111 C
ATOM 706 C SER A 94 18.449 -15.768 22.321 1.00 34.07 C
ANISOU 706 C SER A 94 4359 4531 4057 -101 37 40 C
ATOM 707 O SER A 94 18.672 -16.984 22.298 1.00 34.72 O
ANISOU 707 O SER A 94 4487 4527 4179 -71 18 37 O
ATOM 708 CB SER A 94 16.116 -14.927 21.961 1.00 23.00 C
ANISOU 708 CB SER A 94 2916 3131 2692 -234 40 87 C
ATOM 709 OG SER A 94 14.884 -14.635 22.591 1.00 24.64 O
ANISOU 709 OG SER A 94 3092 3350 2918 -282 56 152 O
ATOM 710 N LEU A 95 19.280 -14.882 21.767 1.00 31.03 N
ANISOU 710 N LEU A 95 3944 4230 3616 -83 42 -18 N
ATOM 711 CA LEU A 95 20.494 -15.335 21.098 1.00 26.78 C
ANISOU 711 CA LEU A 95 3413 3708 3053 -24 31 -90 C
ATOM 712 C LEU A 95 21.479 -15.944 22.089 1.00 28.65 C
ANISOU 712 C LEU A 95 3659 3946 3281 62 33 -72 C
ATOM 713 O LEU A 95 22.135 -16.947 21.783 1.00 32.19 O
ANISOU 713 O LEU A 95 4138 4353 3742 127 13 -113 O
ATOM 714 CB LEU A 95 21.132 -14.176 20.335 1.00 37.56 C
ANISOU 714 CB LEU A 95 4734 5179 4359 -39 44 -138 C
ATOM 715 CG LEU A 95 20.348 -13.678 19.117 1.00 23.57 C
ANISOU 715 CG LEU A 95 2961 3413 2583 -105 35 -161 C
ATOM 716 CD1 LEU A 95 20.939 -12.384 18.590 1.00 22.16 C
ANISOU 716 CD1 LEU A 95 2741 3332 2345 -128 53 -177 C
ATOM 717 CD2 LEU A 95 20.310 -14.738 18.025 1.00 23.17 C
ANISOU 717 CD2 LEU A 95 2942 3315 2546 -89 7 -226 C
ATOM 718 N LEU A 96 21.590 -15.361 23.286 1.00 27.11 N
ANISOU 718 N LEU A 96 3439 3802 3060 74 52 -18 N
ATOM 719 CA LEU A 96 22.475 -15.925 24.300 1.00 30.00 C
ANISOU 719 CA LEU A 96 3810 4181 3408 162 49 5 C
ATOM 720 C LEU A 96 21.959 -17.265 24.811 1.00 34.20 C
ANISOU 720 C LEU A 96 4406 4593 3995 186 35 70 C
ATOM 721 O LEU A 96 22.757 -18.154 25.130 1.00 31.43 O
ANISOU 721 O LEU A 96 4084 4213 3646 274 18 70 O
ATOM 722 CB LEU A 96 22.643 -14.940 25.459 1.00 27.88 C
ANISOU 722 CB LEU A 96 3498 4004 3090 167 68 41 C
ATOM 723 CG LEU A 96 23.533 -15.360 26.634 1.00 32.04 C
ANISOU 723 CG LEU A 96 4021 4573 3582 261 62 69 C
ATOM 724 CD1 LEU A 96 24.938 -15.713 26.162 1.00 34.77 C
ANISOU 724 CD1 LEU A 96 4346 4964 3902 338 44 -4 C
ATOM 725 CD2 LEU A 96 23.581 -14.262 27.685 1.00 23.62 C
ANISOU 725 CD2 LEU A 96 2908 3605 2462 256 75 86 C
ATOM 726 N ALA A 97 20.637 -17.431 24.889 1.00 33.51 N
ANISOU 726 N ALA A 97 4340 4437 3956 109 42 128 N
ATOM 727 CA ALA A 97 20.079 -18.702 25.338 1.00 32.59 C
ANISOU 727 CA ALA A 97 4283 4195 3902 109 30 200 C
ATOM 728 C ALA A 97 20.289 -19.797 24.300 1.00 38.06 C
ANISOU 728 C ALA A 97 5034 4775 4654 126 -9 137 C
ATOM 729 O ALA A 97 20.552 -20.952 24.654 1.00 29.73 O
ANISOU 729 O ALA A 97 4040 3616 3640 180 -31 169 O
ATOM 730 CB ALA A 97 18.592 -18.540 25.652 1.00 25.46 C
ANISOU 730 CB ALA A 97 3371 3267 3035 9 50 277 C
ATOM 731 N ILE A 98 20.173 -19.454 23.014 1.00 38.02 N
ANISOU 731 N ILE A 98 5012 4785 4649 88 -21 44 N
ATOM 732 CA ILE A 98 20.373 -20.440 21.955 1.00 31.76 C
ANISOU 732 CA ILE A 98 4269 3898 3900 112 -62 -38 C
ATOM 733 C ILE A 98 21.801 -20.968 21.980 1.00 36.63 C
ANISOU 733 C ILE A 98 4902 4528 4486 241 -77 -91 C
ATOM 734 O ILE A 98 22.035 -22.176 21.847 1.00 28.23 O
ANISOU 734 O ILE A 98 3906 3344 3475 299 -114 -112 O
ATOM 735 CB ILE A 98 20.017 -19.831 20.586 1.00 26.14 C
ANISOU 735 CB ILE A 98 3527 3236 3169 54 -70 -126 C
ATOM 736 CG1 ILE A 98 18.503 -19.680 20.446 1.00 26.01 C
ANISOU 736 CG1 ILE A 98 3505 3175 3202 -63 -72 -83 C
ATOM 737 CG2 ILE A 98 20.572 -20.680 19.462 1.00 26.92 C
ANISOU 737 CG2 ILE A 98 3664 3285 3279 109 -109 -238 C
ATOM 738 CD1 ILE A 98 18.080 -18.966 19.182 1.00 25.55 C
ANISOU 738 CD1 ILE A 98 3414 3182 3114 -115 -82 -156 C
ATOM 739 N ALA A 99 22.777 -20.072 22.152 1.00 28.15 N
ANISOU 739 N ALA A 99 3764 3600 3332 289 -53 -116 N
ATOM 740 CA ALA A 99 24.168 -20.504 22.219 1.00 27.12 C
ANISOU 740 CA ALA A 99 3629 3511 3165 416 -65 -168 C
ATOM 741 C ALA A 99 24.421 -21.355 23.456 1.00 27.90 C
ANISOU 741 C ALA A 99 3775 3537 3288 494 -79 -85 C
ATOM 742 O ALA A 99 25.143 -22.355 23.390 1.00 28.91 O
ANISOU 742 O ALA A 99 3947 3604 3434 602 -111 -118 O
ATOM 743 CB ALA A 99 25.098 -19.291 22.199 1.00 26.40 C
ANISOU 743 CB ALA A 99 3445 3599 2985 428 -36 -205 C
ATOM 744 N ILE A 100 23.833 -20.974 24.593 1.00 35.00 N
ANISOU 744 N ILE A 100 4667 4447 4183 449 -55 24 N
ATOM 745 CA ILE A 100 23.970 -21.779 25.802 1.00 36.24 C
ANISOU 745 CA ILE A 100 4873 4542 4354 517 -65 123 C
ATOM 746 C ILE A 100 23.288 -23.130 25.623 1.00 34.78 C
ANISOU 746 C ILE A 100 4788 4157 4269 504 -96 163 C
ATOM 747 O ILE A 100 23.817 -24.167 26.040 1.00 30.67 O
ANISOU 747 O ILE A 100 4332 3547 3776 602 -126 194 O
ATOM 748 CB ILE A 100 23.418 -21.012 27.018 1.00 29.03 C
ANISOU 748 CB ILE A 100 3924 3705 3401 469 -28 228 C
ATOM 749 CG1 ILE A 100 24.344 -19.842 27.361 1.00 34.59 C
ANISOU 749 CG1 ILE A 100 4542 4590 4012 507 -12 181 C
ATOM 750 CG2 ILE A 100 23.245 -21.942 28.212 1.00 28.92 C
ANISOU 750 CG2 ILE A 100 3971 3612 3404 516 -33 355 C
ATOM 751 CD1 ILE A 100 23.896 -19.022 28.550 1.00 47.35 C
ANISOU 751 CD1 ILE A 100 6121 6292 5578 475 18 258 C
ATOM 752 N ASP A 101 22.114 -23.142 24.990 1.00 29.33 N
ANISOU 752 N ASP A 101 4113 3392 3639 382 -94 162 N
ATOM 753 CA ASP A 101 21.429 -24.401 24.715 1.00 30.51 C
ANISOU 753 CA ASP A 101 4353 3344 3895 348 -130 186 C
ATOM 754 C ASP A 101 22.295 -25.322 23.861 1.00 31.45 C
ANISOU 754 C ASP A 101 4529 3377 4044 454 -182 73 C
ATOM 755 O ASP A 101 22.433 -26.514 24.157 1.00 32.81 O
ANISOU 755 O ASP A 101 4791 3392 4284 512 -220 109 O
ATOM 756 CB ASP A 101 20.087 -24.124 24.034 1.00 30.11 C
ANISOU 756 CB ASP A 101 4287 3261 3895 198 -125 177 C
ATOM 757 CG ASP A 101 19.410 -25.385 23.538 1.00 36.14 C
ANISOU 757 CG ASP A 101 5135 3820 4774 148 -172 172 C
ATOM 758 OD1 ASP A 101 18.707 -26.041 24.335 1.00 37.48 O
ANISOU 758 OD1 ASP A 101 5349 3880 5009 92 -168 295 O
ATOM 759 OD2 ASP A 101 19.582 -25.721 22.347 1.00 31.71 O
ANISOU 759 OD2 ASP A 101 4596 3213 4238 162 -213 43 O
ATOM 760 N ARG A 102 22.906 -24.779 22.803 1.00 30.87 N
ANISOU 760 N ARG A 102 4404 3408 3917 485 -185 -62 N
ATOM 761 CA ARG A 102 23.736 -25.606 21.931 1.00 31.84 C
ANISOU 761 CA ARG A 102 4569 3474 4054 596 -231 -185 C
ATOM 762 C ARG A 102 25.013 -26.062 22.625 1.00 32.56 C
ANISOU 762 C ARG A 102 4672 3589 4111 760 -244 -176 C
ATOM 763 O ARG A 102 25.501 -27.167 22.356 1.00 33.90 O
ANISOU 763 O ARG A 102 4916 3639 4327 867 -293 -229 O
ATOM 764 CB ARG A 102 24.066 -24.853 20.643 1.00 31.13 C
ANISOU 764 CB ARG A 102 4410 3519 3898 587 -221 -321 C
ATOM 765 CG ARG A 102 22.871 -24.622 19.721 1.00 32.48 C
ANISOU 765 CG ARG A 102 4582 3653 4104 452 -227 -355 C
ATOM 766 CD ARG A 102 22.274 -25.935 19.210 1.00 32.14 C
ANISOU 766 CD ARG A 102 4639 3405 4169 440 -288 -399 C
ATOM 767 NE ARG A 102 21.340 -26.543 20.153 1.00 32.68 N
ANISOU 767 NE ARG A 102 4767 3316 4333 362 -296 -268 N
ATOM 768 CZ ARG A 102 21.007 -27.827 20.151 1.00 34.18 C
ANISOU 768 CZ ARG A 102 5058 3296 4632 364 -350 -265 C
ATOM 769 NH1 ARG A 102 21.519 -28.671 19.272 1.00 35.30 N
ANISOU 769 NH1 ARG A 102 5261 3349 4804 452 -407 -400 N
ATOM 770 NH2 ARG A 102 20.143 -28.275 21.059 1.00 34.69 N
ANISOU 770 NH2 ARG A 102 5166 3237 4778 276 -346 -124 N
ATOM 771 N TYR A 103 25.569 -25.238 23.515 1.00 31.82 N
ANISOU 771 N TYR A 103 4506 3648 3936 788 -206 -117 N
ATOM 772 CA TYR A 103 26.733 -25.675 24.279 1.00 33.59 C
ANISOU 772 CA TYR A 103 4735 3905 4124 946 -223 -99 C
ATOM 773 C TYR A 103 26.383 -26.840 25.198 1.00 41.48 C
ANISOU 773 C TYR A 103 5844 4718 5198 985 -254 21 C
ATOM 774 O TYR A 103 27.206 -27.738 25.409 1.00 35.17 O
ANISOU 774 O TYR A 103 5097 3855 4411 1134 -296 10 O
ATOM 775 CB TYR A 103 27.306 -24.512 25.086 1.00 31.62 C
ANISOU 775 CB TYR A 103 4382 3859 3774 952 -182 -63 C
ATOM 776 CG TYR A 103 28.523 -24.890 25.898 1.00 32.46 C
ANISOU 776 CG TYR A 103 4476 4027 3831 1115 -204 -49 C
ATOM 777 CD1 TYR A 103 29.765 -25.040 25.293 1.00 32.98 C
ANISOU 777 CD1 TYR A 103 4494 4182 3853 1242 -224 -168 C
ATOM 778 CD2 TYR A 103 28.429 -25.103 27.267 1.00 32.87 C
ANISOU 778 CD2 TYR A 103 4556 4061 3871 1148 -205 85 C
ATOM 779 CE1 TYR A 103 30.879 -25.388 26.030 1.00 36.12 C
ANISOU 779 CE1 TYR A 103 4871 4649 4204 1400 -248 -159 C
ATOM 780 CE2 TYR A 103 29.539 -25.451 28.012 1.00 42.01 C
ANISOU 780 CE2 TYR A 103 5701 5284 4976 1306 -231 99 C
ATOM 781 CZ TYR A 103 30.760 -25.591 27.389 1.00 47.25 C
ANISOU 781 CZ TYR A 103 6314 6034 5604 1432 -255 -25 C
ATOM 782 OH TYR A 103 31.865 -25.937 28.131 1.00 53.71 O
ANISOU 782 OH TYR A 103 7109 6930 6368 1597 -286 -15 O
ATOM 783 N ILE A 104 25.169 -26.842 25.752 1.00 33.73 N
ANISOU 783 N ILE A 104 4897 3652 4267 856 -234 143 N
ATOM 784 CA ILE A 104 24.743 -27.946 26.604 1.00 35.11 C
ANISOU 784 CA ILE A 104 5178 3645 4516 869 -258 277 C
ATOM 785 C ILE A 104 24.511 -29.198 25.768 1.00 36.50 C
ANISOU 785 C ILE A 104 5464 3594 4810 882 -317 218 C
ATOM 786 O ILE A 104 24.812 -30.317 26.200 1.00 38.08 O
ANISOU 786 O ILE A 104 5765 3635 5068 976 -361 272 O
ATOM 787 CB ILE A 104 23.484 -27.552 27.399 1.00 34.64 C
ANISOU 787 CB ILE A 104 5108 3582 4470 718 -212 424 C
ATOM 788 CG1 ILE A 104 23.782 -26.378 28.335 1.00 33.51 C
ANISOU 788 CG1 ILE A 104 4868 3657 4210 728 -162 474 C
ATOM 789 CG2 ILE A 104 22.952 -28.731 28.195 1.00 36.24 C
ANISOU 789 CG2 ILE A 104 5421 3592 4757 708 -230 576 C
ATOM 790 CD1 ILE A 104 22.564 -25.871 29.085 1.00 33.04 C
ANISOU 790 CD1 ILE A 104 4782 3627 4145 593 -112 600 C
ATOM 791 N ALA A 105 23.997 -29.032 24.547 1.00 36.06 N
ANISOU 791 N ALA A 105 5394 3517 4788 796 -326 100 N
ATOM 792 CA ALA A 105 23.732 -30.172 23.680 1.00 37.43 C
ANISOU 792 CA ALA A 105 5669 3481 5073 801 -389 19 C
ATOM 793 C ALA A 105 25.012 -30.860 23.206 1.00 38.51 C
ANISOU 793 C ALA A 105 5844 3590 5196 998 -440 -105 C
ATOM 794 O ALA A 105 24.973 -32.054 22.878 1.00 44.01 O
ANISOU 794 O ALA A 105 6655 4074 5993 1048 -504 -143 O
ATOM 795 CB ALA A 105 22.888 -29.712 22.491 1.00 36.67 C
ANISOU 795 CB ALA A 105 5533 3405 4994 666 -386 -85 C
ATOM 796 N ILE A 106 26.148 -30.159 23.200 1.00 37.77 N
ANISOU 796 N ILE A 106 5658 3707 4987 1112 -416 -168 N
ATOM 797 CA ILE A 106 27.402 -30.738 22.725 1.00 42.01 C
ANISOU 797 CA ILE A 106 6208 4256 5498 1308 -459 -294 C
ATOM 798 C ILE A 106 28.373 -31.071 23.865 1.00 39.59 C
ANISOU 798 C ILE A 106 5912 3976 5154 1468 -470 -209 C
ATOM 799 O ILE A 106 29.207 -31.977 23.703 1.00 41.09 O
ANISOU 799 O ILE A 106 6159 4088 5364 1643 -524 -276 O
ATOM 800 CB ILE A 106 28.099 -29.827 21.689 1.00 53.74 C
ANISOU 800 CB ILE A 106 7572 5970 6879 1335 -430 -451 C
ATOM 801 CG1 ILE A 106 29.113 -30.649 20.863 1.00 42.78 C
ANISOU 801 CG1 ILE A 106 6210 4559 5485 1520 -481 -613 C
ATOM 802 CG2 ILE A 106 28.797 -28.659 22.341 1.00 36.56 C
ANISOU 802 CG2 ILE A 106 5268 4038 4585 1347 -373 -407 C
ATOM 803 CD1 ILE A 106 29.680 -29.914 19.664 1.00 38.59 C
ANISOU 803 CD1 ILE A 106 5569 4237 4856 1536 -453 -772 C
ATOM 804 N ARG A 107 28.275 -30.406 25.021 1.00 43.46 N
ANISOU 804 N ARG A 107 6353 4571 5590 1424 -426 -67 N
ATOM 805 CA ARG A 107 29.124 -30.686 26.177 1.00 39.54 C
ANISOU 805 CA ARG A 107 5863 4113 5047 1571 -439 24 C
ATOM 806 C ARG A 107 28.600 -31.851 26.992 1.00 48.00 C
ANISOU 806 C ARG A 107 7080 4943 6216 1587 -477 176 C
ATOM 807 O ARG A 107 29.402 -32.635 27.498 1.00 53.18 O
ANISOU 807 O ARG A 107 7794 5539 6872 1761 -522 206 O
ATOM 808 CB ARG A 107 29.231 -29.458 27.079 1.00 42.24 C
ANISOU 808 CB ARG A 107 6090 4679 5280 1518 -380 104 C
ATOM 809 CG ARG A 107 30.389 -29.488 28.076 1.00 51.44 C
ANISOU 809 CG ARG A 107 7218 5966 6360 1688 -395 147 C
ATOM 810 CD ARG A 107 31.733 -29.441 27.373 1.00 53.85 C
ANISOU 810 CD ARG A 107 7447 6408 6608 1844 -418 -16 C
ATOM 811 NE ARG A 107 32.799 -29.075 28.295 1.00 73.45 N
ANISOU 811 NE ARG A 107 9844 9076 8987 1969 -422 10 N
ATOM 812 CZ ARG A 107 34.088 -29.051 27.983 1.00 97.85 C
ANISOU 812 CZ ARG A 107 12851 12315 12013 2123 -443 -106 C
ATOM 813 NH1 ARG A 107 34.512 -29.374 26.772 1.00 82.68 N
ANISOU 813 NH1 ARG A 107 10919 10384 10111 2182 -458 -258 N
ATOM 814 NH2 ARG A 107 34.973 -28.698 28.911 1.00 99.11 N
ANISOU 814 NH2 ARG A 107 12928 12649 12080 2223 -450 -74 N
ATOM 815 N ILE A 108 27.281 -31.968 27.143 1.00 50.61 N
ANISOU 815 N ILE A 108 7466 5138 6625 1410 -458 279 N
ATOM 816 CA ILE A 108 26.667 -33.035 27.935 1.00 47.24 C
ANISOU 816 CA ILE A 108 7174 4479 6296 1391 -485 446 C
ATOM 817 C ILE A 108 25.429 -33.553 27.211 1.00 50.54 C
ANISOU 817 C ILE A 108 7667 4688 6848 1222 -500 436 C
ATOM 818 O ILE A 108 24.312 -33.432 27.737 1.00 42.81 O
ANISOU 818 O ILE A 108 6695 3663 5906 1056 -463 574 O
ATOM 819 CB ILE A 108 26.308 -32.551 29.350 1.00 42.18 C
ANISOU 819 CB ILE A 108 6501 3937 5589 1338 -432 644 C
ATOM 820 CG1 ILE A 108 25.688 -31.152 29.304 1.00 40.27 C
ANISOU 820 CG1 ILE A 108 6128 3901 5273 1183 -359 630 C
ATOM 821 CG2 ILE A 108 27.529 -32.565 30.251 1.00 42.71 C
ANISOU 821 CG2 ILE A 108 6546 4126 5555 1534 -447 685 C
ATOM 822 CD1 ILE A 108 25.142 -30.685 30.635 1.00 47.47 C
ANISOU 822 CD1 ILE A 108 7009 4902 6123 1116 -305 813 C
ATOM 823 N PRO A 109 25.571 -34.145 26.021 1.00 48.82 N
ANISOU 823 N PRO A 109 7501 4348 6703 1259 -556 272 N
ATOM 824 CA PRO A 109 24.375 -34.572 25.272 1.00 48.32 C
ANISOU 824 CA PRO A 109 7496 4102 6763 1088 -576 242 C
ATOM 825 C PRO A 109 23.541 -35.623 25.987 1.00 49.91 C
ANISOU 825 C PRO A 109 7829 4038 7096 1004 -602 416 C
ATOM 826 O PRO A 109 22.334 -35.719 25.732 1.00 48.17 O
ANISOU 826 O PRO A 109 7623 3716 6962 811 -596 451 O
ATOM 827 CB PRO A 109 24.963 -35.116 23.962 1.00 44.88 C
ANISOU 827 CB PRO A 109 7098 3593 6361 1197 -643 21 C
ATOM 828 CG PRO A 109 26.355 -35.518 24.313 1.00 45.78 C
ANISOU 828 CG PRO A 109 7234 3739 6421 1440 -674 -8 C
ATOM 829 CD PRO A 109 26.818 -34.527 25.337 1.00 46.00 C
ANISOU 829 CD PRO A 109 7151 4011 6318 1464 -607 104 C
ATOM 830 N LEU A 110 24.145 -36.417 26.875 1.00 59.52 N
ANISOU 830 N LEU A 110 9140 5143 8331 1139 -633 531 N
ATOM 831 CA LEU A 110 23.384 -37.443 27.581 1.00 57.09 C
ANISOU 831 CA LEU A 110 8965 4575 8150 1056 -656 717 C
ATOM 832 C LEU A 110 22.429 -36.836 28.601 1.00 58.54 C
ANISOU 832 C LEU A 110 9087 4860 8295 884 -573 923 C
ATOM 833 O LEU A 110 21.380 -37.422 28.892 1.00 58.09 O
ANISOU 833 O LEU A 110 9097 4624 8349 725 -571 1058 O
ATOM 834 CB LEU A 110 24.335 -38.423 28.268 1.00 57.81 C
ANISOU 834 CB LEU A 110 9177 4527 8260 1264 -712 795 C
ATOM 835 CG LEU A 110 25.290 -39.206 27.363 1.00 72.20 C
ANISOU 835 CG LEU A 110 11079 6221 10132 1460 -802 601 C
ATOM 836 CD1 LEU A 110 26.239 -40.062 28.190 1.00 57.54 C
ANISOU 836 CD1 LEU A 110 9330 4256 8278 1680 -854 699 C
ATOM 837 CD2 LEU A 110 24.515 -40.064 26.374 1.00 53.82 C
ANISOU 837 CD2 LEU A 110 8860 3616 7975 1351 -867 502 C
ATOM 838 N ARG A 111 22.768 -35.670 29.147 1.00 57.49 N
ANISOU 838 N ARG A 111 8823 5014 8008 912 -505 947 N
ATOM 839 CA ARG A 111 21.967 -35.013 30.170 1.00 45.93 C
ANISOU 839 CA ARG A 111 7290 3679 6483 781 -425 1127 C
ATOM 840 C ARG A 111 21.171 -33.832 29.628 1.00 52.67 C
ANISOU 840 C ARG A 111 8008 4711 7293 621 -367 1048 C
ATOM 841 O ARG A 111 20.551 -33.106 30.412 1.00 50.22 O
ANISOU 841 O ARG A 111 7620 4546 6914 527 -297 1167 O
ATOM 842 CB ARG A 111 22.867 -34.553 31.319 1.00 49.54 C
ANISOU 842 CB ARG A 111 7702 4327 6795 931 -395 1220 C
ATOM 843 CG ARG A 111 23.576 -35.688 32.043 1.00 61.06 C
ANISOU 843 CG ARG A 111 9292 5625 8283 1093 -449 1336 C
ATOM 844 CD ARG A 111 24.556 -35.161 33.080 1.00 73.34 C
ANISOU 844 CD ARG A 111 10786 7402 9679 1257 -429 1398 C
ATOM 845 NE ARG A 111 25.943 -35.342 32.664 1.00 96.60 N
ANISOU 845 NE ARG A 111 13734 10383 12587 1478 -489 1250 N
ATOM 846 CZ ARG A 111 26.993 -34.918 33.354 1.00 95.23 C
ANISOU 846 CZ ARG A 111 13497 10407 12279 1644 -489 1256 C
ATOM 847 NH1 ARG A 111 26.852 -34.264 34.496 1.00 87.07 N
ANISOU 847 NH1 ARG A 111 12397 9555 11130 1621 -435 1392 N
ATOM 848 NH2 ARG A 111 28.215 -35.155 32.887 1.00 96.22 N
ANISOU 848 NH2 ARG A 111 13618 10560 12382 1841 -546 1114 N
ATOM 849 N TYR A 112 21.168 -33.628 28.309 1.00 54.16 N
ANISOU 849 N TYR A 112 8170 4895 7515 597 -396 850 N
ATOM 850 CA TYR A 112 20.516 -32.452 27.739 1.00 41.25 C
ANISOU 850 CA TYR A 112 6407 3437 5827 469 -347 769 C
ATOM 851 C TYR A 112 19.005 -32.508 27.925 1.00 47.85 C
ANISOU 851 C TYR A 112 7234 4207 6740 253 -316 882 C
ATOM 852 O TYR A 112 18.391 -31.541 28.390 1.00 40.28 O
ANISOU 852 O TYR A 112 6172 3423 5709 163 -248 947 O
ATOM 853 CB TYR A 112 20.872 -32.324 26.256 1.00 40.70 C
ANISOU 853 CB TYR A 112 6320 3373 5771 500 -390 541 C
ATOM 854 CG TYR A 112 20.099 -31.242 25.535 1.00 39.03 C
ANISOU 854 CG TYR A 112 5996 3309 5523 362 -352 462 C
ATOM 855 CD1 TYR A 112 20.531 -29.923 25.550 1.00 37.19 C
ANISOU 855 CD1 TYR A 112 5644 3328 5158 392 -301 416 C
ATOM 856 CD2 TYR A 112 18.937 -31.542 24.835 1.00 39.42 C
ANISOU 856 CD2 TYR A 112 6062 3243 5674 201 -372 434 C
ATOM 857 CE1 TYR A 112 19.825 -28.933 24.892 1.00 36.64 C
ANISOU 857 CE1 TYR A 112 5483 3381 5058 275 -270 352 C
ATOM 858 CE2 TYR A 112 18.224 -30.560 24.177 1.00 38.01 C
ANISOU 858 CE2 TYR A 112 5781 3204 5457 88 -342 366 C
ATOM 859 CZ TYR A 112 18.671 -29.258 24.208 1.00 41.44 C
ANISOU 859 CZ TYR A 112 6108 3880 5760 130 -291 330 C
ATOM 860 OH TYR A 112 17.962 -28.280 23.551 1.00 34.94 O
ANISOU 860 OH TYR A 112 5192 3182 4901 26 -266 270 O
ATOM 861 N ASN A 113 18.385 -33.635 27.561 1.00 52.03 N
ANISOU 861 N ASN A 113 7866 4483 7419 169 -367 901 N
ATOM 862 CA ASN A 113 16.928 -33.722 27.592 1.00 50.41 C
ANISOU 862 CA ASN A 113 7640 4217 7298 -50 -342 990 C
ATOM 863 C ASN A 113 16.381 -33.602 29.008 1.00 64.86 C
ANISOU 863 C ASN A 113 9445 6110 9089 -117 -271 1227 C
ATOM 864 O ASN A 113 15.280 -33.072 29.204 1.00 63.94 O
ANISOU 864 O ASN A 113 9240 6087 8967 -276 -216 1294 O
ATOM 865 CB ASN A 113 16.469 -35.030 26.949 1.00 52.15 C
ANISOU 865 CB ASN A 113 7982 4137 7696 -127 -421 959 C
ATOM 866 CG ASN A 113 16.693 -35.048 25.450 1.00 61.87 C
ANISOU 866 CG ASN A 113 9215 5332 8959 -99 -486 713 C
ATOM 867 OD1 ASN A 113 16.536 -34.029 24.777 1.00 56.69 O
ANISOU 867 OD1 ASN A 113 8447 4868 8224 -128 -461 596 O
ATOM 868 ND2 ASN A 113 17.066 -36.208 24.919 1.00 62.83 N
ANISOU 868 ND2 ASN A 113 9469 5208 9194 -38 -573 633 N
ATOM 869 N GLY A 114 17.127 -34.080 30.006 1.00 52.05 N
ANISOU 869 N GLY A 114 7894 4452 7432 9 -270 1355 N
ATOM 870 CA GLY A 114 16.688 -33.924 31.381 1.00 45.30 C
ANISOU 870 CA GLY A 114 7012 3687 6515 -36 -199 1580 C
ATOM 871 C GLY A 114 16.907 -32.533 31.934 1.00 54.91 C
ANISOU 871 C GLY A 114 8092 5214 7557 14 -128 1572 C
ATOM 872 O GLY A 114 16.149 -32.084 32.799 1.00 56.88 O
ANISOU 872 O GLY A 114 8273 5589 7750 -76 -57 1713 O
ATOM 873 N LEU A 115 17.929 -31.830 31.446 1.00 48.91 N
ANISOU 873 N LEU A 115 7288 4585 6712 152 -146 1405 N
ATOM 874 CA LEU A 115 18.276 -30.507 31.952 1.00 40.11 C
ANISOU 874 CA LEU A 115 6053 3748 5440 208 -91 1382 C
ATOM 875 C LEU A 115 17.514 -29.396 31.237 1.00 47.98 C
ANISOU 875 C LEU A 115 6933 4881 6415 88 -57 1273 C
ATOM 876 O LEU A 115 16.973 -28.494 31.885 1.00 48.44 O
ANISOU 876 O LEU A 115 6899 5115 6389 36 6 1334 O
ATOM 877 CB LEU A 115 19.787 -30.281 31.826 1.00 39.56 C
ANISOU 877 CB LEU A 115 5985 3757 5290 408 -128 1266 C
ATOM 878 CG LEU A 115 20.306 -28.846 31.973 1.00 60.73 C
ANISOU 878 CG LEU A 115 8540 6708 7827 461 -90 1178 C
ATOM 879 CD1 LEU A 115 19.984 -28.290 33.347 1.00 57.31 C
ANISOU 879 CD1 LEU A 115 8054 6434 7290 451 -28 1328 C
ATOM 880 CD2 LEU A 115 21.804 -28.770 31.705 1.00 70.87 C
ANISOU 880 CD2 LEU A 115 9823 8052 9054 642 -133 1056 C
ATOM 881 N VAL A 116 17.460 -29.449 29.911 1.00 46.04 N
ANISOU 881 N VAL A 116 6692 4559 6240 54 -101 1111 N
ATOM 882 CA VAL A 116 16.877 -28.395 29.089 1.00 36.41 C
ANISOU 882 CA VAL A 116 5371 3468 4997 -36 -80 994 C
ATOM 883 C VAL A 116 15.530 -28.903 28.589 1.00 49.69 C
ANISOU 883 C VAL A 116 7061 5020 6797 -214 -88 1021 C
ATOM 884 O VAL A 116 15.460 -29.666 27.619 1.00 64.09 O
ANISOU 884 O VAL A 116 8949 6676 8726 -243 -150 930 O
ATOM 885 CB VAL A 116 17.802 -28.009 27.929 1.00 51.51 C
ANISOU 885 CB VAL A 116 7271 5419 6882 56 -121 793 C
ATOM 886 CG1 VAL A 116 17.246 -26.820 27.178 1.00 36.77 C
ANISOU 886 CG1 VAL A 116 5300 3699 4974 -26 -97 694 C
ATOM 887 CG2 VAL A 116 19.204 -27.712 28.445 1.00 37.24 C
ANISOU 887 CG2 VAL A 116 5458 3720 4972 232 -121 772 C
ATOM 888 N THR A 117 14.453 -28.479 29.245 1.00 44.77 N
ANISOU 888 N THR A 117 6366 4486 6158 -333 -29 1139 N
ATOM 889 CA THR A 117 13.102 -28.898 28.903 1.00 42.03 C
ANISOU 889 CA THR A 117 6004 4049 5918 -515 -29 1180 C
ATOM 890 C THR A 117 12.290 -27.711 28.401 1.00 39.18 C
ANISOU 890 C THR A 117 5514 3863 5508 -596 2 1104 C
ATOM 891 O THR A 117 12.658 -26.550 28.594 1.00 40.48 O
ANISOU 891 O THR A 117 5607 4219 5556 -522 37 1060 O
ATOM 892 CB THR A 117 12.395 -29.529 30.108 1.00 53.53 C
ANISOU 892 CB THR A 117 7477 5459 7403 -600 17 1402 C
ATOM 893 OG1 THR A 117 12.109 -28.514 31.078 1.00 47.56 O
ANISOU 893 OG1 THR A 117 6617 4934 6518 -590 96 1488 O
ATOM 894 CG2 THR A 117 13.273 -30.598 30.746 1.00 40.97 C
ANISOU 894 CG2 THR A 117 6016 3709 5840 -498 -11 1500 C
ATOM 895 N GLY A 118 11.163 -28.023 27.758 1.00 49.04 N
ANISOU 895 N GLY A 118 6737 5041 6854 -749 -16 1088 N
ATOM 896 CA GLY A 118 10.316 -26.971 27.220 1.00 36.00 C
ANISOU 896 CA GLY A 118 4966 3548 5165 -823 5 1016 C
ATOM 897 C GLY A 118 9.678 -26.118 28.301 1.00 48.03 C
ANISOU 897 C GLY A 118 6387 5264 6599 -848 88 1136 C
ATOM 898 O GLY A 118 9.495 -24.910 28.124 1.00 36.02 O
ANISOU 898 O GLY A 118 4776 3918 4994 -824 113 1070 O
ATOM 899 N THR A 119 9.328 -26.732 29.433 1.00 43.52 N
ANISOU 899 N THR A 119 5830 4663 6041 -893 132 1316 N
ATOM 900 CA THR A 119 8.745 -25.972 30.534 1.00 44.14 C
ANISOU 900 CA THR A 119 5811 4940 6021 -904 215 1432 C
ATOM 901 C THR A 119 9.738 -24.962 31.092 1.00 36.10 C
ANISOU 901 C THR A 119 4777 4080 4858 -740 240 1393 C
ATOM 902 O THR A 119 9.378 -23.812 31.369 1.00 43.03 O
ANISOU 902 O THR A 119 5557 5148 5644 -722 283 1370 O
ATOM 903 CB THR A 119 8.273 -26.922 31.634 1.00 38.71 C
ANISOU 903 CB THR A 119 5150 4190 5368 -980 258 1643 C
ATOM 904 OG1 THR A 119 7.335 -27.858 31.087 1.00 67.63 O
ANISOU 904 OG1 THR A 119 8823 7695 9178 -1151 230 1675 O
ATOM 905 CG2 THR A 119 7.605 -26.141 32.753 1.00 45.22 C
ANISOU 905 CG2 THR A 119 5862 5243 6078 -990 349 1757 C
ATOM 906 N ARG A 120 10.997 -25.370 31.261 1.00 40.09 N
ANISOU 906 N ARG A 120 5378 4510 5345 -617 210 1380 N
ATOM 907 CA ARG A 120 12.008 -24.437 31.744 1.00 38.37 C
ANISOU 907 CA ARG A 120 5141 4441 4997 -468 225 1331 C
ATOM 908 C ARG A 120 12.334 -23.375 30.704 1.00 43.47 C
ANISOU 908 C ARG A 120 5741 5163 5613 -432 198 1147 C
ATOM 909 O ARG A 120 12.627 -22.230 31.064 1.00 45.89 O
ANISOU 909 O ARG A 120 5987 5634 5815 -364 225 1106 O
ATOM 910 CB ARG A 120 13.269 -25.198 32.149 1.00 41.85 C
ANISOU 910 CB ARG A 120 5686 4787 5428 -344 194 1361 C
ATOM 911 CG ARG A 120 13.054 -26.171 33.295 1.00 36.38 C
ANISOU 911 CG ARG A 120 5046 4029 4746 -360 222 1562 C
ATOM 912 CD ARG A 120 14.254 -27.078 33.485 1.00 40.06 C
ANISOU 912 CD ARG A 120 5629 4363 5227 -236 174 1584 C
ATOM 913 NE ARG A 120 14.038 -28.047 34.552 1.00 39.59 N
ANISOU 913 NE ARG A 120 5634 4226 5182 -251 198 1792 N
ATOM 914 CZ ARG A 120 14.889 -29.014 34.867 1.00 40.25 C
ANISOU 914 CZ ARG A 120 5831 4172 5291 -154 157 1855 C
ATOM 915 NH1 ARG A 120 16.022 -29.179 34.204 1.00 51.72 N
ANISOU 915 NH1 ARG A 120 7340 5554 6759 -28 92 1718 N
ATOM 916 NH2 ARG A 120 14.594 -29.836 35.869 1.00 55.41 N
ANISOU 916 NH2 ARG A 120 7808 6028 7218 -178 184 2064 N
ATOM 917 N ALA A 121 12.277 -23.725 29.417 1.00 33.61 N
ANISOU 917 N ALA A 121 4522 3797 4452 -477 144 1037 N
ATOM 918 CA ALA A 121 12.567 -22.751 28.369 1.00 33.58 C
ANISOU 918 CA ALA A 121 4478 3867 4415 -448 120 877 C
ATOM 919 C ALA A 121 11.541 -21.625 28.366 1.00 41.85 C
ANISOU 919 C ALA A 121 5417 5063 5420 -511 157 869 C
ATOM 920 O ALA A 121 11.899 -20.444 28.300 1.00 37.25 O
ANISOU 920 O ALA A 121 4788 4609 4756 -450 168 798 O
ATOM 921 CB ALA A 121 12.612 -23.443 27.008 1.00 31.09 C
ANISOU 921 CB ALA A 121 4214 3404 4194 -485 55 767 C
ATOM 922 N LYS A 122 10.252 -21.976 28.438 1.00 30.86 N
ANISOU 922 N LYS A 122 3984 3655 4088 -635 174 941 N
ATOM 923 CA LYS A 122 9.203 -20.960 28.449 1.00 41.50 C
ANISOU 923 CA LYS A 122 5221 5149 5397 -686 207 935 C
ATOM 924 C LYS A 122 9.334 -20.047 29.660 1.00 39.25 C
ANISOU 924 C LYS A 122 4886 5031 4997 -609 266 993 C
ATOM 925 O LYS A 122 9.050 -18.846 29.575 1.00 34.66 O
ANISOU 925 O LYS A 122 4235 4581 4354 -582 280 933 O
ATOM 926 CB LYS A 122 7.825 -21.622 28.425 1.00 39.56 C
ANISOU 926 CB LYS A 122 4930 4866 5236 -834 217 1014 C
ATOM 927 CG LYS A 122 7.551 -22.431 27.171 1.00 32.15 C
ANISOU 927 CG LYS A 122 4029 3773 4412 -921 150 936 C
ATOM 928 CD LYS A 122 6.210 -23.136 27.240 1.00 50.70 C
ANISOU 928 CD LYS A 122 6327 6084 6854 -1081 158 1020 C
ATOM 929 CE LYS A 122 5.978 -23.985 25.998 1.00 71.66 C
ANISOU 929 CE LYS A 122 9026 8576 9627 -1168 79 928 C
ATOM 930 NZ LYS A 122 4.686 -24.720 26.050 1.00 98.60 N
ANISOU 930 NZ LYS A 122 12384 11941 13140 -1341 80 1006 N
ATOM 931 N GLY A 123 9.755 -20.599 30.800 1.00 30.64 N
ANISOU 931 N GLY A 123 3833 3936 3874 -568 298 1107 N
ATOM 932 CA GLY A 123 10.011 -19.764 31.960 1.00 33.24 C
ANISOU 932 CA GLY A 123 4120 4429 4082 -479 346 1147 C
ATOM 933 C GLY A 123 11.163 -18.805 31.735 1.00 35.69 C
ANISOU 933 C GLY A 123 4445 4795 4322 -362 320 1023 C
ATOM 934 O GLY A 123 11.090 -17.633 32.111 1.00 34.93 O
ANISOU 934 O GLY A 123 4288 4839 4144 -315 342 981 O
ATOM 935 N ILE A 124 12.243 -19.290 31.116 1.00 38.47 N
ANISOU 935 N ILE A 124 4873 5037 4708 -316 272 960 N
ATOM 936 CA ILE A 124 13.370 -18.420 30.787 1.00 32.15 C
ANISOU 936 CA ILE A 124 4077 4289 3848 -222 247 842 C
ATOM 937 C ILE A 124 12.924 -17.302 29.857 1.00 32.20 C
ANISOU 937 C ILE A 124 4029 4351 3854 -256 237 735 C
ATOM 938 O ILE A 124 13.293 -16.136 30.040 1.00 30.25 O
ANISOU 938 O ILE A 124 3747 4209 3538 -202 243 675 O
ATOM 939 CB ILE A 124 14.518 -19.237 30.168 1.00 27.69 C
ANISOU 939 CB ILE A 124 3593 3604 3325 -171 199 791 C
ATOM 940 CG1 ILE A 124 15.075 -20.239 31.179 1.00 38.70 C
ANISOU 940 CG1 ILE A 124 5046 4950 4708 -111 204 900 C
ATOM 941 CG2 ILE A 124 15.620 -18.315 29.672 1.00 26.59 C
ANISOU 941 CG2 ILE A 124 3441 3531 3131 -95 177 666 C
ATOM 942 CD1 ILE A 124 15.751 -19.597 32.359 1.00 61.99 C
ANISOU 942 CD1 ILE A 124 7969 8042 7543 -12 228 927 C
ATOM 943 N ILE A 125 12.120 -17.637 28.846 1.00 35.33 N
ANISOU 943 N ILE A 125 4420 4674 4329 -346 216 710 N
ATOM 944 CA ILE A 125 11.675 -16.634 27.884 1.00 35.53 C
ANISOU 944 CA ILE A 125 4400 4748 4353 -373 200 616 C
ATOM 945 C ILE A 125 10.780 -15.602 28.559 1.00 32.46 C
ANISOU 945 C ILE A 125 3930 4493 3910 -375 239 644 C
ATOM 946 O ILE A 125 10.897 -14.397 28.304 1.00 29.51 O
ANISOU 946 O ILE A 125 3528 4192 3491 -337 233 572 O
ATOM 947 CB ILE A 125 10.968 -17.316 26.700 1.00 35.49 C
ANISOU 947 CB ILE A 125 4404 4644 4438 -465 164 584 C
ATOM 948 CG1 ILE A 125 11.959 -18.192 25.933 1.00 29.44 C
ANISOU 948 CG1 ILE A 125 3719 3754 3713 -440 119 525 C
ATOM 949 CG2 ILE A 125 10.333 -16.280 25.782 1.00 27.37 C
ANISOU 949 CG2 ILE A 125 3319 3680 3398 -491 148 507 C
ATOM 950 CD1 ILE A 125 11.313 -19.076 24.894 1.00 30.80 C
ANISOU 950 CD1 ILE A 125 3912 3814 3978 -526 76 491 C
ATOM 951 N ALA A 126 9.879 -16.053 29.435 1.00 33.00 N
ANISOU 951 N ALA A 126 3961 4596 3982 -417 280 751 N
ATOM 952 CA ALA A 126 8.999 -15.126 30.137 1.00 26.58 C
ANISOU 952 CA ALA A 126 3063 3925 3109 -406 321 775 C
ATOM 953 C ALA A 126 9.791 -14.190 31.042 1.00 36.37 C
ANISOU 953 C ALA A 126 4304 5266 4250 -296 337 748 C
ATOM 954 O ALA A 126 9.491 -12.993 31.123 1.00 39.71 O
ANISOU 954 O ALA A 126 4680 5783 4626 -257 342 691 O
ATOM 955 CB ALA A 126 7.959 -15.901 30.945 1.00 27.85 C
ANISOU 955 CB ALA A 126 3178 4117 3286 -475 369 905 C
ATOM 956 N ILE A 127 10.805 -14.718 31.730 1.00 32.11 N
ANISOU 956 N ILE A 127 3818 4705 3679 -241 341 785 N
ATOM 957 CA ILE A 127 11.627 -13.884 32.601 1.00 25.93 C
ANISOU 957 CA ILE A 127 3032 4021 2800 -139 348 750 C
ATOM 958 C ILE A 127 12.421 -12.874 31.781 1.00 31.14 C
ANISOU 958 C ILE A 127 3706 4669 3457 -105 305 619 C
ATOM 959 O ILE A 127 12.522 -11.697 32.149 1.00 29.23 O
ANISOU 959 O ILE A 127 3435 4514 3157 -54 306 559 O
ATOM 960 CB ILE A 127 12.549 -14.764 33.466 1.00 42.79 C
ANISOU 960 CB ILE A 127 5218 6138 4901 -85 353 822 C
ATOM 961 CG1 ILE A 127 11.727 -15.587 34.461 1.00 40.83 C
ANISOU 961 CG1 ILE A 127 4951 5925 4636 -116 404 971 C
ATOM 962 CG2 ILE A 127 13.580 -13.914 34.194 1.00 33.09 C
ANISOU 962 CG2 ILE A 127 3988 5006 3578 20 344 761 C
ATOM 963 CD1 ILE A 127 12.548 -16.579 35.261 1.00 34.09 C
ANISOU 963 CD1 ILE A 127 4159 5038 3756 -65 407 1063 C
ATOM 964 N CYS A 128 12.983 -13.311 30.652 1.00 24.44 N
ANISOU 964 N CYS A 128 2904 3712 2670 -134 268 572 N
ATOM 965 CA CYS A 128 13.816 -12.425 29.847 1.00 24.81 C
ANISOU 965 CA CYS A 128 2963 3754 2711 -110 233 463 C
ATOM 966 C CYS A 128 13.004 -11.307 29.201 1.00 32.35 C
ANISOU 966 C CYS A 128 3879 4739 3673 -139 226 410 C
ATOM 967 O CYS A 128 13.542 -10.225 28.942 1.00 31.54 O
ANISOU 967 O CYS A 128 3776 4662 3544 -111 208 336 O
ATOM 968 CB CYS A 128 14.562 -13.233 28.785 1.00 24.11 C
ANISOU 968 CB CYS A 128 2926 3560 2675 -128 201 428 C
ATOM 969 SG CYS A 128 15.786 -14.388 29.465 1.00 66.13 S
ANISOU 969 SG CYS A 128 8299 8842 7983 -61 196 469 S
ATOM 970 N TRP A 129 11.717 -11.541 28.932 1.00 30.03 N
ANISOU 970 N TRP A 129 3551 4442 3416 -197 238 448 N
ATOM 971 CA TRP A 129 10.878 -10.466 28.411 1.00 31.30 C
ANISOU 971 CA TRP A 129 3671 4644 3578 -208 228 404 C
ATOM 972 C TRP A 129 10.618 -9.406 29.474 1.00 30.74 C
ANISOU 972 C TRP A 129 3560 4680 3440 -142 251 395 C
ATOM 973 O TRP A 129 10.622 -8.207 29.174 1.00 35.71 O
ANISOU 973 O TRP A 129 4185 5329 4055 -111 230 328 O
ATOM 974 CB TRP A 129 9.563 -11.029 27.872 1.00 38.28 C
ANISOU 974 CB TRP A 129 4515 5514 4517 -284 230 443 C
ATOM 975 CG TRP A 129 9.651 -11.443 26.436 1.00 44.61 C
ANISOU 975 CG TRP A 129 5347 6225 5377 -338 188 399 C
ATOM 976 CD1 TRP A 129 9.768 -12.713 25.952 1.00 37.01 C
ANISOU 976 CD1 TRP A 129 4419 5172 4471 -393 173 418 C
ATOM 977 CD2 TRP A 129 9.644 -10.577 25.295 1.00 35.23 C
ANISOU 977 CD2 TRP A 129 4164 5033 4190 -338 151 326 C
ATOM 978 NE1 TRP A 129 9.827 -12.693 24.579 1.00 41.00 N
ANISOU 978 NE1 TRP A 129 4944 5628 5005 -422 130 350 N
ATOM 979 CE2 TRP A 129 9.753 -11.394 24.150 1.00 35.69 C
ANISOU 979 CE2 TRP A 129 4253 5013 4296 -390 118 301 C
ATOM 980 CE3 TRP A 129 9.552 -9.192 25.129 1.00 22.43 C
ANISOU 980 CE3 TRP A 129 2528 3460 2533 -295 141 282 C
ATOM 981 CZ2 TRP A 129 9.775 -10.871 22.858 1.00 28.38 C
ANISOU 981 CZ2 TRP A 129 3336 4076 3369 -400 80 238 C
ATOM 982 CZ3 TRP A 129 9.574 -8.674 23.847 1.00 30.04 C
ANISOU 982 CZ3 TRP A 129 3508 4398 3507 -309 102 232 C
ATOM 983 CH2 TRP A 129 9.685 -9.513 22.727 1.00 38.65 C
ANISOU 983 CH2 TRP A 129 4623 5430 4632 -361 75 213 C
ATOM 984 N VAL A 130 10.394 -9.826 30.722 1.00 29.60 N
ANISOU 984 N VAL A 130 3391 4604 3253 -116 291 463 N
ATOM 985 CA VAL A 130 10.205 -8.867 31.806 1.00 42.98 C
ANISOU 985 CA VAL A 130 5048 6412 4870 -39 312 443 C
ATOM 986 C VAL A 130 11.481 -8.067 32.039 1.00 26.58 C
ANISOU 986 C VAL A 130 3011 4334 2753 23 283 362 C
ATOM 987 O VAL A 130 11.434 -6.857 32.294 1.00 35.87 O
ANISOU 987 O VAL A 130 4175 5557 3897 74 269 292 O
ATOM 988 CB VAL A 130 9.747 -9.590 33.087 1.00 39.30 C
ANISOU 988 CB VAL A 130 4546 6034 4352 -25 365 542 C
ATOM 989 CG1 VAL A 130 9.608 -8.605 34.237 1.00 36.00 C
ANISOU 989 CG1 VAL A 130 4089 5752 3840 68 385 508 C
ATOM 990 CG2 VAL A 130 8.434 -10.314 32.845 1.00 31.12 C
ANISOU 990 CG2 VAL A 130 3457 5005 3363 -104 395 624 C
ATOM 991 N LEU A 131 12.641 -8.722 31.951 1.00 23.40 N
ANISOU 991 N LEU A 131 2656 3878 2357 21 269 366 N
ATOM 992 CA LEU A 131 13.903 -8.005 32.095 1.00 32.08 C
ANISOU 992 CA LEU A 131 3781 4983 3424 67 239 287 C
ATOM 993 C LEU A 131 14.151 -7.058 30.927 1.00 28.82 C
ANISOU 993 C LEU A 131 3386 4509 3054 37 202 207 C
ATOM 994 O LEU A 131 14.727 -5.982 31.118 1.00 35.92 O
ANISOU 994 O LEU A 131 4291 5428 3931 67 179 134 O
ATOM 995 CB LEU A 131 15.062 -8.994 32.227 1.00 23.09 C
ANISOU 995 CB LEU A 131 2678 3814 2282 78 233 313 C
ATOM 996 CG LEU A 131 15.046 -9.890 33.465 1.00 24.65 C
ANISOU 996 CG LEU A 131 2870 4068 2426 121 263 401 C
ATOM 997 CD1 LEU A 131 16.231 -10.844 33.461 1.00 40.06 C
ANISOU 997 CD1 LEU A 131 4863 5976 4381 144 247 420 C
ATOM 998 CD2 LEU A 131 15.037 -9.050 34.725 1.00 27.95 C
ANISOU 998 CD2 LEU A 131 3255 4613 2752 195 273 375 C
ATOM 999 N SER A 132 13.727 -7.433 29.718 1.00 32.50 N
ANISOU 999 N SER A 132 3863 4904 3582 -26 194 220 N
ATOM 1000 CA SER A 132 13.942 -6.564 28.566 1.00 33.41 C
ANISOU 1000 CA SER A 132 3997 4969 3728 -54 161 159 C
ATOM 1001 C SER A 132 13.135 -5.276 28.685 1.00 33.96 C
ANISOU 1001 C SER A 132 4047 5067 3789 -29 152 124 C
ATOM 1002 O SER A 132 13.604 -4.206 28.280 1.00 32.73 O
ANISOU 1002 O SER A 132 3915 4884 3639 -26 123 68 O
ATOM 1003 CB SER A 132 13.591 -7.302 27.275 1.00 28.06 C
ANISOU 1003 CB SER A 132 3333 4225 3104 -117 152 179 C
ATOM 1004 OG SER A 132 14.420 -8.435 27.099 1.00 24.46 O
ANISOU 1004 OG SER A 132 2903 3732 2660 -128 153 194 O
ATOM 1005 N PHE A 133 11.922 -5.357 29.236 1.00 32.24 N
ANISOU 1005 N PHE A 133 3787 4904 3560 -9 175 160 N
ATOM 1006 CA PHE A 133 11.134 -4.148 29.458 1.00 30.43 C
ANISOU 1006 CA PHE A 133 3535 4711 3317 38 165 120 C
ATOM 1007 C PHE A 133 11.798 -3.250 30.493 1.00 32.35 C
ANISOU 1007 C PHE A 133 3788 4993 3510 106 156 58 C
ATOM 1008 O PHE A 133 11.898 -2.033 30.306 1.00 29.71 O
ANISOU 1008 O PHE A 133 3476 4628 3184 131 122 -8 O
ATOM 1009 CB PHE A 133 9.713 -4.513 29.892 1.00 25.23 C
ANISOU 1009 CB PHE A 133 2811 4127 2648 49 198 171 C
ATOM 1010 CG PHE A 133 8.767 -4.742 28.750 1.00 33.52 C
ANISOU 1010 CG PHE A 133 3840 5145 3751 -5 185 195 C
ATOM 1011 CD1 PHE A 133 8.623 -6.002 28.192 1.00 35.46 C
ANISOU 1011 CD1 PHE A 133 4083 5356 4036 -81 195 251 C
ATOM 1012 CD2 PHE A 133 8.016 -3.697 28.236 1.00 36.58 C
ANISOU 1012 CD2 PHE A 133 4213 5536 4148 27 158 157 C
ATOM 1013 CE1 PHE A 133 7.751 -6.215 27.139 1.00 35.10 C
ANISOU 1013 CE1 PHE A 133 4013 5289 4036 -132 176 261 C
ATOM 1014 CE2 PHE A 133 7.141 -3.903 27.183 1.00 41.86 C
ANISOU 1014 CE2 PHE A 133 4857 6190 4858 -16 140 176 C
ATOM 1015 CZ PHE A 133 7.009 -5.164 26.634 1.00 32.39 C
ANISOU 1015 CZ PHE A 133 3647 4966 3693 -98 148 224 C
ATOM 1016 N ALA A 134 12.270 -3.843 31.592 1.00 38.53 N
ANISOU 1016 N ALA A 134 4559 5839 4241 136 181 79 N
ATOM 1017 CA ALA A 134 12.913 -3.063 32.643 1.00 39.20 C
ANISOU 1017 CA ALA A 134 4648 5976 4268 204 167 11 C
ATOM 1018 C ALA A 134 14.200 -2.415 32.146 1.00 27.89 C
ANISOU 1018 C ALA A 134 3261 4472 2862 178 123 -58 C
ATOM 1019 O ALA A 134 14.537 -1.295 32.548 1.00 29.58 O
ANISOU 1019 O ALA A 134 3488 4687 3064 213 91 -140 O
ATOM 1020 CB ALA A 134 13.189 -3.953 33.854 1.00 31.93 C
ANISOU 1020 CB ALA A 134 3705 5149 3278 242 202 59 C
ATOM 1021 N ILE A 135 14.933 -3.100 31.270 1.00 24.57 N
ANISOU 1021 N ILE A 135 2863 3992 2480 115 120 -29 N
ATOM 1022 CA ILE A 135 16.179 -2.542 30.754 1.00 24.97 C
ANISOU 1022 CA ILE A 135 2943 3993 2552 81 86 -86 C
ATOM 1023 C ILE A 135 15.889 -1.457 29.725 1.00 32.78 C
ANISOU 1023 C ILE A 135 3960 4903 3593 43 57 -116 C
ATOM 1024 O ILE A 135 16.424 -0.345 29.802 1.00 22.20 O
ANISOU 1024 O ILE A 135 2639 3532 2261 41 24 -181 O
ATOM 1025 CB ILE A 135 17.062 -3.654 30.162 1.00 31.23 C
ANISOU 1025 CB ILE A 135 3741 4765 3358 39 95 -49 C
ATOM 1026 CG1 ILE A 135 17.588 -4.567 31.270 1.00 27.46 C
ANISOU 1026 CG1 ILE A 135 3247 4360 2828 88 112 -24 C
ATOM 1027 CG2 ILE A 135 18.210 -3.054 29.364 1.00 27.48 C
ANISOU 1027 CG2 ILE A 135 3284 4249 2909 -10 67 -98 C
ATOM 1028 CD1 ILE A 135 18.315 -5.788 30.753 1.00 22.54 C
ANISOU 1028 CD1 ILE A 135 2634 3711 2220 68 119 16 C
ATOM 1029 N GLY A 136 15.033 -1.763 28.748 1.00 24.60 N
ANISOU 1029 N GLY A 136 2926 3829 2591 12 66 -68 N
ATOM 1030 CA GLY A 136 14.791 -0.829 27.663 1.00 24.59 C
ANISOU 1030 CA GLY A 136 2956 3755 2632 -21 37 -82 C
ATOM 1031 C GLY A 136 14.061 0.429 28.087 1.00 27.42 C
ANISOU 1031 C GLY A 136 3324 4102 2994 34 13 -125 C
ATOM 1032 O GLY A 136 14.265 1.493 27.498 1.00 23.54 O
ANISOU 1032 O GLY A 136 2874 3536 2536 15 -22 -152 O
ATOM 1033 N LEU A 137 13.207 0.330 29.104 1.00 22.49 N
ANISOU 1033 N LEU A 137 2663 3549 2335 104 30 -130 N
ATOM 1034 CA LEU A 137 12.416 1.455 29.581 1.00 23.11 C
ANISOU 1034 CA LEU A 137 2744 3630 2409 178 8 -182 C
ATOM 1035 C LEU A 137 12.988 2.087 30.841 1.00 23.65 C
ANISOU 1035 C LEU A 137 2815 3733 2437 236 -7 -263 C
ATOM 1036 O LEU A 137 12.284 2.850 31.510 1.00 27.20 O
ANISOU 1036 O LEU A 137 3258 4211 2866 320 -20 -316 O
ATOM 1037 CB LEU A 137 10.974 1.016 29.832 1.00 23.37 C
ANISOU 1037 CB LEU A 137 2719 3740 2420 226 38 -142 C
ATOM 1038 CG LEU A 137 10.290 0.302 28.668 1.00 22.99 C
ANISOU 1038 CG LEU A 137 2655 3673 2408 168 48 -70 C
ATOM 1039 CD1 LEU A 137 8.872 -0.103 29.044 1.00 26.34 C
ANISOU 1039 CD1 LEU A 137 3007 4190 2813 209 78 -36 C
ATOM 1040 CD2 LEU A 137 10.298 1.190 27.432 1.00 22.93 C
ANISOU 1040 CD2 LEU A 137 2697 3566 2448 145 3 -81 C
ATOM 1041 N THR A 138 14.239 1.784 31.182 1.00 23.48 N
ANISOU 1041 N THR A 138 2801 3719 2400 202 -9 -281 N
ATOM 1042 CA THR A 138 14.897 2.446 32.306 1.00 32.73 C
ANISOU 1042 CA THR A 138 3977 4924 3535 250 -36 -371 C
ATOM 1043 C THR A 138 14.890 3.969 32.210 1.00 24.71 C
ANISOU 1043 C THR A 138 3010 3816 2561 267 -93 -459 C
ATOM 1044 O THR A 138 14.722 4.618 33.257 1.00 30.51 O
ANISOU 1044 O THR A 138 3742 4591 3260 348 -114 -544 O
ATOM 1045 CB THR A 138 16.334 1.915 32.445 1.00 26.45 C
ANISOU 1045 CB THR A 138 3178 4146 2727 197 -38 -376 C
ATOM 1046 OG1 THR A 138 16.300 0.572 32.943 1.00 45.88 O
ANISOU 1046 OG1 THR A 138 5598 6699 5134 216 8 -309 O
ATOM 1047 CG2 THR A 138 17.154 2.778 33.393 1.00 24.53 C
ANISOU 1047 CG2 THR A 138 2941 3920 2460 226 -82 -484 C
ATOM 1048 N PRO A 139 15.061 4.601 31.040 1.00 24.58 N
ANISOU 1048 N PRO A 139 3043 3679 2619 201 -121 -444 N
ATOM 1049 CA PRO A 139 14.934 6.066 30.994 1.00 27.53 C
ANISOU 1049 CA PRO A 139 3473 3947 3039 224 -179 -518 C
ATOM 1050 C PRO A 139 13.607 6.584 31.519 1.00 31.85 C
ANISOU 1050 C PRO A 139 4016 4520 3568 344 -186 -556 C
ATOM 1051 O PRO A 139 13.553 7.704 32.043 1.00 27.11 O
ANISOU 1051 O PRO A 139 3453 3866 2982 402 -236 -652 O
ATOM 1052 CB PRO A 139 15.118 6.379 29.504 1.00 27.29 C
ANISOU 1052 CB PRO A 139 3490 3799 3079 133 -192 -453 C
ATOM 1053 CG PRO A 139 16.016 5.306 29.026 1.00 24.33 C
ANISOU 1053 CG PRO A 139 3084 3468 2690 46 -155 -393 C
ATOM 1054 CD PRO A 139 15.584 4.074 29.763 1.00 23.89 C
ANISOU 1054 CD PRO A 139 2966 3540 2569 99 -107 -367 C
ATOM 1055 N MET A 140 12.533 5.798 31.412 1.00 31.87 N
ANISOU 1055 N MET A 140 3966 4604 3537 382 -141 -489 N
ATOM 1056 CA MET A 140 11.252 6.218 31.964 1.00 38.97 C
ANISOU 1056 CA MET A 140 4838 5560 4408 502 -141 -524 C
ATOM 1057 C MET A 140 11.259 6.229 33.487 1.00 34.31 C
ANISOU 1057 C MET A 140 4210 5089 3736 593 -130 -604 C
ATOM 1058 O MET A 140 10.451 6.943 34.092 1.00 40.64 O
ANISOU 1058 O MET A 140 5003 5925 4513 707 -146 -676 O
ATOM 1059 CB MET A 140 10.131 5.313 31.450 1.00 32.13 C
ANISOU 1059 CB MET A 140 3912 4767 3528 503 -93 -428 C
ATOM 1060 CG MET A 140 10.116 5.156 29.936 1.00 40.10 C
ANISOU 1060 CG MET A 140 4952 5683 4602 416 -103 -350 C
ATOM 1061 SD MET A 140 8.621 4.359 29.318 1.00 43.44 S
ANISOU 1061 SD MET A 140 5302 6186 5017 430 -68 -266 S
ATOM 1062 CE MET A 140 7.408 5.632 29.643 1.00 43.19 C
ANISOU 1062 CE MET A 140 5266 6160 4985 573 -106 -335 C
ATOM 1063 N LEU A 141 12.151 5.466 34.116 1.00 26.69 N
ANISOU 1063 N LEU A 141 3221 4196 2724 556 -105 -596 N
ATOM 1064 CA LEU A 141 12.252 5.443 35.569 1.00 27.38 C
ANISOU 1064 CA LEU A 141 3273 4412 2720 643 -97 -668 C
ATOM 1065 C LEU A 141 12.960 6.665 36.138 1.00 30.95 C
ANISOU 1065 C LEU A 141 3776 4800 3182 679 -168 -810 C
ATOM 1066 O LEU A 141 13.077 6.774 37.364 1.00 38.21 O
ANISOU 1066 O LEU A 141 4670 5828 4019 761 -172 -891 O
ATOM 1067 CB LEU A 141 12.976 4.177 36.030 1.00 26.85 C
ANISOU 1067 CB LEU A 141 3165 4442 2595 598 -52 -601 C
ATOM 1068 CG LEU A 141 12.328 2.839 35.672 1.00 34.63 C
ANISOU 1068 CG LEU A 141 4101 5490 3566 562 16 -464 C
ATOM 1069 CD1 LEU A 141 13.086 1.704 36.335 1.00 38.47 C
ANISOU 1069 CD1 LEU A 141 4560 6065 3991 542 51 -411 C
ATOM 1070 CD2 LEU A 141 10.863 2.820 36.080 1.00 26.78 C
ANISOU 1070 CD2 LEU A 141 3050 4596 2528 646 54 -445 C
ATOM 1071 N GLY A 142 13.436 7.576 35.293 1.00 28.32 N
ANISOU 1071 N GLY A 142 3516 4299 2947 616 -224 -842 N
ATOM 1072 CA GLY A 142 14.025 8.806 35.782 1.00 34.94 C
ANISOU 1072 CA GLY A 142 4410 5054 3813 640 -299 -981 C
ATOM 1073 C GLY A 142 15.347 9.174 35.143 1.00 29.22 C
ANISOU 1073 C GLY A 142 3735 4200 3168 506 -342 -987 C
ATOM 1074 O GLY A 142 15.837 10.292 35.325 1.00 39.47 O
ANISOU 1074 O GLY A 142 5090 5390 4518 498 -412 -1093 O
ATOM 1075 N TRP A 143 15.940 8.246 34.393 1.00 28.13 N
ANISOU 1075 N TRP A 143 3574 4073 3042 400 -301 -878 N
ATOM 1076 CA TRP A 143 17.218 8.495 33.725 1.00 28.89 C
ANISOU 1076 CA TRP A 143 3699 4074 3205 268 -329 -872 C
ATOM 1077 C TRP A 143 16.953 9.043 32.323 1.00 34.65 C
ANISOU 1077 C TRP A 143 4488 4650 4027 197 -341 -802 C
ATOM 1078 O TRP A 143 17.181 8.393 31.302 1.00 27.02 O
ANISOU 1078 O TRP A 143 3512 3676 3078 114 -304 -696 O
ATOM 1079 CB TRP A 143 18.057 7.223 33.688 1.00 27.12 C
ANISOU 1079 CB TRP A 143 3415 3954 2936 206 -281 -804 C
ATOM 1080 CG TRP A 143 19.489 7.440 33.270 1.00 31.52 C
ANISOU 1080 CG TRP A 143 3977 4461 3540 85 -309 -819 C
ATOM 1081 CD1 TRP A 143 20.056 8.610 32.852 1.00 27.98 C
ANISOU 1081 CD1 TRP A 143 3579 3877 3174 7 -365 -870 C
ATOM 1082 CD2 TRP A 143 20.532 6.456 33.233 1.00 26.66 C
ANISOU 1082 CD2 TRP A 143 3306 3934 2891 28 -280 -780 C
ATOM 1083 NE1 TRP A 143 21.383 8.416 32.558 1.00 27.94 N
ANISOU 1083 NE1 TRP A 143 3544 3885 3187 -104 -368 -863 N
ATOM 1084 CE2 TRP A 143 21.700 7.103 32.785 1.00 27.13 C
ANISOU 1084 CE2 TRP A 143 3373 3922 3011 -84 -318 -813 C
ATOM 1085 CE3 TRP A 143 20.590 5.092 33.538 1.00 25.96 C
ANISOU 1085 CE3 TRP A 143 3162 3972 2730 64 -228 -717 C
ATOM 1086 CZ2 TRP A 143 22.913 6.432 32.631 1.00 28.54 C
ANISOU 1086 CZ2 TRP A 143 3496 4174 3173 -154 -304 -794 C
ATOM 1087 CZ3 TRP A 143 21.794 4.428 33.383 1.00 26.04 C
ANISOU 1087 CZ3 TRP A 143 3130 4036 2728 4 -220 -699 C
ATOM 1088 CH2 TRP A 143 22.939 5.099 32.933 1.00 26.16 C
ANISOU 1088 CH2 TRP A 143 3144 3998 2798 -99 -256 -741 C
ATOM 1089 N ASN A 144 16.459 10.280 32.292 1.00 28.84 N
ANISOU 1089 N ASN A 144 3820 3792 3347 240 -397 -864 N
ATOM 1090 CA ASN A 144 16.083 10.928 31.045 1.00 28.97 C
ANISOU 1090 CA ASN A 144 3903 3659 3444 195 -416 -796 C
ATOM 1091 C ASN A 144 16.452 12.404 31.113 1.00 41.61 C
ANISOU 1091 C ASN A 144 5592 5088 5131 176 -498 -883 C
ATOM 1092 O ASN A 144 16.906 12.911 32.145 1.00 31.21 O
ANISOU 1092 O ASN A 144 4279 3770 3807 205 -542 -1010 O
ATOM 1093 CB ASN A 144 14.589 10.743 30.757 1.00 28.75 C
ANISOU 1093 CB ASN A 144 3867 3662 3395 301 -393 -746 C
ATOM 1094 CG ASN A 144 13.714 11.197 31.908 1.00 30.24 C
ANISOU 1094 CG ASN A 144 4046 3904 3542 456 -414 -854 C
ATOM 1095 OD1 ASN A 144 13.609 12.390 32.189 1.00 32.50 O
ANISOU 1095 OD1 ASN A 144 4398 4077 3875 509 -480 -949 O
ATOM 1096 ND2 ASN A 144 13.075 10.244 32.576 1.00 31.36 N
ANISOU 1096 ND2 ASN A 144 4104 4217 3593 530 -357 -840 N
ATOM 1097 N ASN A 145 16.253 13.098 29.991 1.00 30.69 N
ANISOU 1097 N ASN A 145 4282 3552 3827 127 -522 -813 N
ATOM 1098 CA ASN A 145 16.491 14.531 29.892 1.00 33.48 C
ANISOU 1098 CA ASN A 145 4736 3707 4277 103 -603 -872 C
ATOM 1099 C ASN A 145 15.196 15.337 29.912 1.00 35.82 C
ANISOU 1099 C ASN A 145 5096 3916 4598 248 -645 -904 C
ATOM 1100 O ASN A 145 15.162 16.458 29.393 1.00 46.29 O
ANISOU 1100 O ASN A 145 6524 5049 6016 231 -707 -901 O
ATOM 1101 CB ASN A 145 17.287 14.850 28.626 1.00 32.26 C
ANISOU 1101 CB ASN A 145 4630 3431 4198 -61 -606 -762 C
ATOM 1102 CG ASN A 145 18.622 14.132 28.577 1.00 37.52 C
ANISOU 1102 CG ASN A 145 5226 4188 4841 -200 -567 -739 C
ATOM 1103 OD1 ASN A 145 19.307 13.993 29.592 1.00 40.97 O
ANISOU 1103 OD1 ASN A 145 5618 4696 5252 -204 -579 -842 O
ATOM 1104 ND2 ASN A 145 18.999 13.669 27.390 1.00 42.06 N
ANISOU 1104 ND2 ASN A 145 5789 4772 5419 -306 -522 -607 N
ATOM 1105 N CYS A 146 14.128 14.785 30.492 1.00 39.28 N
ANISOU 1105 N CYS A 146 5474 4494 4956 393 -612 -930 N
ATOM 1106 CA CYS A 146 12.878 15.530 30.585 1.00 39.05 C
ANISOU 1106 CA CYS A 146 5488 4408 4941 548 -652 -973 C
ATOM 1107 C CYS A 146 13.000 16.709 31.539 1.00 46.57 C
ANISOU 1107 C CYS A 146 6508 5253 5935 628 -734 -1140 C
ATOM 1108 O CYS A 146 12.291 17.709 31.379 1.00 54.93 O
ANISOU 1108 O CYS A 146 7647 6176 7050 726 -794 -1178 O
ATOM 1109 CB CYS A 146 11.742 14.608 31.023 1.00 54.65 C
ANISOU 1109 CB CYS A 146 7363 6585 6815 673 -590 -960 C
ATOM 1110 SG CYS A 146 11.401 13.255 29.868 1.00 53.00 S
ANISOU 1110 SG CYS A 146 7082 6486 6570 593 -507 -779 S
ATOM 1111 N GLY A 147 13.886 16.615 32.532 1.00 54.57 N
ANISOU 1111 N GLY A 147 7493 6323 6919 593 -744 -1246 N
ATOM 1112 CA GLY A 147 14.116 17.724 33.439 1.00 47.06 C
ANISOU 1112 CA GLY A 147 6606 5267 6008 655 -830 -1420 C
ATOM 1113 C GLY A 147 14.921 18.862 32.848 1.00 53.90 C
ANISOU 1113 C GLY A 147 7590 5877 7012 532 -910 -1429 C
ATOM 1114 O GLY A 147 15.002 19.928 33.469 1.00 49.23 O
ANISOU 1114 O GLY A 147 7074 5152 6478 586 -996 -1575 O
ATOM 1115 N GLN A 148 15.514 18.664 31.672 1.00 67.34 N
ANISOU 1115 N GLN A 148 9309 7507 8769 369 -883 -1277 N
ATOM 1116 CA GLN A 148 16.292 19.692 30.981 1.00 66.31 C
ANISOU 1116 CA GLN A 148 9285 7138 8770 228 -947 -1249 C
ATOM 1117 C GLN A 148 15.806 19.798 29.540 1.00 56.16 C
ANISOU 1117 C GLN A 148 8054 5755 7530 190 -927 -1070 C
ATOM 1118 O GLN A 148 16.521 19.431 28.600 1.00 60.03 O
ANISOU 1118 O GLN A 148 8530 6242 8036 31 -886 -936 O
ATOM 1119 CB GLN A 148 17.788 19.377 31.027 1.00 55.38 C
ANISOU 1119 CB GLN A 148 7854 5788 7400 35 -933 -1244 C
ATOM 1120 CG GLN A 148 18.388 19.352 32.422 1.00 55.60 C
ANISOU 1120 CG GLN A 148 7832 5908 7386 61 -966 -1424 C
ATOM 1121 CD GLN A 148 18.146 18.041 33.142 1.00 69.53 C
ANISOU 1121 CD GLN A 148 9470 7946 9004 149 -889 -1434 C
ATOM 1122 OE1 GLN A 148 17.880 17.014 32.516 1.00 68.45 O
ANISOU 1122 OE1 GLN A 148 9272 7929 8809 135 -806 -1296 O
ATOM 1123 NE2 GLN A 148 18.236 18.069 34.467 1.00 92.00 N
ANISOU 1123 NE2 GLN A 148 12279 10890 11786 241 -919 -1597 N
ATOM 1124 N PRO A 149 14.592 20.305 29.331 1.00 58.41 N
ANISOU 1124 N PRO A 149 8397 5969 7828 344 -958 -1066 N
ATOM 1125 CA PRO A 149 14.048 20.356 27.971 1.00 59.86 C
ANISOU 1125 CA PRO A 149 8625 6082 8037 327 -942 -895 C
ATOM 1126 C PRO A 149 14.683 21.464 27.148 1.00 59.37 C
ANISOU 1126 C PRO A 149 8694 5761 8104 199 -1004 -825 C
ATOM 1127 O PRO A 149 15.173 22.465 27.677 1.00 66.37 O
ANISOU 1127 O PRO A 149 9664 6472 9080 173 -1082 -930 O
ATOM 1128 CB PRO A 149 12.557 20.621 28.201 1.00 45.62 C
ANISOU 1128 CB PRO A 149 6834 4294 6205 551 -966 -941 C
ATOM 1129 CG PRO A 149 12.524 21.396 29.473 1.00 50.66 C
ANISOU 1129 CG PRO A 149 7510 4872 6868 660 -1036 -1141 C
ATOM 1130 CD PRO A 149 13.656 20.868 30.321 1.00 58.24 C
ANISOU 1130 CD PRO A 149 8399 5940 7792 550 -1010 -1223 C
ATOM 1131 N LYS A 150 14.672 21.268 25.831 1.00 63.78 N
ANISOU 1131 N LYS A 150 9271 6298 8667 115 -968 -642 N
ATOM 1132 CA LYS A 150 15.154 22.272 24.883 1.00 59.63 C
ANISOU 1132 CA LYS A 150 8870 5537 8250 -5 -1016 -534 C
ATOM 1133 C LYS A 150 14.063 23.324 24.728 1.00 48.94 C
ANISOU 1133 C LYS A 150 7638 3998 6959 158 -1098 -544 C
ATOM 1134 O LYS A 150 13.154 23.193 23.907 1.00 53.17 O
ANISOU 1134 O LYS A 150 8185 4558 7460 246 -1086 -433 O
ATOM 1135 CB LYS A 150 15.507 21.627 23.548 1.00 51.28 C
ANISOU 1135 CB LYS A 150 7778 4552 7153 -139 -944 -335 C
ATOM 1136 CG LYS A 150 16.393 20.394 23.660 1.00 63.58 C
ANISOU 1136 CG LYS A 150 9199 6328 8629 -258 -856 -326 C
ATOM 1137 CD LYS A 150 17.839 20.759 23.957 1.00 69.04 C
ANISOU 1137 CD LYS A 150 9894 6952 9386 -444 -869 -363 C
ATOM 1138 CE LYS A 150 18.480 21.473 22.776 1.00 84.91 C
ANISOU 1138 CE LYS A 150 11987 8803 11473 -612 -878 -206 C
ATOM 1139 NZ LYS A 150 19.932 21.734 22.993 1.00 93.11 N
ANISOU 1139 NZ LYS A 150 13003 9804 12570 -814 -880 -230 N
ATOM 1140 N GLU A 151 14.156 24.388 25.531 1.00 51.02 N
ANISOU 1140 N GLU A 151 7995 4075 7315 207 -1189 -686 N
ATOM 1141 CA GLU A 151 13.114 25.413 25.529 1.00 58.00 C
ANISOU 1141 CA GLU A 151 8999 4779 8261 390 -1276 -724 C
ATOM 1142 C GLU A 151 13.026 26.133 24.190 1.00 65.75 C
ANISOU 1142 C GLU A 151 10106 5557 9320 331 -1309 -534 C
ATOM 1143 O GLU A 151 11.946 26.599 23.807 1.00 58.95 O
ANISOU 1143 O GLU A 151 9311 4620 8467 499 -1353 -499 O
ATOM 1144 CB GLU A 151 13.361 26.418 26.654 1.00 48.10 C
ANISOU 1144 CB GLU A 151 7827 3351 7098 441 -1373 -927 C
ATOM 1145 CG GLU A 151 13.295 25.823 28.051 1.00 56.87 C
ANISOU 1145 CG GLU A 151 8823 4666 8119 539 -1352 -1126 C
ATOM 1146 CD GLU A 151 11.902 25.348 28.427 1.00 89.61 C
ANISOU 1146 CD GLU A 151 12896 8993 12158 783 -1326 -1177 C
ATOM 1147 OE1 GLU A 151 10.922 25.780 27.782 1.00 95.42 O
ANISOU 1147 OE1 GLU A 151 13694 9647 12914 911 -1355 -1108 O
ATOM 1148 OE2 GLU A 151 11.788 24.541 29.374 1.00 97.26 O
ANISOU 1148 OE2 GLU A 151 13741 10193 13020 846 -1275 -1283 O
ATOM 1149 N GLY A 152 14.142 26.239 23.468 1.00 64.32 N
ANISOU 1149 N GLY A 152 9954 5294 9189 99 -1288 -407 N
ATOM 1150 CA GLY A 152 14.098 26.851 22.152 1.00 48.70 C
ANISOU 1150 CA GLY A 152 8089 3147 7267 32 -1307 -203 C
ATOM 1151 C GLY A 152 13.327 26.018 21.147 1.00 64.07 C
ANISOU 1151 C GLY A 152 9969 5277 9098 97 -1240 -50 C
ATOM 1152 O GLY A 152 12.536 26.550 20.364 1.00 67.76 O
ANISOU 1152 O GLY A 152 10526 5638 9581 196 -1281 58 O
ATOM 1153 N LYS A 153 13.543 24.699 21.155 1.00 62.14 N
ANISOU 1153 N LYS A 153 9567 5307 8735 47 -1141 -43 N
ATOM 1154 CA LYS A 153 12.823 23.829 20.231 1.00 62.13 C
ANISOU 1154 CA LYS A 153 9494 5489 8623 102 -1080 84 C
ATOM 1155 C LYS A 153 11.355 23.704 20.616 1.00 62.73 C
ANISOU 1155 C LYS A 153 9541 5644 8650 351 -1106 5 C
ATOM 1156 O LYS A 153 10.484 23.612 19.742 1.00 67.47 O
ANISOU 1156 O LYS A 153 10148 6282 9204 441 -1109 114 O
ATOM 1157 CB LYS A 153 13.477 22.448 20.184 1.00 67.43 C
ANISOU 1157 CB LYS A 153 10012 6415 9192 -17 -975 100 C
ATOM 1158 CG LYS A 153 14.885 22.432 19.615 1.00 67.11 C
ANISOU 1158 CG LYS A 153 9975 6347 9179 -257 -935 198 C
ATOM 1159 CD LYS A 153 15.420 21.009 19.537 1.00 62.03 C
ANISOU 1159 CD LYS A 153 9179 5965 8427 -340 -834 207 C
ATOM 1160 CE LYS A 153 16.800 20.968 18.902 1.00 68.27 C
ANISOU 1160 CE LYS A 153 9956 6752 9231 -568 -790 308 C
ATOM 1161 NZ LYS A 153 17.307 19.574 18.775 1.00 66.81 N
ANISOU 1161 NZ LYS A 153 9626 6818 8938 -630 -696 314 N
ATOM 1162 N ASN A 154 11.059 23.693 21.918 1.00 61.09 N
ANISOU 1162 N ASN A 154 9292 5478 8442 466 -1126 -186 N
ATOM 1163 CA ASN A 154 9.678 23.528 22.356 1.00 54.72 C
ANISOU 1163 CA ASN A 154 8436 4777 7579 701 -1141 -267 C
ATOM 1164 C ASN A 154 8.849 24.778 22.090 1.00 63.36 C
ANISOU 1164 C ASN A 154 9668 5654 8751 861 -1243 -260 C
ATOM 1165 O ASN A 154 7.642 24.676 21.842 1.00 71.66 O
ANISOU 1165 O ASN A 154 10689 6788 9752 1038 -1254 -246 O
ATOM 1166 CB ASN A 154 9.639 23.158 23.840 1.00 42.78 C
ANISOU 1166 CB ASN A 154 6836 3389 6031 778 -1126 -467 C
ATOM 1167 CG ASN A 154 10.355 21.846 24.135 1.00 67.87 C
ANISOU 1167 CG ASN A 154 9873 6791 9123 646 -1028 -469 C
ATOM 1168 OD1 ASN A 154 10.513 20.998 23.254 1.00 54.86 O
ANISOU 1168 OD1 ASN A 154 8165 5260 7419 549 -962 -335 O
ATOM 1169 ND2 ASN A 154 10.791 21.675 25.378 1.00 61.47 N
ANISOU 1169 ND2 ASN A 154 9014 6044 8300 650 -1022 -623 N
ATOM 1170 N HIS A 155 9.471 25.958 22.129 1.00 61.29 N
ANISOU 1170 N HIS A 155 9559 5114 8615 801 -1320 -271 N
ATOM 1171 CA HIS A 155 8.746 27.186 21.819 1.00 56.70 C
ANISOU 1171 CA HIS A 155 9129 4294 8120 951 -1425 -253 C
ATOM 1172 C HIS A 155 8.643 27.428 20.319 1.00 66.68 C
ANISOU 1172 C HIS A 155 10471 5473 9391 894 -1431 -19 C
ATOM 1173 O HIS A 155 7.638 27.976 19.854 1.00 75.29 O
ANISOU 1173 O HIS A 155 11630 6488 10491 1070 -1492 29 O
ATOM 1174 CB HIS A 155 9.415 28.382 22.499 1.00 75.82 C
ANISOU 1174 CB HIS A 155 11693 6429 10684 914 -1516 -365 C
ATOM 1175 CG HIS A 155 9.187 28.443 23.978 1.00 78.72 C
ANISOU 1175 CG HIS A 155 12016 6849 11046 1049 -1542 -615 C
ATOM 1176 ND1 HIS A 155 8.443 27.501 24.656 1.00 78.51 N
ANISOU 1176 ND1 HIS A 155 11829 7109 10892 1187 -1482 -715 N
ATOM 1177 CD2 HIS A 155 9.601 29.335 24.908 1.00 73.45 C
ANISOU 1177 CD2 HIS A 155 11440 5989 10479 1065 -1624 -785 C
ATOM 1178 CE1 HIS A 155 8.410 27.809 25.940 1.00 76.09 C
ANISOU 1178 CE1 HIS A 155 11517 6797 10597 1290 -1520 -931 C
ATOM 1179 NE2 HIS A 155 9.106 28.918 26.120 1.00 83.22 N
ANISOU 1179 NE2 HIS A 155 12570 7412 11636 1222 -1610 -986 N
ATOM 1180 N SER A 156 9.662 27.031 19.551 1.00 65.44 N
ANISOU 1180 N SER A 156 10303 5339 9223 661 -1369 127 N
ATOM 1181 CA SER A 156 9.608 27.214 18.103 1.00 66.14 C
ANISOU 1181 CA SER A 156 10458 5373 9299 602 -1368 356 C
ATOM 1182 C SER A 156 8.500 26.372 17.483 1.00 55.16 C
ANISOU 1182 C SER A 156 8963 4217 7778 740 -1330 418 C
ATOM 1183 O SER A 156 7.765 26.848 16.610 1.00 79.04 O
ANISOU 1183 O SER A 156 12062 7172 10797 844 -1379 539 O
ATOM 1184 CB SER A 156 10.959 26.871 17.476 1.00 58.98 C
ANISOU 1184 CB SER A 156 9536 4484 8389 326 -1298 485 C
ATOM 1185 OG SER A 156 11.247 25.489 17.595 1.00 79.52 O
ANISOU 1185 OG SER A 156 11963 7377 10875 255 -1194 456 O
ATOM 1186 N GLN A 157 8.362 25.123 17.923 1.00 69.29 N
ANISOU 1186 N GLN A 157 10581 6283 9465 741 -1249 338 N
ATOM 1187 CA GLN A 157 7.283 24.261 17.459 1.00 57.92 C
ANISOU 1187 CA GLN A 157 9026 5073 7908 864 -1216 372 C
ATOM 1188 C GLN A 157 5.986 24.485 18.225 1.00 52.87 C
ANISOU 1188 C GLN A 157 8355 4473 7261 1117 -1267 234 C
ATOM 1189 O GLN A 157 4.967 23.874 17.883 1.00 61.32 O
ANISOU 1189 O GLN A 157 9327 5729 8244 1235 -1251 254 O
ATOM 1190 CB GLN A 157 7.704 22.794 17.561 1.00 52.48 C
ANISOU 1190 CB GLN A 157 8172 4650 7118 745 -1107 355 C
ATOM 1191 CG GLN A 157 6.948 21.878 16.617 1.00 58.98 C
ANISOU 1191 CG GLN A 157 8899 5682 7828 784 -1068 452 C
ATOM 1192 CD GLN A 157 7.252 20.418 16.857 1.00 74.47 C
ANISOU 1192 CD GLN A 157 10702 7892 9703 691 -971 411 C
ATOM 1193 OE1 GLN A 157 6.424 19.548 16.583 1.00 64.00 O
ANISOU 1193 OE1 GLN A 157 9266 6758 8291 759 -943 416 O
ATOM 1194 NE2 GLN A 157 8.444 20.139 17.371 1.00 67.16 N
ANISOU 1194 NE2 GLN A 157 9761 6957 8800 534 -924 369 N
ATOM 1195 N GLY A 158 5.998 25.339 19.245 1.00 62.24 N
ANISOU 1195 N GLY A 158 9614 5499 8534 1204 -1328 89 N
ATOM 1196 CA GLY A 158 4.790 25.692 19.962 1.00 65.51 C
ANISOU 1196 CA GLY A 158 10007 5940 8944 1460 -1382 -47 C
ATOM 1197 C GLY A 158 4.183 24.549 20.747 1.00 49.48 C
ANISOU 1197 C GLY A 158 7784 4210 6806 1533 -1309 -163 C
ATOM 1198 O GLY A 158 2.973 24.314 20.673 1.00 79.67 O
ANISOU 1198 O GLY A 158 11526 8176 10567 1709 -1316 -178 O
ATOM 1199 N CYS A 159 5.006 23.831 21.503 1.00 49.66 N
ANISOU 1199 N CYS A 159 7729 4336 6805 1398 -1239 -240 N
ATOM 1200 CA CYS A 159 4.491 22.741 22.312 1.00 57.72 C
ANISOU 1200 CA CYS A 159 8574 5632 7726 1456 -1167 -339 C
ATOM 1201 C CYS A 159 3.828 23.279 23.576 1.00 58.82 C
ANISOU 1201 C CYS A 159 8702 5773 7875 1658 -1209 -530 C
ATOM 1202 O CYS A 159 4.120 24.383 24.045 1.00 51.27 O
ANISOU 1202 O CYS A 159 7873 4599 7009 1710 -1286 -619 O
ATOM 1203 CB CYS A 159 5.605 21.759 22.677 1.00 51.97 C
ANISOU 1203 CB CYS A 159 7768 5015 6962 1254 -1080 -346 C
ATOM 1204 SG CYS A 159 6.425 20.992 21.260 1.00 58.82 S
ANISOU 1204 SG CYS A 159 8627 5920 7801 1025 -1019 -143 S
ATOM 1205 N GLY A 160 2.921 22.476 24.128 1.00 54.63 N
ANISOU 1205 N GLY A 160 8015 5496 7247 1772 -1158 -596 N
ATOM 1206 CA GLY A 160 2.190 22.859 25.315 1.00 63.33 C
ANISOU 1206 CA GLY A 160 9077 6654 8330 1976 -1183 -774 C
ATOM 1207 C GLY A 160 2.972 22.617 26.589 1.00 59.97 C
ANISOU 1207 C GLY A 160 8621 6277 7890 1916 -1148 -914 C
ATOM 1208 O GLY A 160 4.085 22.090 26.593 1.00 52.41 O
ANISOU 1208 O GLY A 160 7661 5318 6936 1716 -1101 -876 O
ATOM 1209 N GLU A 161 2.362 23.020 27.701 1.00 63.78 N
ANISOU 1209 N GLU A 161 9073 6814 8347 2106 -1173 -1086 N
ATOM 1210 CA GLU A 161 2.995 22.857 29.001 1.00 72.63 C
ANISOU 1210 CA GLU A 161 10161 7998 9438 2082 -1148 -1236 C
ATOM 1211 C GLU A 161 3.183 21.378 29.313 1.00 69.46 C
ANISOU 1211 C GLU A 161 9595 7868 8926 1966 -1030 -1190 C
ATOM 1212 O GLU A 161 2.260 20.573 29.155 1.00 72.20 O
ANISOU 1212 O GLU A 161 9811 8431 9193 2022 -970 -1136 O
ATOM 1213 CB GLU A 161 2.155 23.533 30.085 1.00 76.87 C
ANISOU 1213 CB GLU A 161 10684 8575 9947 2334 -1194 -1429 C
ATOM 1214 CG GLU A 161 1.679 24.940 29.727 1.00 95.36 C
ANISOU 1214 CG GLU A 161 13177 10664 12391 2498 -1314 -1474 C
ATOM 1215 CD GLU A 161 2.819 25.922 29.508 1.00110.48 C
ANISOU 1215 CD GLU A 161 15286 12246 14444 2376 -1399 -1483 C
ATOM 1216 OE1 GLU A 161 3.926 25.691 30.041 1.00113.36 O
ANISOU 1216 OE1 GLU A 161 15659 12596 14819 2215 -1376 -1530 O
ATOM 1217 OE2 GLU A 161 2.604 26.929 28.801 1.00104.16 O
ANISOU 1217 OE2 GLU A 161 14629 11201 13745 2440 -1490 -1440 O
ATOM 1218 N GLY A 162 4.389 21.021 29.752 1.00 58.08 N
ANISOU 1218 N GLY A 162 8164 6415 7489 1800 -1000 -1210 N
ATOM 1219 CA GLY A 162 4.738 19.638 29.987 1.00 49.64 C
ANISOU 1219 CA GLY A 162 6963 5568 6330 1675 -897 -1154 C
ATOM 1220 C GLY A 162 5.130 18.861 28.752 1.00 52.92 C
ANISOU 1220 C GLY A 162 7365 5986 6756 1495 -851 -969 C
ATOM 1221 O GLY A 162 5.568 17.709 28.878 1.00 50.53 O
ANISOU 1221 O GLY A 162 6970 5837 6392 1377 -771 -919 O
ATOM 1222 N GLN A 163 4.993 19.444 27.567 1.00 44.28 N
ANISOU 1222 N GLN A 163 6363 4731 5732 1477 -900 -865 N
ATOM 1223 CA GLN A 163 5.356 18.796 26.318 1.00 50.50 C
ANISOU 1223 CA GLN A 163 7145 5520 6522 1318 -863 -694 C
ATOM 1224 C GLN A 163 6.749 19.220 25.872 1.00 58.66 C
ANISOU 1224 C GLN A 163 8290 6362 7634 1135 -885 -645 C
ATOM 1225 O GLN A 163 7.248 20.291 26.230 1.00 50.89 O
ANISOU 1225 O GLN A 163 7420 5186 6731 1143 -954 -721 O
ATOM 1226 CB GLN A 163 4.343 19.124 25.218 1.00 38.64 C
ANISOU 1226 CB GLN A 163 5665 3985 5032 1408 -900 -595 C
ATOM 1227 CG GLN A 163 2.969 18.528 25.433 1.00 45.56 C
ANISOU 1227 CG GLN A 163 6403 5080 5826 1557 -868 -615 C
ATOM 1228 CD GLN A 163 2.039 18.784 24.264 1.00 42.99 C
ANISOU 1228 CD GLN A 163 6091 4738 5507 1634 -908 -512 C
ATOM 1229 OE1 GLN A 163 2.361 19.546 23.352 1.00 53.77 O
ANISOU 1229 OE1 GLN A 163 7583 5909 6937 1601 -967 -429 O
ATOM 1230 NE2 GLN A 163 0.879 18.143 24.284 1.00 57.37 N
ANISOU 1230 NE2 GLN A 163 7774 6767 7256 1732 -877 -510 N
ATOM 1231 N VAL A 164 7.373 18.359 25.071 1.00 36.68 N
ANISOU 1231 N VAL A 164 5471 3638 4827 968 -827 -521 N
ATOM 1232 CA VAL A 164 8.680 18.618 24.486 1.00 50.01 C
ANISOU 1232 CA VAL A 164 7241 5185 6576 781 -833 -450 C
ATOM 1233 C VAL A 164 8.642 18.178 23.028 1.00 36.00 C
ANISOU 1233 C VAL A 164 5466 3428 4783 692 -806 -277 C
ATOM 1234 O VAL A 164 7.707 17.512 22.581 1.00 37.21 O
ANISOU 1234 O VAL A 164 5544 3721 4874 760 -779 -226 O
ATOM 1235 CB VAL A 164 9.817 17.888 25.235 1.00 42.67 C
ANISOU 1235 CB VAL A 164 6248 4346 5619 651 -779 -505 C
ATOM 1236 CG1 VAL A 164 9.955 18.423 26.648 1.00 36.42 C
ANISOU 1236 CG1 VAL A 164 5468 3530 4842 733 -815 -680 C
ATOM 1237 CG2 VAL A 164 9.562 16.387 25.252 1.00 33.83 C
ANISOU 1237 CG2 VAL A 164 4990 3467 4399 630 -690 -464 C
ATOM 1238 N ALA A 165 9.674 18.570 22.284 1.00 41.79 N
ANISOU 1238 N ALA A 165 6282 4027 5570 537 -816 -188 N
ATOM 1239 CA ALA A 165 9.856 18.136 20.902 1.00 39.71 C
ANISOU 1239 CA ALA A 165 6018 3792 5277 434 -784 -25 C
ATOM 1240 C ALA A 165 10.457 16.736 20.926 1.00 39.80 C
ANISOU 1240 C ALA A 165 5911 3998 5214 322 -695 -13 C
ATOM 1241 O ALA A 165 11.614 16.555 21.322 1.00 46.91 O
ANISOU 1241 O ALA A 165 6801 4894 6129 197 -668 -43 O
ATOM 1242 CB ALA A 165 10.746 19.113 20.137 1.00 49.97 C
ANISOU 1242 CB ALA A 165 7446 4884 6656 310 -822 70 C
ATOM 1243 N CYS A 166 9.671 15.750 20.512 1.00 32.96 N
ANISOU 1243 N CYS A 166 4954 3298 4270 367 -655 27 N
ATOM 1244 CA CYS A 166 10.041 14.349 20.679 1.00 42.20 C
ANISOU 1244 CA CYS A 166 6010 4650 5372 292 -577 21 C
ATOM 1245 C CYS A 166 11.199 14.002 19.756 1.00 36.61 C
ANISOU 1245 C CYS A 166 5316 3937 4656 122 -541 116 C
ATOM 1246 O CYS A 166 10.999 13.719 18.574 1.00 38.55 O
ANISOU 1246 O CYS A 166 5564 4218 4867 92 -531 222 O
ATOM 1247 CB CYS A 166 8.842 13.450 20.410 1.00 30.67 C
ANISOU 1247 CB CYS A 166 4458 3352 3846 378 -553 40 C
ATOM 1248 SG CYS A 166 9.111 11.777 20.999 1.00 40.32 S
ANISOU 1248 SG CYS A 166 5546 4774 5000 317 -467 4 S
ATOM 1249 N LEU A 167 12.417 14.014 20.299 1.00 40.20 N
ANISOU 1249 N LEU A 167 5773 4365 5137 16 -522 74 N
ATOM 1250 CA LEU A 167 13.632 13.672 19.571 1.00 32.49 C
ANISOU 1250 CA LEU A 167 4792 3404 4150 -145 -481 149 C
ATOM 1251 C LEU A 167 14.445 12.719 20.429 1.00 34.46 C
ANISOU 1251 C LEU A 167 4953 3772 4369 -199 -430 71 C
ATOM 1252 O LEU A 167 14.586 12.938 21.635 1.00 50.99 O
ANISOU 1252 O LEU A 167 7038 5851 6486 -160 -446 -37 O
ATOM 1253 CB LEU A 167 14.461 14.918 19.239 1.00 40.11 C
ANISOU 1253 CB LEU A 167 5861 4186 5192 -240 -521 193 C
ATOM 1254 CG LEU A 167 13.738 16.006 18.442 1.00 48.37 C
ANISOU 1254 CG LEU A 167 7016 5084 6279 -184 -582 279 C
ATOM 1255 CD1 LEU A 167 14.618 17.234 18.267 1.00 54.74 C
ANISOU 1255 CD1 LEU A 167 7931 5692 7177 -292 -622 320 C
ATOM 1256 CD2 LEU A 167 13.286 15.471 17.091 1.00 32.82 C
ANISOU 1256 CD2 LEU A 167 5030 3202 4237 -188 -556 407 C
ATOM 1257 N PHE A 168 14.967 11.659 19.804 1.00 28.44 N
ANISOU 1257 N PHE A 168 4127 3128 3549 -278 -372 124 N
ATOM 1258 CA PHE A 168 15.702 10.637 20.543 1.00 27.46 C
ANISOU 1258 CA PHE A 168 3920 3124 3392 -315 -324 61 C
ATOM 1259 C PHE A 168 16.819 11.255 21.376 1.00 28.03 C
ANISOU 1259 C PHE A 168 4006 3133 3512 -382 -341 -8 C
ATOM 1260 O PHE A 168 16.939 10.970 22.574 1.00 32.90 O
ANISOU 1260 O PHE A 168 4581 3800 4121 -338 -340 -107 O
ATOM 1261 CB PHE A 168 16.257 9.591 19.570 1.00 26.70 C
ANISOU 1261 CB PHE A 168 3772 3136 3238 -396 -269 132 C
ATOM 1262 CG PHE A 168 16.835 8.366 20.237 1.00 28.52 C
ANISOU 1262 CG PHE A 168 3916 3494 3427 -408 -222 75 C
ATOM 1263 CD1 PHE A 168 18.114 8.384 20.773 1.00 25.79 C
ANISOU 1263 CD1 PHE A 168 3546 3161 3094 -484 -209 33 C
ATOM 1264 CD2 PHE A 168 16.105 7.190 20.303 1.00 33.15 C
ANISOU 1264 CD2 PHE A 168 4445 4186 3965 -346 -194 69 C
ATOM 1265 CE1 PHE A 168 18.642 7.263 21.376 1.00 35.60 C
ANISOU 1265 CE1 PHE A 168 4713 4518 4295 -482 -171 -13 C
ATOM 1266 CE2 PHE A 168 16.631 6.064 20.906 1.00 25.25 C
ANISOU 1266 CE2 PHE A 168 3377 3284 2931 -353 -154 29 C
ATOM 1267 CZ PHE A 168 17.900 6.102 21.442 1.00 31.42 C
ANISOU 1267 CZ PHE A 168 4139 4078 3720 -414 -144 -11 C
ATOM 1268 N GLU A 169 17.628 12.119 20.773 1.00 28.98 N
ANISOU 1268 N GLU A 169 4184 3148 3681 -491 -359 44 N
ATOM 1269 CA GLU A 169 18.771 12.699 21.465 1.00 41.68 C
ANISOU 1269 CA GLU A 169 5797 4700 5341 -579 -378 -20 C
ATOM 1270 C GLU A 169 18.394 13.872 22.362 1.00 30.78 C
ANISOU 1270 C GLU A 169 4490 3172 4034 -517 -450 -110 C
ATOM 1271 O GLU A 169 19.261 14.393 23.071 1.00 39.07 O
ANISOU 1271 O GLU A 169 5544 4170 5131 -581 -478 -186 O
ATOM 1272 CB GLU A 169 19.839 13.121 20.448 1.00 30.41 C
ANISOU 1272 CB GLU A 169 4390 3229 3938 -739 -362 76 C
ATOM 1273 CG GLU A 169 20.135 12.042 19.410 1.00 29.53 C
ANISOU 1273 CG GLU A 169 4213 3262 3745 -785 -294 164 C
ATOM 1274 CD GLU A 169 21.548 12.110 18.862 1.00 44.97 C
ANISOU 1274 CD GLU A 169 6133 5251 5701 -944 -260 214 C
ATOM 1275 OE1 GLU A 169 22.334 12.958 19.337 1.00 48.32 O
ANISOU 1275 OE1 GLU A 169 6576 5587 6194 -1032 -289 180 O
ATOM 1276 OE2 GLU A 169 21.869 11.306 17.959 1.00 40.46 O
ANISOU 1276 OE2 GLU A 169 5511 4801 5061 -981 -204 281 O
ATOM 1277 N ASP A 170 17.128 14.286 22.366 1.00 36.67 N
ANISOU 1277 N ASP A 170 5288 3856 4789 -388 -485 -112 N
ATOM 1278 CA ASP A 170 16.658 15.335 23.260 1.00 32.16 C
ANISOU 1278 CA ASP A 170 4785 3156 4280 -298 -556 -214 C
ATOM 1279 C ASP A 170 16.053 14.804 24.553 1.00 31.57 C
ANISOU 1279 C ASP A 170 4645 3194 4154 -164 -551 -339 C
ATOM 1280 O ASP A 170 15.895 15.578 25.504 1.00 38.39 O
ANISOU 1280 O ASP A 170 5548 3982 5057 -93 -606 -454 O
ATOM 1281 CB ASP A 170 15.623 16.224 22.553 1.00 47.54 C
ANISOU 1281 CB ASP A 170 6829 4965 6268 -218 -605 -149 C
ATOM 1282 CG ASP A 170 16.260 17.237 21.619 1.00 43.56 C
ANISOU 1282 CG ASP A 170 6425 4284 5841 -341 -638 -49 C
ATOM 1283 OD1 ASP A 170 17.458 17.091 21.300 1.00 39.90 O
ANISOU 1283 OD1 ASP A 170 5937 3836 5385 -502 -606 -7 O
ATOM 1284 OD2 ASP A 170 15.559 18.190 21.212 1.00 60.55 O
ANISOU 1284 OD2 ASP A 170 8678 6282 8045 -276 -695 -8 O
ATOM 1285 N VAL A 171 15.708 13.518 24.619 1.00 30.18 N
ANISOU 1285 N VAL A 171 4375 3198 3894 -127 -488 -320 N
ATOM 1286 CA VAL A 171 15.038 12.985 25.801 1.00 29.74 C
ANISOU 1286 CA VAL A 171 4256 3259 3783 0 -476 -416 C
ATOM 1287 C VAL A 171 15.797 11.791 26.371 1.00 30.93 C
ANISOU 1287 C VAL A 171 4313 3568 3870 -48 -419 -437 C
ATOM 1288 O VAL A 171 15.808 11.577 27.590 1.00 33.53 O
ANISOU 1288 O VAL A 171 4602 3975 4163 17 -419 -534 O
ATOM 1289 CB VAL A 171 13.574 12.612 25.495 1.00 37.43 C
ANISOU 1289 CB VAL A 171 5207 4296 4718 121 -462 -375 C
ATOM 1290 CG1 VAL A 171 12.768 13.860 25.156 1.00 30.63 C
ANISOU 1290 CG1 VAL A 171 4438 3286 3916 204 -528 -377 C
ATOM 1291 CG2 VAL A 171 13.490 11.596 24.364 1.00 28.32 C
ANISOU 1291 CG2 VAL A 171 4009 3225 3524 57 -409 -255 C
ATOM 1292 N VAL A 172 16.436 11.006 25.509 1.00 27.87 N
ANISOU 1292 N VAL A 172 3892 3235 3463 -152 -373 -348 N
ATOM 1293 CA VAL A 172 17.206 9.843 25.933 1.00 30.84 C
ANISOU 1293 CA VAL A 172 4184 3750 3783 -193 -323 -359 C
ATOM 1294 C VAL A 172 18.642 10.295 26.180 1.00 27.52 C
ANISOU 1294 C VAL A 172 3767 3293 3396 -301 -342 -402 C
ATOM 1295 O VAL A 172 19.291 10.786 25.241 1.00 27.95 O
ANISOU 1295 O VAL A 172 3856 3269 3496 -412 -348 -341 O
ATOM 1296 CB VAL A 172 17.158 8.719 24.890 1.00 25.95 C
ANISOU 1296 CB VAL A 172 3525 3212 3124 -236 -267 -256 C
ATOM 1297 CG1 VAL A 172 17.758 7.444 25.463 1.00 26.01 C
ANISOU 1297 CG1 VAL A 172 3452 3358 3075 -244 -220 -274 C
ATOM 1298 CG2 VAL A 172 15.732 8.482 24.429 1.00 25.68 C
ANISOU 1298 CG2 VAL A 172 3494 3191 3073 -151 -262 -208 C
ATOM 1299 N PRO A 173 19.167 10.164 27.398 1.00 29.78 N
ANISOU 1299 N PRO A 173 4014 3643 3660 -277 -352 -503 N
ATOM 1300 CA PRO A 173 20.547 10.589 27.656 1.00 28.30 C
ANISOU 1300 CA PRO A 173 3814 3433 3503 -384 -377 -553 C
ATOM 1301 C PRO A 173 21.541 9.690 26.942 1.00 32.52 C
ANISOU 1301 C PRO A 173 4286 4058 4010 -485 -325 -481 C
ATOM 1302 O PRO A 173 21.367 8.472 26.869 1.00 26.58 O
ANISOU 1302 O PRO A 173 3480 3426 3194 -445 -274 -442 O
ATOM 1303 CB PRO A 173 20.684 10.466 29.179 1.00 28.51 C
ANISOU 1303 CB PRO A 173 3802 3543 3487 -304 -398 -679 C
ATOM 1304 CG PRO A 173 19.292 10.383 29.694 1.00 34.01 C
ANISOU 1304 CG PRO A 173 4513 4262 4148 -156 -396 -700 C
ATOM 1305 CD PRO A 173 18.497 9.708 28.624 1.00 36.73 C
ANISOU 1305 CD PRO A 173 4855 4622 4479 -149 -347 -577 C
ATOM 1306 N MET A 174 22.598 10.307 26.416 1.00 28.37 N
ANISOU 1306 N MET A 174 3768 3475 3536 -618 -339 -465 N
ATOM 1307 CA MET A 174 23.566 9.541 25.648 1.00 31.80 C
ANISOU 1307 CA MET A 174 4137 4004 3941 -712 -288 -398 C
ATOM 1308 C MET A 174 24.469 8.695 26.540 1.00 27.60 C
ANISOU 1308 C MET A 174 3513 3619 3357 -700 -274 -468 C
ATOM 1309 O MET A 174 25.034 7.705 26.061 1.00 29.73 O
ANISOU 1309 O MET A 174 3718 3998 3580 -723 -226 -422 O
ATOM 1310 CB MET A 174 24.392 10.479 24.767 1.00 28.99 C
ANISOU 1310 CB MET A 174 3808 3556 3652 -864 -301 -347 C
ATOM 1311 CG MET A 174 25.064 9.784 23.597 1.00 31.77 C
ANISOU 1311 CG MET A 174 4107 3998 3966 -948 -239 -248 C
ATOM 1312 SD MET A 174 23.916 9.002 22.444 1.00 44.30 S
ANISOU 1312 SD MET A 174 5723 5608 5500 -876 -192 -138 S
ATOM 1313 CE MET A 174 23.240 10.435 21.611 1.00 44.05 C
ANISOU 1313 CE MET A 174 5809 5388 5540 -918 -231 -59 C
ATOM 1314 N ASN A 175 24.611 9.045 27.823 1.00 29.18 N
ANISOU 1314 N ASN A 175 3704 3828 3556 -653 -320 -581 N
ATOM 1315 CA ASN A 175 25.381 8.189 28.722 1.00 27.85 C
ANISOU 1315 CA ASN A 175 3447 3810 3323 -621 -311 -642 C
ATOM 1316 C ASN A 175 24.640 6.893 29.029 1.00 26.68 C
ANISOU 1316 C ASN A 175 3275 3767 3096 -498 -265 -608 C
ATOM 1317 O ASN A 175 25.274 5.852 29.234 1.00 27.04 O
ANISOU 1317 O ASN A 175 3252 3936 3086 -481 -235 -601 O
ATOM 1318 CB ASN A 175 25.742 8.936 30.014 1.00 28.85 C
ANISOU 1318 CB ASN A 175 3570 3930 3461 -602 -377 -777 C
ATOM 1319 CG ASN A 175 24.540 9.583 30.690 1.00 34.28 C
ANISOU 1319 CG ASN A 175 4331 4537 4158 -494 -414 -835 C
ATOM 1320 OD1 ASN A 175 23.389 9.270 30.388 1.00 33.18 O
ANISOU 1320 OD1 ASN A 175 4227 4379 4000 -414 -384 -775 O
ATOM 1321 ND2 ASN A 175 24.811 10.492 31.620 1.00 30.28 N
ANISOU 1321 ND2 ASN A 175 3840 3987 3676 -489 -483 -961 N
ATOM 1322 N TYR A 176 23.306 6.930 29.054 1.00 26.31 N
ANISOU 1322 N TYR A 176 3280 3671 3045 -412 -259 -584 N
ATOM 1323 CA TYR A 176 22.540 5.691 29.141 1.00 25.30 C
ANISOU 1323 CA TYR A 176 3130 3630 2856 -322 -210 -531 C
ATOM 1324 C TYR A 176 22.743 4.832 27.898 1.00 24.59 C
ANISOU 1324 C TYR A 176 3021 3560 2760 -375 -162 -433 C
ATOM 1325 O TYR A 176 22.896 3.610 27.999 1.00 23.97 O
ANISOU 1325 O TYR A 176 2899 3576 2633 -339 -125 -406 O
ATOM 1326 CB TYR A 176 21.054 5.995 29.336 1.00 25.23 C
ANISOU 1326 CB TYR A 176 3167 3570 2848 -232 -215 -525 C
ATOM 1327 CG TYR A 176 20.157 4.817 29.018 1.00 24.30 C
ANISOU 1327 CG TYR A 176 3031 3512 2690 -177 -163 -444 C
ATOM 1328 CD1 TYR A 176 19.904 3.836 29.967 1.00 25.78 C
ANISOU 1328 CD1 TYR A 176 3174 3809 2811 -97 -136 -448 C
ATOM 1329 CD2 TYR A 176 19.573 4.680 27.763 1.00 23.88 C
ANISOU 1329 CD2 TYR A 176 3004 3406 2664 -210 -143 -362 C
ATOM 1330 CE1 TYR A 176 19.091 2.757 29.680 1.00 23.31 C
ANISOU 1330 CE1 TYR A 176 2846 3537 2473 -64 -92 -372 C
ATOM 1331 CE2 TYR A 176 18.765 3.603 27.465 1.00 23.28 C
ANISOU 1331 CE2 TYR A 176 2908 3381 2558 -171 -103 -298 C
ATOM 1332 CZ TYR A 176 18.526 2.644 28.427 1.00 35.35 C
ANISOU 1332 CZ TYR A 176 4394 5004 4034 -103 -77 -304 C
ATOM 1333 OH TYR A 176 17.716 1.571 28.133 1.00 31.80 O
ANISOU 1333 OH TYR A 176 3926 4591 3566 -79 -40 -238 O
ATOM 1334 N MET A 177 22.736 5.456 26.717 1.00 24.78 N
ANISOU 1334 N MET A 177 3085 3498 2834 -456 -162 -380 N
ATOM 1335 CA MET A 177 22.825 4.700 25.471 1.00 24.22 C
ANISOU 1335 CA MET A 177 3001 3454 2748 -496 -118 -293 C
ATOM 1336 C MET A 177 24.190 4.043 25.309 1.00 25.41 C
ANISOU 1336 C MET A 177 3083 3702 2872 -550 -94 -299 C
ATOM 1337 O MET A 177 24.292 2.947 24.747 1.00 27.54 O
ANISOU 1337 O MET A 177 3322 4038 3104 -535 -55 -258 O
ATOM 1338 CB MET A 177 22.534 5.613 24.279 1.00 25.63 C
ANISOU 1338 CB MET A 177 3238 3527 2972 -567 -127 -231 C
ATOM 1339 CG MET A 177 21.101 6.113 24.196 1.00 24.61 C
ANISOU 1339 CG MET A 177 3173 3313 2864 -499 -148 -211 C
ATOM 1340 SD MET A 177 19.903 4.773 24.056 1.00 33.53 S
ANISOU 1340 SD MET A 177 4281 4516 3943 -404 -111 -171 S
ATOM 1341 CE MET A 177 20.556 3.879 22.650 1.00 26.09 C
ANISOU 1341 CE MET A 177 3312 3631 2972 -476 -68 -99 C
ATOM 1342 N VAL A 178 25.248 4.699 25.782 1.00 25.00 N
ANISOU 1342 N VAL A 178 3001 3660 2840 -612 -121 -357 N
ATOM 1343 CA VAL A 178 26.607 4.207 25.592 1.00 25.23 C
ANISOU 1343 CA VAL A 178 2949 3792 2844 -668 -102 -366 C
ATOM 1344 C VAL A 178 26.990 3.265 26.727 1.00 31.63 C
ANISOU 1344 C VAL A 178 3703 4715 3601 -578 -104 -423 C
ATOM 1345 O VAL A 178 27.347 2.106 26.492 1.00 28.48 O
ANISOU 1345 O VAL A 178 3260 4404 3157 -540 -70 -399 O
ATOM 1346 CB VAL A 178 27.605 5.374 25.484 1.00 29.66 C
ANISOU 1346 CB VAL A 178 3493 4320 3456 -794 -131 -395 C
ATOM 1347 CG1 VAL A 178 29.030 4.856 25.467 1.00 26.73 C
ANISOU 1347 CG1 VAL A 178 3018 4084 3054 -842 -113 -419 C
ATOM 1348 CG2 VAL A 178 27.317 6.197 24.237 1.00 26.75 C
ANISOU 1348 CG2 VAL A 178 3183 3847 3134 -887 -122 -313 C
ATOM 1349 N TYR A 179 26.920 3.757 27.965 1.00 29.58 N
ANISOU 1349 N TYR A 179 3447 4452 3341 -538 -147 -500 N
ATOM 1350 CA TYR A 179 27.380 2.963 29.100 1.00 32.30 C
ANISOU 1350 CA TYR A 179 3736 4913 3625 -454 -154 -552 C
ATOM 1351 C TYR A 179 26.406 1.838 29.427 1.00 25.77 C
ANISOU 1351 C TYR A 179 2929 4112 2749 -338 -123 -505 C
ATOM 1352 O TYR A 179 26.808 0.678 29.565 1.00 40.29 O
ANISOU 1352 O TYR A 179 4728 6037 4542 -286 -100 -483 O
ATOM 1353 CB TYR A 179 27.586 3.861 30.320 1.00 32.50 C
ANISOU 1353 CB TYR A 179 3757 4938 3654 -443 -214 -655 C
ATOM 1354 CG TYR A 179 28.771 4.790 30.214 1.00 27.22 C
ANISOU 1354 CG TYR A 179 3047 4266 3030 -562 -251 -714 C
ATOM 1355 CD1 TYR A 179 29.951 4.379 29.608 1.00 27.43 C
ANISOU 1355 CD1 TYR A 179 2994 4378 3050 -632 -230 -695 C
ATOM 1356 CD2 TYR A 179 28.711 6.082 30.720 1.00 28.15 C
ANISOU 1356 CD2 TYR A 179 3200 4296 3199 -606 -310 -794 C
ATOM 1357 CE1 TYR A 179 31.040 5.228 29.512 1.00 28.54 C
ANISOU 1357 CE1 TYR A 179 3082 4526 3234 -756 -261 -745 C
ATOM 1358 CE2 TYR A 179 29.792 6.938 30.627 1.00 37.42 C
ANISOU 1358 CE2 TYR A 179 4335 5456 4426 -732 -349 -847 C
ATOM 1359 CZ TYR A 179 30.954 6.506 30.022 1.00 29.46 C
ANISOU 1359 CZ TYR A 179 3239 4545 3410 -813 -322 -818 C
ATOM 1360 OH TYR A 179 32.030 7.355 29.930 1.00 38.41 O
ANISOU 1360 OH TYR A 179 4320 5676 4597 -952 -357 -867 O
ATOM 1361 N PHE A 180 25.120 2.161 29.564 1.00 26.91 N
ANISOU 1361 N PHE A 180 3134 4182 2906 -297 -124 -487 N
ATOM 1362 CA PHE A 180 24.159 1.173 30.043 1.00 23.65 C
ANISOU 1362 CA PHE A 180 2733 3803 2450 -198 -96 -445 C
ATOM 1363 C PHE A 180 23.680 0.265 28.917 1.00 25.66 C
ANISOU 1363 C PHE A 180 3002 4032 2714 -209 -52 -357 C
ATOM 1364 O PHE A 180 23.732 -0.964 29.036 1.00 37.45 O
ANISOU 1364 O PHE A 180 4476 5580 4174 -161 -26 -321 O
ATOM 1365 CB PHE A 180 22.978 1.883 30.710 1.00 32.28 C
ANISOU 1365 CB PHE A 180 3868 4851 3545 -143 -113 -470 C
ATOM 1366 CG PHE A 180 22.059 0.969 31.481 1.00 27.71 C
ANISOU 1366 CG PHE A 180 3284 4333 2911 -44 -84 -434 C
ATOM 1367 CD1 PHE A 180 21.060 0.255 30.834 1.00 22.91 C
ANISOU 1367 CD1 PHE A 180 2694 3698 2314 -34 -46 -351 C
ATOM 1368 CD2 PHE A 180 22.172 0.851 32.858 1.00 35.68 C
ANISOU 1368 CD2 PHE A 180 4269 5433 3856 35 -97 -481 C
ATOM 1369 CE1 PHE A 180 20.206 -0.572 31.542 1.00 42.41 C
ANISOU 1369 CE1 PHE A 180 5154 6222 4739 40 -17 -308 C
ATOM 1370 CE2 PHE A 180 21.316 0.027 33.572 1.00 29.48 C
ANISOU 1370 CE2 PHE A 180 3476 4710 3015 118 -64 -431 C
ATOM 1371 CZ PHE A 180 20.335 -0.686 32.913 1.00 26.94 C
ANISOU 1371 CZ PHE A 180 3169 4352 2712 114 -23 -341 C
ATOM 1372 N ASN A 181 23.215 0.846 27.813 1.00 22.80 N
ANISOU 1372 N ASN A 181 2678 3586 2398 -270 -49 -324 N
ATOM 1373 CA ASN A 181 22.612 0.033 26.764 1.00 26.46 C
ANISOU 1373 CA ASN A 181 3158 4031 2867 -274 -15 -252 C
ATOM 1374 C ASN A 181 23.669 -0.671 25.921 1.00 29.36 C
ANISOU 1374 C ASN A 181 3490 4444 3222 -315 6 -237 C
ATOM 1375 O ASN A 181 23.654 -1.901 25.798 1.00 34.91 O
ANISOU 1375 O ASN A 181 4181 5183 3901 -272 29 -211 O
ATOM 1376 CB ASN A 181 21.706 0.894 25.886 1.00 22.20 C
ANISOU 1376 CB ASN A 181 2669 3400 2368 -310 -24 -221 C
ATOM 1377 CG ASN A 181 20.872 0.065 24.931 1.00 24.67 C
ANISOU 1377 CG ASN A 181 2995 3700 2678 -303 2 -157 C
ATOM 1378 OD1 ASN A 181 21.285 -0.202 23.803 1.00 32.05 O
ANISOU 1378 OD1 ASN A 181 3928 4637 3612 -352 16 -128 O
ATOM 1379 ND2 ASN A 181 19.695 -0.359 25.384 1.00 28.51 N
ANISOU 1379 ND2 ASN A 181 3488 4184 3158 -242 8 -139 N
ATOM 1380 N PHE A 182 24.600 0.087 25.338 1.00 22.60 N
ANISOU 1380 N PHE A 182 2618 3588 2383 -396 -1 -253 N
ATOM 1381 CA PHE A 182 25.573 -0.510 24.427 1.00 31.24 C
ANISOU 1381 CA PHE A 182 3669 4743 3457 -434 24 -238 C
ATOM 1382 C PHE A 182 26.595 -1.357 25.179 1.00 30.97 C
ANISOU 1382 C PHE A 182 3572 4809 3385 -383 26 -279 C
ATOM 1383 O PHE A 182 26.732 -2.558 24.920 1.00 37.25 O
ANISOU 1383 O PHE A 182 4354 5646 4154 -330 47 -264 O
ATOM 1384 CB PHE A 182 26.271 0.578 23.610 1.00 28.89 C
ANISOU 1384 CB PHE A 182 3363 4431 3185 -544 22 -232 C
ATOM 1385 CG PHE A 182 27.325 0.050 22.673 1.00 36.62 C
ANISOU 1385 CG PHE A 182 4284 5498 4133 -584 55 -220 C
ATOM 1386 CD1 PHE A 182 27.108 -1.111 21.944 1.00 23.79 C
ANISOU 1386 CD1 PHE A 182 2659 3906 2474 -534 84 -195 C
ATOM 1387 CD2 PHE A 182 28.530 0.716 22.515 1.00 25.54 C
ANISOU 1387 CD2 PHE A 182 2823 4147 2734 -672 55 -239 C
ATOM 1388 CE1 PHE A 182 28.072 -1.596 21.079 1.00 29.05 C
ANISOU 1388 CE1 PHE A 182 3270 4664 3103 -555 114 -196 C
ATOM 1389 CE2 PHE A 182 29.498 0.235 21.650 1.00 30.85 C
ANISOU 1389 CE2 PHE A 182 3429 4922 3369 -702 91 -229 C
ATOM 1390 CZ PHE A 182 29.268 -0.922 20.931 1.00 24.29 C
ANISOU 1390 CZ PHE A 182 2602 4132 2497 -636 121 -211 C
ATOM 1391 N PHE A 183 27.330 -0.744 26.108 1.00 29.19 N
ANISOU 1391 N PHE A 183 3310 4624 3158 -394 -3 -336 N
ATOM 1392 CA PHE A 183 28.419 -1.446 26.782 1.00 26.89 C
ANISOU 1392 CA PHE A 183 2949 4443 2826 -346 -9 -378 C
ATOM 1393 C PHE A 183 27.900 -2.630 27.589 1.00 28.45 C
ANISOU 1393 C PHE A 183 3163 4660 2987 -228 -4 -360 C
ATOM 1394 O PHE A 183 28.292 -3.778 27.357 1.00 26.90 O
ANISOU 1394 O PHE A 183 2947 4509 2765 -173 13 -343 O
ATOM 1395 CB PHE A 183 29.193 -0.480 27.684 1.00 24.48 C
ANISOU 1395 CB PHE A 183 2600 4176 2525 -383 -50 -450 C
ATOM 1396 CG PHE A 183 30.133 0.434 26.945 1.00 25.18 C
ANISOU 1396 CG PHE A 183 2644 4277 2646 -508 -53 -467 C
ATOM 1397 CD1 PHE A 183 30.362 0.271 25.588 1.00 34.24 C
ANISOU 1397 CD1 PHE A 183 3783 5429 3799 -568 -12 -414 C
ATOM 1398 CD2 PHE A 183 30.801 1.448 27.615 1.00 26.04 C
ANISOU 1398 CD2 PHE A 183 2717 4399 2777 -571 -96 -536 C
ATOM 1399 CE1 PHE A 183 31.232 1.111 24.911 1.00 25.93 C
ANISOU 1399 CE1 PHE A 183 2684 4398 2771 -692 -7 -414 C
ATOM 1400 CE2 PHE A 183 31.672 2.287 26.944 1.00 28.48 C
ANISOU 1400 CE2 PHE A 183 2982 4716 3124 -703 -97 -541 C
ATOM 1401 CZ PHE A 183 31.887 2.118 25.590 1.00 26.81 C
ANISOU 1401 CZ PHE A 183 2759 4513 2914 -766 -48 -473 C
ATOM 1402 N ALA A 184 27.000 -2.367 28.537 1.00 27.76 N
ANISOU 1402 N ALA A 184 3115 4538 2897 -184 -20 -361 N
ATOM 1403 CA ALA A 184 26.593 -3.394 29.491 1.00 29.41 C
ANISOU 1403 CA ALA A 184 3332 4779 3064 -80 -15 -337 C
ATOM 1404 C ALA A 184 25.587 -4.373 28.895 1.00 22.48 C
ANISOU 1404 C ALA A 184 2502 3839 2200 -55 18 -262 C
ATOM 1405 O ALA A 184 25.727 -5.589 29.058 1.00 32.14 O
ANISOU 1405 O ALA A 184 3725 5084 3402 8 30 -230 O
ATOM 1406 CB ALA A 184 26.014 -2.740 30.747 1.00 29.84 C
ANISOU 1406 CB ALA A 184 3401 4841 3096 -41 -39 -367 C
ATOM 1407 N CYS A 185 24.562 -3.870 28.210 1.00 32.53 N
ANISOU 1407 N CYS A 185 3818 5031 3511 -102 28 -236 N
ATOM 1408 CA CYS A 185 23.433 -4.715 27.841 1.00 21.67 C
ANISOU 1408 CA CYS A 185 2482 3603 2150 -80 52 -173 C
ATOM 1409 C CYS A 185 23.530 -5.297 26.438 1.00 21.44 C
ANISOU 1409 C CYS A 185 2462 3541 2143 -117 67 -152 C
ATOM 1410 O CYS A 185 22.781 -6.228 26.121 1.00 28.52 O
ANISOU 1410 O CYS A 185 3386 4398 3053 -98 81 -109 O
ATOM 1411 CB CYS A 185 22.123 -3.934 27.970 1.00 24.39 C
ANISOU 1411 CB CYS A 185 2857 3894 2515 -93 50 -158 C
ATOM 1412 SG CYS A 185 21.752 -3.385 29.650 1.00 48.22 S
ANISOU 1412 SG CYS A 185 5866 6961 5493 -28 36 -187 S
ATOM 1413 N VAL A 186 24.418 -4.781 25.589 1.00 24.95 N
ANISOU 1413 N VAL A 186 2883 4005 2590 -173 66 -181 N
ATOM 1414 CA VAL A 186 24.574 -5.261 24.221 1.00 22.50 C
ANISOU 1414 CA VAL A 186 2577 3686 2286 -202 83 -168 C
ATOM 1415 C VAL A 186 25.971 -5.820 23.978 1.00 30.06 C
ANISOU 1415 C VAL A 186 3484 4725 3214 -183 89 -203 C
ATOM 1416 O VAL A 186 26.128 -6.960 23.531 1.00 35.26 O
ANISOU 1416 O VAL A 186 4145 5388 3863 -137 98 -202 O
ATOM 1417 CB VAL A 186 24.244 -4.154 23.195 1.00 33.71 C
ANISOU 1417 CB VAL A 186 4015 5069 3725 -285 83 -156 C
ATOM 1418 CG1 VAL A 186 24.586 -4.615 21.787 1.00 21.57 C
ANISOU 1418 CG1 VAL A 186 2472 3552 2172 -312 102 -149 C
ATOM 1419 CG2 VAL A 186 22.774 -3.765 23.285 1.00 21.91 C
ANISOU 1419 CG2 VAL A 186 2568 3498 2257 -285 75 -123 C
ATOM 1420 N LEU A 187 27.003 -5.031 24.278 1.00 35.09 N
ANISOU 1420 N LEU A 187 4033 5749 3552 -163 -235 79 N
ATOM 1421 CA LEU A 187 28.363 -5.436 23.938 1.00 30.07 C
ANISOU 1421 CA LEU A 187 3318 5057 3051 -132 -215 33 C
ATOM 1422 C LEU A 187 28.813 -6.629 24.774 1.00 27.34 C
ANISOU 1422 C LEU A 187 2959 4681 2749 -65 -279 64 C
ATOM 1423 O LEU A 187 29.346 -7.606 24.237 1.00 37.23 O
ANISOU 1423 O LEU A 187 4200 5872 4076 -48 -236 54 O
ATOM 1424 CB LEU A 187 29.322 -4.258 24.111 1.00 33.35 C
ANISOU 1424 CB LEU A 187 3642 5487 3542 -126 -240 -16 C
ATOM 1425 CG LEU A 187 30.709 -4.435 23.494 1.00 31.73 C
ANISOU 1425 CG LEU A 187 3343 5227 3484 -107 -195 -59 C
ATOM 1426 CD1 LEU A 187 30.591 -4.889 22.046 1.00 40.60 C
ANISOU 1426 CD1 LEU A 187 4496 6315 4615 -141 -68 -73 C
ATOM 1427 CD2 LEU A 187 31.496 -3.140 23.584 1.00 41.83 C
ANISOU 1427 CD2 LEU A 187 4532 6521 4842 -116 -219 -98 C
ATOM 1428 N VAL A 188 28.606 -6.570 26.092 1.00 27.44 N
ANISOU 1428 N VAL A 188 2974 4738 2713 -20 -381 104 N
ATOM 1429 CA VAL A 188 29.015 -7.683 26.954 1.00 35.38 C
ANISOU 1429 CA VAL A 188 3963 5722 3757 47 -445 144 C
ATOM 1430 C VAL A 188 28.290 -8.977 26.605 1.00 32.74 C
ANISOU 1430 C VAL A 188 3695 5345 3401 40 -407 197 C
ATOM 1431 O VAL A 188 28.955 -10.022 26.501 1.00 35.57 O
ANISOU 1431 O VAL A 188 4027 5641 3848 74 -400 198 O
ATOM 1432 CB VAL A 188 28.860 -7.291 28.435 1.00 30.28 C
ANISOU 1432 CB VAL A 188 3312 5145 3046 103 -561 179 C
ATOM 1433 CG1 VAL A 188 28.955 -8.524 29.327 1.00 28.87 C
ANISOU 1433 CG1 VAL A 188 3134 4958 2879 171 -620 245 C
ATOM 1434 CG2 VAL A 188 29.917 -6.269 28.825 1.00 32.04 C
ANISOU 1434 CG2 VAL A 188 3452 5385 3335 124 -617 114 C
ATOM 1435 N PRO A 189 26.965 -9.000 26.412 1.00 39.88 N
ANISOU 1435 N PRO A 189 4681 6272 4198 -3 -385 244 N
ATOM 1436 CA PRO A 189 26.329 -10.258 25.986 1.00 27.49 C
ANISOU 1436 CA PRO A 189 3169 4646 2630 -16 -354 291 C
ATOM 1437 C PRO A 189 26.822 -10.769 24.642 1.00 28.30 C
ANISOU 1437 C PRO A 189 3270 4669 2812 -45 -266 227 C
ATOM 1438 O PRO A 189 26.898 -11.988 24.450 1.00 34.81 O
ANISOU 1438 O PRO A 189 4110 5424 3690 -26 -259 243 O
ATOM 1439 CB PRO A 189 24.838 -9.900 25.944 1.00 37.86 C
ANISOU 1439 CB PRO A 189 4560 6007 3818 -67 -346 347 C
ATOM 1440 CG PRO A 189 24.698 -8.763 26.886 1.00 37.24 C
ANISOU 1440 CG PRO A 189 4466 6017 3665 -45 -403 358 C
ATOM 1441 CD PRO A 189 25.959 -7.968 26.729 1.00 26.68 C
ANISOU 1441 CD PRO A 189 3053 4677 2407 -33 -402 269 C
ATOM 1442 N LEU A 190 27.161 -9.881 23.703 1.00 27.44 N
ANISOU 1442 N LEU A 190 3145 4568 2713 -84 -198 157 N
ATOM 1443 CA LEU A 190 27.691 -10.341 22.422 1.00 27.78 C
ANISOU 1443 CA LEU A 190 3186 4545 2823 -97 -109 96 C
ATOM 1444 C LEU A 190 29.049 -11.009 22.595 1.00 32.10 C
ANISOU 1444 C LEU A 190 3659 5039 3499 -32 -116 69 C
ATOM 1445 O LEU A 190 29.312 -12.059 21.997 1.00 29.24 O
ANISOU 1445 O LEU A 190 3313 4604 3192 -13 -76 51 O
ATOM 1446 CB LEU A 190 27.792 -9.177 21.439 1.00 27.35 C
ANISOU 1446 CB LEU A 190 3119 4522 2751 -146 -31 40 C
ATOM 1447 CG LEU A 190 26.486 -8.711 20.797 1.00 36.24 C
ANISOU 1447 CG LEU A 190 4326 5682 3763 -217 8 55 C
ATOM 1448 CD1 LEU A 190 26.727 -7.463 19.964 1.00 36.93 C
ANISOU 1448 CD1 LEU A 190 4383 5806 3842 -256 79 7 C
ATOM 1449 CD2 LEU A 190 25.888 -9.820 19.947 1.00 26.68 C
ANISOU 1449 CD2 LEU A 190 3191 4410 2536 -237 49 54 C
ATOM 1450 N LEU A 191 29.923 -10.413 23.411 1.00 31.20 N
ANISOU 1450 N LEU A 191 3462 4957 3434 7 -170 63 N
ATOM 1451 CA LEU A 191 31.215 -11.030 23.687 1.00 29.90 C
ANISOU 1451 CA LEU A 191 3219 4746 3394 71 -186 48 C
ATOM 1452 C LEU A 191 31.052 -12.362 24.407 1.00 40.64 C
ANISOU 1452 C LEU A 191 4602 6066 4773 118 -242 105 C
ATOM 1453 O LEU A 191 31.886 -13.260 24.249 1.00 32.44 O
ANISOU 1453 O LEU A 191 3528 4963 3836 163 -226 93 O
ATOM 1454 CB LEU A 191 32.082 -10.078 24.511 1.00 33.41 C
ANISOU 1454 CB LEU A 191 3573 5236 3885 98 -252 36 C
ATOM 1455 CG LEU A 191 32.397 -8.728 23.862 1.00 42.18 C
ANISOU 1455 CG LEU A 191 4641 6378 5008 56 -204 -16 C
ATOM 1456 CD1 LEU A 191 33.165 -7.831 24.823 1.00 30.10 C
ANISOU 1456 CD1 LEU A 191 3025 4886 3527 83 -294 -25 C
ATOM 1457 CD2 LEU A 191 33.170 -8.918 22.565 1.00 30.22 C
ANISOU 1457 CD2 LEU A 191 3090 4812 3581 53 -92 -62 C
ATOM 1458 N LEU A 192 29.985 -12.510 25.198 1.00 29.96 N
ANISOU 1458 N LEU A 192 3306 4750 3327 110 -303 174 N
ATOM 1459 CA LEU A 192 29.722 -13.785 25.856 1.00 30.43 C
ANISOU 1459 CA LEU A 192 3385 4771 3405 151 -352 244 C
ATOM 1460 C LEU A 192 29.308 -14.852 24.851 1.00 34.13 C
ANISOU 1460 C LEU A 192 3915 5153 3901 127 -289 235 C
ATOM 1461 O LEU A 192 29.759 -15.999 24.939 1.00 31.35 O
ANISOU 1461 O LEU A 192 3548 4729 3635 171 -297 249 O
ATOM 1462 CB LEU A 192 28.646 -13.614 26.927 1.00 32.29 C
ANISOU 1462 CB LEU A 192 3662 5077 3532 153 -426 332 C
ATOM 1463 CG LEU A 192 29.056 -12.847 28.184 1.00 45.52 C
ANISOU 1463 CG LEU A 192 5284 6833 5178 202 -513 350 C
ATOM 1464 CD1 LEU A 192 27.882 -12.716 29.142 1.00 41.72 C
ANISOU 1464 CD1 LEU A 192 4854 6425 4573 211 -572 440 C
ATOM 1465 CD2 LEU A 192 30.232 -13.534 28.859 1.00 38.78 C
ANISOU 1465 CD2 LEU A 192 4354 5951 4431 278 -564 357 C
ATOM 1466 N MET A 193 28.443 -14.498 23.895 1.00 29.97 N
ANISOU 1466 N MET A 193 3456 4628 3303 60 -230 210 N
ATOM 1467 CA MET A 193 28.059 -15.455 22.861 1.00 30.21 C
ANISOU 1467 CA MET A 193 3550 4574 3356 36 -176 186 C
ATOM 1468 C MET A 193 29.261 -15.860 22.021 1.00 32.06 C
ANISOU 1468 C MET A 193 3744 4742 3694 73 -110 104 C
ATOM 1469 O MET A 193 29.373 -17.018 21.601 1.00 38.31 O
ANISOU 1469 O MET A 193 4563 5446 4549 96 -95 91 O
ATOM 1470 CB MET A 193 26.966 -14.867 21.968 1.00 29.43 C
ANISOU 1470 CB MET A 193 3527 4501 3155 -42 -128 169 C
ATOM 1471 CG MET A 193 25.736 -14.392 22.710 1.00 35.70 C
ANISOU 1471 CG MET A 193 4358 5363 3842 -78 -182 252 C
ATOM 1472 SD MET A 193 24.637 -13.450 21.638 1.00 44.93 S
ANISOU 1472 SD MET A 193 5599 6575 4898 -169 -119 226 S
ATOM 1473 CE MET A 193 23.733 -12.501 22.856 1.00 29.41 C
ANISOU 1473 CE MET A 193 3636 4717 2824 -181 -185 316 C
ATOM 1474 N LEU A 194 30.165 -14.914 21.756 1.00 30.93 N
ANISOU 1474 N LEU A 194 3536 4638 3576 81 -70 51 N
ATOM 1475 CA LEU A 194 31.409 -15.253 21.074 1.00 36.94 C
ANISOU 1475 CA LEU A 194 4244 5346 4444 128 -6 -13 C
ATOM 1476 C LEU A 194 32.197 -16.288 21.865 1.00 37.46 C
ANISOU 1476 C LEU A 194 4259 5358 4616 200 -58 19 C
ATOM 1477 O LEU A 194 32.784 -17.208 21.286 1.00 39.22 O
ANISOU 1477 O LEU A 194 4480 5501 4920 241 -14 -16 O
ATOM 1478 CB LEU A 194 32.247 -13.993 20.851 1.00 31.88 C
ANISOU 1478 CB LEU A 194 3525 4763 3825 125 32 -53 C
ATOM 1479 CG LEU A 194 33.620 -14.178 20.199 1.00 40.99 C
ANISOU 1479 CG LEU A 194 4605 5875 5096 178 103 -105 C
ATOM 1480 CD1 LEU A 194 33.480 -14.655 18.762 1.00 43.18 C
ANISOU 1480 CD1 LEU A 194 4944 6103 5360 174 209 -164 C
ATOM 1481 CD2 LEU A 194 34.437 -12.894 20.268 1.00 43.51 C
ANISOU 1481 CD2 LEU A 194 4827 6252 5453 174 115 -120 C
ATOM 1482 N GLY A 195 32.211 -16.161 23.194 1.00 32.55 N
ANISOU 1482 N GLY A 195 3596 4779 3990 223 -152 85 N
ATOM 1483 CA GLY A 195 32.925 -17.127 24.011 1.00 37.07 C
ANISOU 1483 CA GLY A 195 4118 5308 4659 293 -207 125 C
ATOM 1484 C GLY A 195 32.243 -18.480 24.045 1.00 35.64 C
ANISOU 1484 C GLY A 195 4000 5051 4491 301 -224 169 C
ATOM 1485 O GLY A 195 32.907 -19.521 24.042 1.00 44.17 O
ANISOU 1485 O GLY A 195 5055 6054 5675 355 -221 169 O
ATOM 1486 N VAL A 196 30.911 -18.485 24.075 1.00 33.10 N
ANISOU 1486 N VAL A 196 3758 4745 4072 248 -245 212 N
ATOM 1487 CA VAL A 196 30.171 -19.742 24.098 1.00 33.45 C
ANISOU 1487 CA VAL A 196 3861 4712 4137 247 -269 262 C
ATOM 1488 C VAL A 196 30.375 -20.504 22.794 1.00 33.99 C
ANISOU 1488 C VAL A 196 3972 4676 4264 245 -195 181 C
ATOM 1489 O VAL A 196 30.629 -21.714 22.798 1.00 34.83 O
ANISOU 1489 O VAL A 196 4081 4689 4464 285 -207 191 O
ATOM 1490 CB VAL A 196 28.680 -19.478 24.377 1.00 32.67 C
ANISOU 1490 CB VAL A 196 3830 4658 3924 187 -305 331 C
ATOM 1491 CG1 VAL A 196 27.875 -20.762 24.251 1.00 33.10 C
ANISOU 1491 CG1 VAL A 196 3942 4620 4014 176 -328 383 C
ATOM 1492 CG2 VAL A 196 28.501 -18.872 25.760 1.00 35.57 C
ANISOU 1492 CG2 VAL A 196 4158 5125 4232 210 -382 416 C
ATOM 1493 N TYR A 197 30.280 -19.809 21.658 1.00 33.58 N
ANISOU 1493 N TYR A 197 3957 4642 4160 203 -118 99 N
ATOM 1494 CA TYR A 197 30.431 -20.488 20.374 1.00 34.15 C
ANISOU 1494 CA TYR A 197 4081 4625 4269 208 -46 15 C
ATOM 1495 C TYR A 197 31.856 -20.986 20.170 1.00 35.13 C
ANISOU 1495 C TYR A 197 4140 4696 4513 288 -5 -34 C
ATOM 1496 O TYR A 197 32.065 -22.051 19.577 1.00 40.11 O
ANISOU 1496 O TYR A 197 4804 5227 5210 322 21 -75 O
ATOM 1497 CB TYR A 197 30.008 -19.566 19.229 1.00 33.52 C
ANISOU 1497 CB TYR A 197 4052 4591 4094 152 28 -54 C
ATOM 1498 CG TYR A 197 28.511 -19.506 19.042 1.00 41.66 C
ANISOU 1498 CG TYR A 197 5172 5631 5024 75 0 -22 C
ATOM 1499 CD1 TYR A 197 27.797 -20.632 18.646 1.00 35.67 C
ANISOU 1499 CD1 TYR A 197 4491 4778 4286 62 -23 -22 C
ATOM 1500 CD2 TYR A 197 27.809 -18.327 19.260 1.00 31.81 C
ANISOU 1500 CD2 TYR A 197 3932 4484 3671 17 -7 10 C
ATOM 1501 CE1 TYR A 197 26.426 -20.586 18.477 1.00 32.76 C
ANISOU 1501 CE1 TYR A 197 4196 4415 3835 -10 -54 15 C
ATOM 1502 CE2 TYR A 197 26.436 -18.271 19.090 1.00 33.03 C
ANISOU 1502 CE2 TYR A 197 4163 4650 3738 -52 -31 47 C
ATOM 1503 CZ TYR A 197 25.751 -19.405 18.702 1.00 35.40 C
ANISOU 1503 CZ TYR A 197 4533 4856 4062 -67 -56 52 C
ATOM 1504 OH TYR A 197 24.386 -19.361 18.534 1.00 36.28 O
ANISOU 1504 OH TYR A 197 4715 4975 4096 -137 -85 96 O
ATOM 1505 N LEU A 198 32.850 -20.237 20.655 1.00 35.12 N
ANISOU 1505 N LEU A 198 4043 4757 4545 320 0 -31 N
ATOM 1506 CA LEU A 198 34.225 -20.723 20.591 1.00 42.13 C
ANISOU 1506 CA LEU A 198 4854 5596 5556 398 33 -60 C
ATOM 1507 C LEU A 198 34.394 -21.995 21.410 1.00 36.87 C
ANISOU 1507 C LEU A 198 4173 4856 4981 450 -34 -1 C
ATOM 1508 O LEU A 198 35.127 -22.906 21.011 1.00 39.22 O
ANISOU 1508 O LEU A 198 4457 5067 5379 510 2 -35 O
ATOM 1509 CB LEU A 198 35.195 -19.641 21.065 1.00 35.97 C
ANISOU 1509 CB LEU A 198 3968 4898 4802 415 33 -55 C
ATOM 1510 CG LEU A 198 35.466 -18.532 20.046 1.00 51.06 C
ANISOU 1510 CG LEU A 198 5867 6859 6674 388 124 -121 C
ATOM 1511 CD1 LEU A 198 36.437 -17.502 20.601 1.00 51.93 C
ANISOU 1511 CD1 LEU A 198 5862 7036 6832 402 108 -108 C
ATOM 1512 CD2 LEU A 198 35.990 -19.123 18.747 1.00 42.13 C
ANISOU 1512 CD2 LEU A 198 4760 5659 5588 428 231 -197 C
ATOM 1513 N ARG A 199 33.714 -22.078 22.557 1.00 36.50 N
ANISOU 1513 N ARG A 199 4126 4841 4901 433 -128 92 N
ATOM 1514 CA ARG A 199 33.753 -23.305 23.343 1.00 37.23 C
ANISOU 1514 CA ARG A 199 4204 4865 5078 480 -191 162 C
ATOM 1515 C ARG A 199 32.988 -24.432 22.661 1.00 37.63 C
ANISOU 1515 C ARG A 199 4345 4804 5149 464 -181 148 C
ATOM 1516 O ARG A 199 33.352 -25.604 22.813 1.00 38.58 O
ANISOU 1516 O ARG A 199 4453 4828 5377 515 -198 166 O
ATOM 1517 CB ARG A 199 33.196 -23.053 24.743 1.00 36.79 C
ANISOU 1517 CB ARG A 199 4124 4884 4970 472 -290 274 C
ATOM 1518 CG ARG A 199 34.052 -22.130 25.594 1.00 36.67 C
ANISOU 1518 CG ARG A 199 4014 4964 4953 504 -324 289 C
ATOM 1519 CD ARG A 199 33.501 -22.018 27.006 1.00 43.81 C
ANISOU 1519 CD ARG A 199 4903 5942 5802 513 -424 399 C
ATOM 1520 N ILE A 200 31.935 -24.102 21.910 1.00 36.99 N
ANISOU 1520 N ILE A 200 4352 4730 4973 393 -159 116 N
ATOM 1521 CA ILE A 200 31.192 -25.126 21.181 1.00 37.44 C
ANISOU 1521 CA ILE A 200 4498 4677 5050 373 -157 91 C
ATOM 1522 C ILE A 200 32.068 -25.752 20.103 1.00 38.40 C
ANISOU 1522 C ILE A 200 4634 4707 5251 427 -82 -18 C
ATOM 1523 O ILE A 200 32.160 -26.979 19.990 1.00 39.36 O
ANISOU 1523 O ILE A 200 4776 4711 5468 465 -99 -23 O
ATOM 1524 CB ILE A 200 29.902 -24.536 20.583 1.00 36.56 C
ANISOU 1524 CB ILE A 200 4474 4602 4814 285 -152 79 C
ATOM 1525 CG1 ILE A 200 28.908 -24.176 21.687 1.00 35.80 C
ANISOU 1525 CG1 ILE A 200 4372 4578 4651 241 -231 201 C
ATOM 1526 CG2 ILE A 200 29.274 -25.515 19.605 1.00 37.14 C
ANISOU 1526 CG2 ILE A 200 4642 4558 4913 266 -145 25 C
ATOM 1527 CD1 ILE A 200 27.621 -23.563 21.167 1.00 34.92 C
ANISOU 1527 CD1 ILE A 200 4340 4508 4421 154 -227 201 C
ATOM 1528 N PHE A 201 32.726 -24.916 19.297 1.00 38.24 N
ANISOU 1528 N PHE A 201 4599 4738 5193 436 5 -102 N
ATOM 1529 CA PHE A 201 33.602 -25.432 18.251 1.00 39.21 C
ANISOU 1529 CA PHE A 201 4731 4787 5379 499 89 -203 C
ATOM 1530 C PHE A 201 34.816 -26.140 18.837 1.00 40.18 C
ANISOU 1530 C PHE A 201 4767 4860 5641 588 84 -180 C
ATOM 1531 O PHE A 201 35.293 -27.126 18.264 1.00 46.44 O
ANISOU 1531 O PHE A 201 5582 5549 6516 648 118 -235 O
ATOM 1532 CB PHE A 201 34.034 -24.296 17.324 1.00 38.82 C
ANISOU 1532 CB PHE A 201 4674 4819 5259 492 187 -279 C
ATOM 1533 CG PHE A 201 32.896 -23.669 16.569 1.00 38.01 C
ANISOU 1533 CG PHE A 201 4661 4758 5023 412 203 -312 C
ATOM 1534 CD1 PHE A 201 31.995 -24.455 15.873 1.00 42.58 C
ANISOU 1534 CD1 PHE A 201 5349 5255 5575 387 189 -354 C
ATOM 1535 CD2 PHE A 201 32.719 -22.295 16.569 1.00 37.00 C
ANISOU 1535 CD2 PHE A 201 4507 4747 4802 360 227 -300 C
ATOM 1536 CE1 PHE A 201 30.943 -23.882 15.181 1.00 52.66 C
ANISOU 1536 CE1 PHE A 201 6706 6572 6730 313 200 -381 C
ATOM 1537 CE2 PHE A 201 31.669 -21.717 15.882 1.00 36.27 C
ANISOU 1537 CE2 PHE A 201 4494 4695 4590 288 244 -325 C
ATOM 1538 CZ PHE A 201 30.780 -22.511 15.187 1.00 36.56 C
ANISOU 1538 CZ PHE A 201 4640 4656 4597 264 230 -364 C
ATOM 1539 N LEU A 202 35.326 -25.658 19.973 1.00 43.23 N
ANISOU 1539 N LEU A 202 5055 5317 6053 600 39 -101 N
ATOM 1540 CA LEU A 202 36.418 -26.356 20.644 1.00 45.47 C
ANISOU 1540 CA LEU A 202 5251 5557 6469 682 21 -64 C
ATOM 1541 C LEU A 202 35.971 -27.722 21.144 1.00 41.49 C
ANISOU 1541 C LEU A 202 4777 4946 6042 701 -47 -9 C
ATOM 1542 O LEU A 202 36.706 -28.708 21.013 1.00 42.60 O
ANISOU 1542 O LEU A 202 4895 4990 6299 772 -29 -27 O
ATOM 1543 CB LEU A 202 36.952 -25.516 21.803 1.00 44.57 C
ANISOU 1543 CB LEU A 202 5032 5547 6356 686 -30 10 C
ATOM 1544 CG LEU A 202 37.966 -24.429 21.449 1.00 49.52 C
ANISOU 1544 CG LEU A 202 5582 6248 6985 702 36 -37 C
ATOM 1545 CD1 LEU A 202 38.301 -23.595 22.674 1.00 55.20 C
ANISOU 1545 CD1 LEU A 202 6210 7066 7697 696 -40 35 C
ATOM 1546 CD2 LEU A 202 39.220 -25.058 20.869 1.00 65.86 C
ANISOU 1546 CD2 LEU A 202 7602 8247 9176 787 110 -85 C
ATOM 1547 N ALA A 203 34.771 -27.800 21.724 1.00 41.51 N
ANISOU 1547 N ALA A 203 4825 4962 5986 640 -125 65 N
ATOM 1548 CA ALA A 203 34.265 -29.085 22.192 1.00 41.56 C
ANISOU 1548 CA ALA A 203 4855 4863 6073 653 -192 131 C
ATOM 1549 C ALA A 203 34.058 -30.046 21.030 1.00 42.38 C
ANISOU 1549 C ALA A 203 5046 4830 6225 662 -154 39 C
ATOM 1550 O ALA A 203 34.313 -31.249 21.156 1.00 49.32 O
ANISOU 1550 O ALA A 203 5920 5592 7226 712 -177 53 O
ATOM 1551 CB ALA A 203 32.964 -28.887 22.970 1.00 40.76 C
ANISOU 1551 CB ALA A 203 4783 4812 5893 585 -273 236 C
ATOM 1552 N ALA A 204 33.606 -29.533 19.885 1.00 41.97 N
ANISOU 1552 N ALA A 204 5075 4791 6081 619 -97 -59 N
ATOM 1553 CA ALA A 204 33.413 -30.390 18.720 1.00 47.67 C
ANISOU 1553 CA ALA A 204 5888 5389 6834 634 -65 -161 C
ATOM 1554 C ALA A 204 34.748 -30.859 18.155 1.00 48.10 C
ANISOU 1554 C ALA A 204 5911 5385 6981 733 13 -244 C
ATOM 1555 O ALA A 204 34.914 -32.040 17.830 1.00 47.02 O
ANISOU 1555 O ALA A 204 5808 5114 6944 783 7 -282 O
ATOM 1556 CB ALA A 204 32.604 -29.652 17.655 1.00 42.13 C
ANISOU 1556 CB ALA A 204 5280 4731 5997 566 -25 -242 C
ATOM 1557 N ARG A 205 35.714 -29.946 18.030 1.00 43.68 N
ANISOU 1557 N ARG A 205 5282 4920 6395 765 87 -270 N
ATOM 1558 CA ARG A 205 37.021 -30.328 17.504 1.00 44.77 C
ANISOU 1558 CA ARG A 205 5378 5011 6620 864 170 -336 C
ATOM 1559 C ARG A 205 37.710 -31.335 18.417 1.00 53.07 C
ANISOU 1559 C ARG A 205 6355 5986 7823 932 123 -266 C
ATOM 1560 O ARG A 205 38.394 -32.251 17.942 1.00 46.91 O
ANISOU 1560 O ARG A 205 5580 5102 7140 1013 164 -321 O
ATOM 1561 CB ARG A 205 37.897 -29.089 17.315 1.00 44.30 C
ANISOU 1561 CB ARG A 205 5241 5074 6516 878 249 -353 C
ATOM 1562 CG ARG A 205 39.241 -29.380 16.665 1.00 45.44 C
ANISOU 1562 CG ARG A 205 5338 5182 6744 982 349 -417 C
ATOM 1563 CD ARG A 205 40.150 -28.161 16.681 1.00 61.65 C
ANISOU 1563 CD ARG A 205 7288 7354 8780 993 413 -405 C
ATOM 1564 NE ARG A 205 40.626 -27.841 18.022 1.00 62.98 N
ANISOU 1564 NE ARG A 205 7342 7578 9010 988 341 -299 N
ATOM 1565 CZ ARG A 205 41.506 -26.886 18.294 1.00 66.34 C
ANISOU 1565 CZ ARG A 205 7660 8093 9455 1000 369 -273 C
ATOM 1566 NH1 ARG A 205 42.024 -26.132 17.338 1.00 66.02 N
ANISOU 1566 NH1 ARG A 205 7602 8101 9384 1015 474 -331 N
ATOM 1567 NH2 ARG A 205 41.878 -26.685 19.555 1.00 58.81 N
ANISOU 1567 NH2 ARG A 205 6610 7182 8554 998 287 -182 N
ATOM 1568 N ARG A 206 37.537 -31.187 19.733 1.00 45.16 N
ANISOU 1568 N ARG A 206 5284 5036 6838 905 38 -144 N
ATOM 1569 CA ARG A 206 38.178 -32.102 20.670 1.00 49.56 C
ANISOU 1569 CA ARG A 206 5764 5532 7534 969 -10 -64 C
ATOM 1570 C ARG A 206 37.536 -33.482 20.622 1.00 46.86 C
ANISOU 1570 C ARG A 206 5488 5040 7275 976 -63 -53 C
ATOM 1571 O ARG A 206 38.234 -34.500 20.695 1.00 48.04 O
ANISOU 1571 O ARG A 206 5608 5087 7558 1052 -58 -53 O
ATOM 1572 CB ARG A 206 38.121 -31.528 22.087 1.00 50.51 C
ANISOU 1572 CB ARG A 206 5798 5758 7635 943 -90 65 C
ATOM 1573 CG ARG A 206 38.837 -32.364 23.134 1.00 48.44 C
ANISOU 1573 CG ARG A 206 5444 5454 7506 1012 -141 158 C
ATOM 1574 CD ARG A 206 38.890 -31.652 24.482 1.00 78.31 C
ANISOU 1574 CD ARG A 206 9143 9362 11251 998 -216 272 C
ATOM 1575 NE ARG A 206 39.756 -30.477 24.463 1.00 97.54 N
ANISOU 1575 NE ARG A 206 11507 11907 13646 1006 -176 238 N
ATOM 1576 CZ ARG A 206 39.326 -29.223 24.404 1.00 86.80 C
ANISOU 1576 CZ ARG A 206 10162 10660 12160 942 -174 220 C
ATOM 1577 NH1 ARG A 206 38.035 -28.936 24.359 1.00 80.94 N
ANISOU 1577 NH1 ARG A 206 9503 9944 11307 866 -205 234 N
ATOM 1578 NH2 ARG A 206 40.213 -28.232 24.394 1.00 70.54 N
ANISOU 1578 NH2 ARG A 206 8027 8683 10092 954 -142 193 N
ATOM 1579 N GLN A 207 36.208 -33.540 20.493 1.00 46.80 N
ANISOU 1579 N GLN A 207 5568 5015 7199 896 -115 -42 N
ATOM 1580 CA GLN A 207 35.532 -34.832 20.448 1.00 48.23 C
ANISOU 1580 CA GLN A 207 5808 5047 7470 894 -175 -26 C
ATOM 1581 C GLN A 207 35.789 -35.550 19.127 1.00 48.24 C
ANISOU 1581 C GLN A 207 5893 4921 7514 940 -116 -172 C
ATOM 1582 O GLN A 207 35.895 -36.781 19.095 1.00 49.44 O
ANISOU 1582 O GLN A 207 6061 4928 7796 987 -145 -177 O
ATOM 1583 CB GLN A 207 34.031 -34.647 20.677 1.00 46.32 C
ANISOU 1583 CB GLN A 207 5628 4824 7148 793 -250 35 C
ATOM 1584 CG GLN A 207 33.671 -34.185 22.078 1.00 45.51 C
ANISOU 1584 CG GLN A 207 5450 4828 7014 761 -320 192 C
ATOM 1585 CD GLN A 207 32.189 -33.935 22.248 1.00 46.24 C
ANISOU 1585 CD GLN A 207 5602 4947 7021 666 -382 256 C
ATOM 1586 OE1 GLN A 207 31.367 -34.488 21.515 1.00 50.43 O
ANISOU 1586 OE1 GLN A 207 6220 5378 7562 626 -401 211 O
ATOM 1587 NE2 GLN A 207 31.836 -33.094 23.215 1.00 53.40 N
ANISOU 1587 NE2 GLN A 207 6460 5989 7841 634 -416 361 N
ATOM 1588 N LEU A 208 35.880 -34.800 18.025 1.00 52.16 N
ANISOU 1588 N LEU A 208 6446 5470 7902 933 -34 -290 N
ATOM 1589 CA LEU A 208 36.225 -35.409 16.744 1.00 49.02 C
ANISOU 1589 CA LEU A 208 6128 4968 7528 994 33 -435 C
ATOM 1590 C LEU A 208 37.632 -35.989 16.775 1.00 50.19 C
ANISOU 1590 C LEU A 208 6205 5064 7800 1112 92 -456 C
ATOM 1591 O LEU A 208 37.883 -37.057 16.205 1.00 51.52 O
ANISOU 1591 O LEU A 208 6423 5093 8058 1179 104 -530 O
ATOM 1592 CB LEU A 208 36.088 -34.382 15.618 1.00 48.40 C
ANISOU 1592 CB LEU A 208 6112 4980 7297 970 116 -542 C
ATOM 1593 CG LEU A 208 34.660 -34.000 15.222 1.00 60.80 C
ANISOU 1593 CG LEU A 208 7782 6572 8749 864 67 -558 C
ATOM 1594 CD1 LEU A 208 34.651 -32.717 14.402 1.00 46.69 C
ANISOU 1594 CD1 LEU A 208 6019 4915 6806 836 153 -625 C
ATOM 1595 CD2 LEU A 208 34.007 -35.137 14.451 1.00 54.20 C
ANISOU 1595 CD2 LEU A 208 7062 5575 7956 869 25 -644 C
ATOM 1596 N ALA A1001 38.561 -35.303 17.444 1.00 49.78 N
ANISOU 1596 N ALA A1001 6036 5120 7760 1140 126 -390 N
ATOM 1597 CA ALA A1001 39.916 -35.825 17.575 1.00 58.64 C
ANISOU 1597 CA ALA A1001 7075 6198 9007 1249 178 -391 C
ATOM 1598 C ALA A1001 39.945 -37.081 18.437 1.00 59.98 C
ANISOU 1598 C ALA A1001 7211 6248 9331 1282 98 -308 C
ATOM 1599 O ALA A1001 40.716 -38.009 18.165 1.00 53.11 O
ANISOU 1599 O ALA A1001 6331 5269 8581 1375 132 -348 O
ATOM 1600 CB ALA A1001 40.835 -34.752 18.156 1.00 50.24 C
ANISOU 1600 CB ALA A1001 5886 5278 7924 1260 217 -330 C
ATOM 1601 N ASP A1002 39.108 -37.133 19.477 1.00 51.47 N
ANISOU 1601 N ASP A1002 6114 5189 8254 1211 -7 -188 N
ATOM 1602 CA ASP A1002 39.098 -38.295 20.362 1.00 51.95 C
ANISOU 1602 CA ASP A1002 6134 5144 8463 1241 -85 -90 C
ATOM 1603 C ASP A1002 38.590 -39.539 19.642 1.00 64.18 C
ANISOU 1603 C ASP A1002 7782 6508 10095 1258 -108 -163 C
ATOM 1604 O ASP A1002 39.103 -40.642 19.863 1.00 71.51 O
ANISOU 1604 O ASP A1002 8682 7313 11177 1329 -122 -144 O
ATOM 1605 CB ASP A1002 38.250 -38.008 21.602 1.00 51.00 C
ANISOU 1605 CB ASP A1002 5972 5098 8308 1165 -186 62 C
ATOM 1606 CG ASP A1002 38.832 -36.902 22.467 1.00 83.51 C
ANISOU 1606 CG ASP A1002 9985 9384 12362 1162 -181 138 C
ATOM 1607 OD1 ASP A1002 39.963 -36.449 22.185 1.00 87.14 O
ANISOU 1607 OD1 ASP A1002 10389 9891 12830 1219 -106 86 O
ATOM 1608 OD2 ASP A1002 38.154 -36.482 23.429 1.00 95.32 O
ANISOU 1608 OD2 ASP A1002 11453 10964 13800 1106 -255 250 O
ATOM 1609 N LEU A1003 37.581 -39.386 18.780 1.00 52.78 N
ANISOU 1609 N LEU A1003 6456 5040 8558 1193 -117 -248 N
ATOM 1610 CA LEU A1003 37.073 -40.533 18.033 1.00 53.96 C
ANISOU 1610 CA LEU A1003 6708 5010 8785 1207 -149 -332 C
ATOM 1611 C LEU A1003 38.130 -41.088 17.087 1.00 64.48 C
ANISOU 1611 C LEU A1003 8067 6254 10178 1322 -59 -468 C
ATOM 1612 O LEU A1003 38.262 -42.309 16.944 1.00 61.13 O
ANISOU 1612 O LEU A1003 7669 5664 9893 1379 -87 -497 O
ATOM 1613 CB LEU A1003 35.812 -40.147 17.263 1.00 53.32 C
ANISOU 1613 CB LEU A1003 6745 4933 8579 1114 -178 -401 C
ATOM 1614 CG LEU A1003 34.578 -39.842 18.114 1.00 65.71 C
ANISOU 1614 CG LEU A1003 8305 6554 10108 1002 -277 -267 C
ATOM 1615 CD1 LEU A1003 33.388 -39.490 17.233 1.00 51.72 C
ANISOU 1615 CD1 LEU A1003 6652 4780 8219 916 -300 -344 C
ATOM 1616 CD2 LEU A1003 34.251 -41.019 19.021 1.00 64.54 C
ANISOU 1616 CD2 LEU A1003 8116 6280 10126 1005 -375 -145 C
ATOM 1617 N GLU A1004 38.898 -40.211 16.437 1.00 72.75 N
ANISOU 1617 N GLU A1004 9105 7408 11130 1363 52 -547 N
ATOM 1618 CA GLU A1004 39.957 -40.684 15.552 1.00 67.05 C
ANISOU 1618 CA GLU A1004 8399 6617 10458 1484 150 -666 C
ATOM 1619 C GLU A1004 41.111 -41.296 16.337 1.00 59.53 C
ANISOU 1619 C GLU A1004 7329 5625 9664 1574 164 -587 C
ATOM 1620 O GLU A1004 41.736 -42.255 15.869 1.00 58.71 O
ANISOU 1620 O GLU A1004 7246 5394 9668 1674 200 -657 O
ATOM 1621 CB GLU A1004 40.456 -39.542 14.667 1.00 72.88 C
ANISOU 1621 CB GLU A1004 9149 7490 11053 1504 269 -753 C
ATOM 1622 CG GLU A1004 39.420 -39.021 13.681 1.00 81.07 C
ANISOU 1622 CG GLU A1004 10314 8557 11934 1435 270 -853 C
ATOM 1623 CD GLU A1004 39.016 -40.059 12.648 1.00 98.18 C
ANISOU 1623 CD GLU A1004 12616 10562 14125 1479 257 -993 C
ATOM 1624 OE1 GLU A1004 39.849 -40.931 12.316 1.00 87.52 O
ANISOU 1624 OE1 GLU A1004 11269 9105 12879 1593 301 -1055 O
ATOM 1625 OE2 GLU A1004 37.862 -40.003 12.170 1.00 88.85 O
ANISOU 1625 OE2 GLU A1004 11540 9358 12860 1400 199 -1042 O
ATOM 1626 N ASP A1005 41.406 -40.764 17.525 1.00 56.36 N
ANISOU 1626 N ASP A1005 6804 5331 9278 1544 134 -443 N
ATOM 1627 CA ASP A1005 42.455 -41.348 18.354 1.00 57.17 C
ANISOU 1627 CA ASP A1005 6789 5401 9532 1625 135 -355 C
ATOM 1628 C ASP A1005 42.080 -42.756 18.799 1.00 58.26 C
ANISOU 1628 C ASP A1005 6943 5367 9826 1642 48 -308 C
ATOM 1629 O ASP A1005 42.889 -43.684 18.698 1.00 59.66 O
ANISOU 1629 O ASP A1005 7094 5431 10141 1742 78 -329 O
ATOM 1630 CB ASP A1005 42.733 -40.452 19.561 1.00 56.03 C
ANISOU 1630 CB ASP A1005 6518 5412 9359 1584 104 -213 C
ATOM 1631 CG ASP A1005 43.364 -39.131 19.165 1.00 89.17 C
ANISOU 1631 CG ASP A1005 10674 9763 13442 1584 193 -254 C
ATOM 1632 OD1 ASP A1005 44.082 -39.100 18.143 1.00 76.73 O
ANISOU 1632 OD1 ASP A1005 9122 8169 11862 1657 300 -363 O
ATOM 1633 OD2 ASP A1005 43.140 -38.124 19.873 1.00100.40 O
ANISOU 1633 OD2 ASP A1005 12042 11323 14781 1515 157 -176 O
ATOM 1634 N ASN A1006 40.852 -42.935 19.292 1.00 57.69 N
ANISOU 1634 N ASN A1006 6909 5270 9741 1548 -58 -238 N
ATOM 1635 CA ASN A1006 40.394 -44.268 19.672 1.00 58.77 C
ANISOU 1635 CA ASN A1006 7061 5235 10034 1555 -145 -187 C
ATOM 1636 C ASN A1006 40.307 -45.191 18.466 1.00 70.86 C
ANISOU 1636 C ASN A1006 8711 6591 11622 1607 -124 -346 C
ATOM 1637 O ASN A1006 40.575 -46.393 18.584 1.00 61.57 O
ANISOU 1637 O ASN A1006 7527 5254 10614 1670 -154 -338 O
ATOM 1638 CB ASN A1006 39.040 -44.183 20.373 1.00 57.87 C
ANISOU 1638 CB ASN A1006 6963 5140 9887 1440 -257 -74 C
ATOM 1639 CG ASN A1006 39.155 -43.678 21.804 1.00 67.34 C
ANISOU 1639 CG ASN A1006 8036 6472 11077 1415 -300 107 C
ATOM 1640 OD1 ASN A1006 40.164 -43.898 22.475 1.00 60.56 O
ANISOU 1640 OD1 ASN A1006 7072 5631 10307 1488 -281 176 O
ATOM 1641 ND2 ASN A1006 38.108 -43.010 22.281 1.00 57.76 N
ANISOU 1641 ND2 ASN A1006 6834 5355 9756 1315 -359 186 N
ATOM 1642 N TRP A1007 39.943 -44.651 17.300 1.00 62.58 N
ANISOU 1642 N TRP A1007 7772 5568 10437 1586 -76 -492 N
ATOM 1643 CA TRP A1007 39.834 -45.476 16.102 1.00 61.23 C
ANISOU 1643 CA TRP A1007 7727 5239 10300 1641 -60 -658 C
ATOM 1644 C TRP A1007 41.205 -45.909 15.601 1.00 62.56 C
ANISOU 1644 C TRP A1007 7871 5359 10541 1786 46 -740 C
ATOM 1645 O TRP A1007 41.391 -47.067 15.210 1.00 74.77 O
ANISOU 1645 O TRP A1007 9466 6728 12214 1861 33 -812 O
ATOM 1646 CB TRP A1007 39.079 -44.718 15.014 1.00 62.98 C
ANISOU 1646 CB TRP A1007 8070 5520 10340 1584 -37 -785 C
ATOM 1647 CG TRP A1007 39.157 -45.366 13.670 1.00 70.22 C
ANISOU 1647 CG TRP A1007 9117 6308 11256 1660 0 -976 C
ATOM 1648 CD1 TRP A1007 39.917 -44.965 12.609 1.00 72.51 C
ANISOU 1648 CD1 TRP A1007 9451 6648 11451 1749 124 -1114 C
ATOM 1649 CD2 TRP A1007 38.454 -46.536 13.240 1.00 66.00 C
ANISOU 1649 CD2 TRP A1007 8686 5572 10819 1660 -91 -1052 C
ATOM 1650 NE1 TRP A1007 39.725 -45.811 11.544 1.00 66.93 N
ANISOU 1650 NE1 TRP A1007 8876 5790 10764 1811 118 -1277 N
ATOM 1651 CE2 TRP A1007 38.832 -46.784 11.905 1.00 64.47 C
ANISOU 1651 CE2 TRP A1007 8604 5317 10573 1755 -19 -1248 C
ATOM 1652 CE3 TRP A1007 37.539 -47.397 13.853 1.00 63.63 C
ANISOU 1652 CE3 TRP A1007 8392 5135 10649 1592 -228 -971 C
ATOM 1653 CZ2 TRP A1007 38.328 -47.857 11.174 1.00 66.00 C
ANISOU 1653 CZ2 TRP A1007 8923 5315 10839 1783 -87 -1376 C
ATOM 1654 CZ3 TRP A1007 37.040 -48.459 13.127 1.00 65.13 C
ANISOU 1654 CZ3 TRP A1007 8697 5126 10924 1612 -297 -1090 C
ATOM 1655 CH2 TRP A1007 37.435 -48.681 11.801 1.00 66.31 C
ANISOU 1655 CH2 TRP A1007 8963 5214 11016 1707 -230 -1296 C
ATOM 1656 N GLU A1008 42.178 -44.994 15.600 1.00 61.99 N
ANISOU 1656 N GLU A1008 7721 5437 10397 1829 151 -731 N
ATOM 1657 CA GLU A1008 43.529 -45.364 15.191 1.00 63.26 C
ANISOU 1657 CA GLU A1008 7842 5563 10633 1970 258 -789 C
ATOM 1658 C GLU A1008 44.206 -46.251 16.229 1.00 64.10 C
ANISOU 1658 C GLU A1008 7835 5588 10934 2025 222 -667 C
ATOM 1659 O GLU A1008 45.010 -47.117 15.869 1.00 65.65 O
ANISOU 1659 O GLU A1008 8031 5668 11246 2142 272 -724 O
ATOM 1660 CB GLU A1008 44.366 -44.112 14.927 1.00 62.46 C
ANISOU 1660 CB GLU A1008 7675 5644 10412 1994 377 -796 C
ATOM 1661 CG GLU A1008 43.914 -43.307 13.715 1.00 63.30 C
ANISOU 1661 CG GLU A1008 7892 5824 10334 1971 440 -930 C
ATOM 1662 N THR A1009 43.898 -46.049 17.515 1.00 63.16 N
ANISOU 1662 N THR A1009 7619 5531 10848 1949 138 -499 N
ATOM 1663 CA THR A1009 44.431 -46.930 18.551 1.00 63.98 C
ANISOU 1663 CA THR A1009 7617 5558 11135 1997 92 -371 C
ATOM 1664 C THR A1009 43.978 -48.367 18.338 1.00 65.47 C
ANISOU 1664 C THR A1009 7877 5524 11474 2026 26 -409 C
ATOM 1665 O THR A1009 44.735 -49.306 18.608 1.00 66.80 O
ANISOU 1665 O THR A1009 7992 5583 11808 2119 36 -380 O
ATOM 1666 CB THR A1009 44.002 -46.438 19.936 1.00 62.71 C
ANISOU 1666 CB THR A1009 7356 5511 10960 1906 5 -186 C
ATOM 1667 OG1 THR A1009 44.475 -45.101 20.140 1.00 70.62 O
ANISOU 1667 OG1 THR A1009 8290 6711 11832 1884 59 -159 O
ATOM 1668 CG2 THR A1009 44.562 -47.337 21.030 1.00 63.60 C
ANISOU 1668 CG2 THR A1009 7355 5555 11256 1960 -42 -45 C
ATOM 1669 N LEU A1010 42.755 -48.555 17.841 1.00 65.32 N
ANISOU 1669 N LEU A1010 7979 5432 11408 1949 -44 -474 N
ATOM 1670 CA LEU A1010 42.256 -49.899 17.579 1.00 75.06 C
ANISOU 1670 CA LEU A1010 9287 6443 12790 1969 -118 -519 C
ATOM 1671 C LEU A1010 43.015 -50.560 16.435 1.00 68.47 C
ANISOU 1671 C LEU A1010 8529 5483 12002 2098 -36 -696 C
ATOM 1672 O LEU A1010 43.302 -51.762 16.487 1.00 70.05 O
ANISOU 1672 O LEU A1010 8730 5505 12381 2171 -64 -705 O
ATOM 1673 CB LEU A1010 40.762 -49.846 17.258 1.00 73.86 C
ANISOU 1673 CB LEU A1010 9245 6250 12569 1851 -215 -551 C
ATOM 1674 CG LEU A1010 39.990 -51.166 17.261 1.00 78.97 C
ANISOU 1674 CG LEU A1010 9949 6672 13385 1835 -330 -552 C
ATOM 1675 CD1 LEU A1010 39.815 -51.667 18.685 1.00 78.71 C
ANISOU 1675 CD1 LEU A1010 9791 6616 13500 1800 -415 -334 C
ATOM 1676 CD2 LEU A1010 38.641 -50.999 16.577 1.00 68.83 C
ANISOU 1676 CD2 LEU A1010 8793 5351 12007 1732 -405 -633 C
ATOM 1677 N ASN A1011 43.348 -49.797 15.389 1.00 70.04 N
ANISOU 1677 N ASN A1011 8795 5773 12045 2134 68 -836 N
ATOM 1678 CA ASN A1011 43.950 -50.409 14.210 1.00 69.86 C
ANISOU 1678 CA ASN A1011 8864 5636 12043 2263 147 -1016 C
ATOM 1679 C ASN A1011 45.463 -50.543 14.352 1.00 71.99 C
ANISOU 1679 C ASN A1011 9030 5930 12394 2398 262 -992 C
ATOM 1680 O ASN A1011 46.048 -51.525 13.881 1.00 88.42 O
ANISOU 1680 O ASN A1011 11144 7861 14590 2517 296 -1076 O
ATOM 1681 CB ASN A1011 43.596 -49.596 12.965 1.00 69.40 C
ANISOU 1681 CB ASN A1011 8928 5661 11779 2252 210 -1176 C
ATOM 1682 CG ASN A1011 42.104 -49.502 12.735 1.00 70.73 C
ANISOU 1682 CG ASN A1011 9205 5797 11871 2124 97 -1209 C
ATOM 1683 OD1 ASN A1011 41.352 -50.409 13.090 1.00 69.31 O
ANISOU 1683 OD1 ASN A1011 9054 5464 11817 2078 -25 -1177 O
ATOM 1684 ND2 ASN A1011 41.666 -48.399 12.144 1.00 79.82 N
ANISOU 1684 ND2 ASN A1011 10411 7093 12823 2064 136 -1265 N
ATOM 1685 N ASP A1012 46.115 -49.570 14.993 1.00 69.50 N
ANISOU 1685 N ASP A1012 8587 5797 12024 2382 319 -878 N
ATOM 1686 CA ASP A1012 47.561 -49.649 15.173 1.00 70.27 C
ANISOU 1686 CA ASP A1012 8572 5924 12204 2504 423 -841 C
ATOM 1687 C ASP A1012 47.939 -50.757 16.150 1.00 72.39 C
ANISOU 1687 C ASP A1012 8749 6065 12690 2545 361 -723 C
ATOM 1688 O ASP A1012 48.935 -51.460 15.945 1.00 72.76 O
ANISOU 1688 O ASP A1012 8764 6025 12857 2675 429 -752 O
ATOM 1689 CB ASP A1012 48.104 -48.299 15.643 1.00 73.32 C
ANISOU 1689 CB ASP A1012 8840 6533 12484 2466 482 -746 C
ATOM 1690 CG ASP A1012 48.125 -47.265 14.535 1.00 89.04 C
ANISOU 1690 CG ASP A1012 10901 8644 14285 2469 583 -868 C
ATOM 1691 OD1 ASP A1012 48.210 -47.662 13.356 1.00 90.61 O
ANISOU 1691 OD1 ASP A1012 11214 8763 14452 2554 649 -1026 O
ATOM 1692 OD2 ASP A1012 48.057 -46.055 14.844 1.00 85.51 O
ANISOU 1692 OD2 ASP A1012 10396 8372 13722 2392 596 -804 O
ATOM 1693 N ASN A1013 47.154 -50.933 17.214 1.00 70.55 N
ANISOU 1693 N ASN A1013 8472 5821 12513 2441 235 -584 N
ATOM 1694 CA ASN A1013 47.431 -52.003 18.164 1.00 76.06 C
ANISOU 1694 CA ASN A1013 9082 6398 13420 2476 171 -460 C
ATOM 1695 C ASN A1013 47.128 -53.380 17.590 1.00 76.07 C
ANISOU 1695 C ASN A1013 9184 6156 13563 2534 130 -560 C
ATOM 1696 O ASN A1013 47.611 -54.381 18.130 1.00 74.56 O
ANISOU 1696 O ASN A1013 8926 5841 13562 2600 107 -488 O
ATOM 1697 CB ASN A1013 46.640 -51.783 19.451 1.00 73.15 C
ANISOU 1697 CB ASN A1013 8638 6095 13060 2355 52 -276 C
ATOM 1698 CG ASN A1013 47.314 -50.799 20.384 1.00 75.59 C
ANISOU 1698 CG ASN A1013 8802 6605 13311 2338 81 -139 C
ATOM 1699 OD1 ASN A1013 48.528 -50.611 20.329 1.00 80.17 O
ANISOU 1699 OD1 ASN A1013 9304 7238 13919 2430 173 -141 O
ATOM 1700 ND2 ASN A1013 46.530 -50.172 21.254 1.00 81.59 N
ANISOU 1700 ND2 ASN A1013 9527 7479 13996 2225 -2 -18 N
ATOM 1701 N LEU A1014 46.339 -53.457 16.515 1.00 73.57 N
ANISOU 1701 N LEU A1014 9025 5766 13162 2512 116 -724 N
ATOM 1702 CA LEU A1014 46.170 -54.731 15.824 1.00 76.80 C
ANISOU 1702 CA LEU A1014 9540 5940 13700 2584 83 -849 C
ATOM 1703 C LEU A1014 47.457 -55.146 15.123 1.00 82.00 C
ANISOU 1703 C LEU A1014 10201 6546 14410 2755 211 -957 C
ATOM 1704 O LEU A1014 47.806 -56.332 15.102 1.00 85.46 O
ANISOU 1704 O LEU A1014 10646 6797 15028 2844 194 -980 O
ATOM 1705 CB LEU A1014 45.018 -54.645 14.823 1.00 81.22 C
ANISOU 1705 CB LEU A1014 10270 6445 14144 2519 30 -1006 C
ATOM 1706 CG LEU A1014 43.601 -54.781 15.382 1.00 85.48 C
ANISOU 1706 CG LEU A1014 10834 6938 14707 2368 -123 -920 C
ATOM 1707 CD1 LEU A1014 42.574 -54.566 14.282 1.00 83.04 C
ANISOU 1707 CD1 LEU A1014 10692 6595 14265 2311 -162 -1086 C
ATOM 1708 CD2 LEU A1014 43.411 -56.140 16.037 1.00 83.28 C
ANISOU 1708 CD2 LEU A1014 10518 6449 14676 2381 -227 -835 C
ATOM 1709 N LYS A1015 48.178 -54.181 14.545 1.00 82.70 N
ANISOU 1709 N LYS A1015 10280 6795 14346 2805 342 -1017 N
ATOM 1710 CA LYS A1015 49.454 -54.488 13.910 1.00 77.93 C
ANISOU 1710 CA LYS A1015 9665 6162 13784 2973 477 -1100 C
ATOM 1711 C LYS A1015 50.495 -54.928 14.930 1.00 78.46 C
ANISOU 1711 C LYS A1015 9565 6219 14027 3037 498 -942 C
ATOM 1712 O LYS A1015 51.351 -55.764 14.619 1.00 89.02 O
ANISOU 1712 O LYS A1015 10896 7438 15489 3177 562 -991 O
ATOM 1713 CB LYS A1015 49.962 -53.275 13.131 1.00 77.16 C
ANISOU 1713 CB LYS A1015 9578 6254 13486 3004 612 -1173 C
ATOM 1714 CG LYS A1015 48.960 -52.698 12.144 1.00 85.94 C
ANISOU 1714 CG LYS A1015 10844 7405 14404 2938 599 -1317 C
ATOM 1715 CD LYS A1015 49.530 -51.478 11.436 1.00 90.70 C
ANISOU 1715 CD LYS A1015 11439 8203 14821 2973 740 -1367 C
ATOM 1716 CE LYS A1015 49.952 -50.408 12.433 1.00 82.24 C
ANISOU 1716 CE LYS A1015 10201 7325 13722 2898 758 -1188 C
ATOM 1717 NZ LYS A1015 50.557 -49.220 11.766 1.00 73.47 N
ANISOU 1717 NZ LYS A1015 9068 6397 12452 2932 895 -1225 N
ATOM 1718 N VAL A1016 50.439 -54.378 16.146 1.00 77.05 N
ANISOU 1718 N VAL A1016 9253 6165 13859 2942 445 -753 N
ATOM 1719 CA VAL A1016 51.374 -54.779 17.193 1.00 80.18 C
ANISOU 1719 CA VAL A1016 9486 6559 14419 2995 451 -592 C
ATOM 1720 C VAL A1016 51.179 -56.244 17.557 1.00 91.85 C
ANISOU 1720 C VAL A1016 10972 7811 16114 3033 367 -562 C
ATOM 1721 O VAL A1016 52.143 -56.943 17.896 1.00 97.36 O
ANISOU 1721 O VAL A1016 11582 8438 16973 3139 407 -506 O
ATOM 1722 CB VAL A1016 51.215 -53.859 18.422 1.00 75.70 C
ANISOU 1722 CB VAL A1016 8788 6175 13798 2879 394 -405 C
ATOM 1723 CG1 VAL A1016 52.185 -54.255 19.526 1.00 76.61 C
ANISOU 1723 CG1 VAL A1016 8735 6298 14076 2936 393 -236 C
ATOM 1724 CG2 VAL A1016 51.421 -52.407 18.025 1.00 76.86 C
ANISOU 1724 CG2 VAL A1016 8928 6533 13742 2843 474 -440 C
ATOM 1725 N ILE A1017 49.943 -56.739 17.476 1.00 82.69 N
ANISOU 1725 N ILE A1017 9915 6531 14973 2948 250 -597 N
ATOM 1726 CA ILE A1017 49.666 -58.123 17.846 1.00 88.37 C
ANISOU 1726 CA ILE A1017 10637 7026 15911 2972 158 -559 C
ATOM 1727 C ILE A1017 50.116 -59.082 16.750 1.00 85.22 C
ANISOU 1727 C ILE A1017 10346 6436 15598 3113 214 -744 C
ATOM 1728 O ILE A1017 50.677 -60.147 17.034 1.00 99.29 O
ANISOU 1728 O ILE A1017 12080 8064 17582 3204 210 -708 O
ATOM 1729 CB ILE A1017 48.170 -58.289 18.170 1.00 80.25 C
ANISOU 1729 CB ILE A1017 9670 5937 14884 2827 8 -518 C
ATOM 1730 CG1 ILE A1017 47.782 -57.409 19.359 1.00 77.96 C
ANISOU 1730 CG1 ILE A1017 9265 5837 14519 2705 -45 -320 C
ATOM 1731 CG2 ILE A1017 47.838 -59.747 18.455 1.00 92.85 C
ANISOU 1731 CG2 ILE A1017 11274 7284 16719 2851 -91 -486 C
ATOM 1732 CD1 ILE A1017 46.305 -57.442 19.688 1.00 77.18 C
ANISOU 1732 CD1 ILE A1017 9218 5704 14403 2562 -180 -266 C
ATOM 1733 N GLU A1018 49.889 -58.723 15.484 1.00 82.79 N
ANISOU 1733 N GLU A1018 10185 6135 15137 3139 268 -945 N
ATOM 1734 CA GLU A1018 50.234 -59.621 14.387 1.00 84.87 C
ANISOU 1734 CA GLU A1018 10569 6217 15461 3278 315 -1138 C
ATOM 1735 C GLU A1018 51.741 -59.777 14.227 1.00 89.70 C
ANISOU 1735 C GLU A1018 11102 6850 16131 3445 463 -1142 C
ATOM 1736 O GLU A1018 52.205 -60.813 13.737 1.00108.17 O
ANISOU 1736 O GLU A1018 13492 9009 18600 3577 490 -1239 O
ATOM 1737 CB GLU A1018 49.618 -59.118 13.083 1.00 84.71 C
ANISOU 1737 CB GLU A1018 10724 6222 15239 3269 339 -1347 C
ATOM 1738 CG GLU A1018 48.110 -58.974 13.129 1.00 83.73 C
ANISOU 1738 CG GLU A1018 10686 6070 15057 3108 194 -1356 C
ATOM 1739 CD GLU A1018 47.530 -58.562 11.794 1.00 90.58 C
ANISOU 1739 CD GLU A1018 11731 6951 15733 3109 213 -1570 C
ATOM 1740 OE1 GLU A1018 48.279 -58.566 10.795 1.00108.23 O
ANISOU 1740 OE1 GLU A1018 14036 9188 17898 3249 333 -1723 O
ATOM 1741 OE2 GLU A1018 46.328 -58.232 11.744 1.00 91.54 O
ANISOU 1741 OE2 GLU A1018 11922 7086 15773 2974 110 -1580 O
ATOM 1742 N LYS A1019 52.517 -58.771 14.628 1.00102.60 N
ANISOU 1742 N LYS A1019 12610 8696 17676 3445 556 -1038 N
ATOM 1743 CA LYS A1019 53.968 -58.806 14.505 1.00 92.96 C
ANISOU 1743 CA LYS A1019 11298 7515 16507 3597 700 -1023 C
ATOM 1744 C LYS A1019 54.664 -59.035 15.840 1.00 91.97 C
ANISOU 1744 C LYS A1019 10981 7416 16547 3596 679 -804 C
ATOM 1745 O LYS A1019 55.877 -58.820 15.941 1.00106.95 O
ANISOU 1745 O LYS A1019 12768 9392 18476 3694 792 -750 O
ATOM 1746 CB LYS A1019 54.473 -57.510 13.866 1.00 94.44 C
ANISOU 1746 CB LYS A1019 11480 7918 16486 3616 832 -1072 C
ATOM 1747 CG LYS A1019 53.875 -57.224 12.498 1.00 90.27 C
ANISOU 1747 CG LYS A1019 11138 7384 15778 3631 868 -1287 C
ATOM 1748 CD LYS A1019 54.432 -55.942 11.906 1.00 94.91 C
ANISOU 1748 CD LYS A1019 11702 8188 16171 3656 1006 -1314 C
ATOM 1749 CE LYS A1019 53.848 -55.675 10.529 1.00 97.48 C
ANISOU 1749 CE LYS A1019 12213 8514 16312 3680 1045 -1524 C
ATOM 1750 NZ LYS A1019 54.395 -54.430 9.922 1.00110.54 N
ANISOU 1750 NZ LYS A1019 13840 10379 17782 3709 1186 -1542 N
ATOM 1751 N ALA A1020 53.932 -59.468 16.862 1.00 87.00 N
ANISOU 1751 N ALA A1020 10304 6725 16025 3490 539 -670 N
ATOM 1752 CA ALA A1020 54.519 -59.676 18.174 1.00 97.35 C
ANISOU 1752 CA ALA A1020 11435 8071 17483 3486 510 -455 C
ATOM 1753 C ALA A1020 55.230 -61.026 18.244 1.00 97.21 C
ANISOU 1753 C ALA A1020 11384 7851 17699 3621 526 -447 C
ATOM 1754 O ALA A1020 55.027 -61.913 17.411 1.00 91.07 O
ANISOU 1754 O ALA A1020 10732 6880 16989 3695 526 -600 O
ATOM 1755 CB ALA A1020 53.448 -59.591 19.262 1.00 90.13 C
ANISOU 1755 CB ALA A1020 10479 7182 16583 3327 358 -303 C
ATOM 1756 N ASP A1021 56.073 -61.167 19.255 1.00100.40 N
ANISOU 1756 N ASP A1021 11618 8302 18228 3654 538 -268 N
ATOM 1757 CA ASP A1021 56.835 -62.388 19.495 1.00108.59 C
ANISOU 1757 CA ASP A1021 12594 9167 19498 3780 556 -225 C
ATOM 1758 C ASP A1021 56.719 -62.881 20.928 1.00104.30 C
ANISOU 1758 C ASP A1021 11919 8625 19086 3708 445 1 C
ATOM 1759 O ASP A1021 56.633 -64.092 21.151 1.00103.81 O
ANISOU 1759 O ASP A1021 11876 8411 19155 3721 387 29 O
ATOM 1760 CB ASP A1021 58.315 -62.161 19.141 1.00120.63 C
ANISOU 1760 CB ASP A1021 14051 10792 20990 3908 709 -238 C
ATOM 1761 CG ASP A1021 58.506 -61.672 17.718 1.00121.54 C
ANISOU 1761 CG ASP A1021 14291 10927 20963 3991 832 -450 C
ATOM 1762 OD1 ASP A1021 57.846 -62.216 16.808 1.00129.31 O
ANISOU 1762 OD1 ASP A1021 15444 11766 21922 4011 811 -624 O
ATOM 1763 OD2 ASP A1021 59.312 -60.740 17.511 1.00 99.07 O
ANISOU 1763 OD2 ASP A1021 11374 8245 18024 4035 947 -438 O
ATOM 1764 N ASN A1022 56.715 -61.976 21.902 1.00 88.17 N
ANISOU 1764 N ASN A1022 9748 6760 16991 3628 414 164 N
ATOM 1765 CA ASN A1022 56.566 -62.335 23.303 1.00 94.42 C
ANISOU 1765 CA ASN A1022 10411 7574 17891 3564 310 386 C
ATOM 1766 C ASN A1022 55.104 -62.229 23.720 1.00 88.15 C
ANISOU 1766 C ASN A1022 9670 6764 17058 3421 175 433 C
ATOM 1767 O ASN A1022 54.335 -61.442 23.162 1.00 92.28 O
ANISOU 1767 O ASN A1022 10300 7366 17398 3335 165 330 O
ATOM 1768 CB ASN A1022 57.430 -61.431 24.185 1.00 91.35 C
ANISOU 1768 CB ASN A1022 9852 7403 17453 3562 344 542 C
ATOM 1769 CG ASN A1022 57.474 -61.892 25.630 1.00103.03 C
ANISOU 1769 CG ASN A1022 11200 8925 19020 3511 247 768 C
ATOM 1770 OD1 ASN A1022 57.192 -63.052 25.933 1.00 91.23 O
ANISOU 1770 OD1 ASN A1022 9723 7292 17648 3507 185 814 O
ATOM 1771 ND2 ASN A1022 57.832 -60.982 26.531 1.00 91.50 N
ANISOU 1771 ND2 ASN A1022 9610 7664 17493 3473 232 908 N
ATOM 1772 N ALA A1023 54.725 -63.041 24.710 1.00 89.51 N
ANISOU 1772 N ALA A1023 9775 6861 17374 3383 72 595 N
ATOM 1773 CA ALA A1023 53.351 -63.011 25.200 1.00 85.80 C
ANISOU 1773 CA ALA A1023 9337 6370 16892 3255 -57 670 C
ATOM 1774 C ALA A1023 53.003 -61.660 25.810 1.00 90.86 C
ANISOU 1774 C ALA A1023 9932 7267 17322 3144 -80 756 C
ATOM 1775 O ALA A1023 51.845 -61.231 25.746 1.00 91.92 O
ANISOU 1775 O ALA A1023 10146 7437 17342 3028 -150 737 O
ATOM 1776 CB ALA A1023 53.130 -64.130 26.218 1.00 91.93 C
ANISOU 1776 CB ALA A1023 10042 7066 17822 3224 -150 846 C
ATOM 1777 N ALA A1024 53.985 -60.972 26.397 1.00 93.46 N
ANISOU 1777 N ALA A1024 10134 7775 17601 3178 -26 848 N
ATOM 1778 CA ALA A1024 53.721 -59.655 26.967 1.00 88.94 C
ANISOU 1778 CA ALA A1024 9519 7445 16829 3080 -49 920 C
ATOM 1779 C ALA A1024 53.459 -58.614 25.884 1.00 92.74 C
ANISOU 1779 C ALA A1024 10121 8017 17099 3037 14 735 C
ATOM 1780 O ALA A1024 52.728 -57.646 26.123 1.00 86.35 O
ANISOU 1780 O ALA A1024 9334 7357 16120 2927 -30 755 O
ATOM 1781 CB ALA A1024 54.887 -59.219 27.854 1.00 96.21 C
ANISOU 1781 CB ALA A1024 10271 8521 17764 3132 -17 1059 C
ATOM 1782 N GLN A1025 54.044 -58.789 24.696 1.00100.11 N
ANISOU 1782 N GLN A1025 11131 8868 18038 3127 119 557 N
ATOM 1783 CA GLN A1025 53.781 -57.861 23.601 1.00 83.58 C
ANISOU 1783 CA GLN A1025 9156 6853 15746 3096 183 381 C
ATOM 1784 C GLN A1025 52.332 -57.938 23.141 1.00 96.86 C
ANISOU 1784 C GLN A1025 10987 8461 17356 2992 102 296 C
ATOM 1785 O GLN A1025 51.761 -56.926 22.719 1.00 77.96 O
ANISOU 1785 O GLN A1025 8663 6190 14767 2910 109 223 O
ATOM 1786 CB GLN A1025 54.726 -58.141 22.433 1.00 93.25 C
ANISOU 1786 CB GLN A1025 10432 7999 17000 3232 316 217 C
ATOM 1787 CG GLN A1025 56.195 -57.942 22.767 1.00100.39 C
ANISOU 1787 CG GLN A1025 11189 8990 17964 3334 409 294 C
ATOM 1788 CD GLN A1025 57.115 -58.378 21.644 1.00106.25 C
ANISOU 1788 CD GLN A1025 11978 9635 18757 3484 543 146 C
ATOM 1789 OE1 GLN A1025 56.682 -59.006 20.678 1.00106.37 O
ANISOU 1789 OE1 GLN A1025 12137 9494 18785 3523 558 -13 O
ATOM 1790 NE2 GLN A1025 58.395 -58.048 21.768 1.00127.04 N
ANISOU 1790 NE2 GLN A1025 14489 12360 21421 3571 640 199 N
ATOM 1791 N VAL A1026 51.726 -59.124 23.211 1.00 98.40 N
ANISOU 1791 N VAL A1026 11226 8452 17711 2994 23 307 N
ATOM 1792 CA VAL A1026 50.306 -59.247 22.910 1.00 82.85 C
ANISOU 1792 CA VAL A1026 9378 6405 15695 2887 -72 254 C
ATOM 1793 C VAL A1026 49.464 -58.790 24.096 1.00 78.67 C
ANISOU 1793 C VAL A1026 8777 5996 15118 2761 -177 443 C
ATOM 1794 O VAL A1026 48.374 -58.237 23.912 1.00 91.14 O
ANISOU 1794 O VAL A1026 10438 7626 16566 2650 -232 412 O
ATOM 1795 CB VAL A1026 49.970 -60.693 22.504 1.00 82.84 C
ANISOU 1795 CB VAL A1026 9450 6128 15896 2936 -123 191 C
ATOM 1796 CG1 VAL A1026 48.518 -60.805 22.062 1.00 81.67 C
ANISOU 1796 CG1 VAL A1026 9436 5892 15704 2827 -223 118 C
ATOM 1797 CG2 VAL A1026 50.904 -61.167 21.401 1.00 83.57 C
ANISOU 1797 CG2 VAL A1026 9608 6108 16036 3081 -13 10 C
ATOM 1798 N LYS A1027 49.951 -58.996 25.322 1.00 78.78 N
ANISOU 1798 N LYS A1027 8637 6063 15231 2781 -206 643 N
ATOM 1799 CA LYS A1027 49.193 -58.589 26.502 1.00 82.16 C
ANISOU 1799 CA LYS A1027 8993 6614 15610 2677 -303 831 C
ATOM 1800 C LYS A1027 49.114 -57.070 26.608 1.00 87.86 C
ANISOU 1800 C LYS A1027 9709 7582 16090 2605 -277 824 C
ATOM 1801 O LYS A1027 48.038 -56.509 26.845 1.00 93.50 O
ANISOU 1801 O LYS A1027 10465 8374 16685 2494 -344 860 O
ATOM 1802 CB LYS A1027 49.822 -59.185 27.762 1.00 78.30 C
ANISOU 1802 CB LYS A1027 8342 6130 15280 2731 -335 1042 C
ATOM 1803 CG LYS A1027 49.031 -58.924 29.038 1.00 89.42 C
ANISOU 1803 CG LYS A1027 9672 7650 16652 2642 -438 1251 C
ATOM 1804 CD LYS A1027 49.794 -59.392 30.270 1.00 92.21 C
ANISOU 1804 CD LYS A1027 9859 8038 17136 2709 -458 1456 C
ATOM 1805 CE LYS A1027 48.950 -59.261 31.530 1.00 88.57 C
ANISOU 1805 CE LYS A1027 9327 7678 16646 2634 -562 1670 C
ATOM 1806 NZ LYS A1027 48.430 -57.879 31.712 1.00 86.83 N
ANISOU 1806 NZ LYS A1027 9134 7678 16179 2542 -574 1662 N
ATOM 1807 N ASP A1028 50.249 -56.386 26.434 1.00102.11 N
ANISOU 1807 N ASP A1028 11460 9509 17829 2668 -182 782 N
ATOM 1808 CA ASP A1028 50.261 -54.931 26.553 1.00 98.28 C
ANISOU 1808 CA ASP A1028 10959 9252 17131 2604 -159 777 C
ATOM 1809 C ASP A1028 49.480 -54.275 25.420 1.00 89.05 C
ANISOU 1809 C ASP A1028 9942 8098 15797 2536 -133 601 C
ATOM 1810 O ASP A1028 48.827 -53.244 25.626 1.00 88.57 O
ANISOU 1810 O ASP A1028 9899 8188 15565 2439 -163 619 O
ATOM 1811 CB ASP A1028 51.702 -54.417 26.583 1.00 98.34 C
ANISOU 1811 CB ASP A1028 10865 9368 17132 2690 -65 775 C
ATOM 1812 CG ASP A1028 52.437 -54.799 27.859 1.00111.25 C
ANISOU 1812 CG ASP A1028 12337 11041 18894 2740 -104 968 C
ATOM 1813 OD1 ASP A1028 51.789 -54.871 28.925 1.00118.26 O
ANISOU 1813 OD1 ASP A1028 13174 11974 19785 2681 -204 1123 O
ATOM 1814 OD2 ASP A1028 53.664 -55.022 27.797 1.00109.96 O
ANISOU 1814 OD2 ASP A1028 12092 10864 18823 2843 -32 969 O
ATOM 1815 N ALA A1029 49.531 -54.856 24.219 1.00 81.52 N
ANISOU 1815 N ALA A1029 9099 6988 14886 2591 -78 429 N
ATOM 1816 CA ALA A1029 48.768 -54.305 23.103 1.00 75.72 C
ANISOU 1816 CA ALA A1029 8515 6260 13995 2533 -57 259 C
ATOM 1817 C ALA A1029 47.271 -54.495 23.312 1.00 87.80 C
ANISOU 1817 C ALA A1029 10119 7737 15504 2416 -174 295 C
ATOM 1818 O ALA A1029 46.474 -53.616 22.964 1.00 78.05 O
ANISOU 1818 O ALA A1029 8959 6600 14097 2323 -187 241 O
ATOM 1819 CB ALA A1029 49.212 -54.949 21.791 1.00 74.52 C
ANISOU 1819 CB ALA A1029 8466 5952 13896 2635 26 66 C
ATOM 1820 N LEU A1030 46.869 -55.634 23.880 1.00 79.64 N
ANISOU 1820 N LEU A1030 9060 6547 14651 2418 -260 394 N
ATOM 1821 CA LEU A1030 45.453 -55.866 24.143 1.00 76.37 C
ANISOU 1821 CA LEU A1030 8701 6076 14239 2307 -375 451 C
ATOM 1822 C LEU A1030 44.948 -55.025 25.307 1.00 77.44 C
ANISOU 1822 C LEU A1030 8751 6405 14269 2216 -432 631 C
ATOM 1823 O LEU A1030 43.772 -54.642 25.326 1.00 74.01 O
ANISOU 1823 O LEU A1030 8377 6005 13740 2110 -496 648 O
ATOM 1824 CB LEU A1030 45.205 -57.347 24.415 1.00 74.81 C
ANISOU 1824 CB LEU A1030 8492 5650 14283 2340 -449 515 C
ATOM 1825 CG LEU A1030 45.200 -58.269 23.199 1.00 76.41 C
ANISOU 1825 CG LEU A1030 8819 5626 14588 2401 -434 323 C
ATOM 1826 CD1 LEU A1030 45.317 -59.711 23.649 1.00 78.24 C
ANISOU 1826 CD1 LEU A1030 8999 5643 15084 2458 -493 410 C
ATOM 1827 CD2 LEU A1030 43.935 -58.059 22.386 1.00 75.92 C
ANISOU 1827 CD2 LEU A1030 8905 5515 14426 2303 -491 203 C
ATOM 1828 N THR A1031 45.811 -54.733 26.284 1.00 81.83 N
ANISOU 1828 N THR A1031 9168 7086 14836 2259 -412 766 N
ATOM 1829 CA THR A1031 45.399 -53.898 27.408 1.00 85.40 C
ANISOU 1829 CA THR A1031 9542 7731 15176 2186 -466 929 C
ATOM 1830 C THR A1031 45.068 -52.484 26.946 1.00 71.46 C
ANISOU 1830 C THR A1031 7839 6140 13173 2112 -432 835 C
ATOM 1831 O THR A1031 44.101 -51.875 27.421 1.00 66.93 O
ANISOU 1831 O THR A1031 7278 5669 12484 2017 -493 909 O
ATOM 1832 CB THR A1031 46.496 -53.872 28.474 1.00 79.49 C
ANISOU 1832 CB THR A1031 8636 7079 14486 2259 -454 1073 C
ATOM 1833 OG1 THR A1031 46.772 -55.207 28.912 1.00 84.60 O
ANISOU 1833 OG1 THR A1031 9222 7562 15359 2328 -486 1169 O
ATOM 1834 CG2 THR A1031 46.063 -53.035 29.670 1.00 84.78 C
ANISOU 1834 CG2 THR A1031 9230 7948 15033 2194 -517 1237 C
ATOM 1835 N LYS A1032 45.854 -51.949 26.013 1.00 71.10 N
ANISOU 1835 N LYS A1032 7831 6130 13055 2158 -331 678 N
ATOM 1836 CA LYS A1032 45.604 -50.620 25.473 1.00 66.55 C
ANISOU 1836 CA LYS A1032 7312 5709 12264 2094 -289 582 C
ATOM 1837 C LYS A1032 44.457 -50.595 24.472 1.00 75.81 C
ANISOU 1837 C LYS A1032 8639 6808 13358 2020 -306 452 C
ATOM 1838 O LYS A1032 44.007 -49.506 24.098 1.00 83.36 O
ANISOU 1838 O LYS A1032 9648 7892 14133 1950 -287 392 O
ATOM 1839 CB LYS A1032 46.881 -50.075 24.829 1.00 66.70 C
ANISOU 1839 CB LYS A1032 7306 5793 12245 2175 -170 474 C
ATOM 1840 CG LYS A1032 48.046 -49.969 25.807 1.00 82.73 C
ANISOU 1840 CG LYS A1032 9178 7912 14344 2242 -157 601 C
ATOM 1841 CD LYS A1032 49.333 -49.538 25.123 1.00 93.81 C
ANISOU 1841 CD LYS A1032 10549 9360 15737 2327 -37 503 C
ATOM 1842 CE LYS A1032 50.488 -49.491 26.114 1.00 99.18 C
ANISOU 1842 CE LYS A1032 11065 10117 16500 2392 -35 635 C
ATOM 1843 NZ LYS A1032 51.773 -49.112 25.467 1.00 91.51 N
ANISOU 1843 NZ LYS A1032 10048 9182 15538 2478 82 554 N
ATOM 1844 N MET A1033 43.974 -51.757 24.032 1.00 67.48 N
ANISOU 1844 N MET A1033 7654 5547 12438 2034 -346 408 N
ATOM 1845 CA MET A1033 42.777 -51.819 23.203 1.00 67.28 C
ANISOU 1845 CA MET A1033 7769 5440 12353 1956 -388 303 C
ATOM 1846 C MET A1033 41.509 -51.890 24.041 1.00 68.04 C
ANISOU 1846 C MET A1033 7853 5546 12453 1850 -504 454 C
ATOM 1847 O MET A1033 40.513 -51.240 23.708 1.00 65.55 O
ANISOU 1847 O MET A1033 7616 5290 12001 1754 -532 417 O
ATOM 1848 CB MET A1033 42.836 -53.027 22.268 1.00 69.06 C
ANISOU 1848 CB MET A1033 8084 5430 12725 2022 -385 170 C
ATOM 1849 CG MET A1033 43.882 -52.918 21.185 1.00 78.50 C
ANISOU 1849 CG MET A1033 9327 6612 13888 2125 -264 -9 C
ATOM 1850 SD MET A1033 43.903 -54.352 20.093 1.00 89.19 S
ANISOU 1850 SD MET A1033 10799 7685 15404 2212 -268 -177 S
ATOM 1851 CE MET A1033 42.245 -54.278 19.426 1.00 79.89 C
ANISOU 1851 CE MET A1033 9774 6444 14139 2086 -366 -263 C
ATOM 1852 N ARG A1034 41.533 -52.674 25.123 1.00 67.31 N
ANISOU 1852 N ARG A1034 7660 5400 12516 1869 -568 631 N
ATOM 1853 CA ARG A1034 40.357 -52.798 25.977 1.00 66.84 C
ANISOU 1853 CA ARG A1034 7577 5351 12470 1780 -673 796 C
ATOM 1854 C ARG A1034 39.973 -51.453 26.580 1.00 73.75 C
ANISOU 1854 C ARG A1034 8421 6463 13138 1706 -675 872 C
ATOM 1855 O ARG A1034 38.784 -51.143 26.719 1.00 75.32 O
ANISOU 1855 O ARG A1034 8661 6695 13262 1611 -736 924 O
ATOM 1856 CB ARG A1034 40.614 -53.831 27.075 1.00 74.28 C
ANISOU 1856 CB ARG A1034 8400 6212 13612 1830 -727 984 C
ATOM 1857 CG ARG A1034 39.355 -54.312 27.777 1.00 79.16 C
ANISOU 1857 CG ARG A1034 9001 6777 14298 1752 -836 1150 C
ATOM 1858 CD ARG A1034 39.680 -55.252 28.926 1.00 69.15 C
ANISOU 1858 CD ARG A1034 7603 5454 13219 1809 -881 1353 C
ATOM 1859 NE ARG A1034 38.483 -55.893 29.458 1.00 79.68 N
ANISOU 1859 NE ARG A1034 8922 6699 14653 1744 -981 1508 N
ATOM 1860 CZ ARG A1034 37.669 -55.341 30.347 1.00 90.44 C
ANISOU 1860 CZ ARG A1034 10239 8206 15918 1679 -1029 1674 C
ATOM 1861 NH1 ARG A1034 37.888 -54.128 30.825 1.00 88.44 N
ANISOU 1861 NH1 ARG A1034 9955 8188 15460 1668 -993 1701 N
ATOM 1862 NH2 ARG A1034 36.606 -56.024 30.764 1.00 89.73 N
ANISOU 1862 NH2 ARG A1034 10132 8018 15944 1627 -1116 1820 N
ATOM 1863 N ALA A1035 40.967 -50.638 26.941 1.00 82.49 N
ANISOU 1863 N ALA A1035 9453 7732 14155 1751 -611 881 N
ATOM 1864 CA ALA A1035 40.675 -49.289 27.413 1.00 62.72 C
ANISOU 1864 CA ALA A1035 6930 5450 11450 1688 -611 927 C
ATOM 1865 C ALA A1035 40.125 -48.422 26.289 1.00 68.38 C
ANISOU 1865 C ALA A1035 7770 6210 12002 1620 -571 761 C
ATOM 1866 O ALA A1035 39.142 -47.699 26.480 1.00 79.65 O
ANISOU 1866 O ALA A1035 9230 7736 13297 1529 -610 800 O
ATOM 1867 CB ALA A1035 41.928 -48.657 28.016 1.00 73.78 C
ANISOU 1867 CB ALA A1035 8221 6999 12813 1754 -560 966 C
ATOM 1868 N ALA A1036 40.742 -48.487 25.105 1.00 75.20 N
ANISOU 1868 N ALA A1036 8703 7003 12868 1668 -491 578 N
ATOM 1869 CA ALA A1036 40.241 -47.720 23.969 1.00 69.46 C
ANISOU 1869 CA ALA A1036 8095 6312 11986 1612 -450 417 C
ATOM 1870 C ALA A1036 38.872 -48.212 23.521 1.00 73.18 C
ANISOU 1870 C ALA A1036 8672 6664 12471 1532 -526 392 C
ATOM 1871 O ALA A1036 38.105 -47.447 22.924 1.00 78.25 O
ANISOU 1871 O ALA A1036 9399 7370 12963 1454 -523 318 O
ATOM 1872 CB ALA A1036 41.234 -47.785 22.808 1.00 62.06 C
ANISOU 1872 CB ALA A1036 7205 5321 11055 1698 -344 236 C
ATOM 1873 N ALA A1037 38.549 -49.478 23.796 1.00 67.92 N
ANISOU 1873 N ALA A1037 7998 5821 11989 1547 -596 458 N
ATOM 1874 CA ALA A1037 37.228 -49.998 23.461 1.00 68.72 C
ANISOU 1874 CA ALA A1037 8185 5797 12127 1466 -683 453 C
ATOM 1875 C ALA A1037 36.171 -49.464 24.420 1.00 70.90 C
ANISOU 1875 C ALA A1037 8419 6191 12327 1368 -755 627 C
ATOM 1876 O ALA A1037 35.117 -48.979 23.992 1.00 81.15 O
ANISOU 1876 O ALA A1037 9797 7516 13519 1277 -786 592 O
ATOM 1877 CB ALA A1037 37.247 -51.527 23.474 1.00 64.83 C
ANISOU 1877 CB ALA A1037 7689 5071 11874 1514 -739 475 C
ATOM 1878 N LEU A1038 36.437 -49.541 25.726 1.00 77.15 N
ANISOU 1878 N LEU A1038 9086 7058 13169 1392 -782 818 N
ATOM 1879 CA LEU A1038 35.469 -49.057 26.706 1.00 74.90 C
ANISOU 1879 CA LEU A1038 8756 6893 12809 1316 -846 994 C
ATOM 1880 C LEU A1038 35.359 -47.538 26.674 1.00 81.01 C
ANISOU 1880 C LEU A1038 9550 7886 13347 1267 -802 956 C
ATOM 1881 O LEU A1038 34.266 -46.985 26.842 1.00 72.34 O
ANISOU 1881 O LEU A1038 8482 6861 12143 1180 -843 1013 O
ATOM 1882 CB LEU A1038 35.854 -49.536 28.106 1.00 68.76 C
ANISOU 1882 CB LEU A1038 7840 6149 12137 1369 -882 1205 C
ATOM 1883 CG LEU A1038 35.987 -51.046 28.310 1.00 76.31 C
ANISOU 1883 CG LEU A1038 8757 6896 13342 1420 -928 1275 C
ATOM 1884 CD1 LEU A1038 36.372 -51.358 29.747 1.00 90.40 C
ANISOU 1884 CD1 LEU A1038 10398 8749 15202 1474 -957 1495 C
ATOM 1885 CD2 LEU A1038 34.703 -51.763 27.929 1.00 68.05 C
ANISOU 1885 CD2 LEU A1038 7778 5687 12390 1344 -1009 1293 C
ATOM 1886 N ASP A1039 36.479 -46.845 26.458 1.00 70.90 N
ANISOU 1886 N ASP A1039 8246 6706 11987 1322 -718 865 N
ATOM 1887 CA ASP A1039 36.459 -45.389 26.427 1.00 71.21 C
ANISOU 1887 CA ASP A1039 8296 6946 11816 1279 -676 827 C
ATOM 1888 C ASP A1039 35.779 -44.838 25.182 1.00 70.12 C
ANISOU 1888 C ASP A1039 8286 6797 11558 1210 -648 667 C
ATOM 1889 O ASP A1039 35.517 -43.631 25.122 1.00 77.93 O
ANISOU 1889 O ASP A1039 9294 7944 12373 1158 -623 644 O
ATOM 1890 CB ASP A1039 37.883 -44.842 26.523 1.00 75.11 C
ANISOU 1890 CB ASP A1039 8719 7537 12281 1358 -599 780 C
ATOM 1891 CG ASP A1039 37.995 -43.684 27.490 1.00 90.42 C
ANISOU 1891 CG ASP A1039 10584 9690 14081 1339 -608 877 C
ATOM 1892 OD1 ASP A1039 36.945 -43.194 27.954 1.00 88.12 O
ANISOU 1892 OD1 ASP A1039 10310 9480 13690 1265 -660 960 O
ATOM 1893 OD2 ASP A1039 39.134 -43.271 27.793 1.00 98.27 O
ANISOU 1893 OD2 ASP A1039 11501 10767 15069 1400 -566 871 O
ATOM 1894 N ALA A1040 35.492 -45.684 24.193 1.00 61.45 N
ANISOU 1894 N ALA A1040 7278 5520 10550 1211 -656 554 N
ATOM 1895 CA ALA A1040 34.773 -45.259 23.000 1.00 80.34 C
ANISOU 1895 CA ALA A1040 9798 7894 12832 1147 -640 404 C
ATOM 1896 C ALA A1040 33.262 -45.347 23.177 1.00 88.69 C
ANISOU 1896 C ALA A1040 10900 8925 13874 1042 -732 487 C
ATOM 1897 O ALA A1040 32.529 -44.492 22.669 1.00 69.35 O
ANISOU 1897 O ALA A1040 8520 6557 11273 966 -726 432 O
ATOM 1898 CB ALA A1040 35.208 -46.099 21.796 1.00 59.07 C
ANISOU 1898 CB ALA A1040 7189 5023 10231 1206 -607 228 C
ATOM 1899 N GLN A1041 32.780 -46.367 23.893 1.00 77.62 N
ANISOU 1899 N GLN A1041 9452 7408 12631 1037 -817 628 N
ATOM 1900 CA GLN A1041 31.345 -46.516 24.106 1.00 70.44 C
ANISOU 1900 CA GLN A1041 8571 6465 11726 941 -906 727 C
ATOM 1901 C GLN A1041 30.829 -45.600 25.208 1.00 84.25 C
ANISOU 1901 C GLN A1041 10250 8409 13351 894 -922 898 C
ATOM 1902 O GLN A1041 29.650 -45.231 25.197 1.00 95.09 O
ANISOU 1902 O GLN A1041 11661 9816 14651 805 -967 949 O
ATOM 1903 CB GLN A1041 31.008 -47.973 24.434 1.00 61.53 C
ANISOU 1903 CB GLN A1041 7415 5134 10830 954 -991 822 C
ATOM 1904 CG GLN A1041 31.684 -48.496 25.691 1.00 79.39 C
ANISOU 1904 CG GLN A1041 9543 7412 13211 1026 -1000 996 C
ATOM 1905 CD GLN A1041 31.224 -49.890 26.073 1.00 76.61 C
ANISOU 1905 CD GLN A1041 9154 6863 13091 1030 -1088 1114 C
ATOM 1906 OE1 GLN A1041 30.358 -50.474 25.421 1.00 84.68 O
ANISOU 1906 OE1 GLN A1041 10251 7731 14194 973 -1151 1069 O
ATOM 1907 NE2 GLN A1041 31.802 -50.430 27.138 1.00 68.54 N
ANISOU 1907 NE2 GLN A1041 8014 5844 12184 1097 -1097 1271 N
ATOM 1908 N LYS A1042 31.684 -45.224 26.155 1.00 72.93 N
ANISOU 1908 N LYS A1042 8716 7103 11891 955 -889 986 N
ATOM 1909 CA LYS A1042 31.281 -44.347 27.249 1.00 70.64 C
ANISOU 1909 CA LYS A1042 8362 7004 11476 927 -906 1141 C
ATOM 1910 C LYS A1042 31.353 -42.880 26.835 1.00 82.10 C
ANISOU 1910 C LYS A1042 9856 8628 12710 891 -844 1037 C
ATOM 1911 O LYS A1042 31.197 -42.547 25.660 1.00 68.19 O
ANISOU 1911 O LYS A1042 8191 6835 10884 854 -807 874 O
ATOM 1912 CB LYS A1042 32.157 -44.589 28.480 1.00 74.36 C
ANISOU 1912 CB LYS A1042 8706 7536 12010 1012 -909 1280 C
ATOM 1913 N GLU A1057 17.730 -49.313 17.734 1.00 90.17 N
ANISOU 1913 N GLU A1057 11849 7834 14577 -97 -1911 565 N
ATOM 1914 CA GLU A1057 18.967 -49.716 17.078 1.00 92.33 C
ANISOU 1914 CA GLU A1057 12187 8034 14861 10 -1856 354 C
ATOM 1915 C GLU A1057 20.177 -49.326 17.918 1.00 98.26 C
ANISOU 1915 C GLU A1057 12852 8932 15552 107 -1730 414 C
ATOM 1916 O GLU A1057 21.321 -49.531 17.510 1.00 94.25 O
ANISOU 1916 O GLU A1057 12376 8397 15037 205 -1662 263 O
ATOM 1917 CB GLU A1057 19.065 -49.091 15.685 1.00106.45 C
ANISOU 1917 CB GLU A1057 14123 9861 16463 9 -1819 97 C
ATOM 1918 N MET A1058 19.916 -48.758 19.097 1.00100.58 N
ANISOU 1918 N MET A1058 13033 9385 15799 83 -1700 637 N
ATOM 1919 CA MET A1058 20.998 -48.400 20.007 1.00 93.04 C
ANISOU 1919 CA MET A1058 11986 8571 14794 171 -1596 712 C
ATOM 1920 C MET A1058 21.615 -49.622 20.674 1.00103.66 C
ANISOU 1920 C MET A1058 13249 9765 16372 244 -1628 799 C
ATOM 1921 O MET A1058 22.766 -49.556 21.118 1.00100.71 O
ANISOU 1921 O MET A1058 12824 9458 15983 338 -1546 794 O
ATOM 1922 CB MET A1058 20.492 -47.419 21.066 1.00 75.82 C
ANISOU 1922 CB MET A1058 9719 6606 12485 129 -1562 918 C
ATOM 1923 N LYS A1059 20.877 -50.732 20.752 1.00 97.38 N
ANISOU 1923 N LYS A1059 12436 8766 15799 203 -1749 883 N
ATOM 1924 CA LYS A1059 21.413 -51.971 21.303 1.00 97.28 C
ANISOU 1924 CA LYS A1059 12348 8586 16028 270 -1788 961 C
ATOM 1925 C LYS A1059 22.405 -52.648 20.369 1.00 98.48 C
ANISOU 1925 C LYS A1059 12584 8584 16251 354 -1771 726 C
ATOM 1926 O LYS A1059 23.274 -53.386 20.844 1.00 94.47 O
ANISOU 1926 O LYS A1059 12011 7999 15883 441 -1752 762 O
ATOM 1927 CB LYS A1059 20.276 -52.940 21.629 1.00 87.43 C
ANISOU 1927 CB LYS A1059 11052 7157 15008 195 -1927 1125 C
ATOM 1928 N ASP A1060 22.294 -52.419 19.057 1.00 96.42 N
ANISOU 1928 N ASP A1060 12463 8279 15894 337 -1775 490 N
ATOM 1929 CA ASP A1060 23.279 -52.964 18.131 1.00100.20 C
ANISOU 1929 CA ASP A1060 13028 8634 16409 432 -1744 257 C
ATOM 1930 C ASP A1060 24.644 -52.320 18.330 1.00 96.11 C
ANISOU 1930 C ASP A1060 12480 8282 15755 536 -1594 204 C
ATOM 1931 O ASP A1060 25.672 -52.983 18.150 1.00 85.92 O
ANISOU 1931 O ASP A1060 11192 6894 14560 639 -1558 113 O
ATOM 1932 CB ASP A1060 22.811 -52.780 16.686 1.00 95.18 C
ANISOU 1932 CB ASP A1060 12552 7936 15674 395 -1779 21 C
ATOM 1933 CG ASP A1060 21.670 -53.714 16.312 1.00117.37 C
ANISOU 1933 CG ASP A1060 15406 10519 18670 313 -1945 26 C
ATOM 1934 OD1 ASP A1060 21.314 -54.588 17.132 1.00114.40 O
ANISOU 1934 OD1 ASP A1060 14932 10014 18519 292 -2029 208 O
ATOM 1935 OD2 ASP A1060 21.128 -53.575 15.195 1.00115.66 O
ANISOU 1935 OD2 ASP A1060 15317 10252 18378 271 -1994 -148 O
ATOM 1936 N PHE A1061 24.679 -51.035 18.699 1.00 97.29 N
ANISOU 1936 N PHE A1061 12599 8678 15690 512 -1508 262 N
ATOM 1937 CA PHE A1061 25.958 -50.397 18.996 1.00 96.09 C
ANISOU 1937 CA PHE A1061 12401 8685 15424 604 -1376 234 C
ATOM 1938 C PHE A1061 26.517 -50.873 20.331 1.00 91.98 C
ANISOU 1938 C PHE A1061 11735 8175 15038 658 -1369 435 C
ATOM 1939 O PHE A1061 27.739 -50.940 20.503 1.00 82.26 O
ANISOU 1939 O PHE A1061 10465 6974 13817 758 -1289 396 O
ATOM 1940 CB PHE A1061 25.805 -48.875 18.990 1.00 82.58 C
ANISOU 1940 CB PHE A1061 10699 7225 13454 560 -1296 233 C
ATOM 1941 N ARG A1062 25.642 -51.199 21.286 1.00102.85 N
ANISOU 1941 N ARG A1062 13028 9533 16518 596 -1451 656 N
ATOM 1942 CA ARG A1062 26.081 -51.801 22.540 1.00 88.70 C
ANISOU 1942 CA ARG A1062 11099 7730 14873 650 -1458 858 C
ATOM 1943 C ARG A1062 26.472 -53.262 22.346 1.00 76.99 C
ANISOU 1943 C ARG A1062 9612 5993 13647 708 -1515 822 C
ATOM 1944 O ARG A1062 27.445 -53.731 22.946 1.00 84.47 O
ANISOU 1944 O ARG A1062 10479 6925 14691 799 -1476 878 O
ATOM 1945 CB ARG A1062 24.983 -51.676 23.595 1.00 98.77 C
ANISOU 1945 CB ARG A1062 12286 9072 16170 572 -1522 1113 C
ATOM 1946 N HIS A1063 25.726 -53.991 21.510 1.00 85.55 N
ANISOU 1946 N HIS A1063 10783 6874 14848 658 -1611 729 N
ATOM 1947 CA HIS A1063 26.080 -55.373 21.203 1.00 88.36 C
ANISOU 1947 CA HIS A1063 11151 6972 15450 715 -1672 667 C
ATOM 1948 C HIS A1063 27.394 -55.457 20.437 1.00 89.29 C
ANISOU 1948 C HIS A1063 11334 7064 15529 829 -1580 445 C
ATOM 1949 O HIS A1063 28.095 -56.471 20.520 1.00 86.38 O
ANISOU 1949 O HIS A1063 10937 6537 15347 912 -1589 430 O
ATOM 1950 CB HIS A1063 24.955 -56.036 20.404 1.00 79.56 C
ANISOU 1950 CB HIS A1063 10125 5649 14454 631 -1804 596 C
ATOM 1951 CG HIS A1063 25.224 -57.462 20.036 1.00 79.77 C
ANISOU 1951 CG HIS A1063 10173 5393 14742 683 -1882 522 C
ATOM 1952 ND1 HIS A1063 25.348 -58.464 20.974 1.00 90.72 N
ANISOU 1952 ND1 HIS A1063 11440 6657 16373 712 -1930 709 N
ATOM 1953 CD2 HIS A1063 25.381 -58.056 18.829 1.00 84.68 C
ANISOU 1953 CD2 HIS A1063 10925 5830 15420 715 -1921 279 C
ATOM 1954 CE1 HIS A1063 25.575 -59.612 20.362 1.00 89.45 C
ANISOU 1954 CE1 HIS A1063 11332 6240 16416 756 -1998 584 C
ATOM 1955 NE2 HIS A1063 25.599 -59.393 19.060 1.00 86.26 N
ANISOU 1955 NE2 HIS A1063 11082 5792 15898 761 -1995 319 N
ATOM 1956 N GLY A1064 27.743 -54.406 19.693 1.00 82.68 N
ANISOU 1956 N GLY A1064 10580 6380 14456 839 -1488 280 N
ATOM 1957 CA GLY A1064 29.000 -54.412 18.965 1.00 68.19 C
ANISOU 1957 CA GLY A1064 8799 4538 12572 954 -1390 82 C
ATOM 1958 C GLY A1064 30.205 -54.318 19.881 1.00 75.63 C
ANISOU 1958 C GLY A1064 9620 5585 13531 1047 -1297 185 C
ATOM 1959 O GLY A1064 31.202 -55.019 19.684 1.00 69.13 O
ANISOU 1959 O GLY A1064 8793 4656 12819 1152 -1259 107 O
ATOM 1960 N PHE A1065 30.133 -53.452 20.895 1.00 67.80 N
ANISOU 1960 N PHE A1065 8529 4801 12429 1012 -1262 361 N
ATOM 1961 CA PHE A1065 31.231 -53.352 21.851 1.00 66.12 C
ANISOU 1961 CA PHE A1065 8194 4693 12234 1096 -1188 472 C
ATOM 1962 C PHE A1065 31.317 -54.585 22.739 1.00 80.46 C
ANISOU 1962 C PHE A1065 9909 6358 14304 1132 -1255 639 C
ATOM 1963 O PHE A1065 32.410 -54.939 23.195 1.00 82.90 O
ANISOU 1963 O PHE A1065 10142 6664 14691 1229 -1203 671 O
ATOM 1964 CB PHE A1065 31.079 -52.094 22.703 1.00 65.75 C
ANISOU 1964 CB PHE A1065 8076 4907 12000 1051 -1146 609 C
ATOM 1965 CG PHE A1065 31.507 -50.836 22.007 1.00 73.34 C
ANISOU 1965 CG PHE A1065 9101 6041 12724 1054 -1046 456 C
ATOM 1966 CD1 PHE A1065 32.822 -50.406 22.073 1.00 65.60 C
ANISOU 1966 CD1 PHE A1065 8076 5163 11684 1145 -941 403 C
ATOM 1967 CD2 PHE A1065 30.597 -50.082 21.287 1.00 66.38 C
ANISOU 1967 CD2 PHE A1065 8316 5218 11688 965 -1058 372 C
ATOM 1968 CE1 PHE A1065 33.220 -49.248 21.432 1.00 67.36 C
ANISOU 1968 CE1 PHE A1065 8349 5542 11703 1148 -850 274 C
ATOM 1969 CE2 PHE A1065 30.989 -48.923 20.645 1.00 66.07 C
ANISOU 1969 CE2 PHE A1065 8330 5337 11438 968 -964 240 C
ATOM 1970 CZ PHE A1065 32.302 -48.506 20.717 1.00 60.49 C
ANISOU 1970 CZ PHE A1065 7575 4728 10679 1060 -860 193 C
ATOM 1971 N ASP A1066 30.186 -55.246 22.998 1.00 78.01 N
ANISOU 1971 N ASP A1066 9590 5920 14131 1055 -1371 754 N
ATOM 1972 CA ASP A1066 30.211 -56.471 23.791 1.00 72.41 C
ANISOU 1972 CA ASP A1066 8782 5050 13680 1087 -1439 919 C
ATOM 1973 C ASP A1066 31.007 -57.560 23.083 1.00 74.50 C
ANISOU 1973 C ASP A1066 9094 5093 14121 1178 -1438 762 C
ATOM 1974 O ASP A1066 31.824 -58.251 23.703 1.00 86.77 O
ANISOU 1974 O ASP A1066 10556 6589 15823 1263 -1420 847 O
ATOM 1975 CB ASP A1066 28.784 -56.943 24.075 1.00 98.57 C
ANISOU 1975 CB ASP A1066 12082 8260 17112 981 -1565 1064 C
ATOM 1976 CG ASP A1066 27.996 -55.953 24.911 1.00113.73 C
ANISOU 1976 CG ASP A1066 13941 10396 18874 902 -1563 1248 C
ATOM 1977 OD1 ASP A1066 28.578 -54.933 25.339 1.00108.42 O
ANISOU 1977 OD1 ASP A1066 13234 9950 18010 932 -1472 1266 O
ATOM 1978 OD2 ASP A1066 26.791 -56.194 25.138 1.00101.15 O
ANISOU 1978 OD2 ASP A1066 12334 8745 17353 813 -1656 1376 O
ATOM 1979 N ILE A1067 30.779 -57.728 21.779 1.00 82.86 N
ANISOU 1979 N ILE A1067 10296 6026 15161 1168 -1460 533 N
ATOM 1980 CA ILE A1067 31.572 -58.678 21.003 1.00 73.93 C
ANISOU 1980 CA ILE A1067 9226 4693 14169 1267 -1450 356 C
ATOM 1981 C ILE A1067 33.027 -58.233 20.954 1.00 73.55 C
ANISOU 1981 C ILE A1067 9156 4771 14020 1384 -1309 275 C
ATOM 1982 O ILE A1067 33.947 -59.051 21.076 1.00 79.95 O
ANISOU 1982 O ILE A1067 9924 5468 14984 1487 -1283 264 O
ATOM 1983 CB ILE A1067 30.985 -58.837 19.588 1.00 74.63 C
ANISOU 1983 CB ILE A1067 9485 4644 14225 1235 -1503 116 C
ATOM 1984 CG1 ILE A1067 29.503 -59.207 19.657 1.00 93.30 C
ANISOU 1984 CG1 ILE A1067 11865 6894 16692 1109 -1650 207 C
ATOM 1985 CG2 ILE A1067 31.763 -59.884 18.802 1.00 76.65 C
ANISOU 1985 CG2 ILE A1067 9811 4681 14631 1347 -1501 -68 C
ATOM 1986 CD1 ILE A1067 28.814 -59.212 18.308 1.00 90.26 C
ANISOU 1986 CD1 ILE A1067 11646 6400 16247 1063 -1712 -19 C
ATOM 1987 N LEU A1068 33.256 -56.930 20.783 1.00 71.80 N
ANISOU 1987 N LEU A1068 8954 4781 13546 1370 -1218 224 N
ATOM 1988 CA LEU A1068 34.615 -56.408 20.691 1.00 71.40 C
ANISOU 1988 CA LEU A1068 8878 4858 13394 1474 -1084 149 C
ATOM 1989 C LEU A1068 35.387 -56.654 21.982 1.00 71.47 C
ANISOU 1989 C LEU A1068 8725 4924 13505 1532 -1058 350 C
ATOM 1990 O LEU A1068 36.449 -57.287 21.978 1.00 72.61 O
ANISOU 1990 O LEU A1068 8834 4988 13766 1641 -1010 316 O
ATOM 1991 CB LEU A1068 34.574 -54.916 20.360 1.00 69.47 C
ANISOU 1991 CB LEU A1068 8672 4852 12870 1431 -1004 85 C
ATOM 1992 CG LEU A1068 35.922 -54.200 20.283 1.00 68.89 C
ANISOU 1992 CG LEU A1068 8562 4934 12678 1525 -866 21 C
ATOM 1993 CD1 LEU A1068 36.690 -54.622 19.042 1.00 70.16 C
ANISOU 1993 CD1 LEU A1068 8824 4979 12854 1627 -801 -210 C
ATOM 1994 CD2 LEU A1068 35.722 -52.696 20.312 1.00 75.29 C
ANISOU 1994 CD2 LEU A1068 9376 5992 13241 1461 -810 27 C
ATOM 1995 N VAL A1069 34.863 -56.155 23.105 1.00 70.30 N
ANISOU 1995 N VAL A1069 8479 4920 13312 1463 -1090 564 N
ATOM 1996 CA VAL A1069 35.538 -56.341 24.385 1.00 70.35 C
ANISOU 1996 CA VAL A1069 8332 4998 13400 1518 -1073 764 C
ATOM 1997 C VAL A1069 35.535 -57.810 24.788 1.00 72.25 C
ANISOU 1997 C VAL A1069 8516 5012 13923 1558 -1146 862 C
ATOM 1998 O VAL A1069 36.489 -58.292 25.413 1.00 72.99 O
ANISOU 1998 O VAL A1069 8512 5093 14130 1648 -1112 944 O
ATOM 1999 CB VAL A1069 34.888 -55.451 25.460 1.00 68.74 C
ANISOU 1999 CB VAL A1069 8048 5003 13066 1440 -1095 962 C
ATOM 2000 CG1 VAL A1069 35.593 -55.618 26.799 1.00 68.84 C
ANISOU 2000 CG1 VAL A1069 7906 5103 13149 1503 -1082 1167 C
ATOM 2001 CG2 VAL A1069 34.917 -53.994 25.023 1.00 74.29 C
ANISOU 2001 CG2 VAL A1069 8808 5919 13500 1402 -1023 856 C
ATOM 2002 N GLY A1070 34.479 -58.547 24.437 1.00 73.15 N
ANISOU 2002 N GLY A1070 8687 4940 14164 1492 -1251 858 N
ATOM 2003 CA GLY A1070 34.459 -59.972 24.725 1.00 75.09 C
ANISOU 2003 CA GLY A1070 8885 4950 14696 1528 -1326 939 C
ATOM 2004 C GLY A1070 35.544 -60.730 23.985 1.00 79.75 C
ANISOU 2004 C GLY A1070 9521 5381 15401 1646 -1277 763 C
ATOM 2005 O GLY A1070 36.106 -61.697 24.506 1.00 77.99 O
ANISOU 2005 O GLY A1070 9213 5034 15386 1718 -1289 855 O
ATOM 2006 N GLN A1071 35.854 -60.302 22.759 1.00 76.47 N
ANISOU 2006 N GLN A1071 9237 4969 14850 1672 -1218 513 N
ATOM 2007 CA GLN A1071 36.950 -60.919 22.020 1.00 77.89 C
ANISOU 2007 CA GLN A1071 9463 5020 15110 1798 -1154 338 C
ATOM 2008 C GLN A1071 38.305 -60.493 22.570 1.00 77.40 C
ANISOU 2008 C GLN A1071 9300 5117 14992 1896 -1033 390 C
ATOM 2009 O GLN A1071 39.258 -61.280 22.542 1.00 78.80 O
ANISOU 2009 O GLN A1071 9444 5180 15318 2007 -996 362 O
ATOM 2010 CB GLN A1071 36.849 -60.574 20.535 1.00 77.94 C
ANISOU 2010 CB GLN A1071 9644 4995 14977 1804 -1124 60 C
ATOM 2011 CG GLN A1071 35.744 -61.301 19.788 1.00 83.81 C
ANISOU 2011 CG GLN A1071 10502 5518 15824 1740 -1249 -40 C
ATOM 2012 CD GLN A1071 35.583 -60.805 18.364 1.00 78.97 C
ANISOU 2012 CD GLN A1071 10060 4910 15034 1742 -1219 -306 C
ATOM 2013 OE1 GLN A1071 35.884 -59.651 18.060 1.00 85.06 O
ANISOU 2013 OE1 GLN A1071 10858 5892 15568 1741 -1121 -370 O
ATOM 2014 NE2 GLN A1071 35.110 -61.677 17.481 1.00 84.05 N
ANISOU 2014 NE2 GLN A1071 10821 5319 15794 1748 -1307 -462 N
ATOM 2015 N ILE A1072 38.411 -59.258 23.070 1.00 75.50 N
ANISOU 2015 N ILE A1072 9008 5134 14545 1858 -976 464 N
ATOM 2016 CA ILE A1072 39.664 -58.803 23.665 1.00 75.03 C
ANISOU 2016 CA ILE A1072 8842 5231 14436 1942 -875 526 C
ATOM 2017 C ILE A1072 39.972 -59.596 24.929 1.00 75.83 C
ANISOU 2017 C ILE A1072 8793 5288 14733 1979 -916 754 C
ATOM 2018 O ILE A1072 41.122 -59.978 25.174 1.00 76.64 O
ANISOU 2018 O ILE A1072 8822 5373 14924 2086 -855 770 O
ATOM 2019 CB ILE A1072 39.606 -57.288 23.938 1.00 72.87 C
ANISOU 2019 CB ILE A1072 8549 5234 13903 1883 -822 556 C
ATOM 2020 CG1 ILE A1072 39.556 -56.510 22.621 1.00 74.96 C
ANISOU 2020 CG1 ILE A1072 8954 5548 13981 1870 -760 323 C
ATOM 2021 CG2 ILE A1072 40.797 -56.840 24.769 1.00 72.41 C
ANISOU 2021 CG2 ILE A1072 8360 5338 13815 1957 -745 658 C
ATOM 2022 CD1 ILE A1072 39.518 -55.005 22.800 1.00 70.17 C
ANISOU 2022 CD1 ILE A1072 8332 5202 13128 1814 -705 340 C
ATOM 2023 N ASP A1073 38.949 -59.869 25.745 1.00 75.70 N
ANISOU 2023 N ASP A1073 8723 5252 14788 1896 -1017 940 N
ATOM 2024 CA ASP A1073 39.153 -60.684 26.938 1.00 76.60 C
ANISOU 2024 CA ASP A1073 8693 5316 15094 1933 -1060 1169 C
ATOM 2025 C ASP A1073 39.529 -62.119 26.584 1.00 78.82 C
ANISOU 2025 C ASP A1073 8981 5323 15642 2010 -1087 1122 C
ATOM 2026 O ASP A1073 40.289 -62.756 27.322 1.00 85.33 O
ANISOU 2026 O ASP A1073 9692 6114 16618 2090 -1073 1248 O
ATOM 2027 CB ASP A1073 37.898 -60.661 27.813 1.00 79.26 C
ANISOU 2027 CB ASP A1073 8978 5691 15447 1829 -1158 1380 C
ATOM 2028 CG ASP A1073 37.628 -59.291 28.415 1.00 89.19 C
ANISOU 2028 CG ASP A1073 10204 7230 16455 1770 -1131 1464 C
ATOM 2029 OD1 ASP A1073 38.485 -58.393 28.273 1.00 75.38 O
ANISOU 2029 OD1 ASP A1073 8455 5646 14539 1810 -1041 1377 O
ATOM 2030 OD2 ASP A1073 36.555 -59.112 29.031 1.00 78.33 O
ANISOU 2030 OD2 ASP A1073 8800 5908 15054 1685 -1200 1620 O
ATOM 2031 N ASP A1074 39.012 -62.645 25.469 1.00 79.75 N
ANISOU 2031 N ASP A1074 9233 5245 15824 1991 -1129 940 N
ATOM 2032 CA ASP A1074 39.384 -63.993 25.047 1.00 81.96 C
ANISOU 2032 CA ASP A1074 9533 5254 16354 2071 -1157 870 C
ATOM 2033 C ASP A1074 40.866 -64.066 24.703 1.00 82.57 C
ANISOU 2033 C ASP A1074 9599 5341 16431 2209 -1039 755 C
ATOM 2034 O ASP A1074 41.583 -64.959 25.170 1.00 83.94 O
ANISOU 2034 O ASP A1074 9685 5405 16802 2297 -1032 837 O
ATOM 2035 CB ASP A1074 38.536 -64.429 23.850 1.00 88.70 C
ANISOU 2035 CB ASP A1074 10546 5908 17249 2024 -1230 672 C
ATOM 2036 CG ASP A1074 37.076 -64.646 24.210 1.00 86.11 C
ANISOU 2036 CG ASP A1074 10213 5513 16992 1894 -1362 804 C
ATOM 2037 OD1 ASP A1074 36.709 -64.439 25.385 1.00 89.21 O
ANISOU 2037 OD1 ASP A1074 10480 6022 17392 1845 -1389 1052 O
ATOM 2038 OD2 ASP A1074 36.294 -65.027 23.311 1.00 83.46 O
ANISOU 2038 OD2 ASP A1074 9998 5009 16703 1845 -1441 662 O
ATOM 2039 N ALA A1075 41.344 -63.126 23.884 1.00 81.60 N
ANISOU 2039 N ALA A1075 9561 5352 16091 2233 -943 572 N
ATOM 2040 CA ALA A1075 42.757 -63.107 23.521 1.00 83.93 C
ANISOU 2040 CA ALA A1075 9842 5672 16374 2365 -822 467 C
ATOM 2041 C ALA A1075 43.638 -62.740 24.709 1.00 88.00 C
ANISOU 2041 C ALA A1075 10190 6364 16881 2407 -768 663 C
ATOM 2042 O ALA A1075 44.782 -63.201 24.795 1.00 90.20 O
ANISOU 2042 O ALA A1075 10406 6601 17263 2523 -701 661 O
ATOM 2043 CB ALA A1075 42.985 -62.139 22.361 1.00 81.25 C
ANISOU 2043 CB ALA A1075 9627 5442 15801 2376 -732 240 C
ATOM 2044 N LEU A1076 43.129 -61.917 25.630 1.00 79.85 N
ANISOU 2044 N LEU A1076 9084 5529 15728 2318 -798 831 N
ATOM 2045 CA LEU A1076 43.886 -61.602 26.837 1.00 79.33 C
ANISOU 2045 CA LEU A1076 8859 5629 15656 2356 -766 1025 C
ATOM 2046 C LEU A1076 44.076 -62.836 27.709 1.00 80.92 C
ANISOU 2046 C LEU A1076 8946 5683 16118 2407 -821 1205 C
ATOM 2047 O LEU A1076 45.139 -63.015 28.316 1.00 89.40 O
ANISOU 2047 O LEU A1076 9907 6803 17259 2496 -771 1294 O
ATOM 2048 CB LEU A1076 43.190 -60.491 27.622 1.00 77.38 C
ANISOU 2048 CB LEU A1076 8570 5614 15219 2252 -798 1158 C
ATOM 2049 CG LEU A1076 43.648 -59.070 27.296 1.00 89.76 C
ANISOU 2049 CG LEU A1076 10163 7410 16530 2241 -711 1058 C
ATOM 2050 CD1 LEU A1076 42.760 -58.037 27.975 1.00 74.50 C
ANISOU 2050 CD1 LEU A1076 8212 5678 14418 2131 -757 1172 C
ATOM 2051 CD2 LEU A1076 45.101 -58.884 27.708 1.00 75.91 C
ANISOU 2051 CD2 LEU A1076 8302 5755 14787 2346 -626 1091 C
ATOM 2052 N LYS A1077 43.060 -63.699 27.788 1.00 83.42 N
ANISOU 2052 N LYS A1077 9285 5821 16591 2351 -925 1268 N
ATOM 2053 CA LYS A1077 43.209 -64.937 28.546 1.00 87.25 C
ANISOU 2053 CA LYS A1077 9673 6186 17291 2380 -970 1426 C
ATOM 2054 C LYS A1077 44.243 -65.851 27.901 1.00 85.24 C
ANISOU 2054 C LYS A1077 9448 5783 17155 2486 -909 1286 C
ATOM 2055 O LYS A1077 45.037 -66.491 28.599 1.00103.16 O
ANISOU 2055 O LYS A1077 11614 8071 19510 2540 -882 1398 O
ATOM 2056 CB LYS A1077 41.860 -65.647 28.670 1.00 84.06 C
ANISOU 2056 CB LYS A1077 9301 5664 16974 2268 -1085 1500 C
ATOM 2057 CG LYS A1077 41.914 -66.960 29.443 1.00 91.40 C
ANISOU 2057 CG LYS A1077 10140 6513 18074 2264 -1125 1654 C
ATOM 2058 CD LYS A1077 40.522 -67.534 29.671 1.00 99.16 C
ANISOU 2058 CD LYS A1077 11133 7411 19133 2144 -1238 1753 C
ATOM 2059 CE LYS A1077 39.820 -67.828 28.354 1.00115.28 C
ANISOU 2059 CE LYS A1077 13333 9249 21218 2105 -1290 1535 C
ATOM 2060 NZ LYS A1077 38.435 -68.340 28.557 1.00 99.54 N
ANISOU 2060 NZ LYS A1077 11344 7178 19300 1981 -1404 1634 N
ATOM 2061 N LEU A1078 44.256 -65.912 26.570 1.00 85.71 N
ANISOU 2061 N LEU A1078 9651 5703 17210 2519 -884 1039 N
ATOM 2062 CA LEU A1078 45.246 -66.726 25.874 1.00 87.46 C
ANISOU 2062 CA LEU A1078 9915 5794 17522 2630 -818 891 C
ATOM 2063 C LEU A1078 46.639 -66.116 25.960 1.00 91.64 C
ANISOU 2063 C LEU A1078 10374 6464 17981 2741 -692 875 C
ATOM 2064 O LEU A1078 47.631 -66.850 26.032 1.00 88.42 O
ANISOU 2064 O LEU A1078 9922 6010 17665 2830 -638 876 O
ATOM 2065 CB LEU A1078 44.830 -66.916 24.420 1.00 88.35 C
ANISOU 2065 CB LEU A1078 10210 5738 17622 2637 -827 626 C
ATOM 2066 CG LEU A1078 43.454 -67.551 24.218 1.00 88.74 C
ANISOU 2066 CG LEU A1078 10337 5636 17746 2524 -959 621 C
ATOM 2067 CD1 LEU A1078 43.029 -67.449 22.763 1.00 89.05 C
ANISOU 2067 CD1 LEU A1078 10562 5552 17720 2527 -968 348 C
ATOM 2068 CD2 LEU A1078 43.458 -69.006 24.678 1.00 90.84 C
ANISOU 2068 CD2 LEU A1078 10550 5754 18209 2523 -1016 718 C
ATOM 2069 N ALA A1079 46.736 -64.784 25.967 1.00 88.54 N
ANISOU 2069 N ALA A1079 9966 6249 17425 2734 -645 866 N
ATOM 2070 CA ALA A1079 48.045 -64.145 26.056 1.00 88.46 C
ANISOU 2070 CA ALA A1079 9886 6403 17322 2821 -527 853 C
ATOM 2071 C ALA A1079 48.651 -64.319 27.443 1.00 90.23 C
ANISOU 2071 C ALA A1079 9932 6734 17618 2842 -535 1096 C
ATOM 2072 O ALA A1079 49.870 -64.478 27.579 1.00 88.57 O
ANISOU 2072 O ALA A1079 9652 6567 17434 2935 -455 1104 O
ATOM 2073 CB ALA A1079 47.935 -62.664 25.701 1.00 82.66 C
ANISOU 2073 CB ALA A1079 9202 5902 16303 2758 -474 769 C
ATOM 2074 N ASN A1080 47.816 -64.290 28.486 1.00 84.10 N
ANISOU 2074 N ASN A1080 9089 6028 16837 2747 -628 1293 N
ATOM 2075 CA ASN A1080 48.318 -64.500 29.839 1.00 88.06 C
ANISOU 2075 CA ASN A1080 9436 6660 17363 2753 -640 1519 C
ATOM 2076 C ASN A1080 48.793 -65.932 30.046 1.00 86.44 C
ANISOU 2076 C ASN A1080 9195 6311 17336 2798 -644 1562 C
ATOM 2077 O ASN A1080 49.726 -66.168 30.822 1.00 86.98 O
ANISOU 2077 O ASN A1080 9148 6465 17435 2850 -611 1679 O
ATOM 2078 CB ASN A1080 47.239 -64.147 30.864 1.00 83.19 C
ANISOU 2078 CB ASN A1080 8767 6159 16682 2644 -734 1713 C
ATOM 2079 CG ASN A1080 46.826 -62.693 30.795 1.00 87.77 C
ANISOU 2079 CG ASN A1080 9366 6901 17080 2603 -731 1693 C
ATOM 2080 OD1 ASN A1080 47.566 -61.850 30.289 1.00 93.24 O
ANISOU 2080 OD1 ASN A1080 10084 7712 17628 2633 -646 1563 O
ATOM 2081 ND2 ASN A1080 45.637 -62.390 31.304 1.00101.35 N
ANISOU 2081 ND2 ASN A1080 11092 8682 18733 2499 -813 1804 N
ATOM 2082 N GLU A1081 48.171 -66.897 29.365 1.00 87.74 N
ANISOU 2082 N GLU A1081 9458 6258 17620 2777 -689 1466 N
ATOM 2083 CA GLU A1081 48.607 -68.285 29.452 1.00 89.91 C
ANISOU 2083 CA GLU A1081 9710 6379 18073 2823 -693 1488 C
ATOM 2084 C GLU A1081 49.910 -68.544 28.714 1.00 96.24 C
ANISOU 2084 C GLU A1081 10536 7124 18907 2952 -587 1336 C
ATOM 2085 O GLU A1081 50.481 -69.630 28.864 1.00104.39 O
ANISOU 2085 O GLU A1081 11532 8051 20079 3006 -577 1365 O
ATOM 2086 CB GLU A1081 47.517 -69.210 28.904 1.00 91.05 C
ANISOU 2086 CB GLU A1081 9955 6306 18333 2759 -782 1421 C
ATOM 2087 CG GLU A1081 46.225 -69.203 29.704 1.00 95.71 C
ANISOU 2087 CG GLU A1081 10507 6935 18925 2631 -889 1596 C
ATOM 2088 CD GLU A1081 45.063 -69.814 28.944 1.00101.80 C
ANISOU 2088 CD GLU A1081 11397 7506 19776 2557 -976 1494 C
ATOM 2089 OE1 GLU A1081 45.217 -70.085 27.734 1.00102.48 O
ANISOU 2089 OE1 GLU A1081 11612 7439 19886 2603 -956 1266 O
ATOM 2090 OE2 GLU A1081 43.994 -70.021 29.554 1.00112.56 O
ANISOU 2090 OE2 GLU A1081 12724 8872 21171 2453 -1066 1640 O
ATOM 2091 N GLY A1082 50.394 -67.581 27.932 1.00101.99 N
ANISOU 2091 N GLY A1082 11320 7923 19509 3004 -504 1183 N
ATOM 2092 CA GLY A1082 51.580 -67.760 27.115 1.00 96.63 C
ANISOU 2092 CA GLY A1082 10674 7198 18843 3130 -393 1028 C
ATOM 2093 C GLY A1082 51.299 -68.143 25.679 1.00112.70 C
ANISOU 2093 C GLY A1082 12884 9048 20891 3166 -376 777 C
ATOM 2094 O GLY A1082 52.235 -68.185 24.874 1.00129.21 O
ANISOU 2094 O GLY A1082 15019 11111 22963 3277 -274 629 O
ATOM 2095 N LYS A1083 50.042 -68.420 25.338 1.00110.75 N
ANISOU 2095 N LYS A1083 12736 8679 20666 3078 -473 726 N
ATOM 2096 CA LYS A1083 49.671 -68.807 23.980 1.00 97.86 C
ANISOU 2096 CA LYS A1083 11280 6869 19034 3104 -475 482 C
ATOM 2097 C LYS A1083 49.772 -67.591 23.073 1.00 93.36 C
ANISOU 2097 C LYS A1083 10794 6395 18284 3131 -397 311 C
ATOM 2098 O LYS A1083 48.872 -66.749 23.039 1.00100.35 O
ANISOU 2098 O LYS A1083 11713 7345 19070 3041 -444 309 O
ATOM 2099 CB LYS A1083 48.264 -69.388 23.965 1.00 93.54 C
ANISOU 2099 CB LYS A1083 10801 6182 18560 2987 -612 494 C
ATOM 2100 CG LYS A1083 48.042 -70.420 25.051 1.00 94.36 C
ANISOU 2100 CG LYS A1083 10794 6229 18831 2940 -692 706 C
ATOM 2101 CD LYS A1083 46.672 -71.075 24.947 1.00102.74 C
ANISOU 2101 CD LYS A1083 11921 7139 19979 2828 -825 711 C
ATOM 2102 CE LYS A1083 46.609 -72.366 25.761 1.00 99.14 C
ANISOU 2102 CE LYS A1083 11371 6580 19718 2807 -888 876 C
ATOM 2103 NZ LYS A1083 47.035 -72.160 27.173 1.00 97.21 N
ANISOU 2103 NZ LYS A1083 10945 6509 19480 2797 -870 1135 N
ATOM 2104 N VAL A1084 50.871 -67.495 22.328 1.00 96.08 N
ANISOU 2104 N VAL A1084 11171 6753 18584 3257 -273 171 N
ATOM 2105 CA VAL A1084 51.069 -66.352 21.443 1.00 95.66 C
ANISOU 2105 CA VAL A1084 11188 6800 18358 3293 -183 11 C
ATOM 2106 C VAL A1084 50.301 -66.540 20.143 1.00 93.07 C
ANISOU 2106 C VAL A1084 11056 6328 17976 3288 -211 -228 C
ATOM 2107 O VAL A1084 49.562 -65.648 19.710 1.00 96.88 O
ANISOU 2107 O VAL A1084 11609 6866 18336 3225 -229 -307 O
ATOM 2108 CB VAL A1084 52.569 -66.123 21.183 1.00113.82 C
ANISOU 2108 CB VAL A1084 13433 9192 20621 3431 -32 -28 C
ATOM 2109 CG1 VAL A1084 52.765 -65.092 20.076 1.00 97.29 C
ANISOU 2109 CG1 VAL A1084 11431 7181 18355 3480 71 -219 C
ATOM 2110 CG2 VAL A1084 53.263 -65.672 22.459 1.00110.58 C
ANISOU 2110 CG2 VAL A1084 12829 8958 20228 3421 -12 202 C
ATOM 2111 N LYS A1085 50.458 -67.703 19.505 1.00 93.72 N
ANISOU 2111 N LYS A1085 11232 6229 18147 3353 -219 -347 N
ATOM 2112 CA LYS A1085 49.782 -67.949 18.235 1.00 94.52 C
ANISOU 2112 CA LYS A1085 11529 6194 18188 3357 -250 -585 C
ATOM 2113 C LYS A1085 48.270 -68.005 18.411 1.00 93.88 C
ANISOU 2113 C LYS A1085 11500 6039 18131 3204 -405 -554 C
ATOM 2114 O LYS A1085 47.523 -67.466 17.587 1.00 93.22 O
ANISOU 2114 O LYS A1085 11544 5949 17928 3161 -431 -708 O
ATOM 2115 CB LYS A1085 50.299 -69.243 17.606 1.00 97.13 C
ANISOU 2115 CB LYS A1085 11943 6347 18616 3463 -233 -705 C
ATOM 2116 CG LYS A1085 51.733 -69.161 17.105 1.00 97.95 C
ANISOU 2116 CG LYS A1085 12037 6513 18664 3628 -71 -785 C
ATOM 2117 CD LYS A1085 51.868 -68.126 16.001 1.00103.18 C
ANISOU 2117 CD LYS A1085 12806 7279 19120 3682 29 -976 C
ATOM 2118 CE LYS A1085 53.283 -68.080 15.454 1.00 98.63 C
ANISOU 2118 CE LYS A1085 12220 6766 18487 3852 196 -1050 C
ATOM 2119 NZ LYS A1085 53.679 -69.377 14.841 1.00100.72 N
ANISOU 2119 NZ LYS A1085 12584 6852 18833 3961 203 -1165 N
ATOM 2120 N GLU A1086 47.800 -68.647 19.482 1.00 94.10 N
ANISOU 2120 N GLU A1086 11427 6019 18309 3119 -508 -352 N
ATOM 2121 CA GLU A1086 46.368 -68.711 19.746 1.00 99.49 C
ANISOU 2121 CA GLU A1086 12138 6642 19022 2970 -653 -291 C
ATOM 2122 C GLU A1086 45.788 -67.355 20.129 1.00 91.01 C
ANISOU 2122 C GLU A1086 11023 5743 17815 2880 -662 -212 C
ATOM 2123 O GLU A1086 44.595 -67.125 19.908 1.00 90.36 O
ANISOU 2123 O GLU A1086 11014 5623 17696 2772 -760 -240 O
ATOM 2124 CB GLU A1086 46.079 -69.744 20.837 1.00 94.51 C
ANISOU 2124 CB GLU A1086 11395 5932 18584 2911 -746 -77 C
ATOM 2125 CG GLU A1086 44.616 -70.155 20.922 1.00 94.66 C
ANISOU 2125 CG GLU A1086 11460 5840 18668 2770 -900 -38 C
ATOM 2126 CD GLU A1086 44.377 -71.329 21.853 1.00103.99 C
ANISOU 2126 CD GLU A1086 12537 6923 20051 2725 -984 152 C
ATOM 2127 OE1 GLU A1086 45.337 -72.079 22.137 1.00113.99 O
ANISOU 2127 OE1 GLU A1086 13740 8150 21422 2816 -931 192 O
ATOM 2128 OE2 GLU A1086 43.221 -71.505 22.293 1.00110.60 O
ANISOU 2128 OE2 GLU A1086 13354 7726 20943 2598 -1100 264 O
ATOM 2129 N ALA A1087 46.601 -66.451 20.677 1.00 89.65 N
ANISOU 2129 N ALA A1087 10735 5759 17568 2924 -565 -116 N
ATOM 2130 CA ALA A1087 46.120 -65.103 20.959 1.00 88.30 C
ANISOU 2130 CA ALA A1087 10542 5809 17197 2826 -559 -58 C
ATOM 2131 C ALA A1087 46.184 -64.218 19.721 1.00 88.35 C
ANISOU 2131 C ALA A1087 10690 5914 16967 2840 -476 -287 C
ATOM 2132 O ALA A1087 45.320 -63.356 19.529 1.00 85.11 O
ANISOU 2132 O ALA A1087 10338 5622 16377 2728 -508 -311 O
ATOM 2133 CB ALA A1087 46.925 -64.476 22.097 1.00 86.17 C
ANISOU 2133 CB ALA A1087 10100 5755 16887 2838 -496 145 C
ATOM 2134 N GLN A1088 47.203 -64.410 18.877 1.00 87.73 N
ANISOU 2134 N GLN A1088 10661 5792 16881 2981 -365 -449 N
ATOM 2135 CA GLN A1088 47.273 -63.668 17.622 1.00 87.35 C
ANISOU 2135 CA GLN A1088 10751 5822 16615 3010 -282 -672 C
ATOM 2136 C GLN A1088 46.082 -63.987 16.729 1.00 87.85 C
ANISOU 2136 C GLN A1088 10986 5737 16655 2947 -383 -836 C
ATOM 2137 O GLN A1088 45.527 -63.094 16.077 1.00 86.68 O
ANISOU 2137 O GLN A1088 10934 5707 16294 2883 -372 -940 O
ATOM 2138 CB GLN A1088 48.580 -63.982 16.894 1.00 88.79 C
ANISOU 2138 CB GLN A1088 10953 5961 16821 3190 -146 -806 C
ATOM 2139 CG GLN A1088 49.811 -63.332 17.498 1.00 91.49 C
ANISOU 2139 CG GLN A1088 11144 6497 17120 3251 -22 -683 C
ATOM 2140 CD GLN A1088 51.092 -63.770 16.817 1.00 89.69 C
ANISOU 2140 CD GLN A1088 10925 6206 16945 3435 110 -798 C
ATOM 2141 OE1 GLN A1088 51.217 -64.916 16.380 1.00 97.44 O
ANISOU 2141 OE1 GLN A1088 11971 6963 18087 3528 91 -893 O
ATOM 2142 NE2 GLN A1088 52.052 -62.857 16.718 1.00 88.91 N
ANISOU 2142 NE2 GLN A1088 10762 6306 16715 3491 245 -787 N
ATOM 2143 N ALA A1089 45.676 -65.256 16.684 1.00 89.64 N
ANISOU 2143 N ALA A1089 11252 5703 17104 2964 -487 -860 N
ATOM 2144 CA ALA A1089 44.528 -65.630 15.868 1.00 90.29 C
ANISOU 2144 CA ALA A1089 11493 5626 17187 2902 -602 -1013 C
ATOM 2145 C ALA A1089 43.228 -65.131 16.485 1.00 88.69 C
ANISOU 2145 C ALA A1089 11266 5499 16935 2718 -719 -875 C
ATOM 2146 O ALA A1089 42.307 -64.729 15.766 1.00 92.37 O
ANISOU 2146 O ALA A1089 11856 5971 17269 2640 -773 -996 O
ATOM 2147 CB ALA A1089 44.490 -67.144 15.679 1.00 92.77 C
ANISOU 2147 CB ALA A1089 11858 5705 17688 2940 -675 -1058 C
ATOM 2148 N ALA A1090 43.136 -65.147 17.817 1.00 87.93 N
ANISOU 2148 N ALA A1090 11008 5463 16937 2653 -758 -618 N
ATOM 2149 CA ALA A1090 41.939 -64.642 18.479 1.00 86.41 C
ANISOU 2149 CA ALA A1090 10781 5359 16693 2489 -858 -467 C
ATOM 2150 C ALA A1090 41.786 -63.141 18.272 1.00 85.74 C
ANISOU 2150 C ALA A1090 10721 5545 16311 2423 -787 -495 C
ATOM 2151 O ALA A1090 40.666 -62.640 18.122 1.00 83.17 O
ANISOU 2151 O ALA A1090 10456 5266 15881 2300 -860 -499 O
ATOM 2152 CB ALA A1090 41.981 -64.978 19.969 1.00 86.19 C
ANISOU 2152 CB ALA A1090 10571 5353 16824 2456 -901 -181 C
ATOM 2153 N ALA A1091 42.902 -62.408 18.253 1.00 87.02 N
ANISOU 2153 N ALA A1091 10835 5886 16344 2503 -646 -512 N
ATOM 2154 CA ALA A1091 42.849 -60.970 18.022 1.00 91.61 C
ANISOU 2154 CA ALA A1091 11435 6720 16653 2449 -572 -542 C
ATOM 2155 C ALA A1091 42.541 -60.625 16.570 1.00 94.39 C
ANISOU 2155 C ALA A1091 11965 7054 16843 2462 -543 -795 C
ATOM 2156 O ALA A1091 42.155 -59.485 16.286 1.00 94.80 O
ANISOU 2156 O ALA A1091 12055 7287 16676 2390 -512 -827 O
ATOM 2157 CB ALA A1091 44.165 -60.318 18.447 1.00 80.82 C
ANISOU 2157 CB ALA A1091 9954 5538 15217 2532 -437 -477 C
ATOM 2158 N GLU A1092 42.699 -61.579 15.649 1.00 83.63 N
ANISOU 2158 N GLU A1092 10714 5478 15582 2555 -554 -976 N
ATOM 2159 CA GLU A1092 42.350 -61.341 14.253 1.00 84.00 C
ANISOU 2159 CA GLU A1092 10940 5498 15478 2574 -539 -1222 C
ATOM 2160 C GLU A1092 40.846 -61.301 14.032 1.00 93.77 C
ANISOU 2160 C GLU A1092 12269 6676 16684 2431 -681 -1245 C
ATOM 2161 O GLU A1092 40.392 -60.659 13.079 1.00 95.25 O
ANISOU 2161 O GLU A1092 12581 6930 16680 2404 -667 -1400 O
ATOM 2162 CB GLU A1092 42.980 -62.409 13.360 1.00 95.57 C
ANISOU 2162 CB GLU A1092 12502 6751 17062 2729 -514 -1412 C
ATOM 2163 CG GLU A1092 43.034 -62.048 11.884 1.00 89.92 C
ANISOU 2163 CG GLU A1092 11958 6052 16156 2799 -448 -1673 C
ATOM 2164 CD GLU A1092 43.977 -60.892 11.596 1.00111.38 C
ANISOU 2164 CD GLU A1092 14642 9019 18659 2863 -272 -1694 C
ATOM 2165 OE1 GLU A1092 44.875 -60.634 12.424 1.00109.39 O
ANISOU 2165 OE1 GLU A1092 14239 8876 18448 2897 -190 -1540 O
ATOM 2166 OE2 GLU A1092 43.821 -60.240 10.542 1.00123.82 O
ANISOU 2166 OE2 GLU A1092 16338 10678 20029 2880 -218 -1860 O
ATOM 2167 N GLN A1093 40.066 -61.950 14.897 1.00 91.67 N
ANISOU 2167 N GLN A1093 11937 6292 16600 2339 -815 -1084 N
ATOM 2168 CA GLN A1093 38.614 -61.873 14.811 1.00 83.27 C
ANISOU 2168 CA GLN A1093 10936 5182 15518 2193 -953 -1072 C
ATOM 2169 C GLN A1093 38.087 -60.477 15.112 1.00 83.10 C
ANISOU 2169 C GLN A1093 10886 5423 15267 2077 -924 -984 C
ATOM 2170 O GLN A1093 36.916 -60.201 14.830 1.00 80.26 O
ANISOU 2170 O GLN A1093 10598 5058 14840 1962 -1015 -1005 O
ATOM 2171 CB GLN A1093 37.975 -62.880 15.771 1.00 84.07 C
ANISOU 2171 CB GLN A1093 10950 5109 15884 2128 -1092 -888 C
ATOM 2172 CG GLN A1093 38.421 -64.320 15.561 1.00 86.56 C
ANISOU 2172 CG GLN A1093 11285 5147 16457 2234 -1136 -958 C
ATOM 2173 CD GLN A1093 37.910 -64.913 14.262 1.00 91.83 C
ANISOU 2173 CD GLN A1093 12137 5610 17144 2257 -1214 -1212 C
ATOM 2174 OE1 GLN A1093 36.956 -64.408 13.667 1.00103.50 O
ANISOU 2174 OE1 GLN A1093 13717 7122 18487 2164 -1274 -1299 O
ATOM 2175 NE2 GLN A1093 38.544 -65.992 13.815 1.00 91.39 N
ANISOU 2175 NE2 GLN A1093 12128 5362 17235 2377 -1210 -1330 N
ATOM 2176 N LEU A1094 38.919 -59.599 15.678 1.00 85.52 N
ANISOU 2176 N LEU A1094 11088 5950 15458 2104 -803 -886 N
ATOM 2177 CA LEU A1094 38.489 -58.232 15.950 1.00 77.19 C
ANISOU 2177 CA LEU A1094 10005 5142 14181 2003 -771 -812 C
ATOM 2178 C LEU A1094 38.286 -57.437 14.667 1.00 76.70 C
ANISOU 2178 C LEU A1094 10089 5163 13892 2001 -717 -1023 C
ATOM 2179 O LEU A1094 37.530 -56.459 14.661 1.00 79.16 O
ANISOU 2179 O LEU A1094 10418 5623 14035 1893 -730 -994 O
ATOM 2180 CB LEU A1094 39.509 -57.535 16.849 1.00 76.05 C
ANISOU 2180 CB LEU A1094 9713 5199 13984 2042 -663 -667 C
ATOM 2181 CG LEU A1094 39.683 -58.120 18.251 1.00 77.59 C
ANISOU 2181 CG LEU A1094 9750 5363 14368 2036 -713 -430 C
ATOM 2182 CD1 LEU A1094 40.966 -57.615 18.885 1.00 75.67 C
ANISOU 2182 CD1 LEU A1094 9380 5281 14089 2115 -597 -343 C
ATOM 2183 CD2 LEU A1094 38.489 -57.769 19.117 1.00 74.98 C
ANISOU 2183 CD2 LEU A1094 9370 5101 14018 1891 -815 -250 C
ATOM 2184 N LYS A1095 38.953 -57.832 13.579 1.00 78.12 N
ANISOU 2184 N LYS A1095 10371 5251 14061 2125 -652 -1232 N
ATOM 2185 CA LYS A1095 38.809 -57.107 12.320 1.00 78.64 C
ANISOU 2185 CA LYS A1095 10575 5398 13905 2139 -594 -1433 C
ATOM 2186 C LYS A1095 37.382 -57.189 11.794 1.00 83.85 C
ANISOU 2186 C LYS A1095 11356 5974 14531 2024 -728 -1505 C
ATOM 2187 O LYS A1095 36.835 -56.192 11.308 1.00 76.53 O
ANISOU 2187 O LYS A1095 10489 5194 13397 1954 -709 -1555 O
ATOM 2188 CB LYS A1095 39.793 -57.645 11.282 1.00 80.00 C
ANISOU 2188 CB LYS A1095 10836 5475 14085 2310 -503 -1638 C
ATOM 2189 CG LYS A1095 41.227 -57.196 11.494 1.00 89.08 C
ANISOU 2189 CG LYS A1095 11887 6767 15194 2426 -337 -1600 C
ATOM 2190 CD LYS A1095 42.082 -57.510 10.279 1.00 82.58 C
ANISOU 2190 CD LYS A1095 11169 5884 14323 2593 -232 -1818 C
ATOM 2191 CE LYS A1095 43.500 -57.000 10.459 1.00101.91 C
ANISOU 2191 CE LYS A1095 13510 8481 16730 2705 -63 -1770 C
ATOM 2192 NZ LYS A1095 44.138 -57.575 11.674 1.00105.09 N
ANISOU 2192 NZ LYS A1095 13753 8837 17338 2726 -73 -1585 N
ATOM 2193 N THR A1096 36.763 -58.368 11.882 1.00 81.44 N
ANISOU 2193 N THR A1096 11081 5429 14432 2002 -867 -1506 N
ATOM 2194 CA THR A1096 35.384 -58.508 11.425 1.00 83.65 C
ANISOU 2194 CA THR A1096 11466 5613 14704 1887 -1009 -1564 C
ATOM 2195 C THR A1096 34.431 -57.688 12.286 1.00 77.43 C
ANISOU 2195 C THR A1096 10594 4975 13848 1725 -1061 -1364 C
ATOM 2196 O THR A1096 33.512 -57.045 11.765 1.00 76.58 O
ANISOU 2196 O THR A1096 10569 4935 13593 1632 -1102 -1420 O
ATOM 2197 CB THR A1096 34.976 -59.980 11.425 1.00 88.03 C
ANISOU 2197 CB THR A1096 12053 5868 15525 1898 -1153 -1590 C
ATOM 2198 OG1 THR A1096 35.203 -60.542 12.724 1.00105.60 O
ANISOU 2198 OG1 THR A1096 14118 8044 17960 1884 -1182 -1362 O
ATOM 2199 CG2 THR A1096 35.783 -60.754 10.391 1.00100.74 C
ANISOU 2199 CG2 THR A1096 13778 7323 17177 2060 -1111 -1824 C
ATOM 2200 N THR A1097 34.635 -57.694 13.606 1.00 81.47 N
ANISOU 2200 N THR A1097 10946 5546 14463 1695 -1058 -1130 N
ATOM 2201 CA THR A1097 33.797 -56.889 14.488 1.00 74.79 C
ANISOU 2201 CA THR A1097 10016 4856 13544 1557 -1097 -933 C
ATOM 2202 C THR A1097 34.018 -55.400 14.256 1.00 82.74 C
ANISOU 2202 C THR A1097 11030 6132 14276 1537 -980 -960 C
ATOM 2203 O THR A1097 33.075 -54.606 14.371 1.00 71.41 O
ANISOU 2203 O THR A1097 9604 4813 12716 1419 -1017 -900 O
ATOM 2204 CB THR A1097 34.077 -57.242 15.949 1.00 74.58 C
ANISOU 2204 CB THR A1097 9818 4841 13678 1550 -1111 -682 C
ATOM 2205 OG1 THR A1097 34.078 -58.665 16.106 1.00 79.90 O
ANISOU 2205 OG1 THR A1097 10480 5259 14620 1591 -1201 -666 O
ATOM 2206 CG2 THR A1097 33.013 -56.642 16.855 1.00 73.02 C
ANISOU 2206 CG2 THR A1097 9546 4762 13436 1409 -1178 -477 C
ATOM 2207 N ARG A1098 35.251 -55.006 13.929 1.00 75.71 N
ANISOU 2207 N ARG A1098 10131 5341 13296 1651 -838 -1045 N
ATOM 2208 CA ARG A1098 35.537 -53.602 13.652 1.00 79.94 C
ANISOU 2208 CA ARG A1098 10668 6121 13584 1640 -723 -1075 C
ATOM 2209 C ARG A1098 34.780 -53.115 12.423 1.00 78.32 C
ANISOU 2209 C ARG A1098 10617 5934 13207 1596 -737 -1253 C
ATOM 2210 O ARG A1098 34.274 -51.987 12.402 1.00 79.38 O
ANISOU 2210 O ARG A1098 10754 6246 13160 1511 -715 -1221 O
ATOM 2211 CB ARG A1098 37.042 -53.412 13.468 1.00 71.39 C
ANISOU 2211 CB ARG A1098 9542 5112 12469 1781 -573 -1133 C
ATOM 2212 CG ARG A1098 37.439 -52.060 12.913 1.00 70.03 C
ANISOU 2212 CG ARG A1098 9389 5164 12054 1790 -447 -1202 C
ATOM 2213 CD ARG A1098 38.800 -52.139 12.255 1.00 71.01 C
ANISOU 2213 CD ARG A1098 9523 5297 12160 1947 -309 -1326 C
ATOM 2214 NE ARG A1098 38.851 -53.212 11.269 1.00 73.08 N
ANISOU 2214 NE ARG A1098 9911 5351 12504 2039 -334 -1510 N
ATOM 2215 CZ ARG A1098 39.933 -53.548 10.581 1.00 75.85 C
ANISOU 2215 CZ ARG A1098 10292 5662 12863 2192 -228 -1638 C
ATOM 2216 NH1 ARG A1098 41.078 -52.904 10.736 1.00 88.81 N
ANISOU 2216 NH1 ARG A1098 11843 7455 14444 2269 -87 -1599 N
ATOM 2217 NH2 ARG A1098 39.866 -54.556 9.716 1.00 80.22 N
ANISOU 2217 NH2 ARG A1098 10971 6018 13492 2273 -266 -1809 N
ATOM 2218 N ASN A1099 34.686 -53.956 11.392 1.00 78.29 N
ANISOU 2218 N ASN A1099 10744 5746 13258 1658 -778 -1443 N
ATOM 2219 CA ASN A1099 34.026 -53.547 10.157 1.00 82.92 C
ANISOU 2219 CA ASN A1099 11484 6345 13677 1631 -793 -1626 C
ATOM 2220 C ASN A1099 32.514 -53.469 10.337 1.00 89.76 C
ANISOU 2220 C ASN A1099 12380 7178 14547 1472 -938 -1557 C
ATOM 2221 O ASN A1099 31.891 -52.451 10.016 1.00 87.88 O
ANISOU 2221 O ASN A1099 12180 7091 14121 1390 -925 -1567 O
ATOM 2222 CB ASN A1099 34.380 -54.517 9.028 1.00 74.96 C
ANISOU 2222 CB ASN A1099 10611 5144 12726 1753 -803 -1855 C
ATOM 2223 CG ASN A1099 35.877 -54.689 8.854 1.00 89.70 C
ANISOU 2223 CG ASN A1099 12446 7031 14606 1921 -658 -1916 C
ATOM 2224 OD1 ASN A1099 36.647 -53.743 9.023 1.00 82.21 O
ANISOU 2224 OD1 ASN A1099 11425 6283 13528 1954 -521 -1868 O
ATOM 2225 ND2 ASN A1099 36.297 -55.905 8.519 1.00 77.90 N
ANISOU 2225 ND2 ASN A1099 11001 5320 13276 2028 -689 -2021 N
ATOM 2226 N ALA A1100 31.910 -54.535 10.858 1.00 80.07 N
ANISOU 2226 N ALA A1100 11128 5752 13542 1426 -1077 -1476 N
ATOM 2227 CA ALA A1100 30.459 -54.662 10.903 1.00 72.96 C
ANISOU 2227 CA ALA A1100 10265 4778 12679 1285 -1228 -1425 C
ATOM 2228 C ALA A1100 29.819 -53.959 12.093 1.00 73.75 C
ANISOU 2228 C ALA A1100 10237 5027 12758 1161 -1249 -1176 C
ATOM 2229 O ALA A1100 28.588 -53.969 12.201 1.00 86.76 O
ANISOU 2229 O ALA A1100 11901 6635 14430 1039 -1366 -1108 O
ATOM 2230 CB ALA A1100 30.067 -56.142 10.914 1.00 80.89 C
ANISOU 2230 CB ALA A1100 11295 5491 13948 1291 -1375 -1444 C
ATOM 2231 N TYR A1101 30.604 -53.352 12.984 1.00 85.38 N
ANISOU 2231 N TYR A1101 11585 6670 14187 1190 -1143 -1038 N
ATOM 2232 CA TYR A1101 30.031 -52.700 14.157 1.00 83.78 C
ANISOU 2232 CA TYR A1101 11263 6611 13958 1085 -1163 -803 C
ATOM 2233 C TYR A1101 30.746 -51.398 14.499 1.00 75.93 C
ANISOU 2233 C TYR A1101 10203 5880 12768 1104 -1023 -757 C
ATOM 2234 O TYR A1101 30.122 -50.332 14.534 1.00 79.82 O
ANISOU 2234 O TYR A1101 10700 6536 13091 1017 -1010 -715 O
ATOM 2235 CB TYR A1101 30.070 -53.641 15.365 1.00 73.53 C
ANISOU 2235 CB TYR A1101 9839 5199 12899 1086 -1231 -605 C
ATOM 2236 CG TYR A1101 29.156 -54.840 15.247 1.00 82.11 C
ANISOU 2236 CG TYR A1101 10964 6036 14199 1038 -1388 -596 C
ATOM 2237 CD1 TYR A1101 27.829 -54.767 15.649 1.00 85.84 C
ANISOU 2237 CD1 TYR A1101 11417 6498 14702 905 -1499 -460 C
ATOM 2238 CD2 TYR A1101 29.622 -56.045 14.737 1.00 75.97 C
ANISOU 2238 CD2 TYR A1101 10238 5029 13600 1126 -1425 -722 C
ATOM 2239 CE1 TYR A1101 26.989 -55.862 15.545 1.00 95.36 C
ANISOU 2239 CE1 TYR A1101 12648 7467 16118 856 -1649 -444 C
ATOM 2240 CE2 TYR A1101 28.791 -57.144 14.629 1.00 82.47 C
ANISOU 2240 CE2 TYR A1101 11093 5611 14632 1079 -1578 -716 C
ATOM 2241 CZ TYR A1101 27.476 -57.048 15.034 1.00 86.81 C
ANISOU 2241 CZ TYR A1101 11617 6152 15217 942 -1691 -574 C
ATOM 2242 OH TYR A1101 26.646 -58.141 14.927 1.00105.57 O
ANISOU 2242 OH TYR A1101 14016 8281 17816 891 -1848 -561 O
ATOM 2243 N ILE A1102 32.053 -51.476 14.755 1.00 70.00 N
ANISOU 2243 N ILE A1102 9388 5164 12047 1218 -922 -761 N
ATOM 2244 CA ILE A1102 32.782 -50.317 15.259 1.00 65.06 C
ANISOU 2244 CA ILE A1102 8674 4773 11271 1234 -804 -690 C
ATOM 2245 C ILE A1102 32.883 -49.233 14.193 1.00 73.28 C
ANISOU 2245 C ILE A1102 9807 5955 12081 1237 -712 -849 C
ATOM 2246 O ILE A1102 32.810 -48.036 14.498 1.00 62.51 O
ANISOU 2246 O ILE A1102 8400 4793 10557 1185 -659 -783 O
ATOM 2247 CB ILE A1102 34.169 -50.746 15.771 1.00 67.99 C
ANISOU 2247 CB ILE A1102 8949 5132 11750 1356 -726 -654 C
ATOM 2248 CG1 ILE A1102 34.023 -51.835 16.834 1.00 70.68 C
ANISOU 2248 CG1 ILE A1102 9197 5333 12323 1353 -819 -487 C
ATOM 2249 CG2 ILE A1102 34.927 -49.551 16.335 1.00 73.35 C
ANISOU 2249 CG2 ILE A1102 9531 6048 12289 1370 -618 -576 C
ATOM 2250 CD1 ILE A1102 33.144 -51.434 18.001 1.00 65.39 C
ANISOU 2250 CD1 ILE A1102 8436 4761 11648 1242 -890 -265 C
ATOM 2251 N GLN A1103 33.049 -49.626 12.928 1.00 68.84 N
ANISOU 2251 N GLN A1103 9372 5289 11494 1302 -693 -1059 N
ATOM 2252 CA GLN A1103 33.169 -48.632 11.867 1.00 66.31 C
ANISOU 2252 CA GLN A1103 9138 5103 10953 1315 -600 -1208 C
ATOM 2253 C GLN A1103 31.864 -47.873 11.659 1.00 67.01 C
ANISOU 2253 C GLN A1103 9283 5274 10906 1179 -663 -1190 C
ATOM 2254 O GLN A1103 31.886 -46.710 11.239 1.00 62.29 O
ANISOU 2254 O GLN A1103 8704 4852 10111 1158 -582 -1228 O
ATOM 2255 CB GLN A1103 33.617 -49.301 10.566 1.00 68.21 C
ANISOU 2255 CB GLN A1103 9508 5212 11197 1427 -570 -1436 C
ATOM 2256 CG GLN A1103 34.094 -48.327 9.496 1.00 75.13 C
ANISOU 2256 CG GLN A1103 10454 6238 11854 1482 -440 -1583 C
ATOM 2257 CD GLN A1103 34.647 -49.029 8.268 1.00105.07 C
ANISOU 2257 CD GLN A1103 14368 9906 15647 1616 -400 -1802 C
ATOM 2258 OE1 GLN A1103 34.404 -50.218 8.054 1.00107.97 O
ANISOU 2258 OE1 GLN A1103 14800 10062 16163 1647 -494 -1873 O
ATOM 2259 NE2 GLN A1103 35.400 -48.293 7.457 1.00109.79 N
ANISOU 2259 NE2 GLN A1103 14997 10636 16080 1702 -258 -1908 N
ATOM 2260 N LYS A1104 30.724 -48.501 11.954 1.00 71.82 N
ANISOU 2260 N LYS A1104 9911 5756 11622 1086 -806 -1123 N
ATOM 2261 CA LYS A1104 29.448 -47.803 11.830 1.00 62.72 C
ANISOU 2261 CA LYS A1104 8799 4678 10352 954 -870 -1087 C
ATOM 2262 C LYS A1104 29.298 -46.737 12.908 1.00 71.47 C
ANISOU 2262 C LYS A1104 9790 5990 11374 881 -834 -894 C
ATOM 2263 O LYS A1104 28.764 -45.653 12.647 1.00 68.53 O
ANISOU 2263 O LYS A1104 9444 5769 10824 810 -807 -897 O
ATOM 2264 CB LYS A1104 28.291 -48.799 11.898 1.00 63.73 C
ANISOU 2264 CB LYS A1104 8968 4609 10639 876 -1035 -1053 C
ATOM 2265 CG LYS A1104 28.354 -49.895 10.847 1.00 84.95 C
ANISOU 2265 CG LYS A1104 11778 7077 13422 943 -1092 -1250 C
ATOM 2266 CD LYS A1104 28.293 -49.320 9.442 1.00 81.46 C
ANISOU 2266 CD LYS A1104 11480 6692 12781 968 -1043 -1466 C
ATOM 2267 CE LYS A1104 26.976 -48.606 9.193 1.00 80.75 C
ANISOU 2267 CE LYS A1104 11437 6676 12567 831 -1113 -1440 C
ATOM 2268 NZ LYS A1104 26.897 -48.066 7.808 1.00 94.06 N
ANISOU 2268 NZ LYS A1104 13262 8419 14056 858 -1069 -1647 N
ATOM 2269 N TYR A1105 29.763 -47.025 14.126 1.00 76.16 N
ANISOU 2269 N TYR A1105 10255 6592 12090 901 -835 -727 N
ATOM 2270 CA TYR A1105 29.680 -46.041 15.201 1.00 63.37 C
ANISOU 2270 CA TYR A1105 8525 5166 10388 846 -806 -549 C
ATOM 2271 C TYR A1105 30.644 -44.885 14.969 1.00 57.80 C
ANISOU 2271 C TYR A1105 7796 4652 9512 897 -666 -607 C
ATOM 2272 O TYR A1105 30.340 -43.739 15.325 1.00 56.19 O
ANISOU 2272 O TYR A1105 7557 4628 9166 834 -636 -534 O
ATOM 2273 CB TYR A1105 29.960 -46.709 16.547 1.00 65.66 C
ANISOU 2273 CB TYR A1105 8685 5412 10851 866 -847 -359 C
ATOM 2274 CG TYR A1105 30.161 -45.737 17.689 1.00 83.29 C
ANISOU 2274 CG TYR A1105 10800 7849 12997 842 -804 -191 C
ATOM 2275 CD1 TYR A1105 29.076 -45.169 18.342 1.00 89.41 C
ANISOU 2275 CD1 TYR A1105 11546 8717 13708 736 -862 -48 C
ATOM 2276 CD2 TYR A1105 31.438 -45.393 18.120 1.00 94.32 C
ANISOU 2276 CD2 TYR A1105 12114 9344 14380 928 -711 -177 C
ATOM 2277 CE1 TYR A1105 29.254 -44.281 19.389 1.00 77.92 C
ANISOU 2277 CE1 TYR A1105 9991 7448 12167 723 -828 97 C
ATOM 2278 CE2 TYR A1105 31.626 -44.506 19.166 1.00 83.56 C
ANISOU 2278 CE2 TYR A1105 10648 8163 12938 909 -684 -33 C
ATOM 2279 CZ TYR A1105 30.530 -43.954 19.796 1.00 85.70 C
ANISOU 2279 CZ TYR A1105 10900 8524 13138 809 -743 99 C
ATOM 2280 OH TYR A1105 30.711 -43.072 20.837 1.00 84.69 O
ANISOU 2280 OH TYR A1105 10677 8577 12926 798 -720 233 O
ATOM 2281 N LEU A1106 31.813 -45.167 14.383 1.00 58.73 N
ANISOU 2281 N LEU A1106 7930 4735 9651 1015 -579 -734 N
ATOM 2282 CA LEU A1106 32.802 -44.119 14.149 1.00 58.56 C
ANISOU 2282 CA LEU A1106 7875 4886 9490 1070 -444 -781 C
ATOM 2283 C LEU A1106 32.241 -43.018 13.260 1.00 64.61 C
ANISOU 2283 C LEU A1106 8724 5776 10048 1011 -403 -873 C
ATOM 2284 O LEU A1106 32.540 -41.834 13.455 1.00 68.53 O
ANISOU 2284 O LEU A1106 9168 6456 10413 994 -327 -834 O
ATOM 2285 CB LEU A1106 34.063 -44.719 13.518 1.00 66.98 C
ANISOU 2285 CB LEU A1106 8956 5872 10622 1211 -359 -909 C
ATOM 2286 CG LEU A1106 34.979 -43.766 12.736 1.00 81.37 C
ANISOU 2286 CG LEU A1106 10789 7836 12292 1280 -214 -1018 C
ATOM 2287 CD1 LEU A1106 35.718 -42.812 13.667 1.00 57.66 C
ANISOU 2287 CD1 LEU A1106 7648 5011 9250 1280 -147 -888 C
ATOM 2288 CD2 LEU A1106 35.959 -44.535 11.854 1.00 68.79 C
ANISOU 2288 CD2 LEU A1106 9247 6131 10760 1421 -143 -1170 C
ATOM 2289 N GLU A 219 31.417 -43.388 12.282 1.00 59.82 N
ANISOU 2289 N GLU A 219 8246 5070 9414 980 -458 -994 N
ATOM 2290 CA GLU A 219 30.944 -42.447 11.281 1.00 78.53 C
ANISOU 2290 CA GLU A 219 10706 7544 11587 939 -415 -1101 C
ATOM 2291 C GLU A 219 29.530 -41.941 11.539 1.00 74.55 C
ANISOU 2291 C GLU A 219 10222 7090 11015 797 -505 -1014 C
ATOM 2292 O GLU A 219 29.127 -40.947 10.926 1.00 63.37 O
ANISOU 2292 O GLU A 219 8855 5797 9426 751 -464 -1064 O
ATOM 2293 CB GLU A 219 31.040 -43.084 9.888 1.00 75.11 C
ANISOU 2293 CB GLU A 219 10411 6988 11138 1012 -406 -1312 C
ATOM 2294 CG GLU A 219 32.483 -43.241 9.413 1.00 90.32 C
ANISOU 2294 CG GLU A 219 12327 8918 13073 1162 -280 -1414 C
ATOM 2295 CD GLU A 219 32.621 -44.173 8.227 1.00102.75 C
ANISOU 2295 CD GLU A 219 14033 10333 14673 1254 -287 -1611 C
ATOM 2296 OE1 GLU A 219 31.713 -45.002 8.015 1.00103.36 O
ANISOU 2296 OE1 GLU A 219 14192 10253 14829 1208 -414 -1652 O
ATOM 2297 OE2 GLU A 219 33.639 -44.077 7.508 1.00106.20 O
ANISOU 2297 OE2 GLU A 219 14492 10802 15055 1376 -168 -1725 O
ATOM 2298 N ARG A 220 28.772 -42.580 12.432 1.00 57.73 N
ANISOU 2298 N ARG A 220 8050 4870 9016 730 -621 -876 N
ATOM 2299 CA ARG A 220 27.510 -41.985 12.857 1.00 54.50 C
ANISOU 2299 CA ARG A 220 7633 4534 8540 600 -691 -761 C
ATOM 2300 C ARG A 220 27.737 -40.934 13.934 1.00 52.84 C
ANISOU 2300 C ARG A 220 7306 4516 8255 572 -639 -604 C
ATOM 2301 O ARG A 220 27.098 -39.876 13.918 1.00 51.48 O
ANISOU 2301 O ARG A 220 7141 4484 7937 495 -626 -569 O
ATOM 2302 CB ARG A 220 26.546 -43.062 13.355 1.00 55.32 C
ANISOU 2302 CB ARG A 220 7736 4470 8815 540 -836 -665 C
ATOM 2303 CG ARG A 220 26.088 -44.051 12.288 1.00 74.33 C
ANISOU 2303 CG ARG A 220 10266 6679 11296 546 -916 -819 C
ATOM 2304 CD ARG A 220 25.797 -43.366 10.959 1.00 84.28 C
ANISOU 2304 CD ARG A 220 11650 8000 12370 533 -877 -993 C
ATOM 2305 NE ARG A 220 26.916 -43.484 10.031 1.00 99.54 N
ANISOU 2305 NE ARG A 220 13642 9919 14258 658 -778 -1177 N
ATOM 2306 CZ ARG A 220 26.971 -42.900 8.842 1.00 98.84 C
ANISOU 2306 CZ ARG A 220 13654 9898 14002 682 -715 -1338 C
ATOM 2307 NH1 ARG A 220 25.982 -42.142 8.397 1.00 94.69 N
ANISOU 2307 NH1 ARG A 220 13184 9457 13338 587 -742 -1346 N
ATOM 2308 NH2 ARG A 220 28.046 -43.081 8.079 1.00 98.40 N
ANISOU 2308 NH2 ARG A 220 13641 9828 13918 809 -620 -1488 N
ATOM 2309 N ALA A 221 28.646 -41.207 14.874 1.00 63.24 N
ANISOU 2309 N ALA A 221 8515 5841 9670 637 -612 -512 N
ATOM 2310 CA ALA A 221 29.015 -40.201 15.863 1.00 51.58 C
ANISOU 2310 CA ALA A 221 6931 4548 8119 626 -562 -384 C
ATOM 2311 C ALA A 221 29.769 -39.044 15.222 1.00 55.04 C
ANISOU 2311 C ALA A 221 7378 5138 8397 660 -439 -486 C
ATOM 2312 O ALA A 221 29.663 -37.902 15.685 1.00 51.78 O
ANISOU 2312 O ALA A 221 6916 4892 7867 615 -407 -415 O
ATOM 2313 CB ALA A 221 29.854 -40.835 16.972 1.00 52.11 C
ANISOU 2313 CB ALA A 221 6884 4582 8334 695 -568 -270 C
ATOM 2314 N ARG A 222 30.535 -39.318 14.164 1.00 62.77 N
ANISOU 2314 N ARG A 222 8416 6061 9372 743 -368 -650 N
ATOM 2315 CA ARG A 222 31.202 -38.246 13.433 1.00 55.20 C
ANISOU 2315 CA ARG A 222 7470 5240 8265 778 -247 -746 C
ATOM 2316 C ARG A 222 30.200 -37.420 12.639 1.00 50.28 C
ANISOU 2316 C ARG A 222 6935 4692 7477 692 -249 -803 C
ATOM 2317 O ARG A 222 30.340 -36.197 12.532 1.00 60.12 O
ANISOU 2317 O ARG A 222 8157 6099 8587 669 -176 -798 O
ATOM 2318 CB ARG A 222 32.270 -38.829 12.508 1.00 52.55 C
ANISOU 2318 CB ARG A 222 7174 4823 7971 901 -168 -897 C
ATOM 2319 CG ARG A 222 33.147 -37.795 11.828 1.00 59.33 C
ANISOU 2319 CG ARG A 222 8021 5822 8701 955 -30 -976 C
ATOM 2320 CD ARG A 222 34.205 -38.463 10.964 1.00 74.89 C
ANISOU 2320 CD ARG A 222 10026 7708 10720 1089 51 -1112 C
ATOM 2321 NE ARG A 222 33.626 -39.141 9.811 1.00 92.06 N
ANISOU 2321 NE ARG A 222 12347 9763 12871 1105 21 -1263 N
ATOM 2322 CZ ARG A 222 34.304 -39.931 8.989 1.00112.21 C
ANISOU 2322 CZ ARG A 222 14958 12208 15468 1221 67 -1397 C
ATOM 2323 NH1 ARG A 222 35.589 -40.185 9.177 1.00105.07 N
ANISOU 2323 NH1 ARG A 222 13979 11298 14644 1333 150 -1394 N
ATOM 2324 NH2 ARG A 222 33.678 -40.479 7.951 1.00100.51 N
ANISOU 2324 NH2 ARG A 222 13616 10623 13949 1230 26 -1539 N
ATOM 2325 N SER A 223 29.182 -38.073 12.073 1.00 50.91 N
ANISOU 2325 N SER A 223 7116 4653 7574 644 -335 -856 N
ATOM 2326 CA SER A 223 28.180 -37.348 11.301 1.00 50.19 C
ANISOU 2326 CA SER A 223 7111 4626 7332 561 -345 -909 C
ATOM 2327 C SER A 223 27.334 -36.456 12.199 1.00 53.43 C
ANISOU 2327 C SER A 223 7462 5162 7676 452 -382 -751 C
ATOM 2328 O SER A 223 26.980 -35.335 11.814 1.00 47.46 O
ANISOU 2328 O SER A 223 6726 4541 6764 402 -336 -766 O
ATOM 2329 CB SER A 223 27.299 -38.333 10.533 1.00 51.40 C
ANISOU 2329 CB SER A 223 7383 4611 7536 535 -443 -1000 C
ATOM 2330 OG SER A 223 26.367 -37.654 9.710 1.00 66.21 O
ANISOU 2330 OG SER A 223 9346 6549 9263 461 -454 -1059 O
ATOM 2331 N THR A 224 27.007 -36.932 13.402 1.00 48.45 N
ANISOU 2331 N THR A 224 6757 4492 7161 420 -463 -596 N
ATOM 2332 CA THR A 224 26.229 -36.117 14.330 1.00 47.01 C
ANISOU 2332 CA THR A 224 6515 4432 6915 331 -496 -440 C
ATOM 2333 C THR A 224 27.021 -34.898 14.791 1.00 45.81 C
ANISOU 2333 C THR A 224 6282 4462 6661 354 -400 -403 C
ATOM 2334 O THR A 224 26.483 -33.786 14.845 1.00 44.53 O
ANISOU 2334 O THR A 224 6117 4435 6365 288 -382 -366 O
ATOM 2335 CB THR A 224 25.788 -36.964 15.526 1.00 47.35 C
ANISOU 2335 CB THR A 224 6491 4393 7107 309 -596 -276 C
ATOM 2336 OG1 THR A 224 24.992 -38.064 15.066 1.00 48.51 O
ANISOU 2336 OG1 THR A 224 6711 4362 7359 278 -693 -306 O
ATOM 2337 CG2 THR A 224 24.972 -36.132 16.503 1.00 45.96 C
ANISOU 2337 CG2 THR A 224 6256 4349 6856 229 -626 -110 C
ATOM 2338 N LEU A 225 28.304 -35.085 15.114 1.00 46.27 N
ANISOU 2338 N LEU A 225 6270 4522 6787 448 -343 -414 N
ATOM 2339 CA LEU A 225 29.134 -33.963 15.540 1.00 45.28 C
ANISOU 2339 CA LEU A 225 6062 4559 6585 473 -261 -384 C
ATOM 2340 C LEU A 225 29.294 -32.934 14.428 1.00 44.75 C
ANISOU 2340 C LEU A 225 6046 4588 6367 468 -166 -504 C
ATOM 2341 O LEU A 225 29.321 -31.725 14.691 1.00 43.53 O
ANISOU 2341 O LEU A 225 5849 4584 6108 434 -125 -463 O
ATOM 2342 CB LEU A 225 30.501 -34.467 16.002 1.00 46.08 C
ANISOU 2342 CB LEU A 225 6080 4627 6802 578 -222 -379 C
ATOM 2343 CG LEU A 225 30.544 -35.066 17.406 1.00 60.21 C
ANISOU 2343 CG LEU A 225 7779 6387 8713 586 -297 -224 C
ATOM 2344 CD1 LEU A 225 31.926 -35.622 17.711 1.00 47.17 C
ANISOU 2344 CD1 LEU A 225 6051 4691 7179 694 -255 -233 C
ATOM 2345 CD2 LEU A 225 30.146 -34.018 18.435 1.00 44.82 C
ANISOU 2345 CD2 LEU A 225 5761 4594 6674 528 -319 -93 C
ATOM 2346 N GLN A 226 29.408 -33.391 13.179 1.00 45.70 N
ANISOU 2346 N GLN A 226 6260 4628 6477 506 -131 -652 N
ATOM 2347 CA GLN A 226 29.523 -32.456 12.065 1.00 45.31 C
ANISOU 2347 CA GLN A 226 6263 4673 6281 507 -39 -761 C
ATOM 2348 C GLN A 226 28.226 -31.689 11.839 1.00 44.41 C
ANISOU 2348 C GLN A 226 6204 4632 6038 395 -76 -735 C
ATOM 2349 O GLN A 226 28.260 -30.535 11.396 1.00 48.81 O
ANISOU 2349 O GLN A 226 6760 5320 6466 374 -3 -760 O
ATOM 2350 CB GLN A 226 29.939 -33.199 10.796 1.00 46.76 C
ANISOU 2350 CB GLN A 226 6538 4751 6476 588 5 -924 C
ATOM 2351 CG GLN A 226 31.386 -33.664 10.812 1.00 58.79 C
ANISOU 2351 CG GLN A 226 8005 6239 8095 712 80 -964 C
ATOM 2352 CD GLN A 226 31.740 -34.526 9.616 1.00 79.68 C
ANISOU 2352 CD GLN A 226 10749 8768 10758 802 115 -1125 C
ATOM 2353 OE1 GLN A 226 30.862 -35.004 8.897 1.00 86.88 O
ANISOU 2353 OE1 GLN A 226 11774 9596 11638 770 56 -1204 O
ATOM 2354 NE2 GLN A 226 33.035 -34.729 9.397 1.00 61.34 N
ANISOU 2354 NE2 GLN A 226 8382 6438 8486 918 208 -1174 N
ATOM 2355 N LYS A 227 27.079 -32.305 12.135 1.00 44.30 N
ANISOU 2355 N LYS A 227 6232 4535 6066 324 -187 -678 N
ATOM 2356 CA LYS A 227 25.818 -31.577 12.061 1.00 43.24 C
ANISOU 2356 CA LYS A 227 6136 4472 5820 215 -228 -631 C
ATOM 2357 C LYS A 227 25.729 -30.505 13.138 1.00 41.77 C
ANISOU 2357 C LYS A 227 5856 4435 5580 170 -217 -494 C
ATOM 2358 O LYS A 227 25.143 -29.443 12.906 1.00 47.13 O
ANISOU 2358 O LYS A 227 6550 5227 6128 106 -193 -482 O
ATOM 2359 CB LYS A 227 24.637 -32.540 12.178 1.00 43.79 C
ANISOU 2359 CB LYS A 227 6261 4411 5967 151 -353 -588 C
ATOM 2360 CG LYS A 227 24.453 -33.454 10.983 1.00 45.18 C
ANISOU 2360 CG LYS A 227 6552 4444 6172 176 -382 -737 C
ATOM 2361 CD LYS A 227 23.203 -34.306 11.138 1.00 66.12 C
ANISOU 2361 CD LYS A 227 9248 6968 8906 99 -518 -683 C
ATOM 2362 CE LYS A 227 23.252 -35.132 12.416 1.00 71.19 C
ANISOU 2362 CE LYS A 227 9803 7529 9716 105 -589 -538 C
ATOM 2363 NZ LYS A 227 22.036 -35.976 12.593 1.00 87.97 N
ANISOU 2363 NZ LYS A 227 11960 9525 11940 30 -722 -469 N
ATOM 2364 N GLU A 228 26.296 -30.763 14.319 1.00 46.03 N
ANISOU 2364 N GLU A 228 6299 4976 6215 206 -238 -391 N
ATOM 2365 CA GLU A 228 26.293 -29.750 15.368 1.00 44.27 C
ANISOU 2365 CA GLU A 228 5989 4895 5937 176 -232 -272 C
ATOM 2366 C GLU A 228 27.219 -28.590 15.028 1.00 39.90 C
ANISOU 2366 C GLU A 228 5397 4468 5296 210 -125 -332 C
ATOM 2367 O GLU A 228 26.929 -27.443 15.388 1.00 45.65 O
ANISOU 2367 O GLU A 228 6093 5326 5926 162 -110 -278 O
ATOM 2368 CB GLU A 228 26.681 -30.374 16.709 1.00 40.80 C
ANISOU 2368 CB GLU A 228 5460 4425 5619 215 -286 -149 C
ATOM 2369 CG GLU A 228 25.520 -31.033 17.440 1.00 40.86 C
ANISOU 2369 CG GLU A 228 5473 4371 5681 157 -394 -21 C
ATOM 2370 CD GLU A 228 25.943 -31.688 18.742 1.00 54.50 C
ANISOU 2370 CD GLU A 228 7109 6072 7528 205 -443 105 C
ATOM 2371 OE1 GLU A 228 26.745 -32.644 18.695 1.00 57.89 O
ANISOU 2371 OE1 GLU A 228 7520 6393 8082 276 -441 67 O
ATOM 2372 OE2 GLU A 228 25.478 -31.243 19.813 1.00 41.06 O
ANISOU 2372 OE2 GLU A 228 5351 4458 5791 177 -481 242 O
ATOM 2373 N VAL A 229 28.329 -28.863 14.341 1.00 40.75 N
ANISOU 2373 N VAL A 229 5502 4538 5442 293 -50 -438 N
ATOM 2374 CA VAL A 229 29.213 -27.788 13.899 1.00 40.32 C
ANISOU 2374 CA VAL A 229 5407 4597 5315 326 56 -493 C
ATOM 2375 C VAL A 229 28.519 -26.933 12.848 1.00 43.92 C
ANISOU 2375 C VAL A 229 5939 5122 5626 269 101 -560 C
ATOM 2376 O VAL A 229 28.539 -25.699 12.914 1.00 44.12 O
ANISOU 2376 O VAL A 229 5926 5276 5561 236 146 -535 O
ATOM 2377 CB VAL A 229 30.537 -28.368 13.368 1.00 41.52 C
ANISOU 2377 CB VAL A 229 5540 4687 5549 437 130 -584 C
ATOM 2378 CG1 VAL A 229 31.436 -27.260 12.847 1.00 41.18 C
ANISOU 2378 CG1 VAL A 229 5449 4759 5439 471 244 -631 C
ATOM 2379 CG2 VAL A 229 31.237 -29.159 14.452 1.00 42.10 C
ANISOU 2379 CG2 VAL A 229 5530 4699 5766 492 86 -509 C
ATOM 2380 N HIS A 230 27.888 -27.582 11.866 1.00 45.17 N
ANISOU 2380 N HIS A 230 6205 5194 5762 258 84 -645 N
ATOM 2381 CA HIS A 230 27.202 -26.851 10.805 1.00 39.94 C
ANISOU 2381 CA HIS A 230 5621 4593 4960 207 123 -712 C
ATOM 2382 C HIS A 230 26.040 -26.034 11.359 1.00 39.30 C
ANISOU 2382 C HIS A 230 5537 4599 4799 99 69 -609 C
ATOM 2383 O HIS A 230 25.823 -24.889 10.943 1.00 37.73 O
ANISOU 2383 O HIS A 230 5340 4514 4483 60 125 -618 O
ATOM 2384 CB HIS A 230 26.716 -27.832 9.737 1.00 41.08 C
ANISOU 2384 CB HIS A 230 5886 4617 5106 220 94 -823 C
ATOM 2385 CG HIS A 230 26.221 -27.175 8.487 1.00 69.57 C
ANISOU 2385 CG HIS A 230 9578 8286 8568 192 145 -913 C
ATOM 2386 ND1 HIS A 230 24.975 -26.592 8.394 1.00 74.24 N
ANISOU 2386 ND1 HIS A 230 10212 8930 9065 89 98 -870 N
ATOM 2387 CD2 HIS A 230 26.803 -27.015 7.274 1.00 71.31 C
ANISOU 2387 CD2 HIS A 230 9847 8528 8721 261 240 -1038 C
ATOM 2388 CE1 HIS A 230 24.812 -26.098 7.180 1.00 71.06 C
ANISOU 2388 CE1 HIS A 230 9880 8578 8542 91 160 -966 C
ATOM 2389 NE2 HIS A 230 25.907 -26.341 6.481 1.00 74.74 N
ANISOU 2389 NE2 HIS A 230 10351 9029 9018 196 248 -1069 N
ATOM 2390 N ALA A 231 25.286 -26.601 12.305 1.00 38.46 N
ANISOU 2390 N ALA A 231 5420 4438 4755 52 -35 -505 N
ATOM 2391 CA ALA A 231 24.161 -25.874 12.887 1.00 37.27 C
ANISOU 2391 CA ALA A 231 5263 4368 4531 -42 -84 -398 C
ATOM 2392 C ALA A 231 24.636 -24.710 13.749 1.00 39.69 C
ANISOU 2392 C ALA A 231 5474 4813 4795 -42 -45 -322 C
ATOM 2393 O ALA A 231 24.032 -23.632 13.732 1.00 35.14 O
ANISOU 2393 O ALA A 231 4899 4342 4110 -103 -29 -289 O
ATOM 2394 CB ALA A 231 23.285 -26.824 13.703 1.00 37.55 C
ANISOU 2394 CB ALA A 231 5302 4310 4653 -81 -200 -294 C
ATOM 2395 N ALA A 232 25.712 -24.906 14.515 1.00 36.49 N
ANISOU 2395 N ALA A 232 4983 4404 4476 27 -34 -295 N
ATOM 2396 CA ALA A 232 26.226 -23.822 15.343 1.00 35.60 C
ANISOU 2396 CA ALA A 232 4779 4416 4332 32 -8 -233 C
ATOM 2397 C ALA A 232 26.794 -22.692 14.496 1.00 43.46 C
ANISOU 2397 C ALA A 232 5765 5503 5245 39 95 -313 C
ATOM 2398 O ALA A 232 26.714 -21.525 14.893 1.00 34.22 O
ANISOU 2398 O ALA A 232 4550 4446 4006 5 110 -269 O
ATOM 2399 CB ALA A 232 27.287 -24.349 16.309 1.00 36.56 C
ANISOU 2399 CB ALA A 232 4812 4508 4572 108 -26 -190 C
ATOM 2400 N LYS A 233 27.369 -23.013 13.335 1.00 36.78 N
ANISOU 2400 N LYS A 233 4958 4610 4404 87 166 -428 N
ATOM 2401 CA LYS A 233 27.837 -21.963 12.436 1.00 35.71 C
ANISOU 2401 CA LYS A 233 4816 4565 4189 94 270 -495 C
ATOM 2402 C LYS A 233 26.672 -21.146 11.896 1.00 34.83 C
ANISOU 2402 C LYS A 233 4767 4522 3944 7 272 -492 C
ATOM 2403 O LYS A 233 26.771 -19.921 11.767 1.00 34.05 O
ANISOU 2403 O LYS A 233 4631 4532 3774 -18 327 -482 O
ATOM 2404 CB LYS A 233 28.644 -22.567 11.287 1.00 41.69 C
ANISOU 2404 CB LYS A 233 5608 5258 4972 175 349 -614 C
ATOM 2405 CG LYS A 233 30.015 -23.086 11.687 1.00 37.75 C
ANISOU 2405 CG LYS A 233 5028 4717 4596 271 378 -621 C
ATOM 2406 CD LYS A 233 30.754 -23.649 10.484 1.00 53.63 C
ANISOU 2406 CD LYS A 233 7082 6672 6622 358 464 -739 C
ATOM 2407 CE LYS A 233 32.138 -24.153 10.865 1.00 46.32 C
ANISOU 2407 CE LYS A 233 6070 5705 5823 457 499 -740 C
ATOM 2408 NZ LYS A 233 32.885 -24.655 9.679 1.00 55.65 N
ANISOU 2408 NZ LYS A 233 7292 6841 7013 553 594 -852 N
ATOM 2409 N SER A 234 25.558 -21.806 11.575 1.00 34.99 N
ANISOU 2409 N SER A 234 4879 4476 3938 -42 210 -496 N
ATOM 2410 CA SER A 234 24.386 -21.083 11.098 1.00 34.18 C
ANISOU 2410 CA SER A 234 4835 4437 3715 -128 204 -484 C
ATOM 2411 C SER A 234 23.865 -20.125 12.162 1.00 35.42 C
ANISOU 2411 C SER A 234 4935 4691 3834 -189 169 -367 C
ATOM 2412 O SER A 234 23.510 -18.980 11.858 1.00 32.09 O
ANISOU 2412 O SER A 234 4511 4369 3313 -235 212 -359 O
ATOM 2413 CB SER A 234 23.300 -22.073 10.677 1.00 34.71 C
ANISOU 2413 CB SER A 234 5002 4402 3782 -170 126 -501 C
ATOM 2414 OG SER A 234 23.791 -22.969 9.696 1.00 35.97 O
ANISOU 2414 OG SER A 234 5222 4468 3975 -106 152 -620 O
ATOM 2415 N LEU A 235 23.830 -20.571 13.420 1.00 32.86 N
ANISOU 2415 N LEU A 235 4562 4340 3584 -183 94 -274 N
ATOM 2416 CA LEU A 235 23.375 -19.708 14.505 1.00 31.81 C
ANISOU 2416 CA LEU A 235 4376 4300 3410 -225 58 -164 C
ATOM 2417 C LEU A 235 24.393 -18.622 14.827 1.00 31.37 C
ANISOU 2417 C LEU A 235 4233 4339 3346 -191 118 -172 C
ATOM 2418 O LEU A 235 24.021 -17.556 15.331 1.00 41.79 O
ANISOU 2418 O LEU A 235 5524 5756 4599 -230 113 -116 O
ATOM 2419 CB LEU A 235 23.078 -20.548 15.747 1.00 38.15 C
ANISOU 2419 CB LEU A 235 5153 5052 4292 -216 -37 -60 C
ATOM 2420 CG LEU A 235 21.976 -21.594 15.565 1.00 38.76 C
ANISOU 2420 CG LEU A 235 5303 5031 4394 -258 -109 -28 C
ATOM 2421 CD1 LEU A 235 21.971 -22.584 16.717 1.00 32.96 C
ANISOU 2421 CD1 LEU A 235 4528 4229 3766 -228 -190 70 C
ATOM 2422 CD2 LEU A 235 20.622 -20.917 15.426 1.00 36.24 C
ANISOU 2422 CD2 LEU A 235 5029 4773 3968 -348 -130 28 C
ATOM 2423 N ALA A 236 25.675 -18.870 14.549 1.00 37.88 N
ANISOU 2423 N ALA A 236 5015 5135 4244 -117 171 -238 N
ATOM 2424 CA ALA A 236 26.683 -17.835 14.747 1.00 32.13 C
ANISOU 2424 CA ALA A 236 4198 4490 3522 -87 227 -247 C
ATOM 2425 C ALA A 236 26.557 -16.728 13.710 1.00 31.31 C
ANISOU 2425 C ALA A 236 4111 4462 3324 -121 313 -298 C
ATOM 2426 O ALA A 236 26.938 -15.584 13.978 1.00 31.84 O
ANISOU 2426 O ALA A 236 4111 4614 3372 -130 342 -279 O
ATOM 2427 CB ALA A 236 28.084 -18.446 14.705 1.00 32.79 C
ANISOU 2427 CB ALA A 236 4223 4518 3718 4 263 -294 C
ATOM 2428 N ILE A 237 26.034 -17.048 12.525 1.00 32.44 N
ANISOU 2428 N ILE A 237 4341 4574 3411 -139 350 -362 N
ATOM 2429 CA ILE A 237 25.821 -16.024 11.508 1.00 33.20 C
ANISOU 2429 CA ILE A 237 4457 4747 3409 -172 431 -402 C
ATOM 2430 C ILE A 237 24.745 -15.045 11.957 1.00 30.00 C
ANISOU 2430 C ILE A 237 4059 4423 2916 -257 395 -328 C
ATOM 2431 O ILE A 237 24.855 -13.833 11.732 1.00 30.62 O
ANISOU 2431 O ILE A 237 4100 4590 2944 -280 450 -323 O
ATOM 2432 CB ILE A 237 25.469 -16.677 10.159 1.00 35.20 C
ANISOU 2432 CB ILE A 237 4811 4949 3615 -164 470 -490 C
ATOM 2433 CG1 ILE A 237 26.677 -17.431 9.602 1.00 39.55 C
ANISOU 2433 CG1 ILE A 237 5348 5437 4242 -66 529 -572 C
ATOM 2434 CG2 ILE A 237 24.983 -15.636 9.161 1.00 34.10 C
ANISOU 2434 CG2 ILE A 237 4702 4896 3356 -209 540 -514 C
ATOM 2435 CD1 ILE A 237 26.417 -18.086 8.266 1.00 46.28 C
ANISOU 2435 CD1 ILE A 237 6303 6239 5042 -42 566 -671 C
ATOM 2436 N ILE A 238 23.694 -15.550 12.606 1.00 29.70 N
ANISOU 2436 N ILE A 238 4065 4355 2864 -303 305 -263 N
ATOM 2437 CA ILE A 238 22.618 -14.683 13.079 1.00 28.64 C
ANISOU 2437 CA ILE A 238 3939 4296 2646 -378 270 -185 C
ATOM 2438 C ILE A 238 23.142 -13.694 14.111 1.00 32.87 C
ANISOU 2438 C ILE A 238 4384 4910 3197 -366 264 -133 C
ATOM 2439 O ILE A 238 22.747 -12.522 14.128 1.00 34.15 O
ANISOU 2439 O ILE A 238 4532 5157 3287 -409 285 -107 O
ATOM 2440 CB ILE A 238 21.463 -15.533 13.638 1.00 33.80 C
ANISOU 2440 CB ILE A 238 4648 4896 3300 -418 174 -112 C
ATOM 2441 CG1 ILE A 238 20.854 -16.381 12.523 1.00 31.17 C
ANISOU 2441 CG1 ILE A 238 4410 4486 2948 -440 172 -172 C
ATOM 2442 CG2 ILE A 238 20.403 -14.650 14.284 1.00 27.56 C
ANISOU 2442 CG2 ILE A 238 3856 4188 2427 -482 139 -17 C
ATOM 2443 CD1 ILE A 238 19.675 -17.182 12.966 1.00 43.73 C
ANISOU 2443 CD1 ILE A 238 6049 6018 4549 -487 76 -96 C
ATOM 2444 N VAL A 239 24.043 -14.147 14.984 1.00 30.74 N
ANISOU 2444 N VAL A 239 4050 4609 3021 -305 230 -118 N
ATOM 2445 CA VAL A 239 24.675 -13.234 15.929 1.00 28.08 C
ANISOU 2445 CA VAL A 239 3624 4339 2705 -285 217 -84 C
ATOM 2446 C VAL A 239 25.558 -12.236 15.191 1.00 31.70 C
ANISOU 2446 C VAL A 239 4030 4847 3169 -273 308 -145 C
ATOM 2447 O VAL A 239 25.581 -11.044 15.519 1.00 29.29 O
ANISOU 2447 O VAL A 239 3678 4617 2833 -297 313 -123 O
ATOM 2448 CB VAL A 239 25.465 -14.026 16.987 1.00 28.68 C
ANISOU 2448 CB VAL A 239 3644 4369 2883 -219 157 -56 C
ATOM 2449 CG1 VAL A 239 26.210 -13.082 17.916 1.00 28.41 C
ANISOU 2449 CG1 VAL A 239 3518 4403 2874 -194 136 -33 C
ATOM 2450 CG2 VAL A 239 24.528 -14.929 17.779 1.00 34.45 C
ANISOU 2450 CG2 VAL A 239 4419 5062 3609 -231 69 24 C
ATOM 2451 N GLY A 240 26.287 -12.701 14.175 1.00 32.79 N
ANISOU 2451 N GLY A 240 4172 4940 3347 -234 380 -220 N
ATOM 2452 CA GLY A 240 27.145 -11.801 13.423 1.00 28.94 C
ANISOU 2452 CA GLY A 240 3627 4499 2872 -216 475 -266 C
ATOM 2453 C GLY A 240 26.365 -10.755 12.650 1.00 31.82 C
ANISOU 2453 C GLY A 240 4025 4935 3130 -281 527 -267 C
ATOM 2454 O GLY A 240 26.752 -9.584 12.611 1.00 34.41 O
ANISOU 2454 O GLY A 240 4288 5328 3460 -292 567 -259 O
ATOM 2455 N LEU A 241 25.258 -11.159 12.024 1.00 28.07 N
ANISOU 2455 N LEU A 241 3650 4446 2570 -325 523 -274 N
ATOM 2456 CA LEU A 241 24.435 -10.197 11.302 1.00 33.98 C
ANISOU 2456 CA LEU A 241 4433 5264 3213 -388 567 -268 C
ATOM 2457 C LEU A 241 23.740 -9.231 12.252 1.00 30.61 C
ANISOU 2457 C LEU A 241 3983 4902 2745 -444 513 -192 C
ATOM 2458 O LEU A 241 23.511 -8.071 11.895 1.00 25.83 O
ANISOU 2458 O LEU A 241 3359 4368 2089 -482 559 -181 O
ATOM 2459 CB LEU A 241 23.414 -10.927 10.430 1.00 27.57 C
ANISOU 2459 CB LEU A 241 3734 4417 2323 -421 564 -294 C
ATOM 2460 CG LEU A 241 24.013 -11.731 9.273 1.00 32.38 C
ANISOU 2460 CG LEU A 241 4382 4974 2948 -364 629 -385 C
ATOM 2461 CD1 LEU A 241 22.923 -12.420 8.472 1.00 34.90 C
ANISOU 2461 CD1 LEU A 241 4817 5255 3187 -400 606 -415 C
ATOM 2462 CD2 LEU A 241 24.858 -10.837 8.379 1.00 28.84 C
ANISOU 2462 CD2 LEU A 241 3880 4589 2490 -332 746 -423 C
ATOM 2463 N PHE A 242 23.401 -9.686 13.460 1.00 29.29 N
ANISOU 2463 N PHE A 242 3816 4713 2600 -443 418 -135 N
ATOM 2464 CA PHE A 242 22.888 -8.775 14.478 1.00 25.37 C
ANISOU 2464 CA PHE A 242 3292 4280 2068 -476 365 -66 C
ATOM 2465 C PHE A 242 23.910 -7.690 14.795 1.00 33.43 C
ANISOU 2465 C PHE A 242 4214 5347 3140 -451 391 -80 C
ATOM 2466 O PHE A 242 23.579 -6.499 14.842 1.00 28.54 O
ANISOU 2466 O PHE A 242 3575 4794 2475 -489 405 -60 O
ATOM 2467 CB PHE A 242 22.516 -9.558 15.739 1.00 25.39 C
ANISOU 2467 CB PHE A 242 3305 4252 2091 -459 264 -2 C
ATOM 2468 CG PHE A 242 21.928 -8.710 16.834 1.00 28.90 C
ANISOU 2468 CG PHE A 242 3730 4765 2484 -480 207 71 C
ATOM 2469 CD1 PHE A 242 22.746 -8.072 17.755 1.00 38.55 C
ANISOU 2469 CD1 PHE A 242 4874 6022 3753 -439 176 74 C
ATOM 2470 CD2 PHE A 242 20.556 -8.562 16.950 1.00 29.19 C
ANISOU 2470 CD2 PHE A 242 3829 4833 2429 -535 180 135 C
ATOM 2471 CE1 PHE A 242 22.208 -7.291 18.758 1.00 28.00 C
ANISOU 2471 CE1 PHE A 242 3528 4748 2361 -449 121 132 C
ATOM 2472 CE2 PHE A 242 20.011 -7.787 17.956 1.00 32.21 C
ANISOU 2472 CE2 PHE A 242 4198 5282 2759 -543 133 202 C
ATOM 2473 CZ PHE A 242 20.838 -7.151 18.861 1.00 36.08 C
ANISOU 2473 CZ PHE A 242 4616 5805 3286 -497 103 196 C
ATOM 2474 N ALA A 243 25.165 -8.088 15.017 1.00 29.59 N
ANISOU 2474 N ALA A 243 3662 4823 2758 -387 394 -113 N
ATOM 2475 CA ALA A 243 26.217 -7.115 15.291 1.00 26.11 C
ANISOU 2475 CA ALA A 243 3118 4416 2387 -363 412 -126 C
ATOM 2476 C ALA A 243 26.442 -6.196 14.098 1.00 26.06 C
ANISOU 2476 C ALA A 243 3088 4447 2366 -386 517 -158 C
ATOM 2477 O ALA A 243 26.643 -4.989 14.265 1.00 28.02 O
ANISOU 2477 O ALA A 243 3275 4745 2624 -406 526 -146 O
ATOM 2478 CB ALA A 243 27.513 -7.833 15.664 1.00 27.00 C
ANISOU 2478 CB ALA A 243 3163 4474 2620 -289 398 -150 C
ATOM 2479 N LEU A 244 26.407 -6.748 12.884 1.00 26.47 N
ANISOU 2479 N LEU A 244 3188 4476 2392 -380 595 -199 N
ATOM 2480 CA LEU A 244 26.633 -5.929 11.699 1.00 26.53 C
ANISOU 2480 CA LEU A 244 3174 4527 2379 -392 703 -224 C
ATOM 2481 C LEU A 244 25.531 -4.891 11.517 1.00 33.55 C
ANISOU 2481 C LEU A 244 4096 5482 3168 -467 709 -188 C
ATOM 2482 O LEU A 244 25.796 -3.783 11.037 1.00 27.77 O
ANISOU 2482 O LEU A 244 3309 4800 2442 -484 772 -183 O
ATOM 2483 CB LEU A 244 26.739 -6.825 10.464 1.00 40.19 C
ANISOU 2483 CB LEU A 244 4964 6223 4085 -359 779 -279 C
ATOM 2484 CG LEU A 244 27.087 -6.160 9.131 1.00 48.83 C
ANISOU 2484 CG LEU A 244 6036 7363 5153 -351 903 -305 C
ATOM 2485 CD1 LEU A 244 28.461 -5.510 9.197 1.00 52.38 C
ANISOU 2485 CD1 LEU A 244 6356 7825 5720 -304 955 -300 C
ATOM 2486 CD2 LEU A 244 27.022 -7.171 7.997 1.00 54.54 C
ANISOU 2486 CD2 LEU A 244 6842 8052 5829 -313 961 -365 C
ATOM 2487 N CYS A 245 24.297 -5.221 11.909 1.00 29.81 N
ANISOU 2487 N CYS A 245 3707 5010 2610 -512 645 -155 N
ATOM 2488 CA CYS A 245 23.173 -4.313 11.706 1.00 24.18 C
ANISOU 2488 CA CYS A 245 3032 4359 1798 -583 652 -117 C
ATOM 2489 C CYS A 245 23.059 -3.258 12.800 1.00 30.16 C
ANISOU 2489 C CYS A 245 3735 5158 2565 -603 596 -70 C
ATOM 2490 O CYS A 245 22.525 -2.173 12.547 1.00 25.35 O
ANISOU 2490 O CYS A 245 3121 4605 1905 -649 625 -46 O
ATOM 2491 CB CYS A 245 21.864 -5.101 11.625 1.00 26.51 C
ANISOU 2491 CB CYS A 245 3436 4636 2002 -623 608 -94 C
ATOM 2492 SG CYS A 245 21.705 -6.170 10.177 1.00 53.02 S
ANISOU 2492 SG CYS A 245 6877 7948 5319 -613 667 -156 S
ATOM 2493 N TRP A 246 23.541 -3.545 14.011 1.00 23.70 N
ANISOU 2493 N TRP A 246 2879 4316 1810 -564 514 -59 N
ATOM 2494 CA TRP A 246 23.356 -2.635 15.133 1.00 27.49 C
ANISOU 2494 CA TRP A 246 3323 4835 2287 -574 446 -21 C
ATOM 2495 C TRP A 246 24.615 -1.897 15.564 1.00 27.01 C
ANISOU 2495 C TRP A 246 3152 4775 2336 -538 438 -46 C
ATOM 2496 O TRP A 246 24.497 -0.834 16.181 1.00 24.88 O
ANISOU 2496 O TRP A 246 2848 4544 2064 -554 400 -29 O
ATOM 2497 CB TRP A 246 22.792 -3.387 16.348 1.00 29.92 C
ANISOU 2497 CB TRP A 246 3673 5129 2567 -556 343 23 C
ATOM 2498 CG TRP A 246 21.321 -3.609 16.266 1.00 24.15 C
ANISOU 2498 CG TRP A 246 3034 4418 1724 -606 330 75 C
ATOM 2499 CD1 TRP A 246 20.686 -4.746 15.866 1.00 32.60 C
ANISOU 2499 CD1 TRP A 246 4177 5447 2761 -618 326 87 C
ATOM 2500 CD2 TRP A 246 20.292 -2.666 16.588 1.00 32.49 C
ANISOU 2500 CD2 TRP A 246 4115 5536 2694 -650 314 125 C
ATOM 2501 NE1 TRP A 246 19.325 -4.572 15.921 1.00 35.17 N
ANISOU 2501 NE1 TRP A 246 4567 5806 2990 -670 308 148 N
ATOM 2502 CE2 TRP A 246 19.057 -3.302 16.360 1.00 35.37 C
ANISOU 2502 CE2 TRP A 246 4565 5898 2977 -689 305 174 C
ATOM 2503 CE3 TRP A 246 20.296 -1.344 17.046 1.00 26.58 C
ANISOU 2503 CE3 TRP A 246 3324 4841 1934 -660 305 134 C
ATOM 2504 CZ2 TRP A 246 17.837 -2.663 16.574 1.00 31.74 C
ANISOU 2504 CZ2 TRP A 246 4130 5380 2551 -682 268 218 C
ATOM 2505 CZ3 TRP A 246 19.084 -0.712 17.259 1.00 21.76 C
ANISOU 2505 CZ3 TRP A 246 2752 4205 1309 -669 276 179 C
ATOM 2506 CH2 TRP A 246 17.872 -1.372 17.022 1.00 32.48 C
ANISOU 2506 CH2 TRP A 246 4179 5482 2678 -666 256 216 C
ATOM 2507 N LEU A 247 25.802 -2.423 15.270 1.00 24.36 N
ANISOU 2507 N LEU A 247 2760 4397 2101 -489 468 -85 N
ATOM 2508 CA LEU A 247 27.023 -1.737 15.686 1.00 24.81 C
ANISOU 2508 CA LEU A 247 2703 4449 2275 -457 454 -102 C
ATOM 2509 C LEU A 247 27.172 -0.330 15.113 1.00 26.73 C
ANISOU 2509 C LEU A 247 2885 4732 2539 -494 512 -101 C
ATOM 2510 O LEU A 247 27.611 0.558 15.865 1.00 24.64 O
ANISOU 2510 O LEU A 247 2549 4476 2336 -491 455 -98 O
ATOM 2511 CB LEU A 247 28.251 -2.587 15.341 1.00 31.79 C
ANISOU 2511 CB LEU A 247 3535 5280 3265 -396 489 -135 C
ATOM 2512 CG LEU A 247 28.611 -3.635 16.395 1.00 36.02 C
ANISOU 2512 CG LEU A 247 4072 5772 3842 -345 399 -133 C
ATOM 2513 CD1 LEU A 247 29.833 -4.430 15.966 1.00 34.70 C
ANISOU 2513 CD1 LEU A 247 3850 5552 3783 -284 444 -164 C
ATOM 2514 CD2 LEU A 247 28.839 -2.973 17.749 1.00 26.03 C
ANISOU 2514 CD2 LEU A 247 2753 4526 2609 -334 291 -115 C
ATOM 2515 N PRO A 248 26.857 -0.051 13.838 1.00 24.51 N
ANISOU 2515 N PRO A 248 2626 4474 2214 -525 618 -102 N
ATOM 2516 CA PRO A 248 27.024 1.332 13.353 1.00 29.79 C
ANISOU 2516 CA PRO A 248 3225 5179 2914 -558 672 -90 C
ATOM 2517 C PRO A 248 26.263 2.357 14.175 1.00 26.79 C
ANISOU 2517 C PRO A 248 2854 4834 2491 -601 601 -64 C
ATOM 2518 O PRO A 248 26.815 3.415 14.500 1.00 26.68 O
ANISOU 2518 O PRO A 248 2752 4823 2560 -605 581 -63 O
ATOM 2519 CB PRO A 248 26.507 1.259 11.911 1.00 33.01 C
ANISOU 2519 CB PRO A 248 3684 5615 3243 -584 789 -88 C
ATOM 2520 CG PRO A 248 26.736 -0.145 11.510 1.00 24.83 C
ANISOU 2520 CG PRO A 248 2700 4540 2195 -540 810 -120 C
ATOM 2521 CD PRO A 248 26.474 -0.960 12.741 1.00 24.67 C
ANISOU 2521 CD PRO A 248 2722 4484 2167 -524 695 -118 C
ATOM 2522 N LEU A 249 25.011 2.064 14.533 1.00 23.88 N
ANISOU 2522 N LEU A 249 2587 4488 2000 -629 560 -40 N
ATOM 2523 CA LEU A 249 24.229 3.001 15.332 1.00 22.32 C
ANISOU 2523 CA LEU A 249 2405 4326 1749 -660 496 -13 C
ATOM 2524 C LEU A 249 24.834 3.185 16.720 1.00 24.94 C
ANISOU 2524 C LEU A 249 2687 4640 2148 -618 383 -27 C
ATOM 2525 O LEU A 249 24.854 4.301 17.250 1.00 27.56 O
ANISOU 2525 O LEU A 249 2978 4990 2504 -628 340 -28 O
ATOM 2526 CB LEU A 249 22.780 2.519 15.420 1.00 21.63 C
ANISOU 2526 CB LEU A 249 2433 4265 1520 -692 480 25 C
ATOM 2527 CG LEU A 249 21.732 3.474 15.994 1.00 30.19 C
ANISOU 2527 CG LEU A 249 3549 5397 2523 -727 441 64 C
ATOM 2528 CD1 LEU A 249 21.895 4.869 15.407 1.00 28.13 C
ANISOU 2528 CD1 LEU A 249 3229 5148 2312 -758 492 61 C
ATOM 2529 CD2 LEU A 249 20.328 2.943 15.730 1.00 20.32 C
ANISOU 2529 CD2 LEU A 249 2405 4065 1251 -719 411 100 C
ATOM 2530 N HIS A 250 25.342 2.105 17.321 1.00 25.08 N
ANISOU 2530 N HIS A 250 2708 4623 2197 -567 329 -40 N
ATOM 2531 CA HIS A 250 26.012 2.229 18.613 1.00 23.41 C
ANISOU 2531 CA HIS A 250 2446 4398 2051 -519 219 -54 C
ATOM 2532 C HIS A 250 27.323 2.993 18.488 1.00 24.07 C
ANISOU 2532 C HIS A 250 2406 4456 2282 -506 224 -88 C
ATOM 2533 O HIS A 250 27.667 3.794 19.364 1.00 24.24 O
ANISOU 2533 O HIS A 250 2377 4479 2353 -493 139 -103 O
ATOM 2534 CB HIS A 250 26.272 0.848 19.214 1.00 26.17 C
ANISOU 2534 CB HIS A 250 2822 4717 2406 -467 168 -52 C
ATOM 2535 CG HIS A 250 25.039 0.152 19.699 1.00 24.07 C
ANISOU 2535 CG HIS A 250 2661 4472 2013 -471 131 -8 C
ATOM 2536 ND1 HIS A 250 24.363 0.541 20.835 1.00 25.63 N
ANISOU 2536 ND1 HIS A 250 2891 4710 2139 -459 44 22 N
ATOM 2537 CD2 HIS A 250 24.372 -0.921 19.213 1.00 23.13 C
ANISOU 2537 CD2 HIS A 250 2618 4338 1834 -483 166 16 C
ATOM 2538 CE1 HIS A 250 23.328 -0.257 21.023 1.00 23.81 C
ANISOU 2538 CE1 HIS A 250 2746 4491 1810 -464 34 72 C
ATOM 2539 NE2 HIS A 250 23.309 -1.151 20.052 1.00 22.70 N
ANISOU 2539 NE2 HIS A 250 2632 4313 1681 -482 103 69 N
ATOM 2540 N ILE A 251 28.076 2.746 17.415 1.00 24.53 N
ANISOU 2540 N ILE A 251 2414 4489 2417 -504 320 -99 N
ATOM 2541 CA ILE A 251 29.361 3.416 17.244 1.00 25.26 C
ANISOU 2541 CA ILE A 251 2377 4554 2665 -490 332 -117 C
ATOM 2542 C ILE A 251 29.162 4.912 17.034 1.00 29.82 C
ANISOU 2542 C ILE A 251 2909 5155 3266 -538 345 -109 C
ATOM 2543 O ILE A 251 29.944 5.731 17.531 1.00 34.23 O
ANISOU 2543 O ILE A 251 3372 5692 3942 -531 286 -123 O
ATOM 2544 CB ILE A 251 30.147 2.767 16.089 1.00 31.70 C
ANISOU 2544 CB ILE A 251 3154 5346 3546 -469 445 -121 C
ATOM 2545 CG1 ILE A 251 30.590 1.354 16.484 1.00 30.32 C
ANISOU 2545 CG1 ILE A 251 3003 5134 3385 -412 413 -135 C
ATOM 2546 CG2 ILE A 251 31.348 3.616 15.703 1.00 26.59 C
ANISOU 2546 CG2 ILE A 251 2367 4679 3058 -463 482 -120 C
ATOM 2547 CD1 ILE A 251 31.218 0.558 15.357 1.00 26.92 C
ANISOU 2547 CD1 ILE A 251 2556 4678 2993 -382 525 -144 C
ATOM 2548 N ILE A 252 28.107 5.296 16.312 1.00 24.30 N
ANISOU 2548 N ILE A 252 2276 4496 2462 -588 415 -84 N
ATOM 2549 CA ILE A 252 27.833 6.714 16.109 1.00 24.05 C
ANISOU 2549 CA ILE A 252 2203 4485 2449 -634 430 -71 C
ATOM 2550 C ILE A 252 27.465 7.381 17.430 1.00 28.21 C
ANISOU 2550 C ILE A 252 2745 5017 2958 -631 300 -86 C
ATOM 2551 O ILE A 252 27.880 8.514 17.705 1.00 24.08 O
ANISOU 2551 O ILE A 252 2144 4479 2527 -642 261 -98 O
ATOM 2552 CB ILE A 252 26.736 6.899 15.044 1.00 26.14 C
ANISOU 2552 CB ILE A 252 2540 4796 2597 -685 534 -37 C
ATOM 2553 CG1 ILE A 252 27.252 6.469 13.671 1.00 23.80 C
ANISOU 2553 CG1 ILE A 252 2214 4498 2330 -680 665 -28 C
ATOM 2554 CG2 ILE A 252 26.277 8.342 14.989 1.00 23.02 C
ANISOU 2554 CG2 ILE A 252 2116 4423 2206 -732 538 -18 C
ATOM 2555 CD1 ILE A 252 26.221 6.576 12.573 1.00 27.61 C
ANISOU 2555 CD1 ILE A 252 2769 5029 2693 -724 764 1 C
ATOM 2556 N ASN A 253 26.695 6.687 18.275 1.00 23.39 N
ANISOU 2556 N ASN A 253 2231 4426 2231 -610 230 -84 N
ATOM 2557 CA ASN A 253 26.381 7.224 19.596 1.00 23.29 C
ANISOU 2557 CA ASN A 253 2238 4425 2188 -589 106 -99 C
ATOM 2558 C ASN A 253 27.646 7.431 20.422 1.00 24.17 C
ANISOU 2558 C ASN A 253 2253 4494 2437 -544 7 -142 C
ATOM 2559 O ASN A 253 27.745 8.400 21.185 1.00 39.03 O
ANISOU 2559 O ASN A 253 4105 6371 4353 -538 -82 -170 O
ATOM 2560 CB ASN A 253 25.403 6.300 20.325 1.00 22.82 C
ANISOU 2560 CB ASN A 253 2292 4398 1983 -564 58 -75 C
ATOM 2561 CG ASN A 253 23.981 6.401 19.784 1.00 25.78 C
ANISOU 2561 CG ASN A 253 2759 4818 2217 -613 123 -29 C
ATOM 2562 OD1 ASN A 253 23.644 7.333 19.053 1.00 27.84 O
ANISOU 2562 OD1 ASN A 253 3006 5094 2478 -662 188 -18 O
ATOM 2563 ND2 ASN A 253 23.140 5.442 20.150 1.00 24.45 N
ANISOU 2563 ND2 ASN A 253 2682 4670 1937 -599 105 6 N
ATOM 2564 N CYS A 254 28.629 6.538 20.279 1.00 31.47 N
ANISOU 2564 N CYS A 254 3128 5382 3445 -510 17 -152 N
ATOM 2565 CA CYS A 254 29.892 6.714 20.989 1.00 25.69 C
ANISOU 2565 CA CYS A 254 2296 4608 2858 -470 -74 -188 C
ATOM 2566 C CYS A 254 30.613 7.975 20.529 1.00 26.15 C
ANISOU 2566 C CYS A 254 2238 4636 3063 -503 -58 -199 C
ATOM 2567 O CYS A 254 31.210 8.688 21.342 1.00 26.72 O
ANISOU 2567 O CYS A 254 2244 4681 3227 -487 -168 -233 O
ATOM 2568 CB CYS A 254 30.784 5.487 20.798 1.00 30.00 C
ANISOU 2568 CB CYS A 254 2807 5122 3468 -429 -49 -186 C
ATOM 2569 SG CYS A 254 30.192 3.993 21.626 1.00 27.21 S
ANISOU 2569 SG CYS A 254 2564 4787 2987 -379 -104 -174 S
ATOM 2570 N PHE A 255 30.572 8.268 19.228 1.00 26.00 N
ANISOU 2570 N PHE A 255 2190 4620 3069 -546 76 -168 N
ATOM 2571 CA PHE A 255 31.198 9.489 18.733 1.00 26.46 C
ANISOU 2571 CA PHE A 255 2132 4650 3271 -580 101 -162 C
ATOM 2572 C PHE A 255 30.487 10.729 19.262 1.00 33.04 C
ANISOU 2572 C PHE A 255 2986 5494 4073 -611 33 -176 C
ATOM 2573 O PHE A 255 31.139 11.691 19.683 1.00 32.77 O
ANISOU 2573 O PHE A 255 2860 5419 4172 -615 -44 -201 O
ATOM 2574 CB PHE A 255 31.220 9.492 17.204 1.00 26.39 C
ANISOU 2574 CB PHE A 255 2095 4654 3276 -611 268 -116 C
ATOM 2575 CG PHE A 255 32.425 8.813 16.617 1.00 30.58 C
ANISOU 2575 CG PHE A 255 2538 5155 3927 -577 331 -105 C
ATOM 2576 CD1 PHE A 255 33.581 9.532 16.360 1.00 31.64 C
ANISOU 2576 CD1 PHE A 255 2522 5248 4253 -577 340 -90 C
ATOM 2577 CD2 PHE A 255 32.404 7.458 16.324 1.00 31.63 C
ANISOU 2577 CD2 PHE A 255 2735 5297 3987 -541 382 -105 C
ATOM 2578 CE1 PHE A 255 34.692 8.914 15.820 1.00 36.20 C
ANISOU 2578 CE1 PHE A 255 3013 5799 4940 -539 405 -70 C
ATOM 2579 CE2 PHE A 255 33.513 6.834 15.785 1.00 27.99 C
ANISOU 2579 CE2 PHE A 255 2195 4808 3633 -501 444 -95 C
ATOM 2580 CZ PHE A 255 34.658 7.563 15.533 1.00 41.58 C
ANISOU 2580 CZ PHE A 255 3765 6494 5538 -498 459 -76 C
ATOM 2581 N THR A 256 29.151 10.721 19.255 1.00 25.16 N
ANISOU 2581 N THR A 256 2107 4548 2905 -632 56 -162 N
ATOM 2582 CA THR A 256 28.398 11.878 19.732 1.00 26.21 C
ANISOU 2582 CA THR A 256 2268 4694 2997 -656 0 -173 C
ATOM 2583 C THR A 256 28.670 12.142 21.207 1.00 31.19 C
ANISOU 2583 C THR A 256 2899 5306 3647 -608 -168 -230 C
ATOM 2584 O THR A 256 28.771 13.299 21.631 1.00 41.87 O
ANISOU 2584 O THR A 256 4209 6634 5067 -618 -241 -260 O
ATOM 2585 CB THR A 256 26.902 11.663 19.490 1.00 32.93 C
ANISOU 2585 CB THR A 256 3249 5608 3655 -680 58 -138 C
ATOM 2586 OG1 THR A 256 26.665 11.462 18.090 1.00 32.31 O
ANISOU 2586 OG1 THR A 256 3170 5548 3558 -723 207 -91 O
ATOM 2587 CG2 THR A 256 26.096 12.867 19.964 1.00 28.91 C
ANISOU 2587 CG2 THR A 256 2770 5114 3101 -700 8 -145 C
ATOM 2588 N PHE A 257 28.811 11.080 21.999 1.00 34.83 N
ANISOU 2588 N PHE A 257 3405 5776 4051 -553 -234 -246 N
ATOM 2589 CA PHE A 257 29.011 11.160 23.442 1.00 27.47 C
ANISOU 2589 CA PHE A 257 2488 4841 3109 -495 -395 -296 C
ATOM 2590 C PHE A 257 30.466 11.409 23.832 1.00 26.98 C
ANISOU 2590 C PHE A 257 2301 4716 3236 -471 -484 -340 C
ATOM 2591 O PHE A 257 30.744 12.275 24.668 1.00 35.63 O
ANISOU 2591 O PHE A 257 3364 5786 4387 -454 -610 -392 O
ATOM 2592 CB PHE A 257 28.505 9.879 24.114 1.00 25.54 C
ANISOU 2592 CB PHE A 257 2344 4640 2721 -443 -423 -281 C
ATOM 2593 CG PHE A 257 28.674 9.873 25.607 1.00 27.12 C
ANISOU 2593 CG PHE A 257 2566 4850 2890 -372 -583 -326 C
ATOM 2594 CD1 PHE A 257 27.904 10.703 26.405 1.00 25.90 C
ANISOU 2594 CD1 PHE A 257 2472 4727 2643 -352 -661 -350 C
ATOM 2595 CD2 PHE A 257 29.598 9.036 26.214 1.00 30.74 C
ANISOU 2595 CD2 PHE A 257 2985 5288 3407 -318 -654 -343 C
ATOM 2596 CE1 PHE A 257 28.056 10.705 27.775 1.00 26.48 C
ANISOU 2596 CE1 PHE A 257 2570 4816 2674 -276 -808 -395 C
ATOM 2597 CE2 PHE A 257 29.751 9.033 27.589 1.00 36.34 C
ANISOU 2597 CE2 PHE A 257 3715 6013 4078 -247 -803 -383 C
ATOM 2598 CZ PHE A 257 28.979 9.870 28.368 1.00 27.19 C
ANISOU 2598 CZ PHE A 257 2620 4890 2819 -224 -881 -411 C
ATOM 2599 N PHE A 258 31.400 10.660 23.251 1.00 27.41 N
ANISOU 2599 N PHE A 258 2282 4740 3391 -468 -427 -320 N
ATOM 2600 CA PHE A 258 32.793 10.721 23.678 1.00 39.16 C
ANISOU 2600 CA PHE A 258 3651 6171 5058 -440 -514 -352 C
ATOM 2601 C PHE A 258 33.592 11.827 23.005 1.00 31.49 C
ANISOU 2601 C PHE A 258 2542 5142 4280 -486 -490 -348 C
ATOM 2602 O PHE A 258 34.581 12.286 23.586 1.00 40.07 O
ANISOU 2602 O PHE A 258 3530 6175 5519 -471 -602 -384 O
ATOM 2603 CB PHE A 258 33.489 9.379 23.430 1.00 31.51 C
ANISOU 2603 CB PHE A 258 2659 5194 4118 -407 -467 -327 C
ATOM 2604 CG PHE A 258 33.088 8.302 24.401 1.00 40.65 C
ANISOU 2604 CG PHE A 258 3914 6389 5142 -348 -538 -336 C
ATOM 2605 CD1 PHE A 258 33.102 8.540 25.768 1.00 33.59 C
ANISOU 2605 CD1 PHE A 258 3043 5504 4217 -299 -698 -381 C
ATOM 2606 CD2 PHE A 258 32.692 7.053 23.948 1.00 28.14 C
ANISOU 2606 CD2 PHE A 258 2398 4828 3464 -337 -446 -296 C
ATOM 2607 CE1 PHE A 258 32.734 7.552 26.660 1.00 35.63 C
ANISOU 2607 CE1 PHE A 258 3385 5802 4351 -239 -758 -377 C
ATOM 2608 CE2 PHE A 258 32.321 6.065 24.837 1.00 28.02 C
ANISOU 2608 CE2 PHE A 258 2465 4844 3339 -284 -510 -292 C
ATOM 2609 CZ PHE A 258 32.341 6.315 26.193 1.00 31.02 C
ANISOU 2609 CZ PHE A 258 2860 5239 3686 -234 -662 -328 C
ATOM 2610 N CYS A 259 33.203 12.266 21.806 1.00 44.21 N
ANISOU 2610 N CYS A 259 5636 5814 5349 -703 -1359 -951 N
ATOM 2611 CA CYS A 259 33.895 13.349 21.107 1.00 45.39 C
ANISOU 2611 CA CYS A 259 5732 5813 5701 -859 -1354 -966 C
ATOM 2612 C CYS A 259 32.964 14.544 20.956 1.00 45.55 C
ANISOU 2612 C CYS A 259 5950 5695 5660 -838 -1307 -1004 C
ATOM 2613 O CYS A 259 32.293 14.691 19.922 1.00 44.45 O
ANISOU 2613 O CYS A 259 5841 5525 5522 -825 -1140 -910 O
ATOM 2614 CB CYS A 259 34.404 12.895 19.742 1.00 44.67 C
ANISOU 2614 CB CYS A 259 5460 5743 5770 -945 -1185 -844 C
ATOM 2615 SG CYS A 259 35.402 14.168 18.918 1.00 72.51 S
ANISOU 2615 SG CYS A 259 8904 9092 9555 -1166 -1164 -842 S
ATOM 2616 N PRO A 260 32.886 15.428 21.956 1.00 47.09 N
ANISOU 2616 N PRO A 260 6291 5798 5804 -828 -1458 -1145 N
ATOM 2617 CA PRO A 260 32.079 16.646 21.792 1.00 68.53 C
ANISOU 2617 CA PRO A 260 9186 8350 8501 -805 -1418 -1192 C
ATOM 2618 C PRO A 260 32.681 17.651 20.822 1.00 60.18 C
ANISOU 2618 C PRO A 260 8087 7109 7668 -972 -1388 -1149 C
ATOM 2619 O PRO A 260 31.982 18.595 20.431 1.00 70.81 O
ANISOU 2619 O PRO A 260 9574 8308 9024 -952 -1335 -1147 O
ATOM 2620 CB PRO A 260 32.012 17.219 23.213 1.00 57.52 C
ANISOU 2620 CB PRO A 260 7951 6910 6993 -756 -1600 -1379 C
ATOM 2621 CG PRO A 260 33.254 16.731 23.862 1.00 50.45 C
ANISOU 2621 CG PRO A 260 6928 6085 6157 -847 -1780 -1423 C
ATOM 2622 CD PRO A 260 33.489 15.349 23.297 1.00 48.65 C
ANISOU 2622 CD PRO A 260 6511 6031 5943 -827 -1679 -1273 C
ATOM 2623 N ASP A 261 33.945 17.488 20.431 1.00 53.98 N
ANISOU 2623 N ASP A 261 7112 6326 7073 -1136 -1418 -1111 N
ATOM 2624 CA ASP A 261 34.575 18.370 19.458 1.00 58.93 C
ANISOU 2624 CA ASP A 261 7684 6790 7916 -1317 -1360 -1048 C
ATOM 2625 C ASP A 261 34.426 17.878 18.026 1.00 49.22 C
ANISOU 2625 C ASP A 261 6370 5618 6715 -1344 -1133 -868 C
ATOM 2626 O ASP A 261 34.707 18.639 17.093 1.00 50.16 O
ANISOU 2626 O ASP A 261 6491 5601 6965 -1480 -1046 -787 O
ATOM 2627 CB ASP A 261 36.061 18.546 19.785 1.00 53.09 C
ANISOU 2627 CB ASP A 261 6766 6013 7392 -1498 -1502 -1109 C
ATOM 2628 CG ASP A 261 36.292 19.484 20.953 1.00 81.58 C
ANISOU 2628 CG ASP A 261 10494 9486 11018 -1532 -1738 -1291 C
ATOM 2629 OD1 ASP A 261 35.304 20.060 21.459 1.00 88.32 O
ANISOU 2629 OD1 ASP A 261 11578 10262 11718 -1413 -1767 -1374 O
ATOM 2630 OD2 ASP A 261 37.460 19.648 21.365 1.00 75.34 O
ANISOU 2630 OD2 ASP A 261 9562 8665 10399 -1676 -1896 -1360 O
ATOM 2631 N CYS A 262 34.004 16.633 17.829 1.00 54.35 N
ANISOU 2631 N CYS A 262 6958 6456 7236 -1227 -1036 -803 N
ATOM 2632 CA CYS A 262 33.710 16.137 16.494 1.00 51.13 C
ANISOU 2632 CA CYS A 262 6508 6107 6814 -1235 -828 -651 C
ATOM 2633 C CYS A 262 32.372 16.682 16.020 1.00 49.34 C
ANISOU 2633 C CYS A 262 6481 5807 6460 -1137 -756 -596 C
ATOM 2634 O CYS A 262 31.441 16.862 16.811 1.00 47.72 O
ANISOU 2634 O CYS A 262 6410 5593 6128 -994 -829 -672 O
ATOM 2635 CB CYS A 262 33.676 14.608 16.477 1.00 45.74 C
ANISOU 2635 CB CYS A 262 5700 5632 6046 -1140 -764 -615 C
ATOM 2636 SG CYS A 262 35.217 13.787 16.933 1.00 59.80 S
ANISOU 2636 SG CYS A 262 7216 7508 7996 -1223 -846 -661 S
ATOM 2637 N SER A 263 32.284 16.956 14.723 1.00 45.17 N
ANISOU 2637 N SER A 263 5970 5225 5966 -1214 -612 -464 N
ATOM 2638 CA SER A 263 31.002 17.307 14.133 1.00 51.76 C
ANISOU 2638 CA SER A 263 6973 6010 6682 -1111 -552 -388 C
ATOM 2639 C SER A 263 30.039 16.134 14.261 1.00 42.33 C
ANISOU 2639 C SER A 263 5770 4999 5313 -937 -508 -378 C
ATOM 2640 O SER A 263 30.421 14.974 14.089 1.00 53.86 O
ANISOU 2640 O SER A 263 7098 6618 6750 -939 -444 -355 O
ATOM 2641 CB SER A 263 31.180 17.689 12.663 1.00 45.04 C
ANISOU 2641 CB SER A 263 6146 5089 5876 -1237 -413 -229 C
ATOM 2642 OG SER A 263 32.161 18.698 12.513 1.00 60.05 O
ANISOU 2642 OG SER A 263 8036 6824 7956 -1424 -434 -222 O
ATOM 2643 N HIS A 264 28.786 16.439 14.584 1.00 41.86 N
ANISOU 2643 N HIS A 264 5846 4911 5149 -786 -540 -400 N
ATOM 2644 CA HIS A 264 27.785 15.391 14.705 1.00 40.10 C
ANISOU 2644 CA HIS A 264 5610 4850 4777 -632 -494 -386 C
ATOM 2645 C HIS A 264 27.593 14.697 13.361 1.00 46.03 C
ANISOU 2645 C HIS A 264 6319 5682 5487 -664 -364 -246 C
ATOM 2646 O HIS A 264 27.644 15.334 12.304 1.00 39.87 O
ANISOU 2646 O HIS A 264 5600 4806 4744 -747 -313 -148 O
ATOM 2647 CB HIS A 264 26.461 15.977 15.199 1.00 40.19 C
ANISOU 2647 CB HIS A 264 5755 4801 4713 -472 -536 -432 C
ATOM 2648 CG HIS A 264 25.487 14.948 15.685 1.00 38.76 C
ANISOU 2648 CG HIS A 264 5544 4787 4396 -320 -502 -448 C
ATOM 2649 ND1 HIS A 264 24.881 14.040 14.844 1.00 37.43 N
ANISOU 2649 ND1 HIS A 264 5324 4733 4164 -286 -412 -343 N
ATOM 2650 CD2 HIS A 264 25.012 14.686 16.925 1.00 38.68 C
ANISOU 2650 CD2 HIS A 264 5555 4845 4297 -203 -541 -555 C
ATOM 2651 CE1 HIS A 264 24.075 13.263 15.545 1.00 36.57 C
ANISOU 2651 CE1 HIS A 264 5191 4747 3956 -162 -398 -380 C
ATOM 2652 NE2 HIS A 264 24.136 13.634 16.811 1.00 37.31 N
ANISOU 2652 NE2 HIS A 264 5331 4821 4026 -108 -466 -502 N
ATOM 2653 N ALA A 265 27.394 13.382 13.411 1.00 37.70 N
ANISOU 2653 N ALA A 265 5173 4798 4351 -603 -314 -239 N
ATOM 2654 CA ALA A 265 27.174 12.609 12.198 1.00 38.75 C
ANISOU 2654 CA ALA A 265 5277 5017 4430 -624 -199 -133 C
ATOM 2655 C ALA A 265 26.016 13.207 11.403 1.00 36.96 C
ANISOU 2655 C ALA A 265 5181 4724 4139 -570 -190 -49 C
ATOM 2656 O ALA A 265 25.007 13.615 11.990 1.00 36.91 O
ANISOU 2656 O ALA A 265 5242 4682 4100 -444 -256 -85 O
ATOM 2657 CB ALA A 265 26.879 11.147 12.541 1.00 35.41 C
ANISOU 2657 CB ALA A 265 4762 4762 3930 -540 -171 -154 C
ATOM 2658 N PRO A 266 26.132 13.291 10.079 1.00 37.35 N
ANISOU 2658 N PRO A 266 5269 4754 4168 -657 -111 62 N
ATOM 2659 CA PRO A 266 25.108 13.984 9.290 1.00 37.85 C
ANISOU 2659 CA PRO A 266 5470 4734 4176 -612 -135 158 C
ATOM 2660 C PRO A 266 23.764 13.273 9.343 1.00 36.70 C
ANISOU 2660 C PRO A 266 5319 4691 3933 -460 -162 160 C
ATOM 2661 O PRO A 266 23.654 12.100 9.704 1.00 35.46 O
ANISOU 2661 O PRO A 266 5063 4678 3731 -416 -130 113 O
ATOM 2662 CB PRO A 266 25.686 13.982 7.869 1.00 38.60 C
ANISOU 2662 CB PRO A 266 5606 4825 4237 -757 -32 277 C
ATOM 2663 CG PRO A 266 26.673 12.861 7.859 1.00 40.22 C
ANISOU 2663 CG PRO A 266 5665 5165 4451 -828 71 230 C
ATOM 2664 CD PRO A 266 27.243 12.804 9.245 1.00 37.66 C
ANISOU 2664 CD PRO A 266 5234 4844 4233 -802 6 106 C
ATOM 2665 N LEU A 267 22.725 14.026 8.973 1.00 39.98 N
ANISOU 2665 N LEU A 267 5838 5017 4334 -381 -227 219 N
ATOM 2666 CA LEU A 267 21.358 13.520 9.057 1.00 36.64 C
ANISOU 2666 CA LEU A 267 5393 4675 3854 -233 -266 220 C
ATOM 2667 C LEU A 267 21.178 12.252 8.231 1.00 35.69 C
ANISOU 2667 C LEU A 267 5220 4707 3633 -264 -208 269 C
ATOM 2668 O LEU A 267 20.542 11.293 8.683 1.00 34.64 O
ANISOU 2668 O LEU A 267 4999 4693 3470 -183 -203 223 O
ATOM 2669 CB LEU A 267 20.381 14.601 8.596 1.00 37.90 C
ANISOU 2669 CB LEU A 267 5663 4698 4040 -153 -356 293 C
ATOM 2670 CG LEU A 267 18.892 14.266 8.573 1.00 37.66 C
ANISOU 2670 CG LEU A 267 5594 4730 3986 2 -412 304 C
ATOM 2671 CD1 LEU A 267 18.277 14.508 9.933 1.00 37.63 C
ANISOU 2671 CD1 LEU A 267 5532 4718 4050 149 -430 181 C
ATOM 2672 CD2 LEU A 267 18.194 15.092 7.512 1.00 73.96 C
ANISOU 2672 CD2 LEU A 267 10304 9212 8586 31 -504 433 C
ATOM 2673 N TRP A 268 21.732 12.228 7.017 1.00 36.24 N
ANISOU 2673 N TRP A 268 5354 4770 3646 -386 -157 359 N
ATOM 2674 CA TRP A 268 21.545 11.071 6.149 1.00 40.42 C
ANISOU 2674 CA TRP A 268 5860 5431 4066 -416 -105 390 C
ATOM 2675 C TRP A 268 22.217 9.831 6.725 1.00 34.41 C
ANISOU 2675 C TRP A 268 4964 4792 3318 -436 -22 297 C
ATOM 2676 O TRP A 268 21.701 8.716 6.583 1.00 33.59 O
ANISOU 2676 O TRP A 268 4805 4797 3160 -398 -10 279 O
ATOM 2677 CB TRP A 268 22.077 11.373 4.747 1.00 36.84 C
ANISOU 2677 CB TRP A 268 5528 4944 3527 -548 -49 498 C
ATOM 2678 CG TRP A 268 23.562 11.583 4.686 1.00 37.38 C
ANISOU 2678 CG TRP A 268 5577 4982 3645 -692 70 486 C
ATOM 2679 CD1 TRP A 268 24.226 12.771 4.775 1.00 38.61 C
ANISOU 2679 CD1 TRP A 268 5790 4996 3885 -770 71 523 C
ATOM 2680 CD2 TRP A 268 24.566 10.574 4.515 1.00 36.96 C
ANISOU 2680 CD2 TRP A 268 5424 5034 3584 -775 205 430 C
ATOM 2681 NE1 TRP A 268 25.581 12.566 4.671 1.00 39.00 N
ANISOU 2681 NE1 TRP A 268 5768 5066 3984 -906 200 498 N
ATOM 2682 CE2 TRP A 268 25.816 11.225 4.512 1.00 39.47 C
ANISOU 2682 CE2 TRP A 268 5726 5280 3991 -902 287 438 C
ATOM 2683 CE3 TRP A 268 24.530 9.183 4.366 1.00 43.43 C
ANISOU 2683 CE3 TRP A 268 6162 5992 4348 -752 264 371 C
ATOM 2684 CZ2 TRP A 268 27.018 10.535 4.366 1.00 43.04 C
ANISOU 2684 CZ2 TRP A 268 6063 5804 4485 -997 429 388 C
ATOM 2685 CZ3 TRP A 268 25.724 8.499 4.222 1.00 54.48 C
ANISOU 2685 CZ3 TRP A 268 7467 7450 5784 -837 402 318 C
ATOM 2686 CH2 TRP A 268 26.952 9.176 4.222 1.00 40.05 C
ANISOU 2686 CH2 TRP A 268 5606 5559 4053 -954 486 326 C
ATOM 2687 N LEU A 269 23.369 10.004 7.376 1.00 34.46 N
ANISOU 2687 N LEU A 269 4912 4772 3409 -497 23 240 N
ATOM 2688 CA LEU A 269 24.067 8.862 7.955 1.00 33.55 C
ANISOU 2688 CA LEU A 269 4665 4758 3325 -506 81 161 C
ATOM 2689 C LEU A 269 23.350 8.338 9.191 1.00 35.46 C
ANISOU 2689 C LEU A 269 4840 5055 3578 -380 18 94 C
ATOM 2690 O LEU A 269 23.350 7.125 9.438 1.00 31.72 O
ANISOU 2690 O LEU A 269 4283 4679 3089 -355 48 62 O
ATOM 2691 CB LEU A 269 25.505 9.243 8.291 1.00 34.20 C
ANISOU 2691 CB LEU A 269 4690 4794 3512 -606 124 123 C
ATOM 2692 CG LEU A 269 26.388 8.134 8.865 1.00 35.14 C
ANISOU 2692 CG LEU A 269 4660 5001 3689 -615 168 48 C
ATOM 2693 CD1 LEU A 269 26.314 6.884 8.004 1.00 33.16 C
ANISOU 2693 CD1 LEU A 269 4378 4849 3372 -622 261 59 C
ATOM 2694 CD2 LEU A 269 27.817 8.625 8.971 1.00 38.72 C
ANISOU 2694 CD2 LEU A 269 5042 5403 4267 -730 205 24 C
ATOM 2695 N MET A 270 22.737 9.228 9.973 1.00 32.84 N
ANISOU 2695 N MET A 270 4550 4656 3271 -299 -62 73 N
ATOM 2696 CA MET A 270 21.954 8.789 11.122 1.00 32.20 C
ANISOU 2696 CA MET A 270 4420 4635 3179 -179 -97 14 C
ATOM 2697 C MET A 270 20.829 7.861 10.688 1.00 31.55 C
ANISOU 2697 C MET A 270 4305 4645 3038 -122 -85 52 C
ATOM 2698 O MET A 270 20.652 6.773 11.247 1.00 30.81 O
ANISOU 2698 O MET A 270 4134 4644 2928 -90 -61 25 O
ATOM 2699 CB MET A 270 21.390 9.997 11.869 1.00 32.97 C
ANISOU 2699 CB MET A 270 4582 4637 3307 -96 -164 -23 C
ATOM 2700 CG MET A 270 22.439 10.888 12.504 1.00 35.81 C
ANISOU 2700 CG MET A 270 4976 4898 3732 -151 -198 -85 C
ATOM 2701 SD MET A 270 23.400 10.031 13.762 1.00 33.30 S
ANISOU 2701 SD MET A 270 4567 4671 3415 -166 -204 -176 S
ATOM 2702 CE MET A 270 22.102 9.380 14.810 1.00 33.15 C
ANISOU 2702 CE MET A 270 4534 4754 3307 -13 -201 -213 C
ATOM 2703 N TYR A 271 20.060 8.272 9.682 1.00 32.02 N
ANISOU 2703 N TYR A 271 4425 4672 3070 -114 -114 122 N
ATOM 2704 CA TYR A 271 18.939 7.457 9.239 1.00 35.16 C
ANISOU 2704 CA TYR A 271 4784 5150 3427 -66 -129 154 C
ATOM 2705 C TYR A 271 19.380 6.269 8.396 1.00 31.20 C
ANISOU 2705 C TYR A 271 4260 4724 2872 -153 -74 167 C
ATOM 2706 O TYR A 271 18.621 5.303 8.269 1.00 35.07 O
ANISOU 2706 O TYR A 271 4697 5289 3342 -127 -80 168 O
ATOM 2707 CB TYR A 271 17.931 8.326 8.485 1.00 32.64 C
ANISOU 2707 CB TYR A 271 4532 4766 3103 -18 -212 223 C
ATOM 2708 CG TYR A 271 17.146 9.222 9.418 1.00 33.18 C
ANISOU 2708 CG TYR A 271 4588 4777 3243 110 -259 189 C
ATOM 2709 CD1 TYR A 271 16.181 8.692 10.262 1.00 41.50 C
ANISOU 2709 CD1 TYR A 271 5538 5908 4322 211 -247 146 C
ATOM 2710 CD2 TYR A 271 17.385 10.589 9.475 1.00 40.57 C
ANISOU 2710 CD2 TYR A 271 5616 5572 4226 126 -302 196 C
ATOM 2711 CE1 TYR A 271 15.463 9.495 11.126 1.00 53.74 C
ANISOU 2711 CE1 TYR A 271 7072 7412 5934 335 -263 99 C
ATOM 2712 CE2 TYR A 271 16.670 11.404 10.340 1.00 43.31 C
ANISOU 2712 CE2 TYR A 271 5957 5855 4644 255 -336 144 C
ATOM 2713 CZ TYR A 271 15.709 10.849 11.163 1.00 44.54 C
ANISOU 2713 CZ TYR A 271 6004 6103 4814 364 -309 90 C
ATOM 2714 OH TYR A 271 14.989 11.645 12.028 1.00 46.73 O
ANISOU 2714 OH TYR A 271 6272 6325 5158 500 -317 23 O
ATOM 2715 N LEU A 272 20.588 6.306 7.833 1.00 31.41 N
ANISOU 2715 N LEU A 272 4321 4728 2886 -257 -12 169 N
ATOM 2716 CA LEU A 272 21.138 5.101 7.225 1.00 31.09 C
ANISOU 2716 CA LEU A 272 4246 4757 2810 -323 64 150 C
ATOM 2717 C LEU A 272 21.435 4.045 8.284 1.00 30.22 C
ANISOU 2717 C LEU A 272 4022 4704 2757 -287 91 86 C
ATOM 2718 O LEU A 272 21.196 2.852 8.065 1.00 29.84 O
ANISOU 2718 O LEU A 272 3932 4714 2694 -287 115 70 O
ATOM 2719 CB LEU A 272 22.399 5.440 6.431 1.00 32.41 C
ANISOU 2719 CB LEU A 272 4459 4890 2966 -438 150 161 C
ATOM 2720 CG LEU A 272 23.053 4.261 5.710 1.00 31.87 C
ANISOU 2720 CG LEU A 272 4359 4885 2864 -501 254 125 C
ATOM 2721 CD1 LEU A 272 22.046 3.585 4.794 1.00 34.46 C
ANISOU 2721 CD1 LEU A 272 4748 5261 3084 -493 224 143 C
ATOM 2722 CD2 LEU A 272 24.275 4.723 4.928 1.00 44.05 C
ANISOU 2722 CD2 LEU A 272 5938 6399 4402 -615 367 137 C
ATOM 2723 N ALA A 273 21.944 4.470 9.443 1.00 30.09 N
ANISOU 2723 N ALA A 273 3968 4664 2803 -257 75 51 N
ATOM 2724 CA ALA A 273 22.207 3.533 10.529 1.00 29.53 C
ANISOU 2724 CA ALA A 273 3808 4642 2769 -218 79 7 C
ATOM 2725 C ALA A 273 20.912 3.054 11.173 1.00 29.13 C
ANISOU 2725 C ALA A 273 3737 4641 2692 -131 48 18 C
ATOM 2726 O ALA A 273 20.802 1.886 11.563 1.00 28.74 O
ANISOU 2726 O ALA A 273 3630 4642 2650 -117 66 14 O
ATOM 2727 CB ALA A 273 23.117 4.182 11.571 1.00 29.81 C
ANISOU 2727 CB ALA A 273 3828 4640 2859 -216 48 -35 C
ATOM 2728 N ILE A 274 19.928 3.947 11.308 1.00 29.44 N
ANISOU 2728 N ILE A 274 3814 4657 2713 -73 6 34 N
ATOM 2729 CA ILE A 274 18.637 3.555 11.868 1.00 32.07 C
ANISOU 2729 CA ILE A 274 4103 5043 3038 7 -4 45 C
ATOM 2730 C ILE A 274 17.958 2.534 10.965 1.00 29.18 C
ANISOU 2730 C ILE A 274 3701 4723 2664 -23 1 79 C
ATOM 2731 O ILE A 274 17.403 1.534 11.436 1.00 28.97 O
ANISOU 2731 O ILE A 274 3608 4751 2650 -6 21 84 O
ATOM 2732 CB ILE A 274 17.754 4.797 12.090 1.00 30.02 C
ANISOU 2732 CB ILE A 274 3877 4740 2788 87 -44 45 C
ATOM 2733 CG1 ILE A 274 18.333 5.675 13.203 1.00 30.36 C
ANISOU 2733 CG1 ILE A 274 3962 4738 2836 124 -51 -14 C
ATOM 2734 CG2 ILE A 274 16.323 4.394 12.417 1.00 30.23 C
ANISOU 2734 CG2 ILE A 274 3830 4827 2828 164 -39 60 C
ATOM 2735 CD1 ILE A 274 17.667 7.034 13.318 1.00 36.26 C
ANISOU 2735 CD1 ILE A 274 4761 5406 3609 202 -89 -30 C
ATOM 2736 N VAL A 275 18.002 2.765 9.653 1.00 29.47 N
ANISOU 2736 N VAL A 275 3792 4733 2672 -78 -20 105 N
ATOM 2737 CA VAL A 275 17.413 1.823 8.708 1.00 29.55 C
ANISOU 2737 CA VAL A 275 3789 4782 2657 -117 -33 121 C
ATOM 2738 C VAL A 275 18.176 0.502 8.720 1.00 29.11 C
ANISOU 2738 C VAL A 275 3699 4749 2611 -170 30 85 C
ATOM 2739 O VAL A 275 17.574 -0.576 8.661 1.00 33.82 O
ANISOU 2739 O VAL A 275 4247 5378 3225 -178 26 82 O
ATOM 2740 CB VAL A 275 17.361 2.458 7.305 1.00 32.71 C
ANISOU 2740 CB VAL A 275 4288 5148 2990 -165 -78 158 C
ATOM 2741 CG1 VAL A 275 17.280 1.397 6.224 1.00 40.54 C
ANISOU 2741 CG1 VAL A 275 5303 6175 3925 -236 -76 146 C
ATOM 2742 CG2 VAL A 275 16.175 3.407 7.206 1.00 30.94 C
ANISOU 2742 CG2 VAL A 275 4074 4903 2780 -94 -174 206 C
ATOM 2743 N LEU A 276 19.506 0.561 8.828 1.00 30.46 N
ANISOU 2743 N LEU A 276 3883 4896 2794 -204 84 55 N
ATOM 2744 CA LEU A 276 20.299 -0.666 8.841 1.00 28.77 C
ANISOU 2744 CA LEU A 276 3626 4691 2615 -237 141 17 C
ATOM 2745 C LEU A 276 19.955 -1.541 10.040 1.00 28.41 C
ANISOU 2745 C LEU A 276 3507 4667 2620 -186 132 22 C
ATOM 2746 O LEU A 276 19.936 -2.773 9.932 1.00 28.42 O
ANISOU 2746 O LEU A 276 3476 4669 2654 -203 151 11 O
ATOM 2747 CB LEU A 276 21.790 -0.332 8.834 1.00 28.94 C
ANISOU 2747 CB LEU A 276 3643 4683 2670 -272 195 -15 C
ATOM 2748 CG LEU A 276 22.733 -1.538 8.821 1.00 34.27 C
ANISOU 2748 CG LEU A 276 4256 5356 3411 -289 255 -62 C
ATOM 2749 CD1 LEU A 276 22.436 -2.454 7.639 1.00 29.38 C
ANISOU 2749 CD1 LEU A 276 3670 4741 2751 -330 297 -92 C
ATOM 2750 CD2 LEU A 276 24.178 -1.077 8.790 1.00 38.45 C
ANISOU 2750 CD2 LEU A 276 4750 5861 3999 -324 308 -93 C
ATOM 2751 N SER A 277 19.679 -0.926 11.192 1.00 28.29 N
ANISOU 2751 N SER A 277 3478 4663 2607 -127 106 40 N
ATOM 2752 CA SER A 277 19.318 -1.715 12.366 1.00 28.21 C
ANISOU 2752 CA SER A 277 3421 4682 2616 -86 110 61 C
ATOM 2753 C SER A 277 17.967 -2.395 12.192 1.00 33.50 C
ANISOU 2753 C SER A 277 4054 5383 3293 -86 110 95 C
ATOM 2754 O SER A 277 17.748 -3.483 12.736 1.00 28.47 O
ANISOU 2754 O SER A 277 3377 4753 2686 -90 129 120 O
ATOM 2755 CB SER A 277 19.311 -0.834 13.615 1.00 28.34 C
ANISOU 2755 CB SER A 277 3454 4712 2603 -24 93 60 C
ATOM 2756 OG SER A 277 18.301 0.154 13.530 1.00 28.57 O
ANISOU 2756 OG SER A 277 3500 4749 2606 16 81 65 O
ATOM 2757 N HIS A 278 17.053 -1.777 11.441 1.00 28.59 N
ANISOU 2757 N HIS A 278 3438 4769 2654 -85 80 103 N
ATOM 2758 CA HIS A 278 15.745 -2.386 11.230 1.00 28.97 C
ANISOU 2758 CA HIS A 278 3426 4849 2734 -92 64 131 C
ATOM 2759 C HIS A 278 15.817 -3.550 10.252 1.00 35.20 C
ANISOU 2759 C HIS A 278 4217 5616 3542 -169 52 113 C
ATOM 2760 O HIS A 278 15.020 -4.490 10.355 1.00 33.66 O
ANISOU 2760 O HIS A 278 3961 5430 3398 -195 48 132 O
ATOM 2761 CB HIS A 278 14.750 -1.336 10.739 1.00 29.44 C
ANISOU 2761 CB HIS A 278 3479 4920 2788 -56 9 145 C
ATOM 2762 CG HIS A 278 14.482 -0.251 11.734 1.00 30.96 C
ANISOU 2762 CG HIS A 278 3664 5122 2979 33 27 147 C
ATOM 2763 ND1 HIS A 278 14.118 1.026 11.366 1.00 30.04 N
ANISOU 2763 ND1 HIS A 278 3577 4977 2859 83 -23 147 N
ATOM 2764 CD2 HIS A 278 14.528 -0.254 13.087 1.00 43.66 C
ANISOU 2764 CD2 HIS A 278 5253 6757 4580 82 88 143 C
ATOM 2765 CE1 HIS A 278 13.952 1.763 12.449 1.00 35.69 C
ANISOU 2765 CE1 HIS A 278 4286 5697 3579 165 13 128 C
ATOM 2766 NE2 HIS A 278 14.192 1.010 13.507 1.00 30.07 N
ANISOU 2766 NE2 HIS A 278 3550 5026 2851 163 83 123 N
ATOM 2767 N THR A 279 16.761 -3.514 9.306 1.00 29.00 N
ANISOU 2767 N THR A 279 3502 4799 2719 -211 56 71 N
ATOM 2768 CA THR A 279 16.908 -4.616 8.360 1.00 30.63 C
ANISOU 2768 CA THR A 279 3729 4979 2930 -277 58 29 C
ATOM 2769 C THR A 279 17.262 -5.924 9.050 1.00 29.31 C
ANISOU 2769 C THR A 279 3516 4779 2842 -283 99 24 C
ATOM 2770 O THR A 279 17.118 -6.990 8.444 1.00 29.79 O
ANISOU 2770 O THR A 279 3582 4804 2933 -332 94 -12 O
ATOM 2771 CB THR A 279 17.980 -4.298 7.314 1.00 29.49 C
ANISOU 2771 CB THR A 279 3671 4813 2721 -315 92 -22 C
ATOM 2772 OG1 THR A 279 19.246 -4.127 7.963 1.00 32.38 O
ANISOU 2772 OG1 THR A 279 4021 5160 3120 -292 156 -35 O
ATOM 2773 CG2 THR A 279 17.629 -3.036 6.546 1.00 29.79 C
ANISOU 2773 CG2 THR A 279 3779 4868 2671 -321 45 4 C
ATOM 2774 N ASN A 280 17.728 -5.867 10.299 1.00 28.95 N
ANISOU 2774 N ASN A 280 3439 4736 2826 -233 128 58 N
ATOM 2775 CA ASN A 280 18.041 -7.094 11.019 1.00 31.56 C
ANISOU 2775 CA ASN A 280 3737 5025 3228 -232 150 76 C
ATOM 2776 C ASN A 280 16.796 -7.945 11.235 1.00 31.99 C
ANISOU 2776 C ASN A 280 3747 5079 3331 -265 138 122 C
ATOM 2777 O ASN A 280 16.894 -9.172 11.342 1.00 30.64 O
ANISOU 2777 O ASN A 280 3566 4844 3232 -294 146 129 O
ATOM 2778 CB ASN A 280 18.709 -6.759 12.353 1.00 28.91 C
ANISOU 2778 CB ASN A 280 3395 4703 2888 -172 160 116 C
ATOM 2779 CG ASN A 280 19.204 -7.991 13.080 1.00 31.85 C
ANISOU 2779 CG ASN A 280 3751 5020 3329 -164 163 150 C
ATOM 2780 OD1 ASN A 280 18.692 -8.349 14.140 1.00 33.33 O
ANISOU 2780 OD1 ASN A 280 3930 5222 3511 -149 165 227 O
ATOM 2781 ND2 ASN A 280 20.198 -8.656 12.505 1.00 29.53 N
ANISOU 2781 ND2 ASN A 280 3457 4661 3103 -171 170 97 N
ATOM 2782 N SER A 281 15.621 -7.320 11.285 1.00 29.79 N
ANISOU 2782 N SER A 281 3429 4858 3030 -262 118 154 N
ATOM 2783 CA SER A 281 14.367 -8.051 11.405 1.00 30.52 C
ANISOU 2783 CA SER A 281 3450 4956 3190 -307 110 196 C
ATOM 2784 C SER A 281 13.953 -8.738 10.108 1.00 31.08 C
ANISOU 2784 C SER A 281 3527 4987 3297 -386 50 141 C
ATOM 2785 O SER A 281 12.916 -9.410 10.085 1.00 31.89 O
ANISOU 2785 O SER A 281 3560 5083 3476 -442 25 166 O
ATOM 2786 CB SER A 281 13.256 -7.109 11.875 1.00 34.58 C
ANISOU 2786 CB SER A 281 3895 5550 3692 -267 114 238 C
ATOM 2787 OG SER A 281 13.559 -6.556 13.147 1.00 40.38 O
ANISOU 2787 OG SER A 281 4640 6322 4381 -197 176 275 O
ATOM 2788 N VAL A 282 14.736 -8.601 9.040 1.00 35.03 N
ANISOU 2788 N VAL A 282 4110 5460 3741 -399 28 63 N
ATOM 2789 CA VAL A 282 14.444 -9.261 7.776 1.00 31.66 C
ANISOU 2789 CA VAL A 282 3722 4995 3313 -474 -29 -9 C
ATOM 2790 C VAL A 282 15.372 -10.440 7.508 1.00 31.96 C
ANISOU 2790 C VAL A 282 3811 4939 3394 -501 12 -76 C
ATOM 2791 O VAL A 282 14.970 -11.368 6.788 1.00 35.11 O
ANISOU 2791 O VAL A 282 4230 5280 3829 -570 -30 -135 O
ATOM 2792 CB VAL A 282 14.497 -8.257 6.602 1.00 31.71 C
ANISOU 2792 CB VAL A 282 3806 5043 3200 -477 -80 -52 C
ATOM 2793 CG1 VAL A 282 13.911 -8.861 5.342 1.00 36.11 C
ANISOU 2793 CG1 VAL A 282 4411 5579 3729 -559 -168 -120 C
ATOM 2794 CG2 VAL A 282 13.772 -6.965 6.965 1.00 38.67 C
ANISOU 2794 CG2 VAL A 282 4640 5995 4056 -423 -118 17 C
ATOM 2795 N VAL A 283 16.574 -10.460 8.085 1.00 32.67 N
ANISOU 2795 N VAL A 283 3915 5001 3496 -445 83 -76 N
ATOM 2796 CA VAL A 283 17.592 -11.393 7.616 1.00 31.90 C
ANISOU 2796 CA VAL A 283 3863 4814 3442 -450 126 -161 C
ATOM 2797 C VAL A 283 17.439 -12.790 8.221 1.00 32.58 C
ANISOU 2797 C VAL A 283 3918 4796 3664 -466 123 -136 C
ATOM 2798 O VAL A 283 17.765 -13.784 7.561 1.00 33.46 O
ANISOU 2798 O VAL A 283 4070 4810 3832 -493 130 -225 O
ATOM 2799 CB VAL A 283 18.992 -10.818 7.887 1.00 31.34 C
ANISOU 2799 CB VAL A 283 3798 4754 3355 -383 192 -176 C
ATOM 2800 CG1 VAL A 283 19.142 -9.472 7.201 1.00 30.93 C
ANISOU 2800 CG1 VAL A 283 3790 4783 3178 -386 200 -194 C
ATOM 2801 CG2 VAL A 283 19.234 -10.682 9.376 1.00 30.82 C
ANISOU 2801 CG2 VAL A 283 3673 4697 3339 -323 192 -76 C
ATOM 2802 N ASN A 284 16.958 -12.905 9.460 1.00 32.42 N
ANISOU 2802 N ASN A 284 3839 4786 3694 -452 119 -18 N
ATOM 2803 CA ASN A 284 16.914 -14.217 10.110 1.00 41.11 C
ANISOU 2803 CA ASN A 284 4925 5773 4921 -470 120 31 C
ATOM 2804 C ASN A 284 16.085 -15.242 9.345 1.00 38.15 C
ANISOU 2804 C ASN A 284 4559 5312 4624 -566 78 -21 C
ATOM 2805 O ASN A 284 16.562 -16.378 9.177 1.00 35.29 O
ANISOU 2805 O ASN A 284 4232 4813 4366 -575 81 -67 O
ATOM 2806 CB ASN A 284 16.425 -14.071 11.556 1.00 33.13 C
ANISOU 2806 CB ASN A 284 3867 4807 3914 -451 135 180 C
ATOM 2807 CG ASN A 284 17.387 -13.274 12.419 1.00 48.09 C
ANISOU 2807 CG ASN A 284 5773 6759 5741 -358 157 219 C
ATOM 2808 OD1 ASN A 284 18.492 -12.935 11.988 1.00 31.95 O
ANISOU 2808 OD1 ASN A 284 3750 4706 3681 -310 161 144 O
ATOM 2809 ND2 ASN A 284 16.976 -12.980 13.647 1.00 43.25 N
ANISOU 2809 ND2 ASN A 284 5143 6203 5087 -337 174 332 N
ATOM 2810 N PRO A 285 14.873 -14.939 8.860 1.00 38.34 N
ANISOU 2810 N PRO A 285 4548 5396 4621 -638 27 -23 N
ATOM 2811 CA PRO A 285 14.162 -15.940 8.047 1.00 35.99 C
ANISOU 2811 CA PRO A 285 4262 5008 4404 -741 -36 -93 C
ATOM 2812 C PRO A 285 14.938 -16.381 6.817 1.00 36.53 C
ANISOU 2812 C PRO A 285 4437 5000 4441 -745 -44 -258 C
ATOM 2813 O PRO A 285 14.780 -17.527 6.379 1.00 37.83 O
ANISOU 2813 O PRO A 285 4638 5034 4702 -808 -76 -330 O
ATOM 2814 CB PRO A 285 12.859 -15.222 7.673 1.00 36.12 C
ANISOU 2814 CB PRO A 285 4211 5134 4380 -797 -107 -74 C
ATOM 2815 CG PRO A 285 12.664 -14.222 8.753 1.00 35.13 C
ANISOU 2815 CG PRO A 285 4012 5123 4214 -728 -54 47 C
ATOM 2816 CD PRO A 285 14.038 -13.746 9.093 1.00 34.03 C
ANISOU 2816 CD PRO A 285 3941 4991 3998 -628 13 38 C
ATOM 2817 N PHE A 286 15.783 -15.514 6.249 1.00 35.77 N
ANISOU 2817 N PHE A 286 4398 4976 4217 -683 -5 -323 N
ATOM 2818 CA PHE A 286 16.596 -15.920 5.107 1.00 36.52 C
ANISOU 2818 CA PHE A 286 4597 5010 4268 -682 25 -484 C
ATOM 2819 C PHE A 286 17.717 -16.866 5.516 1.00 36.95 C
ANISOU 2819 C PHE A 286 4658 4932 4450 -619 100 -519 C
ATOM 2820 O PHE A 286 18.079 -17.762 4.744 1.00 38.22 O
ANISOU 2820 O PHE A 286 4888 4980 4652 -634 116 -656 O
ATOM 2821 CB PHE A 286 17.174 -14.693 4.400 1.00 35.84 C
ANISOU 2821 CB PHE A 286 4565 5042 4009 -646 65 -527 C
ATOM 2822 CG PHE A 286 16.201 -14.004 3.491 1.00 38.11 C
ANISOU 2822 CG PHE A 286 4898 5420 4162 -712 -28 -543 C
ATOM 2823 CD1 PHE A 286 16.041 -14.423 2.182 1.00 51.43 C
ANISOU 2823 CD1 PHE A 286 6701 7080 5760 -778 -71 -679 C
ATOM 2824 CD2 PHE A 286 15.445 -12.937 3.945 1.00 39.56 C
ANISOU 2824 CD2 PHE A 286 5015 5711 4306 -701 -82 -426 C
ATOM 2825 CE1 PHE A 286 15.144 -13.793 1.342 1.00 40.64 C
ANISOU 2825 CE1 PHE A 286 5385 5797 4261 -837 -187 -684 C
ATOM 2826 CE2 PHE A 286 14.549 -12.302 3.111 1.00 45.80 C
ANISOU 2826 CE2 PHE A 286 5838 6574 4990 -749 -190 -432 C
ATOM 2827 CZ PHE A 286 14.397 -12.731 1.807 1.00 46.40 C
ANISOU 2827 CZ PHE A 286 6032 6626 4972 -819 -253 -554 C
ATOM 2828 N ILE A 287 18.279 -16.686 6.713 1.00 36.14 N
ANISOU 2828 N ILE A 287 4487 4835 4409 -543 137 -404 N
ATOM 2829 CA ILE A 287 19.321 -17.594 7.182 1.00 36.76 C
ANISOU 2829 CA ILE A 287 4559 4780 4629 -471 180 -418 C
ATOM 2830 C ILE A 287 18.756 -18.997 7.375 1.00 38.13 C
ANISOU 2830 C ILE A 287 4747 4785 4956 -525 132 -408 C
ATOM 2831 O ILE A 287 19.378 -19.991 6.978 1.00 39.38 O
ANISOU 2831 O ILE A 287 4946 4790 5226 -498 154 -511 O
ATOM 2832 CB ILE A 287 19.963 -17.053 8.473 1.00 35.80 C
ANISOU 2832 CB ILE A 287 4370 4709 4524 -384 195 -283 C
ATOM 2833 CG1 ILE A 287 20.539 -15.655 8.238 1.00 34.65 C
ANISOU 2833 CG1 ILE A 287 4212 4711 4245 -345 237 -304 C
ATOM 2834 CG2 ILE A 287 21.054 -17.992 8.963 1.00 36.69 C
ANISOU 2834 CG2 ILE A 287 4466 4680 4795 -300 211 -287 C
ATOM 2835 CD1 ILE A 287 21.610 -15.608 7.167 1.00 40.86 C
ANISOU 2835 CD1 ILE A 287 5026 5481 5017 -315 317 -457 C
ATOM 2836 N TYR A 288 17.565 -19.100 7.975 1.00 38.12 N
ANISOU 2836 N TYR A 288 4708 4800 4977 -603 76 -286 N
ATOM 2837 CA TYR A 288 16.933 -20.404 8.153 1.00 39.62 C
ANISOU 2837 CA TYR A 288 4907 4823 5322 -681 31 -262 C
ATOM 2838 C TYR A 288 16.677 -21.079 6.813 1.00 40.94 C
ANISOU 2838 C TYR A 288 5151 4896 5511 -754 -6 -448 C
ATOM 2839 O TYR A 288 16.931 -22.279 6.655 1.00 42.45 O
ANISOU 2839 O TYR A 288 5389 4892 5846 -764 -15 -515 O
ATOM 2840 CB TYR A 288 15.622 -20.259 8.926 1.00 39.55 C
ANISOU 2840 CB TYR A 288 4826 4876 5325 -770 -3 -105 C
ATOM 2841 CG TYR A 288 15.741 -19.485 10.216 1.00 38.42 C
ANISOU 2841 CG TYR A 288 4628 4849 5120 -704 40 63 C
ATOM 2842 CD1 TYR A 288 16.786 -19.718 11.097 1.00 38.33 C
ANISOU 2842 CD1 TYR A 288 4637 4782 5145 -606 68 135 C
ATOM 2843 CD2 TYR A 288 14.808 -18.510 10.549 1.00 37.65 C
ANISOU 2843 CD2 TYR A 288 4462 4915 4928 -735 45 140 C
ATOM 2844 CE1 TYR A 288 16.894 -19.010 12.275 1.00 39.90 C
ANISOU 2844 CE1 TYR A 288 4807 5088 5263 -552 93 276 C
ATOM 2845 CE2 TYR A 288 14.912 -17.792 11.722 1.00 36.84 C
ANISOU 2845 CE2 TYR A 288 4327 4916 4754 -672 92 271 C
ATOM 2846 CZ TYR A 288 15.956 -18.044 12.580 1.00 36.78 C
ANISOU 2846 CZ TYR A 288 4360 4856 4760 -586 113 337 C
ATOM 2847 OH TYR A 288 16.061 -17.332 13.752 1.00 36.19 O
ANISOU 2847 OH TYR A 288 4274 4886 4592 -530 145 456 O
ATOM 2848 N ALA A 289 16.177 -20.322 5.834 1.00 40.62 N
ANISOU 2848 N ALA A 289 5134 4980 5320 -804 -37 -537 N
ATOM 2849 CA ALA A 289 15.849 -20.906 4.539 1.00 42.10 C
ANISOU 2849 CA ALA A 289 5413 5094 5489 -884 -91 -719 C
ATOM 2850 C ALA A 289 17.091 -21.383 3.797 1.00 42.91 C
ANISOU 2850 C ALA A 289 5615 5100 5588 -807 -10 -897 C
ATOM 2851 O ALA A 289 17.026 -22.367 3.053 1.00 44.67 O
ANISOU 2851 O ALA A 289 5924 5176 5870 -854 -37 -1049 O
ATOM 2852 CB ALA A 289 15.079 -19.897 3.690 1.00 41.71 C
ANISOU 2852 CB ALA A 289 5379 5213 5257 -944 -159 -755 C
ATOM 2853 N TYR A 290 18.227 -20.715 3.990 1.00 41.87 N
ANISOU 2853 N TYR A 290 5466 5043 5399 -690 93 -889 N
ATOM 2854 CA TYR A 290 19.431 -21.065 3.248 1.00 46.68 C
ANISOU 2854 CA TYR A 290 6143 5583 6010 -611 197 -1064 C
ATOM 2855 C TYR A 290 20.309 -22.084 3.963 1.00 49.86 C
ANISOU 2855 C TYR A 290 6506 5801 6636 -515 240 -1054 C
ATOM 2856 O TYR A 290 21.045 -22.823 3.299 1.00 45.15 O
ANISOU 2856 O TYR A 290 5969 5079 6108 -464 306 -1227 O
ATOM 2857 CB TYR A 290 20.254 -19.807 2.950 1.00 44.32 C
ANISOU 2857 CB TYR A 290 5833 5456 5549 -546 294 -1073 C
ATOM 2858 CG TYR A 290 19.787 -19.048 1.726 1.00 66.12 C
ANISOU 2858 CG TYR A 290 8696 8348 8078 -622 283 -1164 C
ATOM 2859 CD1 TYR A 290 20.220 -19.407 0.457 1.00 57.17 C
ANISOU 2859 CD1 TYR A 290 7692 7181 6849 -634 352 -1371 C
ATOM 2860 CD2 TYR A 290 18.914 -17.973 1.840 1.00 62.74 C
ANISOU 2860 CD2 TYR A 290 8245 8073 7520 -676 201 -1044 C
ATOM 2861 CE1 TYR A 290 19.797 -18.719 -0.665 1.00 55.08 C
ANISOU 2861 CE1 TYR A 290 7546 7038 6344 -707 330 -1440 C
ATOM 2862 CE2 TYR A 290 18.485 -17.278 0.724 1.00 60.39 C
ANISOU 2862 CE2 TYR A 290 8050 7884 7011 -739 167 -1110 C
ATOM 2863 CZ TYR A 290 18.930 -17.657 -0.526 1.00 74.18 C
ANISOU 2863 CZ TYR A 290 9940 9601 8645 -760 226 -1301 C
ATOM 2864 OH TYR A 290 18.509 -16.973 -1.644 1.00 80.50 O
ANISOU 2864 OH TYR A 290 10869 10512 9207 -826 182 -1354 O
ATOM 2865 N ARG A 291 20.252 -22.157 5.294 1.00 42.87 N
ANISOU 2865 N ARG A 291 5532 4893 5864 -482 201 -860 N
ATOM 2866 CA ARG A 291 21.193 -22.977 6.040 1.00 49.78 C
ANISOU 2866 CA ARG A 291 6369 5606 6938 -372 223 -823 C
ATOM 2867 C ARG A 291 20.564 -24.107 6.843 1.00 47.55 C
ANISOU 2867 C ARG A 291 6094 5138 6836 -418 138 -705 C
ATOM 2868 O ARG A 291 21.301 -24.981 7.315 1.00 45.91 O
ANISOU 2868 O ARG A 291 5880 4752 6813 -329 138 -688 O
ATOM 2869 CB ARG A 291 22.026 -22.101 6.988 1.00 42.26 C
ANISOU 2869 CB ARG A 291 5320 4774 5964 -269 252 -690 C
ATOM 2870 CG ARG A 291 22.934 -21.121 6.266 1.00 41.63 C
ANISOU 2870 CG ARG A 291 5220 4835 5763 -212 354 -805 C
ATOM 2871 CD ARG A 291 24.001 -20.592 7.201 1.00 52.87 C
ANISOU 2871 CD ARG A 291 6536 6309 7242 -99 370 -706 C
ATOM 2872 NE ARG A 291 24.829 -21.671 7.725 1.00 52.26 N
ANISOU 2872 NE ARG A 291 6417 6044 7394 8 354 -702 N
ATOM 2873 CZ ARG A 291 25.946 -22.101 7.154 1.00 55.40 C
ANISOU 2873 CZ ARG A 291 6778 6356 7914 107 440 -854 C
ATOM 2874 NH1 ARG A 291 26.409 -21.552 6.043 1.00 53.48 N
ANISOU 2874 NH1 ARG A 291 6542 6208 7570 103 568 -1021 N
ATOM 2875 NH2 ARG A 291 26.615 -23.105 7.713 1.00 45.24 N
ANISOU 2875 NH2 ARG A 291 5448 4883 6859 215 401 -833 N
ATOM 2876 N ILE A 292 19.246 -24.126 7.014 1.00 44.59 N
ANISOU 2876 N ILE A 292 5724 4791 6428 -554 66 -616 N
ATOM 2877 CA ILE A 292 18.567 -25.157 7.794 1.00 45.78 C
ANISOU 2877 CA ILE A 292 5876 4771 6747 -624 0 -483 C
ATOM 2878 C ILE A 292 17.566 -25.846 6.876 1.00 47.21 C
ANISOU 2878 C ILE A 292 6119 4852 6968 -770 -59 -607 C
ATOM 2879 O ILE A 292 16.557 -25.246 6.483 1.00 46.64 O
ANISOU 2879 O ILE A 292 6024 4920 6777 -880 -100 -609 O
ATOM 2880 CB ILE A 292 17.878 -24.578 9.038 1.00 44.63 C
ANISOU 2880 CB ILE A 292 5658 4752 6548 -664 -18 -237 C
ATOM 2881 CG1 ILE A 292 18.870 -23.749 9.855 1.00 43.25 C
ANISOU 2881 CG1 ILE A 292 5437 4698 6298 -526 23 -142 C
ATOM 2882 CG2 ILE A 292 17.307 -25.695 9.895 1.00 46.17 C
ANISOU 2882 CG2 ILE A 292 5865 4761 6918 -737 -62 -81 C
ATOM 2883 CD1 ILE A 292 18.247 -23.033 11.039 1.00 42.18 C
ANISOU 2883 CD1 ILE A 292 5249 4711 6067 -554 19 71 C
ATOM 2884 N ARG A 293 17.841 -27.110 6.540 1.00 52.16 N
ANISOU 2884 N ARG A 293 6819 5224 7774 -769 -78 -714 N
ATOM 2885 CA ARG A 293 17.008 -27.824 5.576 1.00 50.98 C
ANISOU 2885 CA ARG A 293 6745 4957 7668 -907 -147 -871 C
ATOM 2886 C ARG A 293 15.584 -28.006 6.089 1.00 51.30 C
ANISOU 2886 C ARG A 293 6729 4998 7766 -1082 -233 -714 C
ATOM 2887 O ARG A 293 14.623 -27.924 5.315 1.00 54.97 O
ANISOU 2887 O ARG A 293 7201 5509 8176 -1217 -307 -806 O
ATOM 2888 CB ARG A 293 17.634 -29.179 5.241 1.00 53.35 C
ANISOU 2888 CB ARG A 293 7139 4956 8176 -861 -147 -1015 C
ATOM 2889 CG ARG A 293 16.814 -30.005 4.259 1.00 61.39 C
ANISOU 2889 CG ARG A 293 8253 5821 9250 -1009 -231 -1198 C
ATOM 2890 CD ARG A 293 17.408 -31.387 4.030 1.00 60.91 C
ANISOU 2890 CD ARG A 293 8291 5430 9420 -958 -232 -1338 C
ATOM 2891 NE ARG A 293 18.665 -31.339 3.292 1.00 87.65 N
ANISOU 2891 NE ARG A 293 11737 8806 12761 -790 -123 -1556 N
ATOM 2892 CZ ARG A 293 19.864 -31.467 3.844 1.00 82.45 C
ANISOU 2892 CZ ARG A 293 11034 8081 12213 -605 -41 -1514 C
ATOM 2893 NH1 ARG A 293 20.010 -31.657 5.145 1.00 84.51 N
ANISOU 2893 NH1 ARG A 293 11217 8277 12615 -559 -72 -1259 N
ATOM 2894 NH2 ARG A 293 20.944 -31.408 3.070 1.00 87.44 N
ANISOU 2894 NH2 ARG A 293 11699 8713 12810 -465 74 -1734 N
ATOM 2895 N GLU A 294 15.427 -28.253 7.392 1.00 52.51 N
ANISOU 2895 N GLU A 294 6822 5104 8027 -1085 -224 -473 N
ATOM 2896 CA GLU A 294 14.091 -28.466 7.939 1.00 53.86 C
ANISOU 2896 CA GLU A 294 6923 5274 8267 -1257 -273 -313 C
ATOM 2897 C GLU A 294 13.244 -27.202 7.840 1.00 54.47 C
ANISOU 2897 C GLU A 294 6898 5637 8159 -1312 -275 -271 C
ATOM 2898 O GLU A 294 12.035 -27.279 7.593 1.00 50.97 O
ANISOU 2898 O GLU A 294 6394 5218 7755 -1469 -340 -262 O
ATOM 2899 CB GLU A 294 14.182 -28.944 9.387 1.00 52.26 C
ANISOU 2899 CB GLU A 294 6698 4974 8183 -1242 -239 -52 C
ATOM 2900 CG GLU A 294 12.916 -29.614 9.886 1.00 53.88 C
ANISOU 2900 CG GLU A 294 6857 5084 8531 -1437 -272 98 C
ATOM 2901 CD GLU A 294 12.618 -30.910 9.155 1.00 62.73 C
ANISOU 2901 CD GLU A 294 8054 5918 9864 -1552 -354 -39 C
ATOM 2902 OE1 GLU A 294 13.543 -31.736 9.010 1.00 78.85 O
ANISOU 2902 OE1 GLU A 294 10203 7732 12026 -1458 -364 -119 O
ATOM 2903 OE2 GLU A 294 11.463 -31.099 8.716 1.00 57.50 O
ANISOU 2903 OE2 GLU A 294 7337 5250 9260 -1735 -417 -74 O
ATOM 2904 N PHE A 295 13.858 -26.029 8.026 1.00 48.04 N
ANISOU 2904 N PHE A 295 6057 5033 7162 -1184 -212 -247 N
ATOM 2905 CA PHE A 295 13.130 -24.780 7.816 1.00 46.59 C
ANISOU 2905 CA PHE A 295 5791 5104 6808 -1215 -220 -229 C
ATOM 2906 C PHE A 295 12.832 -24.556 6.338 1.00 46.97 C
ANISOU 2906 C PHE A 295 5888 5195 6764 -1268 -297 -447 C
ATOM 2907 O PHE A 295 11.741 -24.094 5.982 1.00 47.07 O
ANISOU 2907 O PHE A 295 5831 5321 6733 -1370 -369 -444 O
ATOM 2908 CB PHE A 295 13.920 -23.596 8.382 1.00 49.42 C
ANISOU 2908 CB PHE A 295 6124 5648 7004 -1068 -140 -156 C
ATOM 2909 CG PHE A 295 13.555 -23.237 9.796 1.00 43.83 C
ANISOU 2909 CG PHE A 295 5334 5024 6294 -1062 -89 77 C
ATOM 2910 CD1 PHE A 295 12.400 -22.520 10.069 1.00 43.43 C
ANISOU 2910 CD1 PHE A 295 5178 5135 6189 -1137 -88 164 C
ATOM 2911 CD2 PHE A 295 14.372 -23.608 10.853 1.00 43.87 C
ANISOU 2911 CD2 PHE A 295 5372 4951 6347 -974 -44 204 C
ATOM 2912 CE1 PHE A 295 12.063 -22.188 11.370 1.00 43.12 C
ANISOU 2912 CE1 PHE A 295 5075 5180 6130 -1128 -16 363 C
ATOM 2913 CE2 PHE A 295 14.040 -23.279 12.156 1.00 43.57 C
ANISOU 2913 CE2 PHE A 295 5286 4998 6269 -972 5 413 C
ATOM 2914 CZ PHE A 295 12.886 -22.568 12.415 1.00 43.20 C
ANISOU 2914 CZ PHE A 295 5143 5115 6154 -1050 33 487 C
ATOM 2915 N ARG A 296 13.787 -24.879 5.463 1.00 47.42 N
ANISOU 2915 N ARG A 296 6065 5165 6787 -1198 -282 -639 N
ATOM 2916 CA ARG A 296 13.602 -24.624 4.038 1.00 47.96 C
ANISOU 2916 CA ARG A 296 6215 5287 6720 -1241 -344 -849 C
ATOM 2917 C ARG A 296 12.509 -25.508 3.450 1.00 50.11 C
ANISOU 2917 C ARG A 296 6506 5432 7103 -1414 -478 -934 C
ATOM 2918 O ARG A 296 11.682 -25.038 2.660 1.00 50.44 O
ANISOU 2918 O ARG A 296 6542 5585 7038 -1503 -584 -1003 O
ATOM 2919 CB ARG A 296 14.920 -24.832 3.293 1.00 48.28 C
ANISOU 2919 CB ARG A 296 6384 5261 6700 -1125 -264 -1039 C
ATOM 2920 CG ARG A 296 14.813 -24.657 1.788 1.00 50.55 C
ANISOU 2920 CG ARG A 296 6795 5596 6817 -1171 -310 -1267 C
ATOM 2921 CD ARG A 296 16.170 -24.763 1.112 1.00 55.82 C
ANISOU 2921 CD ARG A 296 7575 6222 7411 -1048 -185 -1448 C
ATOM 2922 NE ARG A 296 16.806 -26.058 1.327 1.00 63.83 N
ANISOU 2922 NE ARG A 296 8629 6980 8642 -998 -142 -1526 N
ATOM 2923 CZ ARG A 296 17.804 -26.275 2.174 1.00 52.60 C
ANISOU 2923 CZ ARG A 296 7150 5484 7353 -864 -45 -1443 C
ATOM 2924 NH1 ARG A 296 18.310 -25.300 2.912 1.00 48.80 N
ANISOU 2924 NH1 ARG A 296 6570 5166 6806 -773 21 -1288 N
ATOM 2925 NH2 ARG A 296 18.309 -27.501 2.281 1.00 52.54 N
ANISOU 2925 NH2 ARG A 296 7186 5221 7557 -817 -28 -1522 N
ATOM 2926 N GLN A 297 12.491 -26.790 3.822 1.00 51.80 N
ANISOU 2926 N GLN A 297 6742 5400 7538 -1465 -490 -927 N
ATOM 2927 CA GLN A 297 11.472 -27.698 3.305 1.00 54.11 C
ANISOU 2927 CA GLN A 297 7050 5544 7966 -1645 -624 -1010 C
ATOM 2928 C GLN A 297 10.085 -27.312 3.799 1.00 54.05 C
ANISOU 2928 C GLN A 297 6872 5654 8009 -1784 -698 -842 C
ATOM 2929 O GLN A 297 9.103 -27.412 3.053 1.00 55.42 O
ANISOU 2929 O GLN A 297 7022 5839 8195 -1927 -840 -933 O
ATOM 2930 CB GLN A 297 11.804 -29.136 3.699 1.00 56.03 C
ANISOU 2930 CB GLN A 297 7354 5476 8457 -1666 -612 -1017 C
ATOM 2931 CG GLN A 297 13.050 -29.687 3.026 1.00 62.54 C
ANISOU 2931 CG GLN A 297 8340 6150 9274 -1538 -556 -1232 C
ATOM 2932 CD GLN A 297 13.410 -31.078 3.511 1.00 74.65 C
ANISOU 2932 CD GLN A 297 9929 7357 11078 -1535 -548 -1220 C
ATOM 2933 OE1 GLN A 297 13.354 -31.365 4.707 1.00 70.33 O
ANISOU 2933 OE1 GLN A 297 9306 6739 10676 -1533 -517 -986 O
ATOM 2934 NE2 GLN A 297 13.781 -31.951 2.581 1.00 67.66 N
ANISOU 2934 NE2 GLN A 297 9188 6264 10255 -1533 -577 -1473 N
ATOM 2935 N THR A 298 9.982 -26.866 5.052 1.00 52.70 N
ANISOU 2935 N THR A 298 6577 5575 7869 -1744 -604 -604 N
ATOM 2936 CA THR A 298 8.693 -26.419 5.565 1.00 57.74 C
ANISOU 2936 CA THR A 298 7038 6346 8556 -1859 -638 -447 C
ATOM 2937 C THR A 298 8.259 -25.116 4.901 1.00 53.68 C
ANISOU 2937 C THR A 298 6467 6084 7844 -1832 -698 -500 C
ATOM 2938 O THR A 298 7.065 -24.906 4.656 1.00 52.43 O
ANISOU 2938 O THR A 298 6183 6001 7735 -1953 -803 -483 O
ATOM 2939 CB THR A 298 8.762 -26.260 7.085 1.00 51.81 C
ANISOU 2939 CB THR A 298 6195 5633 7856 -1812 -500 -191 C
ATOM 2940 OG1 THR A 298 9.278 -27.465 7.662 1.00 53.07 O
ANISOU 2940 OG1 THR A 298 6434 5544 8185 -1821 -459 -133 O
ATOM 2941 CG2 THR A 298 7.372 -25.992 7.655 1.00 52.43 C
ANISOU 2941 CG2 THR A 298 6079 5820 8023 -1945 -506 -36 C
ATOM 2942 N PHE A 299 9.213 -24.230 4.601 1.00 49.68 N
ANISOU 2942 N PHE A 299 6045 5702 7128 -1676 -638 -557 N
ATOM 2943 CA PHE A 299 8.884 -23.010 3.869 1.00 48.75 C
ANISOU 2943 CA PHE A 299 5909 5798 6817 -1647 -704 -608 C
ATOM 2944 C PHE A 299 8.311 -23.332 2.495 1.00 50.59 C
ANISOU 2944 C PHE A 299 6215 5994 7013 -1760 -881 -801 C
ATOM 2945 O PHE A 299 7.357 -22.686 2.047 1.00 50.94 O
ANISOU 2945 O PHE A 299 6175 6172 7009 -1821 -1008 -796 O
ATOM 2946 CB PHE A 299 10.120 -22.121 3.735 1.00 46.79 C
ANISOU 2946 CB PHE A 299 5760 5655 6363 -1476 -600 -642 C
ATOM 2947 CG PHE A 299 10.545 -21.471 5.018 1.00 44.94 C
ANISOU 2947 CG PHE A 299 5444 5511 6121 -1366 -465 -457 C
ATOM 2948 CD1 PHE A 299 9.696 -21.434 6.110 1.00 44.96 C
ANISOU 2948 CD1 PHE A 299 5294 5550 6238 -1414 -438 -274 C
ATOM 2949 CD2 PHE A 299 11.798 -20.894 5.129 1.00 43.42 C
ANISOU 2949 CD2 PHE A 299 5325 5368 5803 -1221 -362 -472 C
ATOM 2950 CE1 PHE A 299 10.088 -20.837 7.290 1.00 43.50 C
ANISOU 2950 CE1 PHE A 299 5060 5451 6018 -1314 -317 -117 C
ATOM 2951 CE2 PHE A 299 12.197 -20.294 6.305 1.00 41.92 C
ANISOU 2951 CE2 PHE A 299 5072 5258 5599 -1126 -261 -315 C
ATOM 2952 CZ PHE A 299 11.340 -20.265 7.388 1.00 43.73 C
ANISOU 2952 CZ PHE A 299 5174 5523 5917 -1170 -242 -141 C
ATOM 2953 N ARG A 300 8.883 -24.324 1.808 1.00 51.99 N
ANISOU 2953 N ARG A 300 6553 5988 7212 -1785 -902 -978 N
ATOM 2954 CA ARG A 300 8.332 -24.748 0.524 1.00 54.12 C
ANISOU 2954 CA ARG A 300 6918 6206 7441 -1905 -1081 -1179 C
ATOM 2955 C ARG A 300 6.919 -25.291 0.692 1.00 55.98 C
ANISOU 2955 C ARG A 300 6998 6383 7887 -2092 -1233 -1124 C
ATOM 2956 O ARG A 300 6.005 -24.923 -0.055 1.00 61.12 O
ANISOU 2956 O ARG A 300 7607 7129 8486 -2183 -1413 -1180 O
ATOM 2957 CB ARG A 300 9.229 -25.806 -0.120 1.00 58.98 C
ANISOU 2957 CB ARG A 300 7737 6610 8064 -1890 -1050 -1390 C
ATOM 2958 CG ARG A 300 10.629 -25.342 -0.488 1.00 58.08 C
ANISOU 2958 CG ARG A 300 7769 6550 7751 -1718 -900 -1483 C
ATOM 2959 CD ARG A 300 11.205 -26.230 -1.588 1.00 74.35 C
ANISOU 2959 CD ARG A 300 10041 8445 9761 -1729 -913 -1758 C
ATOM 2960 NE ARG A 300 12.663 -26.241 -1.601 1.00 79.60 N
ANISOU 2960 NE ARG A 300 10804 9076 10363 -1563 -720 -1832 N
ATOM 2961 CZ ARG A 300 13.408 -27.188 -1.046 1.00 80.37 C
ANISOU 2961 CZ ARG A 300 10913 8965 10658 -1495 -618 -1846 C
ATOM 2962 NH1 ARG A 300 12.863 -28.217 -0.418 1.00 66.76 N
ANISOU 2962 NH1 ARG A 300 9133 7037 9196 -1584 -683 -1782 N
ATOM 2963 NH2 ARG A 300 14.733 -27.102 -1.125 1.00 78.26 N
ANISOU 2963 NH2 ARG A 300 10710 8689 10337 -1336 -449 -1921 N
ATOM 2964 N LYS A 301 6.725 -26.174 1.676 1.00 61.44 N
ANISOU 2964 N LYS A 301 7600 6915 8828 -2155 -1167 -1004 N
ATOM 2965 CA LYS A 301 5.415 -26.780 1.897 1.00 58.65 C
ANISOU 2965 CA LYS A 301 7086 6489 8710 -2352 -1286 -941 C
ATOM 2966 C LYS A 301 4.359 -25.724 2.201 1.00 60.75 C
ANISOU 2966 C LYS A 301 7127 6989 8968 -2377 -1331 -796 C
ATOM 2967 O LYS A 301 3.218 -25.823 1.733 1.00 59.88 O
ANISOU 2967 O LYS A 301 6896 6897 8959 -2526 -1509 -830 O
ATOM 2968 CB LYS A 301 5.503 -27.801 3.032 1.00 59.31 C
ANISOU 2968 CB LYS A 301 7123 6372 9042 -2402 -1167 -795 C
ATOM 2969 CG LYS A 301 4.174 -28.398 3.455 1.00 61.46 C
ANISOU 2969 CG LYS A 301 7201 6571 9579 -2615 -1243 -687 C
ATOM 2970 CD LYS A 301 3.606 -29.308 2.383 1.00 74.10 C
ANISOU 2970 CD LYS A 301 8863 7997 11293 -2794 -1455 -895 C
ATOM 2971 CE LYS A 301 2.268 -29.891 2.811 1.00 84.24 C
ANISOU 2971 CE LYS A 301 9928 9209 12871 -3023 -1532 -782 C
ATOM 2972 NZ LYS A 301 1.706 -30.814 1.785 1.00 89.51 N
ANISOU 2972 NZ LYS A 301 10654 9689 13666 -3214 -1762 -993 N
ATOM 2973 N ILE A 302 4.721 -24.701 2.977 1.00 55.60 N
ANISOU 2973 N ILE A 302 6411 6510 8206 -2228 -1181 -644 N
ATOM 2974 CA ILE A 302 3.772 -23.638 3.294 1.00 55.07 C
ANISOU 2974 CA ILE A 302 6132 6658 8133 -2224 -1207 -517 C
ATOM 2975 C ILE A 302 3.447 -22.821 2.050 1.00 57.67 C
ANISOU 2975 C ILE A 302 6501 7124 8286 -2210 -1397 -650 C
ATOM 2976 O ILE A 302 2.280 -22.509 1.784 1.00 59.21 O
ANISOU 2976 O ILE A 302 6524 7406 8567 -2298 -1549 -629 O
ATOM 2977 CB ILE A 302 4.324 -22.748 4.423 1.00 53.33 C
ANISOU 2977 CB ILE A 302 5866 6572 7824 -2061 -999 -344 C
ATOM 2978 CG1 ILE A 302 4.401 -23.531 5.733 1.00 52.83 C
ANISOU 2978 CG1 ILE A 302 5745 6392 7935 -2097 -835 -179 C
ATOM 2979 CG2 ILE A 302 3.468 -21.506 4.593 1.00 52.00 C
ANISOU 2979 CG2 ILE A 302 5512 6628 7620 -2020 -1025 -252 C
ATOM 2980 CD1 ILE A 302 5.024 -22.747 6.869 1.00 50.65 C
ANISOU 2980 CD1 ILE A 302 5457 6235 7551 -1940 -643 -22 C
ATOM 2981 N ILE A 303 4.466 -22.473 1.262 1.00 54.29 N
ANISOU 2981 N ILE A 303 6296 6716 7615 -2101 -1393 -782 N
ATOM 2982 CA ILE A 303 4.268 -21.538 0.159 1.00 57.38 C
ANISOU 2982 CA ILE A 303 6754 7256 7793 -2068 -1550 -873 C
ATOM 2983 C ILE A 303 3.555 -22.213 -1.008 1.00 70.00 C
ANISOU 2983 C ILE A 303 8409 8775 9413 -2227 -1802 -1046 C
ATOM 2984 O ILE A 303 2.644 -21.633 -1.610 1.00 81.66 O
ANISOU 2984 O ILE A 303 9803 10367 10857 -2274 -2004 -1053 O
ATOM 2985 CB ILE A 303 5.617 -20.928 -0.264 1.00 60.45 C
ANISOU 2985 CB ILE A 303 7363 7696 7908 -1911 -1436 -943 C
ATOM 2986 CG1 ILE A 303 6.134 -19.993 0.832 1.00 53.63 C
ANISOU 2986 CG1 ILE A 303 6416 6947 7015 -1760 -1240 -767 C
ATOM 2987 CG2 ILE A 303 5.483 -20.182 -1.583 1.00 72.22 C
ANISOU 2987 CG2 ILE A 303 8984 9302 9155 -1904 -1606 -1055 C
ATOM 2988 CD1 ILE A 303 7.628 -19.759 0.793 1.00 50.20 C
ANISOU 2988 CD1 ILE A 303 6160 6504 6409 -1624 -1075 -815 C
ATOM 2989 N ARG A 304 3.943 -23.447 -1.342 1.00 67.35 N
ANISOU 2989 N ARG A 304 8217 8234 9141 -2310 -1810 -1193 N
ATOM 2990 CA ARG A 304 3.318 -24.121 -2.478 1.00 61.48 C
ANISOU 2990 CA ARG A 304 7555 7402 8401 -2466 -2059 -1384 C
ATOM 2991 C ARG A 304 1.869 -24.493 -2.190 1.00 77.37 C
ANISOU 2991 C ARG A 304 9308 9392 10696 -2644 -2226 -1309 C
ATOM 2992 O ARG A 304 1.072 -24.639 -3.124 1.00 99.94 O
ANISOU 2992 O ARG A 304 12169 12254 13551 -2769 -2490 -1430 O
ATOM 2993 CB ARG A 304 4.114 -25.369 -2.868 1.00 74.91 C
ANISOU 2993 CB ARG A 304 9478 8868 10117 -2504 -2013 -1575 C
ATOM 2994 CG ARG A 304 3.986 -26.535 -1.899 1.00 73.88 C
ANISOU 2994 CG ARG A 304 9245 8519 10307 -2592 -1922 -1501 C
ATOM 2995 CD ARG A 304 4.434 -27.840 -2.542 1.00 83.64 C
ANISOU 2995 CD ARG A 304 10692 9494 11593 -2668 -1966 -1729 C
ATOM 2996 NE ARG A 304 3.473 -28.322 -3.529 1.00 92.38 N
ANISOU 2996 NE ARG A 304 11823 10541 12737 -2856 -2246 -1898 N
ATOM 2997 CZ ARG A 304 2.585 -29.282 -3.305 1.00106.36 C
ANISOU 2997 CZ ARG A 304 13472 12137 14802 -3052 -2367 -1896 C
ATOM 2998 NH1 ARG A 304 2.517 -29.902 -2.138 1.00114.86 N
ANISOU 2998 NH1 ARG A 304 14408 13075 16157 -3091 -2223 -1724 N
ATOM 2999 NH2 ARG A 304 1.746 -29.630 -4.276 1.00 99.73 N
ANISOU 2999 NH2 ARG A 304 12659 11257 13975 -3221 -2647 -2066 N
ATOM 3000 N SER A 305 1.507 -24.646 -0.916 1.00 73.48 N
ANISOU 3000 N SER A 305 8591 8881 10446 -2662 -2079 -1111 N
ATOM 3001 CA SER A 305 0.145 -25.038 -0.571 1.00 75.51 C
ANISOU 3001 CA SER A 305 8577 9115 10999 -2841 -2199 -1030 C
ATOM 3002 C SER A 305 -0.797 -23.839 -0.575 1.00 89.26 C
ANISOU 3002 C SER A 305 10089 11092 12732 -2805 -2301 -922 C
ATOM 3003 O SER A 305 -1.811 -23.833 -1.282 1.00117.75 O
ANISOU 3003 O SER A 305 13584 14733 16421 -2926 -2561 -987 O
ATOM 3004 CB SER A 305 0.125 -25.728 0.796 1.00 79.41 C
ANISOU 3004 CB SER A 305 8934 9491 11747 -2887 -1979 -853 C
ATOM 3005 OG SER A 305 0.858 -26.940 0.773 1.00 76.15 O
ANISOU 3005 OG SER A 305 8715 8827 11393 -2935 -1923 -949 O
TER 3006 SER A 305
HETATM 3007 C1 CLR A2401 36.408 7.792 21.236 1.00 48.03 C
ANISOU 3007 C1 CLR A2401 5339 6644 6264 -703 -1414 -730 C
HETATM 3008 C2 CLR A2401 36.465 9.276 21.250 1.00 45.11 C
ANISOU 3008 C2 CLR A2401 5054 6157 5927 -812 -1454 -807 C
HETATM 3009 C3 CLR A2401 37.476 9.648 20.180 1.00 45.98 C
ANISOU 3009 C3 CLR A2401 4957 6208 6307 -964 -1356 -787 C
HETATM 3010 C4 CLR A2401 36.968 9.270 18.770 1.00 44.33 C
ANISOU 3010 C4 CLR A2401 4731 6020 6093 -960 -1075 -688 C
HETATM 3011 C5 CLR A2401 36.464 7.824 18.643 1.00 42.73 C
ANISOU 3011 C5 CLR A2401 4512 5936 5789 -822 -993 -622 C
HETATM 3012 C6 CLR A2401 37.595 6.935 18.114 1.00 45.49 C
ANISOU 3012 C6 CLR A2401 4596 6330 6356 -850 -939 -599 C
HETATM 3013 C7 CLR A2401 36.995 5.640 17.635 1.00 41.89 C
ANISOU 3013 C7 CLR A2401 4147 5956 5813 -734 -803 -533 C
HETATM 3014 C8 CLR A2401 35.869 5.197 18.587 1.00 40.67 C
ANISOU 3014 C8 CLR A2401 4190 5847 5417 -599 -898 -517 C
HETATM 3015 C9 CLR A2401 35.897 5.796 20.007 1.00 41.70 C
ANISOU 3015 C9 CLR A2401 4423 5960 5459 -583 -1138 -580 C
HETATM 3016 C10 CLR A2401 35.750 7.312 19.936 1.00 42.23 C
ANISOU 3016 C10 CLR A2401 4595 5934 5517 -682 -1148 -640 C
HETATM 3017 C11 CLR A2401 34.776 5.239 20.937 1.00 40.73 C
ANISOU 3017 C11 CLR A2401 4495 5900 5081 -448 -1193 -555 C
HETATM 3018 C12 CLR A2401 34.797 3.729 21.038 1.00 40.27 C
ANISOU 3018 C12 CLR A2401 4365 5913 5022 -352 -1185 -481 C
HETATM 3019 C13 CLR A2401 34.889 3.135 19.639 1.00 39.34 C
ANISOU 3019 C13 CLR A2401 4118 5795 5033 -372 -972 -435 C
HETATM 3020 C14 CLR A2401 36.052 3.725 18.836 1.00 40.48 C
ANISOU 3020 C14 CLR A2401 4074 5890 5415 -493 -923 -476 C
HETATM 3021 C15 CLR A2401 36.010 2.988 17.515 1.00 48.56 C
ANISOU 3021 C15 CLR A2401 5010 6931 6511 -493 -695 -435 C
HETATM 3022 C16 CLR A2401 35.716 1.567 18.026 1.00 48.04 C
ANISOU 3022 C16 CLR A2401 4946 6913 6393 -361 -745 -389 C
HETATM 3023 C17 CLR A2401 35.139 1.612 19.483 1.00 55.58 C
ANISOU 3023 C17 CLR A2401 6063 7890 7164 -288 -944 -378 C
HETATM 3024 C18 CLR A2401 33.573 3.489 18.923 1.00 37.64 C
ANISOU 3024 C18 CLR A2401 4063 5578 4661 -366 -795 -408 C
HETATM 3025 C19 CLR A2401 34.231 7.598 19.913 1.00 40.66 C
ANISOU 3025 C19 CLR A2401 4630 5737 5084 -602 -1052 -620 C
HETATM 3026 C20 CLR A2401 33.955 0.618 19.687 1.00 49.62 C
ANISOU 3026 C20 CLR A2401 5447 7177 6228 -184 -889 -305 C
HETATM 3027 C21 CLR A2401 33.621 0.318 21.173 1.00 38.38 C
ANISOU 3027 C21 CLR A2401 4152 5789 4642 -106 -1074 -275 C
HETATM 3028 C22 CLR A2401 34.188 -0.783 19.052 1.00 47.29 C
ANISOU 3028 C22 CLR A2401 5034 6884 6051 -128 -798 -260 C
HETATM 3029 C23 CLR A2401 33.188 -1.909 19.397 1.00 41.56 C
ANISOU 3029 C23 CLR A2401 4424 6181 5187 -35 -779 -181 C
HETATM 3030 C24 CLR A2401 33.873 -3.206 19.895 1.00 51.57 C
ANISOU 3030 C24 CLR A2401 5592 7429 6573 48 -889 -132 C
HETATM 3031 C25 CLR A2401 33.817 -4.408 18.928 1.00 46.04 C
ANISOU 3031 C25 CLR A2401 4814 6693 5987 87 -742 -113 C
HETATM 3032 C26 CLR A2401 32.414 -5.005 18.806 1.00 63.56 C
ANISOU 3032 C26 CLR A2401 7194 8921 8035 113 -643 -51 C
HETATM 3033 C27 CLR A2401 34.312 -4.037 17.528 1.00 65.88 C
ANISOU 3033 C27 CLR A2401 7200 9192 8639 17 -561 -192 C
HETATM 3034 O1 CLR A2401 37.591 11.043 20.328 1.00 47.25 O
ANISOU 3034 O1 CLR A2401 5202 6238 6511 -1075 -1426 -859 O
HETATM 3035 C1 CLR A2402 31.326 10.470 13.390 1.00 51.06 C
ANISOU 3035 C1 CLR A2402 6308 6775 6316 -852 -206 -287 C
HETATM 3036 C2 CLR A2402 31.138 11.942 13.373 1.00 41.22 C
ANISOU 3036 C2 CLR A2402 5188 5377 5097 -909 -254 -287 C
HETATM 3037 C3 CLR A2402 32.511 12.512 13.044 1.00 51.43 C
ANISOU 3037 C3 CLR A2402 6370 6595 6575 -1085 -233 -288 C
HETATM 3038 C4 CLR A2402 32.954 12.141 11.615 1.00 40.87 C
ANISOU 3038 C4 CLR A2402 4967 5297 5266 -1184 -36 -192 C
HETATM 3039 C5 CLR A2402 32.788 10.664 11.249 1.00 43.86 C
ANISOU 3039 C5 CLR A2402 5264 5833 5569 -1101 60 -179 C
HETATM 3040 C6 CLR A2402 34.138 9.954 11.418 1.00 40.37 C
ANISOU 3040 C6 CLR A2402 4590 5453 5295 -1159 87 -228 C
HETATM 3041 C7 CLR A2402 34.062 8.645 10.680 1.00 43.94 C
ANISOU 3041 C7 CLR A2402 4979 6024 5693 -1105 230 -206 C
HETATM 3042 C8 CLR A2402 32.678 7.999 10.899 1.00 48.08 C
ANISOU 3042 C8 CLR A2402 5638 6604 6024 -951 186 -193 C
HETATM 3043 C9 CLR A2402 31.878 8.495 12.120 1.00 37.00 C
ANISOU 3043 C9 CLR A2402 4343 5165 4551 -858 6 -228 C
HETATM 3044 C10 CLR A2402 31.570 9.983 11.959 1.00 44.83 C
ANISOU 3044 C10 CLR A2402 5470 6027 5535 -922 -25 -204 C
HETATM 3045 C11 CLR A2402 30.531 7.737 12.320 1.00 44.86 C
ANISOU 3045 C11 CLR A2402 5435 6232 5379 -714 -8 -211 C
HETATM 3046 C12 CLR A2402 30.736 6.248 12.464 1.00 37.83 C
ANISOU 3046 C12 CLR A2402 4433 5445 4496 -650 18 -225 C
HETATM 3047 C13 CLR A2402 31.579 5.763 11.301 1.00 37.67 C
ANISOU 3047 C13 CLR A2402 4308 5447 4558 -733 174 -210 C
HETATM 3048 C14 CLR A2402 32.897 6.534 11.178 1.00 46.97 C
ANISOU 3048 C14 CLR A2402 5374 6568 5904 -863 195 -230 C
HETATM 3049 C15 CLR A2402 33.586 5.906 9.981 1.00 44.49 C
ANISOU 3049 C15 CLR A2402 4960 6296 5647 -928 390 -217 C
HETATM 3050 C16 CLR A2402 33.230 4.425 10.216 1.00 55.94 C
ANISOU 3050 C16 CLR A2402 6369 7828 7058 -800 383 -244 C
HETATM 3051 C17 CLR A2402 32.091 4.295 11.291 1.00 52.18 C
ANISOU 3051 C17 CLR A2402 6006 7360 6459 -681 220 -238 C
HETATM 3052 C18 CLR A2402 30.755 6.016 10.023 1.00 35.50 C
ANISOU 3052 C18 CLR A2402 4169 5165 4153 -762 292 -143 C
HETATM 3053 C19 CLR A2402 30.290 10.072 11.114 1.00 50.63 C
ANISOU 3053 C19 CLR A2402 6362 6762 6114 -867 41 -126 C
HETATM 3054 C20 CLR A2402 31.106 3.110 11.011 1.00 40.45 C
ANISOU 3054 C20 CLR A2402 4579 5935 4854 -585 260 -221 C
HETATM 3055 C21 CLR A2402 30.184 2.762 12.203 1.00 42.07 C
ANISOU 3055 C21 CLR A2402 4848 6162 4975 -473 121 -215 C
HETATM 3056 C22 CLR A2402 31.797 1.755 10.687 1.00 46.81 C
ANISOU 3056 C22 CLR A2402 5248 6781 5756 -556 340 -255 C
HETATM 3057 C23 CLR A2402 30.941 0.475 10.804 1.00 44.81 C
ANISOU 3057 C23 CLR A2402 5036 6564 5427 -455 328 -248 C
HETATM 3058 C24 CLR A2402 31.769 -0.805 11.073 1.00 45.65 C
ANISOU 3058 C24 CLR A2402 4992 6676 5676 -397 332 -288 C
HETATM 3059 C25 CLR A2402 31.004 -2.137 10.931 1.00 53.56 C
ANISOU 3059 C25 CLR A2402 6038 7689 6625 -319 350 -283 C
HETATM 3060 C26 CLR A2402 30.379 -2.600 12.249 1.00 32.42 C
ANISOU 3060 C26 CLR A2402 3397 5014 3908 -233 196 -238 C
HETATM 3061 C27 CLR A2402 29.898 -2.047 9.871 1.00 53.79 C
ANISOU 3061 C27 CLR A2402 6211 7734 6492 -353 440 -267 C
HETATM 3062 O1 CLR A2402 32.328 13.903 13.154 1.00 48.09 O
ANISOU 3062 O1 CLR A2402 6077 6007 6188 -1139 -300 -295 O
HETATM 3063 C1 CLR A2403 1.099 10.264 22.299 1.00 53.50 C
ANISOU 3063 C1 CLR A2403 5378 8241 6708 1980 1422 -727 C
HETATM 3064 C2 CLR A2403 1.553 11.658 22.534 1.00 54.22 C
ANISOU 3064 C2 CLR A2403 5652 8171 6780 2123 1371 -871 C
HETATM 3065 C3 CLR A2403 1.233 11.933 23.994 1.00 58.99 C
ANISOU 3065 C3 CLR A2403 6298 8852 7263 2231 1653 -1032 C
HETATM 3066 C4 CLR A2403 2.126 11.091 24.909 1.00 55.31 C
ANISOU 3066 C4 CLR A2403 6032 8502 6480 2076 1751 -1017 C
HETATM 3067 C5 CLR A2403 2.144 9.598 24.581 1.00 53.65 C
ANISOU 3067 C5 CLR A2403 5723 8428 6236 1883 1746 -832 C
HETATM 3068 C6 CLR A2403 1.148 8.883 25.497 1.00 55.76 C
ANISOU 3068 C6 CLR A2403 5827 8877 6482 1890 2045 -828 C
HETATM 3069 C7 CLR A2403 1.469 7.416 25.467 1.00 65.86 C
ANISOU 3069 C7 CLR A2403 7103 10267 7653 1681 2048 -660 C
HETATM 3070 C8 CLR A2403 1.761 6.970 24.023 1.00 51.77 C
ANISOU 3070 C8 CLR A2403 5246 8407 6019 1570 1776 -526 C
HETATM 3071 C9 CLR A2403 1.335 7.931 22.891 1.00 59.02 C
ANISOU 3071 C9 CLR A2403 6045 9192 7186 1687 1589 -553 C
HETATM 3072 C10 CLR A2403 2.015 9.291 23.054 1.00 51.99 C
ANISOU 3072 C10 CLR A2403 5366 8155 6234 1812 1508 -689 C
HETATM 3073 C11 CLR A2403 1.675 7.364 21.480 1.00 49.68 C
ANISOU 3073 C11 CLR A2403 4826 7955 6095 1554 1329 -413 C
HETATM 3074 C12 CLR A2403 0.951 6.067 21.231 1.00 49.82 C
ANISOU 3074 C12 CLR A2403 4630 8092 6206 1430 1383 -292 C
HETATM 3075 C13 CLR A2403 1.238 5.122 22.392 1.00 53.49 C
ANISOU 3075 C13 CLR A2403 5179 8680 6467 1327 1594 -265 C
HETATM 3076 C14 CLR A2403 0.919 5.749 23.755 1.00 64.16 C
ANISOU 3076 C14 CLR A2403 6576 10091 7711 1458 1851 -391 C
HETATM 3077 C15 CLR A2403 1.265 4.665 24.755 1.00 58.97 C
ANISOU 3077 C15 CLR A2403 6024 9553 6830 1326 2022 -324 C
HETATM 3078 C16 CLR A2403 0.700 3.437 24.008 1.00 55.25 C
ANISOU 3078 C16 CLR A2403 5339 9129 6524 1176 1981 -168 C
HETATM 3079 C17 CLR A2403 0.471 3.773 22.486 1.00 65.16 C
ANISOU 3079 C17 CLR A2403 6457 10281 8021 1194 1716 -146 C
HETATM 3080 C18 CLR A2403 2.744 4.829 22.353 1.00 47.40 C
ANISOU 3080 C18 CLR A2403 4686 7852 5473 1215 1461 -235 C
HETATM 3081 C19 CLR A2403 3.393 9.153 22.372 1.00 49.18 C
ANISOU 3081 C19 CLR A2403 5221 7706 5758 1673 1274 -621 C
HETATM 3082 C20 CLR A2403 0.842 2.591 21.524 1.00 48.64 C
ANISOU 3082 C20 CLR A2403 4350 8169 5963 1004 1539 -9 C
HETATM 3083 C21 CLR A2403 0.393 2.791 20.048 1.00 48.23 C
ANISOU 3083 C21 CLR A2403 4145 8044 6138 1009 1299 19 C
HETATM 3084 C22 CLR A2403 0.242 1.209 21.940 1.00 49.58 C
ANISOU 3084 C22 CLR A2403 4328 8396 6113 856 1696 102 C
HETATM 3085 C23 CLR A2403 -0.276 0.272 20.831 1.00 58.64 C
ANISOU 3085 C23 CLR A2403 5285 9531 7463 722 1550 203 C
HETATM 3086 C24 CLR A2403 -1.094 -0.922 21.367 1.00 57.88 C
ANISOU 3086 C24 CLR A2403 5012 9535 7446 590 1741 300 C
HETATM 3087 C25 CLR A2403 -0.681 -2.298 20.819 1.00 73.32 C
ANISOU 3087 C25 CLR A2403 7007 11451 9400 386 1626 416 C
HETATM 3088 C26 CLR A2403 -1.441 -3.445 21.493 1.00 81.66 C
ANISOU 3088 C26 CLR A2403 7913 12588 10524 247 1835 521 C
HETATM 3089 C27 CLR A2403 -0.883 -2.386 19.298 1.00 59.81 C
ANISOU 3089 C27 CLR A2403 5189 9664 7873 344 1348 419 C
HETATM 3090 O1 CLR A2403 1.528 13.299 24.149 1.00 57.52 O
ANISOU 3090 O1 CLR A2403 6263 8491 7099 2381 1595 -1184 O
HETATM 3091 C29 8IM A2404 21.976 16.034 15.053 1.00 39.07 C
ANISOU 3091 C29 8IM A2404 5763 4715 4366 31 -465 -381 C
HETATM 3092 C30 8IM A2404 22.870 17.087 14.826 1.00 40.38 C
ANISOU 3092 C30 8IM A2404 6004 4703 4635 -85 -520 -385 C
HETATM 3093 C31 8IM A2404 23.469 17.256 13.572 1.00 42.86 C
ANISOU 3093 C31 8IM A2404 6324 4959 5001 -226 -495 -251 C
HETATM 3094 C32 8IM A2404 23.152 16.348 12.561 1.00 39.37 C
ANISOU 3094 C32 8IM A2404 5826 4645 4489 -239 -422 -129 C
HETATM 3095 C34 8IM A2404 23.819 19.504 12.818 1.00 67.99 C
ANISOU 3095 C34 8IM A2404 9708 7754 8369 -331 -581 -183 C
HETATM 3096 C35 8IM A2404 22.919 20.252 13.848 1.00 74.73 C
ANISOU 3096 C35 8IM A2404 10642 8503 9250 -153 -654 -321 C
HETATM 3097 C36 8IM A2404 19.077 2.299 19.413 1.00 31.05 C
ANISOU 3097 C36 8IM A2404 4026 5133 2639 249 46 -80 C
HETATM 3098 C15 8IM A2404 17.932 8.532 16.891 1.00 33.00 C
ANISOU 3098 C15 8IM A2404 4458 4955 3126 376 -78 -265 C
HETATM 3099 C20 8IM A2404 19.527 4.699 18.664 1.00 31.42 C
ANISOU 3099 C20 8IM A2404 4147 5035 2755 256 -30 -194 C
HETATM 3100 C22 8IM A2404 16.816 10.643 15.812 1.00 34.54 C
ANISOU 3100 C22 8IM A2404 4724 4944 3455 481 -143 -261 C
HETATM 3101 C23 8IM A2404 17.593 10.945 14.491 1.00 34.25 C
ANISOU 3101 C23 8IM A2404 4730 4823 3461 364 -200 -178 C
HETATM 3102 C19 8IM A2404 16.203 7.135 16.495 1.00 32.47 C
ANISOU 3102 C19 8IM A2404 4242 5035 3060 433 12 -173 C
HETATM 3103 C18 8IM A2404 19.969 8.140 17.920 1.00 32.87 C
ANISOU 3103 C18 8IM A2404 4485 4949 3055 266 -141 -328 C
HETATM 3104 C17 8IM A2404 18.349 6.257 17.705 1.00 31.87 C
ANISOU 3104 C17 8IM A2404 4224 5000 2884 321 -17 -216 C
HETATM 3105 C25 8IM A2404 19.558 14.046 13.238 1.00 36.68 C
ANISOU 3105 C25 8IM A2404 5309 4693 3934 182 -350 -146 C
HETATM 3106 C1 8IM A2404 11.853 18.047 12.589 1.00 58.21 C
ANISOU 3106 C1 8IM A2404 7962 6957 7198 1179 -624 -106 C
HETATM 3107 C16 8IM A2404 17.499 7.191 17.066 1.00 32.32 C
ANISOU 3107 C16 8IM A2404 4288 4994 2997 374 -19 -217 C
HETATM 3108 C2 8IM A2404 12.482 18.275 13.987 1.00 61.54 C
ANISOU 3108 C2 8IM A2404 8434 7368 7581 1186 -524 -286 C
HETATM 3109 C21 8IM A2404 19.870 3.389 19.170 1.00 31.62 C
ANISOU 3109 C21 8IM A2404 4140 5131 2742 233 -22 -146 C
HETATM 3110 C24 8IM A2404 18.791 12.692 13.209 1.00 35.42 C
ANISOU 3110 C24 8IM A2404 5039 4719 3702 234 -295 -118 C
HETATM 3111 C26 8IM A2404 20.214 13.653 15.511 1.00 36.57 C
ANISOU 3111 C26 8IM A2404 5267 4768 3860 223 -337 -353 C
HETATM 3112 C27 8IM A2404 19.438 12.298 15.508 1.00 41.08 C
ANISOU 3112 C27 8IM A2404 5732 5521 4354 277 -267 -309 C
HETATM 3113 C28 8IM A2404 21.650 15.111 14.050 1.00 37.85 C
ANISOU 3113 C28 8IM A2404 5538 4677 4164 12 -404 -257 C
HETATM 3114 C3 8IM A2404 14.865 18.422 13.776 1.00 71.26 C
ANISOU 3114 C3 8IM A2404 9859 8516 8701 878 -550 -261 C
HETATM 3115 C33 8IM A2404 22.263 15.303 12.801 1.00 38.04 C
ANISOU 3115 C33 8IM A2404 5584 4644 4226 -122 -388 -139 C
HETATM 3116 C37 8IM A2404 19.946 1.273 19.899 1.00 31.02 C
ANISOU 3116 C37 8IM A2404 4019 5151 2618 214 6 -42 C
HETATM 3117 C38 8IM A2404 21.201 1.821 19.909 1.00 31.14 C
ANISOU 3117 C38 8IM A2404 4056 5112 2662 182 -86 -94 C
HETATM 3118 C4 8IM A2404 15.976 19.503 13.868 1.00 80.59 C
ANISOU 3118 C4 8IM A2404 11199 9491 9932 779 -605 -296 C
HETATM 3119 C5 8IM A2404 17.733 18.228 12.921 1.00 82.33 C
ANISOU 3119 C5 8IM A2404 11394 9875 10011 460 -564 -156 C
HETATM 3120 C6 8IM A2404 18.805 18.251 11.809 1.00 55.50 C
ANISOU 3120 C6 8IM A2404 8053 6434 6600 262 -573 -24 C
HETATM 3121 C7 8IM A2404 19.891 20.353 11.851 1.00 91.09 C
ANISOU 3121 C7 8IM A2404 12769 10559 11281 151 -666 -42 C
HETATM 3122 C8 8IM A2404 21.330 20.953 11.982 1.00 82.34 C
ANISOU 3122 C8 8IM A2404 11722 9324 10240 -39 -674 -67 C
HETATM 3123 C9 8IM A2404 12.157 16.607 10.752 1.00 78.51 C
ANISOU 3123 C9 8IM A2404 10500 9707 9623 963 -688 130 C
HETATM 3124 N1 8IM A2404 21.776 20.904 13.387 1.00 74.08 N
ANISOU 3124 N1 8IM A2404 10641 8306 9199 -20 -683 -263 N
HETATM 3125 N10 8IM A2404 20.737 13.968 14.147 1.00 38.25 N
ANISOU 3125 N10 8IM A2404 5504 4900 4130 106 -350 -239 N
HETATM 3126 N2 8IM A2404 19.157 9.037 17.307 1.00 34.64 N
ANISOU 3126 N2 8IM A2404 4733 5099 3331 316 -135 -322 N
HETATM 3127 N3 8IM A2404 19.609 6.779 18.130 1.00 32.17 N
ANISOU 3127 N3 8IM A2404 4326 4981 2917 273 -86 -273 N
HETATM 3128 N4 8IM A2404 21.197 8.552 18.362 1.00 35.25 N
ANISOU 3128 N4 8IM A2404 4828 5199 3368 203 -215 -385 N
HETATM 3129 N5 8IM A2404 16.890 9.210 16.242 1.00 33.53 N
ANISOU 3129 N5 8IM A2404 4517 4969 3255 447 -82 -242 N
HETATM 3130 N6 8IM A2404 15.850 8.343 16.004 1.00 33.21 N
ANISOU 3130 N6 8IM A2404 4377 5026 3216 482 -33 -187 N
HETATM 3131 N7 8IM A2404 18.289 4.950 18.035 1.00 34.08 N
ANISOU 3131 N7 8IM A2404 4450 5374 3124 302 23 -169 N
HETATM 3132 N8 8IM A2404 20.358 5.779 18.741 1.00 31.90 N
ANISOU 3132 N8 8IM A2404 4270 5013 2839 235 -100 -261 N
HETATM 3133 N9 8IM A2404 18.273 12.297 14.555 1.00 41.12 N
ANISOU 3133 N9 8IM A2404 5710 5527 4385 340 -259 -220 N
HETATM 3134 O1 8IM A2404 12.364 16.814 12.126 1.00 66.23 O
ANISOU 3134 O1 8IM A2404 8933 8149 8081 1023 -588 -32 O
HETATM 3135 O2 8IM A2404 13.618 19.089 13.766 1.00 86.49 O
ANISOU 3135 O2 8IM A2404 11760 10356 10747 1069 -585 -275 O
HETATM 3136 O3 8IM A2404 16.854 19.320 12.779 1.00 96.09 O
ANISOU 3136 O3 8IM A2404 13204 11443 11863 596 -633 -150 O
HETATM 3137 O4 8IM A2404 19.952 18.977 12.160 1.00 78.20 O
ANISOU 3137 O4 8IM A2404 11002 9176 9535 144 -589 -76 O
HETATM 3138 O7 8IM A2404 24.352 18.294 13.330 1.00 58.50 O
ANISOU 3138 O7 8IM A2404 8373 6760 7096 -359 -535 -240 O
HETATM 3139 O8 8IM A2404 23.209 20.261 15.038 1.00 87.97 O
ANISOU 3139 O8 8IM A2404 12310 10197 10916 -125 -688 -481 O
HETATM 3140 O9 8IM A2404 21.180 3.115 19.465 1.00 31.79 O
ANISOU 3140 O9 8IM A2404 4168 5137 2776 184 -99 -157 O
HETATM 3141 C1 OLA A2405 19.172 -22.181 28.799 1.00 54.42 C
ANISOU 3141 C1 OLA A2405 7860 6866 5952 -272 -195 2636 C
HETATM 3142 O1 OLA A2405 19.223 -21.834 27.593 1.00 52.55 O
ANISOU 3142 O1 OLA A2405 7451 6626 5889 -257 -175 2419 O
HETATM 3143 O2 OLA A2405 18.691 -23.255 29.214 1.00 73.14 O
ANISOU 3143 O2 OLA A2405 10325 9098 8365 -360 -157 2841 O
HETATM 3144 C2 OLA A2405 19.765 -21.184 29.849 1.00 53.72 C
ANISOU 3144 C2 OLA A2405 7888 6960 5564 -184 -278 2648 C
HETATM 3145 C3 OLA A2405 19.410 -19.722 29.549 1.00 51.52 C
ANISOU 3145 C3 OLA A2405 7513 6908 5156 -173 -169 2438 C
HETATM 3146 C4 OLA A2405 20.529 -18.725 29.946 1.00 50.96 C
ANISOU 3146 C4 OLA A2405 7475 6942 4946 -47 -339 2334 C
HETATM 3147 C5 OLA A2405 20.532 -17.394 29.154 1.00 48.41 C
ANISOU 3147 C5 OLA A2405 7004 6757 4633 -16 -286 2078 C
HETATM 3148 C6 OLA A2405 19.422 -16.391 29.552 1.00 48.03 C
ANISOU 3148 C6 OLA A2405 6981 6908 4361 -68 -87 2032 C
HETATM 3149 C7 OLA A2405 19.773 -14.892 29.345 1.00 54.38 C
ANISOU 3149 C7 OLA A2405 7729 7853 5078 -1 -110 1820 C
HETATM 3150 C1 OLA A2406 5.088 11.991 3.851 1.00 79.69 C
ANISOU 3150 C1 OLA A2406 9935 10511 9832 1016 -1645 788 C
HETATM 3151 O1 OLA A2406 4.355 12.998 3.774 1.00 85.79 O
ANISOU 3151 O1 OLA A2406 10670 11169 10759 1173 -1777 835 O
HETATM 3152 O2 OLA A2406 6.338 12.016 3.983 1.00 68.92 O
ANISOU 3152 O2 OLA A2406 8744 9121 8320 906 -1512 770 O
HETATM 3153 C2 OLA A2406 4.408 10.586 3.787 1.00 71.00 C
ANISOU 3153 C2 OLA A2406 8641 9588 8746 950 -1649 748 C
HETATM 3154 C3 OLA A2406 4.474 9.944 2.399 1.00 55.04 C
ANISOU 3154 C3 OLA A2406 6739 7617 6556 811 -1819 830 C
HETATM 3155 C4 OLA A2406 5.275 8.620 2.388 1.00 51.64 C
ANISOU 3155 C4 OLA A2406 6352 7305 5962 631 -1674 764 C
HETATM 3156 C5 OLA A2406 5.059 7.736 1.136 1.00 46.53 C
ANISOU 3156 C5 OLA A2406 5769 6734 5177 504 -1835 802 C
HETATM 3157 C6 OLA A2406 4.982 6.210 1.422 1.00 44.53 C
ANISOU 3157 C6 OLA A2406 5386 6610 4922 395 -1738 706 C
HETATM 3158 C7 OLA A2406 4.080 5.379 0.459 1.00 47.81 C
ANISOU 3158 C7 OLA A2406 5738 7097 5329 327 -1953 719 C
HETATM 3159 C8 OLA A2406 3.853 3.887 0.865 1.00 62.48 C
ANISOU 3159 C8 OLA A2406 7439 9060 7243 227 -1861 622 C
HETATM 3160 C9 OLA A2406 4.973 2.873 0.442 1.00 49.25 C
ANISOU 3160 C9 OLA A2406 5945 7413 5354 62 -1749 562 C
HETATM 3161 C1 OLA A2407 2.658 14.813 13.203 1.00 75.10 C
ANISOU 3161 C1 OLA A2407 8556 9873 10106 2017 -441 -129 C
HETATM 3162 O1 OLA A2407 3.499 15.666 13.565 1.00 67.75 O
ANISOU 3162 O1 OLA A2407 7832 8804 9108 2032 -423 -191 O
HETATM 3163 O2 OLA A2407 1.936 15.054 12.211 1.00 99.54 O
ANISOU 3163 O2 OLA A2407 11560 12917 13344 2076 -630 -29 O
HETATM 3164 C2 OLA A2407 2.518 13.508 13.948 1.00 59.23 C
ANISOU 3164 C2 OLA A2407 6414 8080 8009 1922 -250 -167 C
HETATM 3165 C3 OLA A2407 3.392 12.441 13.298 1.00 50.57 C
ANISOU 3165 C3 OLA A2407 5420 7067 6729 1693 -308 -68 C
HETATM 3166 C4 OLA A2407 2.645 11.116 13.191 1.00 46.98 C
ANISOU 3166 C4 OLA A2407 4749 6791 6308 1615 -268 -22 C
HETATM 3167 C5 OLA A2407 3.594 9.985 12.812 1.00 44.61 C
ANISOU 3167 C5 OLA A2407 4561 6569 5818 1399 -277 40 C
HETATM 3168 C6 OLA A2407 2.835 8.709 12.470 1.00 44.63 C
ANISOU 3168 C6 OLA A2407 4367 6712 5876 1309 -285 97 C
HETATM 3169 C7 OLA A2407 3.531 7.972 11.333 1.00 43.08 C
ANISOU 3169 C7 OLA A2407 4292 6522 5556 1133 -429 184 C
HETATM 3170 C8 OLA A2407 2.630 6.895 10.742 1.00 48.72 C
ANISOU 3170 C8 OLA A2407 4815 7337 6359 1057 -502 238 C
HETATM 3171 C9 OLA A2407 2.974 5.567 11.371 1.00 42.34 C
ANISOU 3171 C9 OLA A2407 3982 6639 5466 921 -344 223 C
HETATM 3172 C10 OLA A2407 2.700 4.319 10.646 1.00 46.80 C
ANISOU 3172 C10 OLA A2407 4472 7270 6039 774 -425 274 C
HETATM 3173 C11 OLA A2407 1.361 4.103 9.982 1.00 44.04 C
ANISOU 3173 C11 OLA A2407 3894 6957 5881 791 -568 311 C
HETATM 3174 C12 OLA A2407 1.274 2.655 9.519 1.00 51.18 C
ANISOU 3174 C12 OLA A2407 4749 7927 6770 613 -605 337 C
HETATM 3175 C13 OLA A2407 1.450 1.723 10.710 1.00 48.87 C
ANISOU 3175 C13 OLA A2407 4404 7706 6456 546 -365 313 C
HETATM 3176 C14 OLA A2407 0.095 1.287 11.252 1.00 83.66 C
ANISOU 3176 C14 OLA A2407 8508 12199 11081 562 -283 319 C
HETATM 3177 C15 OLA A2407 -0.197 -0.155 10.860 1.00 90.83 C
ANISOU 3177 C15 OLA A2407 9329 13148 12035 381 -323 352 C
HETATM 3178 C16 OLA A2407 0.712 -1.105 11.629 1.00 80.23 C
ANISOU 3178 C16 OLA A2407 8119 11816 10546 271 -144 354 C
HETATM 3179 C17 OLA A2407 -0.110 -2.066 12.479 1.00 80.29 C
ANISOU 3179 C17 OLA A2407 7916 11901 10689 196 25 383 C
HETATM 3180 C18 OLA A2407 -0.806 -3.095 11.595 1.00 68.23 C
ANISOU 3180 C18 OLA A2407 6249 10374 9303 49 -127 411 C
HETATM 3181 C1 OLA A2408 -2.616 15.389 13.757 1.00 96.36 C
ANISOU 3181 C1 OLA A2408 10155 12689 13769 2691 -366 -245 C
HETATM 3182 O1 OLA A2408 -3.687 15.078 13.193 1.00 90.67 O
ANISOU 3182 O1 OLA A2408 9164 12029 13258 2740 -478 -179 O
HETATM 3183 O2 OLA A2408 -2.339 16.598 13.916 1.00 94.72 O
ANISOU 3183 O2 OLA A2408 10097 12289 13602 2833 -398 -307 O
HETATM 3184 C2 OLA A2408 -1.667 14.320 14.237 1.00 72.78 C
ANISOU 3184 C2 OLA A2408 7308 9847 10497 2464 -211 -250 C
HETATM 3185 C3 OLA A2408 -1.690 13.163 13.249 1.00 56.06 C
ANISOU 3185 C3 OLA A2408 5130 7844 8327 2269 -362 -105 C
HETATM 3186 C4 OLA A2408 -1.723 11.826 13.974 1.00 54.92 C
ANISOU 3186 C4 OLA A2408 4878 7905 8083 2124 -145 -128 C
HETATM 3187 C5 OLA A2408 -1.262 10.724 13.032 1.00 56.01 C
ANISOU 3187 C5 OLA A2408 5077 8112 8091 1899 -291 -5 C
HETATM 3188 C6 OLA A2408 -2.145 9.497 13.176 1.00 53.45 C
ANISOU 3188 C6 OLA A2408 4480 7962 7868 1814 -210 20 C
HETATM 3189 C7 OLA A2408 -1.304 8.233 13.252 1.00 56.99 C
ANISOU 3189 C7 OLA A2408 5054 8505 8097 1585 -141 58 C
HETATM 3190 C8 OLA A2408 -2.179 7.024 12.965 1.00 51.66 C
ANISOU 3190 C8 OLA A2408 4127 7957 7543 1473 -155 115 C
HETATM 3191 C9 OLA A2408 -1.437 5.769 13.347 1.00 49.61 C
ANISOU 3191 C9 OLA A2408 3972 7784 7094 1274 -29 134 C
HETATM 3192 C10 OLA A2408 -2.128 4.481 13.216 1.00 50.14 C
ANISOU 3192 C10 OLA A2408 3833 7960 7257 1135 -11 184 C
HETATM 3193 C11 OLA A2408 -3.638 4.474 13.242 1.00 52.97 C
ANISOU 3193 C11 OLA A2408 3832 8383 7912 1211 -4 185 C
HETATM 3194 C12 OLA A2408 -4.142 3.155 13.813 1.00 53.48 C
ANISOU 3194 C12 OLA A2408 3713 8572 8034 1062 170 212 C
HETATM 3195 C13 OLA A2408 -3.478 1.961 13.142 1.00 52.40 C
ANISOU 3195 C13 OLA A2408 3715 8433 7762 840 52 275 C
HETATM 3196 C14 OLA A2408 -4.540 0.981 12.660 1.00 68.58 C
ANISOU 3196 C14 OLA A2408 5484 10545 10029 718 -31 323 C
HETATM 3197 C15 OLA A2408 -4.089 -0.466 12.818 1.00 70.75 C
ANISOU 3197 C15 OLA A2408 5831 10849 10201 498 45 364 C
HETATM 3198 C16 OLA A2408 -4.384 -0.990 14.218 1.00 52.89 C
ANISOU 3198 C16 OLA A2408 3459 8677 7961 468 378 371 C
HETATM 3199 C17 OLA A2408 -3.828 -2.398 14.396 1.00 76.61 C
ANISOU 3199 C17 OLA A2408 6572 11681 10854 256 442 427 C
HETATM 3200 C1 OLA A2409 -0.691 10.698 9.018 1.00 87.28 C
ANISOU 3200 C1 OLA A2409 9332 11900 11930 1670 -1089 335 C
HETATM 3201 O1 OLA A2409 0.388 11.279 8.764 1.00 78.83 O
ANISOU 3201 O1 OLA A2409 8540 10721 10692 1633 -1118 356 O
HETATM 3202 O2 OLA A2409 -1.766 11.319 8.857 1.00 74.82 O
ANISOU 3202 O2 OLA A2409 7565 10279 10586 1836 -1198 346 O
HETATM 3203 C2 OLA A2409 -0.693 9.272 9.520 1.00 66.90 C
ANISOU 3203 C2 OLA A2409 6640 9490 9288 1516 -924 303 C
HETATM 3204 C3 OLA A2409 -1.897 8.512 8.971 1.00 52.30 C
ANISOU 3204 C3 OLA A2409 4516 7737 7618 1488 -1051 348 C
HETATM 3205 C4 OLA A2409 -1.459 7.358 8.074 1.00 62.34 C
ANISOU 3205 C4 OLA A2409 5883 9070 8732 1268 -1168 409 C
HETATM 3206 C5 OLA A2409 -2.662 6.633 7.479 1.00 74.19 C
ANISOU 3206 C5 OLA A2409 7117 10653 10418 1228 -1328 446 C
HETATM 3207 C6 OLA A2409 -2.312 5.189 7.135 1.00 65.59 C
ANISOU 3207 C6 OLA A2409 6069 9652 9202 1001 -1324 455 C
HETATM 3208 C7 OLA A2409 -3.379 4.222 7.638 1.00 63.63 C
ANISOU 3208 C7 OLA A2409 5494 9520 9163 950 -1239 432 C
HETATM 3209 C8 OLA A2409 -2.810 2.820 7.833 1.00 67.41 C
ANISOU 3209 C8 OLA A2409 6041 10064 9509 741 -1117 418 C
HETATM 3210 C9 OLA A2409 -3.714 2.042 8.761 1.00 68.00 C
ANISOU 3210 C9 OLA A2409 5814 10239 9782 707 -930 396 C
HETATM 3211 C10 OLA A2409 -3.325 0.708 9.242 1.00 73.19 C
ANISOU 3211 C10 OLA A2409 6497 10951 10360 525 -767 391 C
HETATM 3212 C11 OLA A2409 -2.896 -0.356 8.260 1.00 81.25 C
ANISOU 3212 C11 OLA A2409 7647 11953 11270 332 -932 408 C
HETATM 3213 C1 OLA A2410 35.188 -25.221 13.081 1.00 58.86 C
ANISOU 3213 C1 OLA A2410 6147 6006 10211 1367 -206 -423 C
HETATM 3214 O1 OLA A2410 35.051 -25.142 11.841 1.00 74.68 O
ANISOU 3214 O1 OLA A2410 8159 8040 12175 1320 9 -633 O
HETATM 3215 O2 OLA A2410 35.244 -26.350 13.616 1.00 65.76 O1-
ANISOU 3215 O2 OLA A2410 7061 6650 11274 1466 -339 -330 O1-
HETATM 3216 C2 OLA A2410 35.294 -23.972 13.923 1.00 53.79 C
ANISOU 3216 C2 OLA A2410 5461 5591 9386 1307 -310 -284 C
HETATM 3217 C3 OLA A2410 34.473 -22.844 13.311 1.00 51.13 C
ANISOU 3217 C3 OLA A2410 5209 5475 8741 1130 -161 -343 C
HETATM 3218 C4 OLA A2410 35.288 -21.558 13.234 1.00 54.18 C
ANISOU 3218 C4 OLA A2410 5433 6065 9087 1118 -120 -397 C
HETATM 3219 C5 OLA A2410 35.923 -21.227 14.580 1.00 50.95 C
ANISOU 3219 C5 OLA A2410 4938 5690 8731 1184 -354 -227 C
HETATM 3220 C1 OLA A2411 15.752 11.932 6.378 1.00 56.44 C
ANISOU 3220 C1 OLA A2411 7836 7425 6183 142 -544 480 C
HETATM 3221 O1 OLA A2411 15.613 13.020 5.779 1.00 73.61 O1-
ANISOU 3221 O1 OLA A2411 10129 9465 8376 154 -629 567 O1-
HETATM 3222 O2 OLA A2411 15.138 11.745 7.450 1.00 65.45 O
ANISOU 3222 O2 OLA A2411 8860 8607 7401 253 -529 394 O
HETATM 3223 C2 OLA A2411 16.651 10.865 5.804 1.00 57.18 C
ANISOU 3223 C2 OLA A2411 7936 7625 6165 -2 -453 481 C
HETATM 3224 C3 OLA A2411 16.858 11.161 4.325 1.00 59.46 C
ANISOU 3224 C3 OLA A2411 8375 7874 6343 -99 -493 602 C
HETATM 3225 C4 OLA A2411 16.887 9.881 3.501 1.00 62.30 C
ANISOU 3225 C4 OLA A2411 8724 8370 6577 -177 -458 602 C
HETATM 3226 C5 OLA A2411 18.026 8.977 3.956 1.00 64.28 C
ANISOU 3226 C5 OLA A2411 8904 8698 6822 -260 -304 510 C
HETATM 3227 C6 OLA A2411 17.539 7.557 4.220 1.00 60.40 C
ANISOU 3227 C6 OLA A2411 8290 8336 6325 -232 -288 438 C
HETATM 3228 C7 OLA A2411 18.530 6.554 3.643 1.00 60.03 C
ANISOU 3228 C7 OLA A2411 8255 8357 6195 -346 -169 401 C
HETATM 3229 C8 OLA A2411 17.871 5.225 3.294 1.00 47.39 C
ANISOU 3229 C8 OLA A2411 6602 6855 4548 -343 -190 361 C
HETATM 3230 C9 OLA A2411 18.605 4.626 2.118 1.00 60.09 C
ANISOU 3230 C9 OLA A2411 8308 8501 6024 -457 -109 352 C
HETATM 3231 C10 OLA A2411 18.423 3.210 1.763 1.00 41.07 C
ANISOU 3231 C10 OLA A2411 5863 6170 3571 -482 -86 280 C
HETATM 3232 C11 OLA A2411 18.481 2.156 2.843 1.00 53.30 C
ANISOU 3232 C11 OLA A2411 7254 7756 5243 -439 -40 196 C
HETATM 3233 C12 OLA A2411 18.648 0.776 2.215 1.00 53.77 C
ANISOU 3233 C12 OLA A2411 7319 7863 5249 -493 10 120 C
HETATM 3234 C13 OLA A2411 18.706 -0.313 3.283 1.00 56.45 C
ANISOU 3234 C13 OLA A2411 7513 8218 5718 -452 48 56 C
HETATM 3235 C14 OLA A2411 19.797 -1.333 2.976 1.00 52.78 C
ANISOU 3235 C14 OLA A2411 7044 7756 5253 -501 176 -31 C
HETATM 3236 C1 OLA A2412 3.732 15.533 -4.574 1.00 62.01 C
ANISOU 3236 C1 OLA A2412 8909 7750 6902 944 -3305 1874 C
HETATM 3237 O1 OLA A2412 3.385 16.420 -5.385 1.00 74.31 O1-
ANISOU 3237 O1 OLA A2412 10628 9173 8432 1007 -3555 2053 O1-
HETATM 3238 O2 OLA A2412 4.103 14.423 -5.013 1.00 72.39 O
ANISOU 3238 O2 OLA A2412 10273 9230 8004 776 -3240 1817 O
HETATM 3239 C2 OLA A2412 3.700 15.795 -3.087 1.00 59.81 C
ANISOU 3239 C2 OLA A2412 8395 7429 6900 1072 -3090 1726 C
HETATM 3240 C3 OLA A2412 4.847 15.056 -2.406 1.00 63.11 C
ANISOU 3240 C3 OLA A2412 8828 7949 7203 920 -2758 1585 C
HETATM 3241 C4 OLA A2412 5.892 16.024 -1.864 1.00 68.37 C
ANISOU 3241 C4 OLA A2412 9645 8456 7877 910 -2578 1591 C
HETATM 3242 C5 OLA A2412 7.062 15.270 -1.242 1.00 74.08 C
ANISOU 3242 C5 OLA A2412 10376 9284 8489 758 -2278 1458 C
HETATM 3243 C6 OLA A2412 8.159 15.021 -2.272 1.00 65.70 C
ANISOU 3243 C6 OLA A2412 9585 8250 7128 546 -2225 1543 C
HETATM 3244 C7 OLA A2412 8.320 13.534 -2.570 1.00 52.38 C
ANISOU 3244 C7 OLA A2412 7846 6773 5283 414 -2149 1453 C
HETATM 3245 C8 OLA A2412 9.717 13.243 -3.109 1.00 58.68 C
ANISOU 3245 C8 OLA A2412 8859 7602 5833 214 -1968 1465 C
HETATM 3246 C9 OLA A2412 9.966 11.754 -3.143 1.00 57.68 C
ANISOU 3246 C9 OLA A2412 8653 7664 5599 106 -1851 1336 C
HETATM 3247 C10 OLA A2412 11.313 11.254 -3.453 1.00 56.52 C
ANISOU 3247 C10 OLA A2412 8644 7571 5261 -67 -1633 1299 C
HETATM 3248 C1 OLA A2413 42.442 -22.371 22.887 1.00 96.59 C
ANISOU 3248 C1 OLA A2413 9980 11144 15576 2072 -2534 772 C
HETATM 3249 O1 OLA A2413 42.813 -22.609 21.718 1.00107.40 O
ANISOU 3249 O1 OLA A2413 11158 12458 17193 2118 -2296 575 O
HETATM 3250 O2 OLA A2413 42.373 -23.312 23.708 1.00 97.41 O1-
ANISOU 3250 O2 OLA A2413 10213 11087 15713 2172 -2761 967 O1-
HETATM 3251 C2 OLA A2413 42.074 -20.966 23.294 1.00 81.69 C
ANISOU 3251 C2 OLA A2413 8182 9508 13351 1899 -2542 773 C
HETATM 3252 C3 OLA A2413 41.284 -20.326 22.160 1.00 83.11 C
ANISOU 3252 C3 OLA A2413 8409 9800 13368 1745 -2177 607 C
HETATM 3253 C4 OLA A2413 41.723 -18.885 21.946 1.00 70.59 C
ANISOU 3253 C4 OLA A2413 6680 8424 11718 1638 -2124 480 C
HETATM 3254 C5 OLA A2413 41.599 -18.111 23.251 1.00 72.66 C
ANISOU 3254 C5 OLA A2413 7082 8809 11716 1574 -2389 620 C
HETATM 3255 C6 OLA A2413 41.037 -16.720 22.998 1.00 77.73 C
ANISOU 3255 C6 OLA A2413 7801 9650 12083 1394 -2234 531 C
HETATM 3256 C7 OLA A2413 42.171 -15.708 22.927 1.00 90.09 C
ANISOU 3256 C7 OLA A2413 9103 11317 13812 1370 -2308 413 C
HETATM 3257 C8 OLA A2413 41.733 -14.367 23.499 1.00 65.74 C
ANISOU 3257 C8 OLA A2413 6164 8403 10412 1221 -2363 418 C
HETATM 3258 C9 OLA A2413 40.822 -13.687 22.508 1.00 80.52 C
ANISOU 3258 C9 OLA A2413 8132 10358 12106 1084 -2033 313 C
HETATM 3259 C10 OLA A2413 40.856 -12.224 22.392 1.00 82.08 C
ANISOU 3259 C10 OLA A2413 8310 10696 12179 944 -1983 219 C
HETATM 3260 C11 OLA A2413 41.110 -11.391 23.625 1.00 81.45 C
ANISOU 3260 C11 OLA A2413 8299 10699 11950 905 -2266 272 C
HETATM 3261 C1 OLA A2414 28.400 -15.765 5.511 1.00104.29 C
ANISOU 3261 C1 OLA A2414 12753 13407 13466 31 832 -933 C
HETATM 3262 O1 OLA A2414 29.178 -16.368 4.738 1.00 93.82 O1-
ANISOU 3262 O1 OLA A2414 11402 12016 12228 77 961 -1086 O1-
HETATM 3263 O2 OLA A2414 27.303 -15.357 5.071 1.00105.82 O
ANISOU 3263 O2 OLA A2414 13069 13666 13473 -64 800 -911 O
HETATM 3264 C2 OLA A2414 28.779 -15.533 6.955 1.00 87.04 C
ANISOU 3264 C2 OLA A2414 10454 11221 11396 95 710 -784 C
HETATM 3265 C3 OLA A2414 29.273 -14.103 7.149 1.00 73.69 C
ANISOU 3265 C3 OLA A2414 8701 9673 9627 67 730 -733 C
HETATM 3266 C4 OLA A2414 28.433 -13.365 8.186 1.00 58.92 C
ANISOU 3266 C4 OLA A2414 6866 7872 7648 33 588 -574 C
HETATM 3267 C5 OLA A2414 29.071 -12.037 8.580 1.00 60.72 C
ANISOU 3267 C5 OLA A2414 7023 8205 7843 21 583 -528 C
HETATM 3268 C6 OLA A2414 28.949 -11.821 10.085 1.00 74.93 C
ANISOU 3268 C6 OLA A2414 8793 10013 9664 60 424 -392 C
HETATM 3269 C7 OLA A2414 30.233 -11.249 10.676 1.00 59.66 C
ANISOU 3269 C7 OLA A2414 6720 8102 7846 104 391 -387 C
HETATM 3270 C8 OLA A2414 30.103 -9.751 10.936 1.00 48.75 C
ANISOU 3270 C8 OLA A2414 5361 6828 6334 40 365 -343 C
HETATM 3271 C9 OLA A2414 31.164 -9.306 11.916 1.00 51.97 C
ANISOU 3271 C9 OLA A2414 5646 7245 6856 82 264 -312 C
HETATM 3272 C10 OLA A2414 30.953 -8.097 12.726 1.00 55.72 C
ANISOU 3272 C10 OLA A2414 6159 7792 7222 46 167 -248 C
HETATM 3273 C1 OLA A2415 28.335 -21.778 30.652 1.00 82.38 C
ANISOU 3273 C1 OLA A2415 11347 10115 9839 663 -1849 2549 C
HETATM 3274 O1 OLA A2415 27.913 -22.941 30.829 1.00 88.38 O
ANISOU 3274 O1 OLA A2415 12211 10702 10667 638 -1834 2733 O
HETATM 3275 O2 OLA A2415 29.350 -21.399 31.275 1.00102.74 O1-
ANISOU 3275 O2 OLA A2415 13926 12736 12372 758 -2088 2558 O1-
HETATM 3276 C2 OLA A2415 27.628 -20.851 29.692 1.00 63.77 C
ANISOU 3276 C2 OLA A2415 8865 7900 7463 578 -1599 2325 C
HETATM 3277 C3 OLA A2415 27.614 -19.437 30.261 1.00 77.31 C
ANISOU 3277 C3 OLA A2415 10625 9857 8893 558 -1604 2238 C
HETATM 3278 C4 OLA A2415 28.535 -18.503 29.482 1.00 71.25 C
ANISOU 3278 C4 OLA A2415 9645 9152 8276 618 -1656 1996 C
HETATM 3279 C5 OLA A2415 28.259 -17.039 29.815 1.00 61.58 C
ANISOU 3279 C5 OLA A2415 8458 8149 6791 570 -1603 1879 C
HETATM 3280 C6 OLA A2415 26.784 -16.793 30.116 1.00 60.20 C
ANISOU 3280 C6 OLA A2415 8426 8081 6364 460 -1372 1932 C
HETATM 3281 C7 OLA A2415 26.568 -15.489 30.874 1.00 70.47 C
ANISOU 3281 C7 OLA A2415 9833 9583 7361 438 -1364 1864 C
HETATM 3282 C8 OLA A2415 25.390 -15.630 31.828 1.00 67.07 C
ANISOU 3282 C8 OLA A2415 9619 9236 6629 364 -1224 2018 C
HETATM 3283 C9 OLA A2415 24.171 -16.092 31.066 1.00 72.65 C
ANISOU 3283 C9 OLA A2415 10264 9908 7433 276 -960 2030 C
HETATM 3284 C10 OLA A2415 23.129 -16.861 31.763 1.00 72.61 C
ANISOU 3284 C10 OLA A2415 10416 9894 7277 196 -824 2237 C
HETATM 3285 C11 OLA A2415 23.512 -18.047 32.619 1.00 71.86 C
ANISOU 3285 C11 OLA A2415 10484 9671 7149 213 -975 2488 C
HETATM 3286 C12 OLA A2415 22.270 -18.624 33.288 1.00 75.45 C
ANISOU 3286 C12 OLA A2415 11097 10147 7422 101 -774 2687 C
HETATM 3287 C13 OLA A2415 21.438 -17.509 33.910 1.00 72.40 C
ANISOU 3287 C13 OLA A2415 10799 9991 6717 56 -594 2621 C
HETATM 3288 C14 OLA A2415 21.393 -17.621 35.430 1.00 74.59 C
ANISOU 3288 C14 OLA A2415 11364 10349 6627 45 -637 2818 C
HETATM 3289 C15 OLA A2415 22.409 -16.682 36.068 1.00 71.39 C
ANISOU 3289 C15 OLA A2415 11049 10048 6027 143 -865 2715 C
HETATM 3290 C16 OLA A2415 21.849 -15.268 36.185 1.00 84.53 C
ANISOU 3290 C16 OLA A2415 12710 11918 7488 134 -703 2510 C
HETATM 3291 C17 OLA A2415 20.933 -15.118 37.397 1.00 71.66 C
ANISOU 3291 C17 OLA A2415 11327 10438 5464 73 -520 2628 C
HETATM 3292 C18 OLA A2415 20.127 -13.824 37.328 1.00 67.93 C
ANISOU 3292 C18 OLA A2415 10809 10144 4857 64 -292 2414 C
HETATM 3293 C1 OLA A2416 23.131 13.643 1.319 1.00 69.29 C
ANISOU 3293 C1 OLA A2416 10119 8808 7402 -895 45 891 C
HETATM 3294 O1 OLA A2416 23.860 14.603 0.985 1.00 70.03 O
ANISOU 3294 O1 OLA A2416 10305 8778 7526 -1013 96 977 O
HETATM 3295 O2 OLA A2416 21.942 13.867 1.634 1.00 74.90 O1-
ANISOU 3295 O2 OLA A2416 10842 9485 8132 -750 -114 898 O1-
HETATM 3296 C2 OLA A2416 23.679 12.235 1.340 1.00 53.05 C
ANISOU 3296 C2 OLA A2416 7929 6925 5303 -925 175 781 C
HETATM 3297 C3 OLA A2416 23.544 11.607 -0.040 1.00 79.60 C
ANISOU 3297 C3 OLA A2416 11410 10382 8453 -991 238 844 C
HETATM 3298 C4 OLA A2416 22.769 10.295 0.029 1.00 70.03 C
ANISOU 3298 C4 OLA A2416 10118 9310 7180 -893 192 753 C
HETATM 3299 C5 OLA A2416 23.476 9.272 0.909 1.00 47.13 C
ANISOU 3299 C5 OLA A2416 7019 6496 4391 -880 295 605 C
HETATM 3300 C6 OLA A2416 23.365 7.874 0.311 1.00 66.95 C
ANISOU 3300 C6 OLA A2416 9510 9141 6788 -884 359 537 C
HETATM 3301 C7 OLA A2416 22.235 7.082 0.959 1.00 61.53 C
ANISOU 3301 C7 OLA A2416 8732 8509 6136 -752 229 474 C
HETATM 3302 C1 OLA A2417 1.623 -17.731 13.417 1.00 60.03 C
ANISOU 3302 C1 OLA A2417 5718 8428 8664 -1600 276 855 C
HETATM 3303 O1 OLA A2417 0.923 -17.822 12.385 1.00 71.62 O
ANISOU 3303 O1 OLA A2417 7069 9881 10260 -1678 110 765 O
HETATM 3304 O2 OLA A2417 1.693 -18.707 14.194 1.00 52.62 O1-
ANISOU 3304 O2 OLA A2417 4816 7393 7785 -1695 389 971 O1-
HETATM 3305 C2 OLA A2417 2.371 -16.456 13.721 1.00 46.88 C
ANISOU 3305 C2 OLA A2417 4154 6884 6774 -1399 326 827 C
HETATM 3306 C3 OLA A2417 1.437 -15.268 13.548 1.00 47.20 C
ANISOU 3306 C3 OLA A2417 4002 7085 6846 -1325 316 794 C
HETATM 3307 C4 OLA A2417 1.451 -14.380 14.785 1.00 69.48 C
ANISOU 3307 C4 OLA A2417 6807 10038 9553 -1199 522 870 C
HETATM 3308 C5 OLA A2417 1.728 -12.933 14.394 1.00 57.44 C
ANISOU 3308 C5 OLA A2417 5314 8611 7901 -1024 456 776 C
HETATM 3309 C6 OLA A2417 0.431 -12.180 14.127 1.00 47.74 C
ANISOU 3309 C6 OLA A2417 3829 7489 6820 -998 432 754 C
HETATM 3310 C7 OLA A2417 0.595 -10.695 14.427 1.00 45.78 C
ANISOU 3310 C7 OLA A2417 3601 7347 6448 -804 478 714 C
HETATM 3311 C8 OLA A2417 1.147 -9.962 13.212 1.00 44.30 C
ANISOU 3311 C8 OLA A2417 3527 7131 6175 -726 260 610 C
HETATM 3312 C9 OLA A2417 0.825 -8.490 13.326 1.00 60.35 C
ANISOU 3312 C9 OLA A2417 5495 9256 8181 -557 271 576 C
HETATM 3313 C1 OLA A2418 -2.291 12.188 26.328 1.00 78.35 C
ANISOU 3313 C1 OLA A2418 8156 11622 9991 2645 2509 -1317 C
HETATM 3314 O1 OLA A2418 -3.527 12.300 26.180 1.00 68.08 O
ANISOU 3314 O1 OLA A2418 6541 10363 8963 2768 2625 -1333 O
HETATM 3315 O2 OLA A2418 -1.572 13.207 26.245 1.00 92.32 O1-
ANISOU 3315 O2 OLA A2418 10148 13217 11711 2726 2360 -1421 O1-
HETATM 3316 C2 OLA A2418 -1.674 10.838 26.601 1.00 68.98 C
ANISOU 3316 C2 OLA A2418 7069 10580 8558 2401 2540 -1170 C
HETATM 3317 C3 OLA A2418 -2.318 9.789 25.703 1.00 62.85 C
ANISOU 3317 C3 OLA A2418 6009 9883 7987 2275 2468 -979 C
HETATM 3318 C4 OLA A2418 -2.403 8.445 26.416 1.00 62.89 C
ANISOU 3318 C4 OLA A2418 5992 10078 7824 2099 2678 -873 C
HETATM 3319 C5 OLA A2418 -2.250 7.296 25.428 1.00 60.55 C
ANISOU 3319 C5 OLA A2418 5600 9799 7606 1896 2485 -670 C
HETATM 3320 C6 OLA A2418 -2.949 6.037 25.926 1.00 61.74 C
ANISOU 3320 C6 OLA A2418 5573 10124 7761 1759 2714 -558 C
HETATM 3321 C7 OLA A2418 -3.643 5.330 24.770 1.00 61.30 C
ANISOU 3321 C7 OLA A2418 5224 10071 7995 1663 2560 -422 C
HETATM 3322 C8 OLA A2418 -3.072 3.944 24.498 1.00 59.18 C
ANISOU 3322 C8 OLA A2418 5032 9837 7616 1418 2474 -253 C
HETATM 3323 C9 OLA A2418 -3.375 3.014 25.649 1.00 60.77 C
ANISOU 3323 C9 OLA A2418 5223 10189 7679 1311 2785 -193 C
HETATM 3324 C10 OLA A2418 -3.180 1.567 25.475 1.00 59.69 C
ANISOU 3324 C10 OLA A2418 5082 10089 7508 1080 2756 -18 C
HETATM 3325 C11 OLA A2418 -3.642 0.913 24.195 1.00 58.90 C
ANISOU 3325 C11 OLA A2418 4750 9945 7682 970 2540 83 C
HETATM 3326 C12 OLA A2418 -3.248 -0.560 24.170 1.00 78.23 C
ANISOU 3326 C12 OLA A2418 7265 12407 10050 735 2520 242 C
HETATM 3327 C13 OLA A2418 -4.222 -1.431 24.954 1.00 77.49 C
ANISOU 3327 C13 OLA A2418 6973 12441 10029 629 2819 331 C
HETATM 3328 C14 OLA A2418 -3.622 -2.815 25.179 1.00 83.02 C
ANISOU 3328 C14 OLA A2418 7826 13132 10586 410 2819 488 C
HETATM 3329 C1 OLA A2419 2.034 6.958 29.712 1.00 74.20 C
ANISOU 3329 C1 OLA A2419 8689 11644 7860 1681 2719 -851 C
HETATM 3330 O1 OLA A2419 1.800 8.185 29.772 1.00 85.02 O
ANISOU 3330 O1 OLA A2419 10070 12931 9302 1854 2732 -1027 O
HETATM 3331 O2 OLA A2419 1.408 6.180 30.464 1.00 67.34 O1-
ANISOU 3331 O2 OLA A2419 7757 10930 6901 1629 2972 -786 O1-
HETATM 3332 C2 OLA A2419 3.057 6.421 28.741 1.00 64.87 C
ANISOU 3332 C2 OLA A2419 7570 10372 6706 1536 2413 -717 C
HETATM 3333 C3 OLA A2419 3.717 5.181 29.334 1.00 73.25 C
ANISOU 3333 C3 OLA A2419 8775 11526 7531 1365 2435 -578 C
HETATM 3334 C4 OLA A2419 3.404 3.934 28.516 1.00 71.50 C
ANISOU 3334 C4 OLA A2419 8360 11332 7476 1216 2384 -380 C
HETATM 3335 C5 OLA A2419 1.907 3.644 28.496 1.00 85.98 C
ANISOU 3335 C5 OLA A2419 9897 13262 9509 1242 2611 -347 C
HETATM 3336 C6 OLA A2419 1.645 2.148 28.618 1.00 85.47 C
ANISOU 3336 C6 OLA A2419 9751 13289 9435 1062 2701 -154 C
HETATM 3337 C7 OLA A2419 1.608 1.492 27.243 1.00 61.35 C
ANISOU 3337 C7 OLA A2419 6524 10158 6627 957 2482 -38 C
HETATM 3338 C8 OLA A2419 0.992 0.100 27.309 1.00 63.37 C
ANISOU 3338 C8 OLA A2419 6631 10494 6954 794 2602 132 C
HETATM 3339 C9 OLA A2419 -0.312 0.148 28.071 1.00 81.98 C
ANISOU 3339 C9 OLA A2419 8792 12981 9374 839 2928 114 C
HETATM 3340 C10 OLA A2419 -0.886 -1.103 28.588 1.00 84.27 C
ANISOU 3340 C10 OLA A2419 8991 13369 9660 680 3130 274 C
HETATM 3341 C11 OLA A2419 -0.669 -2.383 27.816 1.00 84.60 C
ANISOU 3341 C11 OLA A2419 8978 13349 9818 487 2966 444 C
HETATM 3342 C12 OLA A2419 -1.040 -3.580 28.683 1.00 74.89 C
ANISOU 3342 C12 OLA A2419 7749 12205 8499 327 3200 608 C
HETATM 3343 C13 OLA A2419 -0.618 -4.879 28.008 1.00 68.47 C
ANISOU 3343 C13 OLA A2419 6947 11300 7770 137 3017 770 C
HETATM 3344 C1 OLA A2420 34.840 9.809 30.223 1.00 77.86 C
ANISOU 3344 C1 OLA A2420 10426 10548 8609 -385 -2664 -1315 C
HETATM 3345 O1 OLA A2420 33.664 10.152 29.970 1.00 74.41 O
ANISOU 3345 O1 OLA A2420 10124 10101 8046 -322 -2444 -1325 O
HETATM 3346 O2 OLA A2420 35.568 10.589 30.873 1.00 77.28 O1-
ANISOU 3346 O2 OLA A2420 10397 10412 8555 -463 -2900 -1451 O1-
HETATM 3347 C2 OLA A2420 35.367 8.471 29.760 1.00 69.82 C
ANISOU 3347 C2 OLA A2420 9190 9608 7731 -363 -2654 -1150 C
HETATM 3348 C3 OLA A2420 35.282 7.464 30.902 1.00 67.28 C
ANISOU 3348 C3 OLA A2420 8990 9406 7167 -265 -2798 -1086 C
HETATM 3349 C4 OLA A2420 36.079 6.205 30.580 1.00 62.32 C
ANISOU 3349 C4 OLA A2420 8133 8822 6723 -247 -2865 -942 C
HETATM 3350 C5 OLA A2420 35.436 5.445 29.427 1.00 56.54 C
ANISOU 3350 C5 OLA A2420 7290 8105 6087 -202 -2568 -813 C
HETATM 3351 C6 OLA A2420 35.977 4.023 29.328 1.00 71.68 C
ANISOU 3351 C6 OLA A2420 9049 10071 8117 -146 -2622 -670 C
HETATM 3352 C7 OLA A2420 34.833 3.020 29.240 1.00 68.63 C
ANISOU 3352 C7 OLA A2420 8769 9748 7558 -45 -2419 -541 C
HETATM 3353 C8 OLA A2420 35.323 1.594 29.004 1.00 48.46 C
ANISOU 3353 C8 OLA A2420 6057 7210 5145 13 -2449 -400 C
HETATM 3354 C9 OLA A2420 34.558 0.651 29.904 1.00 48.75 C
ANISOU 3354 C9 OLA A2420 6294 7318 4912 108 -2460 -282 C
HETATM 3355 C10 OLA A2420 34.514 -0.795 29.635 1.00 55.09 C
ANISOU 3355 C10 OLA A2420 7018 8123 5792 179 -2409 -126 C
HETATM 3356 C11 OLA A2420 33.831 -1.310 28.388 1.00 58.72 C
ANISOU 3356 C11 OLA A2420 7380 8557 6372 186 -2118 -75 C
HETATM 3357 C12 OLA A2420 33.631 -2.818 28.501 1.00 61.01 C
ANISOU 3357 C12 OLA A2420 7671 8845 6665 265 -2105 85 C
HETATM 3358 C13 OLA A2420 32.907 -3.380 27.283 1.00 43.65 C
ANISOU 3358 C13 OLA A2420 5393 6618 4575 266 -1830 124 C
HETATM 3359 C1 OLA A2421 3.648 12.885 9.139 1.00 85.44 C
ANISOU 3359 C1 OLA A2421 10072 11276 11115 1518 -988 319 C
HETATM 3360 O1 OLA A2421 4.309 13.877 8.761 1.00 85.73 O
ANISOU 3360 O1 OLA A2421 10311 11152 11110 1529 -1067 357 O
HETATM 3361 O2 OLA A2421 2.505 13.060 9.614 1.00 92.85 O1-
ANISOU 3361 O2 OLA A2421 10792 12238 12247 1673 -964 272 O1-
HETATM 3362 C2 OLA A2421 4.222 11.494 9.014 1.00 64.43 C
ANISOU 3362 C2 OLA A2421 7424 8768 8288 1321 -916 330 C
HETATM 3363 C3 OLA A2421 3.835 10.919 7.657 1.00 81.11 C
ANISOU 3363 C3 OLA A2421 9521 10923 10376 1233 -1117 443 C
HETATM 3364 C4 OLA A2421 3.597 9.416 7.736 1.00 55.42 C
ANISOU 3364 C4 OLA A2421 6131 7840 7088 1110 -1050 424 C
HETATM 3365 C5 OLA A2421 2.605 8.968 6.668 1.00 60.86 C
ANISOU 3365 C5 OLA A2421 6697 8573 7853 1091 -1262 500 C
HETATM 3366 C6 OLA A2421 2.077 7.569 6.957 1.00 58.66 C
ANISOU 3366 C6 OLA A2421 6224 8447 7617 998 -1188 465 C
HETATM 3367 C7 OLA A2421 2.317 6.645 5.770 1.00 58.51 C
ANISOU 3367 C7 OLA A2421 6296 8472 7464 828 -1335 518 C
HETATM 3368 C8 OLA A2421 1.579 5.327 5.967 1.00 61.61 C
ANISOU 3368 C8 OLA A2421 6472 8988 7949 743 -1302 488 C
HETATM 3369 C9 OLA A2421 1.248 4.717 4.625 1.00 67.79 C
ANISOU 3369 C9 OLA A2421 7282 9792 8682 633 -1540 537 C
HETATM 3370 C10 OLA A2421 0.405 3.514 4.565 1.00 61.31 C
ANISOU 3370 C10 OLA A2421 6252 9066 7976 540 -1577 515 C
HETATM 3371 C11 OLA A2421 0.637 2.388 5.546 1.00 59.17 C
ANISOU 3371 C11 OLA A2421 5896 8867 7719 446 -1341 455 C
HETATM 3372 C12 OLA A2421 -0.449 1.330 5.385 1.00 70.66 C
ANISOU 3372 C12 OLA A2421 7109 10397 9343 358 -1417 448 C
HETATM 3373 C1 OLA A2422 18.149 -9.726 2.837 1.00 68.73 C
ANISOU 3373 C1 OLA A2422 8884 9592 7637 -584 132 -444 C
HETATM 3374 O1 OLA A2422 17.550 -10.021 1.780 1.00 83.02 O1-
ANISOU 3374 O1 OLA A2422 10785 11404 9355 -648 67 -507 O1-
HETATM 3375 O2 OLA A2422 18.390 -10.625 3.672 1.00 54.65 O
ANISOU 3375 O2 OLA A2422 7024 7743 5999 -556 161 -443 O
HETATM 3376 C2 OLA A2422 18.568 -8.300 3.104 1.00 60.61 C
ANISOU 3376 C2 OLA A2422 7852 8630 6546 -547 162 -366 C
HETATM 3377 C3 OLA A2422 17.355 -7.469 3.508 1.00 46.90 C
ANISOU 3377 C3 OLA A2422 6074 6946 4799 -535 45 -262 C
HETATM 3378 C4 OLA A2422 17.362 -6.121 2.793 1.00 52.03 C
ANISOU 3378 C4 OLA A2422 6813 7647 5309 -542 20 -224 C
HETATM 3379 C5 OLA A2422 16.235 -5.214 3.280 1.00 33.02 C
ANISOU 3379 C5 OLA A2422 4349 5276 2921 -504 -91 -125 C
HETATM 3380 C6 OLA A2422 15.983 -4.074 2.297 1.00 51.45 C
ANISOU 3380 C6 OLA A2422 6794 7637 5115 -519 -160 -85 C
HETATM 3381 C7 OLA A2422 14.501 -3.726 2.212 1.00 33.97 C
ANISOU 3381 C7 OLA A2422 4535 5450 2922 -501 -323 -26 C
HETATM 3382 C1 OLA A2423 30.253 -15.226 12.260 1.00 69.24 C
ANISOU 3382 C1 OLA A2423 7919 8936 9454 338 170 -272 C
HETATM 3383 O1 OLA A2423 29.785 -14.867 11.158 1.00 71.35 O
ANISOU 3383 O1 OLA A2423 8240 9254 9615 262 298 -366 O
HETATM 3384 O2 OLA A2423 30.504 -16.436 12.446 1.00 71.58 O1-
ANISOU 3384 O2 OLA A2423 8197 9087 9912 414 130 -265 O1-
HETATM 3385 C2 OLA A2423 30.511 -14.214 13.352 1.00 70.76 C
ANISOU 3385 C2 OLA A2423 8081 9229 9574 338 53 -170 C
HETATM 3386 C3 OLA A2423 30.473 -14.918 14.704 1.00 75.61 C
ANISOU 3386 C3 OLA A2423 8722 9772 10232 405 -118 -24 C
HETATM 3387 C4 OLA A2423 29.490 -14.245 15.657 1.00 61.05 C
ANISOU 3387 C4 OLA A2423 6999 8026 8172 348 -192 103 C
HETATM 3388 C5 OLA A2423 30.191 -13.231 16.555 1.00 64.46 C
ANISOU 3388 C5 OLA A2423 7384 8549 8560 367 -304 139 C
HETATM 3389 C6 OLA A2423 29.972 -11.804 16.066 1.00 70.32 C
ANISOU 3389 C6 OLA A2423 8132 9418 9168 287 -225 69 C
HETATM 3390 C7 OLA A2423 29.714 -10.854 17.230 1.00 35.46 C
ANISOU 3390 C7 OLA A2423 3786 5095 4592 272 -336 148 C
HETATM 3391 C8 OLA A2423 31.021 -10.361 17.839 1.00 40.66 C
ANISOU 3391 C8 OLA A2423 4336 5767 5345 314 -464 132 C
HETATM 3392 C9 OLA A2423 30.776 -9.072 18.588 1.00 53.75 C
ANISOU 3392 C9 OLA A2423 6066 7527 6831 271 -532 147 C
HETATM 3393 C1 OLA A2424 21.841 -12.810 3.790 1.00 76.66 C
ANISOU 3393 C1 OLA A2424 9763 10310 9055 -434 460 -674 C
HETATM 3394 O1 OLA A2424 20.819 -13.487 3.549 1.00 69.02 O
ANISOU 3394 O1 OLA A2424 8836 9300 8086 -486 378 -690 O
HETATM 3395 O2 OLA A2424 22.773 -13.328 4.442 1.00 83.42 O1-
ANISOU 3395 O2 OLA A2424 10539 11100 10057 -364 511 -681 O1-
HETATM 3396 C2 OLA A2424 21.943 -11.388 3.293 1.00 76.93 C
ANISOU 3396 C2 OLA A2424 9839 10461 8928 -460 486 -643 C
HETATM 3397 C3 OLA A2424 23.026 -10.635 4.059 1.00 68.47 C
ANISOU 3397 C3 OLA A2424 8676 9420 7920 -401 549 -588 C
HETATM 3398 C4 OLA A2424 22.673 -9.156 4.156 1.00 59.73 C
ANISOU 3398 C4 OLA A2424 7588 8408 6697 -424 510 -494 C
HETATM 3399 C5 OLA A2424 23.785 -8.340 4.805 1.00 72.56 C
ANISOU 3399 C5 OLA A2424 9132 10055 8381 -385 566 -457 C
HETATM 3400 C6 OLA A2424 23.271 -6.996 5.320 1.00 67.40 C
ANISOU 3400 C6 OLA A2424 8487 9463 7659 -390 493 -351 C
HETATM 3401 C7 OLA A2424 21.749 -6.957 5.425 1.00 64.89 C
ANISOU 3401 C7 OLA A2424 8209 9167 7281 -401 379 -293 C
HETATM 3402 C8 OLA A2424 21.197 -5.593 5.022 1.00 60.17 C
ANISOU 3402 C8 OLA A2424 7677 8623 6562 -426 335 -235 C
HETATM 3403 C9 OLA A2424 21.754 -5.188 3.678 1.00 54.22 C
ANISOU 3403 C9 OLA A2424 7028 7884 5691 -487 412 -282 C
HETATM 3404 C1 OLA A2425 4.848 -21.685 18.264 1.00 67.63 C
ANISOU 3404 C1 OLA A2425 7421 8877 9398 -1699 801 1536 C
HETATM 3405 O1 OLA A2425 5.849 -21.496 17.541 1.00 60.08 O
ANISOU 3405 O1 OLA A2425 6578 7870 8378 -1590 662 1400 O
HETATM 3406 O2 OLA A2425 4.618 -22.838 18.692 1.00 66.22 O1-
ANISOU 3406 O2 OLA A2425 7271 8546 9345 -1837 844 1673 O1-
HETATM 3407 C2 OLA A2425 3.927 -20.537 18.608 1.00 56.87 C
ANISOU 3407 C2 OLA A2425 5885 7748 7976 -1662 923 1534 C
HETATM 3408 C3 OLA A2425 3.740 -19.668 17.371 1.00 52.67 C
ANISOU 3408 C3 OLA A2425 5251 7296 7468 -1597 779 1335 C
HETATM 3409 C4 OLA A2425 3.156 -18.306 17.729 1.00 64.82 C
ANISOU 3409 C4 OLA A2425 6661 9057 8911 -1493 879 1313 C
HETATM 3410 C5 OLA A2425 4.152 -17.462 18.517 1.00 63.34 C
ANISOU 3410 C5 OLA A2425 6641 8957 8468 -1318 944 1324 C
HETATM 3411 C6 OLA A2425 3.512 -16.151 18.958 1.00 60.88 C
ANISOU 3411 C6 OLA A2425 6210 8848 8076 -1217 1060 1299 C
HETATM 3412 C7 OLA A2425 3.674 -15.097 17.869 1.00 51.24 C
ANISOU 3412 C7 OLA A2425 4954 7680 6835 -1106 905 1127 C
HETATM 3413 C8 OLA A2425 3.555 -13.678 18.414 1.00 55.90 C
ANISOU 3413 C8 OLA A2425 5518 8433 7288 -952 999 1090 C
HETATM 3414 C9 OLA A2425 4.305 -12.758 17.481 1.00 57.01 C
ANISOU 3414 C9 OLA A2425 5741 8575 7346 -831 832 948 C
HETATM 3415 C10 OLA A2425 4.538 -11.345 17.815 1.00 63.79 C
ANISOU 3415 C10 OLA A2425 6632 9544 8063 -670 869 888 C
HETATM 3416 C11 OLA A2425 3.378 -10.398 18.009 1.00 66.46 C
ANISOU 3416 C11 OLA A2425 6778 10007 8467 -608 956 864 C
HETATM 3417 C12 OLA A2425 3.904 -8.970 18.090 1.00 49.58 C
ANISOU 3417 C12 OLA A2425 4727 7928 6184 -437 937 774 C
HETATM 3418 C13 OLA A2425 2.761 -7.964 18.024 1.00 43.05 C
ANISOU 3418 C13 OLA A2425 3701 7197 5459 -354 982 727 C
HETATM 3419 C1 OLA A2426 31.103 13.526 7.621 1.00 74.93 C
ANISOU 3419 C1 OLA A2426 9746 9470 9254 -1317 312 190 C
HETATM 3420 O1 OLA A2426 30.912 14.762 7.615 1.00 74.57 O
ANISOU 3420 O1 OLA A2426 9824 9264 9246 -1364 248 237 O
HETATM 3421 O2 OLA A2426 31.654 13.001 8.613 1.00 69.26 O1-
ANISOU 3421 O2 OLA A2426 8877 8808 8632 -1284 252 81 O1-
HETATM 3422 C2 OLA A2426 30.673 12.678 6.447 1.00 62.72 C
ANISOU 3422 C2 OLA A2426 8246 8037 7548 -1301 446 261 C
HETATM 3423 C3 OLA A2426 31.438 11.359 6.461 1.00 68.87 C
ANISOU 3423 C3 OLA A2426 8838 8964 8364 -1301 549 188 C
HETATM 3424 C4 OLA A2426 30.493 10.181 6.674 1.00 63.01 C
ANISOU 3424 C4 OLA A2426 8100 8340 7501 -1141 507 146 C
HETATM 3425 C5 OLA A2426 31.257 8.865 6.769 1.00 47.49 C
ANISOU 3425 C5 OLA A2426 5954 6494 5596 -1126 592 69 C
HETATM 3426 C6 OLA A2426 30.367 7.680 6.411 1.00 49.22 C
ANISOU 3426 C6 OLA A2426 6212 6815 5672 -1018 612 60 C
HETATM 3427 C7 OLA A2426 31.176 6.519 5.843 1.00 55.69 C
ANISOU 3427 C7 OLA A2426 6907 7725 6526 -1043 766 11 C
HETATM 3428 C8 OLA A2426 30.274 5.526 5.117 1.00 56.62 C
ANISOU 3428 C8 OLA A2426 7114 7918 6481 -975 807 12 C
HETATM 3429 C9 OLA A2426 29.207 6.265 4.342 1.00 61.12 C
ANISOU 3429 C9 OLA A2426 7892 8454 6877 -991 774 107 C
HETATM 3430 C10 OLA A2426 28.167 5.511 3.628 1.00 63.27 C
ANISOU 3430 C10 OLA A2426 8272 8786 6982 -935 767 117 C
HETATM 3431 C11 OLA A2426 28.540 4.257 2.874 1.00 69.73 C
ANISOU 3431 C11 OLA A2426 9053 9688 7754 -946 906 51 C
HETATM 3432 C12 OLA A2426 27.315 3.721 2.143 1.00 49.71 C
ANISOU 3432 C12 OLA A2426 6660 7193 5036 -903 855 68 C
HETATM 3433 C1 OLA A2427 8.514 -0.897 33.154 1.00 70.45 C
ANISOU 3433 C1 OLA A2427 9538 11411 5817 622 2169 224 C
HETATM 3434 O1 OLA A2427 7.345 -0.509 33.366 1.00 88.64 O
ANISOU 3434 O1 OLA A2427 11721 13796 8162 679 2420 165 O
HETATM 3435 O2 OLA A2427 9.455 -0.086 33.293 1.00 56.67 O1-
ANISOU 3435 O2 OLA A2427 7950 9612 3969 682 1991 95 O1-
HETATM 3436 C2 OLA A2427 8.784 -2.324 32.740 1.00 68.23 C
ANISOU 3436 C2 OLA A2427 9204 11089 5630 481 2084 443 C
HETATM 3437 C3 OLA A2427 8.832 -3.208 33.980 1.00 54.86 C
ANISOU 3437 C3 OLA A2427 7706 9484 3654 408 2201 595 C
HETATM 3438 C4 OLA A2427 7.686 -4.212 33.990 1.00 58.62 C
ANISOU 3438 C4 OLA A2427 8022 10018 4234 308 2439 763 C
HETATM 3439 C5 OLA A2427 7.904 -5.302 32.948 1.00 59.28 C
ANISOU 3439 C5 OLA A2427 7960 9984 4580 196 2284 910 C
HETATM 3440 C6 OLA A2427 6.591 -6.006 32.632 1.00 72.70 C
ANISOU 3440 C6 OLA A2427 9422 11720 6483 107 2504 1017 C
HETATM 3441 C7 OLA A2427 6.453 -6.254 31.136 1.00 65.41 C
ANISOU 3441 C7 OLA A2427 8255 10684 5915 70 2352 1007 C
HETATM 3442 C8 OLA A2427 6.293 -7.735 30.807 1.00 52.88 C
ANISOU 3442 C8 OLA A2427 6598 9025 4468 -91 2338 1208 C
HETATM 3443 C9 OLA A2427 5.574 -7.835 29.483 1.00 71.51 C
ANISOU 3443 C9 OLA A2427 8671 11329 7172 -126 2296 1172 C
HETATM 3444 C10 OLA A2427 4.970 -9.091 29.016 1.00 67.50 C
ANISOU 3444 C10 OLA A2427 8013 10762 6872 -283 2329 1322 C
HETATM 3445 C11 OLA A2427 5.828 -10.253 28.578 1.00 75.37 C
ANISOU 3445 C11 OLA A2427 9100 11610 7928 -382 2133 1440 C
HETATM 3446 C12 OLA A2427 5.060 -11.018 27.508 1.00 81.99 C
ANISOU 3446 C12 OLA A2427 9700 12371 9081 -500 2108 1479 C
HETATM 3447 C13 OLA A2427 5.889 -12.142 26.901 1.00 84.82 C
ANISOU 3447 C13 OLA A2427 10135 12559 9534 -588 1905 1560 C
HETATM 3448 C14 OLA A2427 5.198 -13.481 27.124 1.00 74.70 C
ANISOU 3448 C14 OLA A2427 8792 11219 8371 -762 2017 1745 C
HETATM 3449 C15 OLA A2427 6.171 -14.636 26.933 1.00 59.00 C
ANISOU 3449 C15 OLA A2427 6954 9053 6411 -829 1843 1850 C
HETATM 3450 C16 OLA A2427 5.428 -15.967 26.936 1.00 63.14 C
ANISOU 3450 C16 OLA A2427 7398 9483 7111 -1015 1929 2019 C
HETATM 3451 C17 OLA A2427 6.356 -17.118 27.306 1.00 67.04 C
ANISOU 3451 C17 OLA A2427 8101 9812 7558 -1068 1821 2176 C
HETATM 3452 C18 OLA A2427 5.641 -18.458 27.176 1.00 63.24 C
ANISOU 3452 C18 OLA A2427 7542 9198 7289 -1262 1884 2335 C
HETATM 3453 C1 OLA A2428 4.516 5.501 33.236 1.00 87.52 C
ANISOU 3453 C1 OLA A2428 11268 13577 8408 1427 2870 -798 C
HETATM 3454 O1 OLA A2428 4.381 6.735 33.079 1.00 97.97 O
ANISOU 3454 O1 OLA A2428 12589 14810 9824 1577 2846 -988 O
HETATM 3455 O2 OLA A2428 3.606 4.862 33.806 1.00 97.28 O1-
ANISOU 3455 O2 OLA A2428 12407 14955 9599 1402 3148 -726 O1-
HETATM 3456 C2 OLA A2428 5.760 4.796 32.749 1.00 83.03 C
ANISOU 3456 C2 OLA A2428 10811 12939 7798 1281 2576 -658 C
HETATM 3457 C3 OLA A2428 5.868 3.404 33.363 1.00 74.63 C
ANISOU 3457 C3 OLA A2428 9815 11991 6551 1132 2662 -460 C
HETATM 3458 C4 OLA A2428 6.265 2.368 32.315 1.00 72.80 C
ANISOU 3458 C4 OLA A2428 9457 11695 6508 992 2467 -268 C
HETATM 3459 C5 OLA A2428 5.157 2.123 31.297 1.00 79.35 C
ANISOU 3459 C5 OLA A2428 9956 12518 7675 987 2538 -209 C
HETATM 3460 C6 OLA A2428 5.324 0.766 30.619 1.00 71.25 C
ANISOU 3460 C6 OLA A2428 8832 11473 6766 823 2436 0 C
HETATM 3461 C7 OLA A2428 4.072 -0.087 30.788 1.00 80.95 C
ANISOU 3461 C7 OLA A2428 9853 12805 8097 755 2687 120 C
HETATM 3462 C8 OLA A2428 4.351 -1.565 30.535 1.00 56.05 C
ANISOU 3462 C8 OLA A2428 6689 9636 4971 576 2618 333 C
HETATM 3463 C9 OLA A2428 4.293 -1.843 29.052 1.00 53.11 C
ANISOU 3463 C9 OLA A2428 6114 9159 4906 527 2418 369 C
HETATM 3464 C10 OLA A2428 3.646 -3.069 28.556 1.00 79.00 C
ANISOU 3464 C10 OLA A2428 9205 12439 8372 383 2457 529 C
HETATM 3465 C11 OLA A2428 3.806 -4.376 29.296 1.00 67.08 C
ANISOU 3465 C11 OLA A2428 7800 10961 6726 237 2550 712 C
HETATM 3466 C12 OLA A2428 2.972 -5.453 28.610 1.00 62.95 C
ANISOU 3466 C12 OLA A2428 7038 10417 6464 97 2583 844 C
HETATM 3467 C1 OLA A2429 37.794 -20.673 25.951 1.00 79.65 C
ANISOU 3467 C1 OLA A2429 9080 9448 11736 1506 -2589 1354 C
HETATM 3468 O1 OLA A2429 38.514 -20.765 24.932 1.00 91.39 O1-
ANISOU 3468 O1 OLA A2429 10315 10880 13527 1569 -2483 1177 O1-
HETATM 3469 O2 OLA A2429 38.007 -21.445 26.912 1.00 67.28 O
ANISOU 3469 O2 OLA A2429 7618 7767 10176 1593 -2834 1553 O
HETATM 3470 C2 OLA A2429 36.688 -19.646 26.021 1.00 82.03 C
ANISOU 3470 C2 OLA A2429 9556 9945 11666 1334 -2421 1328 C
HETATM 3471 C3 OLA A2429 36.783 -18.698 24.830 1.00 55.13 C
ANISOU 3471 C3 OLA A2429 5973 6652 8322 1262 -2186 1086 C
HETATM 3472 C4 OLA A2429 36.610 -17.240 25.246 1.00 68.13 C
ANISOU 3472 C4 OLA A2429 7669 8513 9703 1154 -2198 1036 C
HETATM 3473 C5 OLA A2429 36.493 -16.353 24.011 1.00 61.55 C
ANISOU 3473 C5 OLA A2429 6707 7773 8904 1066 -1939 826 C
HETATM 3474 C6 OLA A2429 37.053 -14.954 24.246 1.00 78.88 C
ANISOU 3474 C6 OLA A2429 8818 10124 11029 1008 -2012 733 C
HETATM 3475 C7 OLA A2429 35.972 -13.886 24.116 1.00 58.86 C
ANISOU 3475 C7 OLA A2429 6440 7732 8193 869 -1843 686 C
HETATM 3476 C8 OLA A2429 35.597 -13.320 25.483 1.00 49.13 C
ANISOU 3476 C8 OLA A2429 5412 6596 6660 837 -2020 794 C
HETATM 3477 C9 OLA A2429 34.790 -14.333 26.262 1.00 72.87 C
ANISOU 3477 C9 OLA A2429 8638 9541 9510 865 -2065 986 C
HETATM 3478 C10 OLA A2429 33.977 -13.919 27.416 1.00 80.58 C
ANISOU 3478 C10 OLA A2429 9871 10618 10128 812 -2124 1095 C
HETATM 3479 C18 OLC A2430 15.330 -2.308 36.294 1.00 66.82 C
ANISOU 3479 C18 OLC A2430 10267 10807 4314 474 948 443 C
HETATM 3480 C10 OLC A2430 16.155 -9.263 39.866 1.00 76.18 C
ANISOU 3480 C10 OLC A2430 12192 11960 4795 55 789 1805 C
HETATM 3481 C9 OLC A2430 14.942 -9.484 39.339 1.00 82.91 C
ANISOU 3481 C9 OLC A2430 12866 12835 5802 9 1091 1834 C
HETATM 3482 C17 OLC A2430 16.303 -2.670 35.176 1.00 56.34 C
ANISOU 3482 C17 OLC A2430 8785 9342 3281 441 698 481 C
HETATM 3483 C11 OLC A2430 16.834 -7.919 39.869 1.00 63.19 C
ANISOU 3483 C11 OLC A2430 10570 10352 3087 151 630 1542 C
HETATM 3484 C8 OLC A2430 14.254 -10.826 39.331 1.00 82.73 C
ANISOU 3484 C8 OLC A2430 12809 12756 5869 -108 1246 2091 C
HETATM 3485 C24 OLC A2430 9.127 -18.556 37.428 1.00 70.86 C
ANISOU 3485 C24 OLC A2430 10609 10626 5688 -1035 2242 3412 C
HETATM 3486 C16 OLC A2430 17.405 -3.626 35.651 1.00 65.07 C
ANISOU 3486 C16 OLC A2430 10016 10410 4296 396 465 637 C
HETATM 3487 C12 OLC A2430 16.545 -7.027 38.641 1.00 60.07 C
ANISOU 3487 C12 OLC A2430 9918 9948 2957 222 703 1339 C
HETATM 3488 C7 OLC A2430 13.702 -11.279 37.957 1.00 85.89 C
ANISOU 3488 C7 OLC A2430 12890 13081 6664 -140 1335 2114 C
HETATM 3489 C15 OLC A2430 16.857 -4.690 36.612 1.00 54.83 C
ANISOU 3489 C15 OLC A2430 8867 9192 2774 346 602 845 C
HETATM 3490 C13 OLC A2430 17.814 -6.731 37.822 1.00 59.77 C
ANISOU 3490 C13 OLC A2430 9766 9786 3160 263 378 1236 C
HETATM 3491 C6 OLC A2430 12.241 -10.830 37.726 1.00 69.96 C
ANISOU 3491 C6 OLC A2430 10695 11172 4716 -170 1688 2034 C
HETATM 3492 C14 OLC A2430 17.542 -6.056 36.468 1.00 56.25 C
ANISOU 3492 C14 OLC A2430 9039 9280 3051 286 434 1066 C
HETATM 3493 C5 OLC A2430 11.575 -11.438 36.472 1.00 60.29 C
ANISOU 3493 C5 OLC A2430 9166 9844 3899 -244 1758 2064 C
HETATM 3494 C4 OLC A2430 10.672 -12.655 36.787 1.00 62.50 C
ANISOU 3494 C4 OLC A2430 9433 10106 4208 -391 1972 2314 C
HETATM 3495 C3 OLC A2430 9.173 -12.331 36.646 1.00 68.96 C
ANISOU 3495 C3 OLC A2430 10046 11039 5118 -439 2319 2262 C
HETATM 3496 C2 OLC A2430 8.256 -13.513 37.036 1.00 82.56 C
ANISOU 3496 C2 OLC A2430 11754 12708 6907 -613 2525 2476 C
HETATM 3497 C21 OLC A2430 8.027 -16.896 35.875 1.00 80.82 C
ANISOU 3497 C21 OLC A2430 11365 12088 7253 -950 2423 3014 C
HETATM 3498 C1 OLC A2430 8.141 -14.512 35.914 1.00 93.69 C
ANISOU 3498 C1 OLC A2430 12952 13978 8668 -705 2451 2600 C
HETATM 3499 C22 OLC A2430 9.039 -18.076 35.940 1.00 76.42 C
ANISOU 3499 C22 OLC A2430 10987 11320 6728 -986 2168 3211 C
HETATM 3500 O19 OLC A2430 7.575 -14.351 34.845 1.00 70.52 O
ANISOU 3500 O19 OLC A2430 9742 11012 6040 -718 2472 2486 O
HETATM 3501 O25 OLC A2430 7.824 -18.499 37.930 1.00 99.11 O
ANISOU 3501 O25 OLC A2430 14133 14285 9239 -1146 2570 3398 O
HETATM 3502 O23 OLC A2430 8.481 -19.085 35.153 1.00 80.46 O
ANISOU 3502 O23 OLC A2430 11320 11673 7580 -1122 2197 3302 O
HETATM 3503 O20 OLC A2430 8.758 -15.711 36.170 1.00101.83 O
ANISOU 3503 O20 OLC A2430 14141 14861 9687 -783 2309 2826 O
HETATM 3504 C10 OLC A2431 28.655 -6.081 32.872 1.00 49.87 C
ANISOU 3504 C10 OLC A2431 7376 7710 3862 424 -1781 741 C
HETATM 3505 C9 OLC A2431 29.491 -5.032 32.912 1.00 73.62 C
ANISOU 3505 C9 OLC A2431 10337 10723 6911 414 -1940 583 C
HETATM 3506 C11 OLC A2431 27.162 -5.945 32.695 1.00 57.75 C
ANISOU 3506 C11 OLC A2431 8448 8767 4728 399 -1473 745 C
HETATM 3507 C8 OLC A2431 29.035 -3.597 32.786 1.00 68.80 C
ANISOU 3507 C8 OLC A2431 9766 10163 6214 381 -1831 395 C
HETATM 3508 C24 OLC A2431 32.831 7.995 34.319 1.00 66.22 C
ANISOU 3508 C24 OLC A2431 9757 9468 5937 -45 -2826 -1273 C
HETATM 3509 C12 OLC A2431 26.336 -7.229 32.932 1.00 59.26 C
ANISOU 3509 C12 OLC A2431 8716 8951 4851 396 -1342 949 C
HETATM 3510 C7 OLC A2431 29.700 -2.762 31.665 1.00 65.60 C
ANISOU 3510 C7 OLC A2431 9139 9690 6097 343 -1839 243 C
HETATM 3511 C6 OLC A2431 30.327 -1.456 32.198 1.00 52.41 C
ANISOU 3511 C6 OLC A2431 7528 8031 4353 315 -2011 75 C
HETATM 3512 C5 OLC A2431 29.647 -0.164 31.691 1.00 58.60 C
ANISOU 3512 C5 OLC A2431 8326 8814 5127 282 -1833 -84 C
HETATM 3513 C4 OLC A2431 30.640 0.985 31.368 1.00 47.47 C
ANISOU 3513 C4 OLC A2431 6813 7339 3886 223 -1982 -246 C
HETATM 3514 C3 OLC A2431 31.893 0.980 32.262 1.00 49.92 C
ANISOU 3514 C3 OLC A2431 7139 7646 4181 211 -2316 -267 C
HETATM 3515 C2 OLC A2431 31.887 2.099 33.327 1.00 70.40 C
ANISOU 3515 C2 OLC A2431 9951 10268 6528 194 -2452 -418 C
HETATM 3516 C21 OLC A2431 32.672 5.565 33.680 1.00 63.23 C
ANISOU 3516 C21 OLC A2431 9162 9215 5648 43 -2680 -909 C
HETATM 3517 C1 OLC A2431 32.204 3.443 32.717 1.00 66.30 C
ANISOU 3517 C1 OLC A2431 9346 9667 6178 122 -2446 -595 C
HETATM 3518 C22 OLC A2431 31.916 6.733 34.376 1.00 64.07 C
ANISOU 3518 C22 OLC A2431 9528 9315 5500 57 -2628 -1087 C
HETATM 3519 O19 OLC A2431 32.821 3.651 31.691 1.00 80.39 O
ANISOU 3519 O19 OLC A2431 10904 11376 8266 66 -2431 -614 O
HETATM 3520 O25 OLC A2431 32.005 9.028 33.867 1.00 67.70 O
ANISOU 3520 O25 OLC A2431 10009 9580 6133 -40 -2620 -1388 O
HETATM 3521 O23 OLC A2431 30.782 6.954 33.593 1.00 73.33 O
ANISOU 3521 O23 OLC A2431 10684 10472 6704 96 -2312 -1076 O
HETATM 3522 O20 OLC A2431 31.735 4.516 33.437 1.00 66.04 O
ANISOU 3522 O20 OLC A2431 9529 9642 5921 120 -2453 -747 O
HETATM 3523 C10 OLC A2432 4.311 -6.979 22.539 1.00 55.74 C
ANISOU 3523 C10 OLC A2432 5793 8998 6390 -137 1529 812 C
HETATM 3524 C9 OLC A2432 5.609 -7.214 22.787 1.00 64.37 C
ANISOU 3524 C9 OLC A2432 7108 10030 7320 -136 1438 827 C
HETATM 3525 C11 OLC A2432 3.588 -5.735 22.994 1.00 62.47 C
ANISOU 3525 C11 OLC A2432 6558 9949 7227 -2 1658 721 C
HETATM 3526 C8 OLC A2432 6.365 -8.446 22.347 1.00 56.79 C
ANISOU 3526 C8 OLC A2432 6228 8955 6393 -249 1314 906 C
HETATM 3527 C24 OLC A2432 7.314 -21.752 23.535 1.00 79.87 C
ANISOU 3527 C24 OLC A2432 9642 10528 10175 -1441 1193 2190 C
HETATM 3528 C12 OLC A2432 2.055 -5.866 23.172 1.00 74.50 C
ANISOU 3528 C12 OLC A2432 7816 11562 8930 -29 1840 752 C
HETATM 3529 C7 OLC A2432 5.532 -9.736 22.134 1.00 77.90 C
ANISOU 3529 C7 OLC A2432 8768 11592 9239 -403 1366 1018 C
HETATM 3530 C13 OLC A2432 1.472 -7.131 22.508 1.00 70.13 C
ANISOU 3530 C13 OLC A2432 7101 10961 8585 -202 1795 854 C
HETATM 3531 C6 OLC A2432 5.828 -10.820 23.202 1.00 76.04 C
ANISOU 3531 C6 OLC A2432 8660 11330 8902 -488 1468 1173 C
HETATM 3532 C14 OLC A2432 0.960 -6.903 21.073 1.00 71.15 C
ANISOU 3532 C14 OLC A2432 7045 11042 8946 -204 1594 789 C
HETATM 3533 C5 OLC A2432 5.505 -12.266 22.750 1.00 68.14 C
ANISOU 3533 C5 OLC A2432 7592 10216 8082 -654 1437 1280 C
HETATM 3534 C4 OLC A2432 6.522 -13.326 23.258 1.00 68.56 C
ANISOU 3534 C4 OLC A2432 7847 10155 8048 -704 1387 1397 C
HETATM 3535 C3 OLC A2432 6.524 -14.617 22.411 1.00 50.39 C
ANISOU 3535 C3 OLC A2432 5505 7690 5951 -837 1278 1440 C
HETATM 3536 C2 OLC A2432 7.323 -15.773 23.055 1.00 62.78 C
ANISOU 3536 C2 OLC A2432 7254 9130 7468 -890 1255 1586 C
HETATM 3537 C21 OLC A2432 6.779 -19.343 23.086 1.00 57.29 C
ANISOU 3537 C21 OLC A2432 6587 8029 7151 -1265 1256 1924 C
HETATM 3538 C1 OLC A2432 6.997 -17.088 22.394 1.00 64.36 C
ANISOU 3538 C1 OLC A2432 7393 9166 7895 -1040 1198 1642 C
HETATM 3539 C22 OLC A2432 7.624 -20.550 22.594 1.00 62.67 C
ANISOU 3539 C22 OLC A2432 7383 8469 7960 -1305 1093 1948 C
HETATM 3540 O19 OLC A2432 6.284 -17.260 21.420 1.00 91.73 O
ANISOU 3540 O19 OLC A2432 10700 12602 11553 -1115 1153 1569 O
HETATM 3541 O25 OLC A2432 6.584 -22.660 22.762 1.00 81.29 O
ANISOU 3541 O25 OLC A2432 9701 10565 10622 -1602 1166 2184 O
HETATM 3542 O23 OLC A2432 7.149 -20.835 21.312 1.00 76.52 O
ANISOU 3542 O23 OLC A2432 8996 10146 9932 -1380 1001 1818 O
HETATM 3543 O20 OLC A2432 7.586 -18.178 22.983 1.00 52.45 O
ANISOU 3543 O20 OLC A2432 6037 7522 6371 -1092 1183 1788 O
HETATM 3544 C10 OLC A2433 1.020 2.115 15.677 1.00 50.98 C
ANISOU 3544 C10 OLC A2433 4508 8170 6692 776 496 183 C
HETATM 3545 C9 OLC A2433 1.118 3.431 15.428 1.00 44.76 C
ANISOU 3545 C9 OLC A2433 3783 7305 5918 922 414 130 C
HETATM 3546 C11 OLC A2433 0.103 1.175 14.932 1.00 53.89 C
ANISOU 3546 C11 OLC A2433 4662 8579 7233 669 405 247 C
HETATM 3547 C8 OLC A2433 2.040 4.365 16.177 1.00 44.05 C
ANISOU 3547 C8 OLC A2433 3909 7159 5668 1013 492 55 C
HETATM 3548 C24 OLC A2433 -1.188 17.192 17.063 1.00 81.30 C
ANISOU 3548 C24 OLC A2433 8686 10613 11593 2916 221 -720 C
HETATM 3549 C12 OLC A2433 -0.312 -0.103 15.699 1.00 60.94 C
ANISOU 3549 C12 OLC A2433 5433 9563 8157 542 589 295 C
HETATM 3550 C7 OLC A2433 1.382 5.627 16.788 1.00 45.96 C
ANISOU 3550 C7 OLC A2433 4080 7376 6008 1216 580 -36 C
HETATM 3551 C6 OLC A2433 2.306 6.868 16.741 1.00 52.26 C
ANISOU 3551 C6 OLC A2433 5109 8041 6706 1304 499 -100 C
HETATM 3552 C5 OLC A2433 1.926 8.009 17.722 1.00 47.09 C
ANISOU 3552 C5 OLC A2433 4449 7353 6089 1495 640 -224 C
HETATM 3553 C4 OLC A2433 1.060 9.119 17.072 1.00 58.32 C
ANISOU 3553 C4 OLC A2433 5747 8675 7737 1667 518 -245 C
HETATM 3554 C3 OLC A2433 1.355 10.541 17.604 1.00 56.13 C
ANISOU 3554 C3 OLC A2433 5613 8265 7450 1835 547 -367 C
HETATM 3555 C2 OLC A2433 0.445 11.604 16.945 1.00 51.99 C
ANISOU 3555 C2 OLC A2433 4956 7622 7177 2018 415 -376 C
HETATM 3556 C21 OLC A2433 -0.137 15.111 18.006 1.00 71.43 C
ANISOU 3556 C21 OLC A2433 7530 9697 9913 2562 480 -696 C
HETATM 3557 C1 OLC A2433 0.134 12.755 17.873 1.00 67.83 C
ANISOU 3557 C1 OLC A2433 6977 9548 9249 2227 553 -532 C
HETATM 3558 C22 OLC A2433 0.146 16.376 17.148 1.00 89.72 C
ANISOU 3558 C22 OLC A2433 9987 11763 12340 2656 236 -669 C
HETATM 3559 O19 OLC A2433 -0.357 12.690 18.985 1.00 65.09 O
ANISOU 3559 O19 OLC A2433 6542 9292 8898 2306 797 -640 O
HETATM 3560 O25 OLC A2433 -1.042 18.045 15.966 1.00 76.80 O
ANISOU 3560 O25 OLC A2433 8212 9834 11133 2963 -58 -621 O
HETATM 3561 O23 OLC A2433 1.099 17.098 17.870 1.00 84.66 O
ANISOU 3561 O23 OLC A2433 9607 11007 11551 2665 300 -791 O
HETATM 3562 O20 OLC A2433 0.447 13.989 17.353 1.00 70.20 O
ANISOU 3562 O20 OLC A2433 7414 9642 9615 2332 384 -552 O
HETATM 3563 C1 PEG A2434 11.546 -28.412 38.065 1.00 85.50 C
ANISOU 3563 C1 PEG A2434 13338 10622 8526 -1566 1342 5116 C
HETATM 3564 O1 PEG A2434 10.550 -29.068 38.830 1.00 87.23 O
ANISOU 3564 O1 PEG A2434 13668 10798 8679 -1724 1608 5276 O
HETATM 3565 C2 PEG A2434 12.176 -27.295 38.838 1.00 83.03 C
ANISOU 3565 C2 PEG A2434 13173 10547 7828 -1397 1277 5018 C
HETATM 3566 O2 PEG A2434 13.139 -26.643 38.022 1.00 79.44 O
ANISOU 3566 O2 PEG A2434 12589 10131 7464 -1258 1020 4855 O
HETATM 3567 C3 PEG A2434 13.737 -25.518 38.651 1.00 81.69 C
ANISOU 3567 C3 PEG A2434 12987 10637 7414 -1106 943 4729 C
HETATM 3568 C4 PEG A2434 14.660 -24.827 37.695 1.00 79.72 C
ANISOU 3568 C4 PEG A2434 12568 10420 7304 -976 700 4530 C
HETATM 3569 O4 PEG A2434 15.721 -25.683 37.308 1.00 75.01 O
ANISOU 3569 O4 PEG A2434 11997 9559 6946 -892 392 4591 O
HETATM 3570 C1 PEG A2435 10.033 -23.568 34.807 1.00 80.84 C
ANISOU 3570 C1 PEG A2435 11681 10888 8149 -1378 1685 3975 C
HETATM 3571 O1 PEG A2435 8.684 -23.903 35.085 1.00 95.97 O
ANISOU 3571 O1 PEG A2435 13510 12858 10098 -1565 1994 4104 O
HETATM 3572 C2 PEG A2435 10.293 -22.113 35.044 1.00 82.82 C
ANISOU 3572 C2 PEG A2435 11933 11384 8149 -1225 1695 3762 C
HETATM 3573 O2 PEG A2435 11.655 -21.823 34.764 1.00 80.31 O
ANISOU 3573 O2 PEG A2435 11686 11002 7825 -1057 1385 3644 O
HETATM 3574 C3 PEG A2435 12.167 -20.766 35.559 1.00 76.39 C
ANISOU 3574 C3 PEG A2435 11340 10698 6988 -932 1350 3565 C
HETATM 3575 C4 PEG A2435 13.605 -20.528 35.219 1.00 76.10 C
ANISOU 3575 C4 PEG A2435 11345 10579 6989 -773 1018 3449 C
HETATM 3576 O4 PEG A2435 14.359 -21.722 35.340 1.00 92.99 O
ANISOU 3576 O4 PEG A2435 13609 12492 9232 -778 814 3645 O
HETATM 3577 O HOH A2501 2.020 -28.546 -0.263 1.00 91.53 O
HETATM 3578 O HOH A2502 38.752 -61.275 11.591 1.00 91.17 O
HETATM 3579 O HOH A2503 20.506 10.571 23.295 1.00 30.02 O
HETATM 3580 O HOH A2504 25.855 -58.404 23.271 1.00 65.35 O
HETATM 3581 O HOH A2505 29.409 17.823 17.555 1.00 78.70 O
HETATM 3582 O HOH A2506 35.545 -63.612 11.940 1.00 95.24 O
HETATM 3583 O HOH A2507 14.609 16.917 2.056 1.00 50.01 O
HETATM 3584 O HOH A2508 31.143 -41.767 23.357 1.00 61.18 O
HETATM 3585 O HOH A2509 13.974 -14.851 24.855 1.00 40.95 O
HETATM 3586 O HOH A2510 17.179 -6.106 15.708 1.00 39.61 O
HETATM 3587 O HOH A2511 16.398 -28.665 21.658 1.00 34.30 O
HETATM 3588 O HOH A2512 14.053 -16.103 14.578 1.00 36.91 O
HETATM 3589 O HOH A2513 20.005 -35.941 26.619 1.00 53.67 O
HETATM 3590 O HOH A2514 13.863 -13.316 13.447 1.00 29.84 O
HETATM 3591 O HOH A2515 25.689 -13.915 3.766 1.00 59.97 O
HETATM 3592 O HOH A2516 28.884 -34.573 22.026 1.00 57.05 O
HETATM 3593 O HOH A2517 24.495 10.160 17.863 1.00 35.75 O
HETATM 3594 O HOH A2518 6.411 -24.343 19.681 1.00 79.77 O
HETATM 3595 O HOH A2519 13.854 11.918 16.759 1.00 34.50 O
HETATM 3596 O HOH A2520 11.418 -30.198 0.298 1.00 72.95 O
HETATM 3597 O HOH A2521 -0.035 20.342 16.457 1.00 65.82 O
HETATM 3598 O HOH A2522 22.737 -17.549 19.286 1.00 26.43 O
HETATM 3599 O HOH A2523 3.991 18.996 17.208 1.00 52.88 O
HETATM 3600 O HOH A2524 13.885 2.296 15.722 1.00 32.42 O
HETATM 3601 O HOH A2525 16.178 24.092 29.411 1.00 72.74 O
HETATM 3602 O HOH A2526 38.769 -63.204 19.785 1.00 61.45 O
HETATM 3603 O HOH A2527 11.656 2.815 16.950 1.00 22.30 O
HETATM 3604 O HOH A2528 46.201 -56.736 31.060 1.00 92.25 O
HETATM 3605 O HOH A2529 6.636 14.579 7.865 1.00 82.57 O
HETATM 3606 O HOH A2530 20.392 -11.572 13.102 1.00 23.92 O
HETATM 3607 O HOH A2531 19.046 -36.549 29.599 1.00 59.86 O
HETATM 3608 O HOH A2532 13.360 7.598 13.391 1.00 27.90 O
HETATM 3609 O HOH A2533 15.732 14.826 33.475 1.00 52.61 O
HETATM 3610 O HOH A2534 33.384 -31.780 24.863 1.00 50.32 O
HETATM 3611 O HOH A2535 21.504 -3.044 19.908 1.00 30.16 O
HETATM 3612 O HOH A2536 47.526 -73.513 22.417 1.00 73.62 O
HETATM 3613 O HOH A2537 26.842 -60.690 15.559 1.00 86.02 O
HETATM 3614 O HOH A2538 10.428 9.041 35.714 1.00 56.66 O
HETATM 3615 O HOH A2539 22.795 -25.428 9.543 1.00 46.30 O
HETATM 3616 O HOH A2540 13.063 18.442 22.507 1.00 30.57 O
HETATM 3617 O HOH A2541 10.871 2.377 19.893 1.00 21.31 O
HETATM 3618 O HOH A2542 15.928 -4.774 14.181 1.00 30.96 O
HETATM 3619 O HOH A2543 23.123 0.423 12.575 1.00 33.13 O
HETATM 3620 O HOH A2544 16.940 25.977 5.240 1.00 67.19 O
HETATM 3621 O HOH A2545 22.742 -28.171 16.934 1.00 36.84 O
HETATM 3622 O HOH A2546 34.464 -64.258 17.871 1.00 62.08 O
HETATM 3623 O HOH A2547 18.227 16.138 18.903 1.00 40.37 O
HETATM 3624 O HOH A2548 20.183 -1.784 21.912 1.00 21.31 O
HETATM 3625 O HOH A2549 25.707 -33.671 36.872 1.00 61.00 O
HETATM 3626 O HOH A2550 13.399 -12.515 25.775 1.00 42.86 O
HETATM 3627 O HOH A2551 13.832 4.703 18.876 1.00 34.92 O
HETATM 3628 O HOH A2552 18.531 -11.124 14.883 1.00 34.47 O
HETATM 3629 O HOH A2553 14.330 -31.173 25.657 1.00 63.23 O
HETATM 3630 O HOH A2554 17.408 -29.201 9.015 1.00 52.66 O
HETATM 3631 O HOH A2555 30.016 -23.950 32.260 1.00 61.95 O
HETATM 3632 O HOH A2556 21.791 -17.644 16.919 1.00 30.94 O
HETATM 3633 O HOH A2557 15.112 -11.251 11.161 1.00 21.31 O
HETATM 3634 O HOH A2558 16.643 29.920 4.183 1.00 64.67 O
HETATM 3635 O HOH A2559 12.227 -11.570 6.829 1.00 37.61 O
HETATM 3636 O HOH A2560 29.584 15.720 9.827 1.00 55.51 O
HETATM 3637 O HOH A2561 25.451 -28.265 19.830 1.00 40.13 O
HETATM 3638 O HOH A2562 34.763 17.800 12.709 1.00 62.95 O
HETATM 3639 O HOH A2563 27.174 -44.212 24.459 1.00 74.58 O
HETATM 3640 O HOH A2564 22.019 -49.892 23.774 1.00 99.93 O
HETATM 3641 O HOH A2565 23.911 3.294 22.014 1.00 21.31 O
HETATM 3642 O HOH A2566 13.199 -12.527 21.769 1.00 21.58 O
HETATM 3643 O HOH A2567 23.756 -33.300 15.235 1.00 53.82 O
HETATM 3644 O HOH A2568 23.463 16.712 8.713 1.00 37.21 O
HETATM 3645 O HOH A2569 14.275 9.788 14.024 1.00 44.13 O
HETATM 3646 O HOH A2570 29.156 14.598 24.826 1.00 48.29 O
HETATM 3647 O HOH A2571 -0.927 -22.551 11.223 1.00 45.26 O
HETATM 3648 O HOH A2572 16.596 -31.835 35.674 1.00 72.59 O
HETATM 3649 O HOH A2573 29.564 14.948 19.154 1.00 68.84 O
HETATM 3650 O HOH A2574 18.513 -2.917 23.922 1.00 42.20 O
HETATM 3651 O HOH A2575 19.787 -31.095 20.840 1.00 40.26 O
HETATM 3652 O HOH A2576 4.543 9.562 33.436 1.00 57.24 O
HETATM 3653 O HOH A2577 26.430 -33.909 21.270 1.00 43.99 O
HETATM 3654 O HOH A2578 11.125 -31.233 21.714 1.00 48.60 O
HETATM 3655 O HOH A2579 28.327 11.988 15.802 1.00 39.01 O
HETATM 3656 O HOH A2580 16.037 3.374 17.169 1.00 41.58 O
HETATM 3657 O HOH A2581 15.986 15.735 4.818 1.00 53.78 O
HETATM 3658 O HOH A2582 18.387 -11.338 -0.676 1.00 58.30 O
HETATM 3659 O HOH A2583 39.904 -28.762 20.696 1.00 55.58 O
HETATM 3660 O HOH A2584 25.004 -26.918 17.532 1.00 39.67 O
HETATM 3661 O HOH A2585 11.825 11.215 35.050 1.00 53.33 O
HETATM 3662 O HOH A2586 16.093 13.937 15.683 1.00 34.70 O
HETATM 3663 O HOH A2587 21.082 -31.370 7.884 1.00 59.95 O
HETATM 3664 O HOH A2588 -4.415 15.050 10.325 1.00 56.46 O
HETATM 3665 O HOH A2589 34.532 -37.953 21.453 1.00 56.20 O
HETATM 3666 O HOH A2590 37.163 13.172 22.351 1.00 46.33 O
HETATM 3667 O HOH A2591 13.262 18.835 24.835 1.00 41.90 O
HETATM 3668 O HOH A2592 26.967 18.067 11.300 1.00 56.14 O
HETATM 3669 O HOH A2593 14.721 -29.939 22.739 1.00 37.86 O
HETATM 3670 O HOH A2594 13.746 17.206 26.796 1.00 39.28 O
HETATM 3671 O HOH A2595 11.426 5.151 17.792 1.00 21.31 O
HETATM 3672 O HOH A2596 27.922 14.439 4.756 1.00 55.11 O
HETATM 3673 O HOH A2597 -0.641 15.157 10.660 1.00 79.71 O
HETATM 3674 O HOH A2598 21.761 12.877 23.791 1.00 49.40 O
HETATM 3675 O HOH A2599 27.413 -18.690 3.941 1.00 67.05 O
HETATM 3676 O HOH A2600 35.947 -40.899 22.438 1.00 69.05 O
HETATM 3677 O HOH A2601 14.478 12.998 35.331 1.00 60.32 O
HETATM 3678 O HOH A2602 -0.851 -24.586 -5.463 1.00 97.12 O
HETATM 3679 O HOH A2603 18.755 -34.406 22.744 1.00 59.12 O
HETATM 3680 O HOH A2604 34.210 -60.997 28.602 1.00 57.35 O
HETATM 3681 O HOH A2605 36.495 -63.577 28.295 1.00 57.49 O
HETATM 3682 O HOH A2606 2.796 -31.180 17.363 1.00 45.85 O
HETATM 3683 O HOH A2607 34.814 -25.161 27.893 1.00 63.94 O
HETATM 3684 O HOH A2608 14.128 21.776 12.375 1.00 72.42 O
HETATM 3685 O HOH A2609 8.379 -32.856 18.518 1.00 45.29 O
HETATM 3686 O HOH A2610 4.552 -32.549 11.894 1.00 48.71 O
HETATM 3687 O HOH A2611 16.477 1.491 15.643 1.00 46.69 O
HETATM 3688 O HOH A2612 39.551 -32.279 15.066 1.00 53.06 O
HETATM 3689 O HOH A2613 30.495 13.270 16.680 1.00 56.57 O
HETATM 3690 O HOH A2614 36.275 15.829 21.670 1.00 52.31 O
HETATM 3691 O HOH A2615 22.362 13.355 29.678 1.00 41.87 O
HETATM 3692 O HOH A2616 18.368 -13.853 -1.754 1.00 62.23 O
HETATM 3693 O HOH A2617 -4.643 12.150 7.940 1.00 52.19 O
HETATM 3694 O HOH A2618 18.818 -25.107 37.374 1.00 71.51 O
HETATM 3695 O HOH A2619 24.384 12.126 28.467 1.00 30.93 O
HETATM 3696 O HOH A2620 1.859 5.376 36.402 1.00 74.41 O
HETATM 3697 O HOH A2621 -1.295 -22.704 -4.208 1.00 76.41 O
HETATM 3698 O HOH A2622 27.056 -36.503 28.199 1.00 57.45 O
HETATM 3699 O HOH A2623 8.594 -30.150 29.236 1.00 55.15 O
HETATM 3700 O HOH A2624 17.012 12.394 37.469 1.00 57.58 O
HETATM 3701 O HOH A2625 33.430 11.545 35.293 1.00 66.27 O
HETATM 3702 O HOH A2626 35.956 21.752 18.791 1.00 71.17 O
HETATM 3703 O HOH A2627 17.392 13.893 18.074 1.00 21.31 O
HETATM 3704 O HOH A2628 20.054 12.386 32.758 1.00 45.51 O
HETATM 3705 O HOH A2629 17.371 -25.407 15.059 1.00 55.16 O
HETATM 3706 O HOH A2630 26.936 14.919 -0.059 1.00 81.24 O
HETATM 3707 O HOH A2631 19.447 11.986 2.607 1.00 93.08 O
HETATM 3708 O HOH A2632 8.451 20.020 3.897 1.00 58.13 O
HETATM 3709 O HOH A2633 18.228 -24.751 32.099 1.00 56.64 O
HETATM 3710 O HOH A2634 21.400 -26.571 4.444 1.00 39.31 O
HETATM 3711 O HOH A2635 23.624 13.991 22.175 1.00 53.40 O
HETATM 3712 O HOH A2636 2.530 -30.630 14.297 1.00 56.10 O
HETATM 3713 O HOH A2637 21.987 15.301 5.866 1.00 47.57 O
HETATM 3714 O HOH A2638 19.979 -28.560 8.596 1.00 59.22 O
HETATM 3715 O HOH A2639 22.265 13.595 26.440 1.00 32.06 O
HETATM 3716 O HOH A2640 22.439 -32.957 20.954 1.00 46.26 O
HETATM 3717 O HOH A2641 21.423 -28.233 6.719 1.00 55.94 O
HETATM 3718 O HOH A2642 18.504 12.231 35.024 1.00 52.72 O
HETATM 3719 O HOH A2643 27.984 10.462 32.634 1.00 53.12 O
HETATM 3720 O HOH A2644 34.589 -58.531 7.383 1.00 81.44 O
HETATM 3721 O HOH A2645 32.401 12.529 27.982 1.00 46.46 O
HETATM 3722 O HOH A2646 47.565 -75.468 27.474 1.00 68.11 O
HETATM 3723 O HOH A2647 32.164 -39.293 25.502 1.00 65.52 O
HETATM 3724 O HOH A2648 -0.451 21.272 24.242 1.00 51.50 O
HETATM 3725 O HOH A2649 24.641 18.312 9.940 1.00 46.49 O
HETATM 3726 O HOH A2650 10.542 -31.183 26.635 1.00 52.84 O
HETATM 3727 O HOH A2651 22.775 -30.554 15.104 1.00 46.86 O
HETATM 3728 O HOH A2652 19.471 19.039 15.559 1.00 69.83 O
HETATM 3729 O HOH A2653 13.645 5.679 15.903 1.00 54.48 O
HETATM 3730 O HOH A2654 29.534 -38.098 31.601 1.00 65.73 O
HETATM 3731 O HOH A2655 55.218 -55.679 18.902 1.00 67.49 O
HETATM 3732 O HOH A2656 35.865 -34.907 25.524 1.00 47.69 O
HETATM 3733 O HOH A2657 23.259 -33.779 18.859 1.00 66.25 O
HETATM 3734 O HOH A2658 26.079 13.690 23.839 1.00 48.36 O
HETATM 3735 O HOH A2659 28.846 -29.550 8.074 1.00 61.22 O
HETATM 3736 O HOH A2660 18.548 14.202 4.178 1.00 57.99 O
HETATM 3737 O HOH A2661 18.342 -27.288 17.275 1.00 64.31 O
HETATM 3738 O HOH A2662 41.476 -34.223 24.531 1.00 64.55 O
HETATM 3739 O HOH A2663 17.912 17.228 16.128 1.00 60.03 O
HETATM 3740 O HOH A2664 24.123 -48.476 15.487 1.00 65.40 O
HETATM 3741 O HOH A2665 41.379 -31.116 19.699 1.00 48.23 O
HETATM 3742 O HOH A2666 45.658 -49.783 30.013 1.00 75.43 O
HETATM 3743 O HOH A2667 37.506 -53.586 5.391 1.00 63.88 O
HETATM 3744 O HOH A2668 12.602 22.351 16.045 1.00 81.06 O
HETATM 3745 O HOH A2669 44.265 -59.300 32.963 1.00 74.90 O
HETATM 3746 O HOH A2670 32.082 -17.045 27.754 1.00 76.80 O
HETATM 3747 O HOH A2671 31.613 -38.282 21.604 1.00 56.92 O
HETATM 3748 O HOH A2672 3.557 -1.687 8.717 1.00 48.55 O
HETATM 3749 O HOH A2673 5.748 -19.195 31.583 1.00 45.71 O
HETATM 3750 O HOH A2674 21.060 -34.142 22.406 1.00 41.12 O
HETATM 3751 O HOH A2675 -3.706 14.723 8.193 1.00 70.96 O
HETATM 3752 O HOH A2676 24.737 -18.586 3.948 1.00 52.05 O
HETATM 3753 O HOH A2677 13.850 19.678 9.719 1.00 61.34 O
HETATM 3754 O HOH A2678 28.207 -33.877 38.268 1.00 62.64 O
HETATM 3755 O HOH A2679 3.986 -19.564 -4.817 1.00 72.16 O
HETATM 3756 O HOH A2680 23.206 -30.031 7.163 1.00 60.01 O
HETATM 3757 O HOH A2681 25.528 -30.578 7.778 1.00 71.36 O
HETATM 3758 O HOH A2682 20.711 20.681 8.523 1.00 94.67 O
HETATM 3759 O HOH A2683 26.784 -40.330 18.451 1.00 73.82 O
HETATM 3760 O HOH A2684 21.126 -27.356 10.858 1.00 40.11 O
HETATM 3761 O HOH A2685 29.453 -38.119 20.003 1.00 54.67 O
HETATM 3762 O HOH A2686 29.987 -39.038 33.617 1.00 90.57 O
HETATM 3763 O HOH A2687 16.393 18.400 8.494 1.00 78.69 O
HETATM 3764 O HOH A2688 24.129 -19.859 2.065 1.00 68.60 O
HETATM 3765 O HOH A2689 45.395 -76.279 26.449 1.00 43.31 O
HETATM 3766 O HOH A2690 26.314 -41.983 20.944 1.00 90.97 O
HETATM 3767 O HOH A2691 10.155 -32.393 29.357 1.00 63.14 O
HETATM 3768 O HOH A2692 27.535 17.958 7.095 1.00 67.63 O
HETATM 3769 O HOH A2693 1.321 22.022 14.932 1.00 71.29 O
HETATM 3770 O HOH A2694 1.866 -6.576 6.247 1.00 54.79 O
HETATM 3771 O HOH A2695 19.565 -46.665 13.549 1.00 71.63 O
HETATM 3772 O HOH A2696 33.060 -41.036 30.774 1.00 68.88 O
HETATM 3773 O HOH A2697 26.808 2.710 7.905 1.00 44.84 O
HETATM 3774 O HOH A2698 14.659 22.547 7.919 1.00 81.35 O
HETATM 3775 O HOH A2699 30.533 11.352 2.381 1.00 58.54 O
HETATM 3776 O HOH A2700 19.647 -27.237 12.939 1.00 62.73 O
HETATM 3777 O HOH A2701 41.153 -53.883 4.169 1.00 77.65 O
CONECT 538 1204
CONECT 554 1110
CONECT 574 1248
CONECT 1110 554
CONECT 1204 538
CONECT 1248 574
CONECT 2615 2636
CONECT 2636 2615
CONECT 3007 3008 3016
CONECT 3008 3007 3009
CONECT 3009 3008 3010 3034
CONECT 3010 3009 3011
CONECT 3011 3010 3012 3016
CONECT 3012 3011 3013
CONECT 3013 3012 3014
CONECT 3014 3013 3015 3020
CONECT 3015 3014 3016 3017
CONECT 3016 3007 3011 3015 3025
CONECT 3017 3015 3018
CONECT 3018 3017 3019
CONECT 3019 3018 3020 3023 3024
CONECT 3020 3014 3019 3021
CONECT 3021 3020 3022
CONECT 3022 3021 3023
CONECT 3023 3019 3022 3026
CONECT 3024 3019
CONECT 3025 3016
CONECT 3026 3023 3027 3028
CONECT 3027 3026
CONECT 3028 3026 3029
CONECT 3029 3028 3030
CONECT 3030 3029 3031
CONECT 3031 3030 3032 3033
CONECT 3032 3031
CONECT 3033 3031
CONECT 3034 3009
CONECT 3035 3036 3044
CONECT 3036 3035 3037
CONECT 3037 3036 3038 3062
CONECT 3038 3037 3039
CONECT 3039 3038 3040 3044
CONECT 3040 3039 3041
CONECT 3041 3040 3042
CONECT 3042 3041 3043 3048
CONECT 3043 3042 3044 3045
CONECT 3044 3035 3039 3043 3053
CONECT 3045 3043 3046
CONECT 3046 3045 3047
CONECT 3047 3046 3048 3051 3052
CONECT 3048 3042 3047 3049
CONECT 3049 3048 3050
CONECT 3050 3049 3051
CONECT 3051 3047 3050 3054
CONECT 3052 3047
CONECT 3053 3044
CONECT 3054 3051 3055 3056
CONECT 3055 3054
CONECT 3056 3054 3057
CONECT 3057 3056 3058
CONECT 3058 3057 3059
CONECT 3059 3058 3060 3061
CONECT 3060 3059
CONECT 3061 3059
CONECT 3062 3037
CONECT 3063 3064 3072
CONECT 3064 3063 3065
CONECT 3065 3064 3066 3090
CONECT 3066 3065 3067
CONECT 3067 3066 3068 3072
CONECT 3068 3067 3069
CONECT 3069 3068 3070
CONECT 3070 3069 3071 3076
CONECT 3071 3070 3072 3073
CONECT 3072 3063 3067 3071 3081
CONECT 3073 3071 3074
CONECT 3074 3073 3075
CONECT 3075 3074 3076 3079 3080
CONECT 3076 3070 3075 3077
CONECT 3077 3076 3078
CONECT 3078 3077 3079
CONECT 3079 3075 3078 3082
CONECT 3080 3075
CONECT 3081 3072
CONECT 3082 3079 3083 3084
CONECT 3083 3082
CONECT 3084 3082 3085
CONECT 3085 3084 3086
CONECT 3086 3085 3087
CONECT 3087 3086 3088 3089
CONECT 3088 3087
CONECT 3089 3087
CONECT 3090 3065
CONECT 3091 3092 3113
CONECT 3092 3091 3093
CONECT 3093 3092 3094 3138
CONECT 3094 3093 3115
CONECT 3095 3096 3138
CONECT 3096 3095 3124 3139
CONECT 3097 3109 3116
CONECT 3098 3107 3126 3129
CONECT 3099 3109 3131 3132
CONECT 3100 3101 3129
CONECT 3101 3100 3133
CONECT 3102 3107 3130
CONECT 3103 3126 3127 3128
CONECT 3104 3107 3127 3131
CONECT 3105 3110 3125
CONECT 3106 3108 3134
CONECT 3107 3098 3102 3104
CONECT 3108 3106 3135
CONECT 3109 3097 3099 3140
CONECT 3110 3105 3133
CONECT 3111 3112 3125
CONECT 3112 3111 3133
CONECT 3113 3091 3115 3125
CONECT 3114 3118 3135
CONECT 3115 3094 3113
CONECT 3116 3097 3117
CONECT 3117 3116 3140
CONECT 3118 3114 3136
CONECT 3119 3120 3136
CONECT 3120 3119 3137
CONECT 3121 3122 3137
CONECT 3122 3121 3124
CONECT 3123 3134
CONECT 3124 3096 3122
CONECT 3125 3105 3111 3113
CONECT 3126 3098 3103
CONECT 3127 3103 3104 3132
CONECT 3128 3103
CONECT 3129 3098 3100 3130
CONECT 3130 3102 3129
CONECT 3131 3099 3104
CONECT 3132 3099 3127
CONECT 3133 3101 3110 3112
CONECT 3134 3106 3123
CONECT 3135 3108 3114
CONECT 3136 3118 3119
CONECT 3137 3120 3121
CONECT 3138 3093 3095
CONECT 3139 3096
CONECT 3140 3109 3117
CONECT 3141 3142 3143 3144
CONECT 3142 3141
CONECT 3143 3141
CONECT 3144 3141 3145
CONECT 3145 3144 3146
CONECT 3146 3145 3147
CONECT 3147 3146 3148
CONECT 3148 3147 3149
CONECT 3149 3148
CONECT 3150 3151 3152 3153
CONECT 3151 3150
CONECT 3152 3150
CONECT 3153 3150 3154
CONECT 3154 3153 3155
CONECT 3155 3154 3156
CONECT 3156 3155 3157
CONECT 3157 3156 3158
CONECT 3158 3157 3159
CONECT 3159 3158 3160
CONECT 3160 3159
CONECT 3161 3162 3163 3164
CONECT 3162 3161
CONECT 3163 3161
CONECT 3164 3161 3165
CONECT 3165 3164 3166
CONECT 3166 3165 3167
CONECT 3167 3166 3168
CONECT 3168 3167 3169
CONECT 3169 3168 3170
CONECT 3170 3169 3171
CONECT 3171 3170 3172
CONECT 3172 3171 3173
CONECT 3173 3172 3174
CONECT 3174 3173 3175
CONECT 3175 3174 3176
CONECT 3176 3175 3177
CONECT 3177 3176 3178
CONECT 3178 3177 3179
CONECT 3179 3178 3180
CONECT 3180 3179
CONECT 3181 3182 3183 3184
CONECT 3182 3181
CONECT 3183 3181
CONECT 3184 3181 3185
CONECT 3185 3184 3186
CONECT 3186 3185 3187
CONECT 3187 3186 3188
CONECT 3188 3187 3189
CONECT 3189 3188 3190
CONECT 3190 3189 3191
CONECT 3191 3190 3192
CONECT 3192 3191 3193
CONECT 3193 3192 3194
CONECT 3194 3193 3195
CONECT 3195 3194 3196
CONECT 3196 3195 3197
CONECT 3197 3196 3198
CONECT 3198 3197 3199
CONECT 3199 3198
CONECT 3200 3201 3202 3203
CONECT 3201 3200
CONECT 3202 3200
CONECT 3203 3200 3204
CONECT 3204 3203 3205
CONECT 3205 3204 3206
CONECT 3206 3205 3207
CONECT 3207 3206 3208
CONECT 3208 3207 3209
CONECT 3209 3208 3210
CONECT 3210 3209 3211
CONECT 3211 3210 3212
CONECT 3212 3211
CONECT 3213 3214 3215 3216
CONECT 3214 3213
CONECT 3215 3213
CONECT 3216 3213 3217
CONECT 3217 3216 3218
CONECT 3218 3217 3219
CONECT 3219 3218
CONECT 3220 3221 3222 3223
CONECT 3221 3220
CONECT 3222 3220
CONECT 3223 3220 3224
CONECT 3224 3223 3225
CONECT 3225 3224 3226
CONECT 3226 3225 3227
CONECT 3227 3226 3228
CONECT 3228 3227 3229
CONECT 3229 3228 3230
CONECT 3230 3229 3231
CONECT 3231 3230 3232
CONECT 3232 3231 3233
CONECT 3233 3232 3234
CONECT 3234 3233 3235
CONECT 3235 3234
CONECT 3236 3237 3238 3239
CONECT 3237 3236
CONECT 3238 3236
CONECT 3239 3236 3240
CONECT 3240 3239 3241
CONECT 3241 3240 3242
CONECT 3242 3241 3243
CONECT 3243 3242 3244
CONECT 3244 3243 3245
CONECT 3245 3244 3246
CONECT 3246 3245 3247
CONECT 3247 3246
CONECT 3248 3249 3250 3251
CONECT 3249 3248
CONECT 3250 3248
CONECT 3251 3248 3252
CONECT 3252 3251 3253
CONECT 3253 3252 3254
CONECT 3254 3253 3255
CONECT 3255 3254 3256
CONECT 3256 3255 3257
CONECT 3257 3256 3258
CONECT 3258 3257 3259
CONECT 3259 3258 3260
CONECT 3260 3259
CONECT 3261 3262 3263 3264
CONECT 3262 3261
CONECT 3263 3261
CONECT 3264 3261 3265
CONECT 3265 3264 3266
CONECT 3266 3265 3267
CONECT 3267 3266 3268
CONECT 3268 3267 3269
CONECT 3269 3268 3270
CONECT 3270 3269 3271
CONECT 3271 3270 3272
CONECT 3272 3271
CONECT 3273 3274 3275 3276
CONECT 3274 3273
CONECT 3275 3273
CONECT 3276 3273 3277
CONECT 3277 3276 3278
CONECT 3278 3277 3279
CONECT 3279 3278 3280
CONECT 3280 3279 3281
CONECT 3281 3280 3282
CONECT 3282 3281 3283
CONECT 3283 3282 3284
CONECT 3284 3283 3285
CONECT 3285 3284 3286
CONECT 3286 3285 3287
CONECT 3287 3286 3288
CONECT 3288 3287 3289
CONECT 3289 3288 3290
CONECT 3290 3289 3291
CONECT 3291 3290 3292
CONECT 3292 3291
CONECT 3293 3294 3295 3296
CONECT 3294 3293
CONECT 3295 3293
CONECT 3296 3293 3297
CONECT 3297 3296 3298
CONECT 3298 3297 3299
CONECT 3299 3298 3300
CONECT 3300 3299 3301
CONECT 3301 3300
CONECT 3302 3303 3304 3305
CONECT 3303 3302
CONECT 3304 3302
CONECT 3305 3302 3306
CONECT 3306 3305 3307
CONECT 3307 3306 3308
CONECT 3308 3307 3309
CONECT 3309 3308 3310
CONECT 3310 3309 3311
CONECT 3311 3310 3312
CONECT 3312 3311
CONECT 3313 3314 3315 3316
CONECT 3314 3313
CONECT 3315 3313
CONECT 3316 3313 3317
CONECT 3317 3316 3318
CONECT 3318 3317 3319
CONECT 3319 3318 3320
CONECT 3320 3319 3321
CONECT 3321 3320 3322
CONECT 3322 3321 3323
CONECT 3323 3322 3324
CONECT 3324 3323 3325
CONECT 3325 3324 3326
CONECT 3326 3325 3327
CONECT 3327 3326 3328
CONECT 3328 3327
CONECT 3329 3330 3331 3332
CONECT 3330 3329
CONECT 3331 3329
CONECT 3332 3329 3333
CONECT 3333 3332 3334
CONECT 3334 3333 3335
CONECT 3335 3334 3336
CONECT 3336 3335 3337
CONECT 3337 3336 3338
CONECT 3338 3337 3339
CONECT 3339 3338 3340
CONECT 3340 3339 3341
CONECT 3341 3340 3342
CONECT 3342 3341 3343
CONECT 3343 3342
CONECT 3344 3345 3346 3347
CONECT 3345 3344
CONECT 3346 3344
CONECT 3347 3344 3348
CONECT 3348 3347 3349
CONECT 3349 3348 3350
CONECT 3350 3349 3351
CONECT 3351 3350 3352
CONECT 3352 3351 3353
CONECT 3353 3352 3354
CONECT 3354 3353 3355
CONECT 3355 3354 3356
CONECT 3356 3355 3357
CONECT 3357 3356 3358
CONECT 3358 3357
CONECT 3359 3360 3361 3362
CONECT 3360 3359
CONECT 3361 3359
CONECT 3362 3359 3363
CONECT 3363 3362 3364
CONECT 3364 3363 3365
CONECT 3365 3364 3366
CONECT 3366 3365 3367
CONECT 3367 3366 3368
CONECT 3368 3367 3369
CONECT 3369 3368 3370
CONECT 3370 3369 3371
CONECT 3371 3370 3372
CONECT 3372 3371
CONECT 3373 3374 3375 3376
CONECT 3374 3373
CONECT 3375 3373
CONECT 3376 3373 3377
CONECT 3377 3376 3378
CONECT 3378 3377 3379
CONECT 3379 3378 3380
CONECT 3380 3379 3381
CONECT 3381 3380
CONECT 3382 3383 3384 3385
CONECT 3383 3382
CONECT 3384 3382
CONECT 3385 3382 3386
CONECT 3386 3385 3387
CONECT 3387 3386 3388
CONECT 3388 3387 3389
CONECT 3389 3388 3390
CONECT 3390 3389 3391
CONECT 3391 3390 3392
CONECT 3392 3391
CONECT 3393 3394 3395 3396
CONECT 3394 3393
CONECT 3395 3393
CONECT 3396 3393 3397
CONECT 3397 3396 3398
CONECT 3398 3397 3399
CONECT 3399 3398 3400
CONECT 3400 3399 3401
CONECT 3401 3400 3402
CONECT 3402 3401 3403
CONECT 3403 3402
CONECT 3404 3405 3406 3407
CONECT 3405 3404
CONECT 3406 3404
CONECT 3407 3404 3408
CONECT 3408 3407 3409
CONECT 3409 3408 3410
CONECT 3410 3409 3411
CONECT 3411 3410 3412
CONECT 3412 3411 3413
CONECT 3413 3412 3414
CONECT 3414 3413 3415
CONECT 3415 3414 3416
CONECT 3416 3415 3417
CONECT 3417 3416 3418
CONECT 3418 3417
CONECT 3419 3420 3421 3422
CONECT 3420 3419
CONECT 3421 3419
CONECT 3422 3419 3423
CONECT 3423 3422 3424
CONECT 3424 3423 3425
CONECT 3425 3424 3426
CONECT 3426 3425 3427
CONECT 3427 3426 3428
CONECT 3428 3427 3429
CONECT 3429 3428 3430
CONECT 3430 3429 3431
CONECT 3431 3430 3432
CONECT 3432 3431
CONECT 3433 3434 3435 3436
CONECT 3434 3433
CONECT 3435 3433
CONECT 3436 3433 3437
CONECT 3437 3436 3438
CONECT 3438 3437 3439
CONECT 3439 3438 3440
CONECT 3440 3439 3441
CONECT 3441 3440 3442
CONECT 3442 3441 3443
CONECT 3443 3442 3444
CONECT 3444 3443 3445
CONECT 3445 3444 3446
CONECT 3446 3445 3447
CONECT 3447 3446 3448
CONECT 3448 3447 3449
CONECT 3449 3448 3450
CONECT 3450 3449 3451
CONECT 3451 3450 3452
CONECT 3452 3451
CONECT 3453 3454 3455 3456
CONECT 3454 3453
CONECT 3455 3453
CONECT 3456 3453 3457
CONECT 3457 3456 3458
CONECT 3458 3457 3459
CONECT 3459 3458 3460
CONECT 3460 3459 3461
CONECT 3461 3460 3462
CONECT 3462 3461 3463
CONECT 3463 3462 3464
CONECT 3464 3463 3465
CONECT 3465 3464 3466
CONECT 3466 3465
CONECT 3467 3468 3469 3470
CONECT 3468 3467
CONECT 3469 3467
CONECT 3470 3467 3471
CONECT 3471 3470 3472
CONECT 3472 3471 3473
CONECT 3473 3472 3474
CONECT 3474 3473 3475
CONECT 3475 3474 3476
CONECT 3476 3475 3477
CONECT 3477 3476 3478
CONECT 3478 3477
CONECT 3479 3482
CONECT 3480 3481 3483
CONECT 3481 3480 3484
CONECT 3482 3479 3486
CONECT 3483 3480 3487
CONECT 3484 3481 3488
CONECT 3485 3499 3501
CONECT 3486 3482 3489
CONECT 3487 3483 3490
CONECT 3488 3484 3491
CONECT 3489 3486 3492
CONECT 3490 3487 3492
CONECT 3491 3488 3493
CONECT 3492 3489 3490
CONECT 3493 3491 3494
CONECT 3494 3493 3495
CONECT 3495 3494 3496
CONECT 3496 3495 3498
CONECT 3497 3499 3503
CONECT 3498 3496 3500 3503
CONECT 3499 3485 3497 3502
CONECT 3500 3498
CONECT 3501 3485
CONECT 3502 3499
CONECT 3503 3497 3498
CONECT 3504 3505 3506
CONECT 3505 3504 3507
CONECT 3506 3504 3509
CONECT 3507 3505 3510
CONECT 3508 3518 3520
CONECT 3509 3506
CONECT 3510 3507 3511
CONECT 3511 3510 3512
CONECT 3512 3511 3513
CONECT 3513 3512 3514
CONECT 3514 3513 3515
CONECT 3515 3514 3517
CONECT 3516 3518 3522
CONECT 3517 3515 3519 3522
CONECT 3518 3508 3516 3521
CONECT 3519 3517
CONECT 3520 3508
CONECT 3521 3518
CONECT 3522 3516 3517
CONECT 3523 3524 3525
CONECT 3524 3523 3526
CONECT 3525 3523 3528
CONECT 3526 3524 3529
CONECT 3527 3539 3541
CONECT 3528 3525 3530
CONECT 3529 3526 3531
CONECT 3530 3528 3532
CONECT 3531 3529 3533
CONECT 3532 3530
CONECT 3533 3531 3534
CONECT 3534 3533 3535
CONECT 3535 3534 3536
CONECT 3536 3535 3538
CONECT 3537 3539 3543
CONECT 3538 3536 3540 3543
CONECT 3539 3527 3537 3542
CONECT 3540 3538
CONECT 3541 3527
CONECT 3542 3539
CONECT 3543 3537 3538
CONECT 3544 3545 3546
CONECT 3545 3544 3547
CONECT 3546 3544 3549
CONECT 3547 3545 3550
CONECT 3548 3558 3560
CONECT 3549 3546
CONECT 3550 3547 3551
CONECT 3551 3550 3552
CONECT 3552 3551 3553
CONECT 3553 3552 3554
CONECT 3554 3553 3555
CONECT 3555 3554 3557
CONECT 3556 3558 3562
CONECT 3557 3555 3559 3562
CONECT 3558 3548 3556 3561
CONECT 3559 3557
CONECT 3560 3548
CONECT 3561 3558
CONECT 3562 3556 3557
CONECT 3563 3564 3565
CONECT 3564 3563
CONECT 3565 3563 3566
CONECT 3566 3565 3567
CONECT 3567 3566 3568
CONECT 3568 3567 3569
CONECT 3569 3568
CONECT 3570 3571 3572
CONECT 3571 3570
CONECT 3572 3570 3573
CONECT 3573 3572 3574
CONECT 3574 3573 3575
CONECT 3575 3574 3576
CONECT 3576 3575
MASTER 391 0 35 20 2 0 0 6 3776 1 578 35
END