HEADER MEMBRANE PROTEIN 07-OCT-21 7PX4
TITLE CRYSTAL STRUCTURE OF THE ADENOSINE A2A RECEPTOR (A2A-PSB1-BRIL) IN
TITLE 2 COMPLEX WITH PRELADENANT CONJUGATE PSB-2113
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 7PX4 1 JRNL
REVDAT 2 06-APR-22 7PX4 1 JRNL
REVDAT 1 02-MAR-22 7PX4 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. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 24291
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.450
REMARK 3 FREE R VALUE TEST SET COUNT : 1082
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 42.8800 - 4.5000 1.00 3069 143 0.1854 0.2454
REMARK 3 2 4.4900 - 3.5700 1.00 2942 137 0.1577 0.2028
REMARK 3 3 3.5700 - 3.1200 1.00 2917 136 0.1875 0.2057
REMARK 3 4 3.1200 - 2.8300 1.00 2884 135 0.1993 0.2412
REMARK 3 5 2.8300 - 2.6300 1.00 2865 134 0.2193 0.2804
REMARK 3 6 2.6300 - 2.4700 1.00 2875 134 0.2305 0.2786
REMARK 3 7 2.4700 - 2.3500 1.00 2858 134 0.2653 0.2496
REMARK 3 8 2.3500 - 2.2500 0.97 2799 129 0.2933 0.3727
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) : 0.313
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.369
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.97
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 : 0.003 3628
REMARK 3 ANGLE : 0.501 4805
REMARK 3 CHIRALITY : 0.036 526
REMARK 3 PLANARITY : 0.003 558
REMARK 3 DIHEDRAL : 13.536 1421
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): 13.6447 -3.8890 20.7360
REMARK 3 T TENSOR
REMARK 3 T11: 0.2239 T22: 0.2656
REMARK 3 T33: 0.2074 T12: -0.0090
REMARK 3 T13: 0.0116 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.9784 L22: 1.1281
REMARK 3 L33: 1.1923 L12: -0.1229
REMARK 3 L13: 0.2265 L23: 0.1273
REMARK 3 S TENSOR
REMARK 3 S11: -0.0344 S12: -0.0448 S13: 0.0166
REMARK 3 S21: -0.0335 S22: 0.0268 S23: 0.0405
REMARK 3 S31: -0.0271 S32: -0.0533 S33: -0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1101 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7033 -48.2695 20.6066
REMARK 3 T TENSOR
REMARK 3 T11: 0.6299 T22: 0.5110
REMARK 3 T33: 0.8853 T12: 0.0673
REMARK 3 T13: -0.0219 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.0489 L22: 1.4271
REMARK 3 L33: 0.1287 L12: -0.5334
REMARK 3 L13: -0.0273 L23: -0.1420
REMARK 3 S TENSOR
REMARK 3 S11: -0.0149 S12: -0.1624 S13: -0.3727
REMARK 3 S21: -0.2470 S22: 0.1014 S23: -0.2319
REMARK 3 S31: 0.2846 S32: 0.1392 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 305 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7201 -13.2077 11.2548
REMARK 3 T TENSOR
REMARK 3 T11: 0.2608 T22: 0.3002
REMARK 3 T33: 0.2275 T12: 0.0162
REMARK 3 T13: 0.0272 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.0416 L22: 1.1884
REMARK 3 L33: 1.4213 L12: -0.1309
REMARK 3 L13: 0.2876 L23: -0.0809
REMARK 3 S TENSOR
REMARK 3 S11: -0.0097 S12: 0.1070 S13: -0.2092
REMARK 3 S21: -0.1533 S22: 0.0462 S23: -0.0092
REMARK 3 S31: 0.2499 S32: 0.0212 S33: 0.0021
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 7PX4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1292118450.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-SEP-20
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 : 24297
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 45.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
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 : 7.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.34500
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: 4EIY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74
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 69.74150
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 69.74150
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 19.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.13100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.13100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.74150
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.80000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.13100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.74150
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.80000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.13100
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 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 470 ARG A 304 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 67.70 -102.38
REMARK 500 LEU A 58 -51.15 -121.74
REMARK 500 CYS A 166 88.38 -68.97
REMARK 500 TYR A1101 -62.15 -137.18
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 8E2 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 2424
REMARK 610 OLA A 2425
REMARK 610 OLA A 2426
REMARK 610 OLA A 2427
REMARK 610 OLA A 2428
REMARK 610 OLA A 2429
REMARK 610 OLA A 2430
REMARK 610 OLC A 2432
REMARK 610 OLC A 2433
DBREF 7PX4 A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 7PX4 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 7PX4 A 219 316 UNP P29274 AA2AR_HUMAN 219 316
SEQADV 7PX4 MET A -24 UNP P29274 INITIATING METHIONINE
SEQADV 7PX4 LYS A -23 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 THR A -22 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ILE A -21 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ILE A -20 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ALA A -19 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 LEU A -18 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 SER A -17 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 TYR A -16 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ILE A -15 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 PHE A -14 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 CYS A -13 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 LEU A -12 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 VAL A -11 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 PHE A -10 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ALA A -9 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ASP A -8 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 TYR A -7 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 LYS A -6 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ASP A -5 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ASP A -4 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ASP A -3 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ASP A -2 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 GLY A -1 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 LYS A 91 UNP P29274 SER 91 ENGINEERED MUTATION
SEQADV 7PX4 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 7PX4 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 7PX4 LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 7PX4 HIS A 317 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 HIS A 318 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 7PX4 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 8E2 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 19
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 17
HET OLA A2420 14
HET OLA A2421 16
HET OLA A2422 14
HET OLA A2423 20
HET OLA A2424 14
HET OLA A2425 12
HET OLA A2426 14
HET OLA A2427 11
HET OLA A2428 11
HET OLA A2429 16
HET OLA A2430 15
HET OLC A2431 25
HET OLC A2432 21
HET OLC A2433 19
HET PEG A2434 7
HET PEG A2435 7
HETNAM CLR CHOLESTEROL
HETNAM 8E2 PRELADENANT CONJUGATE PSB-2113
HETNAM OLA OLEIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN 8E2 ~{TERT}-BUTYL 2-[2-[2-[2-[2-[2-[4-[4-[2-[7-AZANYL-4-
HETSYN 2 8E2 (FURAN-2-YL)-3,5,6,8,10,11-HEXAZATRICYCLO[7.3.0.0^{2,
HETSYN 3 8E2 6}]DODECA-1(9),2,4,7,11-PENTAEN-10-YL]ETHYL]PIPERAZIN-
HETSYN 4 8E2 1-YL]PHENOXY]ETHANOYLAMINO]ETHOXY]ETHOXY]ETHOXY]ETHOXY
HETSYN 5 8E2 ]ETHANOATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 CLR 3(C27 H46 O)
FORMUL 5 8E2 C38 H52 N10 O9
FORMUL 6 OLA 26(C18 H34 O2)
FORMUL 32 OLC 3(C21 H40 O4)
FORMUL 35 PEG 2(C4 H10 O3)
FORMUL 37 HOH *231(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 THR A 68 1 11
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 VAL A 1084 GLN A 1093 1 10
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 ILE A 292 1 27
HELIX 19 AC1 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 2.04
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.02
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.04
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03
CRYST1 39.600 180.262 139.483 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 0.025253 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005547 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007169 0.00000
ATOM 1 N ASP A -2 17.627 27.481 3.248 1.00 82.26 N
ANISOU 1 N ASP A -2 12727 8310 10217 -749 -401 1636 N
ATOM 2 CA ASP A -2 18.195 27.174 1.939 1.00 74.00 C
ANISOU 2 CA ASP A -2 11732 7332 9051 -841 -317 1761 C
ATOM 3 C ASP A -2 18.473 25.682 1.776 1.00 75.10 C
ANISOU 3 C ASP A -2 11728 7694 9112 -847 -231 1705 C
ATOM 4 O ASP A -2 19.170 25.269 0.849 1.00 75.52 O
ANISOU 4 O ASP A -2 11791 7830 9072 -937 -136 1783 O
ATOM 5 CB ASP A -2 19.476 27.975 1.712 1.00 81.24 C
ANISOU 5 CB ASP A -2 12710 8151 10005 -1025 -239 1852 C
ATOM 6 CG ASP A -2 19.198 29.420 1.352 1.00 92.68 C
ANISOU 6 CG ASP A -2 14349 9377 11487 -1032 -316 1960 C
ATOM 7 OD1 ASP A -2 18.012 29.766 1.162 1.00 96.73 O
ANISOU 7 OD1 ASP A -2 14951 9821 11982 -885 -429 1971 O
ATOM 8 OD2 ASP A -2 20.161 30.210 1.258 1.00 97.73 O
ANISOU 8 OD2 ASP A -2 15049 9908 12175 -1184 -266 2035 O
ATOM 9 N GLY A -1 17.927 24.878 2.685 1.00 67.86 N
ANISOU 9 N GLY A -1 10681 6869 8233 -749 -262 1570 N
ATOM 10 CA GLY A -1 17.986 23.442 2.539 1.00 65.33 C
ANISOU 10 CA GLY A -1 10237 6745 7841 -732 -200 1514 C
ATOM 11 C GLY A -1 16.757 22.885 1.844 1.00 67.09 C
ANISOU 11 C GLY A -1 10488 7035 7970 -599 -267 1521 C
ATOM 12 O GLY A -1 15.696 23.509 1.830 1.00 65.53 O
ANISOU 12 O GLY A -1 10365 6746 7787 -490 -376 1532 O
ATOM 13 N ALA A 0 16.922 21.701 1.257 1.00 49.52 N
ANISOU 13 N ALA A 0 8198 4969 5649 -607 -204 1511 N
ATOM 14 CA ALA A 0 15.819 21.040 0.580 1.00 51.41 C
ANISOU 14 CA ALA A 0 8451 5286 5795 -492 -266 1508 C
ATOM 15 C ALA A 0 14.662 20.815 1.555 1.00 56.62 C
ANISOU 15 C ALA A 0 9032 5951 6531 -358 -362 1398 C
ATOM 16 O ALA A 0 14.882 20.625 2.755 1.00 57.62 O
ANISOU 16 O ALA A 0 9052 6088 6754 -362 -346 1301 O
ATOM 17 CB ALA A 0 16.273 19.707 -0.009 1.00 51.53 C
ANISOU 17 CB ALA A 0 8394 5474 5712 -528 -178 1489 C
ATOM 18 N PRO A 1 13.424 20.854 1.068 1.00 53.29 N
ANISOU 18 N PRO A 1 8658 5524 6066 -239 -464 1412 N
ATOM 19 CA PRO A 1 12.266 20.627 1.944 1.00 43.90 C
ANISOU 19 CA PRO A 1 7383 4350 4948 -109 -550 1309 C
ATOM 20 C PRO A 1 12.390 19.307 2.681 1.00 42.52 C
ANISOU 20 C PRO A 1 7046 4320 4791 -114 -493 1197 C
ATOM 21 O PRO A 1 12.692 18.271 2.070 1.00 42.01 O
ANISOU 21 O PRO A 1 6944 4375 4643 -150 -438 1198 O
ATOM 22 CB PRO A 1 11.084 20.615 0.964 1.00 45.16 C
ANISOU 22 CB PRO A 1 7610 4522 5026 -2 -650 1356 C
ATOM 23 CG PRO A 1 11.547 21.464 -0.177 1.00 46.25 C
ANISOU 23 CG PRO A 1 7916 4571 5086 -60 -647 1497 C
ATOM 24 CD PRO A 1 13.020 21.191 -0.309 1.00 47.08 C
ANISOU 24 CD PRO A 1 8009 4713 5164 -215 -509 1527 C
ATOM 25 N PRO A 2 12.180 19.305 4.001 1.00 41.69 N
ANISOU 25 N PRO A 2 6846 4205 4790 -76 -505 1098 N
ATOM 26 CA PRO A 2 12.399 18.074 4.777 1.00 39.11 C
ANISOU 26 CA PRO A 2 6372 4006 4481 -90 -446 999 C
ATOM 27 C PRO A 2 11.473 16.934 4.396 1.00 36.46 C
ANISOU 27 C PRO A 2 5971 3793 4088 -18 -477 962 C
ATOM 28 O PRO A 2 11.824 15.772 4.632 1.00 37.52 O
ANISOU 28 O PRO A 2 6010 4039 4207 -51 -416 908 O
ATOM 29 CB PRO A 2 12.163 18.524 6.227 1.00 44.71 C
ANISOU 29 CB PRO A 2 7020 4662 5305 -46 -472 912 C
ATOM 30 CG PRO A 2 11.317 19.751 6.113 1.00 45.24 C
ANISOU 30 CG PRO A 2 7184 4599 5406 39 -570 945 C
ATOM 31 CD PRO A 2 11.766 20.432 4.854 1.00 37.11 C
ANISOU 31 CD PRO A 2 6297 3493 4310 -19 -570 1072 C
ATOM 32 N ILE A 3 10.310 17.223 3.805 1.00 35.23 N
ANISOU 32 N ILE A 3 5864 3616 3904 79 -574 989 N
ATOM 33 CA ILE A 3 9.382 16.160 3.441 1.00 38.28 C
ANISOU 33 CA ILE A 3 6184 4117 4244 143 -613 950 C
ATOM 34 C ILE A 3 9.929 15.296 2.312 1.00 35.53 C
ANISOU 34 C ILE A 3 5864 3856 3780 78 -562 992 C
ATOM 35 O ILE A 3 9.522 14.138 2.171 1.00 35.40 O
ANISOU 35 O ILE A 3 5773 3948 3730 96 -563 940 O
ATOM 36 CB ILE A 3 8.010 16.751 3.063 1.00 38.60 C
ANISOU 36 CB ILE A 3 6265 4114 4286 266 -739 969 C
ATOM 37 CG1 ILE A 3 6.939 15.659 3.025 1.00 39.43 C
ANISOU 37 CG1 ILE A 3 6265 4338 4377 335 -786 903 C
ATOM 38 CG2 ILE A 3 8.082 17.456 1.724 1.00 41.83 C
ANISOU 38 CG2 ILE A 3 6828 4460 4606 259 -780 1085 C
ATOM 39 CD1 ILE A 3 5.589 16.150 2.555 1.00 51.53 C
ANISOU 39 CD1 ILE A 3 7824 5846 5909 456 -914 920 C
ATOM 40 N MET A 4 10.854 15.821 1.506 1.00 32.80 N
ANISOU 40 N MET A 4 5626 3464 3372 -2 -513 1082 N
ATOM 41 CA MET A 4 11.429 15.023 0.428 1.00 37.45 C
ANISOU 41 CA MET A 4 6245 4140 3842 -62 -454 1118 C
ATOM 42 C MET A 4 12.281 13.890 0.985 1.00 34.32 C
ANISOU 42 C MET A 4 5736 3841 3464 -127 -351 1044 C
ATOM 43 O MET A 4 12.053 12.714 0.678 1.00 32.95 O
ANISOU 43 O MET A 4 5508 3772 3239 -113 -343 998 O
ATOM 44 CB MET A 4 12.246 15.914 -0.507 1.00 34.22 C
ANISOU 44 CB MET A 4 5976 3661 3364 -136 -414 1237 C
ATOM 45 CG MET A 4 11.423 16.989 -1.184 1.00 35.60 C
ANISOU 45 CG MET A 4 6282 3737 3508 -68 -520 1322 C
ATOM 46 SD MET A 4 12.387 17.944 -2.364 1.00 40.65 S
ANISOU 46 SD MET A 4 7096 4299 4049 -165 -466 1476 S
ATOM 47 CE MET A 4 12.800 16.675 -3.557 1.00 37.24 C
ANISOU 47 CE MET A 4 6669 4025 3455 -207 -394 1484 C
ATOM 48 N GLY A 5 13.274 14.227 1.812 1.00 34.93 N
ANISOU 48 N GLY A 5 5777 3882 3615 -198 -278 1032 N
ATOM 49 CA GLY A 5 14.053 13.195 2.471 1.00 32.88 C
ANISOU 49 CA GLY A 5 5402 3708 3383 -247 -193 958 C
ATOM 50 C GLY A 5 13.232 12.373 3.443 1.00 33.57 C
ANISOU 50 C GLY A 5 5375 3849 3532 -177 -233 858 C
ATOM 51 O GLY A 5 13.510 11.189 3.653 1.00 31.50 O
ANISOU 51 O GLY A 5 5030 3678 3260 -192 -186 800 O
ATOM 52 N SER A 6 12.209 12.983 4.045 1.00 32.72 N
ANISOU 52 N SER A 6 5261 3684 3488 -98 -318 837 N
ATOM 53 CA SER A 6 11.329 12.243 4.942 1.00 38.28 C
ANISOU 53 CA SER A 6 5856 4444 4246 -31 -352 748 C
ATOM 54 C SER A 6 10.544 11.179 4.187 1.00 34.31 C
ANISOU 54 C SER A 6 5330 4031 3676 8 -388 731 C
ATOM 55 O SER A 6 10.320 10.078 4.705 1.00 29.41 O
ANISOU 55 O SER A 6 4612 3488 3075 15 -372 662 O
ATOM 56 CB SER A 6 10.382 13.207 5.656 1.00 39.86 C
ANISOU 56 CB SER A 6 6056 4566 4522 52 -432 731 C
ATOM 57 OG SER A 6 9.399 12.509 6.401 1.00 49.76 O
ANISOU 57 OG SER A 6 7205 5883 5819 120 -465 653 O
ATOM 58 N SER A 7 10.121 11.487 2.957 1.00 30.07 N
ANISOU 58 N SER A 7 4886 3481 3057 30 -441 795 N
ATOM 59 CA SER A 7 9.367 10.518 2.168 1.00 29.13 C
ANISOU 59 CA SER A 7 4754 3446 2870 65 -486 776 C
ATOM 60 C SER A 7 10.217 9.303 1.824 1.00 28.44 C
ANISOU 60 C SER A 7 4640 3443 2724 -2 -402 749 C
ATOM 61 O SER A 7 9.726 8.169 1.850 1.00 27.91 O
ANISOU 61 O SER A 7 4504 3450 2650 15 -417 688 O
ATOM 62 CB SER A 7 8.835 11.175 0.895 1.00 33.32 C
ANISOU 62 CB SER A 7 5404 3943 3314 102 -564 854 C
ATOM 63 OG SER A 7 7.963 12.248 1.204 1.00 39.09 O
ANISOU 63 OG SER A 7 6157 4593 4102 179 -653 874 O
ATOM 64 N VAL A 8 11.493 9.520 1.497 1.00 28.89 N
ANISOU 64 N VAL A 8 4746 3489 2743 -80 -312 792 N
ATOM 65 CA VAL A 8 12.393 8.403 1.219 1.00 28.20 C
ANISOU 65 CA VAL A 8 4627 3481 2607 -136 -224 762 C
ATOM 66 C VAL A 8 12.558 7.537 2.461 1.00 27.16 C
ANISOU 66 C VAL A 8 4368 3387 2564 -140 -189 676 C
ATOM 67 O VAL A 8 12.474 6.305 2.397 1.00 27.70 O
ANISOU 67 O VAL A 8 4386 3527 2613 -137 -176 620 O
ATOM 68 CB VAL A 8 13.750 8.918 0.708 1.00 36.04 C
ANISOU 68 CB VAL A 8 5684 4456 3554 -218 -129 826 C
ATOM 69 CG1 VAL A 8 14.761 7.777 0.630 1.00 28.31 C
ANISOU 69 CG1 VAL A 8 4650 3561 2546 -268 -30 782 C
ATOM 70 CG2 VAL A 8 13.588 9.585 -0.646 1.00 30.13 C
ANISOU 70 CG2 VAL A 8 5070 3684 2694 -217 -157 917 C
ATOM 71 N TYR A 9 12.790 8.171 3.612 1.00 29.38 N
ANISOU 71 N TYR A 9 4606 3617 2941 -147 -176 663 N
ATOM 72 CA TYR A 9 13.006 7.421 4.846 1.00 27.71 C
ANISOU 72 CA TYR A 9 4284 3440 2806 -151 -142 589 C
ATOM 73 C TYR A 9 11.758 6.641 5.241 1.00 25.18 C
ANISOU 73 C TYR A 9 3896 3159 2511 -88 -206 532 C
ATOM 74 O TYR A 9 11.835 5.456 5.584 1.00 24.48 O
ANISOU 74 O TYR A 9 3739 3130 2431 -96 -179 478 O
ATOM 75 CB TYR A 9 13.432 8.373 5.965 1.00 27.13 C
ANISOU 75 CB TYR A 9 4189 3300 2820 -166 -128 587 C
ATOM 76 CG TYR A 9 13.433 7.747 7.341 1.00 30.65 C
ANISOU 76 CG TYR A 9 4529 3775 3340 -154 -112 513 C
ATOM 77 CD1 TYR A 9 14.351 6.761 7.677 1.00 32.19 C
ANISOU 77 CD1 TYR A 9 4664 4028 3538 -197 -42 478 C
ATOM 78 CD2 TYR A 9 12.519 8.149 8.307 1.00 30.40 C
ANISOU 78 CD2 TYR A 9 4460 3717 3375 -96 -165 479 C
ATOM 79 CE1 TYR A 9 14.353 6.187 8.934 1.00 30.15 C
ANISOU 79 CE1 TYR A 9 4320 3796 3341 -185 -32 418 C
ATOM 80 CE2 TYR A 9 12.515 7.582 9.565 1.00 27.00 C
ANISOU 80 CE2 TYR A 9 3941 3318 3001 -87 -145 417 C
ATOM 81 CZ TYR A 9 13.433 6.603 9.874 1.00 26.76 C
ANISOU 81 CZ TYR A 9 3861 3341 2967 -133 -81 390 C
ATOM 82 OH TYR A 9 13.427 6.039 11.129 1.00 45.17 O
ANISOU 82 OH TYR A 9 6113 5701 5346 -122 -67 335 O
ATOM 83 N ILE A 10 10.593 7.289 5.183 1.00 25.94 N
ANISOU 83 N ILE A 10 4009 3222 2624 -25 -292 544 N
ATOM 84 CA ILE A 10 9.351 6.631 5.578 1.00 28.92 C
ANISOU 84 CA ILE A 10 4312 3642 3036 31 -352 491 C
ATOM 85 C ILE A 10 9.025 5.479 4.634 1.00 29.25 C
ANISOU 85 C ILE A 10 4354 3750 3008 26 -371 475 C
ATOM 86 O ILE A 10 8.577 4.411 5.068 1.00 30.64 O
ANISOU 86 O ILE A 10 4452 3977 3212 29 -374 419 O
ATOM 87 CB ILE A 10 8.207 7.660 5.645 1.00 29.71 C
ANISOU 87 CB ILE A 10 4426 3694 3170 107 -441 508 C
ATOM 88 CG1 ILE A 10 8.435 8.625 6.809 1.00 31.40 C
ANISOU 88 CG1 ILE A 10 4623 3844 3464 119 -423 499 C
ATOM 89 CG2 ILE A 10 6.858 6.971 5.786 1.00 26.90 C
ANISOU 89 CG2 ILE A 10 3990 3393 2839 162 -507 461 C
ATOM 90 CD1 ILE A 10 7.392 9.708 6.910 1.00 41.34 C
ANISOU 90 CD1 ILE A 10 5901 5046 4761 202 -506 511 C
ATOM 91 N THR A 11 9.253 5.669 3.332 1.00 25.97 N
ANISOU 91 N THR A 11 4034 3333 2499 14 -383 524 N
ATOM 92 CA THR A 11 8.976 4.604 2.373 1.00 26.18 C
ANISOU 92 CA THR A 11 4076 3422 2450 10 -405 502 C
ATOM 93 C THR A 11 9.891 3.405 2.597 1.00 25.48 C
ANISOU 93 C THR A 11 3946 3380 2356 -41 -320 455 C
ATOM 94 O THR A 11 9.444 2.254 2.531 1.00 25.24 O
ANISOU 94 O THR A 11 3873 3396 2323 -38 -340 401 O
ATOM 95 CB THR A 11 9.117 5.135 0.945 1.00 27.26 C
ANISOU 95 CB THR A 11 4336 3549 2473 10 -430 567 C
ATOM 96 OG1 THR A 11 8.263 6.272 0.772 1.00 30.19 O
ANISOU 96 OG1 THR A 11 4749 3868 2854 66 -517 614 O
ATOM 97 CG2 THR A 11 8.730 4.070 -0.066 1.00 27.62 C
ANISOU 97 CG2 THR A 11 4403 3659 2432 14 -467 536 C
ATOM 98 N VAL A 12 11.173 3.653 2.876 1.00 25.24 N
ANISOU 98 N VAL A 12 3926 3335 2330 -88 -228 473 N
ATOM 99 CA VAL A 12 12.107 2.557 3.119 1.00 24.67 C
ANISOU 99 CA VAL A 12 3811 3305 2258 -127 -148 429 C
ATOM 100 C VAL A 12 11.745 1.819 4.403 1.00 25.38 C
ANISOU 100 C VAL A 12 3797 3407 2441 -116 -151 369 C
ATOM 101 O VAL A 12 11.803 0.585 4.460 1.00 28.41 O
ANISOU 101 O VAL A 12 4142 3828 2823 -123 -136 320 O
ATOM 102 CB VAL A 12 13.553 3.086 3.152 1.00 29.27 C
ANISOU 102 CB VAL A 12 4416 3873 2832 -179 -54 464 C
ATOM 103 CG1 VAL A 12 14.509 2.013 3.660 1.00 24.59 C
ANISOU 103 CG1 VAL A 12 3757 3321 2263 -207 23 412 C
ATOM 104 CG2 VAL A 12 13.975 3.555 1.767 1.00 27.08 C
ANISOU 104 CG2 VAL A 12 4243 3600 2445 -199 -34 523 C
ATOM 105 N GLU A 13 11.354 2.557 5.447 1.00 27.80 N
ANISOU 105 N GLU A 13 4060 3678 2826 -96 -171 372 N
ATOM 106 CA GLU A 13 10.977 1.921 6.706 1.00 25.13 C
ANISOU 106 CA GLU A 13 3627 3354 2566 -85 -169 322 C
ATOM 107 C GLU A 13 9.756 1.027 6.535 1.00 24.62 C
ANISOU 107 C GLU A 13 3525 3325 2506 -60 -231 286 C
ATOM 108 O GLU A 13 9.690 -0.065 7.112 1.00 24.40 O
ANISOU 108 O GLU A 13 3437 3324 2510 -72 -214 244 O
ATOM 109 CB GLU A 13 10.710 2.983 7.775 1.00 26.73 C
ANISOU 109 CB GLU A 13 3802 3516 2839 -62 -181 330 C
ATOM 110 CG GLU A 13 11.958 3.684 8.296 1.00 30.19 C
ANISOU 110 CG GLU A 13 4254 3920 3298 -97 -119 348 C
ATOM 111 CD GLU A 13 12.760 2.828 9.263 1.00 37.57 C
ANISOU 111 CD GLU A 13 5122 4884 4268 -125 -60 308 C
ATOM 112 OE1 GLU A 13 12.379 1.662 9.496 1.00 42.24 O
ANISOU 112 OE1 GLU A 13 5667 5516 4866 -118 -62 271 O
ATOM 113 OE2 GLU A 13 13.773 3.321 9.801 1.00 50.54 O
ANISOU 113 OE2 GLU A 13 6762 6507 5936 -154 -15 314 O
ATOM 114 N LEU A 14 8.775 1.473 5.746 1.00 23.41 N
ANISOU 114 N LEU A 14 3404 3167 2322 -26 -309 305 N
ATOM 115 CA LEU A 14 7.592 0.652 5.514 1.00 27.44 C
ANISOU 115 CA LEU A 14 3871 3714 2840 -7 -376 270 C
ATOM 116 C LEU A 14 7.935 -0.598 4.713 1.00 26.23 C
ANISOU 116 C LEU A 14 3745 3594 2629 -40 -365 240 C
ATOM 117 O LEU A 14 7.358 -1.667 4.945 1.00 25.66 O
ANISOU 117 O LEU A 14 3618 3547 2587 -50 -386 194 O
ATOM 118 CB LEU A 14 6.512 1.473 4.810 1.00 30.78 C
ANISOU 118 CB LEU A 14 4323 4128 3243 42 -471 296 C
ATOM 119 CG LEU A 14 5.916 2.609 5.646 1.00 37.43 C
ANISOU 119 CG LEU A 14 5129 4938 4155 91 -497 312 C
ATOM 120 CD1 LEU A 14 4.802 3.317 4.890 1.00 41.34 C
ANISOU 120 CD1 LEU A 14 5648 5427 4632 150 -600 335 C
ATOM 121 CD2 LEU A 14 5.414 2.084 6.984 1.00 33.05 C
ANISOU 121 CD2 LEU A 14 4460 4408 3688 94 -476 265 C
ATOM 122 N ALA A 15 8.872 -0.487 3.769 1.00 23.99 N
ANISOU 122 N ALA A 15 3545 3308 2262 -59 -328 263 N
ATOM 123 CA ALA A 15 9.309 -1.665 3.025 1.00 24.14 C
ANISOU 123 CA ALA A 15 3594 3357 2220 -83 -308 226 C
ATOM 124 C ALA A 15 9.981 -2.676 3.946 1.00 27.05 C
ANISOU 124 C ALA A 15 3902 3731 2646 -110 -240 183 C
ATOM 125 O ALA A 15 9.787 -3.889 3.798 1.00 25.65 O
ANISOU 125 O ALA A 15 3709 3568 2466 -120 -251 134 O
ATOM 126 CB ALA A 15 10.255 -1.253 1.897 1.00 24.72 C
ANISOU 126 CB ALA A 15 3767 3436 2191 -95 -266 261 C
ATOM 127 N ILE A 16 10.768 -2.194 4.909 1.00 25.23 N
ANISOU 127 N ILE A 16 3639 3483 2465 -119 -176 201 N
ATOM 128 CA ILE A 16 11.433 -3.089 5.851 1.00 25.49 C
ANISOU 128 CA ILE A 16 3616 3520 2550 -138 -118 167 C
ATOM 129 C ILE A 16 10.417 -3.734 6.788 1.00 25.38 C
ANISOU 129 C ILE A 16 3526 3506 2609 -132 -157 138 C
ATOM 130 O ILE A 16 10.520 -4.924 7.113 1.00 28.72 O
ANISOU 130 O ILE A 16 3923 3935 3055 -147 -142 101 O
ATOM 131 CB ILE A 16 12.523 -2.325 6.626 1.00 26.11 C
ANISOU 131 CB ILE A 16 3679 3582 2659 -149 -51 193 C
ATOM 132 CG1 ILE A 16 13.627 -1.855 5.678 1.00 23.13 C
ANISOU 132 CG1 ILE A 16 3366 3210 2212 -168 2 221 C
ATOM 133 CG2 ILE A 16 13.112 -3.190 7.731 1.00 21.23 C
ANISOU 133 CG2 ILE A 16 2999 2969 2099 -159 -6 161 C
ATOM 134 CD1 ILE A 16 14.658 -0.975 6.346 1.00 27.40 C
ANISOU 134 CD1 ILE A 16 3890 3733 2788 -190 60 250 C
ATOM 135 N ALA A 17 9.417 -2.966 7.232 1.00 28.70 N
ANISOU 135 N ALA A 17 3913 3922 3069 -110 -205 155 N
ATOM 136 CA ALA A 17 8.411 -3.517 8.135 1.00 24.37 C
ANISOU 136 CA ALA A 17 3285 3384 2589 -108 -233 131 C
ATOM 137 C ALA A 17 7.629 -4.644 7.470 1.00 24.70 C
ANISOU 137 C ALA A 17 3322 3442 2620 -123 -284 96 C
ATOM 138 O ALA A 17 7.351 -5.671 8.100 1.00 28.33 O
ANISOU 138 O ALA A 17 3732 3905 3126 -147 -277 70 O
ATOM 139 CB ALA A 17 7.465 -2.414 8.612 1.00 22.49 C
ANISOU 139 CB ALA A 17 3011 3144 2391 -72 -273 151 C
ATOM 140 N VAL A 18 7.269 -4.473 6.195 1.00 27.80 N
ANISOU 140 N VAL A 18 3770 3843 2950 -114 -341 97 N
ATOM 141 CA VAL A 18 6.532 -5.517 5.484 1.00 28.27 C
ANISOU 141 CA VAL A 18 3830 3916 2994 -130 -401 57 C
ATOM 142 C VAL A 18 7.368 -6.787 5.387 1.00 23.28 C
ANISOU 142 C VAL A 18 3225 3274 2349 -161 -355 19 C
ATOM 143 O VAL A 18 6.888 -7.892 5.672 1.00 28.17 O
ANISOU 143 O VAL A 18 3807 3887 3010 -189 -374 -17 O
ATOM 144 CB VAL A 18 6.098 -5.022 4.092 1.00 24.74 C
ANISOU 144 CB VAL A 18 3452 3482 2468 -109 -474 65 C
ATOM 145 CG1 VAL A 18 5.516 -6.171 3.282 1.00 24.67 C
ANISOU 145 CG1 VAL A 18 3456 3486 2432 -130 -538 13 C
ATOM 146 CG2 VAL A 18 5.087 -3.894 4.220 1.00 24.36 C
ANISOU 146 CG2 VAL A 18 3369 3441 2447 -70 -537 97 C
ATOM 147 N LEU A 19 8.635 -6.649 4.990 1.00 24.64 N
ANISOU 147 N LEU A 19 3459 3440 2464 -157 -292 27 N
ATOM 148 CA LEU A 19 9.494 -7.819 4.841 1.00 23.45 C
ANISOU 148 CA LEU A 19 3333 3279 2297 -173 -247 -13 C
ATOM 149 C LEU A 19 9.790 -8.468 6.188 1.00 29.85 C
ANISOU 149 C LEU A 19 4080 4070 3191 -187 -202 -20 C
ATOM 150 O LEU A 19 9.914 -9.695 6.275 1.00 28.39 O
ANISOU 150 O LEU A 19 3896 3866 3025 -203 -198 -59 O
ATOM 151 CB LEU A 19 10.792 -7.430 4.132 1.00 28.48 C
ANISOU 151 CB LEU A 19 4038 3927 2858 -162 -182 -1 C
ATOM 152 CG LEU A 19 10.643 -6.817 2.736 1.00 28.33 C
ANISOU 152 CG LEU A 19 4100 3929 2737 -149 -216 13 C
ATOM 153 CD1 LEU A 19 11.993 -6.376 2.177 1.00 26.85 C
ANISOU 153 CD1 LEU A 19 3968 3756 2479 -146 -132 34 C
ATOM 154 CD2 LEU A 19 9.958 -7.790 1.785 1.00 29.06 C
ANISOU 154 CD2 LEU A 19 4231 4027 2782 -151 -284 -42 C
ATOM 155 N ALA A 20 9.905 -7.665 7.249 1.00 22.82 N
ANISOU 155 N ALA A 20 3141 3181 2349 -180 -171 17 N
ATOM 156 CA ALA A 20 10.169 -8.231 8.568 1.00 26.38 C
ANISOU 156 CA ALA A 20 3537 3618 2868 -191 -131 16 C
ATOM 157 C ALA A 20 8.973 -9.025 9.075 1.00 28.70 C
ANISOU 157 C ALA A 20 3780 3907 3219 -214 -175 1 C
ATOM 158 O ALA A 20 9.139 -10.098 9.668 1.00 23.37 O
ANISOU 158 O ALA A 20 3090 3210 2580 -234 -156 -14 O
ATOM 159 CB ALA A 20 10.537 -7.123 9.554 1.00 20.92 C
ANISOU 159 CB ALA A 20 2812 2932 2204 -176 -94 53 C
ATOM 160 N ILE A 21 7.761 -8.521 8.847 1.00 27.36 N
ANISOU 160 N ILE A 21 3581 3756 3060 -214 -234 8 N
ATOM 161 CA ILE A 21 6.568 -9.227 9.302 1.00 28.37 C
ANISOU 161 CA ILE A 21 3645 3886 3246 -243 -273 -5 C
ATOM 162 C ILE A 21 6.388 -10.525 8.524 1.00 27.61 C
ANISOU 162 C ILE A 21 3583 3768 3141 -277 -311 -48 C
ATOM 163 O ILE A 21 6.210 -11.598 9.111 1.00 27.03 O
ANISOU 163 O ILE A 21 3484 3668 3116 -313 -303 -60 O
ATOM 164 CB ILE A 21 5.332 -8.319 9.183 1.00 28.18 C
ANISOU 164 CB ILE A 21 3572 3896 3239 -227 -331 8 C
ATOM 165 CG1 ILE A 21 5.458 -7.128 10.133 1.00 22.93 C
ANISOU 165 CG1 ILE A 21 2873 3245 2596 -192 -292 43 C
ATOM 166 CG2 ILE A 21 4.067 -9.103 9.485 1.00 25.32 C
ANISOU 166 CG2 ILE A 21 3136 3547 2940 -265 -373 -8 C
ATOM 167 CD1 ILE A 21 4.447 -6.039 9.873 1.00 22.21 C
ANISOU 167 CD1 ILE A 21 2750 3178 2511 -156 -347 55 C
ATOM 168 N LEU A 22 6.450 -10.449 7.192 1.00 23.21 N
ANISOU 168 N LEU A 22 3089 3215 2516 -266 -354 -72 N
ATOM 169 CA LEU A 22 6.169 -11.616 6.358 1.00 30.67 C
ANISOU 169 CA LEU A 22 4071 4137 3444 -294 -403 -124 C
ATOM 170 C LEU A 22 7.156 -12.747 6.625 1.00 27.04 C
ANISOU 170 C LEU A 22 3648 3632 2992 -305 -350 -149 C
ATOM 171 O LEU A 22 6.758 -13.905 6.802 1.00 28.16 O
ANISOU 171 O LEU A 22 3783 3738 3180 -344 -374 -179 O
ATOM 172 CB LEU A 22 6.198 -11.223 4.879 1.00 24.70 C
ANISOU 172 CB LEU A 22 3390 3400 2595 -271 -452 -144 C
ATOM 173 CG LEU A 22 5.070 -10.330 4.362 1.00 26.87 C
ANISOU 173 CG LEU A 22 3640 3712 2856 -258 -532 -128 C
ATOM 174 CD1 LEU A 22 5.307 -9.946 2.906 1.00 25.27 C
ANISOU 174 CD1 LEU A 22 3532 3527 2543 -230 -572 -140 C
ATOM 175 CD2 LEU A 22 3.729 -11.024 4.522 1.00 31.96 C
ANISOU 175 CD2 LEU A 22 4214 4360 3570 -299 -608 -156 C
ATOM 176 N GLY A 23 8.451 -12.431 6.654 1.00 26.76 N
ANISOU 176 N GLY A 23 3652 3597 2918 -271 -281 -138 N
ATOM 177 CA GLY A 23 9.450 -13.478 6.790 1.00 24.78 C
ANISOU 177 CA GLY A 23 3438 3307 2671 -267 -236 -168 C
ATOM 178 C GLY A 23 9.417 -14.159 8.145 1.00 26.93 C
ANISOU 178 C GLY A 23 3660 3546 3027 -289 -210 -149 C
ATOM 179 O GLY A 23 9.555 -15.383 8.238 1.00 28.83 O
ANISOU 179 O GLY A 23 3925 3736 3295 -305 -215 -179 O
ATOM 180 N ASN A 24 9.239 -13.382 9.212 1.00 25.63 N
ANISOU 180 N ASN A 24 3433 3405 2899 -288 -183 -99 N
ATOM 181 CA ASN A 24 9.241 -13.950 10.551 1.00 25.82 C
ANISOU 181 CA ASN A 24 3416 3406 2989 -306 -153 -74 C
ATOM 182 C ASN A 24 7.913 -14.593 10.918 1.00 29.76 C
ANISOU 182 C ASN A 24 3871 3891 3546 -360 -197 -71 C
ATOM 183 O ASN A 24 7.890 -15.478 11.780 1.00 26.91 O
ANISOU 183 O ASN A 24 3498 3493 3234 -387 -179 -57 O
ATOM 184 CB ASN A 24 9.616 -12.878 11.570 1.00 21.13 C
ANISOU 184 CB ASN A 24 2779 2846 2403 -282 -106 -28 C
ATOM 185 CG ASN A 24 11.078 -12.493 11.484 1.00 23.86 C
ANISOU 185 CG ASN A 24 3158 3196 2711 -241 -56 -28 C
ATOM 186 OD1 ASN A 24 11.947 -13.212 11.979 1.00 26.23 O
ANISOU 186 OD1 ASN A 24 3469 3470 3026 -229 -23 -33 O
ATOM 187 ND2 ASN A 24 11.361 -11.365 10.841 1.00 27.68 N
ANISOU 187 ND2 ASN A 24 3655 3713 3150 -220 -50 -22 N
ATOM 188 N VAL A 25 6.808 -14.174 10.294 1.00 27.68 N
ANISOU 188 N VAL A 25 3580 3657 3281 -378 -254 -80 N
ATOM 189 CA VAL A 25 5.566 -14.930 10.432 1.00 30.38 C
ANISOU 189 CA VAL A 25 3876 3986 3681 -438 -302 -88 C
ATOM 190 C VAL A 25 5.721 -16.303 9.794 1.00 28.39 C
ANISOU 190 C VAL A 25 3686 3668 3433 -470 -334 -136 C
ATOM 191 O VAL A 25 5.211 -17.308 10.307 1.00 28.70 O
ANISOU 191 O VAL A 25 3706 3664 3535 -526 -344 -134 O
ATOM 192 CB VAL A 25 4.383 -14.149 9.828 1.00 31.51 C
ANISOU 192 CB VAL A 25 3969 4180 3821 -443 -365 -94 C
ATOM 193 CG1 VAL A 25 3.221 -15.077 9.513 1.00 29.54 C
ANISOU 193 CG1 VAL A 25 3686 3915 3622 -509 -433 -122 C
ATOM 194 CG2 VAL A 25 3.930 -13.048 10.779 1.00 24.98 C
ANISOU 194 CG2 VAL A 25 3064 3406 3020 -422 -334 -48 C
ATOM 195 N LEU A 26 6.458 -16.370 8.682 1.00 31.71 N
ANISOU 195 N LEU A 26 4185 4077 3787 -435 -347 -180 N
ATOM 196 CA LEU A 26 6.713 -17.649 8.028 1.00 32.32 C
ANISOU 196 CA LEU A 26 4331 4088 3860 -452 -376 -237 C
ATOM 197 C LEU A 26 7.537 -18.569 8.918 1.00 27.08 C
ANISOU 197 C LEU A 26 3691 3362 3238 -450 -323 -225 C
ATOM 198 O LEU A 26 7.342 -19.789 8.913 1.00 28.51 O
ANISOU 198 O LEU A 26 3903 3471 3460 -488 -350 -253 O
ATOM 199 CB LEU A 26 7.424 -17.420 6.694 1.00 32.51 C
ANISOU 199 CB LEU A 26 4436 4126 3792 -404 -386 -286 C
ATOM 200 CG LEU A 26 7.728 -18.654 5.841 1.00 34.55 C
ANISOU 200 CG LEU A 26 4778 4321 4029 -407 -418 -361 C
ATOM 201 CD1 LEU A 26 6.439 -19.343 5.425 1.00 40.32 C
ANISOU 201 CD1 LEU A 26 5499 5024 4798 -474 -511 -398 C
ATOM 202 CD2 LEU A 26 8.555 -18.273 4.622 1.00 41.72 C
ANISOU 202 CD2 LEU A 26 5762 5261 4830 -349 -406 -402 C
ATOM 203 N VAL A 27 8.470 -18.003 9.683 1.00 23.75 N
ANISOU 203 N VAL A 27 3257 2962 2806 -405 -253 -184 N
ATOM 204 CA VAL A 27 9.253 -18.809 10.613 1.00 28.96 C
ANISOU 204 CA VAL A 27 3933 3567 3502 -395 -210 -166 C
ATOM 205 C VAL A 27 8.351 -19.390 11.696 1.00 27.99 C
ANISOU 205 C VAL A 27 3765 3415 3455 -458 -216 -122 C
ATOM 206 O VAL A 27 8.393 -20.592 11.983 1.00 31.32 O
ANISOU 206 O VAL A 27 4222 3758 3920 -486 -226 -127 O
ATOM 207 CB VAL A 27 10.400 -17.974 11.210 1.00 30.38 C
ANISOU 207 CB VAL A 27 4100 3789 3655 -335 -143 -133 C
ATOM 208 CG1 VAL A 27 11.030 -18.697 12.390 1.00 23.00 C
ANISOU 208 CG1 VAL A 27 3168 2809 2764 -326 -107 -101 C
ATOM 209 CG2 VAL A 27 11.447 -17.686 10.144 1.00 28.57 C
ANISOU 209 CG2 VAL A 27 3921 3577 3358 -280 -125 -177 C
ATOM 210 N CYS A 28 7.506 -18.547 12.300 1.00 25.41 N
ANISOU 210 N CYS A 28 3361 3149 3146 -482 -210 -79 N
ATOM 211 CA CYS A 28 6.602 -19.023 13.345 1.00 32.27 C
ANISOU 211 CA CYS A 28 4176 4004 4081 -546 -204 -33 C
ATOM 212 C CYS A 28 5.627 -20.061 12.803 1.00 30.46 C
ANISOU 212 C CYS A 28 3953 3723 3899 -622 -265 -63 C
ATOM 213 O CYS A 28 5.337 -21.061 13.472 1.00 34.17 O
ANISOU 213 O CYS A 28 4426 4131 4424 -677 -260 -37 O
ATOM 214 CB CYS A 28 5.843 -17.848 13.961 1.00 32.39 C
ANISOU 214 CB CYS A 28 4102 4104 4099 -548 -185 7 C
ATOM 215 SG CYS A 28 6.891 -16.666 14.837 1.00 33.17 S
ANISOU 215 SG CYS A 28 4193 4256 4156 -473 -116 44 S
ATOM 216 N TRP A 29 5.114 -19.839 11.591 1.00 31.02 N
ANISOU 216 N TRP A 29 4027 3812 3946 -628 -327 -116 N
ATOM 217 CA TRP A 29 4.221 -20.810 10.966 1.00 35.54 C
ANISOU 217 CA TRP A 29 4607 4333 4562 -701 -398 -157 C
ATOM 218 C TRP A 29 4.933 -22.137 10.727 1.00 31.95 C
ANISOU 218 C TRP A 29 4250 3770 4119 -706 -408 -194 C
ATOM 219 O TRP A 29 4.333 -23.208 10.873 1.00 31.83 O
ANISOU 219 O TRP A 29 4243 3682 4168 -781 -442 -199 O
ATOM 220 CB TRP A 29 3.679 -20.237 9.654 1.00 33.43 C
ANISOU 220 CB TRP A 29 4336 4113 4251 -692 -470 -212 C
ATOM 221 CG TRP A 29 2.462 -20.931 9.123 1.00 47.27 C
ANISOU 221 CG TRP A 29 6062 5844 6056 -775 -554 -249 C
ATOM 222 CD1 TRP A 29 1.845 -22.025 9.654 1.00 53.75 C
ANISOU 222 CD1 TRP A 29 6863 6599 6960 -864 -567 -239 C
ATOM 223 CD2 TRP A 29 1.706 -20.572 7.957 1.00 59.24 C
ANISOU 223 CD2 TRP A 29 7565 7400 7542 -782 -641 -301 C
ATOM 224 NE1 TRP A 29 0.757 -22.373 8.891 1.00 58.59 N
ANISOU 224 NE1 TRP A 29 7445 7211 7606 -930 -658 -286 N
ATOM 225 CE2 TRP A 29 0.649 -21.497 7.843 1.00 52.80 C
ANISOU 225 CE2 TRP A 29 6715 6545 6802 -878 -708 -326 C
ATOM 226 CE3 TRP A 29 1.821 -19.559 6.999 1.00 58.24 C
ANISOU 226 CE3 TRP A 29 7456 7339 7333 -718 -672 -324 C
ATOM 227 CZ2 TRP A 29 -0.286 -21.440 6.811 1.00 61.02 C
ANISOU 227 CZ2 TRP A 29 7732 7614 7839 -908 -811 -381 C
ATOM 228 CZ3 TRP A 29 0.891 -19.506 5.973 1.00 56.96 C
ANISOU 228 CZ3 TRP A 29 7280 7203 7159 -743 -773 -373 C
ATOM 229 CH2 TRP A 29 -0.148 -20.440 5.888 1.00 56.55 C
ANISOU 229 CH2 TRP A 29 7187 7115 7184 -835 -845 -404 C
ATOM 230 N ALA A 30 6.217 -22.087 10.370 1.00 28.94 N
ANISOU 230 N ALA A 30 3941 3374 3679 -626 -379 -220 N
ATOM 231 CA ALA A 30 6.962 -23.313 10.104 1.00 26.91 C
ANISOU 231 CA ALA A 30 3778 3015 3431 -612 -388 -262 C
ATOM 232 C ALA A 30 7.133 -24.136 11.375 1.00 32.60 C
ANISOU 232 C ALA A 30 4503 3666 4219 -640 -352 -204 C
ATOM 233 O ALA A 30 6.932 -25.356 11.371 1.00 35.88 O
ANISOU 233 O ALA A 30 4969 3977 4685 -686 -386 -221 O
ATOM 234 CB ALA A 30 8.320 -22.977 9.485 1.00 26.47 C
ANISOU 234 CB ALA A 30 3781 2977 3298 -513 -353 -301 C
ATOM 235 N VAL A 31 7.502 -23.481 12.479 1.00 26.25 N
ANISOU 235 N VAL A 31 3653 2911 3411 -612 -288 -133 N
ATOM 236 CA VAL A 31 7.663 -24.188 13.747 1.00 32.55 C
ANISOU 236 CA VAL A 31 4458 3651 4258 -634 -254 -67 C
ATOM 237 C VAL A 31 6.333 -24.765 14.211 1.00 34.19 C
ANISOU 237 C VAL A 31 4625 3829 4538 -746 -276 -30 C
ATOM 238 O VAL A 31 6.288 -25.852 14.802 1.00 35.01 O
ANISOU 238 O VAL A 31 4770 3839 4693 -790 -277 1 O
ATOM 239 CB VAL A 31 8.276 -23.247 14.804 1.00 30.55 C
ANISOU 239 CB VAL A 31 4161 3472 3975 -581 -186 -5 C
ATOM 240 CG1 VAL A 31 8.410 -23.956 16.142 1.00 29.60 C
ANISOU 240 CG1 VAL A 31 4054 3299 3893 -602 -154 68 C
ATOM 241 CG2 VAL A 31 9.625 -22.735 14.332 1.00 24.85 C
ANISOU 241 CG2 VAL A 31 3472 2776 3192 -482 -164 -42 C
ATOM 242 N TRP A 32 5.231 -24.062 13.944 1.00 35.93 N
ANISOU 242 N TRP A 32 4762 4127 4764 -793 -296 -32 N
ATOM 243 CA TRP A 32 3.920 -24.560 14.348 1.00 38.73 C
ANISOU 243 CA TRP A 32 5058 4467 5191 -904 -314 0 C
ATOM 244 C TRP A 32 3.571 -25.860 13.632 1.00 37.87 C
ANISOU 244 C TRP A 32 5011 4244 5134 -972 -384 -50 C
ATOM 245 O TRP A 32 3.010 -26.782 14.238 1.00 34.14 O
ANISOU 245 O TRP A 32 4538 3701 4732 -1061 -385 -9 O
ATOM 246 CB TRP A 32 2.852 -23.499 14.074 1.00 40.69 C
ANISOU 246 CB TRP A 32 5196 4826 5436 -927 -330 -4 C
ATOM 247 CG TRP A 32 1.453 -23.931 14.404 1.00 43.55 C
ANISOU 247 CG TRP A 32 5477 5192 5877 -1042 -349 22 C
ATOM 248 CD1 TRP A 32 0.632 -24.714 13.644 1.00 40.80 C
ANISOU 248 CD1 TRP A 32 5126 4792 5583 -1126 -424 -24 C
ATOM 249 CD2 TRP A 32 0.705 -23.586 15.575 1.00 45.53 C
ANISOU 249 CD2 TRP A 32 5630 5507 6162 -1087 -288 98 C
ATOM 250 NE1 TRP A 32 -0.577 -24.885 14.273 1.00 47.17 N
ANISOU 250 NE1 TRP A 32 5832 5629 6463 -1227 -414 22 N
ATOM 251 CE2 TRP A 32 -0.558 -24.201 15.461 1.00 43.93 C
ANISOU 251 CE2 TRP A 32 5361 5292 6038 -1203 -326 97 C
ATOM 252 CE3 TRP A 32 0.982 -22.820 16.711 1.00 52.83 C
ANISOU 252 CE3 TRP A 32 6517 6502 7055 -1042 -206 161 C
ATOM 253 CZ2 TRP A 32 -1.541 -24.074 16.438 1.00 46.98 C
ANISOU 253 CZ2 TRP A 32 5639 5739 6473 -1273 -274 162 C
ATOM 254 CZ3 TRP A 32 0.004 -22.695 17.679 1.00 60.17 C
ANISOU 254 CZ3 TRP A 32 7349 7489 8024 -1106 -157 222 C
ATOM 255 CH2 TRP A 32 -1.242 -23.318 17.537 1.00 54.09 C
ANISOU 255 CH2 TRP A 32 6508 6710 7333 -1220 -187 224 C
ATOM 256 N LEU A 33 3.901 -25.957 12.343 1.00 35.28 N
ANISOU 256 N LEU A 33 4741 3894 4769 -934 -442 -139 N
ATOM 257 CA LEU A 33 3.436 -27.090 11.549 1.00 38.24 C
ANISOU 257 CA LEU A 33 5171 4168 5189 -1001 -520 -203 C
ATOM 258 C LEU A 33 4.334 -28.310 11.703 1.00 34.59 C
ANISOU 258 C LEU A 33 4827 3568 4748 -980 -518 -215 C
ATOM 259 O LEU A 33 3.838 -29.440 11.772 1.00 41.46 O
ANISOU 259 O LEU A 33 5734 4329 5691 -1065 -559 -219 O
ATOM 260 CB LEU A 33 3.344 -26.691 10.072 1.00 43.74 C
ANISOU 260 CB LEU A 33 5888 4904 5828 -968 -589 -299 C
ATOM 261 CG LEU A 33 2.286 -25.656 9.687 1.00 50.43 C
ANISOU 261 CG LEU A 33 6629 5867 6663 -995 -622 -301 C
ATOM 262 CD1 LEU A 33 2.365 -25.350 8.199 1.00 55.26 C
ANISOU 262 CD1 LEU A 33 7288 6507 7202 -950 -692 -393 C
ATOM 263 CD2 LEU A 33 0.892 -26.137 10.064 1.00 49.01 C
ANISOU 263 CD2 LEU A 33 6365 5676 6580 -1122 -659 -276 C
ATOM 264 N ASN A 34 5.646 -28.108 11.761 1.00 35.71 N
ANISOU 264 N ASN A 34 5026 3710 4832 -869 -474 -222 N
ATOM 265 CA ASN A 34 6.610 -29.200 11.700 1.00 37.25 C
ANISOU 265 CA ASN A 34 5334 3780 5039 -823 -481 -252 C
ATOM 266 C ASN A 34 7.070 -29.549 13.110 1.00 39.06 C
ANISOU 266 C ASN A 34 5572 3967 5303 -816 -423 -155 C
ATOM 267 O ASN A 34 7.694 -28.727 13.790 1.00 36.97 O
ANISOU 267 O ASN A 34 5267 3783 4995 -751 -361 -105 O
ATOM 268 CB ASN A 34 7.794 -28.817 10.815 1.00 33.09 C
ANISOU 268 CB ASN A 34 4860 3285 4429 -700 -470 -326 C
ATOM 269 CG ASN A 34 8.652 -30.005 10.446 1.00 32.64 C
ANISOU 269 CG ASN A 34 4919 3098 4384 -648 -492 -387 C
ATOM 270 OD1 ASN A 34 8.543 -31.076 11.043 1.00 41.03 O
ANISOU 270 OD1 ASN A 34 6032 4040 5519 -690 -508 -358 O
ATOM 271 ND2 ASN A 34 9.518 -29.823 9.455 1.00 35.00 N
ANISOU 271 ND2 ASN A 34 5265 3420 4612 -554 -490 -471 N
ATOM 272 N SER A 35 6.769 -30.777 13.543 1.00 38.77 N
ANISOU 272 N SER A 35 5592 3799 5341 -884 -448 -129 N
ATOM 273 CA SER A 35 7.232 -31.240 14.845 1.00 42.69 C
ANISOU 273 CA SER A 35 6116 4240 5865 -876 -401 -35 C
ATOM 274 C SER A 35 8.743 -31.423 14.885 1.00 42.57 C
ANISOU 274 C SER A 35 6176 4189 5811 -741 -382 -56 C
ATOM 275 O SER A 35 9.329 -31.398 15.973 1.00 39.46 O
ANISOU 275 O SER A 35 5786 3796 5411 -701 -337 22 O
ATOM 276 CB SER A 35 6.540 -32.555 15.216 1.00 43.27 C
ANISOU 276 CB SER A 35 6243 4167 6029 -986 -437 1 C
ATOM 277 OG SER A 35 6.892 -33.588 14.313 1.00 52.67 O
ANISOU 277 OG SER A 35 7543 5223 7247 -968 -503 -88 O
ATOM 278 N ASN A 36 9.385 -31.606 13.728 1.00 40.55 N
ANISOU 278 N ASN A 36 5977 3907 5524 -668 -415 -162 N
ATOM 279 CA ASN A 36 10.840 -31.668 13.686 1.00 39.40 C
ANISOU 279 CA ASN A 36 5881 3749 5339 -532 -390 -191 C
ATOM 280 C ASN A 36 11.479 -30.325 14.017 1.00 37.63 C
ANISOU 280 C ASN A 36 5576 3676 5047 -461 -327 -162 C
ATOM 281 O ASN A 36 12.671 -30.281 14.339 1.00 38.58 O
ANISOU 281 O ASN A 36 5714 3801 5144 -359 -297 -158 O
ATOM 282 CB ASN A 36 11.310 -32.150 12.311 1.00 43.11 C
ANISOU 282 CB ASN A 36 6426 4168 5788 -473 -432 -318 C
ATOM 283 CG ASN A 36 10.749 -33.515 11.947 1.00 47.50 C
ANISOU 283 CG ASN A 36 7074 4560 6414 -539 -503 -361 C
ATOM 284 OD1 ASN A 36 10.427 -34.321 12.822 1.00 46.43 O
ANISOU 284 OD1 ASN A 36 6973 4319 6350 -599 -514 -290 O
ATOM 285 ND2 ASN A 36 10.633 -33.782 10.651 1.00 47.91 N
ANISOU 285 ND2 ASN A 36 7174 4587 6444 -531 -553 -476 N
ATOM 286 N LEU A 37 10.716 -29.235 13.942 1.00 33.96 N
ANISOU 286 N LEU A 37 5021 3330 4552 -511 -311 -143 N
ATOM 287 CA LEU A 37 11.183 -27.914 14.338 1.00 39.40 C
ANISOU 287 CA LEU A 37 5634 4154 5185 -458 -255 -109 C
ATOM 288 C LEU A 37 10.708 -27.523 15.731 1.00 32.00 C
ANISOU 288 C LEU A 37 4636 3258 4265 -505 -217 -2 C
ATOM 289 O LEU A 37 10.926 -26.384 16.153 1.00 32.51 O
ANISOU 289 O LEU A 37 4634 3431 4286 -474 -174 28 O
ATOM 290 CB LEU A 37 10.729 -26.865 13.318 1.00 36.63 C
ANISOU 290 CB LEU A 37 5229 3906 4782 -466 -262 -160 C
ATOM 291 CG LEU A 37 11.341 -26.943 11.918 1.00 37.75 C
ANISOU 291 CG LEU A 37 5424 4044 4876 -404 -283 -263 C
ATOM 292 CD1 LEU A 37 10.656 -25.959 10.982 1.00 33.33 C
ANISOU 292 CD1 LEU A 37 4818 3580 4266 -430 -300 -297 C
ATOM 293 CD2 LEU A 37 12.837 -26.678 11.969 1.00 34.93 C
ANISOU 293 CD2 LEU A 37 5080 3715 4476 -290 -234 -277 C
ATOM 294 N GLN A 38 10.065 -28.440 16.451 1.00 32.16 N
ANISOU 294 N GLN A 38 4683 3191 4344 -581 -229 55 N
ATOM 295 CA GLN A 38 9.519 -28.150 17.776 1.00 37.91 C
ANISOU 295 CA GLN A 38 5359 3961 5083 -634 -188 158 C
ATOM 296 C GLN A 38 10.438 -28.729 18.850 1.00 41.57 C
ANISOU 296 C GLN A 38 5882 4365 5549 -580 -167 222 C
ATOM 297 O GLN A 38 10.107 -29.672 19.571 1.00 47.70 O
ANISOU 297 O GLN A 38 6705 5049 6369 -634 -173 286 O
ATOM 298 CB GLN A 38 8.097 -28.691 17.891 1.00 37.78 C
ANISOU 298 CB GLN A 38 5321 3905 5127 -767 -207 190 C
ATOM 299 CG GLN A 38 7.132 -28.061 16.903 1.00 41.62 C
ANISOU 299 CG GLN A 38 5737 4462 5613 -818 -235 131 C
ATOM 300 CD GLN A 38 5.742 -28.658 16.964 1.00 40.87 C
ANISOU 300 CD GLN A 38 5610 4330 5589 -953 -260 154 C
ATOM 301 OE1 GLN A 38 5.422 -29.429 17.868 1.00 51.32 O
ANISOU 301 OE1 GLN A 38 6955 5585 6960 -1020 -242 229 O
ATOM 302 NE2 GLN A 38 4.906 -28.304 15.995 1.00 35.34 N
ANISOU 302 NE2 GLN A 38 4857 3673 4897 -997 -304 93 N
ATOM 303 N ASN A 39 11.621 -28.137 18.936 1.00 39.54 N
ANISOU 303 N ASN A 39 5620 4162 5242 -471 -146 205 N
ATOM 304 CA ASN A 39 12.595 -28.429 19.975 1.00 39.30 C
ANISOU 304 CA ASN A 39 5626 4105 5201 -402 -131 261 C
ATOM 305 C ASN A 39 12.854 -27.159 20.780 1.00 40.85 C
ANISOU 305 C ASN A 39 5746 4434 5340 -370 -84 302 C
ATOM 306 O ASN A 39 12.339 -26.083 20.467 1.00 35.55 O
ANISOU 306 O ASN A 39 5000 3865 4643 -394 -63 282 O
ATOM 307 CB ASN A 39 13.889 -28.984 19.372 1.00 32.70 C
ANISOU 307 CB ASN A 39 4853 3205 4366 -293 -157 195 C
ATOM 308 CG ASN A 39 14.411 -28.135 18.234 1.00 38.75 C
ANISOU 308 CG ASN A 39 5577 4055 5092 -235 -148 103 C
ATOM 309 OD1 ASN A 39 15.066 -27.118 18.454 1.00 42.04 O
ANISOU 309 OD1 ASN A 39 5935 4574 5463 -180 -115 105 O
ATOM 310 ND2 ASN A 39 14.122 -28.550 17.006 1.00 36.70 N
ANISOU 310 ND2 ASN A 39 5350 3749 4844 -251 -179 23 N
ATOM 311 N VAL A 40 13.661 -27.296 21.834 1.00 39.97 N
ANISOU 311 N VAL A 40 5659 4317 5212 -312 -73 358 N
ATOM 312 CA VAL A 40 13.912 -26.168 22.725 1.00 40.31 C
ANISOU 312 CA VAL A 40 5639 4477 5200 -285 -35 398 C
ATOM 313 C VAL A 40 14.685 -25.071 22.005 1.00 36.18 C
ANISOU 313 C VAL A 40 5061 4045 4642 -216 -26 325 C
ATOM 314 O VAL A 40 14.429 -23.877 22.207 1.00 37.88 O
ANISOU 314 O VAL A 40 5207 4365 4822 -226 3 328 O
ATOM 315 CB VAL A 40 14.650 -26.641 23.990 1.00 39.41 C
ANISOU 315 CB VAL A 40 5572 4331 5070 -235 -38 471 C
ATOM 316 CG1 VAL A 40 15.088 -25.449 24.815 1.00 34.97 C
ANISOU 316 CG1 VAL A 40 4950 3891 4447 -193 -9 492 C
ATOM 317 CG2 VAL A 40 13.758 -27.560 24.807 1.00 45.68 C
ANISOU 317 CG2 VAL A 40 6418 5050 5887 -318 -34 560 C
ATOM 318 N THR A 41 15.643 -25.455 21.156 1.00 30.20 N
ANISOU 318 N THR A 41 4333 3246 3895 -145 -48 258 N
ATOM 319 CA THR A 41 16.436 -24.465 20.435 1.00 34.67 C
ANISOU 319 CA THR A 41 4848 3897 4429 -86 -33 194 C
ATOM 320 C THR A 41 15.550 -23.538 19.612 1.00 35.59 C
ANISOU 320 C THR A 41 4914 4081 4527 -143 -19 160 C
ATOM 321 O THR A 41 15.765 -22.321 19.586 1.00 35.01 O
ANISOU 321 O THR A 41 4781 4103 4417 -128 6 152 O
ATOM 322 CB THR A 41 17.458 -25.163 19.537 1.00 30.44 C
ANISOU 322 CB THR A 41 4354 3303 3908 -8 -52 123 C
ATOM 323 OG1 THR A 41 18.177 -26.140 20.300 1.00 40.82 O
ANISOU 323 OG1 THR A 41 5721 4539 5248 49 -75 157 O
ATOM 324 CG2 THR A 41 18.443 -24.154 18.969 1.00 30.66 C
ANISOU 324 CG2 THR A 41 4324 3425 3901 55 -25 70 C
ATOM 325 N ASN A 42 14.533 -24.091 18.950 1.00 29.53 N
ANISOU 325 N ASN A 42 4170 3262 3787 -211 -40 143 N
ATOM 326 CA ASN A 42 13.648 -23.279 18.127 1.00 31.97 C
ANISOU 326 CA ASN A 42 4433 3634 4080 -261 -39 111 C
ATOM 327 C ASN A 42 12.615 -22.506 18.938 1.00 32.54 C
ANISOU 327 C ASN A 42 4442 3773 4147 -322 -17 169 C
ATOM 328 O ASN A 42 11.964 -21.615 18.383 1.00 31.65 O
ANISOU 328 O ASN A 42 4281 3726 4018 -348 -15 147 O
ATOM 329 CB ASN A 42 12.943 -24.150 17.086 1.00 35.24 C
ANISOU 329 CB ASN A 42 4891 3972 4525 -309 -80 62 C
ATOM 330 CG ASN A 42 13.870 -24.578 15.963 1.00 35.95 C
ANISOU 330 CG ASN A 42 5033 4025 4602 -242 -95 -20 C
ATOM 331 OD1 ASN A 42 14.917 -23.969 15.743 1.00 39.64 O
ANISOU 331 OD1 ASN A 42 5484 4547 5032 -168 -69 -45 O
ATOM 332 ND2 ASN A 42 13.485 -25.624 15.242 1.00 41.64 N
ANISOU 332 ND2 ASN A 42 5816 4654 5353 -269 -137 -65 N
ATOM 333 N TYR A 43 12.444 -22.815 20.225 1.00 31.90 N
ANISOU 333 N TYR A 43 4364 3680 4076 -342 0 242 N
ATOM 334 CA TYR A 43 11.590 -21.971 21.055 1.00 37.35 C
ANISOU 334 CA TYR A 43 4990 4450 4750 -385 32 291 C
ATOM 335 C TYR A 43 12.196 -20.584 21.220 1.00 30.80 C
ANISOU 335 C TYR A 43 4112 3717 3872 -327 56 276 C
ATOM 336 O TYR A 43 11.470 -19.584 21.261 1.00 28.74 O
ANISOU 336 O TYR A 43 3793 3531 3597 -350 72 277 O
ATOM 337 CB TYR A 43 11.350 -22.627 22.415 1.00 39.92 C
ANISOU 337 CB TYR A 43 5338 4745 5082 -414 51 374 C
ATOM 338 CG TYR A 43 10.602 -23.941 22.339 1.00 48.25 C
ANISOU 338 CG TYR A 43 6440 5701 6192 -490 31 401 C
ATOM 339 CD1 TYR A 43 9.833 -24.264 21.227 1.00 54.89 C
ANISOU 339 CD1 TYR A 43 7274 6508 7073 -546 0 351 C
ATOM 340 CD2 TYR A 43 10.666 -24.858 23.378 1.00 51.25 C
ANISOU 340 CD2 TYR A 43 6874 6017 6583 -509 40 476 C
ATOM 341 CE1 TYR A 43 9.151 -25.467 21.154 1.00 53.33 C
ANISOU 341 CE1 TYR A 43 7118 6213 6933 -624 -23 371 C
ATOM 342 CE2 TYR A 43 9.988 -26.061 23.313 1.00 56.21 C
ANISOU 342 CE2 TYR A 43 7548 6542 7266 -587 21 505 C
ATOM 343 CZ TYR A 43 9.233 -26.360 22.201 1.00 53.37 C
ANISOU 343 CZ TYR A 43 7177 6148 6954 -647 -10 450 C
ATOM 344 OH TYR A 43 8.558 -27.559 22.138 1.00 65.97 O
ANISOU 344 OH TYR A 43 8818 7635 8611 -734 -33 475 O
ATOM 345 N PHE A 44 13.526 -20.504 21.302 1.00 31.27 N
ANISOU 345 N PHE A 44 4193 3776 3911 -252 55 260 N
ATOM 346 CA PHE A 44 14.191 -19.205 21.310 1.00 24.75 C
ANISOU 346 CA PHE A 44 3323 3032 3047 -205 72 239 C
ATOM 347 C PHE A 44 14.211 -18.578 19.921 1.00 28.86 C
ANISOU 347 C PHE A 44 3827 3578 3560 -200 66 176 C
ATOM 348 O PHE A 44 14.200 -17.347 19.797 1.00 27.47 O
ANISOU 348 O PHE A 44 3609 3471 3359 -192 80 166 O
ATOM 349 CB PHE A 44 15.614 -19.345 21.850 1.00 29.81 C
ANISOU 349 CB PHE A 44 3981 3668 3676 -132 71 241 C
ATOM 350 CG PHE A 44 15.679 -19.802 23.281 1.00 29.34 C
ANISOU 350 CG PHE A 44 3942 3596 3609 -127 72 307 C
ATOM 351 CD1 PHE A 44 15.410 -18.921 24.315 1.00 23.39 C
ANISOU 351 CD1 PHE A 44 3154 2913 2820 -134 94 342 C
ATOM 352 CD2 PHE A 44 16.017 -21.109 23.591 1.00 26.33 C
ANISOU 352 CD2 PHE A 44 3623 3130 3251 -111 51 334 C
ATOM 353 CE1 PHE A 44 15.470 -19.336 25.634 1.00 30.31 C
ANISOU 353 CE1 PHE A 44 4057 3784 3675 -128 96 404 C
ATOM 354 CE2 PHE A 44 16.080 -21.531 24.907 1.00 30.21 C
ANISOU 354 CE2 PHE A 44 4144 3608 3727 -106 50 403 C
ATOM 355 CZ PHE A 44 15.806 -20.643 25.930 1.00 30.71 C
ANISOU 355 CZ PHE A 44 4171 3751 3744 -115 74 439 C
ATOM 356 N VAL A 45 14.245 -19.403 18.871 1.00 27.97 N
ANISOU 356 N VAL A 45 3756 3407 3466 -203 43 135 N
ATOM 357 CA VAL A 45 14.138 -18.885 17.510 1.00 30.52 C
ANISOU 357 CA VAL A 45 4072 3754 3769 -203 35 78 C
ATOM 358 C VAL A 45 12.775 -18.237 17.295 1.00 27.54 C
ANISOU 358 C VAL A 45 3657 3416 3392 -262 26 87 C
ATOM 359 O VAL A 45 12.659 -17.208 16.616 1.00 26.99 O
ANISOU 359 O VAL A 45 3562 3399 3294 -256 27 65 O
ATOM 360 CB VAL A 45 14.405 -20.011 16.491 1.00 29.75 C
ANISOU 360 CB VAL A 45 4036 3584 3685 -192 10 27 C
ATOM 361 CG1 VAL A 45 14.125 -19.538 15.071 1.00 30.00 C
ANISOU 361 CG1 VAL A 45 4072 3642 3685 -199 -2 -29 C
ATOM 362 CG2 VAL A 45 15.838 -20.509 16.615 1.00 23.15 C
ANISOU 362 CG2 VAL A 45 3227 2720 2848 -117 22 9 C
ATOM 363 N VAL A 46 11.725 -18.819 17.880 1.00 24.32 N
ANISOU 363 N VAL A 46 3241 2983 3019 -320 16 123 N
ATOM 364 CA VAL A 46 10.392 -18.236 17.764 1.00 26.69 C
ANISOU 364 CA VAL A 46 3488 3327 3327 -373 8 131 C
ATOM 365 C VAL A 46 10.311 -16.922 18.532 1.00 29.26 C
ANISOU 365 C VAL A 46 3757 3733 3627 -353 40 159 C
ATOM 366 O VAL A 46 9.756 -15.933 18.037 1.00 32.68 O
ANISOU 366 O VAL A 46 4151 4217 4047 -354 32 143 O
ATOM 367 CB VAL A 46 9.326 -19.240 18.238 1.00 32.78 C
ANISOU 367 CB VAL A 46 4255 4054 4147 -447 -3 164 C
ATOM 368 CG1 VAL A 46 7.999 -18.534 18.473 1.00 29.50 C
ANISOU 368 CG1 VAL A 46 3762 3704 3745 -495 2 183 C
ATOM 369 CG2 VAL A 46 9.163 -20.353 17.215 1.00 29.26 C
ANISOU 369 CG2 VAL A 46 3862 3528 3730 -477 -49 121 C
ATOM 370 N SER A 47 10.855 -16.888 19.752 1.00 27.70 N
ANISOU 370 N SER A 47 3559 3544 3420 -330 71 199 N
ATOM 371 CA SER A 47 10.914 -15.632 20.494 1.00 29.28 C
ANISOU 371 CA SER A 47 3717 3817 3593 -303 98 214 C
ATOM 372 C SER A 47 11.735 -14.594 19.740 1.00 26.00 C
ANISOU 372 C SER A 47 3300 3429 3148 -257 94 176 C
ATOM 373 O SER A 47 11.417 -13.399 19.765 1.00 24.04 O
ANISOU 373 O SER A 47 3017 3232 2885 -248 100 171 O
ATOM 374 CB SER A 47 11.495 -15.870 21.887 1.00 25.13 C
ANISOU 374 CB SER A 47 3203 3293 3053 -283 124 258 C
ATOM 375 OG SER A 47 11.621 -14.649 22.594 1.00 28.26 O
ANISOU 375 OG SER A 47 3565 3755 3418 -254 145 262 O
ATOM 376 N LEU A 48 12.798 -15.037 19.065 1.00 29.21 N
ANISOU 376 N LEU A 48 3746 3802 3549 -228 87 147 N
ATOM 377 CA LEU A 48 13.558 -14.148 18.194 1.00 28.01 C
ANISOU 377 CA LEU A 48 3595 3677 3370 -195 90 113 C
ATOM 378 C LEU A 48 12.687 -13.617 17.063 1.00 28.68 C
ANISOU 378 C LEU A 48 3674 3777 3446 -218 68 91 C
ATOM 379 O LEU A 48 12.738 -12.426 16.733 1.00 23.97 O
ANISOU 379 O LEU A 48 3061 3219 2826 -205 72 86 O
ATOM 380 CB LEU A 48 14.772 -14.894 17.636 1.00 32.14 C
ANISOU 380 CB LEU A 48 4157 4164 3890 -160 92 84 C
ATOM 381 CG LEU A 48 15.986 -14.108 17.147 1.00 33.69 C
ANISOU 381 CG LEU A 48 4346 4394 4061 -121 113 60 C
ATOM 382 CD1 LEU A 48 16.565 -13.293 18.279 1.00 29.77 C
ANISOU 382 CD1 LEU A 48 3814 3934 3562 -103 129 85 C
ATOM 383 CD2 LEU A 48 17.035 -15.057 16.588 1.00 33.64 C
ANISOU 383 CD2 LEU A 48 4371 4354 4058 -84 118 27 C
ATOM 384 N ALA A 49 11.869 -14.483 16.463 1.00 25.91 N
ANISOU 384 N ALA A 49 3339 3393 3113 -253 40 78 N
ATOM 385 CA ALA A 49 11.011 -14.042 15.370 1.00 26.78 C
ANISOU 385 CA ALA A 49 3444 3520 3211 -273 7 54 C
ATOM 386 C ALA A 49 9.878 -13.154 15.866 1.00 28.48 C
ANISOU 386 C ALA A 49 3601 3782 3439 -290 2 79 C
ATOM 387 O ALA A 49 9.462 -12.231 15.156 1.00 26.68 O
ANISOU 387 O ALA A 49 3361 3583 3191 -282 -19 68 O
ATOM 388 CB ALA A 49 10.453 -15.250 14.619 1.00 24.71 C
ANISOU 388 CB ALA A 49 3213 3208 2967 -308 -31 26 C
ATOM 389 N ALA A 50 9.370 -13.411 17.073 1.00 27.63 N
ANISOU 389 N ALA A 50 3457 3680 3360 -310 21 113 N
ATOM 390 CA ALA A 50 8.296 -12.584 17.615 1.00 25.81 C
ANISOU 390 CA ALA A 50 3164 3501 3143 -319 24 131 C
ATOM 391 C ALA A 50 8.758 -11.147 17.827 1.00 25.47 C
ANISOU 391 C ALA A 50 3111 3496 3070 -271 40 131 C
ATOM 392 O ALA A 50 8.001 -10.199 17.587 1.00 27.55 O
ANISOU 392 O ALA A 50 3340 3794 3334 -261 24 126 O
ATOM 393 CB ALA A 50 7.781 -13.183 18.925 1.00 27.47 C
ANISOU 393 CB ALA A 50 3343 3716 3379 -349 56 170 C
ATOM 394 N ALA A 51 10.005 -10.966 18.268 1.00 24.18 N
ANISOU 394 N ALA A 51 2977 3326 2886 -241 67 134 N
ATOM 395 CA ALA A 51 10.539 -9.619 18.450 1.00 25.37 C
ANISOU 395 CA ALA A 51 3122 3503 3013 -204 78 131 C
ATOM 396 C ALA A 51 10.691 -8.899 17.116 1.00 22.01 C
ANISOU 396 C ALA A 51 2720 3074 2567 -194 54 111 C
ATOM 397 O ALA A 51 10.401 -7.702 17.015 1.00 23.98 O
ANISOU 397 O ALA A 51 2959 3344 2810 -175 46 112 O
ATOM 398 CB ALA A 51 11.878 -9.679 19.184 1.00 19.08 C
ANISOU 398 CB ALA A 51 2346 2700 2205 -181 105 136 C
ATOM 399 N ASP A 52 11.143 -9.612 16.080 1.00 22.30 N
ANISOU 399 N ASP A 52 2796 3085 2590 -202 43 93 N
ATOM 400 CA ASP A 52 11.282 -8.995 14.765 1.00 22.36 C
ANISOU 400 CA ASP A 52 2836 3096 2566 -194 24 78 C
ATOM 401 C ASP A 52 9.925 -8.666 14.155 1.00 23.66 C
ANISOU 401 C ASP A 52 2983 3273 2733 -205 -22 75 C
ATOM 402 O ASP A 52 9.795 -7.659 13.446 1.00 27.12 O
ANISOU 402 O ASP A 52 3436 3722 3146 -188 -42 78 O
ATOM 403 CB ASP A 52 12.088 -9.906 13.838 1.00 19.54 C
ANISOU 403 CB ASP A 52 2526 2714 2185 -196 28 52 C
ATOM 404 CG ASP A 52 13.572 -9.900 14.168 1.00 30.45 C
ANISOU 404 CG ASP A 52 3918 4093 3559 -174 72 51 C
ATOM 405 OD1 ASP A 52 14.091 -8.830 14.559 1.00 33.94 O
ANISOU 405 OD1 ASP A 52 4345 4554 3996 -162 91 66 O
ATOM 406 OD2 ASP A 52 14.224 -10.958 14.032 1.00 32.25 O
ANISOU 406 OD2 ASP A 52 4166 4298 3789 -168 83 32 O
ATOM 407 N ILE A 53 8.908 -9.494 14.413 1.00 23.72 N
ANISOU 407 N ILE A 53 2959 3280 2775 -233 -43 73 N
ATOM 408 CA ILE A 53 7.549 -9.143 14.001 1.00 25.82 C
ANISOU 408 CA ILE A 53 3187 3568 3054 -241 -90 70 C
ATOM 409 C ILE A 53 7.110 -7.853 14.683 1.00 25.40 C
ANISOU 409 C ILE A 53 3092 3548 3012 -209 -82 88 C
ATOM 410 O ILE A 53 6.529 -6.961 14.050 1.00 24.09 O
ANISOU 410 O ILE A 53 2920 3396 2836 -187 -120 86 O
ATOM 411 CB ILE A 53 6.576 -10.300 14.298 1.00 24.67 C
ANISOU 411 CB ILE A 53 3002 3418 2954 -288 -107 67 C
ATOM 412 CG1 ILE A 53 6.898 -11.508 13.421 1.00 23.38 C
ANISOU 412 CG1 ILE A 53 2891 3211 2780 -316 -130 39 C
ATOM 413 CG2 ILE A 53 5.136 -9.866 14.075 1.00 24.15 C
ANISOU 413 CG2 ILE A 53 2873 3389 2915 -296 -152 64 C
ATOM 414 CD1 ILE A 53 6.090 -12.737 13.769 1.00 25.36 C
ANISOU 414 CD1 ILE A 53 3114 3441 3083 -373 -145 38 C
ATOM 415 N ALA A 54 7.402 -7.725 15.980 1.00 23.37 N
ANISOU 415 N ALA A 54 2810 3300 2770 -202 -36 103 N
ATOM 416 CA ALA A 54 7.042 -6.514 16.712 1.00 24.89 C
ANISOU 416 CA ALA A 54 2968 3520 2970 -166 -26 110 C
ATOM 417 C ALA A 54 7.832 -5.302 16.230 1.00 22.41 C
ANISOU 417 C ALA A 54 2699 3190 2625 -132 -31 110 C
ATOM 418 O ALA A 54 7.368 -4.165 16.377 1.00 20.43 O
ANISOU 418 O ALA A 54 2434 2949 2381 -98 -44 110 O
ATOM 419 CB ALA A 54 7.253 -6.724 18.213 1.00 19.72 C
ANISOU 419 CB ALA A 54 2287 2880 2326 -166 25 122 C
ATOM 420 N VAL A 55 9.019 -5.518 15.661 1.00 20.32 N
ANISOU 420 N VAL A 55 2489 2900 2332 -141 -18 109 N
ATOM 421 CA VAL A 55 9.789 -4.406 15.109 1.00 22.63 C
ANISOU 421 CA VAL A 55 2825 3176 2597 -122 -18 114 C
ATOM 422 C VAL A 55 9.042 -3.779 13.939 1.00 25.66 C
ANISOU 422 C VAL A 55 3229 3557 2962 -109 -68 119 C
ATOM 423 O VAL A 55 8.942 -2.551 13.827 1.00 23.92 O
ANISOU 423 O VAL A 55 3023 3326 2738 -82 -82 130 O
ATOM 424 CB VAL A 55 11.195 -4.877 14.695 1.00 19.40 C
ANISOU 424 CB VAL A 55 2458 2751 2163 -138 13 112 C
ATOM 425 CG1 VAL A 55 11.873 -3.826 13.830 1.00 19.24 C
ANISOU 425 CG1 VAL A 55 2484 2718 2110 -132 14 123 C
ATOM 426 CG2 VAL A 55 12.039 -5.171 15.924 1.00 21.35 C
ANISOU 426 CG2 VAL A 55 2685 3000 2426 -138 52 111 C
ATOM 427 N GLY A 56 8.496 -4.614 13.055 1.00 25.97 N
ANISOU 427 N GLY A 56 3275 3602 2991 -127 -100 108 N
ATOM 428 CA GLY A 56 7.771 -4.088 11.912 1.00 23.20 C
ANISOU 428 CA GLY A 56 2947 3253 2616 -112 -158 112 C
ATOM 429 C GLY A 56 6.406 -3.545 12.285 1.00 27.92 C
ANISOU 429 C GLY A 56 3484 3872 3252 -86 -199 112 C
ATOM 430 O GLY A 56 5.945 -2.554 11.712 1.00 30.58 O
ANISOU 430 O GLY A 56 3837 4204 3576 -51 -242 124 O
ATOM 431 N VAL A 57 5.744 -4.175 13.253 1.00 26.85 N
ANISOU 431 N VAL A 57 3277 3760 3163 -98 -185 102 N
ATOM 432 CA VAL A 57 4.388 -3.767 13.599 1.00 28.29 C
ANISOU 432 CA VAL A 57 3387 3976 3387 -73 -217 97 C
ATOM 433 C VAL A 57 4.397 -2.496 14.441 1.00 31.93 C
ANISOU 433 C VAL A 57 3834 4437 3862 -23 -196 103 C
ATOM 434 O VAL A 57 3.552 -1.613 14.256 1.00 32.85 O
ANISOU 434 O VAL A 57 3926 4563 3994 24 -238 101 O
ATOM 435 CB VAL A 57 3.656 -4.921 14.309 1.00 32.90 C
ANISOU 435 CB VAL A 57 3896 4590 4015 -114 -200 87 C
ATOM 436 CG1 VAL A 57 2.295 -4.467 14.810 1.00 36.56 C
ANISOU 436 CG1 VAL A 57 4267 5100 4526 -88 -219 81 C
ATOM 437 CG2 VAL A 57 3.503 -6.105 13.368 1.00 30.90 C
ANISOU 437 CG2 VAL A 57 3660 4326 3754 -163 -237 74 C
ATOM 438 N LEU A 58 5.356 -2.369 15.359 1.00 23.53 N
ANISOU 438 N LEU A 58 2789 3360 2793 -26 -139 106 N
ATOM 439 CA LEU A 58 5.360 -1.278 16.327 1.00 25.54 C
ANISOU 439 CA LEU A 58 3030 3612 3061 18 -118 102 C
ATOM 440 C LEU A 58 6.614 -0.420 16.269 1.00 20.38 C
ANISOU 440 C LEU A 58 2448 2912 2381 25 -102 110 C
ATOM 441 O LEU A 58 6.508 0.810 16.190 1.00 24.79 O
ANISOU 441 O LEU A 58 3030 3445 2944 66 -124 111 O
ATOM 442 CB LEU A 58 5.177 -1.841 17.747 1.00 23.67 C
ANISOU 442 CB LEU A 58 2736 3411 2844 9 -64 92 C
ATOM 443 CG LEU A 58 3.794 -2.412 18.068 1.00 30.21 C
ANISOU 443 CG LEU A 58 3478 4293 3709 5 -68 86 C
ATOM 444 CD1 LEU A 58 3.752 -2.974 19.481 1.00 23.48 C
ANISOU 444 CD1 LEU A 58 2583 3476 2864 -11 -4 86 C
ATOM 445 CD2 LEU A 58 2.722 -1.350 17.879 1.00 31.59 C
ANISOU 445 CD2 LEU A 58 3610 4485 3908 65 -107 72 C
ATOM 446 N ALA A 59 7.804 -1.027 16.313 1.00 22.36 N
ANISOU 446 N ALA A 59 2733 3151 2612 -14 -67 116 N
ATOM 447 CA ALA A 59 9.031 -0.241 16.425 1.00 27.51 C
ANISOU 447 CA ALA A 59 3436 3768 3249 -16 -47 121 C
ATOM 448 C ALA A 59 9.260 0.646 15.207 1.00 23.92 C
ANISOU 448 C ALA A 59 3042 3275 2772 -11 -78 142 C
ATOM 449 O ALA A 59 9.786 1.757 15.342 1.00 27.87 O
ANISOU 449 O ALA A 59 3577 3738 3274 0 -77 149 O
ATOM 450 CB ALA A 59 10.235 -1.159 16.637 1.00 25.38 C
ANISOU 450 CB ALA A 59 3178 3500 2965 -55 -6 122 C
ATOM 451 N ILE A 60 8.880 0.184 14.021 1.00 21.20 N
ANISOU 451 N ILE A 60 2716 2937 2402 -21 -108 153 N
ATOM 452 CA ILE A 60 9.105 0.956 12.801 1.00 23.19 C
ANISOU 452 CA ILE A 60 3036 3156 2618 -18 -137 181 C
ATOM 453 C ILE A 60 8.066 2.070 12.684 1.00 21.14 C
ANISOU 453 C ILE A 60 2778 2878 2376 35 -192 189 C
ATOM 454 O ILE A 60 8.437 3.205 12.348 1.00 22.53 O
ANISOU 454 O ILE A 60 3011 3006 2541 47 -203 214 O
ATOM 455 CB ILE A 60 9.129 0.045 11.561 1.00 27.30 C
ANISOU 455 CB ILE A 60 3586 3693 3093 -43 -151 185 C
ATOM 456 CG1 ILE A 60 10.438 -0.750 11.524 1.00 25.29 C
ANISOU 456 CG1 ILE A 60 3348 3443 2817 -84 -93 180 C
ATOM 457 CG2 ILE A 60 8.955 0.857 10.285 1.00 25.56 C
ANISOU 457 CG2 ILE A 60 3435 3451 2827 -29 -195 217 C
ATOM 458 CD1 ILE A 60 10.626 -1.576 10.271 1.00 24.07 C
ANISOU 458 CD1 ILE A 60 3235 3302 2610 -104 -99 177 C
ATOM 459 N PRO A 61 6.774 1.826 12.944 1.00 25.73 N
ANISOU 459 N PRO A 61 3298 3493 2987 68 -227 171 N
ATOM 460 CA PRO A 61 5.849 2.967 13.051 1.00 24.54 C
ANISOU 460 CA PRO A 61 3137 3324 2862 131 -274 171 C
ATOM 461 C PRO A 61 6.241 3.953 14.139 1.00 27.84 C
ANISOU 461 C PRO A 61 3560 3708 3309 158 -245 160 C
ATOM 462 O PRO A 61 6.000 5.157 13.986 1.00 24.26 O
ANISOU 462 O PRO A 61 3143 3208 2866 204 -281 169 O
ATOM 463 CB PRO A 61 4.501 2.298 13.347 1.00 22.70 C
ANISOU 463 CB PRO A 61 2812 3150 2664 152 -299 146 C
ATOM 464 CG PRO A 61 4.620 0.960 12.722 1.00 26.49 C
ANISOU 464 CG PRO A 61 3288 3659 3120 96 -297 145 C
ATOM 465 CD PRO A 61 6.041 0.545 12.953 1.00 22.63 C
ANISOU 465 CD PRO A 61 2844 3150 2605 48 -234 151 C
ATOM 466 N PHE A 62 6.844 3.479 15.234 1.00 24.64 N
ANISOU 466 N PHE A 62 3125 3322 2916 132 -188 138 N
ATOM 467 CA PHE A 62 7.356 4.397 16.247 1.00 23.47 C
ANISOU 467 CA PHE A 62 2991 3141 2786 151 -164 121 C
ATOM 468 C PHE A 62 8.512 5.224 15.698 1.00 25.79 C
ANISOU 468 C PHE A 62 3368 3368 3062 123 -164 148 C
ATOM 469 O PHE A 62 8.599 6.431 15.958 1.00 26.08 O
ANISOU 469 O PHE A 62 3443 3349 3118 152 -182 145 O
ATOM 470 CB PHE A 62 7.802 3.628 17.493 1.00 24.78 C
ANISOU 470 CB PHE A 62 3112 3347 2957 127 -109 95 C
ATOM 471 CG PHE A 62 6.670 3.053 18.303 1.00 20.92 C
ANISOU 471 CG PHE A 62 2541 2918 2488 154 -97 70 C
ATOM 472 CD1 PHE A 62 5.352 3.221 17.912 1.00 25.94 C
ANISOU 472 CD1 PHE A 62 3135 3577 3145 197 -136 66 C
ATOM 473 CD2 PHE A 62 6.932 2.351 19.468 1.00 27.64 C
ANISOU 473 CD2 PHE A 62 3356 3808 3336 137 -48 54 C
ATOM 474 CE1 PHE A 62 4.319 2.691 18.664 1.00 22.39 C
ANISOU 474 CE1 PHE A 62 2599 3190 2718 216 -117 46 C
ATOM 475 CE2 PHE A 62 5.903 1.821 20.223 1.00 26.34 C
ANISOU 475 CE2 PHE A 62 3119 3704 3186 154 -27 39 C
ATOM 476 CZ PHE A 62 4.596 1.992 19.820 1.00 28.65 C
ANISOU 476 CZ PHE A 62 3361 4022 3504 191 -58 34 C
ATOM 477 N ALA A 63 9.413 4.591 14.942 1.00 24.30 N
ANISOU 477 N ALA A 63 3209 3183 2840 65 -142 173 N
ATOM 478 CA ALA A 63 10.558 5.311 14.392 1.00 24.59 C
ANISOU 478 CA ALA A 63 3316 3167 2861 28 -130 203 C
ATOM 479 C ALA A 63 10.115 6.375 13.397 1.00 22.31 C
ANISOU 479 C ALA A 63 3094 2824 2560 53 -180 240 C
ATOM 480 O ALA A 63 10.697 7.464 13.338 1.00 25.08 O
ANISOU 480 O ALA A 63 3502 3108 2919 43 -183 261 O
ATOM 481 CB ALA A 63 11.528 4.330 13.734 1.00 27.16 C
ANISOU 481 CB ALA A 63 3650 3521 3149 -31 -89 218 C
ATOM 482 N ILE A 64 9.084 6.076 12.604 1.00 28.62 N
ANISOU 482 N ILE A 64 3889 3645 3340 85 -225 252 N
ATOM 483 CA ILE A 64 8.536 7.071 11.687 1.00 29.15 C
ANISOU 483 CA ILE A 64 4021 3662 3394 123 -285 290 C
ATOM 484 C ILE A 64 7.947 8.241 12.464 1.00 25.59 C
ANISOU 484 C ILE A 64 3569 3161 2995 187 -318 272 C
ATOM 485 O ILE A 64 8.113 9.406 12.084 1.00 31.65 O
ANISOU 485 O ILE A 64 4412 3849 3764 202 -348 304 O
ATOM 486 CB ILE A 64 7.493 6.417 10.761 1.00 27.52 C
ANISOU 486 CB ILE A 64 3797 3501 3157 148 -337 296 C
ATOM 487 CG1 ILE A 64 8.162 5.381 9.853 1.00 24.08 C
ANISOU 487 CG1 ILE A 64 3386 3103 2662 88 -308 312 C
ATOM 488 CG2 ILE A 64 6.758 7.469 9.942 1.00 25.90 C
ANISOU 488 CG2 ILE A 64 3651 3247 2941 205 -413 333 C
ATOM 489 CD1 ILE A 64 7.186 4.561 9.038 1.00 27.12 C
ANISOU 489 CD1 ILE A 64 3749 3536 3018 104 -360 304 C
ATOM 490 N THR A 65 7.265 7.950 13.574 1.00 27.85 N
ANISOU 490 N THR A 65 3773 3487 3321 226 -311 220 N
ATOM 491 CA THR A 65 6.638 9.005 14.365 1.00 27.31 C
ANISOU 491 CA THR A 65 3697 3379 3300 299 -338 190 C
ATOM 492 C THR A 65 7.679 9.946 14.960 1.00 27.32 C
ANISOU 492 C THR A 65 3757 3306 3318 276 -314 186 C
ATOM 493 O THR A 65 7.548 11.172 14.872 1.00 26.71 O
ANISOU 493 O THR A 65 3740 3146 3263 315 -354 194 O
ATOM 494 CB THR A 65 5.781 8.386 15.470 1.00 29.19 C
ANISOU 494 CB THR A 65 3830 3692 3567 337 -317 135 C
ATOM 495 OG1 THR A 65 4.770 7.555 14.886 1.00 28.04 O
ANISOU 495 OG1 THR A 65 3626 3612 3417 351 -345 139 O
ATOM 496 CG2 THR A 65 5.118 9.471 16.301 1.00 25.81 C
ANISOU 496 CG2 THR A 65 3393 3230 3183 422 -339 95 C
ATOM 497 N ILE A 66 8.728 9.387 15.567 1.00 24.76 N
ANISOU 497 N ILE A 66 3416 3005 2987 211 -256 171 N
ATOM 498 CA ILE A 66 9.729 10.205 16.242 1.00 26.60 C
ANISOU 498 CA ILE A 66 3690 3176 3240 182 -238 157 C
ATOM 499 C ILE A 66 10.602 10.987 15.274 1.00 29.73 C
ANISOU 499 C ILE A 66 4177 3491 3626 130 -247 213 C
ATOM 500 O ILE A 66 11.296 11.919 15.694 1.00 33.24 O
ANISOU 500 O ILE A 66 4667 3864 4098 108 -248 207 O
ATOM 501 CB ILE A 66 10.606 9.326 17.158 1.00 34.12 C
ANISOU 501 CB ILE A 66 4592 4185 4188 131 -180 125 C
ATOM 502 CG1 ILE A 66 11.239 10.169 18.265 1.00 41.71 C
ANISOU 502 CG1 ILE A 66 5571 5098 5178 129 -176 84 C
ATOM 503 CG2 ILE A 66 11.681 8.607 16.353 1.00 27.94 C
ANISOU 503 CG2 ILE A 66 3822 3421 3373 50 -145 166 C
ATOM 504 CD1 ILE A 66 12.222 9.408 19.116 1.00 41.19 C
ANISOU 504 CD1 ILE A 66 5464 5082 5104 79 -131 57 C
ATOM 505 N SER A 67 10.586 10.646 13.983 1.00 25.09 N
ANISOU 505 N SER A 67 3622 2915 2997 106 -254 269 N
ATOM 506 CA SER A 67 11.371 11.407 13.019 1.00 29.26 C
ANISOU 506 CA SER A 67 4241 3370 3505 54 -256 332 C
ATOM 507 C SER A 67 10.748 12.761 12.711 1.00 28.14 C
ANISOU 507 C SER A 67 4177 3130 3386 109 -320 358 C
ATOM 508 O SER A 67 11.452 13.658 12.235 1.00 32.63 O
ANISOU 508 O SER A 67 4830 3614 3956 64 -322 406 O
ATOM 509 CB SER A 67 11.547 10.608 11.725 1.00 30.12 C
ANISOU 509 CB SER A 67 4368 3529 3549 16 -240 382 C
ATOM 510 OG SER A 67 10.303 10.388 11.086 1.00 26.11 O
ANISOU 510 OG SER A 67 3858 3045 3019 81 -295 391 O
ATOM 511 N THR A 68 9.449 12.931 12.971 1.00 27.33 N
ANISOU 511 N THR A 68 4047 3033 3304 204 -373 329 N
ATOM 512 CA THR A 68 8.786 14.202 12.712 1.00 28.83 C
ANISOU 512 CA THR A 68 4308 3126 3520 274 -442 349 C
ATOM 513 C THR A 68 9.081 15.249 13.779 1.00 36.99 C
ANISOU 513 C THR A 68 5367 4074 4614 291 -447 305 C
ATOM 514 O THR A 68 8.865 16.441 13.534 1.00 43.37 O
ANISOU 514 O THR A 68 6258 4772 5447 329 -499 328 O
ATOM 515 CB THR A 68 7.273 13.995 12.608 1.00 32.97 C
ANISOU 515 CB THR A 68 4780 3696 4051 378 -499 327 C
ATOM 516 OG1 THR A 68 6.758 13.588 13.881 1.00 33.47 O
ANISOU 516 OG1 THR A 68 4744 3820 4152 422 -476 247 O
ATOM 517 CG2 THR A 68 6.953 12.925 11.578 1.00 32.77 C
ANISOU 517 CG2 THR A 68 4729 3755 3968 358 -504 361 C
ATOM 518 N GLY A 69 9.565 14.838 14.948 1.00 34.95 N
ANISOU 518 N GLY A 69 5046 3858 4375 266 -399 242 N
ATOM 519 CA GLY A 69 9.816 15.781 16.021 1.00 32.54 C
ANISOU 519 CA GLY A 69 4764 3479 4121 285 -408 187 C
ATOM 520 C GLY A 69 8.569 16.412 16.592 1.00 37.55 C
ANISOU 520 C GLY A 69 5388 4088 4791 409 -458 134 C
ATOM 521 O GLY A 69 8.636 17.521 17.132 1.00 33.05 O
ANISOU 521 O GLY A 69 4875 3420 4264 442 -488 102 O
ATOM 522 N PHE A 70 7.432 15.726 16.494 1.00 33.95 N
ANISOU 522 N PHE A 70 4856 3721 4322 478 -467 121 N
ATOM 523 CA PHE A 70 6.155 16.281 16.925 1.00 36.46 C
ANISOU 523 CA PHE A 70 5148 4030 4676 604 -512 73 C
ATOM 524 C PHE A 70 6.154 16.570 18.422 1.00 38.84 C
ANISOU 524 C PHE A 70 5416 4336 5006 644 -485 -19 C
ATOM 525 O PHE A 70 6.876 15.944 19.202 1.00 31.16 O
ANISOU 525 O PHE A 70 4406 3418 4016 581 -428 -49 O
ATOM 526 CB PHE A 70 5.019 15.311 16.585 1.00 35.88 C
ANISOU 526 CB PHE A 70 4976 4071 4586 652 -517 74 C
ATOM 527 CG PHE A 70 4.940 14.118 17.504 1.00 38.70 C
ANISOU 527 CG PHE A 70 5222 4552 4928 628 -450 26 C
ATOM 528 CD1 PHE A 70 5.988 13.215 17.585 1.00 30.63 C
ANISOU 528 CD1 PHE A 70 4192 3574 3873 523 -392 42 C
ATOM 529 CD2 PHE A 70 3.811 13.894 18.277 1.00 42.97 C
ANISOU 529 CD2 PHE A 70 5670 5167 5491 712 -443 -33 C
ATOM 530 CE1 PHE A 70 5.919 12.119 18.427 1.00 32.97 C
ANISOU 530 CE1 PHE A 70 4397 3974 4155 503 -336 5 C
ATOM 531 CE2 PHE A 70 3.734 12.797 19.118 1.00 36.74 C
ANISOU 531 CE2 PHE A 70 4786 4487 4684 684 -378 -68 C
ATOM 532 CZ PHE A 70 4.789 11.909 19.193 1.00 35.45 C
ANISOU 532 CZ PHE A 70 4627 4357 4487 580 -328 -46 C
ATOM 533 N CYS A 71 5.324 17.530 18.820 1.00 38.50 N
ANISOU 533 N CYS A 71 5389 4236 5002 754 -529 -65 N
ATOM 534 CA CYS A 71 5.173 17.846 20.233 1.00 39.87 C
ANISOU 534 CA CYS A 71 5534 4420 5196 810 -505 -162 C
ATOM 535 C CYS A 71 4.480 16.697 20.956 1.00 39.68 C
ANISOU 535 C CYS A 71 5380 4551 5147 835 -448 -204 C
ATOM 536 O CYS A 71 3.454 16.187 20.496 1.00 41.58 O
ANISOU 536 O CYS A 71 5547 4864 5388 883 -457 -188 O
ATOM 537 CB CYS A 71 4.380 19.139 20.411 1.00 34.08 C
ANISOU 537 CB CYS A 71 4849 3588 4511 935 -566 -205 C
ATOM 538 SG CYS A 71 5.187 20.615 19.755 1.00 49.85 S
ANISOU 538 SG CYS A 71 7015 5379 6546 907 -635 -160 S
ATOM 539 N ALA A 72 5.046 16.288 22.090 1.00 35.26 N
ANISOU 539 N ALA A 72 4792 4041 4565 798 -392 -256 N
ATOM 540 CA ALA A 72 4.497 15.177 22.852 1.00 34.06 C
ANISOU 540 CA ALA A 72 4527 4031 4383 809 -330 -288 C
ATOM 541 C ALA A 72 4.934 15.286 24.305 1.00 41.33 C
ANISOU 541 C ALA A 72 5448 4974 5284 814 -288 -366 C
ATOM 542 O ALA A 72 5.974 15.875 24.614 1.00 39.30 O
ANISOU 542 O ALA A 72 5268 4636 5028 769 -302 -382 O
ATOM 543 CB ALA A 72 4.937 13.829 22.270 1.00 34.26 C
ANISOU 543 CB ALA A 72 4509 4136 4374 707 -295 -223 C
ATOM 544 N ALA A 73 4.119 14.716 25.192 1.00 36.60 N
ANISOU 544 N ALA A 73 4758 4485 4662 867 -238 -413 N
ATOM 545 CA ALA A 73 4.513 14.556 26.584 1.00 38.63 C
ANISOU 545 CA ALA A 73 5009 4790 4880 865 -189 -478 C
ATOM 546 C ALA A 73 5.791 13.731 26.653 1.00 37.01 C
ANISOU 546 C ALA A 73 4820 4604 4638 744 -165 -439 C
ATOM 547 O ALA A 73 5.944 12.737 25.942 1.00 30.25 O
ANISOU 547 O ALA A 73 3926 3793 3773 676 -150 -371 O
ATOM 548 CB ALA A 73 3.390 13.880 27.370 1.00 36.69 C
ANISOU 548 CB ALA A 73 4656 4678 4609 928 -127 -514 C
ATOM 549 N CYS A 74 6.727 14.154 27.497 1.00 36.52 N
ANISOU 549 N CYS A 74 4814 4504 4557 719 -168 -486 N
ATOM 550 CA CYS A 74 8.082 13.630 27.366 1.00 39.67 C
ANISOU 550 CA CYS A 74 5239 4894 4940 606 -165 -447 C
ATOM 551 C CYS A 74 8.153 12.137 27.700 1.00 32.05 C
ANISOU 551 C CYS A 74 4200 4052 3926 559 -107 -415 C
ATOM 552 O CYS A 74 8.904 11.392 27.061 1.00 31.17 O
ANISOU 552 O CYS A 74 4084 3949 3813 475 -102 -355 O
ATOM 553 CB CYS A 74 9.029 14.459 28.233 1.00 46.24 C
ANISOU 553 CB CYS A 74 6142 5660 5768 593 -191 -511 C
ATOM 554 SG CYS A 74 10.786 14.161 27.953 1.00 47.01 S
ANISOU 554 SG CYS A 74 6273 5722 5867 457 -205 -469 S
ATOM 555 N HIS A 75 7.341 11.666 28.649 1.00 30.87 N
ANISOU 555 N HIS A 75 3992 3997 3739 614 -59 -452 N
ATOM 556 CA HIS A 75 7.365 10.242 28.970 1.00 36.78 C
ANISOU 556 CA HIS A 75 4678 4852 4443 567 -5 -415 C
ATOM 557 C HIS A 75 6.744 9.393 27.866 1.00 32.30 C
ANISOU 557 C HIS A 75 4054 4319 3900 540 4 -345 C
ATOM 558 O HIS A 75 7.190 8.264 27.640 1.00 31.66 O
ANISOU 558 O HIS A 75 3948 4279 3801 471 27 -295 O
ATOM 559 CB HIS A 75 6.672 9.992 30.307 1.00 39.61 C
ANISOU 559 CB HIS A 75 4997 5304 4750 626 50 -467 C
ATOM 560 CG HIS A 75 7.540 10.293 31.489 1.00 47.60 C
ANISOU 560 CG HIS A 75 6062 6314 5711 623 48 -523 C
ATOM 561 ND1 HIS A 75 8.037 11.554 31.739 1.00 50.30 N
ANISOU 561 ND1 HIS A 75 6478 6564 6069 651 -2 -587 N
ATOM 562 CD2 HIS A 75 8.023 9.497 32.473 1.00 54.01 C
ANISOU 562 CD2 HIS A 75 6868 7198 6455 594 82 -525 C
ATOM 563 CE1 HIS A 75 8.776 11.527 32.833 1.00 44.97 C
ANISOU 563 CE1 HIS A 75 5836 5911 5338 639 -1 -632 C
ATOM 564 NE2 HIS A 75 8.783 10.291 33.299 1.00 59.03 N
ANISOU 564 NE2 HIS A 75 7571 7794 7065 608 50 -593 N
ATOM 565 N GLY A 76 5.722 9.901 27.176 1.00 30.99 N
ANISOU 565 N GLY A 76 3866 4134 3775 598 -18 -343 N
ATOM 566 CA GLY A 76 5.220 9.191 26.010 1.00 27.17 C
ANISOU 566 CA GLY A 76 3338 3671 3315 569 -26 -280 C
ATOM 567 C GLY A 76 6.220 9.175 24.870 1.00 28.64 C
ANISOU 567 C GLY A 76 3584 3785 3514 495 -65 -225 C
ATOM 568 O GLY A 76 6.316 8.195 24.125 1.00 25.70 O
ANISOU 568 O GLY A 76 3185 3443 3136 438 -57 -172 O
ATOM 569 N CYS A 77 6.978 10.263 24.717 1.00 26.92 N
ANISOU 569 N CYS A 77 3447 3470 3312 493 -104 -238 N
ATOM 570 CA CYS A 77 8.047 10.290 23.727 1.00 25.61 C
ANISOU 570 CA CYS A 77 3337 3241 3154 415 -128 -185 C
ATOM 571 C CYS A 77 9.151 9.307 24.089 1.00 28.35 C
ANISOU 571 C CYS A 77 3673 3631 3470 334 -92 -170 C
ATOM 572 O CYS A 77 9.769 8.702 23.205 1.00 25.05 O
ANISOU 572 O CYS A 77 3260 3211 3048 269 -89 -119 O
ATOM 573 CB CYS A 77 8.603 11.709 23.610 1.00 30.67 C
ANISOU 573 CB CYS A 77 4064 3765 3824 424 -174 -203 C
ATOM 574 SG CYS A 77 9.963 11.869 22.446 1.00 44.53 S
ANISOU 574 SG CYS A 77 5886 5445 5588 320 -192 -137 S
ATOM 575 N LEU A 78 9.413 9.135 25.387 1.00 23.80 N
ANISOU 575 N LEU A 78 3081 3094 2866 343 -65 -217 N
ATOM 576 CA LEU A 78 10.406 8.160 25.825 1.00 25.14 C
ANISOU 576 CA LEU A 78 3237 3309 3005 279 -38 -203 C
ATOM 577 C LEU A 78 10.005 6.749 25.415 1.00 27.28 C
ANISOU 577 C LEU A 78 3451 3652 3260 253 -4 -156 C
ATOM 578 O LEU A 78 10.826 5.984 24.896 1.00 28.00 O
ANISOU 578 O LEU A 78 3543 3748 3347 191 3 -118 O
ATOM 579 CB LEU A 78 10.594 8.246 27.341 1.00 27.36 C
ANISOU 579 CB LEU A 78 3518 3626 3250 306 -21 -262 C
ATOM 580 CG LEU A 78 11.516 9.341 27.877 1.00 27.49 C
ANISOU 580 CG LEU A 78 3596 3575 3276 300 -58 -312 C
ATOM 581 CD1 LEU A 78 11.468 9.371 29.397 1.00 23.34 C
ANISOU 581 CD1 LEU A 78 3070 3098 2701 341 -44 -376 C
ATOM 582 CD2 LEU A 78 12.941 9.129 27.388 1.00 25.96 C
ANISOU 582 CD2 LEU A 78 3420 3349 3096 213 -74 -279 C
ATOM 583 N PHE A 79 8.740 6.384 25.643 1.00 25.29 N
ANISOU 583 N PHE A 79 3147 3458 3005 298 18 -161 N
ATOM 584 CA PHE A 79 8.285 5.045 25.283 1.00 25.14 C
ANISOU 584 CA PHE A 79 3074 3501 2978 267 46 -119 C
ATOM 585 C PHE A 79 8.384 4.818 23.778 1.00 24.29 C
ANISOU 585 C PHE A 79 2978 3358 2892 230 17 -72 C
ATOM 586 O PHE A 79 8.784 3.737 23.331 1.00 22.50 O
ANISOU 586 O PHE A 79 2742 3152 2656 177 31 -38 O
ATOM 587 CB PHE A 79 6.852 4.827 25.776 1.00 24.53 C
ANISOU 587 CB PHE A 79 2930 3491 2901 319 73 -134 C
ATOM 588 CG PHE A 79 6.298 3.468 25.451 1.00 29.88 C
ANISOU 588 CG PHE A 79 3550 4227 3578 278 100 -93 C
ATOM 589 CD1 PHE A 79 6.561 2.382 26.271 1.00 32.06 C
ANISOU 589 CD1 PHE A 79 3806 4554 3819 242 145 -78 C
ATOM 590 CD2 PHE A 79 5.509 3.278 24.329 1.00 25.22 C
ANISOU 590 CD2 PHE A 79 2928 3635 3020 276 74 -68 C
ATOM 591 CE1 PHE A 79 6.051 1.132 25.973 1.00 29.92 C
ANISOU 591 CE1 PHE A 79 3489 4324 3554 200 166 -39 C
ATOM 592 CE2 PHE A 79 4.997 2.031 24.026 1.00 27.09 C
ANISOU 592 CE2 PHE A 79 3113 3919 3262 233 91 -36 C
ATOM 593 CZ PHE A 79 5.269 0.957 24.849 1.00 29.22 C
ANISOU 593 CZ PHE A 79 3367 4231 3504 193 139 -21 C
ATOM 594 N ILE A 80 8.034 5.833 22.985 1.00 26.69 N
ANISOU 594 N ILE A 80 3312 3606 3223 261 -24 -72 N
ATOM 595 CA ILE A 80 8.172 5.744 21.533 1.00 28.23 C
ANISOU 595 CA ILE A 80 3533 3766 3427 229 -54 -26 C
ATOM 596 C ILE A 80 9.634 5.563 21.143 1.00 26.38 C
ANISOU 596 C ILE A 80 3345 3498 3179 161 -47 -2 C
ATOM 597 O ILE A 80 9.956 4.828 20.200 1.00 24.62 O
ANISOU 597 O ILE A 80 3127 3282 2945 117 -44 34 O
ATOM 598 CB ILE A 80 7.557 6.992 20.868 1.00 24.14 C
ANISOU 598 CB ILE A 80 3050 3188 2935 282 -104 -27 C
ATOM 599 CG1 ILE A 80 6.034 6.961 20.982 1.00 30.53 C
ANISOU 599 CG1 ILE A 80 3794 4044 3763 350 -115 -44 C
ATOM 600 CG2 ILE A 80 7.981 7.109 19.412 1.00 31.44 C
ANISOU 600 CG2 ILE A 80 4028 4065 3855 244 -136 24 C
ATOM 601 CD1 ILE A 80 5.412 5.771 20.307 1.00 30.48 C
ANISOU 601 CD1 ILE A 80 3732 4098 3752 321 -112 -14 C
ATOM 602 N ALA A 81 10.542 6.220 21.864 1.00 21.77 N
ANISOU 602 N ALA A 81 2793 2880 2597 152 -44 -28 N
ATOM 603 CA ALA A 81 11.952 6.166 21.499 1.00 23.24 C
ANISOU 603 CA ALA A 81 3012 3038 2779 86 -38 -8 C
ATOM 604 C ALA A 81 12.642 4.911 22.016 1.00 24.48 C
ANISOU 604 C ALA A 81 3134 3253 2916 50 -2 -6 C
ATOM 605 O ALA A 81 13.626 4.464 21.417 1.00 25.90 O
ANISOU 605 O ALA A 81 3320 3428 3091 0 9 18 O
ATOM 606 CB ALA A 81 12.679 7.405 22.025 1.00 22.73 C
ANISOU 606 CB ALA A 81 2993 2909 2734 83 -57 -37 C
ATOM 607 N CYS A 82 12.149 4.327 23.108 1.00 23.35 N
ANISOU 607 N CYS A 82 2951 3164 2756 78 17 -30 N
ATOM 608 CA CYS A 82 12.865 3.260 23.793 1.00 22.20 C
ANISOU 608 CA CYS A 82 2784 3064 2589 51 43 -28 C
ATOM 609 C CYS A 82 12.288 1.871 23.555 1.00 23.86 C
ANISOU 609 C CYS A 82 2957 3322 2787 41 66 1 C
ATOM 610 O CYS A 82 12.929 0.886 23.937 1.00 23.01 O
ANISOU 610 O CYS A 82 2838 3240 2665 18 84 11 O
ATOM 611 CB CYS A 82 12.900 3.533 25.303 1.00 23.17 C
ANISOU 611 CB CYS A 82 2901 3210 2690 81 48 -70 C
ATOM 612 SG CYS A 82 13.898 4.964 25.787 1.00 25.95 S
ANISOU 612 SG CYS A 82 3300 3504 3057 78 14 -114 S
ATOM 613 N PHE A 83 11.108 1.754 22.940 1.00 22.44 N
ANISOU 613 N PHE A 83 2758 3152 2618 58 62 13 N
ATOM 614 CA PHE A 83 10.500 0.433 22.809 1.00 19.37 C
ANISOU 614 CA PHE A 83 2331 2804 2223 42 81 36 C
ATOM 615 C PHE A 83 11.321 -0.485 21.910 1.00 25.65 C
ANISOU 615 C PHE A 83 3143 3587 3016 -4 82 62 C
ATOM 616 O PHE A 83 11.311 -1.707 22.100 1.00 20.13 O
ANISOU 616 O PHE A 83 2426 2912 2310 -24 100 76 O
ATOM 617 CB PHE A 83 9.068 0.549 22.287 1.00 19.74 C
ANISOU 617 CB PHE A 83 2346 2867 2289 66 68 38 C
ATOM 618 CG PHE A 83 8.344 -0.765 22.234 1.00 22.81 C
ANISOU 618 CG PHE A 83 2690 3298 2681 41 85 58 C
ATOM 619 CD1 PHE A 83 7.929 -1.389 23.400 1.00 24.09 C
ANISOU 619 CD1 PHE A 83 2815 3507 2832 42 123 58 C
ATOM 620 CD2 PHE A 83 8.090 -1.384 21.022 1.00 22.86 C
ANISOU 620 CD2 PHE A 83 2696 3293 2697 13 62 77 C
ATOM 621 CE1 PHE A 83 7.268 -2.604 23.356 1.00 25.73 C
ANISOU 621 CE1 PHE A 83 2985 3744 3048 8 139 81 C
ATOM 622 CE2 PHE A 83 7.428 -2.599 20.972 1.00 21.92 C
ANISOU 622 CE2 PHE A 83 2539 3202 2586 -18 72 92 C
ATOM 623 CZ PHE A 83 7.017 -3.209 22.139 1.00 28.32 C
ANISOU 623 CZ PHE A 83 3311 4054 3395 -23 111 96 C
ATOM 624 N VAL A 84 12.044 0.077 20.937 1.00 24.68 N
ANISOU 624 N VAL A 84 3056 3424 2896 -20 66 68 N
ATOM 625 CA VAL A 84 12.903 -0.751 20.095 1.00 27.27 C
ANISOU 625 CA VAL A 84 3398 3746 3216 -57 75 86 C
ATOM 626 C VAL A 84 14.052 -1.335 20.912 1.00 21.43 C
ANISOU 626 C VAL A 84 2652 3019 2471 -70 96 80 C
ATOM 627 O VAL A 84 14.550 -2.426 20.606 1.00 23.48 O
ANISOU 627 O VAL A 84 2908 3287 2727 -87 109 90 O
ATOM 628 CB VAL A 84 13.405 0.057 18.881 1.00 24.08 C
ANISOU 628 CB VAL A 84 3035 3304 2810 -72 62 99 C
ATOM 629 CG1 VAL A 84 14.286 1.221 19.322 1.00 19.78 C
ANISOU 629 CG1 VAL A 84 2510 2730 2276 -77 61 88 C
ATOM 630 CG2 VAL A 84 14.137 -0.845 17.893 1.00 21.85 C
ANISOU 630 CG2 VAL A 84 2765 3026 2511 -104 78 112 C
ATOM 631 N LEU A 85 14.477 -0.640 21.972 1.00 25.75 N
ANISOU 631 N LEU A 85 3197 3567 3019 -57 94 60 N
ATOM 632 CA LEU A 85 15.507 -1.187 22.850 1.00 22.92 C
ANISOU 632 CA LEU A 85 2829 3227 2653 -62 103 52 C
ATOM 633 C LEU A 85 14.999 -2.401 23.617 1.00 24.93 C
ANISOU 633 C LEU A 85 3066 3515 2892 -52 117 64 C
ATOM 634 O LEU A 85 15.775 -3.317 23.913 1.00 23.33 O
ANISOU 634 O LEU A 85 2860 3322 2684 -58 123 73 O
ATOM 635 CB LEU A 85 15.997 -0.111 23.820 1.00 22.18 C
ANISOU 635 CB LEU A 85 2742 3126 2559 -51 88 23 C
ATOM 636 CG LEU A 85 16.409 1.224 23.197 1.00 26.00 C
ANISOU 636 CG LEU A 85 3250 3565 3065 -67 71 13 C
ATOM 637 CD1 LEU A 85 16.824 2.218 24.271 1.00 25.90 C
ANISOU 637 CD1 LEU A 85 3246 3540 3055 -57 50 -25 C
ATOM 638 CD2 LEU A 85 17.526 1.022 22.184 1.00 23.60 C
ANISOU 638 CD2 LEU A 85 2945 3247 2774 -109 81 31 C
ATOM 639 N VAL A 86 13.706 -2.422 23.950 1.00 21.73 N
ANISOU 639 N VAL A 86 2648 3129 2482 -36 124 67 N
ATOM 640 CA VAL A 86 13.120 -3.589 24.607 1.00 25.07 C
ANISOU 640 CA VAL A 86 3054 3581 2891 -37 144 88 C
ATOM 641 C VAL A 86 13.166 -4.794 23.678 1.00 21.45 C
ANISOU 641 C VAL A 86 2597 3106 2446 -66 146 111 C
ATOM 642 O VAL A 86 13.575 -5.893 24.073 1.00 25.22 O
ANISOU 642 O VAL A 86 3080 3584 2917 -74 154 129 O
ATOM 643 CB VAL A 86 11.680 -3.285 25.058 1.00 22.05 C
ANISOU 643 CB VAL A 86 2644 3228 2506 -19 158 85 C
ATOM 644 CG1 VAL A 86 11.019 -4.542 25.601 1.00 19.81 C
ANISOU 644 CG1 VAL A 86 2340 2973 2213 -36 185 115 C
ATOM 645 CG2 VAL A 86 11.669 -2.176 26.096 1.00 22.26 C
ANISOU 645 CG2 VAL A 86 2675 3272 2512 18 159 53 C
ATOM 646 N LEU A 87 12.740 -4.606 22.428 1.00 27.53 N
ANISOU 646 N LEU A 87 3370 3858 3233 -77 133 110 N
ATOM 647 CA LEU A 87 12.741 -5.709 21.474 1.00 23.85 C
ANISOU 647 CA LEU A 87 2913 3375 2776 -102 130 122 C
ATOM 648 C LEU A 87 14.160 -6.181 21.189 1.00 27.57 C
ANISOU 648 C LEU A 87 3406 3828 3243 -105 134 119 C
ATOM 649 O LEU A 87 14.427 -7.387 21.137 1.00 22.77 O
ANISOU 649 O LEU A 87 2805 3208 2638 -113 139 128 O
ATOM 650 CB LEU A 87 12.043 -5.285 20.183 1.00 22.19 C
ANISOU 650 CB LEU A 87 2706 3152 2571 -109 109 118 C
ATOM 651 CG LEU A 87 10.604 -4.787 20.330 1.00 20.13 C
ANISOU 651 CG LEU A 87 2413 2913 2323 -98 98 118 C
ATOM 652 CD1 LEU A 87 10.055 -4.326 18.988 1.00 18.89 C
ANISOU 652 CD1 LEU A 87 2266 2742 2168 -98 64 114 C
ATOM 653 CD2 LEU A 87 9.718 -5.865 20.936 1.00 18.98 C
ANISOU 653 CD2 LEU A 87 2232 2789 2189 -117 112 131 C
ATOM 654 N THR A 88 15.087 -5.239 21.005 1.00 24.10 N
ANISOU 654 N THR A 88 2973 3384 2801 -100 133 106 N
ATOM 655 CA THR A 88 16.468 -5.611 20.719 1.00 24.31 C
ANISOU 655 CA THR A 88 3004 3403 2828 -102 141 100 C
ATOM 656 C THR A 88 17.087 -6.362 21.890 1.00 27.68 C
ANISOU 656 C THR A 88 3421 3842 3254 -86 142 103 C
ATOM 657 O THR A 88 17.821 -7.338 21.693 1.00 22.88 O
ANISOU 657 O THR A 88 2816 3226 2652 -80 146 104 O
ATOM 658 CB THR A 88 17.288 -4.366 20.382 1.00 28.83 C
ANISOU 658 CB THR A 88 3578 3971 3403 -110 142 89 C
ATOM 659 OG1 THR A 88 16.743 -3.735 19.216 1.00 27.80 O
ANISOU 659 OG1 THR A 88 3469 3826 3268 -123 138 94 O
ATOM 660 CG2 THR A 88 18.736 -4.740 20.113 1.00 27.68 C
ANISOU 660 CG2 THR A 88 3421 3830 3264 -114 156 80 C
ATOM 661 N GLN A 89 16.790 -5.931 23.118 1.00 23.63 N
ANISOU 661 N GLN A 89 2900 3347 2730 -74 137 104 N
ATOM 662 CA GLN A 89 17.320 -6.623 24.287 1.00 18.51 C
ANISOU 662 CA GLN A 89 2250 2712 2068 -56 132 113 C
ATOM 663 C GLN A 89 16.773 -8.043 24.379 1.00 27.04 C
ANISOU 663 C GLN A 89 3344 3782 3149 -59 140 142 C
ATOM 664 O GLN A 89 17.489 -8.969 24.780 1.00 21.61 O
ANISOU 664 O GLN A 89 2665 3085 2460 -44 133 154 O
ATOM 665 CB GLN A 89 16.992 -5.837 25.556 1.00 22.39 C
ANISOU 665 CB GLN A 89 2740 3232 2536 -41 127 106 C
ATOM 666 CG GLN A 89 17.813 -6.259 26.755 1.00 23.71 C
ANISOU 666 CG GLN A 89 2911 3418 2680 -18 111 109 C
ATOM 667 CD GLN A 89 19.295 -6.054 26.528 1.00 28.37 C
ANISOU 667 CD GLN A 89 3486 4005 3290 -14 90 88 C
ATOM 668 OE1 GLN A 89 19.712 -5.038 25.973 1.00 27.25 O
ANISOU 668 OE1 GLN A 89 3331 3857 3167 -30 86 63 O
ATOM 669 NE2 GLN A 89 20.100 -7.025 26.944 1.00 29.62 N
ANISOU 669 NE2 GLN A 89 3643 4167 3446 6 75 100 N
ATOM 670 N SER A 90 15.505 -8.233 24.007 1.00 20.85 N
ANISOU 670 N SER A 90 2560 2992 2369 -79 150 154 N
ATOM 671 CA SER A 90 14.932 -9.575 23.993 1.00 22.65 C
ANISOU 671 CA SER A 90 2800 3200 2605 -95 155 181 C
ATOM 672 C SER A 90 15.658 -10.473 23.000 1.00 25.17 C
ANISOU 672 C SER A 90 3139 3480 2944 -95 147 173 C
ATOM 673 O SER A 90 15.879 -11.660 23.269 1.00 27.03 O
ANISOU 673 O SER A 90 3397 3688 3186 -92 143 191 O
ATOM 674 CB SER A 90 13.441 -9.501 23.665 1.00 20.94 C
ANISOU 674 CB SER A 90 2566 2991 2398 -123 163 188 C
ATOM 675 OG SER A 90 12.866 -10.794 23.610 1.00 28.74 O
ANISOU 675 OG SER A 90 3564 3953 3401 -151 166 214 O
ATOM 676 N LYS A 91 16.045 -9.923 21.848 1.00 21.14 N
ANISOU 676 N LYS A 91 2627 2966 2440 -96 144 145 N
ATOM 677 CA LYS A 91 16.777 -10.718 20.868 1.00 23.36 C
ANISOU 677 CA LYS A 91 2926 3218 2731 -90 144 129 C
ATOM 678 C LYS A 91 18.168 -11.076 21.378 1.00 24.41 C
ANISOU 678 C LYS A 91 3055 3353 2868 -56 143 124 C
ATOM 679 O LYS A 91 18.659 -12.183 21.128 1.00 25.83 O
ANISOU 679 O LYS A 91 3252 3502 3059 -37 140 120 O
ATOM 680 CB LYS A 91 16.861 -9.969 19.539 1.00 22.73 C
ANISOU 680 CB LYS A 91 2848 3144 2644 -100 148 105 C
ATOM 681 CG LYS A 91 15.506 -9.552 18.991 1.00 25.35 C
ANISOU 681 CG LYS A 91 3182 3478 2972 -125 137 109 C
ATOM 682 CD LYS A 91 15.493 -9.501 17.472 1.00 31.64 C
ANISOU 682 CD LYS A 91 4002 4264 3754 -134 133 89 C
ATOM 683 CE LYS A 91 16.617 -8.640 16.930 1.00 36.96 C
ANISOU 683 CE LYS A 91 4677 4953 4413 -124 152 78 C
ATOM 684 NZ LYS A 91 16.563 -8.534 15.445 1.00 37.99 N
ANISOU 684 NZ LYS A 91 4838 5080 4515 -133 153 64 N
ATOM 685 N ILE A 92 18.813 -10.155 22.096 1.00 25.38 N
ANISOU 685 N ILE A 92 3153 3508 2984 -43 141 120 N
ATOM 686 CA ILE A 92 20.112 -10.446 22.698 1.00 23.94 C
ANISOU 686 CA ILE A 92 2956 3335 2808 -9 131 114 C
ATOM 687 C ILE A 92 19.999 -11.625 23.657 1.00 28.25 C
ANISOU 687 C ILE A 92 3525 3859 3349 12 115 144 C
ATOM 688 O ILE A 92 20.825 -12.545 23.642 1.00 25.23 O
ANISOU 688 O ILE A 92 3148 3456 2981 46 104 142 O
ATOM 689 CB ILE A 92 20.665 -9.194 23.403 1.00 27.37 C
ANISOU 689 CB ILE A 92 3360 3806 3235 -9 122 103 C
ATOM 690 CG1 ILE A 92 21.208 -8.201 22.376 1.00 25.20 C
ANISOU 690 CG1 ILE A 92 3063 3541 2972 -29 138 78 C
ATOM 691 CG2 ILE A 92 21.747 -9.573 24.398 1.00 24.88 C
ANISOU 691 CG2 ILE A 92 3028 3506 2920 27 96 103 C
ATOM 692 CD1 ILE A 92 22.455 -8.687 21.681 1.00 37.85 C
ANISOU 692 CD1 ILE A 92 4641 5148 4594 -13 150 59 C
ATOM 693 N PHE A 93 18.963 -11.618 24.500 1.00 24.66 N
ANISOU 693 N PHE A 93 3086 3409 2875 -5 115 174 N
ATOM 694 CA PHE A 93 18.749 -12.731 25.420 1.00 29.18 C
ANISOU 694 CA PHE A 93 3690 3960 3438 6 106 214 C
ATOM 695 C PHE A 93 18.464 -14.025 24.668 1.00 27.99 C
ANISOU 695 C PHE A 93 3572 3750 3315 -2 106 223 C
ATOM 696 O PHE A 93 18.969 -15.091 25.041 1.00 28.26 O
ANISOU 696 O PHE A 93 3634 3746 3356 26 89 243 O
ATOM 697 CB PHE A 93 17.607 -12.405 26.383 1.00 28.20 C
ANISOU 697 CB PHE A 93 3571 3861 3283 -18 119 245 C
ATOM 698 CG PHE A 93 17.993 -11.462 27.486 1.00 31.62 C
ANISOU 698 CG PHE A 93 3991 4343 3679 4 110 239 C
ATOM 699 CD1 PHE A 93 19.193 -11.615 28.162 1.00 32.40 C
ANISOU 699 CD1 PHE A 93 4092 4451 3766 44 80 237 C
ATOM 700 CD2 PHE A 93 17.152 -10.422 27.850 1.00 25.03 C
ANISOU 700 CD2 PHE A 93 3142 3546 2822 -12 128 230 C
ATOM 701 CE1 PHE A 93 19.545 -10.749 29.182 1.00 38.06 C
ANISOU 701 CE1 PHE A 93 4801 5214 4446 61 63 224 C
ATOM 702 CE2 PHE A 93 17.501 -9.553 28.868 1.00 27.70 C
ANISOU 702 CE2 PHE A 93 3476 3925 3124 10 116 215 C
ATOM 703 CZ PHE A 93 18.699 -9.717 29.534 1.00 35.00 C
ANISOU 703 CZ PHE A 93 4407 4859 4033 43 82 211 C
ATOM 704 N SER A 94 17.656 -13.959 23.608 1.00 25.09 N
ANISOU 704 N SER A 94 3204 3368 2962 -38 119 207 N
ATOM 705 CA SER A 94 17.377 -15.161 22.828 1.00 26.39 C
ANISOU 705 CA SER A 94 3403 3472 3151 -49 113 205 C
ATOM 706 C SER A 94 18.645 -15.692 22.171 1.00 28.79 C
ANISOU 706 C SER A 94 3716 3752 3471 -2 104 171 C
ATOM 707 O SER A 94 18.898 -16.902 22.173 1.00 27.76 O
ANISOU 707 O SER A 94 3623 3564 3360 18 90 177 O
ATOM 708 CB SER A 94 16.304 -14.878 21.777 1.00 27.17 C
ANISOU 708 CB SER A 94 3496 3570 3258 -94 119 186 C
ATOM 709 OG SER A 94 15.041 -14.658 22.379 1.00 31.63 O
ANISOU 709 OG SER A 94 4047 4153 3819 -135 127 218 O
ATOM 710 N LEU A 95 19.464 -14.798 21.613 1.00 26.78 N
ANISOU 710 N LEU A 95 3426 3539 3211 16 115 135 N
ATOM 711 CA LEU A 95 20.688 -15.239 20.956 1.00 27.05 C
ANISOU 711 CA LEU A 95 3455 3563 3260 62 118 99 C
ATOM 712 C LEU A 95 21.658 -15.860 21.951 1.00 29.61 C
ANISOU 712 C LEU A 95 3777 3879 3596 116 95 114 C
ATOM 713 O LEU A 95 22.307 -16.868 21.648 1.00 29.11 O
ANISOU 713 O LEU A 95 3732 3776 3555 161 86 98 O
ATOM 714 CB LEU A 95 21.343 -14.069 20.224 1.00 29.44 C
ANISOU 714 CB LEU A 95 3715 3919 3553 60 142 66 C
ATOM 715 CG LEU A 95 20.608 -13.568 18.983 1.00 28.19 C
ANISOU 715 CG LEU A 95 3568 3764 3378 21 160 48 C
ATOM 716 CD1 LEU A 95 21.258 -12.291 18.499 1.00 27.48 C
ANISOU 716 CD1 LEU A 95 3441 3725 3276 12 184 33 C
ATOM 717 CD2 LEU A 95 20.608 -14.624 17.888 1.00 25.87 C
ANISOU 717 CD2 LEU A 95 3313 3430 3088 34 163 17 C
ATOM 718 N LEU A 96 21.770 -15.276 23.147 1.00 28.68 N
ANISOU 718 N LEU A 96 3639 3797 3462 118 81 142 N
ATOM 719 CA LEU A 96 22.662 -15.832 24.160 1.00 28.96 C
ANISOU 719 CA LEU A 96 3674 3828 3500 172 49 160 C
ATOM 720 C LEU A 96 22.178 -17.197 24.635 1.00 31.95 C
ANISOU 720 C LEU A 96 4118 4137 3884 182 30 202 C
ATOM 721 O LEU A 96 22.989 -18.091 24.906 1.00 25.64 O
ANISOU 721 O LEU A 96 3336 3304 3103 241 2 206 O
ATOM 722 CB LEU A 96 22.782 -14.864 25.338 1.00 33.11 C
ANISOU 722 CB LEU A 96 4174 4410 3996 167 35 177 C
ATOM 723 CG LEU A 96 23.692 -15.284 26.495 1.00 34.35 C
ANISOU 723 CG LEU A 96 4331 4576 4145 223 -9 197 C
ATOM 724 CD1 LEU A 96 25.115 -15.515 26.005 1.00 31.77 C
ANISOU 724 CD1 LEU A 96 3956 4258 3856 279 -24 156 C
ATOM 725 CD2 LEU A 96 23.667 -14.245 27.607 1.00 29.44 C
ANISOU 725 CD2 LEU A 96 3692 4012 3484 212 -25 206 C
ATOM 726 N ALA A 97 20.860 -17.379 24.737 1.00 29.20 N
ANISOU 726 N ALA A 97 3806 3765 3526 126 43 235 N
ATOM 727 CA ALA A 97 20.326 -18.663 25.180 1.00 31.41 C
ANISOU 727 CA ALA A 97 4149 3972 3815 120 28 282 C
ATOM 728 C ALA A 97 20.534 -19.745 24.126 1.00 30.70 C
ANISOU 728 C ALA A 97 4093 3805 3766 139 20 251 C
ATOM 729 O ALA A 97 20.768 -20.912 24.464 1.00 28.64 O
ANISOU 729 O ALA A 97 3886 3473 3524 170 -6 277 O
ATOM 730 CB ALA A 97 18.845 -18.522 25.522 1.00 28.72 C
ANISOU 730 CB ALA A 97 3822 3633 3457 46 51 322 C
ATOM 731 N ILE A 98 20.450 -19.377 22.846 1.00 29.71 N
ANISOU 731 N ILE A 98 3947 3692 3651 123 41 196 N
ATOM 732 CA ILE A 98 20.674 -20.347 21.776 1.00 26.72 C
ANISOU 732 CA ILE A 98 3604 3247 3303 146 34 154 C
ATOM 733 C ILE A 98 22.104 -20.867 21.821 1.00 27.17 C
ANISOU 733 C ILE A 98 3655 3291 3378 236 18 128 C
ATOM 734 O ILE A 98 22.348 -22.073 21.691 1.00 29.79 O
ANISOU 734 O ILE A 98 4039 3541 3739 276 -5 123 O
ATOM 735 CB ILE A 98 20.340 -19.721 20.410 1.00 25.71 C
ANISOU 735 CB ILE A 98 3455 3148 3165 115 60 100 C
ATOM 736 CG1 ILE A 98 18.830 -19.522 20.265 1.00 24.97 C
ANISOU 736 CG1 ILE A 98 3374 3049 3066 33 63 121 C
ATOM 737 CG2 ILE A 98 20.876 -20.583 19.282 1.00 24.38 C
ANISOU 737 CG2 ILE A 98 3318 2929 3015 156 58 41 C
ATOM 738 CD1 ILE A 98 18.428 -18.783 19.002 1.00 21.49 C
ANISOU 738 CD1 ILE A 98 2914 2643 2606 4 79 76 C
ATOM 739 N ALA A 99 23.072 -19.967 22.010 1.00 24.57 N
ANISOU 739 N ALA A 99 3259 3039 3037 271 27 110 N
ATOM 740 CA ALA A 99 24.467 -20.386 22.103 1.00 29.67 C
ANISOU 740 CA ALA A 99 3880 3687 3706 359 10 84 C
ATOM 741 C ALA A 99 24.694 -21.285 23.311 1.00 30.48 C
ANISOU 741 C ALA A 99 4024 3738 3818 404 -38 137 C
ATOM 742 O ALA A 99 25.421 -22.281 23.226 1.00 31.06 O
ANISOU 742 O ALA A 99 4121 3757 3923 478 -64 122 O
ATOM 743 CB ALA A 99 25.379 -19.163 22.172 1.00 26.00 C
ANISOU 743 CB ALA A 99 3326 3320 3231 370 26 60 C
ATOM 744 N ILE A 100 24.084 -20.943 24.448 1.00 24.01 N
ANISOU 744 N ILE A 100 3219 2935 2968 364 -51 199 N
ATOM 745 CA ILE A 100 24.221 -21.766 25.645 1.00 32.77 C
ANISOU 745 CA ILE A 100 4380 3999 4073 401 -96 261 C
ATOM 746 C ILE A 100 23.551 -23.120 25.441 1.00 29.93 C
ANISOU 746 C ILE A 100 4110 3522 3739 390 -107 288 C
ATOM 747 O ILE A 100 24.089 -24.160 25.841 1.00 32.76 O
ANISOU 747 O ILE A 100 4518 3811 4119 454 -148 311 O
ATOM 748 CB ILE A 100 23.651 -21.020 26.867 1.00 32.07 C
ANISOU 748 CB ILE A 100 4290 3965 3932 356 -97 318 C
ATOM 749 CG1 ILE A 100 24.507 -19.790 27.183 1.00 36.48 C
ANISOU 749 CG1 ILE A 100 4766 4623 4471 378 -102 286 C
ATOM 750 CG2 ILE A 100 23.564 -21.944 28.074 1.00 30.32 C
ANISOU 750 CG2 ILE A 100 4139 3689 3691 381 -137 395 C
ATOM 751 CD1 ILE A 100 23.963 -18.925 28.299 1.00 42.98 C
ANISOU 751 CD1 ILE A 100 5587 5504 5238 338 -102 325 C
ATOM 752 N ASP A 101 22.379 -23.131 24.802 1.00 31.44 N
ANISOU 752 N ASP A 101 4325 3688 3933 309 -77 286 N
ATOM 753 CA ASP A 101 21.694 -24.391 24.532 1.00 27.01 C
ANISOU 753 CA ASP A 101 3847 3012 3404 284 -90 306 C
ATOM 754 C ASP A 101 22.544 -25.311 23.662 1.00 29.66 C
ANISOU 754 C ASP A 101 4209 3276 3784 362 -111 246 C
ATOM 755 O ASP A 101 22.605 -26.522 23.902 1.00 26.91 O
ANISOU 755 O ASP A 101 3938 2821 3467 392 -146 272 O
ATOM 756 CB ASP A 101 20.348 -24.121 23.865 1.00 30.88 C
ANISOU 756 CB ASP A 101 4339 3502 3894 184 -58 299 C
ATOM 757 CG ASP A 101 19.697 -25.381 23.353 1.00 34.66 C
ANISOU 757 CG ASP A 101 4894 3860 4414 151 -75 300 C
ATOM 758 OD1 ASP A 101 19.047 -26.081 24.156 1.00 35.53 O
ANISOU 758 OD1 ASP A 101 5060 3908 4531 109 -87 373 O
ATOM 759 OD2 ASP A 101 19.841 -25.678 22.148 1.00 31.15 O
ANISOU 759 OD2 ASP A 101 4459 3384 3994 166 -77 228 O
ATOM 760 N ARG A 102 23.210 -24.755 22.648 1.00 31.25 N
ANISOU 760 N ARG A 102 4352 3534 3988 396 -87 167 N
ATOM 761 CA ARG A 102 24.024 -25.587 21.767 1.00 27.29 C
ANISOU 761 CA ARG A 102 3869 2975 3523 477 -98 100 C
ATOM 762 C ARG A 102 25.304 -26.045 22.453 1.00 28.96 C
ANISOU 762 C ARG A 102 4069 3179 3756 588 -135 106 C
ATOM 763 O ARG A 102 25.791 -27.151 22.189 1.00 29.00 O
ANISOU 763 O ARG A 102 4124 3094 3799 662 -163 81 O
ATOM 764 CB ARG A 102 24.345 -24.834 20.477 1.00 27.51 C
ANISOU 764 CB ARG A 102 3837 3077 3539 478 -52 17 C
ATOM 765 CG ARG A 102 23.146 -24.613 19.565 1.00 27.97 C
ANISOU 765 CG ARG A 102 3921 3127 3581 387 -28 -3 C
ATOM 766 CD ARG A 102 22.546 -25.932 19.096 1.00 28.94 C
ANISOU 766 CD ARG A 102 4137 3123 3736 378 -57 -19 C
ATOM 767 NE ARG A 102 21.586 -26.481 20.048 1.00 33.28 N
ANISOU 767 NE ARG A 102 4743 3602 4301 315 -86 62 N
ATOM 768 CZ ARG A 102 21.274 -27.767 20.137 1.00 32.76 C
ANISOU 768 CZ ARG A 102 4765 3408 4276 315 -122 76 C
ATOM 769 NH1 ARG A 102 21.842 -28.671 19.357 1.00 30.74 N
ANISOU 769 NH1 ARG A 102 4557 3074 4050 383 -141 9 N
ATOM 770 NH2 ARG A 102 20.375 -28.156 21.037 1.00 27.72 N
ANISOU 770 NH2 ARG A 102 4170 2717 3647 244 -138 159 N
ATOM 771 N TYR A 103 25.868 -25.211 23.329 1.00 32.11 N
ANISOU 771 N TYR A 103 4404 3668 4131 604 -141 136 N
ATOM 772 CA TYR A 103 27.046 -25.629 24.080 1.00 29.63 C
ANISOU 772 CA TYR A 103 4073 3350 3834 709 -188 147 C
ATOM 773 C TYR A 103 26.712 -26.777 25.021 1.00 33.62 C
ANISOU 773 C TYR A 103 4681 3744 4348 728 -243 224 C
ATOM 774 O TYR A 103 27.526 -27.687 25.217 1.00 36.70 O
ANISOU 774 O TYR A 103 5100 4072 4773 828 -289 221 O
ATOM 775 CB TYR A 103 27.624 -24.446 24.855 1.00 33.73 C
ANISOU 775 CB TYR A 103 4504 3990 4323 710 -192 161 C
ATOM 776 CG TYR A 103 28.834 -24.799 25.692 1.00 39.02 C
ANISOU 776 CG TYR A 103 5147 4669 5008 817 -252 173 C
ATOM 777 CD1 TYR A 103 30.069 -25.032 25.099 1.00 34.00 C
ANISOU 777 CD1 TYR A 103 4447 4055 4417 914 -257 104 C
ATOM 778 CD2 TYR A 103 28.743 -24.896 27.074 1.00 42.33 C
ANISOU 778 CD2 TYR A 103 5605 5084 5395 823 -303 251 C
ATOM 779 CE1 TYR A 103 31.177 -25.357 25.859 1.00 46.59 C
ANISOU 779 CE1 TYR A 103 6007 5662 6032 1017 -319 112 C
ATOM 780 CE2 TYR A 103 29.846 -25.219 27.842 1.00 48.27 C
ANISOU 780 CE2 TYR A 103 6334 5847 6158 924 -369 263 C
ATOM 781 CZ TYR A 103 31.061 -25.448 27.230 1.00 51.78 C
ANISOU 781 CZ TYR A 103 6707 6312 6656 1023 -381 192 C
ATOM 782 OH TYR A 103 32.161 -25.769 27.993 1.00 53.78 O
ANISOU 782 OH TYR A 103 6929 6580 6926 1130 -454 201 O
ATOM 783 N ILE A 104 25.515 -26.753 25.610 1.00 30.39 N
ANISOU 783 N ILE A 104 4328 3310 3909 633 -236 296 N
ATOM 784 CA ILE A 104 25.090 -27.847 26.476 1.00 34.44 C
ANISOU 784 CA ILE A 104 4947 3714 4427 633 -278 380 C
ATOM 785 C ILE A 104 24.877 -29.117 25.663 1.00 36.65 C
ANISOU 785 C ILE A 104 5309 3854 4763 648 -291 353 C
ATOM 786 O ILE A 104 25.204 -30.222 26.113 1.00 33.99 O
ANISOU 786 O ILE A 104 5052 3408 4454 710 -342 391 O
ATOM 787 CB ILE A 104 23.821 -27.446 27.249 1.00 35.45 C
ANISOU 787 CB ILE A 104 5102 3861 4506 518 -252 460 C
ATOM 788 CG1 ILE A 104 24.139 -26.346 28.263 1.00 31.10 C
ANISOU 788 CG1 ILE A 104 4490 3433 3895 523 -252 490 C
ATOM 789 CG2 ILE A 104 23.201 -28.654 27.938 1.00 29.49 C
ANISOU 789 CG2 ILE A 104 4464 2982 3760 494 -280 550 C
ATOM 790 CD1 ILE A 104 22.926 -25.848 29.011 1.00 34.90 C
ANISOU 790 CD1 ILE A 104 4988 3950 4323 420 -218 558 C
ATOM 791 N ALA A 105 24.340 -28.980 24.449 1.00 33.09 N
ANISOU 791 N ALA A 105 4846 3399 4328 596 -251 285 N
ATOM 792 CA ALA A 105 24.065 -30.154 23.628 1.00 31.80 C
ANISOU 792 CA ALA A 105 4766 3102 4216 603 -267 248 C
ATOM 793 C ALA A 105 25.343 -30.850 23.180 1.00 36.36 C
ANISOU 793 C ALA A 105 5348 3633 4834 743 -298 182 C
ATOM 794 O ALA A 105 25.344 -32.071 22.989 1.00 46.17 O
ANISOU 794 O ALA A 105 6684 4737 6123 782 -336 176 O
ATOM 795 CB ALA A 105 23.224 -29.763 22.413 1.00 31.57 C
ANISOU 795 CB ALA A 105 4719 3093 4184 519 -223 184 C
ATOM 796 N ILE A 106 26.436 -30.106 23.008 1.00 34.68 N
ANISOU 796 N ILE A 106 5034 3533 4611 820 -283 130 N
ATOM 797 CA ILE A 106 27.679 -30.714 22.548 1.00 41.50 C
ANISOU 797 CA ILE A 106 5882 4369 5516 958 -304 59 C
ATOM 798 C ILE A 106 28.615 -31.082 23.696 1.00 41.37 C
ANISOU 798 C ILE A 106 5864 4342 5513 1061 -366 112 C
ATOM 799 O ILE A 106 29.476 -31.959 23.527 1.00 33.51 O
ANISOU 799 O ILE A 106 4889 3277 4564 1183 -404 74 O
ATOM 800 CB ILE A 106 28.391 -29.784 21.547 1.00 37.97 C
ANISOU 800 CB ILE A 106 5319 4050 5056 985 -246 -37 C
ATOM 801 CG1 ILE A 106 29.396 -30.569 20.704 1.00 40.04 C
ANISOU 801 CG1 ILE A 106 5579 4272 5364 1113 -249 -130 C
ATOM 802 CG2 ILE A 106 29.079 -28.636 22.268 1.00 33.97 C
ANISOU 802 CG2 ILE A 106 4701 3685 4523 994 -239 -12 C
ATOM 803 CD1 ILE A 106 29.974 -29.772 19.564 1.00 40.86 C
ANISOU 803 CD1 ILE A 106 5582 4492 5450 1128 -179 -225 C
ATOM 804 N ARG A 107 28.460 -30.457 24.863 1.00 41.93 N
ANISOU 804 N ARG A 107 5914 4476 5542 1020 -382 196 N
ATOM 805 CA ARG A 107 29.320 -30.772 25.997 1.00 42.97 C
ANISOU 805 CA ARG A 107 6048 4603 5675 1117 -450 249 C
ATOM 806 C ARG A 107 28.807 -31.985 26.764 1.00 42.60 C
ANISOU 806 C ARG A 107 6144 4404 5639 1120 -507 341 C
ATOM 807 O ARG A 107 29.594 -32.851 27.162 1.00 44.12 O
ANISOU 807 O ARG A 107 6377 4520 5864 1238 -573 356 O
ATOM 808 CB ARG A 107 29.423 -29.557 26.920 1.00 44.83 C
ANISOU 808 CB ARG A 107 6205 4977 5853 1076 -447 293 C
ATOM 809 CG ARG A 107 30.508 -29.640 27.975 1.00 57.82 C
ANISOU 809 CG ARG A 107 7821 6654 7493 1183 -521 326 C
ATOM 810 CD ARG A 107 31.889 -29.481 27.363 1.00 67.69 C
ANISOU 810 CD ARG A 107 8957 7970 8791 1298 -528 231 C
ATOM 811 NE ARG A 107 32.885 -29.113 28.363 1.00 83.05 N
ANISOU 811 NE ARG A 107 10835 9997 10725 1374 -592 253 N
ATOM 812 CZ ARG A 107 34.172 -28.926 28.105 1.00 92.30 C
ANISOU 812 CZ ARG A 107 11890 11240 11938 1476 -611 183 C
ATOM 813 NH1 ARG A 107 34.662 -29.078 26.885 1.00 91.81 N
ANISOU 813 NH1 ARG A 107 11768 11185 11929 1522 -562 88 N
ATOM 814 NH2 ARG A 107 34.988 -28.577 29.097 1.00 95.00 N
ANISOU 814 NH2 ARG A 107 12172 11657 12267 1535 -680 208 N
ATOM 815 N ILE A 108 27.496 -32.069 26.970 1.00 42.90 N
ANISOU 815 N ILE A 108 6256 4392 5651 993 -482 406 N
ATOM 816 CA ILE A 108 26.888 -33.170 27.714 1.00 38.47 C
ANISOU 816 CA ILE A 108 5833 3687 5099 970 -526 505 C
ATOM 817 C ILE A 108 25.620 -33.636 27.003 1.00 43.40 C
ANISOU 817 C ILE A 108 6528 4216 5746 852 -488 503 C
ATOM 818 O ILE A 108 24.512 -33.444 27.525 1.00 40.23 O
ANISOU 818 O ILE A 108 6159 3817 5311 730 -461 580 O
ATOM 819 CB ILE A 108 26.591 -32.757 29.166 1.00 46.48 C
ANISOU 819 CB ILE A 108 6864 4754 6041 928 -541 622 C
ATOM 820 CG1 ILE A 108 25.995 -31.346 29.218 1.00 32.86 C
ANISOU 820 CG1 ILE A 108 5045 3182 4257 825 -475 613 C
ATOM 821 CG2 ILE A 108 27.855 -32.830 30.010 1.00 46.31 C
ANISOU 821 CG2 ILE A 108 6822 4764 6008 1064 -613 642 C
ATOM 822 CD1 ILE A 108 25.497 -30.948 30.590 1.00 55.30 C
ANISOU 822 CD1 ILE A 108 7914 6075 7022 770 -478 721 C
ATOM 823 N PRO A 109 25.730 -34.267 25.830 1.00 43.22 N
ANISOU 823 N PRO A 109 6529 4110 5781 884 -487 413 N
ATOM 824 CA PRO A 109 24.516 -34.680 25.104 1.00 41.22 C
ANISOU 824 CA PRO A 109 6338 3771 5552 767 -461 400 C
ATOM 825 C PRO A 109 23.692 -35.727 25.833 1.00 46.49 C
ANISOU 825 C PRO A 109 7139 4286 6240 700 -494 507 C
ATOM 826 O PRO A 109 22.485 -35.827 25.583 1.00 45.54 O
ANISOU 826 O PRO A 109 7050 4127 6126 566 -466 528 O
ATOM 827 CB PRO A 109 25.068 -35.224 23.779 1.00 40.25 C
ANISOU 827 CB PRO A 109 6223 3589 5482 848 -466 274 C
ATOM 828 CG PRO A 109 26.469 -35.631 24.094 1.00 36.04 C
ANISOU 828 CG PRO A 109 5679 3041 4972 1015 -514 255 C
ATOM 829 CD PRO A 109 26.962 -34.657 25.122 1.00 35.48 C
ANISOU 829 CD PRO A 109 5521 3113 4848 1032 -512 314 C
ATOM 830 N LEU A 110 24.302 -36.510 26.724 1.00 47.25 N
ANISOU 830 N LEU A 110 7310 4294 6347 786 -555 578 N
ATOM 831 CA LEU A 110 23.543 -37.506 27.472 1.00 53.17 C
ANISOU 831 CA LEU A 110 8196 4894 7113 717 -585 695 C
ATOM 832 C LEU A 110 22.598 -36.856 28.473 1.00 52.40 C
ANISOU 832 C LEU A 110 8083 4881 6946 588 -542 807 C
ATOM 833 O LEU A 110 21.504 -37.377 28.720 1.00 47.32 O
ANISOU 833 O LEU A 110 7516 4150 6314 466 -527 882 O
ATOM 834 CB LEU A 110 24.498 -38.462 28.188 1.00 54.81 C
ANISOU 834 CB LEU A 110 8493 4990 7344 853 -666 748 C
ATOM 835 CG LEU A 110 25.491 -39.241 27.322 1.00 56.92 C
ANISOU 835 CG LEU A 110 8785 5159 7684 1002 -715 641 C
ATOM 836 CD1 LEU A 110 26.524 -39.937 28.195 1.00 55.13 C
ANISOU 836 CD1 LEU A 110 8620 4859 7469 1152 -798 700 C
ATOM 837 CD2 LEU A 110 24.770 -40.248 26.440 1.00 45.12 C
ANISOU 837 CD2 LEU A 110 7393 3489 6260 942 -721 600 C
ATOM 838 N ARG A 111 22.995 -35.724 29.051 1.00 50.52 N
ANISOU 838 N ARG A 111 7747 4811 6638 612 -520 816 N
ATOM 839 CA ARG A 111 22.206 -35.026 30.056 1.00 50.12 C
ANISOU 839 CA ARG A 111 7678 4855 6512 510 -478 913 C
ATOM 840 C ARG A 111 21.405 -33.864 29.480 1.00 50.20 C
ANISOU 840 C ARG A 111 7579 4998 6498 406 -402 857 C
ATOM 841 O ARG A 111 20.816 -33.094 30.245 1.00 47.56 O
ANISOU 841 O ARG A 111 7208 4766 6098 335 -361 917 O
ATOM 842 CB ARG A 111 23.119 -34.521 31.177 1.00 45.66 C
ANISOU 842 CB ARG A 111 7085 4385 5879 604 -510 961 C
ATOM 843 CG ARG A 111 23.573 -35.598 32.151 1.00 57.52 C
ANISOU 843 CG ARG A 111 8712 5766 7376 676 -582 1065 C
ATOM 844 CD ARG A 111 24.672 -35.088 33.076 1.00 59.99 C
ANISOU 844 CD ARG A 111 8985 6180 7628 793 -632 1085 C
ATOM 845 NE ARG A 111 25.998 -35.273 32.497 1.00 78.30 N
ANISOU 845 NE ARG A 111 11258 8491 10002 946 -690 991 N
ATOM 846 CZ ARG A 111 27.130 -34.876 33.063 1.00 79.25 C
ANISOU 846 CZ ARG A 111 11322 8697 10093 1065 -744 981 C
ATOM 847 NH1 ARG A 111 27.137 -34.234 34.220 1.00 76.38 N
ANISOU 847 NH1 ARG A 111 10948 8435 9638 1051 -753 1053 N
ATOM 848 NH2 ARG A 111 28.285 -35.130 32.453 1.00 75.00 N
ANISOU 848 NH2 ARG A 111 10734 8145 9616 1201 -790 891 N
ATOM 849 N TYR A 112 21.358 -33.725 28.152 1.00 45.00 N
ANISOU 849 N TYR A 112 6873 4339 5887 401 -385 744 N
ATOM 850 CA TYR A 112 20.726 -32.550 27.557 1.00 42.46 C
ANISOU 850 CA TYR A 112 6446 4148 5540 321 -322 688 C
ATOM 851 C TYR A 112 19.214 -32.569 27.749 1.00 41.61 C
ANISOU 851 C TYR A 112 6357 4026 5427 166 -280 750 C
ATOM 852 O TYR A 112 18.632 -31.602 28.255 1.00 40.42 O
ANISOU 852 O TYR A 112 6141 3995 5222 102 -233 782 O
ATOM 853 CB TYR A 112 21.077 -32.455 26.071 1.00 38.20 C
ANISOU 853 CB TYR A 112 5863 3609 5043 358 -318 557 C
ATOM 854 CG TYR A 112 20.371 -31.318 25.367 1.00 34.73 C
ANISOU 854 CG TYR A 112 5329 3288 4579 275 -261 503 C
ATOM 855 CD1 TYR A 112 20.870 -30.024 25.425 1.00 29.70 C
ANISOU 855 CD1 TYR A 112 4588 2803 3894 305 -232 471 C
ATOM 856 CD2 TYR A 112 19.198 -31.537 24.653 1.00 37.84 C
ANISOU 856 CD2 TYR A 112 5740 3637 5000 165 -242 485 C
ATOM 857 CE1 TYR A 112 20.224 -28.981 24.791 1.00 32.92 C
ANISOU 857 CE1 TYR A 112 4919 3310 4281 234 -185 427 C
ATOM 858 CE2 TYR A 112 18.545 -30.501 24.018 1.00 34.43 C
ANISOU 858 CE2 TYR A 112 5225 3313 4546 98 -199 439 C
ATOM 859 CZ TYR A 112 19.062 -29.226 24.088 1.00 37.07 C
ANISOU 859 CZ TYR A 112 5464 3791 4830 135 -170 413 C
ATOM 860 OH TYR A 112 18.413 -28.193 23.453 1.00 34.25 O
ANISOU 860 OH TYR A 112 5032 3530 4451 73 -131 372 O
ATOM 861 N ASN A 113 18.558 -33.659 27.343 1.00 41.56 N
ANISOU 861 N ASN A 113 6435 3875 5482 104 -296 763 N
ATOM 862 CA ASN A 113 17.099 -33.703 27.384 1.00 46.67 C
ANISOU 862 CA ASN A 113 7085 4511 6138 -50 -256 811 C
ATOM 863 C ASN A 113 16.562 -33.620 28.808 1.00 44.68 C
ANISOU 863 C ASN A 113 6854 4292 5830 -112 -226 945 C
ATOM 864 O ASN A 113 15.440 -33.145 29.016 1.00 44.85 O
ANISOU 864 O ASN A 113 6829 4380 5834 -228 -172 980 O
ATOM 865 CB ASN A 113 16.593 -34.969 26.692 1.00 47.60 C
ANISOU 865 CB ASN A 113 7294 4453 6338 -105 -290 797 C
ATOM 866 CG ASN A 113 16.862 -34.958 25.200 1.00 50.23 C
ANISOU 866 CG ASN A 113 7601 4770 6713 -67 -308 656 C
ATOM 867 OD1 ASN A 113 16.784 -33.914 24.551 1.00 46.55 O
ANISOU 867 OD1 ASN A 113 7035 4432 6218 -70 -275 583 O
ATOM 868 ND2 ASN A 113 17.189 -36.121 24.647 1.00 61.85 N
ANISOU 868 ND2 ASN A 113 9169 6081 8249 -26 -361 618 N
ATOM 869 N GLY A 114 17.338 -34.067 29.797 1.00 44.18 N
ANISOU 869 N GLY A 114 6860 4188 5736 -32 -261 1020 N
ATOM 870 CA GLY A 114 16.920 -33.920 31.180 1.00 49.07 C
ANISOU 870 CA GLY A 114 7505 4854 6284 -79 -231 1146 C
ATOM 871 C GLY A 114 17.205 -32.559 31.774 1.00 51.25 C
ANISOU 871 C GLY A 114 7686 5315 6473 -43 -198 1136 C
ATOM 872 O GLY A 114 16.564 -32.176 32.758 1.00 51.67 O
ANISOU 872 O GLY A 114 7734 5440 6458 -106 -152 1219 O
ATOM 873 N LEU A 115 18.148 -31.820 31.196 1.00 43.74 N
ANISOU 873 N LEU A 115 6658 4440 5519 55 -218 1034 N
ATOM 874 CA LEU A 115 18.504 -30.497 31.689 1.00 41.83 C
ANISOU 874 CA LEU A 115 6326 4364 5203 90 -196 1013 C
ATOM 875 C LEU A 115 17.729 -29.396 30.972 1.00 46.48 C
ANISOU 875 C LEU A 115 6808 5060 5792 16 -136 942 C
ATOM 876 O LEU A 115 17.166 -28.506 31.618 1.00 41.85 O
ANISOU 876 O LEU A 115 6173 4584 5144 -31 -89 971 O
ATOM 877 CB LEU A 115 20.011 -30.278 31.535 1.00 46.15 C
ANISOU 877 CB LEU A 115 6844 4937 5751 233 -252 948 C
ATOM 878 CG LEU A 115 20.526 -28.854 31.736 1.00 55.97 C
ANISOU 878 CG LEU A 115 7983 6344 6940 272 -237 896 C
ATOM 879 CD1 LEU A 115 20.222 -28.372 33.141 1.00 55.92 C
ANISOU 879 CD1 LEU A 115 7989 6417 6840 248 -221 982 C
ATOM 880 CD2 LEU A 115 22.016 -28.784 31.453 1.00 57.02 C
ANISOU 880 CD2 LEU A 115 8080 6491 7094 403 -294 828 C
ATOM 881 N VAL A 116 17.679 -29.451 29.646 1.00 42.11 N
ANISOU 881 N VAL A 116 6223 4474 5303 9 -139 851 N
ATOM 882 CA VAL A 116 17.082 -28.404 28.826 1.00 37.84 C
ANISOU 882 CA VAL A 116 5585 4030 4764 -44 -96 777 C
ATOM 883 C VAL A 116 15.735 -28.924 28.339 1.00 43.03 C
ANISOU 883 C VAL A 116 6258 4625 5466 -165 -71 792 C
ATOM 884 O VAL A 116 15.659 -29.670 27.355 1.00 49.04 O
ANISOU 884 O VAL A 116 7053 5288 6291 -177 -97 744 O
ATOM 885 CB VAL A 116 17.995 -28.008 27.660 1.00 42.88 C
ANISOU 885 CB VAL A 116 6173 4690 5430 34 -116 663 C
ATOM 886 CG1 VAL A 116 17.476 -26.760 26.981 1.00 38.14 C
ANISOU 886 CG1 VAL A 116 5477 4202 4814 -11 -74 601 C
ATOM 887 CG2 VAL A 116 19.417 -27.793 28.154 1.00 39.84 C
ANISOU 887 CG2 VAL A 116 5778 4341 5019 155 -151 653 C
ATOM 888 N THR A 117 14.664 -28.529 29.021 1.00 39.14 N
ANISOU 888 N THR A 117 5737 4192 4940 -256 -20 855 N
ATOM 889 CA THR A 117 13.311 -28.954 28.695 1.00 39.61 C
ANISOU 889 CA THR A 117 5794 4211 5044 -382 8 878 C
ATOM 890 C THR A 117 12.504 -27.778 28.158 1.00 40.84 C
ANISOU 890 C THR A 117 5838 4487 5191 -432 49 821 C
ATOM 891 O THR A 117 12.898 -26.615 28.280 1.00 35.61 O
ANISOU 891 O THR A 117 5112 3940 4479 -378 65 785 O
ATOM 892 CB THR A 117 12.611 -29.551 29.923 1.00 48.96 C
ANISOU 892 CB THR A 117 7031 5366 6205 -457 40 1004 C
ATOM 893 OG1 THR A 117 12.341 -28.515 30.874 1.00 43.00 O
ANISOU 893 OG1 THR A 117 6219 4752 5370 -460 93 1040 O
ATOM 894 CG2 THR A 117 13.488 -30.609 30.576 1.00 44.96 C
ANISOU 894 CG2 THR A 117 6642 4745 5694 -394 -7 1070 C
ATOM 895 N GLY A 118 11.358 -28.099 27.555 1.00 42.93 N
ANISOU 895 N GLY A 118 6083 4721 5509 -536 61 813 N
ATOM 896 CA GLY A 118 10.510 -27.056 27.001 1.00 32.06 C
ANISOU 896 CA GLY A 118 4600 3450 4130 -581 91 762 C
ATOM 897 C GLY A 118 9.899 -26.166 28.066 1.00 41.45 C
ANISOU 897 C GLY A 118 5728 4762 5260 -608 154 817 C
ATOM 898 O GLY A 118 9.743 -24.959 27.865 1.00 40.27 O
ANISOU 898 O GLY A 118 5497 4723 5082 -586 175 768 O
ATOM 899 N THR A 119 9.546 -26.748 29.216 1.00 44.69 N
ANISOU 899 N THR A 119 6181 5151 5648 -654 187 919 N
ATOM 900 CA THR A 119 8.959 -25.956 30.292 1.00 40.05 C
ANISOU 900 CA THR A 119 5541 4684 4994 -676 255 971 C
ATOM 901 C THR A 119 9.962 -24.954 30.848 1.00 37.87 C
ANISOU 901 C THR A 119 5256 4495 4638 -566 252 947 C
ATOM 902 O THR A 119 9.623 -23.786 31.076 1.00 40.10 O
ANISOU 902 O THR A 119 5462 4895 4879 -555 289 919 O
ATOM 903 CB THR A 119 8.450 -26.871 31.405 1.00 46.42 C
ANISOU 903 CB THR A 119 6409 5446 5784 -747 294 1092 C
ATOM 904 OG1 THR A 119 7.461 -27.764 30.878 1.00 54.93 O
ANISOU 904 OG1 THR A 119 7486 6442 6945 -864 297 1112 O
ATOM 905 CG2 THR A 119 7.835 -26.050 32.530 1.00 46.58 C
ANISOU 905 CG2 THR A 119 6375 5600 5724 -765 372 1141 C
ATOM 906 N ARG A 120 11.202 -25.391 31.071 1.00 38.03 N
ANISOU 906 N ARG A 120 5352 4457 4641 -482 204 954 N
ATOM 907 CA ARG A 120 12.229 -24.474 31.549 1.00 38.30 C
ANISOU 907 CA ARG A 120 5373 4571 4609 -381 190 925 C
ATOM 908 C ARG A 120 12.552 -23.415 30.504 1.00 35.02 C
ANISOU 908 C ARG A 120 4881 4213 4214 -340 175 817 C
ATOM 909 O ARG A 120 12.823 -22.261 30.849 1.00 40.56 O
ANISOU 909 O ARG A 120 5533 5014 4865 -297 188 786 O
ATOM 910 CB ARG A 120 13.485 -25.252 31.939 1.00 37.77 C
ANISOU 910 CB ARG A 120 5395 4426 4531 -300 133 954 C
ATOM 911 CG ARG A 120 13.267 -26.224 33.084 1.00 44.72 C
ANISOU 911 CG ARG A 120 6365 5250 5377 -330 143 1072 C
ATOM 912 CD ARG A 120 14.496 -27.081 33.331 1.00 45.32 C
ANISOU 912 CD ARG A 120 6532 5233 5454 -242 74 1097 C
ATOM 913 NE ARG A 120 14.257 -28.086 34.360 1.00 42.93 N
ANISOU 913 NE ARG A 120 6330 4861 5121 -274 78 1219 N
ATOM 914 CZ ARG A 120 15.106 -29.055 34.675 1.00 49.22 C
ANISOU 914 CZ ARG A 120 7224 5553 5922 -210 18 1265 C
ATOM 915 NH1 ARG A 120 16.271 -29.180 34.061 1.00 46.49 N
ANISOU 915 NH1 ARG A 120 6882 5166 5615 -107 -50 1195 N
ATOM 916 NH2 ARG A 120 14.774 -29.924 35.626 1.00 53.67 N
ANISOU 916 NH2 ARG A 120 7885 6053 6453 -250 27 1387 N
ATOM 917 N ALA A 121 12.522 -23.783 29.221 1.00 34.84 N
ANISOU 917 N ALA A 121 4851 4126 4260 -354 147 758 N
ATOM 918 CA ALA A 121 12.791 -22.807 28.170 1.00 32.81 C
ANISOU 918 CA ALA A 121 4530 3922 4016 -320 136 664 C
ATOM 919 C ALA A 121 11.741 -21.701 28.166 1.00 32.41 C
ANISOU 919 C ALA A 121 4395 3972 3948 -367 180 648 C
ATOM 920 O ALA A 121 12.075 -20.517 28.053 1.00 32.24 O
ANISOU 920 O ALA A 121 4323 4029 3897 -322 185 600 O
ATOM 921 CB ALA A 121 12.852 -23.499 26.810 1.00 32.17 C
ANISOU 921 CB ALA A 121 4467 3754 4001 -331 100 608 C
ATOM 922 N LYS A 122 10.462 -22.073 28.295 1.00 31.48 N
ANISOU 922 N LYS A 122 4258 3850 3853 -457 212 688 N
ATOM 923 CA LYS A 122 9.396 -21.074 28.331 1.00 37.57 C
ANISOU 923 CA LYS A 122 4943 4719 4615 -495 255 673 C
ATOM 924 C LYS A 122 9.557 -20.136 29.520 1.00 35.77 C
ANISOU 924 C LYS A 122 4694 4587 4309 -453 294 696 C
ATOM 925 O LYS A 122 9.326 -18.927 29.402 1.00 36.12 O
ANISOU 925 O LYS A 122 4675 4714 4334 -429 309 649 O
ATOM 926 CB LYS A 122 8.029 -21.758 28.381 1.00 38.28 C
ANISOU 926 CB LYS A 122 5008 4790 4747 -602 285 719 C
ATOM 927 CG LYS A 122 7.684 -22.572 27.148 1.00 51.74 C
ANISOU 927 CG LYS A 122 6723 6406 6531 -654 242 684 C
ATOM 928 CD LYS A 122 6.308 -23.208 27.274 1.00 59.28 C
ANISOU 928 CD LYS A 122 7644 7348 7533 -770 270 730 C
ATOM 929 CE LYS A 122 5.968 -24.034 26.043 1.00 70.84 C
ANISOU 929 CE LYS A 122 9121 8718 9076 -825 216 688 C
ATOM 930 NZ LYS A 122 4.638 -24.694 26.157 1.00 91.30 N
ANISOU 930 NZ LYS A 122 11674 11293 11725 -950 238 732 N
ATOM 931 N GLY A 123 9.942 -20.676 30.677 1.00 35.24 N
ANISOU 931 N GLY A 123 4687 4507 4194 -441 306 766 N
ATOM 932 CA GLY A 123 10.192 -19.826 31.828 1.00 38.06 C
ANISOU 932 CA GLY A 123 5039 4955 4468 -394 335 781 C
ATOM 933 C GLY A 123 11.354 -18.878 31.606 1.00 35.50 C
ANISOU 933 C GLY A 123 4706 4662 4121 -305 294 712 C
ATOM 934 O GLY A 123 11.294 -17.708 31.994 1.00 35.00 O
ANISOU 934 O GLY A 123 4600 4684 4014 -276 313 679 O
ATOM 935 N ILE A 124 12.426 -19.365 30.976 1.00 33.93 N
ANISOU 935 N ILE A 124 4544 4393 3954 -262 239 687 N
ATOM 936 CA ILE A 124 13.561 -18.500 30.663 1.00 32.08 C
ANISOU 936 CA ILE A 124 4292 4189 3709 -188 203 621 C
ATOM 937 C ILE A 124 13.135 -17.387 29.714 1.00 29.04 C
ANISOU 937 C ILE A 124 3835 3850 3349 -198 213 551 C
ATOM 938 O ILE A 124 13.514 -16.223 29.887 1.00 30.58 O
ANISOU 938 O ILE A 124 3997 4107 3514 -160 212 511 O
ATOM 939 CB ILE A 124 14.723 -19.324 30.076 1.00 27.99 C
ANISOU 939 CB ILE A 124 3818 3590 3229 -142 150 606 C
ATOM 940 CG1 ILE A 124 15.261 -20.320 31.106 1.00 31.83 C
ANISOU 940 CG1 ILE A 124 4379 4030 3685 -114 129 678 C
ATOM 941 CG2 ILE A 124 15.833 -18.408 29.584 1.00 30.21 C
ANISOU 941 CG2 ILE A 124 4061 3907 3509 -78 121 535 C
ATOM 942 CD1 ILE A 124 15.688 -19.688 32.406 1.00 48.31 C
ANISOU 942 CD1 ILE A 124 6473 6192 5691 -72 128 702 C
ATOM 943 N ILE A 125 12.330 -17.726 28.704 1.00 29.28 N
ANISOU 943 N ILE A 125 3845 3846 3434 -250 218 536 N
ATOM 944 CA ILE A 125 11.902 -16.739 27.716 1.00 27.67 C
ANISOU 944 CA ILE A 125 3581 3679 3252 -257 219 474 C
ATOM 945 C ILE A 125 11.033 -15.669 28.365 1.00 29.16 C
ANISOU 945 C ILE A 125 3716 3954 3408 -266 259 475 C
ATOM 946 O ILE A 125 11.208 -14.469 28.115 1.00 27.80 O
ANISOU 946 O ILE A 125 3510 3829 3224 -232 255 427 O
ATOM 947 CB ILE A 125 11.170 -17.438 26.556 1.00 31.33 C
ANISOU 947 CB ILE A 125 4039 4089 3777 -312 207 461 C
ATOM 948 CG1 ILE A 125 12.149 -18.288 25.746 1.00 25.09 C
ANISOU 948 CG1 ILE A 125 3301 3218 3016 -285 166 437 C
ATOM 949 CG2 ILE A 125 10.474 -16.422 25.664 1.00 25.66 C
ANISOU 949 CG2 ILE A 125 3259 3417 3073 -323 208 410 C
ATOM 950 CD1 ILE A 125 11.492 -19.093 24.650 1.00 33.04 C
ANISOU 950 CD1 ILE A 125 4317 4161 4076 -337 147 418 C
ATOM 951 N ALA A 126 10.082 -16.082 29.208 1.00 26.34 N
ANISOU 951 N ALA A 126 3354 3619 3036 -310 301 529 N
ATOM 952 CA ALA A 126 9.209 -15.114 29.865 1.00 29.15 C
ANISOU 952 CA ALA A 126 3655 4063 3358 -312 347 526 C
ATOM 953 C ALA A 126 9.998 -14.199 30.794 1.00 31.24 C
ANISOU 953 C ALA A 126 3936 4380 3555 -246 347 510 C
ATOM 954 O ALA A 126 9.714 -12.998 30.882 1.00 28.69 O
ANISOU 954 O ALA A 126 3571 4116 3215 -219 360 466 O
ATOM 955 CB ALA A 126 8.105 -15.840 30.633 1.00 24.61 C
ANISOU 955 CB ALA A 126 3069 3505 2776 -376 401 592 C
ATOM 956 N ILE A 127 10.997 -14.746 31.492 1.00 29.02 N
ANISOU 956 N ILE A 127 3716 4073 3236 -216 327 541 N
ATOM 957 CA ILE A 127 11.819 -13.928 32.381 1.00 29.80 C
ANISOU 957 CA ILE A 127 3833 4220 3270 -155 315 521 C
ATOM 958 C ILE A 127 12.618 -12.909 31.578 1.00 26.57 C
ANISOU 958 C ILE A 127 3398 3811 2886 -115 275 446 C
ATOM 959 O ILE A 127 12.731 -11.739 31.965 1.00 30.27 O
ANISOU 959 O ILE A 127 3848 4331 3323 -83 276 405 O
ATOM 960 CB ILE A 127 12.735 -14.826 33.235 1.00 32.14 C
ANISOU 960 CB ILE A 127 4200 4487 3525 -130 291 573 C
ATOM 961 CG1 ILE A 127 11.919 -15.591 34.282 1.00 38.59 C
ANISOU 961 CG1 ILE A 127 5050 5319 4294 -169 340 654 C
ATOM 962 CG2 ILE A 127 13.833 -14.006 33.898 1.00 31.25 C
ANISOU 962 CG2 ILE A 127 4101 4413 3359 -64 254 537 C
ATOM 963 CD1 ILE A 127 12.709 -16.660 35.018 1.00 35.94 C
ANISOU 963 CD1 ILE A 127 4796 4936 3922 -150 311 720 C
ATOM 964 N CYS A 128 13.172 -13.332 30.440 1.00 23.45 N
ANISOU 964 N CYS A 128 3006 3356 2548 -118 241 427 N
ATOM 965 CA CYS A 128 13.997 -12.436 29.637 1.00 26.64 C
ANISOU 965 CA CYS A 128 3389 3760 2975 -87 210 366 C
ATOM 966 C CYS A 128 13.180 -11.307 29.018 1.00 26.58 C
ANISOU 966 C CYS A 128 3332 3782 2983 -99 226 325 C
ATOM 967 O CYS A 128 13.698 -10.198 28.840 1.00 25.84 O
ANISOU 967 O CYS A 128 3224 3707 2886 -72 210 280 O
ATOM 968 CB CYS A 128 14.726 -13.232 28.555 1.00 27.23 C
ANISOU 968 CB CYS A 128 3479 3770 3098 -86 180 356 C
ATOM 969 SG CYS A 128 15.995 -14.354 29.198 1.00 36.56 S
ANISOU 969 SG CYS A 128 4714 4911 4268 -46 146 389 S
ATOM 970 N TRP A 129 11.911 -11.561 28.684 1.00 25.47 N
ANISOU 970 N TRP A 129 3166 3645 2865 -141 253 340 N
ATOM 971 CA TRP A 129 11.060 -10.488 28.174 1.00 25.96 C
ANISOU 971 CA TRP A 129 3180 3740 2943 -142 263 304 C
ATOM 972 C TRP A 129 10.783 -9.446 29.250 1.00 24.52 C
ANISOU 972 C TRP A 129 2983 3620 2713 -110 286 289 C
ATOM 973 O TRP A 129 10.748 -8.244 28.962 1.00 28.61 O
ANISOU 973 O TRP A 129 3482 4155 3236 -84 276 243 O
ATOM 974 CB TRP A 129 9.751 -11.059 27.629 1.00 28.20 C
ANISOU 974 CB TRP A 129 3430 4021 3265 -193 280 322 C
ATOM 975 CG TRP A 129 9.822 -11.445 26.182 1.00 35.79 C
ANISOU 975 CG TRP A 129 4393 4931 4275 -214 246 303 C
ATOM 976 CD1 TRP A 129 9.976 -12.702 25.675 1.00 33.53 C
ANISOU 976 CD1 TRP A 129 4136 4587 4016 -248 231 323 C
ATOM 977 CD2 TRP A 129 9.746 -10.564 25.054 1.00 33.50 C
ANISOU 977 CD2 TRP A 129 4084 4640 4006 -202 220 259 C
ATOM 978 NE1 TRP A 129 9.999 -12.659 24.303 1.00 33.28 N
ANISOU 978 NE1 TRP A 129 4103 4525 4015 -254 200 288 N
ATOM 979 CE2 TRP A 129 9.860 -11.358 23.896 1.00 36.12 C
ANISOU 979 CE2 TRP A 129 4434 4921 4368 -228 193 253 C
ATOM 980 CE3 TRP A 129 9.593 -9.181 24.912 1.00 28.41 C
ANISOU 980 CE3 TRP A 129 3415 4028 3353 -169 216 226 C
ATOM 981 CZ2 TRP A 129 9.825 -10.816 22.611 1.00 31.52 C
ANISOU 981 CZ2 TRP A 129 3847 4329 3800 -223 164 218 C
ATOM 982 CZ3 TRP A 129 9.558 -8.644 23.636 1.00 29.49 C
ANISOU 982 CZ3 TRP A 129 3548 4146 3511 -166 185 197 C
ATOM 983 CH2 TRP A 129 9.674 -9.461 22.502 1.00 32.22 C
ANISOU 983 CH2 TRP A 129 3913 4451 3878 -193 161 195 C
ATOM 984 N VAL A 130 10.587 -9.886 30.496 1.00 28.88 N
ANISOU 984 N VAL A 130 3552 4205 3216 -110 318 326 N
ATOM 985 CA VAL A 130 10.391 -8.945 31.596 1.00 28.52 C
ANISOU 985 CA VAL A 130 3502 4222 3113 -73 341 305 C
ATOM 986 C VAL A 130 11.643 -8.100 31.798 1.00 27.17 C
ANISOU 986 C VAL A 130 3359 4044 2920 -27 298 261 C
ATOM 987 O VAL A 130 11.571 -6.875 31.951 1.00 29.98 O
ANISOU 987 O VAL A 130 3702 4425 3265 4 294 211 O
ATOM 988 CB VAL A 130 10.001 -9.694 32.884 1.00 33.58 C
ANISOU 988 CB VAL A 130 4165 4902 3693 -85 386 361 C
ATOM 989 CG1 VAL A 130 10.022 -8.747 34.077 1.00 33.09 C
ANISOU 989 CG1 VAL A 130 4113 4906 3555 -36 405 332 C
ATOM 990 CG2 VAL A 130 8.630 -10.331 32.730 1.00 31.15 C
ANISOU 990 CG2 VAL A 130 3812 4610 3412 -138 438 400 C
ATOM 991 N LEU A 131 12.813 -8.744 31.798 1.00 23.51 N
ANISOU 991 N LEU A 131 2933 3546 2455 -23 262 277 N
ATOM 992 CA LEU A 131 14.060 -8.001 31.940 1.00 26.81 C
ANISOU 992 CA LEU A 131 3365 3959 2862 12 216 235 C
ATOM 993 C LEU A 131 14.302 -7.076 30.754 1.00 29.64 C
ANISOU 993 C LEU A 131 3697 4291 3276 10 195 187 C
ATOM 994 O LEU A 131 14.885 -5.999 30.919 1.00 29.79 O
ANISOU 994 O LEU A 131 3715 4315 3287 32 171 142 O
ATOM 995 CB LEU A 131 15.231 -8.970 32.110 1.00 23.97 C
ANISOU 995 CB LEU A 131 3038 3572 2500 21 181 263 C
ATOM 996 CG LEU A 131 15.195 -9.852 33.360 1.00 30.90 C
ANISOU 996 CG LEU A 131 3958 4469 3313 31 191 317 C
ATOM 997 CD1 LEU A 131 16.385 -10.800 33.386 1.00 32.82 C
ANISOU 997 CD1 LEU A 131 4232 4674 3565 50 145 342 C
ATOM 998 CD2 LEU A 131 15.158 -9.000 34.619 1.00 34.22 C
ANISOU 998 CD2 LEU A 131 4394 4952 3657 63 194 294 C
ATOM 999 N SER A 132 13.863 -7.471 29.557 1.00 26.36 N
ANISOU 999 N SER A 132 3263 3842 2912 -19 202 197 N
ATOM 1000 CA SER A 132 14.051 -6.614 28.390 1.00 23.77 C
ANISOU 1000 CA SER A 132 2918 3489 2625 -23 184 160 C
ATOM 1001 C SER A 132 13.247 -5.327 28.520 1.00 26.21 C
ANISOU 1001 C SER A 132 3208 3820 2929 -7 192 127 C
ATOM 1002 O SER A 132 13.737 -4.243 28.179 1.00 28.18 O
ANISOU 1002 O SER A 132 3461 4055 3191 5 170 91 O
ATOM 1003 CB SER A 132 13.665 -7.368 27.118 1.00 24.03 C
ANISOU 1003 CB SER A 132 2943 3488 2701 -54 186 177 C
ATOM 1004 OG SER A 132 14.437 -8.548 26.979 1.00 23.27 O
ANISOU 1004 OG SER A 132 2868 3361 2611 -61 176 200 O
ATOM 1005 N PHE A 133 12.010 -5.425 29.015 1.00 23.75 N
ANISOU 1005 N PHE A 133 2877 3544 2602 -6 226 140 N
ATOM 1006 CA PHE A 133 11.214 -4.226 29.259 1.00 30.11 C
ANISOU 1006 CA PHE A 133 3663 4376 3403 23 237 103 C
ATOM 1007 C PHE A 133 11.858 -3.343 30.319 1.00 28.72 C
ANISOU 1007 C PHE A 133 3514 4217 3183 61 225 65 C
ATOM 1008 O PHE A 133 11.893 -2.116 30.179 1.00 25.48 O
ANISOU 1008 O PHE A 133 3106 3792 2784 85 206 20 O
ATOM 1009 CB PHE A 133 9.794 -4.610 29.676 1.00 26.77 C
ANISOU 1009 CB PHE A 133 3201 3999 2971 19 283 123 C
ATOM 1010 CG PHE A 133 8.855 -4.812 28.522 1.00 32.15 C
ANISOU 1010 CG PHE A 133 3841 4668 3707 -6 281 132 C
ATOM 1011 CD1 PHE A 133 8.725 -6.055 27.923 1.00 33.91 C
ANISOU 1011 CD1 PHE A 133 4059 4869 3955 -54 282 173 C
ATOM 1012 CD2 PHE A 133 8.094 -3.759 28.042 1.00 32.34 C
ANISOU 1012 CD2 PHE A 133 3834 4697 3756 23 273 99 C
ATOM 1013 CE1 PHE A 133 7.857 -6.241 26.862 1.00 34.55 C
ANISOU 1013 CE1 PHE A 133 4103 4940 4083 -78 271 175 C
ATOM 1014 CE2 PHE A 133 7.225 -3.939 26.982 1.00 38.00 C
ANISOU 1014 CE2 PHE A 133 4512 5407 4519 4 261 106 C
ATOM 1015 CZ PHE A 133 7.106 -5.181 26.391 1.00 32.13 C
ANISOU 1015 CZ PHE A 133 3763 4648 3798 -49 259 143 C
ATOM 1016 N ALA A 134 12.373 -3.950 31.389 1.00 29.68 N
ANISOU 1016 N ALA A 134 3659 4364 3253 66 231 83 N
ATOM 1017 CA ALA A 134 13.003 -3.165 32.444 1.00 32.39 C
ANISOU 1017 CA ALA A 134 4031 4728 3546 101 212 42 C
ATOM 1018 C ALA A 134 14.277 -2.493 31.948 1.00 29.87 C
ANISOU 1018 C ALA A 134 3726 4364 3260 97 157 8 C
ATOM 1019 O ALA A 134 14.557 -1.342 32.301 1.00 26.23 O
ANISOU 1019 O ALA A 134 3279 3898 2791 119 133 -45 O
ATOM 1020 CB ALA A 134 13.293 -4.054 33.654 1.00 30.94 C
ANISOU 1020 CB ALA A 134 3877 4585 3295 107 223 75 C
ATOM 1021 N ILE A 135 15.055 -3.190 31.118 1.00 27.86 N
ANISOU 1021 N ILE A 135 3466 4076 3043 68 139 35 N
ATOM 1022 CA ILE A 135 16.295 -2.617 30.602 1.00 28.61 C
ANISOU 1022 CA ILE A 135 3562 4137 3172 58 97 7 C
ATOM 1023 C ILE A 135 15.998 -1.537 29.569 1.00 29.56 C
ANISOU 1023 C ILE A 135 3674 4218 3338 46 94 -18 C
ATOM 1024 O ILE A 135 16.532 -0.423 29.639 1.00 21.14 O
ANISOU 1024 O ILE A 135 2618 3131 2284 48 66 -58 O
ATOM 1025 CB ILE A 135 17.190 -3.721 30.014 1.00 30.79 C
ANISOU 1025 CB ILE A 135 3830 4395 3472 38 87 41 C
ATOM 1026 CG1 ILE A 135 17.759 -4.600 31.128 1.00 34.12 C
ANISOU 1026 CG1 ILE A 135 4269 4846 3849 57 73 61 C
ATOM 1027 CG2 ILE A 135 18.305 -3.112 29.178 1.00 30.46 C
ANISOU 1027 CG2 ILE A 135 3773 4322 3476 18 60 16 C
ATOM 1028 CD1 ILE A 135 18.501 -5.808 30.616 1.00 28.94 C
ANISOU 1028 CD1 ILE A 135 3607 4169 3219 50 64 95 C
ATOM 1029 N GLY A 136 15.146 -1.852 28.590 1.00 25.92 N
ANISOU 1029 N GLY A 136 3199 3745 2906 33 117 8 N
ATOM 1030 CA GLY A 136 14.912 -0.928 27.496 1.00 23.44 C
ANISOU 1030 CA GLY A 136 2884 3392 2631 24 108 -6 C
ATOM 1031 C GLY A 136 14.172 0.327 27.907 1.00 23.59 C
ANISOU 1031 C GLY A 136 2911 3406 2646 57 103 -43 C
ATOM 1032 O GLY A 136 14.348 1.383 27.291 1.00 21.76 O
ANISOU 1032 O GLY A 136 2694 3129 2443 54 81 -63 O
ATOM 1033 N LEU A 137 13.343 0.242 28.946 1.00 20.96 N
ANISOU 1033 N LEU A 137 2571 3117 2275 90 125 -54 N
ATOM 1034 CA LEU A 137 12.551 1.379 29.395 1.00 24.41 C
ANISOU 1034 CA LEU A 137 3013 3555 2706 133 126 -97 C
ATOM 1035 C LEU A 137 13.135 2.045 30.634 1.00 22.65 C
ANISOU 1035 C LEU A 137 2821 3343 2442 159 109 -146 C
ATOM 1036 O LEU A 137 12.437 2.816 31.301 1.00 24.41 O
ANISOU 1036 O LEU A 137 3051 3580 2644 206 117 -189 O
ATOM 1037 CB LEU A 137 11.107 0.946 29.652 1.00 27.15 C
ANISOU 1037 CB LEU A 137 3323 3952 3039 157 169 -84 C
ATOM 1038 CG LEU A 137 10.386 0.290 28.469 1.00 22.39 C
ANISOU 1038 CG LEU A 137 2686 3344 2478 131 178 -42 C
ATOM 1039 CD1 LEU A 137 8.966 -0.085 28.853 1.00 26.16 C
ANISOU 1039 CD1 LEU A 137 3115 3878 2948 150 220 -34 C
ATOM 1040 CD2 LEU A 137 10.396 1.189 27.238 1.00 22.92 C
ANISOU 1040 CD2 LEU A 137 2765 3353 2592 132 141 -51 C
ATOM 1041 N THR A 138 14.395 1.758 30.955 1.00 25.93 N
ANISOU 1041 N THR A 138 3252 3754 2846 134 82 -146 N
ATOM 1042 CA THR A 138 15.065 2.425 32.068 1.00 30.08 C
ANISOU 1042 CA THR A 138 3808 4286 3335 154 52 -198 C
ATOM 1043 C THR A 138 15.016 3.949 31.994 1.00 25.34 C
ANISOU 1043 C THR A 138 3234 3633 2761 172 21 -258 C
ATOM 1044 O THR A 138 14.831 4.578 33.050 1.00 24.55 O
ANISOU 1044 O THR A 138 3160 3548 2618 213 13 -313 O
ATOM 1045 CB THR A 138 16.515 1.923 32.161 1.00 29.74 C
ANISOU 1045 CB THR A 138 3765 4240 3294 119 16 -188 C
ATOM 1046 OG1 THR A 138 16.520 0.565 32.618 1.00 36.02 O
ANISOU 1046 OG1 THR A 138 4552 5085 4050 121 38 -141 O
ATOM 1047 CG2 THR A 138 17.334 2.770 33.126 1.00 21.75 C
ANISOU 1047 CG2 THR A 138 2781 3225 2258 130 -33 -249 C
ATOM 1048 N PRO A 139 15.166 4.603 30.832 1.00 23.27 N
ANISOU 1048 N PRO A 139 2974 3304 2563 146 4 -252 N
ATOM 1049 CA PRO A 139 14.980 6.064 30.806 1.00 21.97 C
ANISOU 1049 CA PRO A 139 2845 3078 2424 168 -25 -304 C
ATOM 1050 C PRO A 139 13.640 6.528 31.353 1.00 24.75 C
ANISOU 1050 C PRO A 139 3201 3451 2751 239 -2 -340 C
ATOM 1051 O PRO A 139 13.557 7.633 31.905 1.00 23.08 O
ANISOU 1051 O PRO A 139 3028 3205 2537 276 -27 -404 O
ATOM 1052 CB PRO A 139 15.132 6.403 29.318 1.00 21.65 C
ANISOU 1052 CB PRO A 139 2805 2972 2448 128 -35 -266 C
ATOM 1053 CG PRO A 139 16.070 5.370 28.814 1.00 22.78 C
ANISOU 1053 CG PRO A 139 2920 3137 2597 73 -27 -219 C
ATOM 1054 CD PRO A 139 15.692 4.109 29.543 1.00 21.52 C
ANISOU 1054 CD PRO A 139 2734 3055 2387 94 5 -200 C
ATOM 1055 N MET A 140 12.586 5.717 31.232 1.00 22.23 N
ANISOU 1055 N MET A 140 2842 3187 2416 260 46 -303 N
ATOM 1056 CA MET A 140 11.294 6.108 31.785 1.00 27.18 C
ANISOU 1056 CA MET A 140 3457 3848 3021 329 76 -338 C
ATOM 1057 C MET A 140 11.285 6.072 33.307 1.00 28.55 C
ANISOU 1057 C MET A 140 3646 4083 3117 368 95 -384 C
ATOM 1058 O MET A 140 10.378 6.644 33.920 1.00 29.12 O
ANISOU 1058 O MET A 140 3719 4181 3165 433 118 -433 O
ATOM 1059 CB MET A 140 10.186 5.211 31.232 1.00 24.90 C
ANISOU 1059 CB MET A 140 3110 3609 2743 330 122 -285 C
ATOM 1060 CG MET A 140 10.111 5.192 29.712 1.00 23.39 C
ANISOU 1060 CG MET A 140 2907 3366 2616 298 101 -241 C
ATOM 1061 SD MET A 140 8.668 4.308 29.095 1.00 33.95 S
ANISOU 1061 SD MET A 140 4172 4758 3970 304 140 -196 S
ATOM 1062 CE MET A 140 7.369 5.480 29.476 1.00 33.30 C
ANISOU 1062 CE MET A 140 4071 4684 3899 398 146 -255 C
ATOM 1063 N LEU A 141 12.266 5.418 33.927 1.00 27.75 N
ANISOU 1063 N LEU A 141 3561 4010 2974 333 84 -373 N
ATOM 1064 CA LEU A 141 12.385 5.398 35.380 1.00 27.53 C
ANISOU 1064 CA LEU A 141 3561 4039 2861 368 92 -416 C
ATOM 1065 C LEU A 141 13.095 6.624 35.936 1.00 25.22 C
ANISOU 1065 C LEU A 141 3324 3697 2562 387 33 -499 C
ATOM 1066 O LEU A 141 13.247 6.726 37.159 1.00 34.39 O
ANISOU 1066 O LEU A 141 4518 4904 3645 420 29 -547 O
ATOM 1067 CB LEU A 141 13.123 4.139 35.838 1.00 25.43 C
ANISOU 1067 CB LEU A 141 3292 3824 2548 330 96 -364 C
ATOM 1068 CG LEU A 141 12.503 2.803 35.437 1.00 32.29 C
ANISOU 1068 CG LEU A 141 4116 4736 3418 305 151 -282 C
ATOM 1069 CD1 LEU A 141 13.231 1.679 36.146 1.00 31.34 C
ANISOU 1069 CD1 LEU A 141 4009 4658 3240 282 149 -240 C
ATOM 1070 CD2 LEU A 141 11.018 2.780 35.757 1.00 33.50 C
ANISOU 1070 CD2 LEU A 141 4238 4944 3546 347 218 -283 C
ATOM 1071 N GLY A 142 13.542 7.543 35.082 1.00 26.47 N
ANISOU 1071 N GLY A 142 3499 3763 2796 364 -14 -517 N
ATOM 1072 CA GLY A 142 14.124 8.780 35.561 1.00 27.95 C
ANISOU 1072 CA GLY A 142 3742 3889 2989 377 -73 -600 C
ATOM 1073 C GLY A 142 15.424 9.168 34.889 1.00 28.29 C
ANISOU 1073 C GLY A 142 3797 3854 3098 302 -134 -592 C
ATOM 1074 O GLY A 142 15.869 10.314 35.006 1.00 32.07 O
ANISOU 1074 O GLY A 142 4321 4258 3607 298 -187 -654 O
ATOM 1075 N TRP A 143 16.047 8.224 34.185 1.00 30.70 N
ANISOU 1075 N TRP A 143 4062 4174 3427 242 -126 -519 N
ATOM 1076 CA TRP A 143 17.306 8.483 33.483 1.00 25.49 C
ANISOU 1076 CA TRP A 143 3399 3456 2831 167 -171 -505 C
ATOM 1077 C TRP A 143 17.002 9.028 32.086 1.00 29.47 C
ANISOU 1077 C TRP A 143 3903 3883 3411 142 -164 -468 C
ATOM 1078 O TRP A 143 17.145 8.354 31.065 1.00 25.85 O
ANISOU 1078 O TRP A 143 3411 3429 2982 103 -139 -401 O
ATOM 1079 CB TRP A 143 18.154 7.217 33.424 1.00 23.38 C
ANISOU 1079 CB TRP A 143 3087 3245 2550 125 -165 -451 C
ATOM 1080 CG TRP A 143 19.589 7.460 33.039 1.00 28.50 C
ANISOU 1080 CG TRP A 143 3722 3856 3252 55 -212 -453 C
ATOM 1081 CD1 TRP A 143 20.153 8.651 32.683 1.00 23.91 C
ANISOU 1081 CD1 TRP A 143 3163 3193 2730 14 -254 -488 C
ATOM 1082 CD2 TRP A 143 20.642 6.486 32.980 1.00 24.45 C
ANISOU 1082 CD2 TRP A 143 3163 3385 2741 17 -221 -417 C
ATOM 1083 NE1 TRP A 143 21.486 8.480 32.403 1.00 23.95 N
ANISOU 1083 NE1 TRP A 143 3130 3195 2775 -54 -283 -476 N
ATOM 1084 CE2 TRP A 143 21.812 7.161 32.578 1.00 23.50 C
ANISOU 1084 CE2 TRP A 143 3028 3216 2684 -47 -265 -436 C
ATOM 1085 CE3 TRP A 143 20.709 5.111 33.226 1.00 25.25 C
ANISOU 1085 CE3 TRP A 143 3235 3558 2802 33 -197 -371 C
ATOM 1086 CZ2 TRP A 143 23.033 6.509 32.416 1.00 25.22 C
ANISOU 1086 CZ2 TRP A 143 3193 3464 2926 -90 -282 -414 C
ATOM 1087 CZ3 TRP A 143 21.922 4.466 33.064 1.00 23.93 C
ANISOU 1087 CZ3 TRP A 143 3025 3412 2657 -4 -221 -350 C
ATOM 1088 CH2 TRP A 143 23.067 5.165 32.663 1.00 23.04 C
ANISOU 1088 CH2 TRP A 143 2887 3258 2607 -62 -262 -374 C
ATOM 1089 N ASN A 144 16.574 10.288 32.057 1.00 28.56 N
ANISOU 1089 N ASN A 144 3835 3694 3323 170 -188 -516 N
ATOM 1090 CA ASN A 144 16.194 10.932 30.808 1.00 29.78 C
ANISOU 1090 CA ASN A 144 4004 3769 3542 157 -188 -482 C
ATOM 1091 C ASN A 144 16.533 12.414 30.880 1.00 33.85 C
ANISOU 1091 C ASN A 144 4584 4176 4103 149 -243 -539 C
ATOM 1092 O ASN A 144 16.904 12.941 31.932 1.00 30.28 O
ANISOU 1092 O ASN A 144 4162 3713 3629 162 -280 -614 O
ATOM 1093 CB ASN A 144 14.706 10.735 30.508 1.00 27.25 C
ANISOU 1093 CB ASN A 144 3670 3476 3210 227 -147 -463 C
ATOM 1094 CG ASN A 144 13.823 11.158 31.662 1.00 28.88 C
ANISOU 1094 CG ASN A 144 3893 3711 3370 315 -140 -536 C
ATOM 1095 OD1 ASN A 144 13.719 12.341 31.977 1.00 35.63 O
ANISOU 1095 OD1 ASN A 144 4799 4495 4242 350 -176 -600 O
ATOM 1096 ND2 ASN A 144 13.182 10.189 32.302 1.00 24.45 N
ANISOU 1096 ND2 ASN A 144 3290 3252 2749 351 -91 -528 N
ATOM 1097 N ASN A 145 16.389 13.088 29.739 1.00 29.99 N
ANISOU 1097 N ASN A 145 4120 3600 3674 127 -252 -501 N
ATOM 1098 CA ASN A 145 16.593 14.526 29.643 1.00 27.58 C
ANISOU 1098 CA ASN A 145 3886 3172 3421 118 -304 -542 C
ATOM 1099 C ASN A 145 15.279 15.303 29.666 1.00 35.73 C
ANISOU 1099 C ASN A 145 4959 4157 4458 216 -309 -575 C
ATOM 1100 O ASN A 145 15.239 16.453 29.213 1.00 39.92 O
ANISOU 1100 O ASN A 145 5555 4570 5043 216 -348 -584 O
ATOM 1101 CB ASN A 145 17.389 14.864 28.380 1.00 27.47 C
ANISOU 1101 CB ASN A 145 3885 3082 3470 25 -314 -474 C
ATOM 1102 CG ASN A 145 18.727 14.139 28.317 1.00 35.75 C
ANISOU 1102 CG ASN A 145 4881 4180 4521 -68 -306 -446 C
ATOM 1103 OD1 ASN A 145 19.381 13.924 29.339 1.00 37.79 O
ANISOU 1103 OD1 ASN A 145 5119 4480 4757 -78 -327 -498 O
ATOM 1104 ND2 ASN A 145 19.138 13.759 27.110 1.00 41.63 N
ANISOU 1104 ND2 ASN A 145 5602 4923 5291 -130 -276 -366 N
ATOM 1105 N CYS A 146 14.205 14.699 30.186 1.00 36.31 N
ANISOU 1105 N CYS A 146 4997 4320 4480 300 -269 -591 N
ATOM 1106 CA CYS A 146 12.935 15.414 30.281 1.00 35.52 C
ANISOU 1106 CA CYS A 146 4921 4189 4386 403 -271 -630 C
ATOM 1107 C CYS A 146 13.037 16.625 31.198 1.00 40.95 C
ANISOU 1107 C CYS A 146 5681 4799 5080 447 -318 -732 C
ATOM 1108 O CYS A 146 12.381 17.644 30.953 1.00 43.35 O
ANISOU 1108 O CYS A 146 6034 5013 5423 510 -346 -762 O
ATOM 1109 CB CYS A 146 11.830 14.466 30.764 1.00 38.87 C
ANISOU 1109 CB CYS A 146 5277 4739 4752 475 -211 -630 C
ATOM 1110 SG CYS A 146 11.397 13.152 29.589 1.00 43.97 S
ANISOU 1110 SG CYS A 146 5846 5458 5402 438 -163 -520 S
ATOM 1111 N GLY A 147 13.853 16.539 32.247 1.00 43.24 N
ANISOU 1111 N GLY A 147 5980 5117 5331 419 -334 -790 N
ATOM 1112 CA GLY A 147 14.051 17.668 33.140 1.00 47.33 C
ANISOU 1112 CA GLY A 147 6572 5560 5851 453 -387 -896 C
ATOM 1113 C GLY A 147 14.903 18.782 32.570 1.00 50.38 C
ANISOU 1113 C GLY A 147 7028 5793 6320 381 -455 -899 C
ATOM 1114 O GLY A 147 14.987 19.850 33.187 1.00 52.90 O
ANISOU 1114 O GLY A 147 7420 6023 6655 410 -508 -990 O
ATOM 1115 N GLN A 148 15.534 18.558 31.419 1.00 55.79 N
ANISOU 1115 N GLN A 148 7695 6445 7056 286 -453 -805 N
ATOM 1116 CA GLN A 148 16.358 19.561 30.745 1.00 54.24 C
ANISOU 1116 CA GLN A 148 7561 6107 6942 201 -506 -788 C
ATOM 1117 C GLN A 148 15.887 19.698 29.302 1.00 48.17 C
ANISOU 1117 C GLN A 148 6802 5283 6219 192 -489 -689 C
ATOM 1118 O GLN A 148 16.572 19.269 28.365 1.00 51.57 O
ANISOU 1118 O GLN A 148 7205 5720 6671 99 -470 -602 O
ATOM 1119 CB GLN A 148 17.842 19.190 30.804 1.00 53.98 C
ANISOU 1119 CB GLN A 148 7494 6095 6922 75 -520 -770 C
ATOM 1120 CG GLN A 148 18.437 19.151 32.208 1.00 66.17 C
ANISOU 1120 CG GLN A 148 9036 7684 8422 76 -556 -868 C
ATOM 1121 CD GLN A 148 18.078 17.889 32.973 1.00 68.38 C
ANISOU 1121 CD GLN A 148 9249 8124 8608 133 -508 -874 C
ATOM 1122 OE1 GLN A 148 17.798 16.847 32.380 1.00 59.02 O
ANISOU 1122 OE1 GLN A 148 8000 7022 7402 131 -450 -792 O
ATOM 1123 NE2 GLN A 148 18.082 17.981 34.298 1.00 80.43 N
ANISOU 1123 NE2 GLN A 148 10795 9691 10073 182 -533 -970 N
ATOM 1124 N PRO A 149 14.717 20.294 29.087 1.00 46.55 N
ANISOU 1124 N PRO A 149 6636 5025 6025 294 -497 -702 N
ATOM 1125 CA PRO A 149 14.170 20.378 27.731 1.00 47.17 C
ANISOU 1125 CA PRO A 149 6725 5061 6137 298 -488 -608 C
ATOM 1126 C PRO A 149 14.815 21.486 26.914 1.00 48.49 C
ANISOU 1126 C PRO A 149 6981 5066 6377 224 -537 -568 C
ATOM 1127 O PRO A 149 15.265 22.507 27.439 1.00 51.64 O
ANISOU 1127 O PRO A 149 7452 5353 6816 207 -589 -632 O
ATOM 1128 CB PRO A 149 12.686 20.672 27.975 1.00 43.86 C
ANISOU 1128 CB PRO A 149 6311 4648 5706 445 -487 -651 C
ATOM 1129 CG PRO A 149 12.686 21.451 29.243 1.00 43.14 C
ANISOU 1129 CG PRO A 149 6269 4513 5610 502 -521 -774 C
ATOM 1130 CD PRO A 149 13.817 20.907 30.082 1.00 44.61 C
ANISOU 1130 CD PRO A 149 6425 4764 5759 417 -514 -807 C
ATOM 1131 N LYS A 150 14.850 21.266 25.601 1.00 48.25 N
ANISOU 1131 N LYS A 150 6949 5022 6361 176 -519 -459 N
ATOM 1132 CA LYS A 150 15.327 22.271 24.651 1.00 53.91 C
ANISOU 1132 CA LYS A 150 7754 5588 7140 106 -555 -397 C
ATOM 1133 C LYS A 150 14.222 23.308 24.488 1.00 46.26 C
ANISOU 1133 C LYS A 150 6869 4505 6203 220 -604 -417 C
ATOM 1134 O LYS A 150 13.314 23.159 23.669 1.00 46.28 O
ANISOU 1134 O LYS A 150 6870 4520 6194 284 -599 -359 O
ATOM 1135 CB LYS A 150 15.694 21.627 23.320 1.00 52.01 C
ANISOU 1135 CB LYS A 150 7487 5387 6888 25 -513 -275 C
ATOM 1136 CG LYS A 150 16.591 20.403 23.442 1.00 51.22 C
ANISOU 1136 CG LYS A 150 7290 5421 6751 -58 -458 -258 C
ATOM 1137 CD LYS A 150 18.036 20.786 23.725 1.00 53.08 C
ANISOU 1137 CD LYS A 150 7531 5609 7027 -184 -470 -271 C
ATOM 1138 CE LYS A 150 18.654 21.508 22.536 1.00 61.76 C
ANISOU 1138 CE LYS A 150 8695 6598 8174 -284 -473 -180 C
ATOM 1139 NZ LYS A 150 20.105 21.788 22.727 1.00 59.79 N
ANISOU 1139 NZ LYS A 150 8432 6317 7969 -421 -475 -184 N
ATOM 1140 N GLU A 151 14.298 24.378 25.284 1.00 52.09 N
ANISOU 1140 N GLU A 151 7682 5129 6981 249 -659 -506 N
ATOM 1141 CA GLU A 151 13.227 25.369 25.290 1.00 58.48 C
ANISOU 1141 CA GLU A 151 8568 5829 7822 376 -708 -543 C
ATOM 1142 C GLU A 151 13.124 26.109 23.962 1.00 55.98 C
ANISOU 1142 C GLU A 151 8340 5376 7553 353 -742 -438 C
ATOM 1143 O GLU A 151 12.038 26.576 23.600 1.00 55.12 O
ANISOU 1143 O GLU A 151 8270 5216 7457 471 -774 -432 O
ATOM 1144 CB GLU A 151 13.435 26.359 26.436 1.00 58.29 C
ANISOU 1144 CB GLU A 151 8614 5703 7830 407 -762 -668 C
ATOM 1145 CG GLU A 151 13.439 25.722 27.817 1.00 59.94 C
ANISOU 1145 CG GLU A 151 8751 6043 7979 447 -734 -777 C
ATOM 1146 CD GLU A 151 12.070 25.224 28.248 1.00 64.58 C
ANISOU 1146 CD GLU A 151 9277 6744 8514 602 -698 -822 C
ATOM 1147 OE1 GLU A 151 11.077 25.477 27.532 1.00 75.10 O
ANISOU 1147 OE1 GLU A 151 10623 8045 9867 690 -706 -781 O
ATOM 1148 OE2 GLU A 151 11.986 24.580 29.315 1.00 75.80 O
ANISOU 1148 OE2 GLU A 151 10635 8290 9873 636 -663 -896 O
ATOM 1149 N GLY A 152 14.231 26.228 23.227 1.00 59.32 N
ANISOU 1149 N GLY A 152 8794 5744 8001 204 -737 -354 N
ATOM 1150 CA GLY A 152 14.171 26.871 21.924 1.00 52.75 C
ANISOU 1150 CA GLY A 152 8051 4792 7201 173 -761 -241 C
ATOM 1151 C GLY A 152 13.379 26.059 20.916 1.00 54.37 C
ANISOU 1151 C GLY A 152 8207 5097 7353 224 -728 -153 C
ATOM 1152 O GLY A 152 12.535 26.597 20.193 1.00 57.72 O
ANISOU 1152 O GLY A 152 8696 5445 7789 305 -769 -105 O
ATOM 1153 N LYS A 153 13.639 24.750 20.854 1.00 51.38 N
ANISOU 1153 N LYS A 153 7716 4890 6917 180 -661 -132 N
ATOM 1154 CA LYS A 153 12.894 23.895 19.935 1.00 49.40 C
ANISOU 1154 CA LYS A 153 7415 4742 6614 224 -633 -58 C
ATOM 1155 C LYS A 153 11.432 23.781 20.348 1.00 52.00 C
ANISOU 1155 C LYS A 153 7707 5121 6932 389 -654 -118 C
ATOM 1156 O LYS A 153 10.537 23.783 19.494 1.00 54.31 O
ANISOU 1156 O LYS A 153 8010 5411 7212 459 -677 -62 O
ATOM 1157 CB LYS A 153 13.531 22.508 19.865 1.00 47.91 C
ANISOU 1157 CB LYS A 153 7117 4714 6371 142 -559 -34 C
ATOM 1158 CG LYS A 153 14.993 22.493 19.454 1.00 59.02 C
ANISOU 1158 CG LYS A 153 8537 6099 7790 -17 -527 21 C
ATOM 1159 CD LYS A 153 15.510 21.064 19.359 1.00 50.66 C
ANISOU 1159 CD LYS A 153 7368 5204 6678 -75 -456 39 C
ATOM 1160 CE LYS A 153 16.988 21.027 19.016 1.00 54.39 C
ANISOU 1160 CE LYS A 153 7834 5666 7164 -226 -420 85 C
ATOM 1161 NZ LYS A 153 17.477 19.630 18.839 1.00 46.59 N
ANISOU 1161 NZ LYS A 153 6743 4833 6127 -269 -353 104 N
ATOM 1162 N ASN A 154 11.171 23.676 21.653 1.00 47.17 N
ANISOU 1162 N ASN A 154 7046 4558 6318 452 -647 -231 N
ATOM 1163 CA ASN A 154 9.802 23.490 22.121 1.00 50.14 C
ANISOU 1163 CA ASN A 154 7368 5002 6680 604 -652 -292 C
ATOM 1164 C ASN A 154 8.965 24.750 21.930 1.00 55.27 C
ANISOU 1164 C ASN A 154 8108 5509 7382 720 -725 -310 C
ATOM 1165 O ASN A 154 7.747 24.658 21.735 1.00 57.02 O
ANISOU 1165 O ASN A 154 8293 5773 7600 843 -740 -316 O
ATOM 1166 CB ASN A 154 9.802 23.060 23.589 1.00 44.24 C
ANISOU 1166 CB ASN A 154 6551 4350 5908 637 -617 -406 C
ATOM 1167 CG ASN A 154 10.553 21.757 23.818 1.00 53.32 C
ANISOU 1167 CG ASN A 154 7610 5643 7006 538 -550 -387 C
ATOM 1168 OD1 ASN A 154 10.675 20.928 22.915 1.00 53.40 O
ANISOU 1168 OD1 ASN A 154 7578 5719 6990 482 -520 -301 O
ATOM 1169 ND2 ASN A 154 11.058 21.570 25.033 1.00 51.53 N
ANISOU 1169 ND2 ASN A 154 7357 5461 6759 522 -532 -470 N
ATOM 1170 N HIS A 155 9.591 25.928 21.980 1.00 50.93 N
ANISOU 1170 N HIS A 155 7678 4788 6886 683 -775 -319 N
ATOM 1171 CA HIS A 155 8.855 27.165 21.740 1.00 56.34 C
ANISOU 1171 CA HIS A 155 8464 5316 7626 792 -852 -330 C
ATOM 1172 C HIS A 155 8.644 27.410 20.250 1.00 58.22 C
ANISOU 1172 C HIS A 155 8766 5485 7870 778 -886 -197 C
ATOM 1173 O HIS A 155 7.573 27.873 19.842 1.00 63.22 O
ANISOU 1173 O HIS A 155 9427 6072 8522 908 -938 -188 O
ATOM 1174 CB HIS A 155 9.584 28.349 22.379 1.00 62.15 C
ANISOU 1174 CB HIS A 155 9313 5880 8421 757 -898 -393 C
ATOM 1175 CG HIS A 155 9.432 28.421 23.867 1.00 66.18 C
ANISOU 1175 CG HIS A 155 9789 6430 8926 827 -890 -542 C
ATOM 1176 ND1 HIS A 155 8.759 27.461 24.592 1.00 74.16 N
ANISOU 1176 ND1 HIS A 155 10675 7622 9880 904 -834 -606 N
ATOM 1177 CD2 HIS A 155 9.860 29.339 24.765 1.00 63.30 C
ANISOU 1177 CD2 HIS A 155 9503 5946 8602 829 -930 -642 C
ATOM 1178 CE1 HIS A 155 8.782 27.783 25.873 1.00 76.03 C
ANISOU 1178 CE1 HIS A 155 10918 7857 10114 954 -836 -735 C
ATOM 1179 NE2 HIS A 155 9.445 28.919 26.005 1.00 80.22 N
ANISOU 1179 NE2 HIS A 155 11571 8207 10703 913 -898 -764 N
ATOM 1180 N SER A 156 9.650 27.103 19.425 1.00 55.60 N
ANISOU 1180 N SER A 156 8457 5149 7519 627 -858 -95 N
ATOM 1181 CA SER A 156 9.521 27.330 17.989 1.00 54.22 C
ANISOU 1181 CA SER A 156 8354 4914 7336 606 -887 36 C
ATOM 1182 C SER A 156 8.449 26.433 17.383 1.00 58.34 C
ANISOU 1182 C SER A 156 8788 5574 7805 694 -879 70 C
ATOM 1183 O SER A 156 7.658 26.878 16.543 1.00 62.23 O
ANISOU 1183 O SER A 156 9335 6007 8302 776 -938 128 O
ATOM 1184 CB SER A 156 10.866 27.108 17.297 1.00 50.89 C
ANISOU 1184 CB SER A 156 7961 4480 6895 422 -842 131 C
ATOM 1185 OG SER A 156 11.312 25.772 17.450 1.00 65.01 O
ANISOU 1185 OG SER A 156 9625 6449 8628 353 -763 126 O
ATOM 1186 N GLN A 157 8.405 25.168 17.798 1.00 55.43 N
ANISOU 1186 N GLN A 157 8286 5387 7389 677 -812 34 N
ATOM 1187 CA GLN A 157 7.367 24.252 17.347 1.00 55.28 C
ANISOU 1187 CA GLN A 157 8171 5505 7327 754 -804 52 C
ATOM 1188 C GLN A 157 6.052 24.443 18.093 1.00 56.46 C
ANISOU 1188 C GLN A 157 8263 5686 7503 921 -834 -41 C
ATOM 1189 O GLN A 157 5.061 23.791 17.750 1.00 58.97 O
ANISOU 1189 O GLN A 157 8497 6112 7799 995 -837 -32 O
ATOM 1190 CB GLN A 157 7.844 22.805 17.490 1.00 51.18 C
ANISOU 1190 CB GLN A 157 7538 5158 6752 665 -721 54 C
ATOM 1191 CG GLN A 157 7.148 21.844 16.545 1.00 64.15 C
ANISOU 1191 CG GLN A 157 9116 6915 8345 685 -716 115 C
ATOM 1192 CD GLN A 157 7.543 20.408 16.780 1.00 59.90 C
ANISOU 1192 CD GLN A 157 8467 6536 7757 610 -638 105 C
ATOM 1193 OE1 GLN A 157 6.744 19.494 16.579 1.00 59.51 O
ANISOU 1193 OE1 GLN A 157 8328 6603 7679 652 -628 104 O
ATOM 1194 NE2 GLN A 157 8.783 20.196 17.205 1.00 55.66 N
ANISOU 1194 NE2 GLN A 157 7933 6000 7215 497 -588 98 N
ATOM 1195 N GLY A 158 6.018 25.315 19.096 1.00 56.29 N
ANISOU 1195 N GLY A 158 8281 5577 7529 982 -855 -134 N
ATOM 1196 CA GLY A 158 4.764 25.636 19.756 1.00 54.72 C
ANISOU 1196 CA GLY A 158 8036 5397 7358 1152 -882 -224 C
ATOM 1197 C GLY A 158 4.206 24.502 20.584 1.00 52.94 C
ANISOU 1197 C GLY A 158 7654 5365 7095 1188 -813 -295 C
ATOM 1198 O GLY A 158 2.988 24.276 20.583 1.00 58.35 O
ANISOU 1198 O GLY A 158 8257 6128 7784 1308 -822 -320 O
ATOM 1199 N CYS A 159 5.069 23.780 21.291 1.00 48.23 N
ANISOU 1199 N CYS A 159 7013 4848 6463 1084 -744 -323 N
ATOM 1200 CA CYS A 159 4.605 22.686 22.123 1.00 55.17 C
ANISOU 1200 CA CYS A 159 7756 5905 7302 1108 -674 -382 C
ATOM 1201 C CYS A 159 3.927 23.223 23.375 1.00 55.28 C
ANISOU 1201 C CYS A 159 7748 5922 7332 1235 -670 -507 C
ATOM 1202 O CYS A 159 4.250 24.305 23.873 1.00 51.73 O
ANISOU 1202 O CYS A 159 7394 5343 6918 1265 -707 -565 O
ATOM 1203 CB CYS A 159 5.770 21.773 22.508 1.00 51.05 C
ANISOU 1203 CB CYS A 159 7204 5460 6735 966 -608 -371 C
ATOM 1204 SG CYS A 159 6.647 21.038 21.112 1.00 52.61 S
ANISOU 1204 SG CYS A 159 7416 5670 6903 818 -597 -236 S
ATOM 1205 N GLY A 160 2.970 22.455 23.878 1.00 57.63 N
ANISOU 1205 N GLY A 160 7919 6371 7605 1308 -622 -549 N
ATOM 1206 CA GLY A 160 2.248 22.841 25.067 1.00 57.63 C
ANISOU 1206 CA GLY A 160 7883 6404 7611 1433 -602 -668 C
ATOM 1207 C GLY A 160 3.081 22.641 26.321 1.00 64.51 C
ANISOU 1207 C GLY A 160 8762 7309 8438 1375 -549 -742 C
ATOM 1208 O GLY A 160 4.269 22.319 26.289 1.00 59.10 O
ANISOU 1208 O GLY A 160 8116 6607 7731 1242 -537 -705 O
ATOM 1209 N GLU A 161 2.421 22.844 27.458 1.00 61.68 N
ANISOU 1209 N GLU A 161 8364 7006 8066 1485 -516 -852 N
ATOM 1210 CA GLU A 161 3.085 22.688 28.742 1.00 61.60 C
ANISOU 1210 CA GLU A 161 8365 7038 8004 1450 -470 -933 C
ATOM 1211 C GLU A 161 3.314 21.212 29.043 1.00 59.91 C
ANISOU 1211 C GLU A 161 8047 6994 7721 1359 -389 -893 C
ATOM 1212 O GLU A 161 2.444 20.369 28.805 1.00 54.86 O
ANISOU 1212 O GLU A 161 7296 6478 7068 1386 -345 -859 O
ATOM 1213 CB GLU A 161 2.256 23.338 29.849 1.00 72.69 C
ANISOU 1213 CB GLU A 161 9761 8458 9402 1603 -455 -1064 C
ATOM 1214 CG GLU A 161 1.853 24.778 29.550 1.00 88.44 C
ANISOU 1214 CG GLU A 161 11851 10281 11470 1717 -537 -1109 C
ATOM 1215 CD GLU A 161 3.035 25.662 29.184 1.00 98.47 C
ANISOU 1215 CD GLU A 161 13272 11360 12780 1628 -613 -1088 C
ATOM 1216 OE1 GLU A 161 4.118 25.506 29.789 1.00 88.35 O
ANISOU 1216 OE1 GLU A 161 12032 10075 11464 1523 -600 -1111 O
ATOM 1217 OE2 GLU A 161 2.881 26.516 28.284 1.00100.45 O
ANISOU 1217 OE2 GLU A 161 13602 11466 13100 1661 -689 -1045 O
ATOM 1218 N GLY A 162 4.499 20.902 29.564 1.00 52.90 N
ANISOU 1218 N GLY A 162 7197 6108 6794 1250 -374 -897 N
ATOM 1219 CA GLY A 162 4.889 19.529 29.794 1.00 45.75 C
ANISOU 1219 CA GLY A 162 6213 5342 5828 1157 -308 -851 C
ATOM 1220 C GLY A 162 5.243 18.753 28.547 1.00 49.96 C
ANISOU 1220 C GLY A 162 6719 5886 6376 1054 -313 -730 C
ATOM 1221 O GLY A 162 5.563 17.563 28.648 1.00 49.40 O
ANISOU 1221 O GLY A 162 6586 5924 6261 978 -262 -688 O
ATOM 1222 N GLN A 163 5.196 19.385 27.378 1.00 43.86 N
ANISOU 1222 N GLN A 163 5999 5004 5660 1053 -373 -674 N
ATOM 1223 CA GLN A 163 5.511 18.743 26.113 1.00 46.07 C
ANISOU 1223 CA GLN A 163 6267 5290 5948 963 -380 -562 C
ATOM 1224 C GLN A 163 6.911 19.124 25.653 1.00 43.23 C
ANISOU 1224 C GLN A 163 5999 4822 5603 846 -412 -518 C
ATOM 1225 O GLN A 163 7.439 20.180 26.009 1.00 44.18 O
ANISOU 1225 O GLN A 163 6209 4824 5752 847 -453 -564 O
ATOM 1226 CB GLN A 163 4.497 19.131 25.035 1.00 46.01 C
ANISOU 1226 CB GLN A 163 6255 5244 5984 1038 -426 -517 C
ATOM 1227 CG GLN A 163 3.125 18.514 25.215 1.00 47.10 C
ANISOU 1227 CG GLN A 163 6273 5509 6113 1130 -392 -537 C
ATOM 1228 CD GLN A 163 2.204 18.803 24.047 1.00 51.67 C
ANISOU 1228 CD GLN A 163 6841 6058 6735 1195 -449 -486 C
ATOM 1229 OE1 GLN A 163 2.422 19.748 23.288 1.00 51.32 O
ANISOU 1229 OE1 GLN A 163 6895 5879 6727 1206 -518 -453 O
ATOM 1230 NE2 GLN A 163 1.171 17.984 23.892 1.00 54.37 N
ANISOU 1230 NE2 GLN A 163 7064 6523 7071 1233 -422 -476 N
ATOM 1231 N VAL A 164 7.508 18.244 24.851 1.00 40.21 N
ANISOU 1231 N VAL A 164 5593 4483 5204 741 -392 -432 N
ATOM 1232 CA VAL A 164 8.795 18.494 24.224 1.00 42.88 C
ANISOU 1232 CA VAL A 164 6001 4736 5556 624 -411 -377 C
ATOM 1233 C VAL A 164 8.694 18.102 22.758 1.00 40.45 C
ANISOU 1233 C VAL A 164 5693 4428 5250 583 -419 -272 C
ATOM 1234 O VAL A 164 7.818 17.337 22.350 1.00 34.71 O
ANISOU 1234 O VAL A 164 4896 3790 4503 622 -402 -246 O
ATOM 1235 CB VAL A 164 9.948 17.724 24.909 1.00 40.23 C
ANISOU 1235 CB VAL A 164 5634 4466 5185 526 -369 -390 C
ATOM 1236 CG1 VAL A 164 10.119 18.178 26.354 1.00 41.26 C
ANISOU 1236 CG1 VAL A 164 5779 4592 5304 564 -372 -495 C
ATOM 1237 CG2 VAL A 164 9.696 16.222 24.848 1.00 38.56 C
ANISOU 1237 CG2 VAL A 164 5322 4402 4925 505 -311 -355 C
ATOM 1238 N ALA A 165 9.600 18.656 21.961 1.00 37.37 N
ANISOU 1238 N ALA A 165 5382 3936 4880 501 -444 -214 N
ATOM 1239 CA ALA A 165 9.783 18.185 20.592 1.00 39.63 C
ANISOU 1239 CA ALA A 165 5674 4232 5150 440 -440 -112 C
ATOM 1240 C ALA A 165 10.334 16.763 20.638 1.00 38.24 C
ANISOU 1240 C ALA A 165 5416 4185 4928 364 -377 -93 C
ATOM 1241 O ALA A 165 11.476 16.549 21.045 1.00 40.37 O
ANISOU 1241 O ALA A 165 5684 4462 5194 279 -350 -102 O
ATOM 1242 CB ALA A 165 10.723 19.114 19.829 1.00 37.34 C
ANISOU 1242 CB ALA A 165 5491 3809 4888 359 -469 -53 C
ATOM 1243 N CYS A 166 9.531 15.781 20.238 1.00 30.47 N
ANISOU 1243 N CYS A 166 4361 3301 3914 395 -358 -70 N
ATOM 1244 CA CYS A 166 9.933 14.390 20.404 1.00 33.36 C
ANISOU 1244 CA CYS A 166 4650 3785 4242 337 -302 -62 C
ATOM 1245 C CYS A 166 11.095 14.028 19.483 1.00 36.84 C
ANISOU 1245 C CYS A 166 5118 4214 4665 227 -282 6 C
ATOM 1246 O CYS A 166 10.891 13.571 18.356 1.00 30.64 O
ANISOU 1246 O CYS A 166 4335 3449 3857 210 -282 67 O
ATOM 1247 CB CYS A 166 8.744 13.462 20.170 1.00 34.27 C
ANISOU 1247 CB CYS A 166 4687 3998 4336 392 -291 -55 C
ATOM 1248 SG CYS A 166 9.080 11.740 20.614 1.00 39.16 S
ANISOU 1248 SG CYS A 166 5214 4751 4913 334 -224 -56 S
ATOM 1249 N LEU A 167 12.323 14.239 19.950 1.00 34.07 N
ANISOU 1249 N LEU A 167 4786 3835 4325 154 -265 -8 N
ATOM 1250 CA LEU A 167 13.530 13.875 19.213 1.00 32.33 C
ANISOU 1250 CA LEU A 167 4575 3617 4094 49 -235 48 C
ATOM 1251 C LEU A 167 14.375 12.941 20.070 1.00 30.28 C
ANISOU 1251 C LEU A 167 4248 3439 3820 3 -193 12 C
ATOM 1252 O LEU A 167 14.523 13.167 21.276 1.00 32.06 O
ANISOU 1252 O LEU A 167 4459 3666 4057 22 -201 -53 O
ATOM 1253 CB LEU A 167 14.339 15.120 18.822 1.00 36.22 C
ANISOU 1253 CB LEU A 167 5154 3987 4623 -9 -260 75 C
ATOM 1254 CG LEU A 167 13.578 16.094 17.917 1.00 38.11 C
ANISOU 1254 CG LEU A 167 5475 4130 4874 35 -307 122 C
ATOM 1255 CD1 LEU A 167 14.298 17.432 17.801 1.00 41.60 C
ANISOU 1255 CD1 LEU A 167 6011 4435 5362 -18 -336 139 C
ATOM 1256 CD2 LEU A 167 13.373 15.475 16.545 1.00 32.18 C
ANISOU 1256 CD2 LEU A 167 4729 3420 4078 17 -292 202 C
ATOM 1257 N PHE A 168 14.933 11.902 19.441 1.00 25.28 N
ANISOU 1257 N PHE A 168 3576 2871 3158 -51 -153 53 N
ATOM 1258 CA PHE A 168 15.599 10.841 20.195 1.00 26.10 C
ANISOU 1258 CA PHE A 168 3612 3060 3246 -78 -117 25 C
ATOM 1259 C PHE A 168 16.731 11.391 21.057 1.00 29.08 C
ANISOU 1259 C PHE A 168 3992 3405 3651 -127 -124 -14 C
ATOM 1260 O PHE A 168 16.753 11.183 22.275 1.00 31.46 O
ANISOU 1260 O PHE A 168 4263 3742 3948 -100 -130 -73 O
ATOM 1261 CB PHE A 168 16.121 9.768 19.238 1.00 24.09 C
ANISOU 1261 CB PHE A 168 3328 2862 2962 -128 -76 75 C
ATOM 1262 CG PHE A 168 16.688 8.555 19.931 1.00 24.64 C
ANISOU 1262 CG PHE A 168 3330 3017 3017 -143 -44 51 C
ATOM 1263 CD1 PHE A 168 18.009 8.532 20.354 1.00 24.99 C
ANISOU 1263 CD1 PHE A 168 3351 3066 3076 -200 -31 37 C
ATOM 1264 CD2 PHE A 168 15.902 7.432 20.149 1.00 24.12 C
ANISOU 1264 CD2 PHE A 168 3221 3022 2923 -100 -30 44 C
ATOM 1265 CE1 PHE A 168 18.532 7.420 20.991 1.00 22.76 C
ANISOU 1265 CE1 PHE A 168 3009 2858 2779 -204 -9 17 C
ATOM 1266 CE2 PHE A 168 16.419 6.314 20.783 1.00 20.52 C
ANISOU 1266 CE2 PHE A 168 2712 2633 2452 -110 -4 28 C
ATOM 1267 CZ PHE A 168 17.736 6.308 21.204 1.00 20.59 C
ANISOU 1267 CZ PHE A 168 2704 2646 2474 -157 4 15 C
ATOM 1268 N GLU A 169 17.681 12.100 20.443 1.00 29.39 N
ANISOU 1268 N GLU A 169 4068 3380 3719 -202 -126 17 N
ATOM 1269 CA GLU A 169 18.843 12.576 21.186 1.00 30.06 C
ANISOU 1269 CA GLU A 169 4145 3438 3838 -262 -136 -19 C
ATOM 1270 C GLU A 169 18.520 13.732 22.127 1.00 30.62 C
ANISOU 1270 C GLU A 169 4264 3429 3939 -226 -189 -81 C
ATOM 1271 O GLU A 169 19.404 14.159 22.877 1.00 30.46 O
ANISOU 1271 O GLU A 169 4241 3387 3948 -271 -209 -125 O
ATOM 1272 CB GLU A 169 19.954 12.979 20.212 1.00 24.41 C
ANISOU 1272 CB GLU A 169 3446 2680 3147 -362 -115 37 C
ATOM 1273 CG GLU A 169 20.523 11.811 19.412 1.00 27.86 C
ANISOU 1273 CG GLU A 169 3827 3204 3554 -400 -58 82 C
ATOM 1274 CD GLU A 169 21.808 12.166 18.688 1.00 30.10 C
ANISOU 1274 CD GLU A 169 4108 3466 3864 -505 -26 124 C
ATOM 1275 OE1 GLU A 169 22.270 13.318 18.826 1.00 32.81 O
ANISOU 1275 OE1 GLU A 169 4490 3722 4254 -558 -52 122 O
ATOM 1276 OE2 GLU A 169 22.360 11.295 17.983 1.00 25.56 O
ANISOU 1276 OE2 GLU A 169 3488 2959 3263 -536 26 158 O
ATOM 1277 N ASP A 170 17.287 14.239 22.117 1.00 32.94 N
ANISOU 1277 N ASP A 170 4602 3683 4229 -144 -214 -92 N
ATOM 1278 CA ASP A 170 16.881 15.277 23.055 1.00 25.54 C
ANISOU 1278 CA ASP A 170 3711 2676 3317 -92 -262 -162 C
ATOM 1279 C ASP A 170 16.297 14.725 24.347 1.00 26.88 C
ANISOU 1279 C ASP A 170 3836 2927 3451 -15 -258 -235 C
ATOM 1280 O ASP A 170 16.282 15.439 25.356 1.00 28.74 O
ANISOU 1280 O ASP A 170 4100 3123 3697 16 -292 -309 O
ATOM 1281 CB ASP A 170 15.855 16.211 22.407 1.00 34.39 C
ANISOU 1281 CB ASP A 170 4904 3705 4457 -32 -294 -140 C
ATOM 1282 CG ASP A 170 16.479 17.155 21.403 1.00 37.78 C
ANISOU 1282 CG ASP A 170 5407 4020 4927 -107 -312 -78 C
ATOM 1283 OD1 ASP A 170 17.702 17.058 21.181 1.00 39.36 O
ANISOU 1283 OD1 ASP A 170 5593 4220 5141 -211 -291 -52 O
ATOM 1284 OD2 ASP A 170 15.749 17.996 20.839 1.00 41.07 O
ANISOU 1284 OD2 ASP A 170 5896 4348 5362 -61 -346 -53 O
ATOM 1285 N VAL A 171 15.818 13.481 24.345 1.00 24.36 N
ANISOU 1285 N VAL A 171 3453 2717 3088 14 -218 -217 N
ATOM 1286 CA VAL A 171 15.108 12.937 25.497 1.00 28.20 C
ANISOU 1286 CA VAL A 171 3900 3282 3534 87 -206 -273 C
ATOM 1287 C VAL A 171 15.846 11.736 26.077 1.00 25.54 C
ANISOU 1287 C VAL A 171 3501 3041 3161 50 -175 -274 C
ATOM 1288 O VAL A 171 15.782 11.488 27.286 1.00 29.26 O
ANISOU 1288 O VAL A 171 3955 3563 3598 84 -175 -328 O
ATOM 1289 CB VAL A 171 13.660 12.568 25.125 1.00 27.91 C
ANISOU 1289 CB VAL A 171 3840 3284 3480 166 -188 -254 C
ATOM 1290 CG1 VAL A 171 12.882 13.813 24.730 1.00 31.60 C
ANISOU 1290 CG1 VAL A 171 4368 3656 3984 223 -228 -264 C
ATOM 1291 CG2 VAL A 171 13.634 11.542 23.999 1.00 24.97 C
ANISOU 1291 CG2 VAL A 171 3432 2962 3096 128 -158 -178 C
ATOM 1292 N VAL A 172 16.548 10.987 25.235 1.00 22.99 N
ANISOU 1292 N VAL A 172 3148 2745 2840 -16 -151 -214 N
ATOM 1293 CA VAL A 172 17.278 9.798 25.670 1.00 22.44 C
ANISOU 1293 CA VAL A 172 3022 2761 2743 -45 -126 -210 C
ATOM 1294 C VAL A 172 18.720 10.212 25.955 1.00 26.16 C
ANISOU 1294 C VAL A 172 3493 3204 3242 -116 -149 -230 C
ATOM 1295 O VAL A 172 19.391 10.730 25.050 1.00 23.07 O
ANISOU 1295 O VAL A 172 3118 2757 2891 -180 -151 -196 O
ATOM 1296 CB VAL A 172 17.221 8.688 24.614 1.00 26.76 C
ANISOU 1296 CB VAL A 172 3533 3355 3278 -67 -86 -144 C
ATOM 1297 CG1 VAL A 172 17.901 7.432 25.130 1.00 24.57 C
ANISOU 1297 CG1 VAL A 172 3203 3158 2976 -84 -64 -142 C
ATOM 1298 CG2 VAL A 172 15.774 8.397 24.234 1.00 23.20 C
ANISOU 1298 CG2 VAL A 172 3081 2924 2811 -6 -73 -126 C
ATOM 1299 N PRO A 173 19.220 10.019 27.177 1.00 27.91 N
ANISOU 1299 N PRO A 173 3696 3465 3443 -109 -169 -283 N
ATOM 1300 CA PRO A 173 20.595 10.438 27.478 1.00 23.45 C
ANISOU 1300 CA PRO A 173 3122 2878 2911 -177 -202 -308 C
ATOM 1301 C PRO A 173 21.600 9.579 26.732 1.00 27.78 C
ANISOU 1301 C PRO A 173 3611 3468 3474 -240 -172 -256 C
ATOM 1302 O PRO A 173 21.449 8.359 26.629 1.00 23.31 O
ANISOU 1302 O PRO A 173 3006 2977 2876 -217 -138 -226 O
ATOM 1303 CB PRO A 173 20.710 10.240 28.995 1.00 27.53 C
ANISOU 1303 CB PRO A 173 3632 3444 3385 -138 -232 -376 C
ATOM 1304 CG PRO A 173 19.317 10.054 29.485 1.00 28.08 C
ANISOU 1304 CG PRO A 173 3722 3543 3404 -49 -211 -391 C
ATOM 1305 CD PRO A 173 18.548 9.452 28.354 1.00 26.24 C
ANISOU 1305 CD PRO A 173 3474 3323 3175 -39 -164 -321 C
ATOM 1306 N MET A 174 22.637 10.232 26.208 1.00 24.04 N
ANISOU 1306 N MET A 174 3133 2947 3054 -320 -183 -246 N
ATOM 1307 CA MET A 174 23.625 9.501 25.427 1.00 23.38 C
ANISOU 1307 CA MET A 174 2988 2906 2988 -378 -147 -200 C
ATOM 1308 C MET A 174 24.514 8.640 26.316 1.00 23.33 C
ANISOU 1308 C MET A 174 2915 2979 2969 -377 -163 -231 C
ATOM 1309 O MET A 174 25.036 7.618 25.857 1.00 25.59 O
ANISOU 1309 O MET A 174 3146 3326 3252 -385 -129 -198 O
ATOM 1310 CB MET A 174 24.463 10.471 24.596 1.00 26.03 C
ANISOU 1310 CB MET A 174 3333 3173 3384 -471 -146 -176 C
ATOM 1311 CG MET A 174 25.205 9.803 23.453 1.00 33.34 C
ANISOU 1311 CG MET A 174 4207 4140 4320 -523 -88 -116 C
ATOM 1312 SD MET A 174 24.107 8.965 22.289 1.00 34.80 S
ANISOU 1312 SD MET A 174 4418 4350 4453 -471 -32 -53 S
ATOM 1313 CE MET A 174 23.558 10.343 21.284 1.00 33.00 C
ANISOU 1313 CE MET A 174 4280 4013 4246 -504 -34 -10 C
ATOM 1314 N ASN A 175 24.686 9.020 27.587 1.00 24.25 N
ANISOU 1314 N ASN A 175 3040 3097 3077 -359 -219 -296 N
ATOM 1315 CA ASN A 175 25.451 8.172 28.497 1.00 23.79 C
ANISOU 1315 CA ASN A 175 2925 3117 2996 -345 -244 -323 C
ATOM 1316 C ASN A 175 24.716 6.870 28.793 1.00 23.03 C
ANISOU 1316 C ASN A 175 2822 3091 2836 -270 -214 -299 C
ATOM 1317 O ASN A 175 25.358 5.831 28.991 1.00 24.11 O
ANISOU 1317 O ASN A 175 2907 3292 2961 -262 -212 -287 O
ATOM 1318 CB ASN A 175 25.784 8.924 29.792 1.00 24.56 C
ANISOU 1318 CB ASN A 175 3042 3199 3089 -343 -318 -401 C
ATOM 1319 CG ASN A 175 24.564 9.543 30.461 1.00 27.79 C
ANISOU 1319 CG ASN A 175 3531 3573 3455 -279 -332 -441 C
ATOM 1320 OD1 ASN A 175 23.426 9.157 30.199 1.00 29.46 O
ANISOU 1320 OD1 ASN A 175 3768 3794 3630 -223 -288 -411 O
ATOM 1321 ND2 ASN A 175 24.806 10.507 31.344 1.00 25.47 N
ANISOU 1321 ND2 ASN A 175 3272 3238 3166 -286 -394 -515 N
ATOM 1322 N TYR A 176 23.380 6.900 28.819 1.00 22.65 N
ANISOU 1322 N TYR A 176 2826 3031 2750 -216 -192 -292 N
ATOM 1323 CA TYR A 176 22.623 5.655 28.890 1.00 21.99 C
ANISOU 1323 CA TYR A 176 2732 3006 2615 -161 -155 -257 C
ATOM 1324 C TYR A 176 22.853 4.809 27.643 1.00 22.42 C
ANISOU 1324 C TYR A 176 2752 3075 2691 -186 -108 -197 C
ATOM 1325 O TYR A 176 23.058 3.592 27.731 1.00 22.71 O
ANISOU 1325 O TYR A 176 2757 3166 2708 -166 -92 -174 O
ATOM 1326 CB TYR A 176 21.132 5.950 29.070 1.00 23.12 C
ANISOU 1326 CB TYR A 176 2925 3135 2726 -106 -137 -262 C
ATOM 1327 CG TYR A 176 20.243 4.761 28.773 1.00 21.18 C
ANISOU 1327 CG TYR A 176 2666 2936 2446 -70 -90 -215 C
ATOM 1328 CD1 TYR A 176 19.963 3.819 29.752 1.00 22.49 C
ANISOU 1328 CD1 TYR A 176 2824 3165 2557 -28 -84 -216 C
ATOM 1329 CD2 TYR A 176 19.682 4.582 27.512 1.00 21.04 C
ANISOU 1329 CD2 TYR A 176 2648 2896 2450 -81 -55 -169 C
ATOM 1330 CE1 TYR A 176 19.151 2.730 29.487 1.00 24.19 C
ANISOU 1330 CE1 TYR A 176 3028 3414 2748 -6 -42 -170 C
ATOM 1331 CE2 TYR A 176 18.873 3.494 27.236 1.00 20.28 C
ANISOU 1331 CE2 TYR A 176 2538 2838 2328 -55 -19 -131 C
ATOM 1332 CZ TYR A 176 18.610 2.572 28.228 1.00 27.05 C
ANISOU 1332 CZ TYR A 176 3386 3752 3141 -21 -12 -132 C
ATOM 1333 OH TYR A 176 17.802 1.489 27.959 1.00 29.63 O
ANISOU 1333 OH TYR A 176 3699 4108 3449 -6 22 -93 O
ATOM 1334 N MET A 177 22.821 5.443 26.469 1.00 23.18 N
ANISOU 1334 N MET A 177 2861 3119 2825 -227 -86 -171 N
ATOM 1335 CA MET A 177 22.945 4.701 25.218 1.00 21.09 C
ANISOU 1335 CA MET A 177 2574 2869 2570 -246 -39 -118 C
ATOM 1336 C MET A 177 24.324 4.068 25.071 1.00 21.25 C
ANISOU 1336 C MET A 177 2531 2931 2614 -280 -32 -114 C
ATOM 1337 O MET A 177 24.456 2.980 24.498 1.00 20.90 O
ANISOU 1337 O MET A 177 2460 2924 2559 -268 2 -85 O
ATOM 1338 CB MET A 177 22.653 5.624 24.034 1.00 21.25 C
ANISOU 1338 CB MET A 177 2632 2826 2615 -283 -21 -89 C
ATOM 1339 CG MET A 177 21.215 6.109 23.963 1.00 21.10 C
ANISOU 1339 CG MET A 177 2669 2771 2577 -238 -26 -86 C
ATOM 1340 SD MET A 177 20.040 4.744 23.882 1.00 22.95 S
ANISOU 1340 SD MET A 177 2893 3062 2764 -177 3 -62 S
ATOM 1341 CE MET A 177 20.662 3.841 22.467 1.00 22.70 C
ANISOU 1341 CE MET A 177 2837 3052 2736 -215 45 -13 C
ATOM 1342 N VAL A 178 25.361 4.729 25.578 1.00 21.88 N
ANISOU 1342 N VAL A 178 2581 3004 2727 -321 -68 -147 N
ATOM 1343 CA VAL A 178 26.728 4.257 25.389 1.00 22.20 C
ANISOU 1343 CA VAL A 178 2547 3087 2802 -356 -62 -147 C
ATOM 1344 C VAL A 178 27.116 3.293 26.503 1.00 22.19 C
ANISOU 1344 C VAL A 178 2508 3146 2775 -306 -98 -172 C
ATOM 1345 O VAL A 178 27.438 2.128 26.246 1.00 21.95 O
ANISOU 1345 O VAL A 178 2441 3162 2738 -278 -75 -150 O
ATOM 1346 CB VAL A 178 27.713 5.438 25.316 1.00 23.04 C
ANISOU 1346 CB VAL A 178 2628 3158 2967 -435 -85 -168 C
ATOM 1347 CG1 VAL A 178 29.147 4.931 25.283 1.00 23.51 C
ANISOU 1347 CG1 VAL A 178 2591 3275 3066 -467 -84 -176 C
ATOM 1348 CG2 VAL A 178 27.421 6.292 24.095 1.00 23.16 C
ANISOU 1348 CG2 VAL A 178 2684 3111 3005 -488 -44 -129 C
ATOM 1349 N TYR A 179 27.084 3.771 27.747 1.00 22.52 N
ANISOU 1349 N TYR A 179 2569 3188 2801 -290 -157 -217 N
ATOM 1350 CA TYR A 179 27.544 2.958 28.867 1.00 22.69 C
ANISOU 1350 CA TYR A 179 2562 3267 2792 -244 -200 -239 C
ATOM 1351 C TYR A 179 26.565 1.833 29.180 1.00 22.07 C
ANISOU 1351 C TYR A 179 2520 3215 2651 -174 -178 -209 C
ATOM 1352 O TYR A 179 26.961 0.669 29.311 1.00 23.50 O
ANISOU 1352 O TYR A 179 2670 3438 2820 -141 -177 -189 O
ATOM 1353 CB TYR A 179 27.758 3.840 30.097 1.00 23.34 C
ANISOU 1353 CB TYR A 179 2664 3342 2864 -247 -272 -300 C
ATOM 1354 CG TYR A 179 28.950 4.767 29.999 1.00 25.91 C
ANISOU 1354 CG TYR A 179 2939 3649 3258 -322 -310 -335 C
ATOM 1355 CD1 TYR A 179 30.150 4.332 29.451 1.00 24.46 C
ANISOU 1355 CD1 TYR A 179 2665 3502 3128 -358 -302 -322 C
ATOM 1356 CD2 TYR A 179 28.876 6.077 30.455 1.00 25.90 C
ANISOU 1356 CD2 TYR A 179 2977 3592 3271 -357 -354 -384 C
ATOM 1357 CE1 TYR A 179 31.243 5.176 29.361 1.00 31.53 C
ANISOU 1357 CE1 TYR A 179 3502 4385 4092 -436 -333 -352 C
ATOM 1358 CE2 TYR A 179 29.962 6.928 30.367 1.00 26.40 C
ANISOU 1358 CE2 TYR A 179 2994 3632 3405 -437 -392 -415 C
ATOM 1359 CZ TYR A 179 31.143 6.473 29.820 1.00 34.86 C
ANISOU 1359 CZ TYR A 179 3967 4746 4531 -481 -379 -397 C
ATOM 1360 OH TYR A 179 32.228 7.316 29.733 1.00 36.05 O
ANISOU 1360 OH TYR A 179 4060 4880 4758 -569 -412 -427 O
ATOM 1361 N PHE A 180 25.279 2.161 29.306 1.00 21.73 N
ANISOU 1361 N PHE A 180 2541 3146 2572 -151 -160 -204 N
ATOM 1362 CA PHE A 180 24.310 1.181 29.785 1.00 22.46 C
ANISOU 1362 CA PHE A 180 2663 3266 2604 -94 -141 -179 C
ATOM 1363 C PHE A 180 23.841 0.260 28.662 1.00 26.69 C
ANISOU 1363 C PHE A 180 3193 3798 3149 -91 -85 -126 C
ATOM 1364 O PHE A 180 23.981 -0.965 28.750 1.00 32.53 O
ANISOU 1364 O PHE A 180 3919 4567 3873 -64 -76 -100 O
ATOM 1365 CB PHE A 180 23.127 1.905 30.432 1.00 24.26 C
ANISOU 1365 CB PHE A 180 2948 3478 2791 -68 -142 -202 C
ATOM 1366 CG PHE A 180 22.226 1.014 31.240 1.00 23.58 C
ANISOU 1366 CG PHE A 180 2889 3432 2638 -14 -125 -182 C
ATOM 1367 CD1 PHE A 180 21.197 0.310 30.635 1.00 21.75 C
ANISOU 1367 CD1 PHE A 180 2666 3201 2399 -2 -73 -136 C
ATOM 1368 CD2 PHE A 180 22.394 0.898 32.610 1.00 30.17 C
ANISOU 1368 CD2 PHE A 180 3742 4306 3414 20 -162 -208 C
ATOM 1369 CE1 PHE A 180 20.360 -0.503 31.375 1.00 28.65 C
ANISOU 1369 CE1 PHE A 180 3560 4110 3216 36 -53 -113 C
ATOM 1370 CE2 PHE A 180 21.560 0.089 33.359 1.00 27.23 C
ANISOU 1370 CE2 PHE A 180 3398 3973 2974 63 -139 -182 C
ATOM 1371 CZ PHE A 180 20.543 -0.615 32.741 1.00 31.16 C
ANISOU 1371 CZ PHE A 180 3898 4469 3474 67 -81 -132 C
ATOM 1372 N ASN A 181 23.287 0.833 27.593 1.00 22.74 N
ANISOU 1372 N ASN A 181 2708 3258 2673 -118 -51 -113 N
ATOM 1373 CA ASN A 181 22.683 0.001 26.558 1.00 20.76 C
ANISOU 1373 CA ASN A 181 2461 3004 2421 -114 -5 -70 C
ATOM 1374 C ASN A 181 23.746 -0.689 25.710 1.00 22.43 C
ANISOU 1374 C ASN A 181 2629 3229 2664 -133 13 -54 C
ATOM 1375 O ASN A 181 23.724 -1.915 25.551 1.00 30.55 O
ANISOU 1375 O ASN A 181 3650 4277 3681 -106 29 -33 O
ATOM 1376 CB ASN A 181 21.745 0.838 25.692 1.00 21.80 C
ANISOU 1376 CB ASN A 181 2627 3093 2563 -130 16 -60 C
ATOM 1377 CG ASN A 181 20.890 -0.013 24.779 1.00 25.70 C
ANISOU 1377 CG ASN A 181 3131 3588 3045 -119 52 -22 C
ATOM 1378 OD1 ASN A 181 19.809 -0.461 25.160 1.00 32.41 O
ANISOU 1378 OD1 ASN A 181 3997 4448 3868 -89 58 -13 O
ATOM 1379 ND2 ASN A 181 21.374 -0.247 23.566 1.00 23.90 N
ANISOU 1379 ND2 ASN A 181 2893 3352 2837 -146 77 -3 N
ATOM 1380 N PHE A 182 24.689 0.076 25.164 1.00 26.31 N
ANISOU 1380 N PHE A 182 3091 3710 3196 -179 14 -66 N
ATOM 1381 CA PHE A 182 25.702 -0.499 24.286 1.00 24.82 C
ANISOU 1381 CA PHE A 182 2853 3542 3036 -197 43 -55 C
ATOM 1382 C PHE A 182 26.699 -1.360 25.056 1.00 25.67 C
ANISOU 1382 C PHE A 182 2908 3694 3150 -166 14 -71 C
ATOM 1383 O PHE A 182 26.745 -2.580 24.863 1.00 28.42 O
ANISOU 1383 O PHE A 182 3248 4061 3489 -127 30 -55 O
ATOM 1384 CB PHE A 182 26.444 0.603 23.526 1.00 24.14 C
ANISOU 1384 CB PHE A 182 2745 3436 2992 -263 58 -58 C
ATOM 1385 CG PHE A 182 27.451 0.085 22.534 1.00 31.46 C
ANISOU 1385 CG PHE A 182 3616 4393 3944 -283 102 -47 C
ATOM 1386 CD1 PHE A 182 27.285 -1.157 21.935 1.00 26.52 C
ANISOU 1386 CD1 PHE A 182 2991 3789 3298 -243 136 -30 C
ATOM 1387 CD2 PHE A 182 28.569 0.835 22.210 1.00 30.92 C
ANISOU 1387 CD2 PHE A 182 3495 4332 3921 -343 112 -55 C
ATOM 1388 CE1 PHE A 182 28.212 -1.637 21.026 1.00 25.75 C
ANISOU 1388 CE1 PHE A 182 2843 3722 3218 -252 181 -28 C
ATOM 1389 CE2 PHE A 182 29.502 0.359 21.300 1.00 28.53 C
ANISOU 1389 CE2 PHE A 182 3133 4068 3639 -359 163 -47 C
ATOM 1390 CZ PHE A 182 29.322 -0.878 20.708 1.00 27.17 C
ANISOU 1390 CZ PHE A 182 2963 3920 3440 -308 199 -36 C
ATOM 1391 N PHE A 183 27.504 -0.735 25.918 1.00 23.06 N
ANISOU 1391 N PHE A 183 2544 3378 2840 -181 -33 -104 N
ATOM 1392 CA PHE A 183 28.588 -1.447 26.591 1.00 28.30 C
ANISOU 1392 CA PHE A 183 3148 4088 3516 -152 -69 -120 C
ATOM 1393 C PHE A 183 28.059 -2.619 27.411 1.00 26.71 C
ANISOU 1393 C PHE A 183 2980 3902 3266 -82 -90 -104 C
ATOM 1394 O PHE A 183 28.471 -3.767 27.219 1.00 24.02 O
ANISOU 1394 O PHE A 183 2616 3581 2931 -43 -82 -89 O
ATOM 1395 CB PHE A 183 29.379 -0.487 27.484 1.00 23.93 C
ANISOU 1395 CB PHE A 183 2562 3546 2986 -181 -130 -164 C
ATOM 1396 CG PHE A 183 30.292 0.445 26.731 1.00 29.73 C
ANISOU 1396 CG PHE A 183 3239 4273 3784 -257 -114 -177 C
ATOM 1397 CD1 PHE A 183 30.456 0.330 25.360 1.00 31.22 C
ANISOU 1397 CD1 PHE A 183 3407 4457 3998 -287 -43 -148 C
ATOM 1398 CD2 PHE A 183 30.998 1.430 27.404 1.00 29.62 C
ANISOU 1398 CD2 PHE A 183 3193 4258 3802 -301 -169 -219 C
ATOM 1399 CE1 PHE A 183 31.299 1.188 24.673 1.00 26.16 C
ANISOU 1399 CE1 PHE A 183 2715 3814 3412 -364 -20 -152 C
ATOM 1400 CE2 PHE A 183 31.843 2.289 26.723 1.00 31.35 C
ANISOU 1400 CE2 PHE A 183 3358 4467 4086 -382 -152 -226 C
ATOM 1401 CZ PHE A 183 31.993 2.167 25.356 1.00 29.24 C
ANISOU 1401 CZ PHE A 183 3069 4198 3842 -415 -73 -189 C
ATOM 1402 N ALA A 184 27.133 -2.345 28.331 1.00 27.33 N
ANISOU 1402 N ALA A 184 3118 3971 3297 -65 -113 -106 N
ATOM 1403 CA ALA A 184 26.717 -3.364 29.288 1.00 29.86 C
ANISOU 1403 CA ALA A 184 3471 4309 3564 -7 -135 -87 C
ATOM 1404 C ALA A 184 25.701 -4.335 28.698 1.00 24.73 C
ANISOU 1404 C ALA A 184 2861 3639 2896 12 -85 -43 C
ATOM 1405 O ALA A 184 25.818 -5.549 28.894 1.00 29.24 O
ANISOU 1405 O ALA A 184 3438 4217 3456 51 -89 -17 O
ATOM 1406 CB ALA A 184 26.144 -2.702 30.542 1.00 27.21 C
ANISOU 1406 CB ALA A 184 3181 3980 3176 4 -171 -108 C
ATOM 1407 N CYS A 185 24.697 -3.833 27.981 1.00 23.94 N
ANISOU 1407 N CYS A 185 2792 3510 2796 -16 -44 -34 N
ATOM 1408 CA CYS A 185 23.570 -4.675 27.600 1.00 24.48 C
ANISOU 1408 CA CYS A 185 2898 3561 2843 -2 -8 2 C
ATOM 1409 C CYS A 185 23.693 -5.280 26.209 1.00 25.23 C
ANISOU 1409 C CYS A 185 2980 3637 2969 -14 31 17 C
ATOM 1410 O CYS A 185 22.975 -6.240 25.907 1.00 27.98 O
ANISOU 1410 O CYS A 185 3355 3970 3306 -1 50 44 O
ATOM 1411 CB CYS A 185 22.265 -3.879 27.692 1.00 27.28 C
ANISOU 1411 CB CYS A 185 3290 3902 3174 -16 9 2 C
ATOM 1412 SG CYS A 185 21.865 -3.357 29.372 1.00 36.52 S
ANISOU 1412 SG CYS A 185 4487 5099 4288 11 -23 -18 S
ATOM 1413 N VAL A 186 24.574 -4.759 25.359 1.00 20.63 N
ANISOU 1413 N VAL A 186 2360 3056 2424 -41 42 -1 N
ATOM 1414 CA VAL A 186 24.695 -5.285 24.005 1.00 26.50 C
ANISOU 1414 CA VAL A 186 3096 3788 3185 -50 84 9 C
ATOM 1415 C VAL A 186 26.095 -5.838 23.778 1.00 28.05 C
ANISOU 1415 C VAL A 186 3235 4010 3413 -33 84 -6 C
ATOM 1416 O VAL A 186 26.261 -6.996 23.379 1.00 24.69 O
ANISOU 1416 O VAL A 186 2810 3581 2990 2 98 0 O
ATOM 1417 CB VAL A 186 24.357 -4.209 22.959 1.00 25.13 C
ANISOU 1417 CB VAL A 186 2934 3596 3019 -97 114 9 C
ATOM 1418 CG1 VAL A 186 24.655 -4.726 21.563 1.00 22.25 C
ANISOU 1418 CG1 VAL A 186 2562 3229 2661 -104 157 15 C
ATOM 1419 CG2 VAL A 186 22.900 -3.795 23.077 1.00 25.27 C
ANISOU 1419 CG2 VAL A 186 3002 3589 3010 -101 112 22 C
ATOM 1420 N LEU A 187 27.112 -5.016 24.036 1.00 26.08 N
ANISOU 1420 N LEU A 187 2997 5129 1784 -695 -23 -237 N
ATOM 1421 CA LEU A 187 28.473 -5.401 23.684 1.00 30.11 C
ANISOU 1421 CA LEU A 187 3443 5578 2418 -656 4 -325 C
ATOM 1422 C LEU A 187 28.951 -6.575 24.531 1.00 31.11 C
ANISOU 1422 C LEU A 187 3507 5650 2663 -589 -65 -252 C
ATOM 1423 O LEU A 187 29.502 -7.549 24.005 1.00 32.43 O
ANISOU 1423 O LEU A 187 3652 5717 2952 -569 -44 -292 O
ATOM 1424 CB LEU A 187 29.410 -4.202 23.827 1.00 36.29 C
ANISOU 1424 CB LEU A 187 4179 6438 3171 -646 28 -395 C
ATOM 1425 CG LEU A 187 30.815 -4.370 23.246 1.00 32.98 C
ANISOU 1425 CG LEU A 187 3693 5954 2883 -617 82 -503 C
ATOM 1426 CD1 LEU A 187 30.752 -4.818 21.793 1.00 36.96 C
ANISOU 1426 CD1 LEU A 187 4256 6359 3428 -648 177 -593 C
ATOM 1427 CD2 LEU A 187 31.595 -3.071 23.373 1.00 36.71 C
ANISOU 1427 CD2 LEU A 187 4119 6504 3324 -616 106 -568 C
ATOM 1428 N VAL A 188 28.737 -6.507 25.848 1.00 29.09 N
ANISOU 1428 N VAL A 188 3230 5456 2367 -549 -145 -141 N
ATOM 1429 CA VAL A 188 29.168 -7.598 26.726 1.00 31.34 C
ANISOU 1429 CA VAL A 188 3464 5691 2753 -478 -214 -67 C
ATOM 1430 C VAL A 188 28.471 -8.914 26.396 1.00 35.98 C
ANISOU 1430 C VAL A 188 4082 6180 3410 -487 -214 -17 C
ATOM 1431 O VAL A 188 29.158 -9.947 26.318 1.00 38.26 O
ANISOU 1431 O VAL A 188 4328 6383 3826 -447 -223 -31 O
ATOM 1432 CB VAL A 188 29.004 -7.189 28.201 1.00 31.65 C
ANISOU 1432 CB VAL A 188 3497 5813 2716 -427 -298 43 C
ATOM 1433 CG1 VAL A 188 29.079 -8.414 29.105 1.00 32.20 C
ANISOU 1433 CG1 VAL A 188 3543 5824 2867 -356 -366 143 C
ATOM 1434 CG2 VAL A 188 30.069 -6.180 28.590 1.00 31.28 C
ANISOU 1434 CG2 VAL A 188 3397 5834 2653 -398 -321 -18 C
ATOM 1435 N PRO A 189 27.145 -8.966 26.201 1.00 31.89 N
ANISOU 1435 N PRO A 189 3632 5661 2824 -536 -206 43 N
ATOM 1436 CA PRO A 189 26.542 -10.250 25.800 1.00 33.14 C
ANISOU 1436 CA PRO A 189 3813 5710 3068 -546 -209 81 C
ATOM 1437 C PRO A 189 27.044 -10.761 24.461 1.00 32.07 C
ANISOU 1437 C PRO A 189 3688 5478 3020 -570 -153 -40 C
ATOM 1438 O PRO A 189 27.187 -11.977 24.285 1.00 31.35 O
ANISOU 1438 O PRO A 189 3586 5286 3039 -547 -165 -28 O
ATOM 1439 CB PRO A 189 25.041 -9.935 25.766 1.00 34.93 C
ANISOU 1439 CB PRO A 189 4105 5964 3204 -602 -208 154 C
ATOM 1440 CG PRO A 189 24.876 -8.788 26.693 1.00 34.22 C
ANISOU 1440 CG PRO A 189 4017 5997 2988 -591 -227 209 C
ATOM 1441 CD PRO A 189 26.108 -7.958 26.496 1.00 30.32 C
ANISOU 1441 CD PRO A 189 3485 5554 2479 -576 -206 98 C
ATOM 1442 N LEU A 190 27.320 -9.867 23.508 1.00 31.58 N
ANISOU 1442 N LEU A 190 3654 5439 2906 -610 -87 -155 N
ATOM 1443 CA LEU A 190 27.848 -10.312 22.222 1.00 30.07 C
ANISOU 1443 CA LEU A 190 3487 5148 2789 -622 -23 -271 C
ATOM 1444 C LEU A 190 29.214 -10.964 22.384 1.00 30.41 C
ANISOU 1444 C LEU A 190 3452 5139 2962 -557 -19 -306 C
ATOM 1445 O LEU A 190 29.500 -11.986 21.750 1.00 27.96 O
ANISOU 1445 O LEU A 190 3152 4718 2752 -543 1 -340 O
ATOM 1446 CB LEU A 190 27.926 -9.141 21.244 1.00 27.99 C
ANISOU 1446 CB LEU A 190 3275 4923 2438 -667 55 -384 C
ATOM 1447 CG LEU A 190 26.611 -8.662 20.626 1.00 33.75 C
ANISOU 1447 CG LEU A 190 4101 5666 3058 -736 65 -384 C
ATOM 1448 CD1 LEU A 190 26.876 -7.476 19.718 1.00 34.15 C
ANISOU 1448 CD1 LEU A 190 4198 5754 3022 -769 147 -501 C
ATOM 1449 CD2 LEU A 190 25.920 -9.785 19.863 1.00 28.06 C
ANISOU 1449 CD2 LEU A 190 3443 4820 2399 -755 52 -382 C
ATOM 1450 N LEU A 191 30.073 -10.389 23.229 1.00 32.72 N
ANISOU 1450 N LEU A 191 3668 5505 3258 -516 -42 -300 N
ATOM 1451 CA LEU A 191 31.371 -11.004 23.484 1.00 35.73 C
ANISOU 1451 CA LEU A 191 3964 5836 3774 -451 -50 -326 C
ATOM 1452 C LEU A 191 31.213 -12.349 24.180 1.00 36.69 C
ANISOU 1452 C LEU A 191 4065 5897 3978 -406 -118 -230 C
ATOM 1453 O LEU A 191 31.992 -13.278 23.935 1.00 33.35 O
ANISOU 1453 O LEU A 191 3605 5386 3682 -367 -108 -259 O
ATOM 1454 CB LEU A 191 32.244 -10.066 24.317 1.00 28.23 C
ANISOU 1454 CB LEU A 191 2937 4977 2812 -416 -79 -334 C
ATOM 1455 CG LEU A 191 32.584 -8.721 23.674 1.00 37.02 C
ANISOU 1455 CG LEU A 191 4056 6148 3862 -454 -7 -434 C
ATOM 1456 CD1 LEU A 191 33.455 -7.892 24.604 1.00 37.21 C
ANISOU 1456 CD1 LEU A 191 3994 6251 3891 -415 -55 -434 C
ATOM 1457 CD2 LEU A 191 33.264 -8.918 22.327 1.00 29.92 C
ANISOU 1457 CD2 LEU A 191 3165 5157 3046 -465 102 -554 C
ATOM 1458 N LEU A 192 30.209 -12.472 25.052 1.00 30.22 N
ANISOU 1458 N LEU A 192 3271 5119 3093 -408 -183 -111 N
ATOM 1459 CA LEU A 192 29.938 -13.758 25.687 1.00 29.45 C
ANISOU 1459 CA LEU A 192 3162 4957 3070 -366 -239 -13 C
ATOM 1460 C LEU A 192 29.501 -14.796 24.663 1.00 35.06 C
ANISOU 1460 C LEU A 192 3920 5550 3851 -398 -205 -39 C
ATOM 1461 O LEU A 192 29.930 -15.954 24.722 1.00 30.62 O
ANISOU 1461 O LEU A 192 3331 4902 3402 -356 -221 -24 O
ATOM 1462 CB LEU A 192 28.876 -13.596 26.774 1.00 31.99 C
ANISOU 1462 CB LEU A 192 3510 5341 3302 -362 -297 123 C
ATOM 1463 CG LEU A 192 29.311 -12.865 28.044 1.00 37.19 C
ANISOU 1463 CG LEU A 192 4133 6099 3900 -307 -354 176 C
ATOM 1464 CD1 LEU A 192 28.125 -12.625 28.964 1.00 38.41 C
ANISOU 1464 CD1 LEU A 192 4336 6308 3950 -306 -390 309 C
ATOM 1465 CD2 LEU A 192 30.396 -13.652 28.762 1.00 40.67 C
ANISOU 1465 CD2 LEU A 192 4505 6497 4450 -221 -408 191 C
ATOM 1466 N MET A 193 28.642 -14.403 23.717 1.00 32.71 N
ANISOU 1466 N MET A 193 3698 5243 3487 -468 -163 -80 N
ATOM 1467 CA MET A 193 28.246 -15.326 22.658 1.00 33.77 C
ANISOU 1467 CA MET A 193 3889 5257 3684 -496 -139 -117 C
ATOM 1468 C MET A 193 29.450 -15.760 21.833 1.00 30.17 C
ANISOU 1468 C MET A 193 3418 4721 3325 -466 -83 -227 C
ATOM 1469 O MET A 193 29.551 -16.926 21.436 1.00 30.94 O
ANISOU 1469 O MET A 193 3529 4708 3519 -449 -85 -230 O
ATOM 1470 CB MET A 193 27.190 -14.684 21.760 1.00 35.89 C
ANISOU 1470 CB MET A 193 4248 5531 3858 -571 -110 -155 C
ATOM 1471 CG MET A 193 25.943 -14.234 22.488 1.00 37.58 C
ANISOU 1471 CG MET A 193 4478 5817 3983 -604 -156 -47 C
ATOM 1472 SD MET A 193 24.808 -13.379 21.382 1.00 37.00 S
ANISOU 1472 SD MET A 193 4505 5752 3802 -692 -124 -105 S
ATOM 1473 CE MET A 193 23.858 -12.418 22.556 1.00 36.67 C
ANISOU 1473 CE MET A 193 4448 5843 3642 -709 -160 17 C
ATOM 1474 N LEU A 194 30.374 -14.835 21.565 1.00 29.97 N
ANISOU 1474 N LEU A 194 3364 4744 3279 -458 -28 -315 N
ATOM 1475 CA LEU A 194 31.598 -15.203 20.861 1.00 37.17 C
ANISOU 1475 CA LEU A 194 4250 5579 4295 -422 36 -411 C
ATOM 1476 C LEU A 194 32.383 -16.251 21.639 1.00 31.62 C
ANISOU 1476 C LEU A 194 3463 4833 3719 -353 -11 -359 C
ATOM 1477 O LEU A 194 32.898 -17.212 21.056 1.00 38.24 O
ANISOU 1477 O LEU A 194 4305 5563 4660 -327 20 -396 O
ATOM 1478 CB LEU A 194 32.458 -13.964 20.611 1.00 36.27 C
ANISOU 1478 CB LEU A 194 4101 5529 4149 -423 102 -500 C
ATOM 1479 CG LEU A 194 33.829 -14.213 19.978 1.00 45.41 C
ANISOU 1479 CG LEU A 194 5214 6611 5427 -380 180 -594 C
ATOM 1480 CD1 LEU A 194 33.690 -14.718 18.548 1.00 45.24 C
ANISOU 1480 CD1 LEU A 194 5295 6470 5423 -396 263 -674 C
ATOM 1481 CD2 LEU A 194 34.680 -12.955 20.032 1.00 46.12 C
ANISOU 1481 CD2 LEU A 194 5244 6776 5503 -376 230 -659 C
ATOM 1482 N GLY A 195 32.475 -16.090 22.960 1.00 32.13 N
ANISOU 1482 N GLY A 195 3459 4976 3773 -319 -86 -273 N
ATOM 1483 CA GLY A 195 33.201 -17.060 23.763 1.00 36.88 C
ANISOU 1483 CA GLY A 195 3987 5539 4487 -248 -139 -221 C
ATOM 1484 C GLY A 195 32.515 -18.412 23.815 1.00 33.00 C
ANISOU 1484 C GLY A 195 3532 4961 4047 -241 -174 -147 C
ATOM 1485 O GLY A 195 33.178 -19.452 23.830 1.00 39.89 O
ANISOU 1485 O GLY A 195 4370 5752 5035 -194 -180 -148 O
ATOM 1486 N VAL A 196 31.182 -18.417 23.842 1.00 32.47 N
ANISOU 1486 N VAL A 196 3532 4905 3901 -289 -197 -82 N
ATOM 1487 CA VAL A 196 30.442 -19.675 23.892 1.00 32.94 C
ANISOU 1487 CA VAL A 196 3623 4877 4018 -288 -232 -8 C
ATOM 1488 C VAL A 196 30.619 -20.447 22.590 1.00 33.41 C
ANISOU 1488 C VAL A 196 3731 4811 4151 -305 -181 -93 C
ATOM 1489 O VAL A 196 30.904 -21.650 22.597 1.00 34.23 O
ANISOU 1489 O VAL A 196 3823 4824 4359 -269 -196 -72 O
ATOM 1490 CB VAL A 196 28.958 -19.410 24.201 1.00 33.37 C
ANISOU 1490 CB VAL A 196 3729 4968 3982 -338 -264 82 C
ATOM 1491 CG1 VAL A 196 28.150 -20.690 24.079 1.00 32.83 C
ANISOU 1491 CG1 VAL A 196 3692 4793 3988 -347 -293 149 C
ATOM 1492 CG2 VAL A 196 28.807 -18.818 25.596 1.00 32.02 C
ANISOU 1492 CG2 VAL A 196 3518 4905 3742 -305 -314 183 C
ATOM 1493 N TYR A 197 30.460 -19.767 21.451 1.00 32.93 N
ANISOU 1493 N TYR A 197 3736 4741 4033 -356 -119 -191 N
ATOM 1494 CA TYR A 197 30.637 -20.443 20.169 1.00 33.41 C
ANISOU 1494 CA TYR A 197 3865 4678 4152 -364 -68 -277 C
ATOM 1495 C TYR A 197 32.076 -20.911 19.983 1.00 34.23 C
ANISOU 1495 C TYR A 197 3914 4728 4363 -301 -21 -338 C
ATOM 1496 O TYR A 197 32.313 -21.983 19.415 1.00 34.98 O
ANISOU 1496 O TYR A 197 4039 4707 4544 -280 -7 -359 O
ATOM 1497 CB TYR A 197 30.205 -19.530 19.021 1.00 32.76 C
ANISOU 1497 CB TYR A 197 3875 4597 3974 -421 -10 -371 C
ATOM 1498 CG TYR A 197 28.704 -19.484 18.832 1.00 34.14 C
ANISOU 1498 CG TYR A 197 4126 4767 4079 -484 -58 -325 C
ATOM 1499 CD1 TYR A 197 28.013 -20.588 18.345 1.00 36.49 C
ANISOU 1499 CD1 TYR A 197 4484 4945 4435 -497 -95 -305 C
ATOM 1500 CD2 TYR A 197 27.978 -18.340 19.138 1.00 32.03 C
ANISOU 1500 CD2 TYR A 197 3867 4607 3694 -529 -68 -301 C
ATOM 1501 CE1 TYR A 197 26.641 -20.554 18.173 1.00 33.41 C
ANISOU 1501 CE1 TYR A 197 4154 4542 4001 -555 -145 -262 C
ATOM 1502 CE2 TYR A 197 26.605 -18.297 18.967 1.00 30.88 C
ANISOU 1502 CE2 TYR A 197 3783 4452 3497 -586 -112 -256 C
ATOM 1503 CZ TYR A 197 25.942 -19.406 18.485 1.00 35.06 C
ANISOU 1503 CZ TYR A 197 4364 4859 4098 -600 -152 -237 C
ATOM 1504 OH TYR A 197 24.578 -19.364 18.315 1.00 34.14 O
ANISOU 1504 OH TYR A 197 4299 4723 3948 -657 -202 -193 O
ATOM 1505 N LEU A 198 33.049 -20.132 20.461 1.00 35.22 N
ANISOU 1505 N LEU A 198 3958 4932 4492 -271 1 -364 N
ATOM 1506 CA LEU A 198 34.434 -20.592 20.411 1.00 35.01 C
ANISOU 1506 CA LEU A 198 3861 4854 4587 -208 39 -410 C
ATOM 1507 C LEU A 198 34.618 -21.859 21.236 1.00 35.80 C
ANISOU 1507 C LEU A 198 3910 4908 4785 -155 -31 -325 C
ATOM 1508 O LEU A 198 35.352 -22.769 20.835 1.00 36.65 O
ANISOU 1508 O LEU A 198 4005 4919 5002 -114 0 -356 O
ATOM 1509 CB LEU A 198 35.380 -19.493 20.891 1.00 34.82 C
ANISOU 1509 CB LEU A 198 3747 4924 4560 -186 57 -445 C
ATOM 1510 CG LEU A 198 35.685 -18.408 19.857 1.00 43.60 C
ANISOU 1510 CG LEU A 198 4896 6046 5623 -219 160 -557 C
ATOM 1511 CD1 LEU A 198 36.414 -17.243 20.500 1.00 49.04 C
ANISOU 1511 CD1 LEU A 198 5491 6840 6301 -206 159 -574 C
ATOM 1512 CD2 LEU A 198 36.499 -18.978 18.706 1.00 40.54 C
ANISOU 1512 CD2 LEU A 198 4537 5533 5331 -192 262 -647 C
ATOM 1513 N ARG A 199 33.948 -21.943 22.388 1.00 35.57 N
ANISOU 1513 N ARG A 199 3855 4943 4717 -151 -119 -214 N
ATOM 1514 CA ARG A 199 34.008 -23.165 23.182 1.00 37.33 C
ANISOU 1514 CA ARG A 199 4041 5118 5023 -100 -182 -126 C
ATOM 1515 C ARG A 199 33.265 -24.309 22.505 1.00 36.67 C
ANISOU 1515 C ARG A 199 4034 4920 4979 -122 -180 -110 C
ATOM 1516 O ARG A 199 33.628 -25.477 22.691 1.00 37.50 O
ANISOU 1516 O ARG A 199 4118 4946 5184 -77 -200 -79 O
ATOM 1517 CB ARG A 199 33.442 -22.918 24.581 1.00 36.03 C
ANISOU 1517 CB ARG A 199 3845 5045 4798 -83 -266 -8 C
ATOM 1518 CG ARG A 199 34.283 -21.994 25.447 1.00 44.39 C
ANISOU 1518 CG ARG A 199 4826 6205 5837 -42 -294 -13 C
ATOM 1519 CD ARG A 199 33.680 -21.842 26.835 1.00 46.82 C
ANISOU 1519 CD ARG A 199 5124 6588 6075 -14 -378 110 C
ATOM 1520 N ILE A 200 32.227 -24.000 21.724 1.00 36.09 N
ANISOU 1520 N ILE A 200 4051 4831 4832 -191 -164 -130 N
ATOM 1521 CA ILE A 200 31.504 -25.043 21.001 1.00 36.96 C
ANISOU 1521 CA ILE A 200 4239 4822 4983 -215 -172 -124 C
ATOM 1522 C ILE A 200 32.401 -25.675 19.945 1.00 37.20 C
ANISOU 1522 C ILE A 200 4300 4740 5094 -188 -107 -222 C
ATOM 1523 O ILE A 200 32.518 -26.903 19.856 1.00 37.99 O
ANISOU 1523 O ILE A 200 4408 4740 5285 -158 -124 -199 O
ATOM 1524 CB ILE A 200 30.217 -24.473 20.379 1.00 35.73 C
ANISOU 1524 CB ILE A 200 4171 4672 4731 -293 -177 -132 C
ATOM 1525 CG1 ILE A 200 29.191 -24.167 21.470 1.00 36.33 C
ANISOU 1525 CG1 ILE A 200 4220 4832 4752 -314 -242 -11 C
ATOM 1526 CG2 ILE A 200 29.645 -25.438 19.352 1.00 36.21 C
ANISOU 1526 CG2 ILE A 200 4325 4592 4840 -317 -182 -161 C
ATOM 1527 CD1 ILE A 200 27.885 -23.623 20.941 1.00 34.52 C
ANISOU 1527 CD1 ILE A 200 4067 4609 4441 -391 -254 -8 C
ATOM 1528 N PHE A 201 33.052 -24.842 19.131 1.00 36.98 N
ANISOU 1528 N PHE A 201 4293 4723 5035 -193 -27 -330 N
ATOM 1529 CA PHE A 201 33.943 -25.356 18.098 1.00 37.70 C
ANISOU 1529 CA PHE A 201 4422 4704 5199 -160 52 -422 C
ATOM 1530 C PHE A 201 35.164 -26.045 18.695 1.00 40.40 C
ANISOU 1530 C PHE A 201 4662 5026 5664 -86 56 -405 C
ATOM 1531 O PHE A 201 35.665 -27.019 18.120 1.00 40.19 O
ANISOU 1531 O PHE A 201 4662 4884 5723 -51 90 -435 O
ATOM 1532 CB PHE A 201 34.367 -24.220 17.169 1.00 37.29 C
ANISOU 1532 CB PHE A 201 4412 4672 5085 -178 149 -534 C
ATOM 1533 CG PHE A 201 33.223 -23.594 16.422 1.00 36.55 C
ANISOU 1533 CG PHE A 201 4433 4582 4872 -245 149 -565 C
ATOM 1534 CD1 PHE A 201 32.322 -24.381 15.723 1.00 37.62 C
ANISOU 1534 CD1 PHE A 201 4679 4612 5003 -271 116 -565 C
ATOM 1535 CD2 PHE A 201 33.040 -22.221 16.432 1.00 35.66 C
ANISOU 1535 CD2 PHE A 201 4318 4574 4655 -282 176 -596 C
ATOM 1536 CE1 PHE A 201 31.259 -23.808 15.039 1.00 40.41 C
ANISOU 1536 CE1 PHE A 201 5137 4962 5253 -332 104 -596 C
ATOM 1537 CE2 PHE A 201 31.980 -21.642 15.751 1.00 35.80 C
ANISOU 1537 CE2 PHE A 201 4443 4596 4564 -343 172 -625 C
ATOM 1538 CZ PHE A 201 31.089 -22.437 15.053 1.00 35.75 C
ANISOU 1538 CZ PHE A 201 4546 4482 4557 -367 134 -626 C
ATOM 1539 N LEU A 202 35.654 -25.561 19.841 1.00 42.15 N
ANISOU 1539 N LEU A 202 4772 5351 5894 -58 19 -357 N
ATOM 1540 CA LEU A 202 36.765 -26.232 20.511 1.00 40.90 C
ANISOU 1540 CA LEU A 202 4513 5173 5855 15 4 -334 C
ATOM 1541 C LEU A 202 36.351 -27.606 21.019 1.00 39.96 C
ANISOU 1541 C LEU A 202 4400 4990 5795 40 -64 -246 C
ATOM 1542 O LEU A 202 37.125 -28.566 20.932 1.00 40.74 O
ANISOU 1542 O LEU A 202 4471 5006 6003 93 -50 -254 O
ATOM 1543 CB LEU A 202 37.285 -25.374 21.665 1.00 39.43 C
ANISOU 1543 CB LEU A 202 4217 5108 5656 41 -41 -302 C
ATOM 1544 CG LEU A 202 38.181 -24.188 21.306 1.00 51.41 C
ANISOU 1544 CG LEU A 202 5688 6675 7173 41 29 -393 C
ATOM 1545 CD1 LEU A 202 38.483 -23.360 22.544 1.00 59.77 C
ANISOU 1545 CD1 LEU A 202 6650 7854 8206 62 -42 -349 C
ATOM 1546 CD2 LEU A 202 39.466 -24.669 20.653 1.00 51.83 C
ANISOU 1546 CD2 LEU A 202 5701 6633 7360 91 111 -467 C
ATOM 1547 N ALA A 203 35.135 -27.719 21.556 1.00 39.40 N
ANISOU 1547 N ALA A 203 4361 4950 5658 5 -135 -159 N
ATOM 1548 CA ALA A 203 34.660 -29.013 22.033 1.00 39.97 C
ANISOU 1548 CA ALA A 203 4440 4955 5790 26 -194 -70 C
ATOM 1549 C ALA A 203 34.479 -29.993 20.881 1.00 40.50 C
ANISOU 1549 C ALA A 203 4595 4882 5911 13 -160 -116 C
ATOM 1550 O ALA A 203 34.822 -31.174 21.003 1.00 42.16 O
ANISOU 1550 O ALA A 203 4793 5011 6216 57 -174 -88 O
ATOM 1551 CB ALA A 203 33.353 -28.844 22.805 1.00 39.39 C
ANISOU 1551 CB ALA A 203 4385 4940 5642 -11 -263 36 C
ATOM 1552 N ALA A 204 33.945 -29.520 19.753 1.00 40.07 N
ANISOU 1552 N ALA A 204 4636 4796 5793 -43 -118 -189 N
ATOM 1553 CA ALA A 204 33.758 -30.395 18.601 1.00 40.62 C
ANISOU 1553 CA ALA A 204 4807 4724 5902 -51 -92 -241 C
ATOM 1554 C ALA A 204 35.094 -30.847 18.025 1.00 41.43 C
ANISOU 1554 C ALA A 204 4899 4751 6090 9 -14 -316 C
ATOM 1555 O ALA A 204 35.261 -32.024 17.682 1.00 42.23 O
ANISOU 1555 O ALA A 204 5036 4740 6271 39 -15 -313 O
ATOM 1556 CB ALA A 204 32.928 -29.685 17.535 1.00 40.01 C
ANISOU 1556 CB ALA A 204 4844 4630 5729 -117 -69 -308 C
ATOM 1557 N ARG A 205 36.057 -29.930 17.913 1.00 41.27 N
ANISOU 1557 N ARG A 205 4829 4788 6063 30 57 -382 N
ATOM 1558 CA ARG A 205 37.363 -30.300 17.379 1.00 43.82 C
ANISOU 1558 CA ARG A 205 5132 5038 6481 90 142 -449 C
ATOM 1559 C ARG A 205 38.061 -31.308 18.285 1.00 46.87 C
ANISOU 1559 C ARG A 205 5420 5406 6982 154 100 -384 C
ATOM 1560 O ARG A 205 38.756 -32.211 17.803 1.00 48.68 O
ANISOU 1560 O ARG A 205 5664 5530 7303 200 144 -411 O
ATOM 1561 CB ARG A 205 38.227 -29.052 17.194 1.00 41.78 C
ANISOU 1561 CB ARG A 205 4822 4848 6206 97 223 -522 C
ATOM 1562 CG ARG A 205 39.538 -29.308 16.470 1.00 48.71 C
ANISOU 1562 CG ARG A 205 5687 5638 7184 156 334 -599 C
ATOM 1563 CD ARG A 205 40.461 -28.104 16.546 1.00 53.75 C
ANISOU 1563 CD ARG A 205 6237 6351 7835 167 404 -653 C
ATOM 1564 NE ARG A 205 40.921 -27.855 17.907 1.00 51.86 N
ANISOU 1564 NE ARG A 205 5847 6214 7642 191 326 -591 N
ATOM 1565 CZ ARG A 205 41.874 -26.990 18.227 1.00 55.37 C
ANISOU 1565 CZ ARG A 205 6184 6719 8135 213 359 -624 C
ATOM 1566 NH1 ARG A 205 42.493 -26.271 17.305 1.00 49.56 N
ANISOU 1566 NH1 ARG A 205 5464 5954 7414 214 482 -714 N
ATOM 1567 NH2 ARG A 205 42.220 -26.848 19.505 1.00 46.82 N
ANISOU 1567 NH2 ARG A 205 4979 5722 7090 239 267 -564 N
ATOM 1568 N ARG A 206 37.879 -31.178 19.602 1.00 43.84 N
ANISOU 1568 N ARG A 206 4944 5120 6592 161 14 -295 N
ATOM 1569 CA ARG A 206 38.522 -32.101 20.531 1.00 43.39 C
ANISOU 1569 CA ARG A 206 4800 5049 6637 228 -33 -231 C
ATOM 1570 C ARG A 206 37.870 -33.478 20.485 1.00 43.90 C
ANISOU 1570 C ARG A 206 4924 5016 6740 231 -76 -172 C
ATOM 1571 O ARG A 206 38.565 -34.500 20.516 1.00 44.78 O
ANISOU 1571 O ARG A 206 5012 5050 6953 286 -68 -166 O
ATOM 1572 CB ARG A 206 38.482 -31.530 21.951 1.00 48.36 C
ANISOU 1572 CB ARG A 206 5334 5805 7235 243 -114 -154 C
ATOM 1573 CG ARG A 206 39.169 -32.403 22.993 1.00 54.52 C
ANISOU 1573 CG ARG A 206 6028 6575 8112 320 -172 -89 C
ATOM 1574 CD ARG A 206 39.211 -31.738 24.367 1.00 74.67 C
ANISOU 1574 CD ARG A 206 8500 9247 10624 345 -252 -22 C
ATOM 1575 NE ARG A 206 40.023 -30.525 24.382 1.00 81.76 N
ANISOU 1575 NE ARG A 206 9332 10220 11514 349 -226 -89 N
ATOM 1576 CZ ARG A 206 39.538 -29.296 24.497 1.00 76.91 C
ANISOU 1576 CZ ARG A 206 8726 9702 10792 303 -232 -98 C
ATOM 1577 NH1 ARG A 206 38.239 -29.073 24.620 1.00 74.14 N
ANISOU 1577 NH1 ARG A 206 8448 9390 10332 249 -261 -43 N
ATOM 1578 NH2 ARG A 206 40.379 -28.263 24.495 1.00 74.67 N
ANISOU 1578 NH2 ARG A 206 8376 9476 10521 311 -208 -162 N
ATOM 1579 N GLN A 207 36.538 -33.525 20.404 1.00 43.50 N
ANISOU 1579 N GLN A 207 4948 4963 6617 172 -122 -129 N
ATOM 1580 CA GLN A 207 35.845 -34.810 20.370 1.00 43.90 C
ANISOU 1580 CA GLN A 207 5050 4915 6713 170 -169 -70 C
ATOM 1581 C GLN A 207 36.097 -35.546 19.060 1.00 46.78 C
ANISOU 1581 C GLN A 207 5511 5140 7124 175 -112 -149 C
ATOM 1582 O GLN A 207 36.235 -36.775 19.052 1.00 49.74 O
ANISOU 1582 O GLN A 207 5899 5421 7581 209 -128 -120 O
ATOM 1583 CB GLN A 207 34.347 -34.605 20.591 1.00 45.89 C
ANISOU 1583 CB GLN A 207 5350 5196 6892 103 -231 -3 C
ATOM 1584 CG GLN A 207 33.989 -34.088 21.972 1.00 42.77 C
ANISOU 1584 CG GLN A 207 4876 4922 6454 109 -289 96 C
ATOM 1585 CD GLN A 207 32.499 -33.885 22.150 1.00 45.38 C
ANISOU 1585 CD GLN A 207 5251 5270 6722 44 -338 166 C
ATOM 1586 OE1 GLN A 207 31.691 -34.435 21.402 1.00 44.61 O
ANISOU 1586 OE1 GLN A 207 5231 5079 6641 1 -350 159 O
ATOM 1587 NE2 GLN A 207 32.126 -33.087 23.145 1.00 43.30 N
ANISOU 1587 NE2 GLN A 207 4939 5122 6390 40 -368 234 N
ATOM 1588 N LEU A 208 36.152 -34.817 17.942 1.00 45.97 N
ANISOU 1588 N LEU A 208 5485 5017 6965 145 -43 -248 N
ATOM 1589 CA LEU A 208 36.453 -35.454 16.663 1.00 44.87 C
ANISOU 1589 CA LEU A 208 5454 4737 6858 160 19 -327 C
ATOM 1590 C LEU A 208 37.866 -36.019 16.650 1.00 47.04 C
ANISOU 1590 C LEU A 208 5671 4965 7238 239 85 -354 C
ATOM 1591 O LEU A 208 38.116 -37.072 16.052 1.00 51.54 O
ANISOU 1591 O LEU A 208 6303 5409 7869 272 107 -372 O
ATOM 1592 CB LEU A 208 36.262 -34.460 15.518 1.00 44.38 C
ANISOU 1592 CB LEU A 208 5492 4666 6704 122 86 -427 C
ATOM 1593 CG LEU A 208 34.824 -34.215 15.054 1.00 60.87 C
ANISOU 1593 CG LEU A 208 7687 6739 8702 48 26 -425 C
ATOM 1594 CD1 LEU A 208 34.773 -33.087 14.034 1.00 51.12 C
ANISOU 1594 CD1 LEU A 208 6542 5513 7369 20 97 -526 C
ATOM 1595 CD2 LEU A 208 34.225 -35.488 14.474 1.00 52.32 C
ANISOU 1595 CD2 LEU A 208 6706 5509 7663 46 -22 -415 C
ATOM 1596 N ALA A1001 38.807 -35.334 17.304 1.00 49.14 N
ANISOU 1596 N ALA A1001 5816 5324 7531 272 113 -358 N
ATOM 1597 CA ALA A1001 40.170 -35.848 17.379 1.00 51.64 C
ANISOU 1597 CA ALA A1001 6060 5598 7964 348 169 -378 C
ATOM 1598 C ALA A1001 40.244 -37.081 18.270 1.00 57.13 C
ANISOU 1598 C ALA A1001 6699 6265 8741 390 95 -290 C
ATOM 1599 O ALA A1001 41.004 -38.014 17.986 1.00 54.16 O
ANISOU 1599 O ALA A1001 6323 5796 8460 445 133 -304 O
ATOM 1600 CB ALA A1001 41.115 -34.759 17.883 1.00 46.31 C
ANISOU 1600 CB ALA A1001 5263 5026 7308 369 205 -404 C
ATOM 1601 N ASP A1002 39.457 -37.106 19.350 1.00 51.05 N
ANISOU 1601 N ASP A1002 5888 5574 7937 369 -6 -197 N
ATOM 1602 CA ASP A1002 39.449 -38.265 20.236 1.00 54.11 C
ANISOU 1602 CA ASP A1002 6230 5934 8395 411 -75 -107 C
ATOM 1603 C ASP A1002 38.858 -39.493 19.554 1.00 56.24 C
ANISOU 1603 C ASP A1002 6604 6070 8693 402 -82 -98 C
ATOM 1604 O ASP A1002 39.287 -40.618 19.832 1.00 53.26 O
ANISOU 1604 O ASP A1002 6207 5627 8404 453 -95 -62 O
ATOM 1605 CB ASP A1002 38.678 -37.942 21.516 1.00 46.85 C
ANISOU 1605 CB ASP A1002 5258 5122 7422 395 -168 -7 C
ATOM 1606 CG ASP A1002 39.386 -36.913 22.380 1.00 58.43 C
ANISOU 1606 CG ASP A1002 6615 6712 8874 423 -180 -7 C
ATOM 1607 OD1 ASP A1002 40.540 -36.556 22.062 1.00 61.77 O
ANISOU 1607 OD1 ASP A1002 6986 7133 9352 457 -121 -79 O
ATOM 1608 OD2 ASP A1002 38.786 -36.460 23.377 1.00 65.45 O
ANISOU 1608 OD2 ASP A1002 7472 7694 9702 412 -249 67 O
ATOM 1609 N LEU A1003 37.878 -39.303 18.667 1.00 52.14 N
ANISOU 1609 N LEU A1003 6200 5506 8104 338 -80 -130 N
ATOM 1610 CA LEU A1003 37.337 -40.436 17.922 1.00 52.54 C
ANISOU 1610 CA LEU A1003 6359 5418 8186 329 -94 -131 C
ATOM 1611 C LEU A1003 38.392 -41.043 17.009 1.00 55.65 C
ANISOU 1611 C LEU A1003 6799 5700 8645 384 -9 -207 C
ATOM 1612 O LEU A1003 38.515 -42.270 16.919 1.00 54.08 O
ANISOU 1612 O LEU A1003 6629 5401 8519 418 -23 -182 O
ATOM 1613 CB LEU A1003 36.115 -40.004 17.114 1.00 52.72 C
ANISOU 1613 CB LEU A1003 6498 5412 8122 252 -118 -161 C
ATOM 1614 CG LEU A1003 34.824 -39.767 17.899 1.00 56.17 C
ANISOU 1614 CG LEU A1003 6911 5916 8515 194 -209 -70 C
ATOM 1615 CD1 LEU A1003 33.735 -39.238 16.980 1.00 51.50 C
ANISOU 1615 CD1 LEU A1003 6432 5292 7844 120 -227 -116 C
ATOM 1616 CD2 LEU A1003 34.373 -41.049 18.585 1.00 52.95 C
ANISOU 1616 CD2 LEU A1003 6480 5450 8188 210 -278 30 C
ATOM 1617 N GLU A1004 39.166 -40.198 16.324 1.00 58.58 N
ANISOU 1617 N GLU A1004 7180 6083 8995 397 86 -297 N
ATOM 1618 CA GLU A1004 40.236 -40.698 15.469 1.00 58.62 C
ANISOU 1618 CA GLU A1004 7225 5981 9066 457 185 -365 C
ATOM 1619 C GLU A1004 41.376 -41.290 16.288 1.00 57.76 C
ANISOU 1619 C GLU A1004 6988 5886 9074 530 195 -326 C
ATOM 1620 O GLU A1004 42.024 -42.245 15.844 1.00 59.56 O
ANISOU 1620 O GLU A1004 7246 6004 9379 584 241 -342 O
ATOM 1621 CB GLU A1004 40.751 -39.580 14.563 1.00 64.06 C
ANISOU 1621 CB GLU A1004 7954 6679 9708 454 295 -465 C
ATOM 1622 CG GLU A1004 39.709 -39.034 13.595 1.00 70.98 C
ANISOU 1622 CG GLU A1004 8979 7523 10467 392 293 -517 C
ATOM 1623 CD GLU A1004 39.254 -40.066 12.577 1.00 80.36 C
ANISOU 1623 CD GLU A1004 10330 8549 11654 399 288 -545 C
ATOM 1624 OE1 GLU A1004 40.070 -40.936 12.205 1.00 80.70 O
ANISOU 1624 OE1 GLU A1004 10397 8490 11774 463 346 -561 O
ATOM 1625 OE2 GLU A1004 38.081 -40.011 12.151 1.00 72.65 O
ANISOU 1625 OE2 GLU A1004 9460 7542 10602 342 222 -549 O
ATOM 1626 N ASP A1005 41.632 -40.745 17.480 1.00 57.40 N
ANISOU 1626 N ASP A1005 6803 5967 9041 538 148 -275 N
ATOM 1627 CA ASP A1005 42.678 -41.295 18.337 1.00 54.94 C
ANISOU 1627 CA ASP A1005 6368 5668 8838 610 139 -236 C
ATOM 1628 C ASP A1005 42.332 -42.708 18.790 1.00 60.51 C
ANISOU 1628 C ASP A1005 7090 6307 9594 634 71 -160 C
ATOM 1629 O ASP A1005 43.169 -43.615 18.721 1.00 61.19 O
ANISOU 1629 O ASP A1005 7156 6317 9777 697 103 -161 O
ATOM 1630 CB ASP A1005 42.910 -40.375 19.538 1.00 59.69 C
ANISOU 1630 CB ASP A1005 6835 6416 9429 613 84 -198 C
ATOM 1631 CG ASP A1005 43.617 -39.087 19.153 1.00 71.29 C
ANISOU 1631 CG ASP A1005 8259 7940 10888 608 162 -277 C
ATOM 1632 OD1 ASP A1005 44.002 -38.950 17.972 1.00 66.05 O
ANISOU 1632 OD1 ASP A1005 7664 7198 10233 609 269 -359 O
ATOM 1633 OD2 ASP A1005 43.787 -38.211 20.028 1.00 80.80 O
ANISOU 1633 OD2 ASP A1005 9365 9262 12076 606 117 -257 O
ATOM 1634 N ASN A1006 41.096 -42.918 19.254 1.00 56.14 N
ANISOU 1634 N ASN A1006 6571 5777 8982 586 -18 -90 N
ATOM 1635 CA ASN A1006 40.671 -44.262 19.634 1.00 60.37 C
ANISOU 1635 CA ASN A1006 7129 6240 9567 605 -77 -15 C
ATOM 1636 C ASN A1006 40.633 -45.196 18.433 1.00 61.43 C
ANISOU 1636 C ASN A1006 7388 6221 9731 609 -33 -63 C
ATOM 1637 O ASN A1006 40.918 -46.392 18.566 1.00 56.51 O
ANISOU 1637 O ASN A1006 6767 5518 9185 654 -44 -30 O
ATOM 1638 CB ASN A1006 39.301 -44.218 20.307 1.00 53.46 C
ANISOU 1638 CB ASN A1006 6268 5414 8631 550 -170 70 C
ATOM 1639 CG ASN A1006 39.369 -43.681 21.721 1.00 69.60 C
ANISOU 1639 CG ASN A1006 8196 7588 10659 570 -225 145 C
ATOM 1640 OD1 ASN A1006 40.399 -43.789 22.392 1.00 66.09 O
ANISOU 1640 OD1 ASN A1006 7660 7178 10274 638 -223 154 O
ATOM 1641 ND2 ASN A1006 38.265 -43.110 22.189 1.00 57.36 N
ANISOU 1641 ND2 ASN A1006 6655 6108 9031 516 -278 199 N
ATOM 1642 N TRP A1007 40.274 -44.674 17.259 1.00 57.92 N
ANISOU 1642 N TRP A1007 7054 5730 9222 566 14 -142 N
ATOM 1643 CA TRP A1007 40.205 -45.511 16.064 1.00 58.03 C
ANISOU 1643 CA TRP A1007 7207 5589 9251 574 52 -193 C
ATOM 1644 C TRP A1007 41.592 -45.971 15.632 1.00 59.54 C
ANISOU 1644 C TRP A1007 7386 5711 9525 654 151 -241 C
ATOM 1645 O TRP A1007 41.798 -47.150 15.320 1.00 60.58 O
ANISOU 1645 O TRP A1007 7572 5728 9716 693 156 -233 O
ATOM 1646 CB TRP A1007 39.515 -44.751 14.933 1.00 57.04 C
ANISOU 1646 CB TRP A1007 7214 5432 9028 517 76 -270 C
ATOM 1647 CG TRP A1007 39.568 -45.450 13.607 1.00 59.48 C
ANISOU 1647 CG TRP A1007 7684 5578 9339 537 123 -338 C
ATOM 1648 CD1 TRP A1007 40.358 -45.128 12.541 1.00 58.55 C
ANISOU 1648 CD1 TRP A1007 7646 5393 9207 575 239 -432 C
ATOM 1649 CD2 TRP A1007 38.801 -46.593 13.208 1.00 61.13 C
ANISOU 1649 CD2 TRP A1007 8002 5660 9565 525 55 -317 C
ATOM 1650 NE1 TRP A1007 40.127 -45.998 11.502 1.00 62.78 N
ANISOU 1650 NE1 TRP A1007 8346 5770 9740 592 247 -470 N
ATOM 1651 CE2 TRP A1007 39.176 -46.907 11.886 1.00 60.25 C
ANISOU 1651 CE2 TRP A1007 8043 5410 9439 560 128 -403 C
ATOM 1652 CE3 TRP A1007 37.833 -47.381 13.840 1.00 58.91 C
ANISOU 1652 CE3 TRP A1007 7706 5364 9314 491 -59 -231 C
ATOM 1653 CZ2 TRP A1007 38.618 -47.974 11.185 1.00 63.11 C
ANISOU 1653 CZ2 TRP A1007 8546 5620 9812 561 80 -410 C
ATOM 1654 CZ3 TRP A1007 37.281 -48.439 13.142 1.00 60.25 C
ANISOU 1654 CZ3 TRP A1007 8002 5383 9506 488 -104 -237 C
ATOM 1655 CH2 TRP A1007 37.674 -48.725 11.828 1.00 63.11 C
ANISOU 1655 CH2 TRP A1007 8520 5611 9850 522 -41 -328 C
ATOM 1656 N GLU A1008 42.561 -45.053 15.616 1.00 58.18 N
ANISOU 1656 N GLU A1008 7139 5602 9364 680 232 -290 N
ATOM 1657 CA GLU A1008 43.918 -45.422 15.231 1.00 63.67 C
ANISOU 1657 CA GLU A1008 7808 6231 10154 758 335 -332 C
ATOM 1658 C GLU A1008 44.606 -46.238 16.317 1.00 59.32 C
ANISOU 1658 C GLU A1008 7127 5700 9710 816 293 -261 C
ATOM 1659 O GLU A1008 45.445 -47.093 16.007 1.00 60.13 O
ANISOU 1659 O GLU A1008 7236 5710 9900 880 351 -272 O
ATOM 1660 CB GLU A1008 44.730 -44.170 14.900 1.00 63.18 C
ANISOU 1660 CB GLU A1008 7694 6224 10089 767 435 -402 C
ATOM 1661 CG GLU A1008 44.201 -43.391 13.705 1.00 72.26 C
ANISOU 1661 CG GLU A1008 8985 7336 11134 723 498 -481 C
ATOM 1662 CD GLU A1008 44.925 -42.075 13.497 1.00 83.49 C
ANISOU 1662 CD GLU A1008 10345 8826 12552 727 594 -542 C
ATOM 1663 OE1 GLU A1008 45.882 -41.794 14.249 1.00 84.50 O
ANISOU 1663 OE1 GLU A1008 10316 9021 12769 764 610 -525 O
ATOM 1664 OE2 GLU A1008 44.534 -41.318 12.583 1.00 87.19 O
ANISOU 1664 OE2 GLU A1008 10922 9275 12930 694 650 -608 O
ATOM 1665 N THR A1009 44.275 -45.990 17.587 1.00 57.80 N
ANISOU 1665 N THR A1009 6826 5627 9510 801 196 -188 N
ATOM 1666 CA THR A1009 44.789 -46.833 18.662 1.00 54.77 C
ANISOU 1666 CA THR A1009 6338 5256 9214 859 142 -116 C
ATOM 1667 C THR A1009 44.343 -48.277 18.479 1.00 60.18 C
ANISOU 1667 C THR A1009 7108 5829 9929 872 110 -74 C
ATOM 1668 O THR A1009 45.089 -49.212 18.794 1.00 60.57 O
ANISOU 1668 O THR A1009 7114 5829 10071 938 117 -48 O
ATOM 1669 CB THR A1009 44.329 -46.297 20.020 1.00 54.48 C
ANISOU 1669 CB THR A1009 6202 5356 9141 841 39 -42 C
ATOM 1670 OG1 THR A1009 44.790 -44.950 20.186 1.00 63.86 O
ANISOU 1670 OG1 THR A1009 7312 6646 10305 831 64 -84 O
ATOM 1671 CG2 THR A1009 44.875 -47.154 21.156 1.00 54.77 C
ANISOU 1671 CG2 THR A1009 6143 5404 9262 911 -20 32 C
ATOM 1672 N LEU A1010 43.132 -48.475 17.956 1.00 60.34 N
ANISOU 1672 N LEU A1010 7249 5801 9876 810 73 -68 N
ATOM 1673 CA LEU A1010 42.641 -49.821 17.690 1.00 62.46 C
ANISOU 1673 CA LEU A1010 7606 5951 10176 817 39 -34 C
ATOM 1674 C LEU A1010 43.447 -50.490 16.583 1.00 57.53 C
ANISOU 1674 C LEU A1010 7067 5191 9601 867 133 -100 C
ATOM 1675 O LEU A1010 43.845 -51.653 16.708 1.00 61.46 O
ANISOU 1675 O LEU A1010 7568 5612 10174 918 131 -70 O
ATOM 1676 CB LEU A1010 41.158 -49.767 17.320 1.00 59.38 C
ANISOU 1676 CB LEU A1010 7321 5534 9706 735 -28 -20 C
ATOM 1677 CG LEU A1010 40.415 -51.097 17.192 1.00 63.51 C
ANISOU 1677 CG LEU A1010 7925 5942 10264 728 -88 29 C
ATOM 1678 CD1 LEU A1010 40.081 -51.652 18.565 1.00 76.02 C
ANISOU 1678 CD1 LEU A1010 9409 7583 11892 740 -168 142 C
ATOM 1679 CD2 LEU A1010 39.157 -50.930 16.354 1.00 66.87 C
ANISOU 1679 CD2 LEU A1010 8480 6305 10622 651 -132 2 C
ATOM 1680 N ASN A1011 43.703 -49.767 15.491 1.00 59.19 N
ANISOU 1680 N ASN A1011 7355 5367 9768 858 222 -191 N
ATOM 1681 CA ASN A1011 44.363 -50.373 14.340 1.00 61.74 C
ANISOU 1681 CA ASN A1011 7788 5547 10124 908 320 -254 C
ATOM 1682 C ASN A1011 45.872 -50.485 14.520 1.00 60.45 C
ANISOU 1682 C ASN A1011 7521 5382 10065 991 414 -268 C
ATOM 1683 O ASN A1011 46.483 -51.420 13.990 1.00 65.57 O
ANISOU 1683 O ASN A1011 8225 5913 10775 1049 473 -281 O
ATOM 1684 CB ASN A1011 44.048 -49.575 13.075 1.00 63.23 C
ANISOU 1684 CB ASN A1011 8115 5687 10220 876 386 -344 C
ATOM 1685 CG ASN A1011 42.583 -49.635 12.703 1.00 64.28 C
ANISOU 1685 CG ASN A1011 8373 5787 10263 801 292 -339 C
ATOM 1686 OD1 ASN A1011 41.897 -50.614 12.995 1.00 65.05 O
ANISOU 1686 OD1 ASN A1011 8499 5834 10382 786 201 -282 O
ATOM 1687 ND2 ASN A1011 42.093 -48.584 12.056 1.00 63.44 N
ANISOU 1687 ND2 ASN A1011 8339 5703 10061 754 311 -399 N
ATOM 1688 N ASP A1012 46.491 -49.553 15.248 1.00 58.85 N
ANISOU 1688 N ASP A1012 7168 5301 9890 998 426 -265 N
ATOM 1689 CA ASP A1012 47.935 -49.626 15.446 1.00 65.17 C
ANISOU 1689 CA ASP A1012 7855 6096 10809 1076 506 -278 C
ATOM 1690 C ASP A1012 48.307 -50.752 16.400 1.00 66.24 C
ANISOU 1690 C ASP A1012 7906 6226 11036 1128 442 -203 C
ATOM 1691 O ASP A1012 49.281 -51.477 16.163 1.00 66.02 O
ANISOU 1691 O ASP A1012 7863 6116 11107 1198 510 -212 O
ATOM 1692 CB ASP A1012 48.469 -48.289 15.958 1.00 67.64 C
ANISOU 1692 CB ASP A1012 8030 6534 11134 1068 524 -299 C
ATOM 1693 CG ASP A1012 48.705 -47.295 14.842 1.00 72.99 C
ANISOU 1693 CG ASP A1012 8775 7185 11772 1053 646 -387 C
ATOM 1694 OD1 ASP A1012 48.898 -47.733 13.687 1.00 75.01 O
ANISOU 1694 OD1 ASP A1012 9162 7310 12026 1080 745 -436 O
ATOM 1695 OD2 ASP A1012 48.705 -46.078 15.118 1.00 74.59 O
ANISOU 1695 OD2 ASP A1012 8906 7494 11943 1019 645 -408 O
ATOM 1696 N ASN A1013 47.548 -50.914 17.486 1.00 66.08 N
ANISOU 1696 N ASN A1013 7834 6288 10985 1098 315 -127 N
ATOM 1697 CA ASN A1013 47.805 -52.017 18.403 1.00 67.67 C
ANISOU 1697 CA ASN A1013 7970 6478 11261 1149 252 -53 C
ATOM 1698 C ASN A1013 47.528 -53.373 17.767 1.00 65.03 C
ANISOU 1698 C ASN A1013 7762 6004 10944 1166 262 -42 C
ATOM 1699 O ASN A1013 48.059 -54.383 18.240 1.00 66.20 O
ANISOU 1699 O ASN A1013 7867 6113 11174 1225 249 1 O
ATOM 1700 CB ASN A1013 46.972 -51.856 19.675 1.00 67.29 C
ANISOU 1700 CB ASN A1013 7859 6543 11167 1117 124 30 C
ATOM 1701 CG ASN A1013 47.551 -50.829 20.628 1.00 67.33 C
ANISOU 1701 CG ASN A1013 7716 6679 11187 1134 96 36 C
ATOM 1702 OD1 ASN A1013 48.759 -50.595 20.647 1.00 64.46 O
ANISOU 1702 OD1 ASN A1013 7262 6318 10911 1188 149 0 O
ATOM 1703 ND2 ASN A1013 46.689 -50.216 21.432 1.00 69.37 N
ANISOU 1703 ND2 ASN A1013 7950 7043 11366 1088 9 84 N
ATOM 1704 N LEU A1014 46.709 -53.420 16.713 1.00 63.17 N
ANISOU 1704 N LEU A1014 7681 5689 10632 1116 280 -80 N
ATOM 1705 CA LEU A1014 46.534 -54.668 15.977 1.00 67.21 C
ANISOU 1705 CA LEU A1014 8325 6052 11162 1137 295 -82 C
ATOM 1706 C LEU A1014 47.820 -55.068 15.266 1.00 71.22 C
ANISOU 1706 C LEU A1014 8848 6465 11748 1217 420 -132 C
ATOM 1707 O LEU A1014 48.186 -56.249 15.253 1.00 68.78 O
ANISOU 1707 O LEU A1014 8562 6067 11503 1269 427 -105 O
ATOM 1708 CB LEU A1014 45.387 -54.538 14.975 1.00 65.82 C
ANISOU 1708 CB LEU A1014 8317 5806 10885 1070 277 -120 C
ATOM 1709 CG LEU A1014 43.963 -54.632 15.525 1.00 64.15 C
ANISOU 1709 CG LEU A1014 8122 5634 10620 996 148 -58 C
ATOM 1710 CD1 LEU A1014 42.945 -54.466 14.407 1.00 64.89 C
ANISOU 1710 CD1 LEU A1014 8384 5643 10628 935 132 -110 C
ATOM 1711 CD2 LEU A1014 43.755 -55.950 16.252 1.00 60.50 C
ANISOU 1711 CD2 LEU A1014 7635 5130 10223 1021 77 26 C
ATOM 1712 N LYS A1015 48.518 -54.099 14.669 1.00 68.61 N
ANISOU 1712 N LYS A1015 8504 6147 11418 1229 525 -201 N
ATOM 1713 CA LYS A1015 49.787 -54.399 14.017 1.00 68.46 C
ANISOU 1713 CA LYS A1015 8488 6036 11488 1310 659 -243 C
ATOM 1714 C LYS A1015 50.848 -54.815 15.025 1.00 66.18 C
ANISOU 1714 C LYS A1015 8027 5791 11329 1376 652 -196 C
ATOM 1715 O LYS A1015 51.714 -55.639 14.707 1.00 70.13 O
ANISOU 1715 O LYS A1015 8534 6194 11916 1448 726 -199 O
ATOM 1716 CB LYS A1015 50.270 -53.191 13.216 1.00 66.88 C
ANISOU 1716 CB LYS A1015 8301 5842 11267 1308 780 -322 C
ATOM 1717 CG LYS A1015 49.242 -52.617 12.257 1.00 73.21 C
ANISOU 1717 CG LYS A1015 9270 6612 11933 1244 783 -375 C
ATOM 1718 CD LYS A1015 49.845 -51.494 11.431 1.00 80.22 C
ANISOU 1718 CD LYS A1015 10178 7493 12808 1257 921 -453 C
ATOM 1719 CE LYS A1015 50.445 -50.420 12.325 1.00 74.56 C
ANISOU 1719 CE LYS A1015 9259 6921 12147 1248 921 -445 C
ATOM 1720 NZ LYS A1015 51.117 -49.346 11.543 1.00 75.13 N
ANISOU 1720 NZ LYS A1015 9337 6981 12228 1265 1066 -518 N
ATOM 1721 N VAL A1016 50.800 -54.258 16.238 1.00 62.52 N
ANISOU 1721 N VAL A1016 7412 5467 10877 1357 562 -153 N
ATOM 1722 CA VAL A1016 51.756 -54.638 17.275 1.00 64.51 C
ANISOU 1722 CA VAL A1016 7503 5761 11248 1423 533 -109 C
ATOM 1723 C VAL A1016 51.584 -56.106 17.644 1.00 71.75 C
ANISOU 1723 C VAL A1016 8455 6610 12194 1458 476 -46 C
ATOM 1724 O VAL A1016 52.564 -56.822 17.884 1.00 69.37 O
ANISOU 1724 O VAL A1016 8088 6265 12003 1533 507 -31 O
ATOM 1725 CB VAL A1016 51.603 -53.719 18.502 1.00 64.87 C
ANISOU 1725 CB VAL A1016 7406 5965 11278 1397 432 -76 C
ATOM 1726 CG1 VAL A1016 52.477 -54.201 19.651 1.00 63.29 C
ANISOU 1726 CG1 VAL A1016 7056 5802 11190 1468 376 -26 C
ATOM 1727 CG2 VAL A1016 51.945 -52.283 18.134 1.00 61.67 C
ANISOU 1727 CG2 VAL A1016 6952 5620 10860 1370 497 -141 C
ATOM 1728 N ILE A1017 50.338 -56.581 17.678 1.00 69.52 N
ANISOU 1728 N ILE A1017 8275 6314 11823 1404 394 -9 N
ATOM 1729 CA ILE A1017 50.078 -57.971 18.038 1.00 68.21 C
ANISOU 1729 CA ILE A1017 8148 6084 11686 1432 338 54 C
ATOM 1730 C ILE A1017 50.514 -58.908 16.918 1.00 66.02 C
ANISOU 1730 C ILE A1017 7992 5649 11444 1475 433 17 C
ATOM 1731 O ILE A1017 51.084 -59.976 17.171 1.00 77.25 O
ANISOU 1731 O ILE A1017 9395 7012 12945 1538 439 51 O
ATOM 1732 CB ILE A1017 48.591 -58.157 18.390 1.00 66.63 C
ANISOU 1732 CB ILE A1017 8014 5908 11394 1359 227 106 C
ATOM 1733 CG1 ILE A1017 48.219 -57.287 19.593 1.00 66.20 C
ANISOU 1733 CG1 ILE A1017 7840 6007 11307 1330 140 152 C
ATOM 1734 CG2 ILE A1017 48.282 -59.620 18.671 1.00 69.90 C
ANISOU 1734 CG2 ILE A1017 8475 6240 11843 1386 177 169 C
ATOM 1735 CD1 ILE A1017 46.739 -57.268 19.899 1.00 61.43 C
ANISOU 1735 CD1 ILE A1017 7293 5431 10615 1254 46 203 C
ATOM 1736 N GLU A1018 50.262 -58.524 15.664 1.00 68.16 N
ANISOU 1736 N GLU A1018 8398 5846 11654 1447 509 -51 N
ATOM 1737 CA GLU A1018 50.586 -59.400 14.542 1.00 73.68 C
ANISOU 1737 CA GLU A1018 9242 6384 12369 1491 597 -86 C
ATOM 1738 C GLU A1018 52.089 -59.586 14.377 1.00 77.75 C
ANISOU 1738 C GLU A1018 9684 6856 13002 1583 718 -106 C
ATOM 1739 O GLU A1018 52.531 -60.627 13.878 1.00 81.47 O
ANISOU 1739 O GLU A1018 10231 7205 13518 1640 774 -105 O
ATOM 1740 CB GLU A1018 49.980 -58.849 13.253 1.00 70.74 C
ANISOU 1740 CB GLU A1018 9042 5942 11896 1448 648 -158 C
ATOM 1741 CG GLU A1018 48.463 -58.815 13.244 1.00 83.21 C
ANISOU 1741 CG GLU A1018 10714 7533 13371 1361 529 -142 C
ATOM 1742 CD GLU A1018 47.907 -58.202 11.976 1.00 88.83 C
ANISOU 1742 CD GLU A1018 11595 8174 13981 1323 572 -220 C
ATOM 1743 OE1 GLU A1018 48.705 -57.691 11.162 1.00 97.98 O
ANISOU 1743 OE1 GLU A1018 12794 9289 15143 1365 703 -284 O
ATOM 1744 OE2 GLU A1018 46.673 -58.233 11.791 1.00 92.92 O
ANISOU 1744 OE2 GLU A1018 12208 8676 14421 1255 477 -215 O
ATOM 1745 N LYS A1019 52.886 -58.599 14.785 1.00 73.78 N
ANISOU 1745 N LYS A1019 9031 6444 12556 1598 760 -125 N
ATOM 1746 CA LYS A1019 54.334 -58.649 14.634 1.00 76.19 C
ANISOU 1746 CA LYS A1019 9248 6710 12993 1681 878 -145 C
ATOM 1747 C LYS A1019 55.057 -58.843 15.961 1.00 78.96 C
ANISOU 1747 C LYS A1019 9400 7147 13455 1724 809 -91 C
ATOM 1748 O LYS A1019 56.274 -58.642 16.027 1.00 86.47 O
ANISOU 1748 O LYS A1019 10234 8090 14531 1786 888 -107 O
ATOM 1749 CB LYS A1019 54.834 -57.377 13.944 1.00 74.77 C
ANISOU 1749 CB LYS A1019 9050 6542 12816 1676 996 -215 C
ATOM 1750 CG LYS A1019 54.256 -57.166 12.553 1.00 75.33 C
ANISOU 1750 CG LYS A1019 9331 6513 12779 1650 1079 -276 C
ATOM 1751 CD LYS A1019 54.873 -55.954 11.874 1.00 81.60 C
ANISOU 1751 CD LYS A1019 10105 7310 13589 1658 1215 -342 C
ATOM 1752 CE LYS A1019 54.356 -55.796 10.452 1.00 77.10 C
ANISOU 1752 CE LYS A1019 9762 6625 12906 1647 1305 -404 C
ATOM 1753 NZ LYS A1019 55.007 -54.657 9.749 1.00 73.32 N
ANISOU 1753 NZ LYS A1019 9275 6138 12447 1664 1456 -467 N
ATOM 1754 N ALA A1020 54.344 -59.229 17.014 1.00 75.27 N
ANISOU 1754 N ALA A1020 8894 6754 12952 1697 665 -26 N
ATOM 1755 CA ALA A1020 54.967 -59.419 18.312 1.00 85.17 C
ANISOU 1755 CA ALA A1020 9977 8088 14297 1744 588 26 C
ATOM 1756 C ALA A1020 55.706 -60.753 18.366 1.00 86.40 C
ANISOU 1756 C ALA A1020 10130 8147 14551 1826 616 56 C
ATOM 1757 O ALA A1020 55.451 -61.672 17.584 1.00 81.74 O
ANISOU 1757 O ALA A1020 9681 7440 13936 1835 663 54 O
ATOM 1758 CB ALA A1020 53.924 -59.352 19.428 1.00 74.41 C
ANISOU 1758 CB ALA A1020 8587 6832 12852 1695 434 88 C
ATOM 1759 N ASP A1021 56.639 -60.844 19.308 1.00 84.88 N
ANISOU 1759 N ASP A1021 9777 8002 14472 1888 581 83 N
ATOM 1760 CA ASP A1021 57.410 -62.059 19.546 1.00 98.15 C
ANISOU 1760 CA ASP A1021 11430 9608 16256 1971 595 117 C
ATOM 1761 C ASP A1021 57.237 -62.607 20.952 1.00 92.20 C
ANISOU 1761 C ASP A1021 10594 8927 15511 1996 452 190 C
ATOM 1762 O ASP A1021 57.230 -63.827 21.136 1.00 91.73 O
ANISOU 1762 O ASP A1021 10578 8804 15471 2037 432 234 O
ATOM 1763 CB ASP A1021 58.902 -61.803 19.279 1.00109.08 C
ANISOU 1763 CB ASP A1021 12696 10952 17796 2043 703 79 C
ATOM 1764 CG ASP A1021 59.189 -61.481 17.824 1.00106.12 C
ANISOU 1764 CG ASP A1021 12421 10476 17425 2040 871 14 C
ATOM 1765 OD1 ASP A1021 58.412 -61.923 16.951 1.00 98.66 O
ANISOU 1765 OD1 ASP A1021 11657 9452 16375 2008 908 3 O
ATOM 1766 OD2 ASP A1021 60.193 -60.789 17.554 1.00107.60 O
ANISOU 1766 OD2 ASP A1021 12506 10654 17721 2073 966 -25 O
ATOM 1767 N ASN A1022 57.095 -61.740 21.948 1.00 88.89 N
ANISOU 1767 N ASN A1022 10065 8635 15074 1978 353 205 N
ATOM 1768 CA ASN A1022 56.904 -62.144 23.332 1.00 87.87 C
ANISOU 1768 CA ASN A1022 9868 8576 14941 2009 216 275 C
ATOM 1769 C ASN A1022 55.425 -62.092 23.698 1.00 83.85 C
ANISOU 1769 C ASN A1022 9451 8122 14287 1936 130 321 C
ATOM 1770 O ASN A1022 54.633 -61.368 23.090 1.00 79.57 O
ANISOU 1770 O ASN A1022 8980 7600 13653 1857 152 292 O
ATOM 1771 CB ASN A1022 57.715 -61.245 24.271 1.00 91.63 C
ANISOU 1771 CB ASN A1022 10172 9150 15492 2046 153 266 C
ATOM 1772 CG ASN A1022 57.722 -61.748 25.704 1.00 95.35 C
ANISOU 1772 CG ASN A1022 10580 9678 15971 2103 16 336 C
ATOM 1773 OD1 ASN A1022 57.455 -62.921 25.964 1.00 90.22 O
ANISOU 1773 OD1 ASN A1022 9992 8978 15311 2134 -9 388 O
ATOM 1774 ND2 ASN A1022 58.032 -60.859 26.641 1.00101.58 N
ANISOU 1774 ND2 ASN A1022 11252 10567 16777 2120 -74 336 N
ATOM 1775 N ALA A1023 55.057 -62.882 24.710 1.00 89.94 N
ANISOU 1775 N ALA A1023 10220 8912 15042 1967 33 396 N
ATOM 1776 CA ALA A1023 53.674 -62.890 25.173 1.00 77.95 C
ANISOU 1776 CA ALA A1023 8776 7440 13404 1907 -46 452 C
ATOM 1777 C ALA A1023 53.295 -61.575 25.843 1.00 83.13 C
ANISOU 1777 C ALA A1023 9366 8225 13995 1868 -114 453 C
ATOM 1778 O ALA A1023 52.143 -61.140 25.739 1.00 81.82 O
ANISOU 1778 O ALA A1023 9269 8093 13724 1792 -138 468 O
ATOM 1779 CB ALA A1023 53.444 -64.061 26.127 1.00 78.63 C
ANISOU 1779 CB ALA A1023 8871 7507 13497 1961 -120 537 C
ATOM 1780 N ALA A1024 54.241 -60.929 26.530 1.00 82.18 N
ANISOU 1780 N ALA A1024 9114 8172 13939 1921 -149 437 N
ATOM 1781 CA ALA A1024 53.935 -59.656 27.174 1.00 80.42 C
ANISOU 1781 CA ALA A1024 8832 8070 13654 1890 -217 435 C
ATOM 1782 C ALA A1024 53.691 -58.552 26.153 1.00 80.38 C
ANISOU 1782 C ALA A1024 8852 8083 13606 1808 -142 364 C
ATOM 1783 O ALA A1024 52.953 -57.601 26.437 1.00 78.78 O
ANISOU 1783 O ALA A1024 8654 7967 13310 1751 -187 369 O
ATOM 1784 CB ALA A1024 55.062 -59.261 28.127 1.00 86.62 C
ANISOU 1784 CB ALA A1024 9472 8910 14529 1971 -283 429 C
ATOM 1785 N GLN A1025 54.299 -58.653 24.969 1.00 82.72 N
ANISOU 1785 N GLN A1025 9170 8294 13965 1806 -24 299 N
ATOM 1786 CA GLN A1025 54.037 -57.670 23.922 1.00 74.21 C
ANISOU 1786 CA GLN A1025 8138 7220 12840 1734 58 231 C
ATOM 1787 C GLN A1025 52.592 -57.747 23.452 1.00 78.00 C
ANISOU 1787 C GLN A1025 8761 7690 13187 1649 48 249 C
ATOM 1788 O GLN A1025 51.952 -56.717 23.211 1.00 68.32 O
ANISOU 1788 O GLN A1025 7558 6525 11877 1580 46 223 O
ATOM 1789 CB GLN A1025 54.995 -57.879 22.750 1.00 74.27 C
ANISOU 1789 CB GLN A1025 8156 7121 12943 1762 196 165 C
ATOM 1790 CG GLN A1025 56.455 -57.627 23.088 1.00 86.82 C
ANISOU 1790 CG GLN A1025 9588 8716 14683 1839 218 139 C
ATOM 1791 CD GLN A1025 57.383 -57.936 21.931 1.00 89.66 C
ANISOU 1791 CD GLN A1025 9964 8957 15145 1874 370 85 C
ATOM 1792 OE1 GLN A1025 57.014 -58.650 20.998 1.00 84.99 O
ANISOU 1792 OE1 GLN A1025 9511 8268 14515 1862 446 78 O
ATOM 1793 NE2 GLN A1025 58.595 -57.397 21.985 1.00101.20 N
ANISOU 1793 NE2 GLN A1025 11287 10422 16744 1922 415 48 N
ATOM 1794 N VAL A1026 52.060 -58.963 23.317 1.00 79.56 N
ANISOU 1794 N VAL A1026 9054 7805 13370 1654 39 292 N
ATOM 1795 CA VAL A1026 50.654 -59.125 22.967 1.00 71.57 C
ANISOU 1795 CA VAL A1026 8168 6774 12250 1576 13 317 C
ATOM 1796 C VAL A1026 49.767 -58.670 24.118 1.00 69.50 C
ANISOU 1796 C VAL A1026 7870 6622 11913 1546 -97 385 C
ATOM 1797 O VAL A1026 48.704 -58.075 23.904 1.00 73.23 O
ANISOU 1797 O VAL A1026 8402 7129 12293 1468 -117 388 O
ATOM 1798 CB VAL A1026 50.373 -60.586 22.572 1.00 71.01 C
ANISOU 1798 CB VAL A1026 8200 6580 12201 1593 26 348 C
ATOM 1799 CG1 VAL A1026 48.905 -60.774 22.220 1.00 71.57 C
ANISOU 1799 CG1 VAL A1026 8393 6621 12178 1512 -12 374 C
ATOM 1800 CG2 VAL A1026 51.260 -61.001 21.409 1.00 66.38 C
ANISOU 1800 CG2 VAL A1026 7661 5880 11681 1629 142 282 C
ATOM 1801 N LYS A1027 50.193 -58.928 25.357 1.00 70.72 N
ANISOU 1801 N LYS A1027 7932 6830 12106 1613 -168 442 N
ATOM 1802 CA LYS A1027 49.383 -58.557 26.513 1.00 72.06 C
ANISOU 1802 CA LYS A1027 8080 7095 12203 1600 -267 515 C
ATOM 1803 C LYS A1027 49.318 -57.045 26.686 1.00 73.30 C
ANISOU 1803 C LYS A1027 8182 7365 12303 1560 -284 480 C
ATOM 1804 O LYS A1027 48.244 -56.491 26.951 1.00 75.12 O
ANISOU 1804 O LYS A1027 8451 7654 12439 1500 -325 514 O
ATOM 1805 CB LYS A1027 49.936 -59.219 27.775 1.00 76.32 C
ANISOU 1805 CB LYS A1027 8550 7654 12794 1695 -337 580 C
ATOM 1806 CG LYS A1027 49.161 -58.882 29.040 1.00 78.08 C
ANISOU 1806 CG LYS A1027 8762 7967 12939 1700 -433 661 C
ATOM 1807 CD LYS A1027 49.785 -59.536 30.261 1.00 80.98 C
ANISOU 1807 CD LYS A1027 9072 8343 13352 1807 -502 720 C
ATOM 1808 CE LYS A1027 48.980 -59.241 31.516 1.00 76.02 C
ANISOU 1808 CE LYS A1027 8455 7793 12638 1822 -589 807 C
ATOM 1809 NZ LYS A1027 49.552 -59.917 32.713 1.00 71.15 N
ANISOU 1809 NZ LYS A1027 7802 7176 12056 1935 -658 865 N
ATOM 1810 N ASP A1028 50.454 -56.358 26.541 1.00 77.10 N
ANISOU 1810 N ASP A1028 8572 7875 12850 1592 -253 415 N
ATOM 1811 CA ASP A1028 50.465 -54.908 26.711 1.00 78.79 C
ANISOU 1811 CA ASP A1028 8727 8192 13017 1557 -270 379 C
ATOM 1812 C ASP A1028 49.673 -54.215 25.611 1.00 72.70 C
ANISOU 1812 C ASP A1028 8042 7416 12165 1459 -206 330 C
ATOM 1813 O ASP A1028 48.999 -53.209 25.863 1.00 73.55 O
ANISOU 1813 O ASP A1028 8149 7612 12184 1406 -241 334 O
ATOM 1814 CB ASP A1028 51.903 -54.391 26.747 1.00 85.24 C
ANISOU 1814 CB ASP A1028 9420 9024 13944 1614 -247 319 C
ATOM 1815 CG ASP A1028 52.638 -54.795 28.012 1.00 97.28 C
ANISOU 1815 CG ASP A1028 10850 10577 15537 1710 -340 365 C
ATOM 1816 OD1 ASP A1028 51.976 -54.962 29.058 1.00103.76 O
ANISOU 1816 OD1 ASP A1028 11690 11448 16287 1725 -435 440 O
ATOM 1817 OD2 ASP A1028 53.877 -54.942 27.962 1.00 92.98 O
ANISOU 1817 OD2 ASP A1028 10214 9997 15118 1773 -317 327 O
ATOM 1818 N ALA A1029 49.738 -54.735 24.384 1.00 67.45 N
ANISOU 1818 N ALA A1029 7457 6645 11524 1440 -113 282 N
ATOM 1819 CA ALA A1029 48.961 -54.147 23.299 1.00 67.61 C
ANISOU 1819 CA ALA A1029 7578 6648 11464 1354 -58 233 C
ATOM 1820 C ALA A1029 47.470 -54.394 23.481 1.00 68.98 C
ANISOU 1820 C ALA A1029 7842 6827 11539 1290 -121 294 C
ATOM 1821 O ALA A1029 46.654 -53.546 23.105 1.00 70.03 O
ANISOU 1821 O ALA A1029 8022 7001 11586 1216 -122 273 O
ATOM 1822 CB ALA A1029 49.432 -54.696 21.953 1.00 62.08 C
ANISOU 1822 CB ALA A1029 6957 5819 10811 1362 54 168 C
ATOM 1823 N LEU A1030 47.095 -55.540 24.055 1.00 65.64 N
ANISOU 1823 N LEU A1030 7442 6360 11136 1318 -173 370 N
ATOM 1824 CA LEU A1030 45.686 -55.833 24.290 1.00 63.83 C
ANISOU 1824 CA LEU A1030 7288 6128 10837 1262 -230 437 C
ATOM 1825 C LEU A1030 45.119 -55.042 25.463 1.00 65.08 C
ANISOU 1825 C LEU A1030 7387 6410 10930 1250 -307 499 C
ATOM 1826 O LEU A1030 43.939 -54.673 25.440 1.00 58.53 O
ANISOU 1826 O LEU A1030 6609 5604 10025 1180 -335 530 O
ATOM 1827 CB LEU A1030 45.492 -57.330 24.529 1.00 65.07 C
ANISOU 1827 CB LEU A1030 7487 6191 11046 1299 -252 501 C
ATOM 1828 CG LEU A1030 45.518 -58.216 23.284 1.00 61.97 C
ANISOU 1828 CG LEU A1030 7200 5658 10688 1288 -192 455 C
ATOM 1829 CD1 LEU A1030 45.682 -59.673 23.675 1.00 64.85 C
ANISOU 1829 CD1 LEU A1030 7577 5941 11122 1347 -210 514 C
ATOM 1830 CD2 LEU A1030 44.249 -58.017 22.470 1.00 60.64 C
ANISOU 1830 CD2 LEU A1030 7143 5447 10449 1195 -200 441 C
ATOM 1831 N THR A1031 45.929 -54.783 26.493 1.00 68.70 N
ANISOU 1831 N THR A1031 7742 6943 11417 1320 -346 521 N
ATOM 1832 CA THR A1031 45.468 -53.961 27.607 1.00 66.11 C
ANISOU 1832 CA THR A1031 7369 6731 11020 1318 -418 576 C
ATOM 1833 C THR A1031 45.137 -52.548 27.142 1.00 63.49 C
ANISOU 1833 C THR A1031 7036 6476 10612 1245 -400 521 C
ATOM 1834 O THR A1031 44.152 -51.949 27.590 1.00 63.31 O
ANISOU 1834 O THR A1031 7034 6519 10503 1200 -440 567 O
ATOM 1835 CB THR A1031 46.527 -53.934 28.712 1.00 71.62 C
ANISOU 1835 CB THR A1031 7964 7482 11767 1416 -470 596 C
ATOM 1836 OG1 THR A1031 46.726 -55.259 29.219 1.00 69.17 O
ANISOU 1836 OG1 THR A1031 7663 7103 11516 1485 -491 655 O
ATOM 1837 CG2 THR A1031 46.100 -53.020 29.853 1.00 69.70 C
ANISOU 1837 CG2 THR A1031 7687 7355 11442 1423 -547 648 C
ATOM 1838 N LYS A1032 45.941 -52.007 26.226 1.00 61.82 N
ANISOU 1838 N LYS A1032 6803 6251 10433 1235 -331 423 N
ATOM 1839 CA LYS A1032 45.688 -50.680 25.684 1.00 65.56 C
ANISOU 1839 CA LYS A1032 7282 6790 10839 1168 -302 363 C
ATOM 1840 C LYS A1032 44.547 -50.667 24.675 1.00 62.56 C
ANISOU 1840 C LYS A1032 7021 6360 10391 1078 -269 346 C
ATOM 1841 O LYS A1032 43.953 -49.609 24.447 1.00 64.94 O
ANISOU 1841 O LYS A1032 7339 6725 10610 1014 -268 322 O
ATOM 1842 CB LYS A1032 46.968 -50.129 25.052 1.00 67.30 C
ANISOU 1842 CB LYS A1032 7440 7004 11128 1194 -229 268 C
ATOM 1843 CG LYS A1032 48.109 -49.996 26.052 1.00 67.41 C
ANISOU 1843 CG LYS A1032 7324 7068 11220 1278 -275 278 C
ATOM 1844 CD LYS A1032 49.449 -49.765 25.375 1.00 80.01 C
ANISOU 1844 CD LYS A1032 8852 8624 12924 1314 -194 192 C
ATOM 1845 CE LYS A1032 50.574 -49.715 26.400 1.00 84.28 C
ANISOU 1845 CE LYS A1032 9259 9205 13560 1400 -256 204 C
ATOM 1846 NZ LYS A1032 51.914 -49.602 25.761 1.00 82.70 N
ANISOU 1846 NZ LYS A1032 8979 8951 13492 1440 -173 128 N
ATOM 1847 N MET A1033 44.225 -51.810 24.064 1.00 62.09 N
ANISOU 1847 N MET A1033 7044 6183 10363 1074 -248 355 N
ATOM 1848 CA MET A1033 43.020 -51.879 23.244 1.00 61.82 C
ANISOU 1848 CA MET A1033 7124 6095 10269 992 -244 349 C
ATOM 1849 C MET A1033 41.771 -51.920 24.111 1.00 62.89 C
ANISOU 1849 C MET A1033 7268 6276 10353 957 -323 447 C
ATOM 1850 O MET A1033 40.768 -51.271 23.795 1.00 61.32 O
ANISOU 1850 O MET A1033 7116 6100 10081 881 -336 445 O
ATOM 1851 CB MET A1033 43.066 -53.099 22.329 1.00 63.58 C
ANISOU 1851 CB MET A1033 7439 6172 10548 1002 -206 328 C
ATOM 1852 CG MET A1033 44.123 -53.022 21.257 1.00 67.05 C
ANISOU 1852 CG MET A1033 7901 6548 11027 1029 -110 229 C
ATOM 1853 SD MET A1033 44.098 -54.444 20.157 1.00 75.70 S
ANISOU 1853 SD MET A1033 9127 7464 12172 1044 -69 206 S
ATOM 1854 CE MET A1033 42.503 -54.227 19.380 1.00 63.62 C
ANISOU 1854 CE MET A1033 7733 5890 10550 942 -109 198 C
ATOM 1855 N ARG A1034 41.817 -52.673 25.213 1.00 59.75 N
ANISOU 1855 N ARG A1034 6824 5884 9992 1014 -372 536 N
ATOM 1856 CA ARG A1034 40.657 -52.775 26.089 1.00 62.70 C
ANISOU 1856 CA ARG A1034 7208 6290 10326 992 -435 640 C
ATOM 1857 C ARG A1034 40.328 -51.438 26.738 1.00 66.47 C
ANISOU 1857 C ARG A1034 7640 6899 10717 968 -463 656 C
ATOM 1858 O ARG A1034 39.156 -51.155 27.008 1.00 64.21 O
ANISOU 1858 O ARG A1034 7384 6637 10377 915 -492 716 O
ATOM 1859 CB ARG A1034 40.901 -53.845 27.152 1.00 57.03 C
ANISOU 1859 CB ARG A1034 6455 5548 9665 1073 -471 730 C
ATOM 1860 CG ARG A1034 39.631 -54.409 27.762 1.00 62.23 C
ANISOU 1860 CG ARG A1034 7151 6180 10314 1051 -511 840 C
ATOM 1861 CD ARG A1034 39.942 -55.414 28.857 1.00 65.20 C
ANISOU 1861 CD ARG A1034 7498 6536 10740 1142 -539 928 C
ATOM 1862 NE ARG A1034 38.738 -56.082 29.332 1.00 68.21 N
ANISOU 1862 NE ARG A1034 7918 6868 11129 1122 -562 1035 N
ATOM 1863 CZ ARG A1034 37.890 -55.561 30.208 1.00 72.95 C
ANISOU 1863 CZ ARG A1034 8511 7533 11675 1113 -588 1121 C
ATOM 1864 NH1 ARG A1034 38.086 -54.361 30.730 1.00 80.57 N
ANISOU 1864 NH1 ARG A1034 9436 8617 12562 1121 -604 1112 N
ATOM 1865 NH2 ARG A1034 36.816 -56.259 30.566 1.00 74.93 N
ANISOU 1865 NH2 ARG A1034 8795 7722 11953 1097 -596 1220 N
ATOM 1866 N ALA A1035 41.339 -50.605 26.994 1.00 71.93 N
ANISOU 1866 N ALA A1035 8258 7672 11400 1005 -455 606 N
ATOM 1867 CA ALA A1035 41.078 -49.266 27.510 1.00 62.11 C
ANISOU 1867 CA ALA A1035 6978 6551 10072 980 -480 610 C
ATOM 1868 C ALA A1035 40.459 -48.380 26.436 1.00 63.50 C
ANISOU 1868 C ALA A1035 7207 6736 10184 885 -441 542 C
ATOM 1869 O ALA A1035 39.477 -47.673 26.690 1.00 69.96 O
ANISOU 1869 O ALA A1035 8045 7615 10923 831 -467 579 O
ATOM 1870 CB ALA A1035 42.370 -48.649 28.045 1.00 59.85 C
ANISOU 1870 CB ALA A1035 6596 6338 9808 1048 -491 570 C
ATOM 1871 N ALA A1036 41.019 -48.412 25.223 1.00 64.44 N
ANISOU 1871 N ALA A1036 7358 6791 10336 868 -376 443 N
ATOM 1872 CA ALA A1036 40.477 -47.627 24.120 1.00 64.45 C
ANISOU 1872 CA ALA A1036 7426 6788 10275 786 -335 372 C
ATOM 1873 C ALA A1036 39.128 -48.148 23.643 1.00 69.70 C
ANISOU 1873 C ALA A1036 8189 7380 10916 719 -358 407 C
ATOM 1874 O ALA A1036 38.396 -47.412 22.972 1.00 68.75 O
ANISOU 1874 O ALA A1036 8124 7270 10728 646 -349 369 O
ATOM 1875 CB ALA A1036 41.465 -47.605 22.952 1.00 60.50 C
ANISOU 1875 CB ALA A1036 6946 6222 9817 799 -250 261 C
ATOM 1876 N ALA A1037 38.787 -49.398 23.965 1.00 66.13 N
ANISOU 1876 N ALA A1037 7757 6847 10523 743 -389 478 N
ATOM 1877 CA ALA A1037 37.479 -49.931 23.601 1.00 64.40 C
ANISOU 1877 CA ALA A1037 7618 6551 10300 680 -421 519 C
ATOM 1878 C ALA A1037 36.406 -49.477 24.582 1.00 66.04 C
ANISOU 1878 C ALA A1037 7796 6835 10459 650 -473 618 C
ATOM 1879 O ALA A1037 35.347 -48.991 24.173 1.00 68.69 O
ANISOU 1879 O ALA A1037 8179 7171 10750 573 -489 620 O
ATOM 1880 CB ALA A1037 37.533 -51.459 23.530 1.00 59.94 C
ANISOU 1880 CB ALA A1037 7086 5862 9826 717 -430 556 C
ATOM 1881 N LEU A1038 36.663 -49.624 25.884 1.00 62.67 N
ANISOU 1881 N LEU A1038 7299 6472 10042 713 -500 703 N
ATOM 1882 CA LEU A1038 35.691 -49.177 26.875 1.00 68.74 C
ANISOU 1882 CA LEU A1038 8046 7310 10760 697 -539 804 C
ATOM 1883 C LEU A1038 35.529 -47.664 26.857 1.00 70.93 C
ANISOU 1883 C LEU A1038 8307 7704 10938 653 -536 767 C
ATOM 1884 O LEU A1038 34.435 -47.153 27.124 1.00 73.88 O
ANISOU 1884 O LEU A1038 8696 8114 11262 602 -555 823 O
ATOM 1885 CB LEU A1038 36.102 -49.644 28.271 1.00 71.41 C
ANISOU 1885 CB LEU A1038 8328 7685 11119 790 -566 898 C
ATOM 1886 CG LEU A1038 36.235 -51.150 28.498 1.00 65.39 C
ANISOU 1886 CG LEU A1038 7577 6817 10452 842 -571 952 C
ATOM 1887 CD1 LEU A1038 36.591 -51.429 29.948 1.00 75.88 C
ANISOU 1887 CD1 LEU A1038 8858 8193 11780 938 -599 1045 C
ATOM 1888 CD2 LEU A1038 34.960 -51.878 28.105 1.00 72.16 C
ANISOU 1888 CD2 LEU A1038 8493 7573 11350 780 -579 1007 C
ATOM 1889 N ASP A1039 36.598 -46.933 26.545 1.00 69.85 N
ANISOU 1889 N ASP A1039 8138 7625 10779 673 -507 675 N
ATOM 1890 CA ASP A1039 36.538 -45.479 26.501 1.00 70.99 C
ANISOU 1890 CA ASP A1039 8263 7878 10831 634 -500 632 C
ATOM 1891 C ASP A1039 35.890 -44.952 25.229 1.00 70.01 C
ANISOU 1891 C ASP A1039 8211 7723 10667 543 -470 556 C
ATOM 1892 O ASP A1039 35.602 -43.753 25.151 1.00 71.60 O
ANISOU 1892 O ASP A1039 8409 8011 10785 499 -466 529 O
ATOM 1893 CB ASP A1039 37.943 -44.893 26.643 1.00 74.33 C
ANISOU 1893 CB ASP A1039 8617 8365 11261 691 -480 562 C
ATOM 1894 CG ASP A1039 37.981 -43.690 27.561 1.00 83.97 C
ANISOU 1894 CG ASP A1039 9783 9720 12402 702 -512 587 C
ATOM 1895 OD1 ASP A1039 36.919 -43.326 28.109 1.00 81.61 O
ANISOU 1895 OD1 ASP A1039 9505 9466 12035 670 -542 663 O
ATOM 1896 OD2 ASP A1039 39.073 -43.111 27.737 1.00 98.09 O
ANISOU 1896 OD2 ASP A1039 11507 11563 14199 744 -506 532 O
ATOM 1897 N ALA A1040 35.658 -45.810 24.236 1.00 71.36 N
ANISOU 1897 N ALA A1040 8453 7770 10890 517 -455 521 N
ATOM 1898 CA ALA A1040 34.980 -45.401 23.013 1.00 72.80 C
ANISOU 1898 CA ALA A1040 8722 7906 11033 437 -439 449 C
ATOM 1899 C ALA A1040 33.467 -45.511 23.122 1.00 78.14 C
ANISOU 1899 C ALA A1040 9437 8556 11696 371 -490 524 C
ATOM 1900 O ALA A1040 32.748 -44.769 22.441 1.00 73.31 O
ANISOU 1900 O ALA A1040 8876 7952 11026 300 -492 482 O
ATOM 1901 CB ALA A1040 35.473 -46.238 21.829 1.00 68.04 C
ANISOU 1901 CB ALA A1040 8192 7171 10487 446 -402 368 C
ATOM 1902 N GLN A1041 32.967 -46.420 23.960 1.00 74.49 N
ANISOU 1902 N GLN A1041 8950 8058 11293 394 -528 634 N
ATOM 1903 CA GLN A1041 31.536 -46.534 24.200 1.00 77.62 C
ANISOU 1903 CA GLN A1041 9366 8427 11698 337 -570 720 C
ATOM 1904 C GLN A1041 31.060 -45.658 25.349 1.00 81.34 C
ANISOU 1904 C GLN A1041 9780 9023 12104 339 -582 808 C
ATOM 1905 O GLN A1041 29.863 -45.355 25.425 1.00 86.12 O
ANISOU 1905 O GLN A1041 10399 9628 12696 280 -605 864 O
ATOM 1906 CB GLN A1041 31.158 -47.992 24.485 1.00 71.06 C
ANISOU 1906 CB GLN A1041 8543 7480 10975 360 -597 801 C
ATOM 1907 CG GLN A1041 31.836 -48.582 25.713 1.00 74.88 C
ANISOU 1907 CG GLN A1041 8960 7998 11493 452 -592 882 C
ATOM 1908 CD GLN A1041 31.379 -49.997 26.014 1.00 77.42 C
ANISOU 1908 CD GLN A1041 9292 8204 11920 474 -613 968 C
ATOM 1909 OE1 GLN A1041 30.403 -50.484 25.443 1.00 78.63 O
ANISOU 1909 OE1 GLN A1041 9491 8257 12127 413 -638 984 O
ATOM 1910 NE2 GLN A1041 32.086 -50.666 26.916 1.00 73.73 N
ANISOU 1910 NE2 GLN A1041 8782 7745 11487 561 -606 1023 N
ATOM 1911 N LYS A1042 31.960 -45.245 26.235 1.00 76.89 N
ANISOU 1911 N LYS A1042 9153 8558 11503 407 -570 822 N
ATOM 1912 CA LYS A1042 31.599 -44.398 27.366 1.00 74.05 C
ANISOU 1912 CA LYS A1042 8750 8314 11071 422 -583 903 C
ATOM 1913 C LYS A1042 31.399 -42.951 26.928 1.00 81.32 C
ANISOU 1913 C LYS A1042 9680 9330 11890 362 -571 838 C
ATOM 1914 O LYS A1042 31.430 -42.642 25.736 1.00 85.93 O
ANISOU 1914 O LYS A1042 10308 9881 12461 306 -552 735 O
ATOM 1915 CB LYS A1042 32.670 -44.474 28.456 1.00 80.68 C
ANISOU 1915 CB LYS A1042 9530 9219 11907 523 -588 934 C
ATOM 1916 N GLU A1057 18.188 -49.431 17.794 1.00 88.37 N
ANISOU 1916 N GLU A1057 11170 8573 13832 -448 -1326 846 N
ATOM 1917 CA GLU A1057 19.426 -49.767 17.101 1.00 90.11 C
ANISOU 1917 CA GLU A1057 11487 8780 13972 -392 -1300 729 C
ATOM 1918 C GLU A1057 20.643 -49.282 17.885 1.00 94.56 C
ANISOU 1918 C GLU A1057 12000 9513 14415 -323 -1181 738 C
ATOM 1919 O GLU A1057 21.783 -49.479 17.462 1.00 98.70 O
ANISOU 1919 O GLU A1057 12584 10045 14874 -269 -1139 653 O
ATOM 1920 CB GLU A1057 19.431 -49.170 15.693 1.00 85.48 C
ANISOU 1920 CB GLU A1057 11039 8146 13294 -423 -1353 575 C
ATOM 1921 N MET A1058 20.392 -48.639 19.029 1.00 93.14 N
ANISOU 1921 N MET A1058 11713 9464 14212 -321 -1128 843 N
ATOM 1922 CA MET A1058 21.488 -48.218 19.895 1.00 85.41 C
ANISOU 1922 CA MET A1058 10680 8640 13134 -252 -1030 863 C
ATOM 1923 C MET A1058 22.128 -49.406 20.598 1.00 90.35 C
ANISOU 1923 C MET A1058 11264 9228 13837 -180 -999 931 C
ATOM 1924 O MET A1058 23.320 -49.365 20.924 1.00 89.17 O
ANISOU 1924 O MET A1058 11104 9159 13618 -112 -936 903 O
ATOM 1925 CB MET A1058 20.992 -47.197 20.919 1.00 78.66 C
ANISOU 1925 CB MET A1058 9736 7925 12226 -266 -991 957 C
ATOM 1926 N LYS A1059 21.355 -50.465 20.845 1.00 90.96 N
ANISOU 1926 N LYS A1059 11315 9180 14066 -194 -1044 1020 N
ATOM 1927 CA LYS A1059 21.914 -51.703 21.371 1.00 91.74 C
ANISOU 1927 CA LYS A1059 11389 9221 14246 -128 -1021 1076 C
ATOM 1928 C LYS A1059 22.677 -52.488 20.312 1.00 92.79 C
ANISOU 1928 C LYS A1059 11619 9248 14388 -106 -1046 961 C
ATOM 1929 O LYS A1059 23.492 -53.346 20.665 1.00 88.47 O
ANISOU 1929 O LYS A1059 11062 8683 13869 -40 -1012 979 O
ATOM 1930 CB LYS A1059 20.804 -52.575 21.963 1.00 86.98 C
ANISOU 1930 CB LYS A1059 10726 8511 13810 -151 -1054 1211 C
ATOM 1931 N ASP A1060 22.424 -52.219 19.026 1.00 90.16 N
ANISOU 1931 N ASP A1060 11387 8840 14028 -156 -1106 845 N
ATOM 1932 CA ASP A1060 23.233 -52.818 17.969 1.00 87.81 C
ANISOU 1932 CA ASP A1060 11201 8450 13712 -126 -1118 727 C
ATOM 1933 C ASP A1060 24.673 -52.327 18.031 1.00 88.25 C
ANISOU 1933 C ASP A1060 11263 8624 13642 -58 -1023 660 C
ATOM 1934 O ASP A1060 25.600 -53.080 17.712 1.00 90.44 O
ANISOU 1934 O ASP A1060 11586 8849 13929 -1 -997 614 O
ATOM 1935 CB ASP A1060 22.621 -52.513 16.600 1.00 92.07 C
ANISOU 1935 CB ASP A1060 11863 8887 14235 -187 -1201 617 C
ATOM 1936 CG ASP A1060 23.515 -52.940 15.448 1.00 95.20 C
ANISOU 1936 CG ASP A1060 12396 9195 14582 -147 -1199 486 C
ATOM 1937 OD1 ASP A1060 23.722 -54.159 15.271 1.00 93.90 O
ANISOU 1937 OD1 ASP A1060 12266 8907 14505 -116 -1224 494 O
ATOM 1938 OD2 ASP A1060 24.006 -52.056 14.714 1.00104.77 O
ANISOU 1938 OD2 ASP A1060 13684 10456 15667 -143 -1167 378 O
ATOM 1939 N PHE A1061 24.879 -51.072 18.436 1.00 86.90 N
ANISOU 1939 N PHE A1061 11045 8611 13361 -62 -972 654 N
ATOM 1940 CA PHE A1061 26.228 -50.576 18.679 1.00 86.31 C
ANISOU 1940 CA PHE A1061 10950 8656 13187 3 -883 606 C
ATOM 1941 C PHE A1061 26.762 -51.043 20.026 1.00 82.52 C
ANISOU 1941 C PHE A1061 10363 8248 12745 69 -838 713 C
ATOM 1942 O PHE A1061 27.973 -51.239 20.174 1.00 78.83 O
ANISOU 1942 O PHE A1061 9883 7817 12250 138 -782 680 O
ATOM 1943 CB PHE A1061 26.252 -49.048 18.604 1.00 84.43 C
ANISOU 1943 CB PHE A1061 10704 8555 12822 -26 -851 557 C
ATOM 1944 N ARG A1062 25.879 -51.221 21.012 1.00 84.75 N
ANISOU 1944 N ARG A1062 10567 8542 13090 53 -858 843 N
ATOM 1945 CA ARG A1062 26.301 -51.793 22.286 1.00 78.90 C
ANISOU 1945 CA ARG A1062 9742 7848 12389 123 -820 951 C
ATOM 1946 C ARG A1062 26.694 -53.256 22.124 1.00 74.96 C
ANISOU 1946 C ARG A1062 9269 7220 11992 166 -831 959 C
ATOM 1947 O ARG A1062 27.662 -53.716 22.741 1.00 74.26 O
ANISOU 1947 O ARG A1062 9146 7168 11903 244 -787 980 O
ATOM 1948 CB ARG A1062 25.190 -51.641 23.324 1.00 81.84 C
ANISOU 1948 CB ARG A1062 10040 8248 12806 100 -830 1092 C
ATOM 1949 N HIS A1063 25.956 -54.002 21.295 1.00 77.73 N
ANISOU 1949 N HIS A1063 9684 7417 12432 118 -894 940 N
ATOM 1950 CA HIS A1063 26.324 -55.385 21.008 1.00 79.71 C
ANISOU 1950 CA HIS A1063 9974 7537 12776 155 -909 936 C
ATOM 1951 C HIS A1063 27.657 -55.467 20.276 1.00 75.10 C
ANISOU 1951 C HIS A1063 9455 6954 12125 207 -869 817 C
ATOM 1952 O HIS A1063 28.358 -56.480 20.374 1.00 71.90 O
ANISOU 1952 O HIS A1063 9058 6492 11770 267 -850 824 O
ATOM 1953 CB HIS A1063 25.224 -56.062 20.185 1.00 77.78 C
ANISOU 1953 CB HIS A1063 9793 7123 12639 88 -998 930 C
ATOM 1954 CG HIS A1063 25.516 -57.488 19.832 1.00 78.62 C
ANISOU 1954 CG HIS A1063 9949 7083 12842 121 -1023 924 C
ATOM 1955 ND1 HIS A1063 25.596 -58.489 20.776 1.00 75.12 N
ANISOU 1955 ND1 HIS A1063 9439 6612 12490 169 -1001 1032 N
ATOM 1956 CD2 HIS A1063 25.740 -58.083 18.635 1.00 76.27 C
ANISOU 1956 CD2 HIS A1063 9767 6654 12559 117 -1065 824 C
ATOM 1957 CE1 HIS A1063 25.859 -59.637 20.178 1.00 69.68 C
ANISOU 1957 CE1 HIS A1063 8817 5785 11871 189 -1031 999 C
ATOM 1958 NE2 HIS A1063 25.951 -59.419 18.878 1.00 71.93 N
ANISOU 1958 NE2 HIS A1063 9215 6004 12111 159 -1071 873 N
ATOM 1959 N GLY A1064 28.022 -54.415 19.541 1.00 76.85 N
ANISOU 1959 N GLY A1064 9726 7237 12238 188 -848 711 N
ATOM 1960 CA GLY A1064 29.299 -54.421 18.847 1.00 70.16 C
ANISOU 1960 CA GLY A1064 8936 6388 11332 241 -794 602 C
ATOM 1961 C GLY A1064 30.476 -54.353 19.801 1.00 66.90 C
ANISOU 1961 C GLY A1064 8433 6090 10895 322 -721 633 C
ATOM 1962 O GLY A1064 31.448 -55.100 19.661 1.00 61.71 O
ANISOU 1962 O GLY A1064 7792 5389 10265 385 -686 605 O
ATOM 1963 N PHE A1065 30.405 -53.454 20.787 1.00 67.14 N
ANISOU 1963 N PHE A1065 8370 6265 10874 323 -701 691 N
ATOM 1964 CA PHE A1065 31.476 -53.368 21.773 1.00 65.78 C
ANISOU 1964 CA PHE A1065 8112 6198 10682 402 -649 724 C
ATOM 1965 C PHE A1065 31.493 -54.581 22.692 1.00 65.40 C
ANISOU 1965 C PHE A1065 8019 6104 10727 456 -659 830 C
ATOM 1966 O PHE A1065 32.553 -54.944 23.213 1.00 65.50 O
ANISOU 1966 O PHE A1065 7990 6149 10747 535 -623 835 O
ATOM 1967 CB PHE A1065 31.344 -52.083 22.591 1.00 63.76 C
ANISOU 1967 CB PHE A1065 7782 6101 10341 393 -635 758 C
ATOM 1968 CG PHE A1065 31.940 -50.879 21.922 1.00 67.60 C
ANISOU 1968 CG PHE A1065 8289 6667 10730 377 -597 647 C
ATOM 1969 CD1 PHE A1065 33.292 -50.604 22.041 1.00 65.92 C
ANISOU 1969 CD1 PHE A1065 8038 6518 10489 442 -543 593 C
ATOM 1970 CD2 PHE A1065 31.151 -50.022 21.174 1.00 69.53 C
ANISOU 1970 CD2 PHE A1065 8586 6915 10917 299 -616 596 C
ATOM 1971 CE1 PHE A1065 33.846 -49.499 21.426 1.00 71.05 C
ANISOU 1971 CE1 PHE A1065 8702 7234 11061 429 -500 494 C
ATOM 1972 CE2 PHE A1065 31.699 -48.913 20.557 1.00 66.98 C
ANISOU 1972 CE2 PHE A1065 8285 6661 10502 288 -574 495 C
ATOM 1973 CZ PHE A1065 33.048 -48.652 20.684 1.00 68.83 C
ANISOU 1973 CZ PHE A1065 8479 6958 10714 353 -512 445 C
ATOM 1974 N ASP A1066 30.338 -55.217 22.905 1.00 68.28 N
ANISOU 1974 N ASP A1066 8389 6387 11169 417 -706 914 N
ATOM 1975 CA ASP A1066 30.311 -56.444 23.695 1.00 69.28 C
ANISOU 1975 CA ASP A1066 8482 6451 11390 468 -711 1014 C
ATOM 1976 C ASP A1066 31.108 -57.549 23.014 1.00 63.13 C
ANISOU 1976 C ASP A1066 7760 5563 10665 510 -703 955 C
ATOM 1977 O ASP A1066 31.829 -58.304 23.676 1.00 67.99 O
ANISOU 1977 O ASP A1066 8338 6177 11316 586 -678 998 O
ATOM 1978 CB ASP A1066 28.867 -56.888 23.932 1.00 74.91 C
ANISOU 1978 CB ASP A1066 9190 7083 12191 411 -759 1113 C
ATOM 1979 CG ASP A1066 28.086 -55.906 24.785 1.00 83.60 C
ANISOU 1979 CG ASP A1066 10227 8288 13248 384 -754 1195 C
ATOM 1980 OD1 ASP A1066 28.680 -54.907 25.244 1.00 85.64 O
ANISOU 1980 OD1 ASP A1066 10449 8686 13403 412 -720 1176 O
ATOM 1981 OD2 ASP A1066 26.875 -56.131 24.994 1.00 87.25 O
ANISOU 1981 OD2 ASP A1066 10675 8689 13786 335 -785 1279 O
ATOM 1982 N ILE A1067 30.994 -57.655 21.688 1.00 62.39 N
ANISOU 1982 N ILE A1067 7763 5371 10572 465 -725 856 N
ATOM 1983 CA ILE A1067 31.806 -58.612 20.944 1.00 61.25 C
ANISOU 1983 CA ILE A1067 7688 5120 10463 509 -711 790 C
ATOM 1984 C ILE A1067 33.272 -58.199 20.972 1.00 61.62 C
ANISOU 1984 C ILE A1067 7710 5255 10447 579 -638 724 C
ATOM 1985 O ILE A1067 34.163 -59.035 21.166 1.00 60.20 O
ANISOU 1985 O ILE A1067 7521 5044 10309 650 -607 729 O
ATOM 1986 CB ILE A1067 31.285 -58.746 19.500 1.00 60.42 C
ANISOU 1986 CB ILE A1067 7710 4884 10362 449 -756 698 C
ATOM 1987 CG1 ILE A1067 29.822 -59.193 19.488 1.00 70.62 C
ANISOU 1987 CG1 ILE A1067 9014 6078 11739 379 -840 765 C
ATOM 1988 CG2 ILE A1067 32.138 -59.725 18.710 1.00 59.55 C
ANISOU 1988 CG2 ILE A1067 7686 4660 10281 501 -735 632 C
ATOM 1989 CD1 ILE A1067 29.186 -59.159 18.109 1.00 66.01 C
ANISOU 1989 CD1 ILE A1067 8556 5370 11153 316 -905 674 C
ATOM 1990 N LEU A1068 33.545 -56.904 20.790 1.00 57.46 N
ANISOU 1990 N LEU A1068 7169 4836 9827 561 -608 664 N
ATOM 1991 CA LEU A1068 34.925 -56.428 20.729 1.00 57.33 C
ANISOU 1991 CA LEU A1068 7124 4894 9764 622 -538 595 C
ATOM 1992 C LEU A1068 35.652 -56.669 22.046 1.00 59.49 C
ANISOU 1992 C LEU A1068 7288 5253 10063 699 -520 671 C
ATOM 1993 O LEU A1068 36.727 -57.279 22.073 1.00 58.09 O
ANISOU 1993 O LEU A1068 7097 5052 9922 770 -483 650 O
ATOM 1994 CB LEU A1068 34.948 -54.943 20.365 1.00 56.38 C
ANISOU 1994 CB LEU A1068 7002 4875 9545 581 -515 526 C
ATOM 1995 CG LEU A1068 36.328 -54.318 20.160 1.00 56.24 C
ANISOU 1995 CG LEU A1068 6956 4926 9488 635 -438 445 C
ATOM 1996 CD1 LEU A1068 36.918 -54.755 18.830 1.00 56.81 C
ANISOU 1996 CD1 LEU A1068 7136 4879 9570 651 -392 343 C
ATOM 1997 CD2 LEU A1068 36.240 -52.805 20.245 1.00 58.01 C
ANISOU 1997 CD2 LEU A1068 7142 5278 9620 597 -423 411 C
ATOM 1998 N VAL A1069 35.078 -56.193 23.154 1.00 59.35 N
ANISOU 1998 N VAL A1069 7196 5331 10025 691 -546 761 N
ATOM 1999 CA VAL A1069 35.697 -56.394 24.460 1.00 61.55 C
ANISOU 1999 CA VAL A1069 7383 5686 10318 770 -539 837 C
ATOM 2000 C VAL A1069 35.755 -57.877 24.805 1.00 58.22 C
ANISOU 2000 C VAL A1069 6969 5162 9988 820 -550 902 C
ATOM 2001 O VAL A1069 36.711 -58.340 25.440 1.00 64.95 O
ANISOU 2001 O VAL A1069 7774 6036 10866 904 -531 921 O
ATOM 2002 CB VAL A1069 34.944 -55.581 25.534 1.00 62.41 C
ANISOU 2002 CB VAL A1069 7433 5904 10376 753 -564 925 C
ATOM 2003 CG1 VAL A1069 35.555 -55.799 26.905 1.00 66.45 C
ANISOU 2003 CG1 VAL A1069 7869 6486 10893 845 -564 1005 C
ATOM 2004 CG2 VAL A1069 34.953 -54.103 25.175 1.00 67.99 C
ANISOU 2004 CG2 VAL A1069 8133 6714 10988 706 -552 856 C
ATOM 2005 N GLY A1070 34.748 -58.646 24.386 1.00 58.58 N
ANISOU 2005 N GLY A1070 7074 5092 10092 770 -583 936 N
ATOM 2006 CA GLY A1070 34.769 -60.078 24.644 1.00 59.54 C
ANISOU 2006 CA GLY A1070 7208 5108 10306 813 -592 995 C
ATOM 2007 C GLY A1070 35.902 -60.785 23.925 1.00 60.17 C
ANISOU 2007 C GLY A1070 7330 5119 10414 864 -558 915 C
ATOM 2008 O GLY A1070 36.552 -61.672 24.486 1.00 60.84 O
ANISOU 2008 O GLY A1070 7387 5181 10549 939 -544 955 O
ATOM 2009 N GLN A1071 36.161 -60.396 22.675 1.00 60.01 N
ANISOU 2009 N GLN A1071 7380 5060 10360 829 -540 803 N
ATOM 2010 CA GLN A1071 37.271 -60.983 21.930 1.00 60.62 C
ANISOU 2010 CA GLN A1071 7504 5069 10461 882 -494 725 C
ATOM 2011 C GLN A1071 38.613 -60.559 22.512 1.00 60.56 C
ANISOU 2011 C GLN A1071 7410 5166 10435 960 -442 705 C
ATOM 2012 O GLN A1071 39.563 -61.351 22.534 1.00 61.28 O
ANISOU 2012 O GLN A1071 7494 5213 10575 1031 -410 696 O
ATOM 2013 CB GLN A1071 37.182 -60.588 20.457 1.00 60.48 C
ANISOU 2013 CB GLN A1071 7597 4982 10403 832 -480 612 C
ATOM 2014 CG GLN A1071 36.026 -61.219 19.704 1.00 65.34 C
ANISOU 2014 CG GLN A1071 8315 5459 11051 767 -542 615 C
ATOM 2015 CD GLN A1071 35.913 -60.710 18.280 1.00 64.06 C
ANISOU 2015 CD GLN A1071 8275 5232 10834 724 -536 500 C
ATOM 2016 OE1 GLN A1071 36.278 -59.572 17.984 1.00 64.73 O
ANISOU 2016 OE1 GLN A1071 8353 5402 10842 714 -494 436 O
ATOM 2017 NE2 GLN A1071 35.409 -61.555 17.388 1.00 61.33 N
ANISOU 2017 NE2 GLN A1071 8047 4730 10526 702 -579 474 N
ATOM 2018 N ILE A1072 38.714 -59.312 22.977 1.00 59.76 N
ANISOU 2018 N ILE A1072 7241 5197 10268 948 -437 698 N
ATOM 2019 CA ILE A1072 39.948 -58.848 23.606 1.00 59.74 C
ANISOU 2019 CA ILE A1072 7147 5294 10258 1021 -403 682 C
ATOM 2020 C ILE A1072 40.218 -59.630 24.886 1.00 62.53 C
ANISOU 2020 C ILE A1072 7432 5667 10660 1097 -429 779 C
ATOM 2021 O ILE A1072 41.356 -60.031 25.158 1.00 60.83 O
ANISOU 2021 O ILE A1072 7173 5454 10486 1176 -404 765 O
ATOM 2022 CB ILE A1072 39.878 -57.331 23.866 1.00 58.77 C
ANISOU 2022 CB ILE A1072 6971 5305 10053 988 -403 658 C
ATOM 2023 CG1 ILE A1072 39.848 -56.561 22.544 1.00 58.33 C
ANISOU 2023 CG1 ILE A1072 6985 5228 9950 929 -363 550 C
ATOM 2024 CG2 ILE A1072 41.055 -56.875 24.710 1.00 60.60 C
ANISOU 2024 CG2 ILE A1072 7098 5639 10290 1065 -389 656 C
ATOM 2025 CD1 ILE A1072 39.772 -55.057 22.715 1.00 58.31 C
ANISOU 2025 CD1 ILE A1072 6935 5353 9866 893 -359 520 C
ATOM 2026 N ASP A1073 39.175 -59.867 25.687 1.00 60.85 N
ANISOU 2026 N ASP A1073 7213 5462 10446 1078 -476 880 N
ATOM 2027 CA ASP A1073 39.337 -60.687 26.884 1.00 61.62 C
ANISOU 2027 CA ASP A1073 7265 5563 10586 1154 -496 979 C
ATOM 2028 C ASP A1073 39.709 -62.121 26.534 1.00 61.74 C
ANISOU 2028 C ASP A1073 7321 5452 10684 1194 -482 981 C
ATOM 2029 O ASP A1073 40.439 -62.774 27.289 1.00 62.34 O
ANISOU 2029 O ASP A1073 7356 5533 10799 1280 -480 1020 O
ATOM 2030 CB ASP A1073 38.057 -60.660 27.720 1.00 63.11 C
ANISOU 2030 CB ASP A1073 7449 5769 10761 1124 -534 1091 C
ATOM 2031 CG ASP A1073 37.852 -59.337 28.428 1.00 66.53 C
ANISOU 2031 CG ASP A1073 7830 6339 11110 1114 -548 1110 C
ATOM 2032 OD1 ASP A1073 38.782 -58.503 28.407 1.00 68.25 O
ANISOU 2032 OD1 ASP A1073 8005 6641 11285 1139 -536 1042 O
ATOM 2033 OD2 ASP A1073 36.764 -59.130 29.004 1.00 68.56 O
ANISOU 2033 OD2 ASP A1073 8088 6614 11347 1082 -569 1196 O
ATOM 2034 N ASP A1074 39.219 -62.627 25.401 1.00 61.93 N
ANISOU 2034 N ASP A1074 7433 5362 10736 1137 -477 939 N
ATOM 2035 CA ASP A1074 39.591 -63.968 24.960 1.00 62.87 C
ANISOU 2035 CA ASP A1074 7603 5354 10929 1174 -463 934 C
ATOM 2036 C ASP A1074 41.069 -64.033 24.598 1.00 63.24 C
ANISOU 2036 C ASP A1074 7633 5407 10990 1242 -409 856 C
ATOM 2037 O ASP A1074 41.778 -64.966 24.994 1.00 64.00 O
ANISOU 2037 O ASP A1074 7709 5466 11141 1318 -397 883 O
ATOM 2038 CB ASP A1074 38.725 -64.389 23.772 1.00 63.00 C
ANISOU 2038 CB ASP A1074 7729 5244 10965 1096 -479 898 C
ATOM 2039 CG ASP A1074 37.284 -64.664 24.163 1.00 62.94 C
ANISOU 2039 CG ASP A1074 7731 5197 10985 1037 -534 988 C
ATOM 2040 OD1 ASP A1074 36.984 -64.686 25.376 1.00 62.89 O
ANISOU 2040 OD1 ASP A1074 7655 5253 10986 1065 -547 1088 O
ATOM 2041 OD2 ASP A1074 36.450 -64.861 23.255 1.00 63.00 O
ANISOU 2041 OD2 ASP A1074 7819 5106 11011 966 -565 961 O
ATOM 2042 N ALA A1075 41.553 -63.045 23.842 1.00 62.77 N
ANISOU 2042 N ALA A1075 7578 5387 10884 1219 -372 761 N
ATOM 2043 CA ALA A1075 42.968 -63.008 23.491 1.00 67.31 C
ANISOU 2043 CA ALA A1075 8125 5966 11483 1284 -312 689 C
ATOM 2044 C ALA A1075 43.839 -62.697 24.702 1.00 65.22 C
ANISOU 2044 C ALA A1075 7738 5811 11232 1361 -321 725 C
ATOM 2045 O ALA A1075 44.976 -63.176 24.784 1.00 63.87 O
ANISOU 2045 O ALA A1075 7529 5621 11118 1437 -288 705 O
ATOM 2046 CB ALA A1075 43.206 -61.985 22.381 1.00 62.66 C
ANISOU 2046 CB ALA A1075 7575 5387 10846 1240 -262 583 C
ATOM 2047 N LEU A1076 43.327 -61.906 25.650 1.00 63.50 N
ANISOU 2047 N LEU A1076 7461 5703 10963 1346 -368 777 N
ATOM 2048 CA LEU A1076 44.087 -61.615 26.864 1.00 65.16 C
ANISOU 2048 CA LEU A1076 7568 6010 11179 1424 -393 814 C
ATOM 2049 C LEU A1076 44.283 -62.868 27.708 1.00 63.52 C
ANISOU 2049 C LEU A1076 7350 5757 11029 1502 -417 894 C
ATOM 2050 O LEU A1076 45.334 -63.042 28.336 1.00 67.33 O
ANISOU 2050 O LEU A1076 7764 6268 11548 1589 -423 895 O
ATOM 2051 CB LEU A1076 43.387 -60.527 27.678 1.00 67.33 C
ANISOU 2051 CB LEU A1076 7803 6402 11376 1393 -439 858 C
ATOM 2052 CG LEU A1076 43.844 -59.091 27.422 1.00 66.71 C
ANISOU 2052 CG LEU A1076 7676 6422 11248 1367 -425 782 C
ATOM 2053 CD1 LEU A1076 42.970 -58.107 28.184 1.00 67.32 C
ANISOU 2053 CD1 LEU A1076 7734 6604 11242 1330 -472 834 C
ATOM 2054 CD2 LEU A1076 45.304 -58.927 27.813 1.00 65.50 C
ANISOU 2054 CD2 LEU A1076 7432 6309 11144 1453 -417 743 C
ATOM 2055 N LYS A1077 43.282 -63.750 27.741 1.00 63.73 N
ANISOU 2055 N LYS A1077 7442 5706 11068 1475 -434 962 N
ATOM 2056 CA LYS A1077 43.424 -64.990 28.497 1.00 64.57 C
ANISOU 2056 CA LYS A1077 7546 5758 11229 1548 -449 1040 C
ATOM 2057 C LYS A1077 44.479 -65.894 27.873 1.00 65.39 C
ANISOU 2057 C LYS A1077 7664 5777 11405 1601 -407 986 C
ATOM 2058 O LYS A1077 45.218 -66.581 28.588 1.00 66.08 O
ANISOU 2058 O LYS A1077 7712 5860 11536 1690 -415 1020 O
ATOM 2059 CB LYS A1077 42.076 -65.708 28.588 1.00 64.64 C
ANISOU 2059 CB LYS A1077 7619 5693 11249 1500 -470 1123 C
ATOM 2060 CG LYS A1077 42.083 -66.949 29.468 1.00 67.60 C
ANISOU 2060 CG LYS A1077 7995 6015 11677 1575 -482 1216 C
ATOM 2061 CD LYS A1077 40.674 -67.486 29.689 1.00 73.36 C
ANISOU 2061 CD LYS A1077 8771 6680 12424 1525 -500 1308 C
ATOM 2062 CE LYS A1077 40.034 -67.921 28.380 1.00 86.39 C
ANISOU 2062 CE LYS A1077 10500 8214 14111 1437 -492 1262 C
ATOM 2063 NZ LYS A1077 38.659 -68.460 28.574 1.00 70.61 N
ANISOU 2063 NZ LYS A1077 8536 6141 12151 1386 -516 1352 N
ATOM 2064 N LEU A1078 44.573 -65.897 26.543 1.00 65.37 N
ANISOU 2064 N LEU A1078 7723 5703 11411 1551 -362 903 N
ATOM 2065 CA LEU A1078 45.580 -66.719 25.880 1.00 67.52 C
ANISOU 2065 CA LEU A1078 8018 5888 11748 1603 -310 853 C
ATOM 2066 C LEU A1078 46.973 -66.125 26.040 1.00 67.95 C
ANISOU 2066 C LEU A1078 7980 6010 11826 1668 -279 796 C
ATOM 2067 O LEU A1078 47.952 -66.861 26.209 1.00 67.12 O
ANISOU 2067 O LEU A1078 7845 5868 11788 1748 -258 795 O
ATOM 2068 CB LEU A1078 45.233 -66.880 24.401 1.00 66.17 C
ANISOU 2068 CB LEU A1078 7958 5612 11572 1538 -269 782 C
ATOM 2069 CG LEU A1078 43.917 -67.598 24.104 1.00 68.76 C
ANISOU 2069 CG LEU A1078 8381 5847 11899 1474 -308 829 C
ATOM 2070 CD1 LEU A1078 43.522 -67.390 22.654 1.00 69.82 C
ANISOU 2070 CD1 LEU A1078 8626 5896 12007 1404 -284 747 C
ATOM 2071 CD2 LEU A1078 44.031 -69.080 24.423 1.00 67.15 C
ANISOU 2071 CD2 LEU A1078 8202 5549 11764 1530 -314 888 C
ATOM 2072 N ALA A1079 47.083 -64.795 25.988 1.00 66.21 N
ANISOU 2072 N ALA A1079 7711 5885 11560 1636 -277 750 N
ATOM 2073 CA ALA A1079 48.389 -64.159 26.126 1.00 72.49 C
ANISOU 2073 CA ALA A1079 8410 6740 12394 1693 -251 695 C
ATOM 2074 C ALA A1079 48.950 -64.342 27.531 1.00 74.02 C
ANISOU 2074 C ALA A1079 8509 7000 12616 1781 -313 756 C
ATOM 2075 O ALA A1079 50.166 -64.491 27.703 1.00 75.47 O
ANISOU 2075 O ALA A1079 8620 7183 12873 1857 -298 728 O
ATOM 2076 CB ALA A1079 48.293 -62.676 25.773 1.00 69.14 C
ANISOU 2076 CB ALA A1079 7957 6400 11912 1634 -238 635 C
ATOM 2077 N ASN A1080 48.084 -64.328 28.547 1.00 71.60 N
ANISOU 2077 N ASN A1080 8204 6745 12256 1778 -382 840 N
ATOM 2078 CA ASN A1080 48.544 -64.555 29.913 1.00 72.17 C
ANISOU 2078 CA ASN A1080 8208 6869 12343 1871 -445 903 C
ATOM 2079 C ASN A1080 49.027 -65.986 30.113 1.00 68.58 C
ANISOU 2079 C ASN A1080 7771 6325 11962 1947 -437 938 C
ATOM 2080 O ASN A1080 49.920 -66.228 30.932 1.00 77.94 O
ANISOU 2080 O ASN A1080 8890 7534 13190 2042 -471 954 O
ATOM 2081 CB ASN A1080 47.428 -64.226 30.906 1.00 70.96 C
ANISOU 2081 CB ASN A1080 8073 6780 12110 1854 -506 991 C
ATOM 2082 CG ASN A1080 47.118 -62.743 30.966 1.00 70.75 C
ANISOU 2082 CG ASN A1080 8014 6859 12009 1799 -525 962 C
ATOM 2083 OD1 ASN A1080 47.596 -61.963 30.143 1.00 72.56 O
ANISOU 2083 OD1 ASN A1080 8217 7108 12245 1760 -488 874 O
ATOM 2084 ND2 ASN A1080 46.310 -62.348 31.942 1.00 71.43 N
ANISOU 2084 ND2 ASN A1080 8106 7010 12024 1800 -578 1040 N
ATOM 2085 N GLU A1081 48.454 -66.942 29.379 1.00 67.53 N
ANISOU 2085 N GLU A1081 7727 6087 11845 1909 -397 951 N
ATOM 2086 CA GLU A1081 48.880 -68.333 29.468 1.00 68.49 C
ANISOU 2086 CA GLU A1081 7874 6117 12034 1976 -384 982 C
ATOM 2087 C GLU A1081 50.210 -68.590 28.773 1.00 74.03 C
ANISOU 2087 C GLU A1081 8542 6771 12815 2024 -326 905 C
ATOM 2088 O GLU A1081 50.766 -69.682 28.927 1.00 72.72 O
ANISOU 2088 O GLU A1081 8381 6538 12710 2092 -316 926 O
ATOM 2089 CB GLU A1081 47.810 -69.248 28.868 1.00 68.55 C
ANISOU 2089 CB GLU A1081 7990 6020 12037 1916 -365 1017 C
ATOM 2090 CG GLU A1081 46.506 -69.290 29.648 1.00 68.18 C
ANISOU 2090 CG GLU A1081 7972 5994 11941 1884 -414 1112 C
ATOM 2091 CD GLU A1081 45.387 -69.954 28.869 1.00 78.90 C
ANISOU 2091 CD GLU A1081 9427 7246 13304 1804 -399 1132 C
ATOM 2092 OE1 GLU A1081 45.473 -69.990 27.623 1.00 81.21 O
ANISOU 2092 OE1 GLU A1081 9775 7471 13609 1754 -360 1056 O
ATOM 2093 OE2 GLU A1081 44.424 -70.441 29.498 1.00 76.84 O
ANISOU 2093 OE2 GLU A1081 9192 6962 13040 1795 -428 1223 O
ATOM 2094 N GLY A1082 50.729 -67.622 28.020 1.00 74.03 N
ANISOU 2094 N GLY A1082 8509 6800 12819 1991 -284 819 N
ATOM 2095 CA GLY A1082 51.937 -67.793 27.251 1.00 75.39 C
ANISOU 2095 CA GLY A1082 8653 6918 13073 2031 -211 748 C
ATOM 2096 C GLY A1082 51.707 -68.162 25.800 1.00 81.76 C
ANISOU 2096 C GLY A1082 9569 7617 13880 1977 -127 696 C
ATOM 2097 O GLY A1082 52.634 -68.044 24.990 1.00 89.30 O
ANISOU 2097 O GLY A1082 10510 8528 14890 1999 -48 627 O
ATOM 2098 N LYS A1083 50.499 -68.610 25.457 1.00 73.56 N
ANISOU 2098 N LYS A1083 8639 6526 12786 1912 -141 728 N
ATOM 2099 CA LYS A1083 50.153 -68.929 24.077 1.00 69.22 C
ANISOU 2099 CA LYS A1083 8210 5866 12224 1859 -79 677 C
ATOM 2100 C LYS A1083 50.233 -67.677 23.214 1.00 70.37 C
ANISOU 2100 C LYS A1083 8362 6045 12331 1804 -30 594 C
ATOM 2101 O LYS A1083 49.376 -66.795 23.315 1.00 73.09 O
ANISOU 2101 O LYS A1083 8710 6457 12603 1734 -69 596 O
ATOM 2102 CB LYS A1083 48.750 -69.534 24.001 1.00 69.97 C
ANISOU 2102 CB LYS A1083 8407 5905 12273 1795 -127 730 C
ATOM 2103 CG LYS A1083 48.533 -70.739 24.903 1.00 69.58 C
ANISOU 2103 CG LYS A1083 8356 5823 12260 1844 -173 821 C
ATOM 2104 CD LYS A1083 47.079 -71.188 24.868 1.00 69.34 C
ANISOU 2104 CD LYS A1083 8409 5740 12197 1773 -220 877 C
ATOM 2105 CE LYS A1083 46.860 -72.458 25.676 1.00 76.43 C
ANISOU 2105 CE LYS A1083 9313 6588 13139 1824 -252 968 C
ATOM 2106 NZ LYS A1083 47.168 -72.268 27.119 1.00 80.37 N
ANISOU 2106 NZ LYS A1083 9709 7191 13638 1890 -292 1034 N
ATOM 2107 N VAL A1084 51.256 -67.587 22.370 1.00 69.05 N
ANISOU 2107 N VAL A1084 8196 5828 12212 1839 61 523 N
ATOM 2108 CA VAL A1084 51.454 -66.403 21.540 1.00 69.97 C
ANISOU 2108 CA VAL A1084 8317 5969 12299 1798 123 443 C
ATOM 2109 C VAL A1084 50.762 -66.544 20.190 1.00 68.86 C
ANISOU 2109 C VAL A1084 8339 5722 12101 1739 170 396 C
ATOM 2110 O VAL A1084 50.096 -65.615 19.727 1.00 67.69 O
ANISOU 2110 O VAL A1084 8232 5606 11880 1668 166 359 O
ATOM 2111 CB VAL A1084 52.963 -66.113 21.382 1.00 73.49 C
ANISOU 2111 CB VAL A1084 8668 6417 12838 1872 206 394 C
ATOM 2112 CG1 VAL A1084 53.530 -65.565 22.679 1.00 79.41 C
ANISOU 2112 CG1 VAL A1084 9252 7289 13630 1914 140 424 C
ATOM 2113 CG2 VAL A1084 53.714 -67.369 20.972 1.00 81.90 C
ANISOU 2113 CG2 VAL A1084 9775 7362 13982 1944 267 397 C
ATOM 2114 N LYS A1085 50.898 -67.703 19.537 1.00 69.26 N
ANISOU 2114 N LYS A1085 8493 5641 12182 1770 208 394 N
ATOM 2115 CA LYS A1085 50.264 -67.895 18.236 1.00 69.29 C
ANISOU 2115 CA LYS A1085 8669 5530 12130 1724 242 346 C
ATOM 2116 C LYS A1085 48.746 -67.918 18.359 1.00 68.65 C
ANISOU 2116 C LYS A1085 8656 5452 11977 1637 142 382 C
ATOM 2117 O LYS A1085 48.040 -67.362 17.510 1.00 68.20 O
ANISOU 2117 O LYS A1085 8698 5364 11851 1573 143 334 O
ATOM 2118 CB LYS A1085 50.768 -69.185 17.590 1.00 70.37 C
ANISOU 2118 CB LYS A1085 8902 5521 12315 1785 298 342 C
ATOM 2119 CG LYS A1085 52.215 -69.136 17.127 1.00 71.09 C
ANISOU 2119 CG LYS A1085 8958 5577 12478 1866 422 295 C
ATOM 2120 CD LYS A1085 52.394 -68.164 15.972 1.00 70.88 C
ANISOU 2120 CD LYS A1085 9003 5521 12407 1845 516 210 C
ATOM 2121 CE LYS A1085 53.816 -68.195 15.432 1.00 71.74 C
ANISOU 2121 CE LYS A1085 9086 5573 12599 1930 655 170 C
ATOM 2122 NZ LYS A1085 54.191 -69.535 14.899 1.00 72.81 N
ANISOU 2122 NZ LYS A1085 9328 5564 12771 1993 704 180 N
ATOM 2123 N GLU A1086 48.228 -68.556 19.411 1.00 68.66 N
ANISOU 2123 N GLU A1086 8606 5484 11998 1638 58 468 N
ATOM 2124 CA GLU A1086 46.784 -68.611 19.601 1.00 68.14 C
ANISOU 2124 CA GLU A1086 8591 5416 11884 1558 -32 512 C
ATOM 2125 C GLU A1086 46.226 -67.261 20.031 1.00 67.08 C
ANISOU 2125 C GLU A1086 8388 5411 11688 1497 -69 511 C
ATOM 2126 O GLU A1086 45.065 -66.951 19.740 1.00 66.55 O
ANISOU 2126 O GLU A1086 8384 5332 11569 1417 -119 514 O
ATOM 2127 CB GLU A1086 46.433 -69.693 20.624 1.00 68.54 C
ANISOU 2127 CB GLU A1086 8605 5456 11982 1585 -96 610 C
ATOM 2128 CG GLU A1086 44.959 -70.063 20.655 1.00 68.87 C
ANISOU 2128 CG GLU A1086 8715 5450 12003 1510 -176 661 C
ATOM 2129 CD GLU A1086 44.672 -71.280 21.516 1.00 72.91 C
ANISOU 2129 CD GLU A1086 9208 5923 12572 1544 -221 756 C
ATOM 2130 OE1 GLU A1086 45.633 -71.931 21.979 1.00 70.09 O
ANISOU 2130 OE1 GLU A1086 8804 5564 12264 1628 -189 775 O
ATOM 2131 OE2 GLU A1086 43.480 -71.587 21.729 1.00 71.13 O
ANISOU 2131 OE2 GLU A1086 9014 5664 12349 1487 -285 812 O
ATOM 2132 N ALA A1087 47.033 -66.446 20.716 1.00 66.79 N
ANISOU 2132 N ALA A1087 8223 5494 11661 1533 -49 506 N
ATOM 2133 CA ALA A1087 46.588 -65.104 21.074 1.00 65.79 C
ANISOU 2133 CA ALA A1087 8036 5490 11472 1479 -78 499 C
ATOM 2134 C ALA A1087 46.597 -64.173 19.870 1.00 66.39 C
ANISOU 2134 C ALA A1087 8181 5548 11495 1432 -19 404 C
ATOM 2135 O ALA A1087 45.765 -63.262 19.788 1.00 64.55 O
ANISOU 2135 O ALA A1087 7960 5372 11192 1360 -52 394 O
ATOM 2136 CB ALA A1087 47.463 -64.536 22.191 1.00 65.70 C
ANISOU 2136 CB ALA A1087 7871 5603 11488 1536 -86 521 C
ATOM 2137 N GLN A1088 47.522 -64.383 18.930 1.00 66.79 N
ANISOU 2137 N GLN A1088 8282 5518 11578 1476 74 337 N
ATOM 2138 CA GLN A1088 47.548 -63.567 17.719 1.00 65.73 C
ANISOU 2138 CA GLN A1088 8234 5350 11391 1443 144 247 C
ATOM 2139 C GLN A1088 46.348 -63.861 16.827 1.00 65.61 C
ANISOU 2139 C GLN A1088 8382 5234 11311 1375 105 229 C
ATOM 2140 O GLN A1088 45.722 -62.936 16.298 1.00 64.93 O
ANISOU 2140 O GLN A1088 8347 5171 11151 1312 98 185 O
ATOM 2141 CB GLN A1088 48.851 -63.801 16.954 1.00 66.55 C
ANISOU 2141 CB GLN A1088 8358 5377 11552 1518 264 188 C
ATOM 2142 CG GLN A1088 50.083 -63.215 17.622 1.00 66.65 C
ANISOU 2142 CG GLN A1088 8206 5484 11635 1576 311 184 C
ATOM 2143 CD GLN A1088 51.375 -63.689 16.984 1.00 67.66 C
ANISOU 2143 CD GLN A1088 8342 5520 11847 1660 429 144 C
ATOM 2144 OE1 GLN A1088 51.482 -64.834 16.543 1.00 68.44 O
ANISOU 2144 OE1 GLN A1088 8532 5501 11972 1697 453 154 O
ATOM 2145 NE2 GLN A1088 52.365 -62.806 16.931 1.00 69.16 N
ANISOU 2145 NE2 GLN A1088 8433 5759 12084 1691 507 101 N
ATOM 2146 N ALA A1089 46.016 -65.141 16.644 1.00 66.30 N
ANISOU 2146 N ALA A1089 8554 5206 11429 1389 73 261 N
ATOM 2147 CA ALA A1089 44.864 -65.491 15.821 1.00 66.30 C
ANISOU 2147 CA ALA A1089 8709 5100 11383 1327 19 246 C
ATOM 2148 C ALA A1089 43.558 -65.029 16.455 1.00 65.47 C
ANISOU 2148 C ALA A1089 8567 5068 11242 1242 -86 297 C
ATOM 2149 O ALA A1089 42.608 -64.694 15.739 1.00 65.15 O
ANISOU 2149 O ALA A1089 8628 4980 11147 1174 -127 264 O
ATOM 2150 CB ALA A1089 44.833 -66.998 15.572 1.00 67.29 C
ANISOU 2150 CB ALA A1089 8923 5084 11559 1363 2 274 C
ATOM 2151 N ALA A1090 43.491 -65.006 17.789 1.00 65.18 N
ANISOU 2151 N ALA A1090 8390 5140 11235 1249 -130 380 N
ATOM 2152 CA ALA A1090 42.296 -64.500 18.455 1.00 64.41 C
ANISOU 2152 CA ALA A1090 8250 5117 11106 1176 -215 436 C
ATOM 2153 C ALA A1090 42.146 -62.998 18.246 1.00 63.46 C
ANISOU 2153 C ALA A1090 8105 5097 10908 1127 -199 385 C
ATOM 2154 O ALA A1090 41.033 -62.503 18.034 1.00 62.89 O
ANISOU 2154 O ALA A1090 8074 5030 10789 1050 -254 386 O
ATOM 2155 CB ALA A1090 42.341 -64.837 19.945 1.00 64.42 C
ANISOU 2155 CB ALA A1090 8121 5204 11151 1211 -253 539 C
ATOM 2156 N ALA A1091 43.258 -62.259 18.297 1.00 63.31 N
ANISOU 2156 N ALA A1091 8016 5157 10883 1172 -126 339 N
ATOM 2157 CA ALA A1091 43.218 -60.826 18.038 1.00 66.44 C
ANISOU 2157 CA ALA A1091 8391 5644 11210 1130 -101 284 C
ATOM 2158 C ALA A1091 42.902 -60.512 16.582 1.00 67.29 C
ANISOU 2158 C ALA A1091 8650 5658 11260 1091 -65 193 C
ATOM 2159 O ALA A1091 42.456 -59.399 16.284 1.00 63.21 O
ANISOU 2159 O ALA A1091 8145 5199 10672 1036 -67 153 O
ATOM 2160 CB ALA A1091 44.547 -60.180 18.433 1.00 62.45 C
ANISOU 2160 CB ALA A1091 7768 5231 10730 1192 -30 257 C
ATOM 2161 N GLU A1092 43.124 -61.464 15.673 1.00 67.45 N
ANISOU 2161 N GLU A1092 8793 5530 11304 1123 -34 159 N
ATOM 2162 CA GLU A1092 42.772 -61.248 14.274 1.00 71.99 C
ANISOU 2162 CA GLU A1092 9537 5999 11818 1095 -10 73 C
ATOM 2163 C GLU A1092 41.261 -61.221 14.078 1.00 74.21 C
ANISOU 2163 C GLU A1092 9895 6244 12057 1007 -119 89 C
ATOM 2164 O GLU A1092 40.769 -60.572 13.148 1.00 72.12 O
ANISOU 2164 O GLU A1092 9740 5942 11721 965 -121 21 O
ATOM 2165 CB GLU A1092 43.411 -62.332 13.403 1.00 72.50 C
ANISOU 2165 CB GLU A1092 9723 5906 11918 1161 48 38 C
ATOM 2166 CG GLU A1092 43.208 -62.152 11.904 1.00 85.38 C
ANISOU 2166 CG GLU A1092 11550 7410 13479 1153 85 -55 C
ATOM 2167 CD GLU A1092 43.969 -60.965 11.339 1.00 94.07 C
ANISOU 2167 CD GLU A1092 12651 8560 14531 1174 199 -133 C
ATOM 2168 OE1 GLU A1092 44.886 -60.458 12.020 1.00 85.50 O
ANISOU 2168 OE1 GLU A1092 11415 7585 13487 1208 263 -118 O
ATOM 2169 OE2 GLU A1092 43.650 -60.541 10.208 1.00100.25 O
ANISOU 2169 OE2 GLU A1092 13590 9264 15238 1158 224 -208 O
ATOM 2170 N GLN A1093 40.512 -61.905 14.948 1.00 69.55 N
ANISOU 2170 N GLN A1093 9249 5662 11516 982 -210 180 N
ATOM 2171 CA GLN A1093 39.055 -61.888 14.863 1.00 65.26 C
ANISOU 2171 CA GLN A1093 8756 5084 10956 897 -316 207 C
ATOM 2172 C GLN A1093 38.479 -60.502 15.119 1.00 69.89 C
ANISOU 2172 C GLN A1093 9285 5796 11473 833 -334 200 C
ATOM 2173 O GLN A1093 37.324 -60.246 14.760 1.00 66.99 O
ANISOU 2173 O GLN A1093 8979 5394 11079 760 -409 195 O
ATOM 2174 CB GLN A1093 38.463 -62.891 15.855 1.00 67.59 C
ANISOU 2174 CB GLN A1093 8984 5366 11333 892 -391 316 C
ATOM 2175 CG GLN A1093 38.836 -64.338 15.572 1.00 74.07 C
ANISOU 2175 CG GLN A1093 9872 6049 12222 946 -388 328 C
ATOM 2176 CD GLN A1093 38.231 -64.852 14.281 1.00 84.36 C
ANISOU 2176 CD GLN A1093 11357 7181 13514 917 -432 266 C
ATOM 2177 OE1 GLN A1093 37.079 -64.556 13.961 1.00 87.72 O
ANISOU 2177 OE1 GLN A1093 11833 7572 13922 842 -514 262 O
ATOM 2178 NE2 GLN A1093 39.008 -65.622 13.528 1.00 86.13 N
ANISOU 2178 NE2 GLN A1093 11684 7293 13749 981 -380 218 N
ATOM 2179 N LEU A1094 39.258 -59.604 15.724 1.00 67.75 N
ANISOU 2179 N LEU A1094 8898 5666 11179 859 -272 197 N
ATOM 2180 CA LEU A1094 38.785 -58.252 15.992 1.00 66.92 C
ANISOU 2180 CA LEU A1094 8737 5685 11003 802 -285 190 C
ATOM 2181 C LEU A1094 38.534 -57.454 14.719 1.00 64.48 C
ANISOU 2181 C LEU A1094 8555 5332 10613 763 -261 87 C
ATOM 2182 O LEU A1094 37.771 -56.484 14.755 1.00 62.74 O
ANISOU 2182 O LEU A1094 8325 5182 10332 699 -296 81 O
ATOM 2183 CB LEU A1094 39.795 -57.516 16.872 1.00 66.46 C
ANISOU 2183 CB LEU A1094 8533 5775 10943 847 -226 203 C
ATOM 2184 CG LEU A1094 40.040 -58.120 18.253 1.00 59.80 C
ANISOU 2184 CG LEU A1094 7562 4994 10166 890 -256 304 C
ATOM 2185 CD1 LEU A1094 41.351 -57.616 18.825 1.00 64.33 C
ANISOU 2185 CD1 LEU A1094 8021 5668 10755 957 -192 291 C
ATOM 2186 CD2 LEU A1094 38.894 -57.782 19.184 1.00 59.17 C
ANISOU 2186 CD2 LEU A1094 7422 4991 10067 834 -337 390 C
ATOM 2187 N LYS A1095 39.152 -57.836 13.597 1.00 67.21 N
ANISOU 2187 N LYS A1095 9026 5560 10951 806 -198 8 N
ATOM 2188 CA LYS A1095 38.989 -57.060 12.370 1.00 69.19 C
ANISOU 2188 CA LYS A1095 9412 5762 11115 783 -165 -93 C
ATOM 2189 C LYS A1095 37.562 -57.140 11.842 1.00 66.58 C
ANISOU 2189 C LYS A1095 9193 5351 10753 707 -276 -99 C
ATOM 2190 O LYS A1095 37.007 -56.132 11.390 1.00 67.19 O
ANISOU 2190 O LYS A1095 9316 5462 10753 656 -290 -147 O
ATOM 2191 CB LYS A1095 39.978 -57.534 11.306 1.00 74.28 C
ANISOU 2191 CB LYS A1095 10179 6283 11760 859 -67 -169 C
ATOM 2192 CG LYS A1095 41.435 -57.261 11.642 1.00 75.84 C
ANISOU 2192 CG LYS A1095 10271 6552 11993 932 57 -178 C
ATOM 2193 CD LYS A1095 42.338 -57.570 10.458 1.00 81.22 C
ANISOU 2193 CD LYS A1095 11088 7104 12667 1005 170 -257 C
ATOM 2194 CE LYS A1095 43.795 -57.285 10.786 1.00 81.64 C
ANISOU 2194 CE LYS A1095 11023 7221 12776 1077 296 -264 C
ATOM 2195 NZ LYS A1095 44.017 -55.862 11.163 1.00 93.65 N
ANISOU 2195 NZ LYS A1095 12430 8889 14263 1050 334 -283 N
ATOM 2196 N THR A1096 36.954 -58.328 11.884 1.00 69.91 N
ANISOU 2196 N THR A1096 9660 5664 11240 699 -360 -52 N
ATOM 2197 CA THR A1096 35.581 -58.467 11.409 1.00 69.65 C
ANISOU 2197 CA THR A1096 9722 5542 11200 626 -478 -55 C
ATOM 2198 C THR A1096 34.618 -57.661 12.270 1.00 67.26 C
ANISOU 2198 C THR A1096 9302 5365 10891 549 -542 8 C
ATOM 2199 O THR A1096 33.687 -57.031 11.753 1.00 69.35 O
ANISOU 2199 O THR A1096 9631 5611 11107 485 -603 -26 O
ATOM 2200 CB THR A1096 35.174 -59.940 11.387 1.00 70.79 C
ANISOU 2200 CB THR A1096 9918 5544 11435 635 -554 -9 C
ATOM 2201 OG1 THR A1096 35.246 -60.476 12.714 1.00 75.04 O
ANISOU 2201 OG1 THR A1096 10296 6160 12057 645 -564 102 O
ATOM 2202 CG2 THR A1096 36.098 -60.730 10.474 1.00 83.09 C
ANISOU 2202 CG2 THR A1096 11610 6971 12992 714 -490 -73 C
ATOM 2203 N THR A1097 34.825 -57.668 13.589 1.00 65.98 N
ANISOU 2203 N THR A1097 8971 5325 10774 558 -531 102 N
ATOM 2204 CA THR A1097 34.001 -56.846 14.469 1.00 58.55 C
ANISOU 2204 CA THR A1097 7918 4509 9819 496 -576 167 C
ATOM 2205 C THR A1097 34.235 -55.364 14.205 1.00 63.69 C
ANISOU 2205 C THR A1097 8560 5273 10365 476 -522 101 C
ATOM 2206 O THR A1097 33.305 -54.553 14.290 1.00 63.67 O
ANISOU 2206 O THR A1097 8545 5324 10322 408 -571 111 O
ATOM 2207 CB THR A1097 34.297 -57.184 15.931 1.00 58.49 C
ANISOU 2207 CB THR A1097 7750 4601 9871 529 -565 278 C
ATOM 2208 OG1 THR A1097 34.276 -58.605 16.108 1.00 59.42 O
ANISOU 2208 OG1 THR A1097 7884 4610 10085 560 -596 331 O
ATOM 2209 CG2 THR A1097 33.258 -56.551 16.848 1.00 59.00 C
ANISOU 2209 CG2 THR A1097 7719 4765 9932 467 -621 362 C
ATOM 2210 N ARG A1098 35.474 -54.994 13.875 1.00 63.29 N
ANISOU 2210 N ARG A1098 8515 5256 10277 536 -418 35 N
ATOM 2211 CA ARG A1098 35.785 -53.600 13.577 1.00 63.79 C
ANISOU 2211 CA ARG A1098 8572 5418 10247 522 -357 -32 C
ATOM 2212 C ARG A1098 35.064 -53.129 12.320 1.00 63.28 C
ANISOU 2212 C ARG A1098 8667 5269 10109 475 -384 -119 C
ATOM 2213 O ARG A1098 34.553 -52.004 12.272 1.00 67.03 O
ANISOU 2213 O ARG A1098 9132 5825 10511 423 -394 -141 O
ATOM 2214 CB ARG A1098 37.296 -53.431 13.424 1.00 59.92 C
ANISOU 2214 CB ARG A1098 8055 4956 9757 602 -235 -83 C
ATOM 2215 CG ARG A1098 37.728 -52.065 12.932 1.00 58.55 C
ANISOU 2215 CG ARG A1098 7890 4858 9497 595 -156 -164 C
ATOM 2216 CD ARG A1098 39.108 -52.138 12.308 1.00 60.16 C
ANISOU 2216 CD ARG A1098 8127 5017 9715 675 -30 -232 C
ATOM 2217 NE ARG A1098 39.130 -53.045 11.167 1.00 64.98 N
ANISOU 2217 NE ARG A1098 8910 5449 10329 707 -17 -284 N
ATOM 2218 CZ ARG A1098 40.228 -53.413 10.520 1.00 58.73 C
ANISOU 2218 CZ ARG A1098 8177 4578 9561 784 90 -335 C
ATOM 2219 NH1 ARG A1098 41.422 -52.971 10.880 1.00 66.41 N
ANISOU 2219 NH1 ARG A1098 9037 5628 10567 836 194 -342 N
ATOM 2220 NH2 ARG A1098 40.125 -54.247 9.490 1.00 67.22 N
ANISOU 2220 NH2 ARG A1098 9427 5485 10630 812 91 -378 N
ATOM 2221 N ASN A1099 35.007 -53.980 11.294 1.00 66.02 N
ANISOU 2221 N ASN A1099 9169 5447 10468 497 -401 -170 N
ATOM 2222 CA ASN A1099 34.379 -53.591 10.035 1.00 67.59 C
ANISOU 2222 CA ASN A1099 9542 5547 10592 465 -433 -261 C
ATOM 2223 C ASN A1099 32.863 -53.526 10.170 1.00 67.82 C
ANISOU 2223 C ASN A1099 9577 5557 10632 377 -569 -222 C
ATOM 2224 O ASN A1099 32.234 -52.544 9.761 1.00 72.54 O
ANISOU 2224 O ASN A1099 10218 6187 11155 326 -595 -265 O
ATOM 2225 CB ASN A1099 34.776 -54.571 8.931 1.00 68.27 C
ANISOU 2225 CB ASN A1099 9803 5448 10686 523 -417 -325 C
ATOM 2226 CG ASN A1099 36.276 -54.704 8.785 1.00 75.25 C
ANISOU 2226 CG ASN A1099 10678 6338 11574 614 -274 -357 C
ATOM 2227 OD1 ASN A1099 37.019 -53.754 9.029 1.00 74.51 O
ANISOU 2227 OD1 ASN A1099 10502 6363 11444 631 -176 -377 O
ATOM 2228 ND2 ASN A1099 36.731 -55.888 8.391 1.00 69.43 N
ANISOU 2228 ND2 ASN A1099 10024 5469 10888 673 -261 -361 N
ATOM 2229 N ALA A1100 32.259 -54.565 10.746 1.00 68.43 N
ANISOU 2229 N ALA A1100 9608 5580 10811 359 -656 -136 N
ATOM 2230 CA ALA A1100 30.808 -54.680 10.785 1.00 65.73 C
ANISOU 2230 CA ALA A1100 9278 5187 10508 279 -788 -96 C
ATOM 2231 C ALA A1100 30.165 -53.900 11.923 1.00 71.88 C
ANISOU 2231 C ALA A1100 9895 6121 11294 222 -809 -8 C
ATOM 2232 O ALA A1100 28.934 -53.798 11.957 1.00 82.60 O
ANISOU 2232 O ALA A1100 11253 7449 12683 151 -908 25 O
ATOM 2233 CB ALA A1100 30.404 -56.153 10.888 1.00 74.86 C
ANISOU 2233 CB ALA A1100 10455 6205 11784 285 -868 -40 C
ATOM 2234 N TYR A1101 30.950 -53.350 12.849 1.00 66.53 N
ANISOU 2234 N TYR A1101 9084 5601 10593 252 -722 31 N
ATOM 2235 CA TYR A1101 30.370 -52.650 13.990 1.00 73.11 C
ANISOU 2235 CA TYR A1101 9772 6578 11427 208 -739 120 C
ATOM 2236 C TYR A1101 31.099 -51.350 14.305 1.00 66.53 C
ANISOU 2236 C TYR A1101 8872 5910 10498 222 -651 89 C
ATOM 2237 O TYR A1101 30.506 -50.268 14.236 1.00 63.26 O
ANISOU 2237 O TYR A1101 8454 5569 10015 168 -665 73 O
ATOM 2238 CB TYR A1101 30.378 -53.548 15.230 1.00 65.66 C
ANISOU 2238 CB TYR A1101 8706 5658 10586 233 -752 244 C
ATOM 2239 CG TYR A1101 29.451 -54.739 15.148 1.00 75.94 C
ANISOU 2239 CG TYR A1101 10044 6813 11999 206 -846 299 C
ATOM 2240 CD1 TYR A1101 28.126 -54.640 15.552 1.00 80.09 C
ANISOU 2240 CD1 TYR A1101 10525 7330 12576 135 -928 374 C
ATOM 2241 CD2 TYR A1101 29.904 -55.965 14.680 1.00 72.13 C
ANISOU 2241 CD2 TYR A1101 9634 6195 11577 252 -851 279 C
ATOM 2242 CE1 TYR A1101 27.276 -55.728 15.486 1.00 84.04 C
ANISOU 2242 CE1 TYR A1101 11047 7688 13195 109 -1014 427 C
ATOM 2243 CE2 TYR A1101 29.061 -57.059 14.610 1.00 75.69 C
ANISOU 2243 CE2 TYR A1101 10115 6508 12137 226 -941 329 C
ATOM 2244 CZ TYR A1101 27.749 -56.935 15.014 1.00 83.81 C
ANISOU 2244 CZ TYR A1101 11092 7527 13225 154 -1024 402 C
ATOM 2245 OH TYR A1101 26.909 -58.024 14.944 1.00 91.56 O
ANISOU 2245 OH TYR A1101 12094 8362 14332 127 -1113 453 O
ATOM 2246 N ILE A1102 32.383 -51.450 14.654 1.00 66.28 N
ANISOU 2246 N ILE A1102 11765 3672 9746 2072 -805 -643 N
ATOM 2247 CA ILE A1102 33.106 -50.303 15.200 1.00 68.26 C
ANISOU 2247 CA ILE A1102 11839 4150 9946 2180 -749 -586 C
ATOM 2248 C ILE A1102 33.205 -49.182 14.174 1.00 62.46 C
ANISOU 2248 C ILE A1102 10992 3618 9121 2203 -672 -727 C
ATOM 2249 O ILE A1102 33.101 -47.998 14.518 1.00 62.69 O
ANISOU 2249 O ILE A1102 10902 3823 9095 2169 -635 -669 O
ATOM 2250 CB ILE A1102 34.495 -50.740 15.699 1.00 65.53 C
ANISOU 2250 CB ILE A1102 11436 3825 9639 2419 -742 -567 C
ATOM 2251 CG1 ILE A1102 34.356 -51.885 16.704 1.00 69.33 C
ANISOU 2251 CG1 ILE A1102 12042 4096 10205 2392 -821 -424 C
ATOM 2252 CG2 ILE A1102 35.232 -49.566 16.327 1.00 63.58 C
ANISOU 2252 CG2 ILE A1102 10997 3816 9343 2518 -694 -500 C
ATOM 2253 CD1 ILE A1102 33.465 -51.552 17.885 1.00 72.76 C
ANISOU 2253 CD1 ILE A1102 12490 4518 10637 2210 -857 -219 C
ATOM 2254 N GLN A1103 33.406 -49.531 12.902 1.00 63.49 N
ANISOU 2254 N GLN A1103 11163 3731 9231 2260 -646 -912 N
ATOM 2255 CA GLN A1103 33.509 -48.504 11.870 1.00 62.08 C
ANISOU 2255 CA GLN A1103 10881 3748 8956 2281 -568 -1048 C
ATOM 2256 C GLN A1103 32.178 -47.796 11.650 1.00 65.19 C
ANISOU 2256 C GLN A1103 11302 4162 9303 2051 -584 -1030 C
ATOM 2257 O GLN A1103 32.159 -46.607 11.311 1.00 61.08 O
ANISOU 2257 O GLN A1103 10668 3836 8704 2042 -524 -1064 O
ATOM 2258 CB GLN A1103 34.015 -49.119 10.564 1.00 64.67 C
ANISOU 2258 CB GLN A1103 11257 4050 9264 2392 -535 -1245 C
ATOM 2259 CG GLN A1103 34.352 -48.099 9.485 1.00 71.54 C
ANISOU 2259 CG GLN A1103 12009 5145 10028 2447 -440 -1384 C
ATOM 2260 CD GLN A1103 34.983 -48.725 8.255 1.00 79.02 C
ANISOU 2260 CD GLN A1103 12994 6081 10948 2575 -397 -1569 C
ATOM 2261 OE1 GLN A1103 35.191 -49.937 8.196 1.00 79.00 O
ANISOU 2261 OE1 GLN A1103 13109 5895 11010 2634 -442 -1602 O
ATOM 2262 NE2 GLN A1103 35.293 -47.897 7.265 1.00 80.29 N
ANISOU 2262 NE2 GLN A1103 13057 6441 11009 2620 -307 -1688 N
ATOM 2263 N LYS A1104 31.059 -48.499 11.844 1.00 67.97 N
ANISOU 2263 N LYS A1104 11796 4322 9706 1858 -665 -972 N
ATOM 2264 CA LYS A1104 29.754 -47.862 11.700 1.00 59.66 C
ANISOU 2264 CA LYS A1104 10760 3290 8620 1624 -687 -942 C
ATOM 2265 C LYS A1104 29.517 -46.834 12.799 1.00 57.50 C
ANISOU 2265 C LYS A1104 10337 3184 8326 1540 -657 -764 C
ATOM 2266 O LYS A1104 28.916 -45.782 12.552 1.00 66.14 O
ANISOU 2266 O LYS A1104 11291 4489 9351 1401 -609 -753 O
ATOM 2267 CB LYS A1104 28.650 -48.918 11.708 1.00 61.31 C
ANISOU 2267 CB LYS A1104 11127 3272 8898 1425 -777 -909 C
ATOM 2268 CG LYS A1104 28.715 -49.890 10.546 1.00 73.14 C
ANISOU 2268 CG LYS A1104 12738 4648 10403 1460 -800 -1084 C
ATOM 2269 CD LYS A1104 28.372 -49.203 9.237 1.00 71.74 C
ANISOU 2269 CD LYS A1104 12533 4595 10130 1416 -770 -1249 C
ATOM 2270 CE LYS A1104 28.376 -50.191 8.083 1.00 79.21 C
ANISOU 2270 CE LYS A1104 13602 5421 11076 1442 -798 -1421 C
ATOM 2271 NZ LYS A1104 27.406 -51.300 8.300 1.00 80.48 N
ANISOU 2271 NZ LYS A1104 13909 5347 11325 1261 -898 -1370 N
ATOM 2272 N TYR A1105 29.977 -47.121 14.020 1.00 61.34 N
ANISOU 2272 N TYR A1105 10825 3616 8865 1612 -679 -616 N
ATOM 2273 CA TYR A1105 29.823 -46.163 15.111 1.00 63.36 C
ANISOU 2273 CA TYR A1105 10912 4071 9090 1533 -640 -443 C
ATOM 2274 C TYR A1105 30.683 -44.926 14.886 1.00 56.90 C
ANISOU 2274 C TYR A1105 9882 3546 8193 1653 -547 -492 C
ATOM 2275 O TYR A1105 30.247 -43.803 15.164 1.00 59.38 O
ANISOU 2275 O TYR A1105 10038 4076 8447 1533 -498 -423 O
ATOM 2276 CB TYR A1105 30.172 -46.822 16.447 1.00 64.28 C
ANISOU 2276 CB TYR A1105 11098 4054 9273 1595 -693 -279 C
ATOM 2277 CG TYR A1105 30.247 -45.850 17.608 1.00 79.70 C
ANISOU 2277 CG TYR A1105 12881 6219 11182 1559 -653 -114 C
ATOM 2278 CD1 TYR A1105 29.100 -45.454 18.283 1.00 84.46 C
ANISOU 2278 CD1 TYR A1105 13447 6875 11767 1329 -651 28 C
ATOM 2279 CD2 TYR A1105 31.466 -45.331 18.031 1.00 79.78 C
ANISOU 2279 CD2 TYR A1105 12765 6378 11168 1758 -617 -105 C
ATOM 2280 CE1 TYR A1105 29.162 -44.565 19.343 1.00 88.56 C
ANISOU 2280 CE1 TYR A1105 13822 7587 12238 1304 -614 168 C
ATOM 2281 CE2 TYR A1105 31.538 -44.441 19.090 1.00 74.69 C
ANISOU 2281 CE2 TYR A1105 11976 5923 10480 1724 -590 37 C
ATOM 2282 CZ TYR A1105 30.383 -44.063 19.742 1.00 85.95 C
ANISOU 2282 CZ TYR A1105 13382 7394 11881 1500 -588 170 C
ATOM 2283 OH TYR A1105 30.449 -43.180 20.797 1.00 85.76 O
ANISOU 2283 OH TYR A1105 13223 7555 11805 1474 -559 301 O
ATOM 2284 N LEU A1106 31.909 -45.113 14.390 1.00 60.68 N
ANISOU 2284 N LEU A1106 10351 4034 8672 1890 -520 -610 N
ATOM 2285 CA LEU A1106 32.808 -43.984 14.168 1.00 61.07 C
ANISOU 2285 CA LEU A1106 10196 4356 8653 2006 -430 -654 C
ATOM 2286 C LEU A1106 32.227 -43.007 13.154 1.00 51.87 C
ANISOU 2286 C LEU A1106 8935 3372 7401 1879 -367 -744 C
ATOM 2287 O LEU A1106 32.226 -41.791 13.375 1.00 55.82 O
ANISOU 2287 O LEU A1106 9257 4110 7842 1823 -308 -691 O
ATOM 2288 CB LEU A1106 34.175 -44.488 13.704 1.00 59.50 C
ANISOU 2288 CB LEU A1106 10011 4119 8476 2281 -411 -775 C
ATOM 2289 CG LEU A1106 35.143 -43.417 13.189 1.00 66.86 C
ANISOU 2289 CG LEU A1106 10739 5323 9340 2404 -310 -854 C
ATOM 2290 CD1 LEU A1106 35.571 -42.485 14.313 1.00 62.54 C
ANISOU 2290 CD1 LEU A1106 10010 4970 8784 2405 -290 -707 C
ATOM 2291 CD2 LEU A1106 36.354 -44.047 12.515 1.00 64.24 C
ANISOU 2291 CD2 LEU A1106 10430 4948 9030 2657 -284 -996 C
ATOM 2292 N GLU A 219 31.725 -43.523 12.031 1.00 57.86 N
ANISOU 2292 N GLU A 219 9818 4018 8148 1834 -384 -881 N
ATOM 2293 CA GLU A 219 31.222 -42.640 10.985 1.00 65.14 C
ANISOU 2293 CA GLU A 219 10662 5110 8980 1730 -330 -974 C
ATOM 2294 C GLU A 219 29.902 -41.989 11.377 1.00 58.97 C
ANISOU 2294 C GLU A 219 9825 4401 8179 1474 -347 -860 C
ATOM 2295 O GLU A 219 29.606 -40.877 10.924 1.00 61.65 O
ANISOU 2295 O GLU A 219 10033 4949 8441 1395 -292 -877 O
ATOM 2296 CB GLU A 219 31.079 -43.413 9.674 1.00 66.39 C
ANISOU 2296 CB GLU A 219 10978 5124 9123 1762 -351 -1158 C
ATOM 2297 CG GLU A 219 32.410 -43.851 9.080 1.00 75.65 C
ANISOU 2297 CG GLU A 219 12177 6277 10291 2028 -308 -1297 C
ATOM 2298 CD GLU A 219 32.249 -44.656 7.806 1.00 91.21 C
ANISOU 2298 CD GLU A 219 14322 8097 12238 2066 -331 -1488 C
ATOM 2299 OE1 GLU A 219 31.162 -45.234 7.599 1.00 91.98 O
ANISOU 2299 OE1 GLU A 219 14564 8026 12358 1899 -413 -1498 O
ATOM 2300 OE2 GLU A 219 33.210 -44.708 7.010 1.00 89.38 O
ANISOU 2300 OE2 GLU A 219 14050 7947 11962 2238 -261 -1616 O
ATOM 2301 N ARG A 220 29.100 -42.651 12.214 1.00 57.84 N
ANISOU 2301 N ARG A 220 9779 4093 8106 1346 -420 -740 N
ATOM 2302 CA ARG A 220 27.864 -42.031 12.680 1.00 53.88 C
ANISOU 2302 CA ARG A 220 9208 3674 7589 1112 -429 -622 C
ATOM 2303 C ARG A 220 28.135 -40.994 13.763 1.00 52.81 C
ANISOU 2303 C ARG A 220 8898 3741 7428 1115 -378 -480 C
ATOM 2304 O ARG A 220 27.504 -39.932 13.780 1.00 46.98 O
ANISOU 2304 O ARG A 220 8031 3186 6635 988 -340 -439 O
ATOM 2305 CB ARG A 220 26.891 -43.095 13.190 1.00 52.13 C
ANISOU 2305 CB ARG A 220 9144 3214 7449 962 -517 -538 C
ATOM 2306 CG ARG A 220 26.304 -43.987 12.103 1.00 69.80 C
ANISOU 2306 CG ARG A 220 11550 5260 9710 895 -581 -673 C
ATOM 2307 CD ARG A 220 25.813 -43.178 10.909 1.00 76.92 C
ANISOU 2307 CD ARG A 220 12376 6322 10526 815 -549 -794 C
ATOM 2308 NE ARG A 220 26.783 -43.169 9.820 1.00 79.64 N
ANISOU 2308 NE ARG A 220 12742 6703 10816 1003 -509 -973 N
ATOM 2309 CZ ARG A 220 26.705 -42.388 8.751 1.00 86.14 C
ANISOU 2309 CZ ARG A 220 13492 7691 11546 992 -464 -1085 C
ATOM 2310 NH1 ARG A 220 25.714 -41.525 8.595 1.00 88.26 N
ANISOU 2310 NH1 ARG A 220 13661 8105 11769 809 -459 -1043 N
ATOM 2311 NH2 ARG A 220 27.649 -42.471 7.816 1.00 83.45 N
ANISOU 2311 NH2 ARG A 220 13180 7375 11154 1173 -421 -1242 N
ATOM 2312 N ALA A 221 29.069 -41.288 14.673 1.00 55.26 N
ANISOU 2312 N ALA A 221 9205 4017 7774 1263 -382 -407 N
ATOM 2313 CA ALA A 221 29.458 -40.306 15.680 1.00 46.44 C
ANISOU 2313 CA ALA A 221 7926 3093 6625 1285 -340 -288 C
ATOM 2314 C ALA A 221 30.159 -39.114 15.042 1.00 51.56 C
ANISOU 2314 C ALA A 221 8406 3984 7200 1366 -259 -374 C
ATOM 2315 O ALA A 221 30.009 -37.977 15.504 1.00 48.47 O
ANISOU 2315 O ALA A 221 7868 3787 6760 1302 -218 -302 O
ATOM 2316 CB ALA A 221 30.358 -40.958 16.729 1.00 51.74 C
ANISOU 2316 CB ALA A 221 8641 3667 7350 1437 -375 -200 C
ATOM 2317 N ARG A 222 30.935 -39.357 13.984 1.00 55.00 N
ANISOU 2317 N ARG A 222 8865 4407 7624 1509 -234 -527 N
ATOM 2318 CA ARG A 222 31.574 -38.262 13.264 1.00 52.22 C
ANISOU 2318 CA ARG A 222 8361 4281 7200 1574 -151 -610 C
ATOM 2319 C ARG A 222 30.547 -37.435 12.500 1.00 50.94 C
ANISOU 2319 C ARG A 222 8152 4232 6969 1398 -124 -645 C
ATOM 2320 O ARG A 222 30.671 -36.209 12.410 1.00 50.37 O
ANISOU 2320 O ARG A 222 7928 4373 6836 1372 -66 -632 O
ATOM 2321 CB ARG A 222 32.635 -38.815 12.315 1.00 56.54 C
ANISOU 2321 CB ARG A 222 8951 4783 7748 1773 -123 -765 C
ATOM 2322 CG ARG A 222 33.418 -37.767 11.550 1.00 61.20 C
ANISOU 2322 CG ARG A 222 9385 5603 8264 1853 -29 -848 C
ATOM 2323 CD ARG A 222 34.400 -38.433 10.600 1.00 70.10 C
ANISOU 2323 CD ARG A 222 10567 6677 9392 2050 4 -1003 C
ATOM 2324 NE ARG A 222 33.720 -39.244 9.597 1.00 77.85 N
ANISOU 2324 NE ARG A 222 11722 7498 10361 2005 -27 -1122 N
ATOM 2325 CZ ARG A 222 34.310 -40.175 8.860 1.00 87.48 C
ANISOU 2325 CZ ARG A 222 13055 8591 11592 2163 -25 -1259 C
ATOM 2326 NH1 ARG A 222 35.593 -40.464 9.008 1.00 81.46 N
ANISOU 2326 NH1 ARG A 222 12248 7842 10862 2384 9 -1292 N
ATOM 2327 NH2 ARG A 222 33.594 -40.837 7.954 1.00 83.65 N
ANISOU 2327 NH2 ARG A 222 12732 7964 11087 2100 -62 -1368 N
ATOM 2328 N SER A 223 29.522 -38.089 11.949 1.00 54.34 N
ANISOU 2328 N SER A 223 8714 4520 7411 1274 -174 -687 N
ATOM 2329 CA SER A 223 28.502 -37.364 11.198 1.00 53.43 C
ANISOU 2329 CA SER A 223 8560 4507 7234 1109 -162 -721 C
ATOM 2330 C SER A 223 27.660 -36.486 12.115 1.00 48.39 C
ANISOU 2330 C SER A 223 7811 3987 6587 952 -160 -573 C
ATOM 2331 O SER A 223 27.286 -35.368 11.742 1.00 48.79 O
ANISOU 2331 O SER A 223 7748 4216 6573 876 -119 -578 O
ATOM 2332 CB SER A 223 27.617 -38.347 10.434 1.00 56.58 C
ANISOU 2332 CB SER A 223 9127 4716 7655 1013 -230 -802 C
ATOM 2333 OG SER A 223 26.675 -37.663 9.625 1.00 64.52 O
ANISOU 2333 OG SER A 223 10092 5825 8596 865 -226 -844 O
ATOM 2334 N THR A 224 27.353 -36.974 13.318 1.00 46.97 N
ANISOU 2334 N THR A 224 7668 3710 6469 905 -201 -440 N
ATOM 2335 CA THR A 224 26.579 -36.174 14.262 1.00 42.67 C
ANISOU 2335 CA THR A 224 7022 3280 5911 768 -192 -300 C
ATOM 2336 C THR A 224 27.364 -34.950 14.720 1.00 44.88 C
ANISOU 2336 C THR A 224 7137 3776 6141 851 -128 -263 C
ATOM 2337 O THR A 224 26.803 -33.854 14.838 1.00 42.30 O
ANISOU 2337 O THR A 224 6696 3609 5766 753 -97 -220 O
ATOM 2338 CB THR A 224 26.164 -37.033 15.457 1.00 48.91 C
ANISOU 2338 CB THR A 224 7897 3917 6769 712 -243 -164 C
ATOM 2339 OG1 THR A 224 25.395 -38.152 14.997 1.00 46.29 O
ANISOU 2339 OG1 THR A 224 7720 3378 6491 618 -307 -198 O
ATOM 2340 CG2 THR A 224 25.327 -36.224 16.437 1.00 44.81 C
ANISOU 2340 CG2 THR A 224 7275 3524 6227 574 -225 -22 C
ATOM 2341 N LEU A 225 28.666 -35.111 14.970 1.00 44.21 N
ANISOU 2341 N LEU A 225 7035 3694 6069 1031 -113 -281 N
ATOM 2342 CA LEU A 225 29.481 -33.974 15.390 1.00 41.50 C
ANISOU 2342 CA LEU A 225 6534 3550 5685 1107 -61 -251 C
ATOM 2343 C LEU A 225 29.621 -32.947 14.273 1.00 38.99 C
ANISOU 2343 C LEU A 225 6118 3398 5298 1102 0 -351 C
ATOM 2344 O LEU A 225 29.618 -31.738 14.530 1.00 39.08 O
ANISOU 2344 O LEU A 225 5998 3585 5264 1062 38 -308 O
ATOM 2345 CB LEU A 225 30.856 -34.452 15.856 1.00 38.85 C
ANISOU 2345 CB LEU A 225 6197 3178 5387 1302 -66 -252 C
ATOM 2346 CG LEU A 225 30.910 -35.010 17.279 1.00 49.88 C
ANISOU 2346 CG LEU A 225 7638 4483 6829 1319 -119 -114 C
ATOM 2347 CD1 LEU A 225 32.285 -35.582 17.585 1.00 43.38 C
ANISOU 2347 CD1 LEU A 225 6822 3612 6047 1527 -135 -130 C
ATOM 2348 CD2 LEU A 225 30.544 -33.928 18.283 1.00 47.21 C
ANISOU 2348 CD2 LEU A 225 7185 4303 6448 1229 -104 4 C
ATOM 2349 N GLN A 226 29.739 -33.405 13.025 1.00 40.54 N
ANISOU 2349 N GLN A 226 6384 3538 5481 1141 10 -483 N
ATOM 2350 CA GLN A 226 29.842 -32.468 11.913 1.00 39.05 C
ANISOU 2350 CA GLN A 226 6116 3505 5218 1132 69 -574 C
ATOM 2351 C GLN A 226 28.543 -31.700 11.700 1.00 35.82 C
ANISOU 2351 C GLN A 226 5674 3171 4766 947 62 -540 C
ATOM 2352 O GLN A 226 28.578 -30.534 11.290 1.00 34.65 O
ANISOU 2352 O GLN A 226 5417 3192 4555 921 109 -551 O
ATOM 2353 CB GLN A 226 30.246 -33.208 10.640 1.00 41.95 C
ANISOU 2353 CB GLN A 226 6579 3790 5569 1222 80 -726 C
ATOM 2354 CG GLN A 226 31.687 -33.689 10.652 1.00 53.96 C
ANISOU 2354 CG GLN A 226 8092 5292 7118 1430 110 -778 C
ATOM 2355 CD GLN A 226 32.005 -34.607 9.492 1.00 67.73 C
ANISOU 2355 CD GLN A 226 9957 6924 8851 1527 115 -930 C
ATOM 2356 OE1 GLN A 226 31.121 -35.267 8.948 1.00 64.28 O
ANISOU 2356 OE1 GLN A 226 9655 6355 8413 1441 67 -982 O
ATOM 2357 NE2 GLN A 226 33.275 -34.652 9.105 1.00 81.53 N
ANISOU 2357 NE2 GLN A 226 11657 8730 10591 1708 174 -1005 N
ATOM 2358 N LYS A 227 27.394 -32.326 11.969 1.00 40.73 N
ANISOU 2358 N LYS A 227 6383 3668 5422 818 2 -495 N
ATOM 2359 CA LYS A 227 26.131 -31.601 11.887 1.00 40.14 C
ANISOU 2359 CA LYS A 227 6260 3673 5316 646 -8 -452 C
ATOM 2360 C LYS A 227 26.041 -30.533 12.969 1.00 34.77 C
ANISOU 2360 C LYS A 227 5450 3137 4625 610 20 -330 C
ATOM 2361 O LYS A 227 25.504 -29.445 12.735 1.00 39.41 O
ANISOU 2361 O LYS A 227 5946 3864 5163 532 43 -318 O
ATOM 2362 CB LYS A 227 24.950 -32.566 11.997 1.00 43.41 C
ANISOU 2362 CB LYS A 227 6787 3924 5782 512 -78 -424 C
ATOM 2363 CG LYS A 227 24.746 -33.472 10.797 1.00 46.14 C
ANISOU 2363 CG LYS A 227 7266 4136 6129 507 -118 -554 C
ATOM 2364 CD LYS A 227 23.424 -34.220 10.908 1.00 60.37 C
ANISOU 2364 CD LYS A 227 9154 5803 7983 338 -192 -517 C
ATOM 2365 CE LYS A 227 23.338 -34.999 12.215 1.00 67.74 C
ANISOU 2365 CE LYS A 227 10137 6605 8997 319 -221 -392 C
ATOM 2366 NZ LYS A 227 22.033 -35.700 12.387 1.00 75.56 N
ANISOU 2366 NZ LYS A 227 11198 7469 10042 138 -287 -340 N
ATOM 2367 N GLU A 228 26.557 -30.828 14.164 1.00 33.93 N
ANISOU 2367 N GLU A 228 5339 2993 4559 671 13 -241 N
ATOM 2368 CA GLU A 228 26.538 -29.840 15.237 1.00 36.01 C
ANISOU 2368 CA GLU A 228 5489 3390 4804 648 35 -134 C
ATOM 2369 C GLU A 228 27.449 -28.661 14.918 1.00 31.64 C
ANISOU 2369 C GLU A 228 4814 3009 4199 729 89 -175 C
ATOM 2370 O GLU A 228 27.139 -27.519 15.273 1.00 31.13 O
ANISOU 2370 O GLU A 228 4650 3082 4097 672 112 -125 O
ATOM 2371 CB GLU A 228 26.935 -30.490 16.561 1.00 33.29 C
ANISOU 2371 CB GLU A 228 5181 2962 4505 702 8 -33 C
ATOM 2372 CG GLU A 228 25.795 -31.221 17.251 1.00 40.79 C
ANISOU 2372 CG GLU A 228 6211 3795 5492 576 -34 62 C
ATOM 2373 CD GLU A 228 26.232 -31.913 18.526 1.00 46.90 C
ANISOU 2373 CD GLU A 228 7037 4480 6303 635 -61 167 C
ATOM 2374 OE1 GLU A 228 26.913 -32.957 18.434 1.00 44.35 O
ANISOU 2374 OE1 GLU A 228 6812 4012 6027 735 -93 137 O
ATOM 2375 OE2 GLU A 228 25.903 -31.407 19.619 1.00 49.36 O
ANISOU 2375 OE2 GLU A 228 7296 4868 6592 588 -53 278 O
ATOM 2376 N VAL A 229 28.576 -28.915 14.249 1.00 32.24 N
ANISOU 2376 N VAL A 229 4895 3080 4275 861 112 -264 N
ATOM 2377 CA VAL A 229 29.445 -27.820 13.827 1.00 31.43 C
ANISOU 2377 CA VAL A 229 4674 3142 4127 925 169 -304 C
ATOM 2378 C VAL A 229 28.730 -26.948 12.803 1.00 35.71 C
ANISOU 2378 C VAL A 229 5183 3780 4606 828 196 -352 C
ATOM 2379 O VAL A 229 28.720 -25.716 12.907 1.00 36.56 O
ANISOU 2379 O VAL A 229 5187 4031 4674 792 226 -321 O
ATOM 2380 CB VAL A 229 30.772 -28.365 13.271 1.00 36.39 C
ANISOU 2380 CB VAL A 229 5311 3746 4769 1088 196 -392 C
ATOM 2381 CG1 VAL A 229 31.630 -27.227 12.743 1.00 39.84 C
ANISOU 2381 CG1 VAL A 229 5620 4360 5159 1137 262 -431 C
ATOM 2382 CG2 VAL A 229 31.516 -29.137 14.340 1.00 33.29 C
ANISOU 2382 CG2 VAL A 229 4941 3269 4440 1195 162 -336 C
ATOM 2383 N HIS A 230 28.110 -27.582 11.803 1.00 35.73 N
ANISOU 2383 N HIS A 230 5280 3698 4597 783 179 -429 N
ATOM 2384 CA HIS A 230 27.420 -26.835 10.756 1.00 37.93 C
ANISOU 2384 CA HIS A 230 5538 4062 4810 696 194 -478 C
ATOM 2385 C HIS A 230 26.239 -26.054 11.321 1.00 33.21 C
ANISOU 2385 C HIS A 230 4887 3527 4205 558 172 -388 C
ATOM 2386 O HIS A 230 26.015 -24.896 10.948 1.00 30.54 O
ANISOU 2386 O HIS A 230 4471 3320 3815 516 198 -385 O
ATOM 2387 CB HIS A 230 26.957 -27.792 9.656 1.00 37.27 C
ANISOU 2387 CB HIS A 230 5580 3864 4718 676 164 -579 C
ATOM 2388 CG HIS A 230 26.436 -27.105 8.434 1.00 57.86 C
ANISOU 2388 CG HIS A 230 8178 6561 7247 612 177 -644 C
ATOM 2389 ND1 HIS A 230 25.155 -26.604 8.351 1.00 55.02 N
ANISOU 2389 ND1 HIS A 230 7800 6235 6868 470 140 -605 N
ATOM 2390 CD2 HIS A 230 27.022 -26.838 7.242 1.00 56.15 C
ANISOU 2390 CD2 HIS A 230 7965 6409 6959 673 222 -742 C
ATOM 2391 CE1 HIS A 230 24.975 -26.056 7.162 1.00 53.66 C
ANISOU 2391 CE1 HIS A 230 7628 6142 6619 448 154 -675 C
ATOM 2392 NE2 HIS A 230 26.092 -26.185 6.470 1.00 58.59 N
ANISOU 2392 NE2 HIS A 230 8270 6787 7206 567 206 -758 N
ATOM 2393 N ALA A 231 25.473 -26.670 12.223 1.00 29.92 N
ANISOU 2393 N ALA A 231 4512 3017 3840 490 127 -312 N
ATOM 2394 CA ALA A 231 24.350 -25.969 12.836 1.00 35.38 C
ANISOU 2394 CA ALA A 231 5143 3773 4525 368 115 -224 C
ATOM 2395 C ALA A 231 24.829 -24.809 13.701 1.00 31.93 C
ANISOU 2395 C ALA A 231 4594 3470 4068 403 151 -156 C
ATOM 2396 O ALA A 231 24.197 -23.747 13.731 1.00 33.17 O
ANISOU 2396 O ALA A 231 4678 3736 4190 336 162 -125 O
ATOM 2397 CB ALA A 231 23.504 -26.944 13.655 1.00 31.77 C
ANISOU 2397 CB ALA A 231 4753 3190 4128 290 69 -151 C
ATOM 2398 N ALA A 232 25.948 -24.986 14.406 1.00 28.02 N
ANISOU 2398 N ALA A 232 4085 2967 3593 511 164 -134 N
ATOM 2399 CA ALA A 232 26.455 -23.897 15.234 1.00 30.01 C
ANISOU 2399 CA ALA A 232 4235 3342 3826 541 189 -77 C
ATOM 2400 C ALA A 232 27.000 -22.759 14.384 1.00 35.45 C
ANISOU 2400 C ALA A 232 4844 4159 4465 566 231 -134 C
ATOM 2401 O ALA A 232 26.895 -21.590 14.774 1.00 34.85 O
ANISOU 2401 O ALA A 232 4687 4193 4361 536 245 -93 O
ATOM 2402 CB ALA A 232 27.531 -24.409 16.192 1.00 31.39 C
ANISOU 2402 CB ALA A 232 4413 3478 4036 650 180 -40 C
ATOM 2403 N LYS A 233 27.576 -23.075 13.221 1.00 35.34 N
ANISOU 2403 N LYS A 233 4859 4132 4437 619 253 -227 N
ATOM 2404 CA LYS A 233 28.038 -22.021 12.325 1.00 32.04 C
ANISOU 2404 CA LYS A 233 4373 3836 3966 631 298 -275 C
ATOM 2405 C LYS A 233 26.869 -21.200 11.797 1.00 29.51 C
ANISOU 2405 C LYS A 233 4040 3572 3599 517 291 -267 C
ATOM 2406 O LYS A 233 26.970 -19.974 11.673 1.00 29.45 O
ANISOU 2406 O LYS A 233 3957 3678 3555 498 316 -251 O
ATOM 2407 CB LYS A 233 28.840 -22.618 11.169 1.00 31.77 C
ANISOU 2407 CB LYS A 233 4379 3776 3915 713 330 -377 C
ATOM 2408 CG LYS A 233 30.195 -23.180 11.573 1.00 42.16 C
ANISOU 2408 CG LYS A 233 5677 5070 5273 847 349 -391 C
ATOM 2409 CD LYS A 233 30.966 -23.668 10.356 1.00 47.51 C
ANISOU 2409 CD LYS A 233 6385 5742 5925 935 394 -499 C
ATOM 2410 CE LYS A 233 32.347 -24.177 10.732 1.00 53.07 C
ANISOU 2410 CE LYS A 233 7052 6438 6675 1081 416 -515 C
ATOM 2411 NZ LYS A 233 33.113 -24.616 9.532 1.00 50.38 N
ANISOU 2411 NZ LYS A 233 6732 6105 6304 1177 472 -624 N
ATOM 2412 N SER A 234 25.751 -21.857 11.483 1.00 29.03 N
ANISOU 2412 N SER A 234 4052 3433 3545 440 252 -278 N
ATOM 2413 CA SER A 234 24.582 -21.126 11.004 1.00 30.05 C
ANISOU 2413 CA SER A 234 4163 3619 3638 336 235 -268 C
ATOM 2414 C SER A 234 24.051 -20.175 12.071 1.00 29.83 C
ANISOU 2414 C SER A 234 4056 3663 3616 289 232 -175 C
ATOM 2415 O SER A 234 23.720 -19.020 11.776 1.00 30.34 O
ANISOU 2415 O SER A 234 4064 3825 3640 255 242 -165 O
ATOM 2416 CB SER A 234 23.496 -22.107 10.564 1.00 27.52 C
ANISOU 2416 CB SER A 234 3926 3196 3333 258 184 -294 C
ATOM 2417 OG SER A 234 23.994 -22.998 9.582 1.00 37.24 O
ANISOU 2417 OG SER A 234 5244 4353 4554 307 184 -390 O
ATOM 2418 N LEU A 235 23.977 -20.639 13.323 1.00 30.26 N
ANISOU 2418 N LEU A 235 4112 3670 3715 292 219 -107 N
ATOM 2419 CA LEU A 235 23.499 -19.788 14.409 1.00 27.09 C
ANISOU 2419 CA LEU A 235 3644 3337 3312 258 220 -24 C
ATOM 2420 C LEU A 235 24.503 -18.696 14.756 1.00 30.33 C
ANISOU 2420 C LEU A 235 3982 3843 3698 323 250 -16 C
ATOM 2421 O LEU A 235 24.115 -17.637 15.264 1.00 26.63 O
ANISOU 2421 O LEU A 235 3455 3454 3209 294 254 27 O
ATOM 2422 CB LEU A 235 23.186 -20.642 15.638 1.00 29.35 C
ANISOU 2422 CB LEU A 235 3963 3548 3641 246 201 48 C
ATOM 2423 CG LEU A 235 22.122 -21.720 15.419 1.00 30.34 C
ANISOU 2423 CG LEU A 235 4156 3572 3800 162 168 54 C
ATOM 2424 CD1 LEU A 235 22.072 -22.695 16.587 1.00 31.52 C
ANISOU 2424 CD1 LEU A 235 4353 3631 3994 162 154 128 C
ATOM 2425 CD2 LEU A 235 20.760 -21.081 15.192 1.00 26.19 C
ANISOU 2425 CD2 LEU A 235 3583 3110 3257 58 159 75 C
ATOM 2426 N ALA A 236 25.791 -18.932 14.499 1.00 30.41 N
ANISOU 2426 N ALA A 236 3991 3848 3714 410 270 -57 N
ATOM 2427 CA ALA A 236 26.787 -17.886 14.704 1.00 31.24 C
ANISOU 2427 CA ALA A 236 4019 4046 3803 460 295 -53 C
ATOM 2428 C ALA A 236 26.680 -16.797 13.644 1.00 33.71 C
ANISOU 2428 C ALA A 236 4297 4443 4068 425 319 -88 C
ATOM 2429 O ALA A 236 26.982 -15.631 13.922 1.00 28.06 O
ANISOU 2429 O ALA A 236 3518 3809 3336 422 330 -64 O
ATOM 2430 CB ALA A 236 28.191 -18.488 14.707 1.00 29.52 C
ANISOU 2430 CB ALA A 236 3797 3807 3611 563 310 -85 C
ATOM 2431 N ILE A 237 26.261 -17.157 12.429 1.00 30.65 N
ANISOU 2431 N ILE A 237 3957 4033 3656 398 323 -144 N
ATOM 2432 CA ILE A 237 26.062 -16.155 11.385 1.00 28.17 C
ANISOU 2432 CA ILE A 237 3620 3794 3286 362 341 -169 C
ATOM 2433 C ILE A 237 24.975 -15.172 11.799 1.00 26.26 C
ANISOU 2433 C ILE A 237 3347 3599 3033 291 316 -115 C
ATOM 2434 O ILE A 237 25.069 -13.968 11.532 1.00 25.55 O
ANISOU 2434 O ILE A 237 3213 3583 2910 277 329 -104 O
ATOM 2435 CB ILE A 237 25.735 -16.843 10.046 1.00 34.26 C
ANISOU 2435 CB ILE A 237 4463 4528 4025 348 341 -241 C
ATOM 2436 CG1 ILE A 237 26.958 -17.602 9.533 1.00 37.51 C
ANISOU 2436 CG1 ILE A 237 4899 4915 4439 436 379 -305 C
ATOM 2437 CG2 ILE A 237 25.265 -15.831 9.016 1.00 29.51 C
ANISOU 2437 CG2 ILE A 237 3851 4002 3359 298 346 -254 C
ATOM 2438 CD1 ILE A 237 26.715 -18.355 8.248 1.00 45.43 C
ANISOU 2438 CD1 ILE A 237 5985 5875 5402 435 379 -388 C
ATOM 2439 N ILE A 238 23.940 -15.667 12.479 1.00 23.44 N
ANISOU 2439 N ILE A 238 3008 3195 2702 247 283 -78 N
ATOM 2440 CA ILE A 238 22.855 -14.799 12.928 1.00 27.90 C
ANISOU 2440 CA ILE A 238 3535 3808 3258 190 264 -28 C
ATOM 2441 C ILE A 238 23.367 -13.784 13.942 1.00 31.73 C
ANISOU 2441 C ILE A 238 3963 4350 3744 221 277 16 C
ATOM 2442 O ILE A 238 22.980 -12.608 13.917 1.00 24.39 O
ANISOU 2442 O ILE A 238 2996 3481 2789 200 274 34 O
ATOM 2443 CB ILE A 238 21.707 -15.651 13.494 1.00 30.06 C
ANISOU 2443 CB ILE A 238 3832 4024 3564 136 235 6 C
ATOM 2444 CG1 ILE A 238 21.073 -16.464 12.365 1.00 37.26 C
ANISOU 2444 CG1 ILE A 238 4799 4885 4474 87 209 -45 C
ATOM 2445 CG2 ILE A 238 20.676 -14.778 14.198 1.00 29.71 C
ANISOU 2445 CG2 ILE A 238 3734 4040 3516 94 226 63 C
ATOM 2446 CD1 ILE A 238 20.390 -17.716 12.831 1.00 41.08 C
ANISOU 2446 CD1 ILE A 238 5325 5279 5005 42 182 -24 C
ATOM 2447 N VAL A 239 24.250 -14.216 14.843 1.00 28.48 N
ANISOU 2447 N VAL A 239 3548 3916 3359 275 284 33 N
ATOM 2448 CA VAL A 239 24.842 -13.289 15.801 1.00 25.53 C
ANISOU 2448 CA VAL A 239 3124 3594 2982 305 287 66 C
ATOM 2449 C VAL A 239 25.732 -12.281 15.084 1.00 24.44 C
ANISOU 2449 C VAL A 239 2949 3515 2823 321 307 36 C
ATOM 2450 O VAL A 239 25.741 -11.090 15.420 1.00 27.33 O
ANISOU 2450 O VAL A 239 3277 3932 3173 310 302 57 O
ATOM 2451 CB VAL A 239 25.612 -14.066 16.885 1.00 31.60 C
ANISOU 2451 CB VAL A 239 3900 4325 3781 361 280 91 C
ATOM 2452 CG1 VAL A 239 26.265 -13.111 17.870 1.00 32.39 C
ANISOU 2452 CG1 VAL A 239 3952 4482 3874 391 272 118 C
ATOM 2453 CG2 VAL A 239 24.679 -15.028 17.608 1.00 23.04 C
ANISOU 2453 CG2 VAL A 239 2860 3181 2715 334 264 133 C
ATOM 2454 N GLY A 240 26.479 -12.735 14.077 1.00 29.04 N
ANISOU 2454 N GLY A 240 3543 4089 3403 346 331 -12 N
ATOM 2455 CA GLY A 240 27.349 -11.828 13.346 1.00 28.55 C
ANISOU 2455 CA GLY A 240 3442 4088 3319 353 360 -33 C
ATOM 2456 C GLY A 240 26.582 -10.790 12.551 1.00 30.96 C
ANISOU 2456 C GLY A 240 3750 4433 3581 296 358 -29 C
ATOM 2457 O GLY A 240 26.985 -9.625 12.483 1.00 30.20 O
ANISOU 2457 O GLY A 240 3617 4386 3470 284 366 -14 O
ATOM 2458 N LEU A 241 25.467 -11.192 11.939 1.00 26.85 N
ANISOU 2458 N LEU A 241 3275 3887 3041 258 342 -41 N
ATOM 2459 CA LEU A 241 24.655 -10.230 11.203 1.00 27.91 C
ANISOU 2459 CA LEU A 241 3412 4058 3134 210 330 -34 C
ATOM 2460 C LEU A 241 23.945 -9.265 12.142 1.00 28.40 C
ANISOU 2460 C LEU A 241 3444 4140 3205 192 302 16 C
ATOM 2461 O LEU A 241 23.697 -8.112 11.771 1.00 25.55 O
ANISOU 2461 O LEU A 241 3072 3816 2818 171 295 30 O
ATOM 2462 CB LEU A 241 23.649 -10.960 10.316 1.00 29.46 C
ANISOU 2462 CB LEU A 241 3659 4225 3308 174 308 -62 C
ATOM 2463 CG LEU A 241 24.280 -11.729 9.154 1.00 39.00 C
ANISOU 2463 CG LEU A 241 4912 5419 4486 194 335 -124 C
ATOM 2464 CD1 LEU A 241 23.223 -12.506 8.395 1.00 40.21 C
ANISOU 2464 CD1 LEU A 241 5123 5535 4621 154 299 -157 C
ATOM 2465 CD2 LEU A 241 25.026 -10.782 8.223 1.00 39.93 C
ANISOU 2465 CD2 LEU A 241 5018 5601 4552 199 372 -132 C
ATOM 2466 N PHE A 242 23.614 -9.711 13.356 1.00 27.21 N
ANISOU 2466 N PHE A 242 3284 3965 3088 203 288 42 N
ATOM 2467 CA PHE A 242 23.068 -8.797 14.353 1.00 21.60 C
ANISOU 2467 CA PHE A 242 2545 3280 2380 200 271 82 C
ATOM 2468 C PHE A 242 24.066 -7.690 14.673 1.00 25.96 C
ANISOU 2468 C PHE A 242 3070 3864 2929 221 276 88 C
ATOM 2469 O PHE A 242 23.711 -6.506 14.707 1.00 25.57 O
ANISOU 2469 O PHE A 242 3011 3840 2864 209 262 102 O
ATOM 2470 CB PHE A 242 22.685 -9.567 15.620 1.00 26.00 C
ANISOU 2470 CB PHE A 242 3104 3812 2964 212 264 112 C
ATOM 2471 CG PHE A 242 22.059 -8.711 16.689 1.00 26.35 C
ANISOU 2471 CG PHE A 242 3123 3888 3000 216 253 148 C
ATOM 2472 CD1 PHE A 242 22.849 -7.991 17.574 1.00 29.95 C
ANISOU 2472 CD1 PHE A 242 3564 4363 3452 252 250 156 C
ATOM 2473 CD2 PHE A 242 20.682 -8.631 16.813 1.00 25.55 C
ANISOU 2473 CD2 PHE A 242 3012 3801 2895 188 245 169 C
ATOM 2474 CE1 PHE A 242 22.278 -7.201 18.553 1.00 26.20 C
ANISOU 2474 CE1 PHE A 242 3077 3915 2962 264 240 179 C
ATOM 2475 CE2 PHE A 242 20.106 -7.845 17.796 1.00 28.61 C
ANISOU 2475 CE2 PHE A 242 3376 4223 3270 204 243 196 C
ATOM 2476 CZ PHE A 242 20.906 -7.131 18.666 1.00 26.40 C
ANISOU 2476 CZ PHE A 242 3094 3956 2979 245 242 198 C
ATOM 2477 N ALA A 243 25.327 -8.062 14.912 1.00 22.48 N
ANISOU 2477 N ALA A 243 2614 3419 2506 254 292 76 N
ATOM 2478 CA ALA A 243 26.352 -7.063 15.196 1.00 26.19 C
ANISOU 2478 CA ALA A 243 3050 3920 2981 263 292 80 C
ATOM 2479 C ALA A 243 26.592 -6.165 13.991 1.00 23.80 C
ANISOU 2479 C ALA A 243 2745 3645 2653 230 308 72 C
ATOM 2480 O ALA A 243 26.761 -4.950 14.138 1.00 27.82 O
ANISOU 2480 O ALA A 243 3241 4172 3158 213 295 88 O
ATOM 2481 CB ALA A 243 27.650 -7.748 15.622 1.00 23.50 C
ANISOU 2481 CB ALA A 243 2682 3578 2671 306 303 70 C
ATOM 2482 N LEU A 244 26.603 -6.743 12.790 1.00 26.32 N
ANISOU 2482 N LEU A 244 3085 3965 2952 222 336 47 N
ATOM 2483 CA LEU A 244 26.816 -5.940 11.591 1.00 26.04 C
ANISOU 2483 CA LEU A 244 3055 3959 2879 190 356 45 C
ATOM 2484 C LEU A 244 25.718 -4.897 11.418 1.00 28.04 C
ANISOU 2484 C LEU A 244 3332 4214 3108 157 322 71 C
ATOM 2485 O LEU A 244 25.977 -3.790 10.932 1.00 31.05 O
ANISOU 2485 O LEU A 244 3713 4613 3469 131 324 91 O
ATOM 2486 CB LEU A 244 26.897 -6.850 10.366 1.00 32.34 C
ANISOU 2486 CB LEU A 244 3884 4759 3646 193 389 7 C
ATOM 2487 CG LEU A 244 27.203 -6.167 9.033 1.00 37.25 C
ANISOU 2487 CG LEU A 244 4519 5420 4213 164 420 6 C
ATOM 2488 CD1 LEU A 244 28.618 -5.603 9.024 1.00 43.90 C
ANISOU 2488 CD1 LEU A 244 5308 6303 5068 165 462 16 C
ATOM 2489 CD2 LEU A 244 26.994 -7.130 7.876 1.00 46.57 C
ANISOU 2489 CD2 LEU A 244 5749 6599 5348 170 442 -39 C
ATOM 2490 N CYS A 245 24.486 -5.225 11.820 1.00 23.54 N
ANISOU 2490 N CYS A 245 2778 3624 2540 158 292 77 N
ATOM 2491 CA CYS A 245 23.368 -4.307 11.625 1.00 23.99 C
ANISOU 2491 CA CYS A 245 2849 3687 2578 139 258 99 C
ATOM 2492 C CYS A 245 23.267 -3.256 12.725 1.00 26.68 C
ANISOU 2492 C CYS A 245 3173 4026 2938 153 235 124 C
ATOM 2493 O CYS A 245 22.772 -2.151 12.467 1.00 25.00 O
ANISOU 2493 O CYS A 245 2973 3815 2710 145 211 142 O
ATOM 2494 CB CYS A 245 22.052 -5.086 11.538 1.00 31.95 C
ANISOU 2494 CB CYS A 245 3869 4687 3585 131 236 94 C
ATOM 2495 SG CYS A 245 21.872 -6.118 10.062 1.00 35.30 S
ANISOU 2495 SG CYS A 245 4333 5107 3974 106 242 56 S
ATOM 2496 N TRP A 246 23.723 -3.567 13.941 1.00 22.82 N
ANISOU 2496 N TRP A 246 2662 3529 2478 179 236 123 N
ATOM 2497 CA TRP A 246 23.551 -2.669 15.078 1.00 26.38 C
ANISOU 2497 CA TRP A 246 3107 3978 2940 199 211 137 C
ATOM 2498 C TRP A 246 24.810 -1.924 15.494 1.00 30.57 C
ANISOU 2498 C TRP A 246 3624 4507 3484 197 206 136 C
ATOM 2499 O TRP A 246 24.698 -0.850 16.089 1.00 29.39 O
ANISOU 2499 O TRP A 246 3484 4348 3335 203 177 142 O
ATOM 2500 CB TRP A 246 23.008 -3.437 16.291 1.00 24.68 C
ANISOU 2500 CB TRP A 246 2882 3762 2735 228 209 142 C
ATOM 2501 CG TRP A 246 21.533 -3.661 16.219 1.00 26.04 C
ANISOU 2501 CG TRP A 246 3055 3941 2898 225 203 153 C
ATOM 2502 CD1 TRP A 246 20.894 -4.812 15.861 1.00 25.71 C
ANISOU 2502 CD1 TRP A 246 3012 3896 2862 207 213 154 C
ATOM 2503 CD2 TRP A 246 20.506 -2.701 16.501 1.00 23.67 C
ANISOU 2503 CD2 TRP A 246 2751 3655 2587 240 183 164 C
ATOM 2504 NE1 TRP A 246 19.530 -4.631 15.908 1.00 27.04 N
ANISOU 2504 NE1 TRP A 246 3166 4082 3026 202 200 168 N
ATOM 2505 CE2 TRP A 246 19.267 -3.343 16.297 1.00 27.05 C
ANISOU 2505 CE2 TRP A 246 3163 4099 3016 229 185 174 C
ATOM 2506 CE3 TRP A 246 20.513 -1.363 16.907 1.00 24.62 C
ANISOU 2506 CE3 TRP A 246 2882 3773 2699 264 162 164 C
ATOM 2507 CZ2 TRP A 246 18.049 -2.692 16.486 1.00 25.57 C
ANISOU 2507 CZ2 TRP A 246 2955 3936 2823 248 170 186 C
ATOM 2508 CZ3 TRP A 246 19.301 -0.719 17.093 1.00 22.93 C
ANISOU 2508 CZ3 TRP A 246 2662 3574 2476 291 147 172 C
ATOM 2509 CH2 TRP A 246 18.088 -1.384 16.884 1.00 22.57 C
ANISOU 2509 CH2 TRP A 246 2586 3555 2433 286 154 184 C
ATOM 2510 N LEU A 247 25.998 -2.459 15.215 1.00 24.43 N
ANISOU 2510 N LEU A 247 2822 3738 2721 192 230 125 N
ATOM 2511 CA LEU A 247 27.221 -1.761 15.608 1.00 27.41 C
ANISOU 2511 CA LEU A 247 3173 4123 3120 182 221 126 C
ATOM 2512 C LEU A 247 27.362 -0.368 14.999 1.00 27.25 C
ANISOU 2512 C LEU A 247 3166 4095 3092 139 210 142 C
ATOM 2513 O LEU A 247 27.817 0.538 15.719 1.00 28.23 O
ANISOU 2513 O LEU A 247 3286 4205 3234 130 176 144 O
ATOM 2514 CB LEU A 247 28.451 -2.614 15.270 1.00 30.64 C
ANISOU 2514 CB LEU A 247 3539 4553 3549 187 256 113 C
ATOM 2515 CG LEU A 247 28.799 -3.710 16.276 1.00 35.02 C
ANISOU 2515 CG LEU A 247 4075 5105 4126 235 249 103 C
ATOM 2516 CD1 LEU A 247 30.043 -4.462 15.837 1.00 37.27 C
ANISOU 2516 CD1 LEU A 247 4314 5412 4435 252 282 88 C
ATOM 2517 CD2 LEU A 247 28.981 -3.124 17.669 1.00 27.88 C
ANISOU 2517 CD2 LEU A 247 3164 4197 3232 250 201 110 C
ATOM 2518 N PRO A 248 27.024 -0.122 13.724 1.00 26.05 N
ANISOU 2518 N PRO A 248 3037 3946 2912 110 230 154 N
ATOM 2519 CA PRO A 248 27.170 1.249 13.201 1.00 29.23 C
ANISOU 2519 CA PRO A 248 3464 4334 3309 67 215 179 C
ATOM 2520 C PRO A 248 26.412 2.291 14.001 1.00 26.77 C
ANISOU 2520 C PRO A 248 3187 3982 3002 82 161 185 C
ATOM 2521 O PRO A 248 26.954 3.367 14.281 1.00 24.35 O
ANISOU 2521 O PRO A 248 2890 3648 2714 55 134 194 O
ATOM 2522 CB PRO A 248 26.635 1.129 11.768 1.00 29.09 C
ANISOU 2522 CB PRO A 248 3478 4329 3247 48 240 193 C
ATOM 2523 CG PRO A 248 26.901 -0.278 11.399 1.00 28.21 C
ANISOU 2523 CG PRO A 248 3343 4249 3128 65 282 166 C
ATOM 2524 CD PRO A 248 26.672 -1.071 12.651 1.00 28.40 C
ANISOU 2524 CD PRO A 248 3347 4262 3183 110 265 144 C
ATOM 2525 N LEU A 249 25.168 1.997 14.384 1.00 20.59 N
ANISOU 2525 N LEU A 249 2423 3196 2207 125 146 177 N
ATOM 2526 CA LEU A 249 24.403 2.938 15.195 1.00 22.35 C
ANISOU 2526 CA LEU A 249 2674 3386 2430 157 102 175 C
ATOM 2527 C LEU A 249 25.043 3.129 16.566 1.00 26.93 C
ANISOU 2527 C LEU A 249 3244 3957 3031 174 80 154 C
ATOM 2528 O LEU A 249 25.117 4.254 17.072 1.00 27.47 O
ANISOU 2528 O LEU A 249 3343 3988 3107 176 41 148 O
ATOM 2529 CB LEU A 249 22.959 2.452 15.327 1.00 25.19 C
ANISOU 2529 CB LEU A 249 3036 3762 2772 200 101 172 C
ATOM 2530 CG LEU A 249 21.907 3.429 15.850 1.00 27.38 C
ANISOU 2530 CG LEU A 249 3340 4018 3044 244 65 172 C
ATOM 2531 CD1 LEU A 249 21.997 4.760 15.120 1.00 23.71 C
ANISOU 2531 CD1 LEU A 249 2922 3509 2579 225 34 191 C
ATOM 2532 CD2 LEU A 249 20.517 2.828 15.691 1.00 18.46 C
ANISOU 2532 CD2 LEU A 249 2191 2920 1902 275 72 176 C
ATOM 2533 N HIS A 250 25.522 2.041 17.178 1.00 22.48 N
ANISOU 2533 N HIS A 250 2643 3422 2475 190 99 141 N
ATOM 2534 CA HIS A 250 26.196 2.156 18.468 1.00 26.03 C
ANISOU 2534 CA HIS A 250 3083 3869 2937 207 71 122 C
ATOM 2535 C HIS A 250 27.489 2.953 18.349 1.00 27.52 C
ANISOU 2535 C HIS A 250 3259 4043 3154 158 48 122 C
ATOM 2536 O HIS A 250 27.817 3.754 19.231 1.00 22.84 O
ANISOU 2536 O HIS A 250 2684 3425 2569 159 1 105 O
ATOM 2537 CB HIS A 250 26.491 0.770 19.040 1.00 25.31 C
ANISOU 2537 CB HIS A 250 2959 3810 2849 235 93 118 C
ATOM 2538 CG HIS A 250 25.283 0.053 19.556 1.00 24.24 C
ANISOU 2538 CG HIS A 250 2836 3685 2688 277 107 121 C
ATOM 2539 ND1 HIS A 250 24.581 0.478 20.663 1.00 25.43 N
ANISOU 2539 ND1 HIS A 250 3011 3836 2815 318 86 114 N
ATOM 2540 CD2 HIS A 250 24.665 -1.074 19.129 1.00 27.76 C
ANISOU 2540 CD2 HIS A 250 3273 4145 3131 281 140 132 C
ATOM 2541 CE1 HIS A 250 23.577 -0.352 20.891 1.00 24.55 C
ANISOU 2541 CE1 HIS A 250 2896 3744 2688 342 113 127 C
ATOM 2542 NE2 HIS A 250 23.604 -1.300 19.972 1.00 27.27 N
ANISOU 2542 NE2 HIS A 250 3220 4092 3048 315 142 139 N
ATOM 2543 N ILE A 251 28.239 2.739 17.266 1.00 22.93 N
ANISOU 2543 N ILE A 251 2646 3479 2588 111 82 139 N
ATOM 2544 CA ILE A 251 29.527 3.409 17.106 1.00 23.20 C
ANISOU 2544 CA ILE A 251 2650 3511 2655 54 70 146 C
ATOM 2545 C ILE A 251 29.331 4.902 16.872 1.00 20.47 C
ANISOU 2545 C ILE A 251 2356 3110 2313 12 34 160 C
ATOM 2546 O ILE A 251 30.114 5.728 17.357 1.00 23.68 O
ANISOU 2546 O ILE A 251 2759 3490 2749 -27 -9 155 O
ATOM 2547 CB ILE A 251 30.327 2.745 15.970 1.00 27.75 C
ANISOU 2547 CB ILE A 251 3174 4131 3239 21 131 162 C
ATOM 2548 CG1 ILE A 251 30.778 1.344 16.387 1.00 28.20 C
ANISOU 2548 CG1 ILE A 251 3180 4229 3306 68 154 142 C
ATOM 2549 CG2 ILE A 251 31.529 3.590 15.584 1.00 24.12 C
ANISOU 2549 CG2 ILE A 251 2677 3675 2812 -53 129 181 C
ATOM 2550 CD1 ILE A 251 31.348 0.525 15.250 1.00 30.35 C
ANISOU 2550 CD1 ILE A 251 3411 4543 3576 59 220 146 C
ATOM 2551 N ILE A 252 28.282 5.277 16.136 1.00 19.97 N
ANISOU 2551 N ILE A 252 2344 3023 2221 20 41 178 N
ATOM 2552 CA ILE A 252 27.997 6.694 15.929 1.00 22.31 C
ANISOU 2552 CA ILE A 252 2702 3254 2520 -7 0 194 C
ATOM 2553 C ILE A 252 27.662 7.369 17.253 1.00 24.88 C
ANISOU 2553 C ILE A 252 3067 3534 2853 35 -61 158 C
ATOM 2554 O ILE A 252 28.115 8.486 17.529 1.00 24.83 O
ANISOU 2554 O ILE A 252 3096 3469 2870 -2 -109 154 O
ATOM 2555 CB ILE A 252 26.865 6.869 14.900 1.00 21.70 C
ANISOU 2555 CB ILE A 252 2670 3166 2410 9 14 221 C
ATOM 2556 CG1 ILE A 252 27.325 6.409 13.516 1.00 20.43 C
ANISOU 2556 CG1 ILE A 252 2486 3046 2231 -41 69 256 C
ATOM 2557 CG2 ILE A 252 26.417 8.316 14.850 1.00 20.79 C
ANISOU 2557 CG2 ILE A 252 2628 2972 2298 4 -38 236 C
ATOM 2558 CD1 ILE A 252 26.221 6.393 12.486 1.00 27.87 C
ANISOU 2558 CD1 ILE A 252 3470 3990 3131 -22 77 279 C
ATOM 2559 N ASN A 253 26.868 6.701 18.095 1.00 20.08 N
ANISOU 2559 N ASN A 253 2457 2950 2220 109 -59 129 N
ATOM 2560 CA ASN A 253 26.552 7.259 19.407 1.00 21.53 C
ANISOU 2560 CA ASN A 253 2681 3104 2396 158 -108 89 C
ATOM 2561 C ASN A 253 27.810 7.437 20.247 1.00 24.07 C
ANISOU 2561 C ASN A 253 2983 3421 2742 124 -148 66 C
ATOM 2562 O ASN A 253 27.905 8.380 21.040 1.00 27.08 O
ANISOU 2562 O ASN A 253 3413 3750 3124 130 -207 34 O
ATOM 2563 CB ASN A 253 25.545 6.368 20.136 1.00 27.43 C
ANISOU 2563 CB ASN A 253 3418 3896 3107 237 -84 72 C
ATOM 2564 CG ASN A 253 24.160 6.426 19.521 1.00 24.52 C
ANISOU 2564 CG ASN A 253 3069 3529 2719 277 -63 87 C
ATOM 2565 OD1 ASN A 253 23.811 7.388 18.837 1.00 24.22 O
ANISOU 2565 OD1 ASN A 253 3071 3444 2687 268 -83 101 O
ATOM 2566 ND2 ASN A 253 23.360 5.395 19.768 1.00 23.88 N
ANISOU 2566 ND2 ASN A 253 2958 3500 2617 319 -26 89 N
ATOM 2567 N CYS A 254 28.788 6.539 20.087 1.00 20.57 N
ANISOU 2567 N CYS A 254 2469 3030 2319 92 -121 77 N
ATOM 2568 CA CYS A 254 30.053 6.690 20.801 1.00 21.43 C
ANISOU 2568 CA CYS A 254 2543 3144 2457 55 -165 59 C
ATOM 2569 C CYS A 254 30.797 7.939 20.347 1.00 21.83 C
ANISOU 2569 C CYS A 254 2606 3138 2548 -32 -203 70 C
ATOM 2570 O CYS A 254 31.362 8.667 21.171 1.00 23.84 O
ANISOU 2570 O CYS A 254 2880 3358 2822 -56 -272 41 O
ATOM 2571 CB CYS A 254 30.927 5.451 20.604 1.00 24.21 C
ANISOU 2571 CB CYS A 254 2807 3566 2827 48 -126 72 C
ATOM 2572 SG CYS A 254 30.361 3.975 21.480 1.00 28.19 S
ANISOU 2572 SG CYS A 254 3300 4120 3293 139 -103 59 S
ATOM 2573 N PHE A 255 30.815 8.201 19.038 1.00 21.88 N
ANISOU 2573 N PHE A 255 2609 3137 2567 -84 -162 115 N
ATOM 2574 CA PHE A 255 31.432 9.429 18.546 1.00 24.14 C
ANISOU 2574 CA PHE A 255 2919 3364 2892 -174 -193 140 C
ATOM 2575 C PHE A 255 30.690 10.656 19.053 1.00 25.41 C
ANISOU 2575 C PHE A 255 3183 3426 3044 -154 -260 116 C
ATOM 2576 O PHE A 255 31.313 11.642 19.465 1.00 27.49 O
ANISOU 2576 O PHE A 255 3476 3626 3342 -212 -325 103 O
ATOM 2577 CB PHE A 255 31.474 9.430 17.019 1.00 27.96 C
ANISOU 2577 CB PHE A 255 3389 3861 3373 -227 -129 199 C
ATOM 2578 CG PHE A 255 32.645 8.692 16.447 1.00 30.26 C
ANISOU 2578 CG PHE A 255 3577 4231 3687 -279 -73 222 C
ATOM 2579 CD1 PHE A 255 33.869 9.322 16.298 1.00 26.83 C
ANISOU 2579 CD1 PHE A 255 3096 3795 3305 -378 -87 246 C
ATOM 2580 CD2 PHE A 255 32.523 7.369 16.055 1.00 27.16 C
ANISOU 2580 CD2 PHE A 255 3134 3915 3269 -229 -7 220 C
ATOM 2581 CE1 PHE A 255 34.951 8.646 15.771 1.00 26.67 C
ANISOU 2581 CE1 PHE A 255 2968 3858 3307 -418 -29 266 C
ATOM 2582 CE2 PHE A 255 33.601 6.686 15.526 1.00 29.87 C
ANISOU 2582 CE2 PHE A 255 3384 4331 3633 -262 48 235 C
ATOM 2583 CZ PHE A 255 34.816 7.325 15.382 1.00 30.93 C
ANISOU 2583 CZ PHE A 255 3461 4474 3816 -353 41 258 C
ATOM 2584 N THR A 256 29.356 10.618 19.025 1.00 22.86 N
ANISOU 2584 N THR A 256 2917 3089 2680 -72 -248 108 N
ATOM 2585 CA THR A 256 28.574 11.752 19.504 1.00 26.73 C
ANISOU 2585 CA THR A 256 3506 3489 3160 -32 -306 81 C
ATOM 2586 C THR A 256 28.847 12.025 20.978 1.00 25.42 C
ANISOU 2586 C THR A 256 3365 3302 2991 -1 -370 14 C
ATOM 2587 O THR A 256 28.895 13.183 21.405 1.00 27.09 O
ANISOU 2587 O THR A 256 3654 3423 3217 -13 -439 -15 O
ATOM 2588 CB THR A 256 27.083 11.496 19.276 1.00 26.60 C
ANISOU 2588 CB THR A 256 3520 3484 3101 63 -275 81 C
ATOM 2589 OG1 THR A 256 26.839 11.300 17.878 1.00 28.89 O
ANISOU 2589 OG1 THR A 256 3797 3793 3389 31 -228 141 O
ATOM 2590 CG2 THR A 256 26.254 12.672 19.770 1.00 27.66 C
ANISOU 2590 CG2 THR A 256 3753 3530 3228 122 -331 49 C
ATOM 2591 N PHE A 257 29.050 10.969 21.764 1.00 29.06 N
ANISOU 2591 N PHE A 257 3770 3842 3429 39 -354 -11 N
ATOM 2592 CA PHE A 257 29.226 11.085 23.206 1.00 27.29 C
ANISOU 2592 CA PHE A 257 3573 3613 3183 80 -412 -73 C
ATOM 2593 C PHE A 257 30.674 11.356 23.598 1.00 26.80 C
ANISOU 2593 C PHE A 257 3475 3543 3164 -5 -472 -86 C
ATOM 2594 O PHE A 257 30.945 12.268 24.386 1.00 31.81 O
ANISOU 2594 O PHE A 257 4172 4114 3802 -18 -554 -134 O
ATOM 2595 CB PHE A 257 28.722 9.809 23.888 1.00 26.49 C
ANISOU 2595 CB PHE A 257 3434 3600 3031 163 -368 -85 C
ATOM 2596 CG PHE A 257 28.863 9.822 25.381 1.00 26.57 C
ANISOU 2596 CG PHE A 257 3477 3620 3000 213 -421 -142 C
ATOM 2597 CD1 PHE A 257 28.021 10.597 26.160 1.00 23.84 C
ANISOU 2597 CD1 PHE A 257 3222 3229 2610 284 -453 -194 C
ATOM 2598 CD2 PHE A 257 29.828 9.050 26.008 1.00 28.64 C
ANISOU 2598 CD2 PHE A 257 3680 3938 3263 197 -440 -147 C
ATOM 2599 CE1 PHE A 257 28.145 10.612 27.534 1.00 28.66 C
ANISOU 2599 CE1 PHE A 257 3870 3852 3167 333 -500 -250 C
ATOM 2600 CE2 PHE A 257 29.956 9.059 27.384 1.00 25.85 C
ANISOU 2600 CE2 PHE A 257 3364 3598 2860 244 -495 -198 C
ATOM 2601 CZ PHE A 257 29.114 9.841 28.147 1.00 26.43 C
ANISOU 2601 CZ PHE A 257 3535 3629 2880 310 -523 -250 C
ATOM 2602 N PHE A 258 31.613 10.579 23.055 1.00 29.39 N
ANISOU 2602 N PHE A 258 3702 3937 3526 -63 -437 -47 N
ATOM 2603 CA PHE A 258 33.004 10.652 23.483 1.00 28.86 C
ANISOU 2603 CA PHE A 258 3576 3887 3504 -137 -491 -58 C
ATOM 2604 C PHE A 258 33.810 11.738 22.782 1.00 36.38 C
ANISOU 2604 C PHE A 258 4524 4777 4522 -259 -523 -30 C
ATOM 2605 O PHE A 258 34.808 12.202 23.343 1.00 31.25 O
ANISOU 2605 O PHE A 258 3851 4111 3912 -326 -597 -53 O
ATOM 2606 CB PHE A 258 33.698 9.302 23.279 1.00 28.47 C
ANISOU 2606 CB PHE A 258 3410 3942 3466 -133 -438 -31 C
ATOM 2607 CG PHE A 258 33.319 8.263 24.295 1.00 31.63 C
ANISOU 2607 CG PHE A 258 3807 4398 3812 -34 -436 -58 C
ATOM 2608 CD1 PHE A 258 33.507 8.497 25.650 1.00 29.33 C
ANISOU 2608 CD1 PHE A 258 3553 4099 3493 -3 -517 -111 C
ATOM 2609 CD2 PHE A 258 32.793 7.043 23.897 1.00 24.62 C
ANISOU 2609 CD2 PHE A 258 2886 3569 2901 23 -356 -31 C
ATOM 2610 CE1 PHE A 258 33.164 7.538 26.588 1.00 33.55 C
ANISOU 2610 CE1 PHE A 258 4091 4687 3970 85 -512 -126 C
ATOM 2611 CE2 PHE A 258 32.451 6.081 24.833 1.00 28.76 C
ANISOU 2611 CE2 PHE A 258 3412 4137 3377 105 -353 -47 C
ATOM 2612 CZ PHE A 258 32.637 6.330 26.179 1.00 28.99 C
ANISOU 2612 CZ PHE A 258 3478 4162 3373 137 -429 -90 C
ATOM 2613 N CYS A 259 33.424 12.163 21.581 1.00 32.46 N
ANISOU 2613 N CYS A 259 4051 4244 4038 -295 -474 21 N
ATOM 2614 CA CYS A 259 34.120 13.244 20.888 1.00 36.09 C
ANISOU 2614 CA CYS A 259 4520 4636 4556 -417 -500 59 C
ATOM 2615 C CYS A 259 33.163 14.409 20.668 1.00 40.53 C
ANISOU 2615 C CYS A 259 5215 5079 5106 -403 -532 58 C
ATOM 2616 O CYS A 259 32.565 14.549 19.591 1.00 41.15 O
ANISOU 2616 O CYS A 259 5322 5140 5173 -403 -479 111 O
ATOM 2617 CB CYS A 259 34.725 12.767 19.572 1.00 33.80 C
ANISOU 2617 CB CYS A 259 4139 4413 4292 -487 -413 133 C
ATOM 2618 SG CYS A 259 35.716 14.022 18.737 1.00 51.22 S
ANISOU 2618 SG CYS A 259 6340 6552 6570 -654 -434 194 S
ATOM 2619 N PRO A 260 33.006 15.281 21.665 1.00 44.56 N
ANISOU 2619 N PRO A 260 5814 5500 5616 -385 -624 -4 N
ATOM 2620 CA PRO A 260 32.198 16.491 21.452 1.00 50.03 C
ANISOU 2620 CA PRO A 260 6638 6063 6308 -371 -664 -7 C
ATOM 2621 C PRO A 260 32.831 17.473 20.479 1.00 53.74 C
ANISOU 2621 C PRO A 260 7129 6450 6839 -505 -680 59 C
ATOM 2622 O PRO A 260 32.114 18.318 19.930 1.00 53.53 O
ANISOU 2622 O PRO A 260 7203 6325 6812 -493 -690 84 O
ATOM 2623 CB PRO A 260 32.082 17.085 22.860 1.00 52.66 C
ANISOU 2623 CB PRO A 260 7054 6331 6625 -322 -761 -101 C
ATOM 2624 CG PRO A 260 33.290 16.574 23.575 1.00 38.41 C
ANISOU 2624 CG PRO A 260 5158 4594 4841 -380 -797 -126 C
ATOM 2625 CD PRO A 260 33.560 15.209 23.029 1.00 34.68 C
ANISOU 2625 CD PRO A 260 4555 4261 4361 -372 -702 -76 C
ATOM 2626 N ASP A 261 34.146 17.391 20.242 1.00 47.57 N
ANISOU 2626 N ASP A 261 6254 5707 6114 -631 -680 93 N
ATOM 2627 CA ASP A 261 34.790 18.278 19.278 1.00 54.85 C
ANISOU 2627 CA ASP A 261 7185 6561 7094 -772 -683 169 C
ATOM 2628 C ASP A 261 34.643 17.790 17.846 1.00 47.67 C
ANISOU 2628 C ASP A 261 6227 5718 6166 -792 -572 260 C
ATOM 2629 O ASP A 261 34.874 18.571 16.914 1.00 52.45 O
ANISOU 2629 O ASP A 261 6869 6261 6800 -889 -563 335 O
ATOM 2630 CB ASP A 261 36.277 18.447 19.606 1.00 64.38 C
ANISOU 2630 CB ASP A 261 8300 7788 8373 -909 -729 171 C
ATOM 2631 CG ASP A 261 36.514 19.347 20.802 1.00 76.61 C
ANISOU 2631 CG ASP A 261 9928 9230 9952 -932 -861 93 C
ATOM 2632 OD1 ASP A 261 35.532 19.917 21.322 1.00 76.21 O
ANISOU 2632 OD1 ASP A 261 10014 9080 9864 -840 -911 38 O
ATOM 2633 OD2 ASP A 261 37.682 19.483 21.224 1.00 91.74 O
ANISOU 2633 OD2 ASP A 261 11768 11162 11926 -1038 -917 82 O
ATOM 2634 N CYS A 262 34.283 16.522 17.655 1.00 50.25 N
ANISOU 2634 N CYS A 262 6480 6167 6443 -705 -492 256 N
ATOM 2635 CA CYS A 262 33.947 16.005 16.336 1.00 50.13 C
ANISOU 2635 CA CYS A 262 6439 6213 6394 -701 -392 327 C
ATOM 2636 C CYS A 262 32.590 16.536 15.892 1.00 46.18 C
ANISOU 2636 C CYS A 262 6062 5633 5850 -625 -400 341 C
ATOM 2637 O CYS A 262 31.664 16.656 16.697 1.00 48.54 O
ANISOU 2637 O CYS A 262 6429 5890 6125 -520 -445 280 O
ATOM 2638 CB CYS A 262 33.907 14.473 16.353 1.00 41.05 C
ANISOU 2638 CB CYS A 262 5187 5205 5207 -624 -317 307 C
ATOM 2639 SG CYS A 262 35.454 13.619 16.768 1.00 48.65 S
ANISOU 2639 SG CYS A 262 5987 6282 6216 -683 -298 294 S
ATOM 2640 N SER A 263 32.466 16.843 14.603 1.00 47.10 N
ANISOU 2640 N SER A 263 6205 5737 5952 -675 -353 424 N
ATOM 2641 CA SER A 263 31.164 17.222 14.072 1.00 44.33 C
ANISOU 2641 CA SER A 263 5959 5328 5558 -595 -358 444 C
ATOM 2642 C SER A 263 30.202 16.045 14.169 1.00 41.59 C
ANISOU 2642 C SER A 263 5574 5076 5152 -467 -311 405 C
ATOM 2643 O SER A 263 30.581 14.891 13.948 1.00 32.08 O
ANISOU 2643 O SER A 263 4270 3989 3929 -465 -243 403 O
ATOM 2644 CB SER A 263 31.284 17.686 12.620 1.00 44.55 C
ANISOU 2644 CB SER A 263 6019 5337 5571 -676 -316 548 C
ATOM 2645 OG SER A 263 32.155 18.797 12.507 1.00 52.11 O
ANISOU 2645 OG SER A 263 7013 6199 6586 -807 -357 596 O
ATOM 2646 N HIS A 264 28.952 16.340 14.518 1.00 34.08 N
ANISOU 2646 N HIS A 264 4701 4072 4175 -357 -350 372 N
ATOM 2647 CA HIS A 264 27.945 15.294 14.612 1.00 31.93 C
ANISOU 2647 CA HIS A 264 4393 3885 3852 -244 -310 340 C
ATOM 2648 C HIS A 264 27.772 14.604 13.264 1.00 35.46 C
ANISOU 2648 C HIS A 264 4804 4409 4258 -261 -236 402 C
ATOM 2649 O HIS A 264 27.816 15.245 12.211 1.00 29.46 O
ANISOU 2649 O HIS A 264 4094 3609 3490 -317 -233 472 O
ATOM 2650 CB HIS A 264 26.616 15.882 15.081 1.00 28.68 C
ANISOU 2650 CB HIS A 264 4068 3405 3425 -130 -361 304 C
ATOM 2651 CG HIS A 264 25.633 14.853 15.544 1.00 29.64 C
ANISOU 2651 CG HIS A 264 4142 3613 3506 -17 -328 259 C
ATOM 2652 ND1 HIS A 264 25.079 13.917 14.698 1.00 27.85 N
ANISOU 2652 ND1 HIS A 264 3867 3474 3243 5 -270 290 N
ATOM 2653 CD2 HIS A 264 25.109 14.611 16.768 1.00 24.96 C
ANISOU 2653 CD2 HIS A 264 3545 3035 2904 72 -345 188 C
ATOM 2654 CE1 HIS A 264 24.255 13.143 15.381 1.00 30.74 C
ANISOU 2654 CE1 HIS A 264 4195 3898 3586 97 -254 243 C
ATOM 2655 NE2 HIS A 264 24.254 13.543 16.639 1.00 28.14 N
ANISOU 2655 NE2 HIS A 264 3891 3530 3269 140 -294 184 N
ATOM 2656 N ALA A 265 27.591 13.287 13.304 1.00 33.72 N
ANISOU 2656 N ALA A 265 4505 4297 4009 -216 -181 376 N
ATOM 2657 CA ALA A 265 27.379 12.526 12.083 1.00 30.54 C
ANISOU 2657 CA ALA A 265 4073 3970 3561 -223 -116 419 C
ATOM 2658 C ALA A 265 26.187 13.099 11.319 1.00 29.07 C
ANISOU 2658 C ALA A 265 3968 3738 3339 -177 -142 455 C
ATOM 2659 O ALA A 265 25.170 13.450 11.932 1.00 32.35 O
ANISOU 2659 O ALA A 265 4425 4111 3757 -91 -190 422 O
ATOM 2660 CB ALA A 265 27.148 11.047 12.406 1.00 27.99 C
ANISOU 2660 CB ALA A 265 3671 3747 3217 -165 -69 373 C
ATOM 2661 N PRO A 266 26.277 13.221 9.997 1.00 29.90 N
ANISOU 2661 N PRO A 266 4097 3857 3408 -228 -112 523 N
ATOM 2662 CA PRO A 266 25.234 13.928 9.245 1.00 30.31 C
ANISOU 2662 CA PRO A 266 4235 3856 3426 -189 -152 567 C
ATOM 2663 C PRO A 266 23.893 13.213 9.308 1.00 29.39 C
ANISOU 2663 C PRO A 266 4101 3788 3277 -81 -160 531 C
ATOM 2664 O PRO A 266 23.790 12.037 9.661 1.00 32.26 O
ANISOU 2664 O PRO A 266 4389 4235 3633 -51 -121 484 O
ATOM 2665 CB PRO A 266 25.783 13.958 7.813 1.00 25.64 C
ANISOU 2665 CB PRO A 266 3660 3296 2789 -274 -104 647 C
ATOM 2666 CG PRO A 266 26.783 12.849 7.760 1.00 32.25 C
ANISOU 2666 CG PRO A 266 4398 4235 3622 -321 -24 626 C
ATOM 2667 CD PRO A 266 27.376 12.763 9.132 1.00 33.96 C
ANISOU 2667 CD PRO A 266 4561 4437 3904 -320 -41 564 C
ATOM 2668 N LEU A 267 22.851 13.969 8.956 1.00 33.41 N
ANISOU 2668 N LEU A 267 4681 4241 3772 -24 -215 557 N
ATOM 2669 CA LEU A 267 21.486 13.456 9.024 1.00 31.76 C
ANISOU 2669 CA LEU A 267 4450 4076 3542 79 -233 527 C
ATOM 2670 C LEU A 267 21.320 12.198 8.178 1.00 31.34 C
ANISOU 2670 C LEU A 267 4340 4131 3436 65 -182 532 C
ATOM 2671 O LEU A 267 20.692 11.225 8.611 1.00 25.73 O
ANISOU 2671 O LEU A 267 3566 3486 2724 116 -167 483 O
ATOM 2672 CB LEU A 267 20.509 14.544 8.574 1.00 35.97 C
ANISOU 2672 CB LEU A 267 5067 4532 4067 138 -304 567 C
ATOM 2673 CG LEU A 267 19.013 14.237 8.524 1.00 40.99 C
ANISOU 2673 CG LEU A 267 5679 5210 4686 247 -335 548 C
ATOM 2674 CD1 LEU A 267 18.404 14.283 9.907 1.00 39.82 C
ANISOU 2674 CD1 LEU A 267 5497 5052 4580 339 -351 476 C
ATOM 2675 CD2 LEU A 267 18.324 15.224 7.605 1.00 53.52 C
ANISOU 2675 CD2 LEU A 267 7350 6734 6250 281 -400 613 C
ATOM 2676 N TRP A 268 21.884 12.192 6.968 1.00 28.18 N
ANISOU 2676 N TRP A 268 3967 3750 2990 -8 -153 589 N
ATOM 2677 CA TRP A 268 21.689 11.050 6.080 1.00 33.03 C
ANISOU 2677 CA TRP A 268 4544 4460 3544 -16 -112 587 C
ATOM 2678 C TRP A 268 22.362 9.798 6.629 1.00 29.31 C
ANISOU 2678 C TRP A 268 3987 4060 3090 -34 -47 530 C
ATOM 2679 O TRP A 268 21.847 8.686 6.462 1.00 30.10 O
ANISOU 2679 O TRP A 268 4044 4226 3165 -5 -29 495 O
ATOM 2680 CB TRP A 268 22.209 11.373 4.679 1.00 34.33 C
ANISOU 2680 CB TRP A 268 4765 4633 3644 -86 -89 661 C
ATOM 2681 CG TRP A 268 23.699 11.527 4.606 1.00 36.16 C
ANISOU 2681 CG TRP A 268 4985 4865 3888 -182 -28 685 C
ATOM 2682 CD1 TRP A 268 24.410 12.686 4.717 1.00 34.77 C
ANISOU 2682 CD1 TRP A 268 4856 4609 3745 -242 -41 735 C
ATOM 2683 CD2 TRP A 268 24.662 10.482 4.410 1.00 33.36 C
ANISOU 2683 CD2 TRP A 268 4562 4596 3518 -227 56 659 C
ATOM 2684 NE1 TRP A 268 25.753 12.429 4.601 1.00 31.42 N
ANISOU 2684 NE1 TRP A 268 4385 4224 3329 -329 31 746 N
ATOM 2685 CE2 TRP A 268 25.935 11.084 4.414 1.00 34.02 C
ANISOU 2685 CE2 TRP A 268 4641 4657 3628 -314 93 698 C
ATOM 2686 CE3 TRP A 268 24.571 9.098 4.234 1.00 31.75 C
ANISOU 2686 CE3 TRP A 268 4301 4480 3284 -202 101 606 C
ATOM 2687 CZ2 TRP A 268 27.109 10.350 4.245 1.00 29.14 C
ANISOU 2687 CZ2 TRP A 268 3951 4113 3006 -368 177 686 C
ATOM 2688 CZ3 TRP A 268 25.736 8.371 4.068 1.00 35.97 C
ANISOU 2688 CZ3 TRP A 268 4778 5076 3813 -248 182 591 C
ATOM 2689 CH2 TRP A 268 26.988 8.998 4.075 1.00 37.40 C
ANISOU 2689 CH2 TRP A 268 4945 5245 4020 -326 222 630 C
ATOM 2690 N LEU A 269 23.511 9.959 7.293 1.00 22.77 N
ANISOU 2690 N LEU A 269 3134 3214 2306 -81 -18 519 N
ATOM 2691 CA LEU A 269 24.199 8.812 7.876 1.00 27.92 C
ANISOU 2691 CA LEU A 269 3704 3926 2977 -89 36 468 C
ATOM 2692 C LEU A 269 23.465 8.292 9.104 1.00 28.93 C
ANISOU 2692 C LEU A 269 3793 4058 3140 -14 12 408 C
ATOM 2693 O LEU A 269 23.460 7.082 9.363 1.00 25.81 O
ANISOU 2693 O LEU A 269 3343 3722 2743 4 46 369 O
ATOM 2694 CB LEU A 269 25.637 9.188 8.231 1.00 27.48 C
ANISOU 2694 CB LEU A 269 3625 3856 2962 -160 64 477 C
ATOM 2695 CG LEU A 269 26.492 8.067 8.820 1.00 27.21 C
ANISOU 2695 CG LEU A 269 3504 3884 2952 -164 115 430 C
ATOM 2696 CD1 LEU A 269 26.606 6.922 7.828 1.00 29.51 C
ANISOU 2696 CD1 LEU A 269 3768 4254 3190 -168 178 425 C
ATOM 2697 CD2 LEU A 269 27.864 8.591 9.203 1.00 27.98 C
ANISOU 2697 CD2 LEU A 269 3570 3966 3096 -235 128 443 C
ATOM 2698 N MET A 270 22.845 9.189 9.875 1.00 25.52 N
ANISOU 2698 N MET A 270 3395 3564 2738 32 -44 401 N
ATOM 2699 CA MET A 270 22.074 8.757 11.035 1.00 30.55 C
ANISOU 2699 CA MET A 270 3997 4214 3397 107 -59 348 C
ATOM 2700 C MET A 270 20.944 7.826 10.617 1.00 26.93 C
ANISOU 2700 C MET A 270 3507 3815 2909 150 -52 339 C
ATOM 2701 O MET A 270 20.801 6.722 11.154 1.00 26.85 O
ANISOU 2701 O MET A 270 3441 3855 2905 167 -24 304 O
ATOM 2702 CB MET A 270 21.525 9.972 11.784 1.00 24.73 C
ANISOU 2702 CB MET A 270 3310 3400 2686 160 -118 341 C
ATOM 2703 CG MET A 270 22.587 10.846 12.430 1.00 29.52 C
ANISOU 2703 CG MET A 270 3948 3940 3329 118 -137 336 C
ATOM 2704 SD MET A 270 23.581 9.933 13.622 1.00 26.97 S
ANISOU 2704 SD MET A 270 3553 3662 3031 100 -103 283 S
ATOM 2705 CE MET A 270 22.308 9.275 14.699 1.00 27.28 C
ANISOU 2705 CE MET A 270 3563 3742 3060 207 -105 232 C
ATOM 2706 N TYR A 271 20.135 8.252 9.644 1.00 25.15 N
ANISOU 2706 N TYR A 271 3320 3585 2653 164 -84 374 N
ATOM 2707 CA TYR A 271 18.996 7.444 9.228 1.00 28.30 C
ANISOU 2707 CA TYR A 271 3686 4040 3027 199 -92 365 C
ATOM 2708 C TYR A 271 19.409 6.257 8.374 1.00 27.25 C
ANISOU 2708 C TYR A 271 3530 3966 2857 148 -48 360 C
ATOM 2709 O TYR A 271 18.650 5.288 8.279 1.00 28.97 O
ANISOU 2709 O TYR A 271 3709 4231 3066 165 -48 338 O
ATOM 2710 CB TYR A 271 17.976 8.312 8.494 1.00 33.21 C
ANISOU 2710 CB TYR A 271 4352 4639 3628 238 -153 403 C
ATOM 2711 CG TYR A 271 17.174 9.177 9.440 1.00 38.08 C
ANISOU 2711 CG TYR A 271 4973 5214 4284 320 -197 390 C
ATOM 2712 CD1 TYR A 271 16.181 8.625 10.241 1.00 37.37 C
ANISOU 2712 CD1 TYR A 271 4815 5170 4215 383 -196 352 C
ATOM 2713 CD2 TYR A 271 17.411 10.540 9.541 1.00 39.95 C
ANISOU 2713 CD2 TYR A 271 5281 5363 4536 335 -235 414 C
ATOM 2714 CE1 TYR A 271 15.443 9.407 11.109 1.00 36.21 C
ANISOU 2714 CE1 TYR A 271 4669 4994 4097 469 -226 335 C
ATOM 2715 CE2 TYR A 271 16.675 11.329 10.408 1.00 44.76 C
ANISOU 2715 CE2 TYR A 271 5901 5929 5177 422 -274 392 C
ATOM 2716 CZ TYR A 271 15.695 10.758 11.188 1.00 44.16 C
ANISOU 2716 CZ TYR A 271 5753 5911 5115 493 -266 350 C
ATOM 2717 OH TYR A 271 14.968 11.547 12.049 1.00 41.51 O
ANISOU 2717 OH TYR A 271 5425 5542 4806 590 -295 324 O
ATOM 2718 N LEU A 272 20.590 6.302 7.755 1.00 20.92 N
ANISOU 2718 N LEU A 272 2752 3162 2034 86 -10 380 N
ATOM 2719 CA LEU A 272 21.123 5.096 7.130 1.00 26.11 C
ANISOU 2719 CA LEU A 272 3385 3876 2661 50 42 360 C
ATOM 2720 C LEU A 272 21.466 4.051 8.183 1.00 29.06 C
ANISOU 2720 C LEU A 272 3696 4269 3076 63 76 310 C
ATOM 2721 O LEU A 272 21.204 2.856 7.996 1.00 29.47 O
ANISOU 2721 O LEU A 272 3723 4359 3117 67 95 280 O
ATOM 2722 CB LEU A 272 22.356 5.429 6.289 1.00 30.12 C
ANISOU 2722 CB LEU A 272 3922 4387 3137 -14 86 393 C
ATOM 2723 CG LEU A 272 23.092 4.231 5.680 1.00 36.78 C
ANISOU 2723 CG LEU A 272 4739 5289 3947 -41 151 366 C
ATOM 2724 CD1 LEU A 272 22.187 3.486 4.715 1.00 38.69 C
ANISOU 2724 CD1 LEU A 272 5004 5568 4128 -28 136 352 C
ATOM 2725 CD2 LEU A 272 24.380 4.663 4.988 1.00 34.23 C
ANISOU 2725 CD2 LEU A 272 4429 4979 3598 -101 206 401 C
ATOM 2726 N ALA A 273 22.047 4.489 9.303 1.00 25.43 N
ANISOU 2726 N ALA A 273 3219 3779 2664 70 78 302 N
ATOM 2727 CA ALA A 273 22.346 3.570 10.396 1.00 28.23 C
ANISOU 2727 CA ALA A 273 3521 4150 3054 90 102 262 C
ATOM 2728 C ALA A 273 21.070 3.064 11.056 1.00 19.96 C
ANISOU 2728 C ALA A 273 2451 3116 2018 141 80 242 C
ATOM 2729 O ALA A 273 20.990 1.893 11.445 1.00 20.71 O
ANISOU 2729 O ALA A 273 2511 3238 2122 148 103 217 O
ATOM 2730 CB ALA A 273 23.250 4.252 11.423 1.00 20.91 C
ANISOU 2730 CB ALA A 273 2587 3191 2168 84 97 257 C
ATOM 2731 N ILE A 274 20.062 3.930 11.192 1.00 21.55 N
ANISOU 2731 N ILE A 274 2670 3298 2219 178 36 255 N
ATOM 2732 CA ILE A 274 18.787 3.504 11.763 1.00 25.87 C
ANISOU 2732 CA ILE A 274 3182 3870 2777 226 20 242 C
ATOM 2733 C ILE A 274 18.119 2.477 10.861 1.00 25.33 C
ANISOU 2733 C ILE A 274 3095 3843 2686 206 22 240 C
ATOM 2734 O ILE A 274 17.620 1.448 11.329 1.00 22.65 O
ANISOU 2734 O ILE A 274 2712 3531 2361 210 36 222 O
ATOM 2735 CB ILE A 274 17.873 4.721 12.005 1.00 30.64 C
ANISOU 2735 CB ILE A 274 3806 4450 3388 280 -27 255 C
ATOM 2736 CG1 ILE A 274 18.470 5.644 13.069 1.00 23.58 C
ANISOU 2736 CG1 ILE A 274 2936 3507 2517 304 -33 242 C
ATOM 2737 CG2 ILE A 274 16.477 4.271 12.419 1.00 34.97 C
ANISOU 2737 CG2 ILE A 274 4301 5041 3945 329 -37 246 C
ATOM 2738 CD1 ILE A 274 17.725 6.952 13.220 1.00 29.42 C
ANISOU 2738 CD1 ILE A 274 3713 4205 3262 363 -81 250 C
ATOM 2739 N VAL A 275 18.105 2.739 9.552 1.00 22.09 N
ANISOU 2739 N VAL A 275 2722 3435 2237 179 4 260 N
ATOM 2740 CA VAL A 275 17.498 1.809 8.605 1.00 24.62 C
ANISOU 2740 CA VAL A 275 3036 3792 2527 157 -5 252 C
ATOM 2741 C VAL A 275 18.242 0.479 8.606 1.00 27.97 C
ANISOU 2741 C VAL A 275 3447 4229 2952 123 44 219 C
ATOM 2742 O VAL A 275 17.625 -0.593 8.565 1.00 25.38 O
ANISOU 2742 O VAL A 275 3094 3920 2629 115 40 197 O
ATOM 2743 CB VAL A 275 17.452 2.448 7.203 1.00 29.16 C
ANISOU 2743 CB VAL A 275 3666 4367 3045 137 -35 282 C
ATOM 2744 CG1 VAL A 275 17.397 1.387 6.118 1.00 27.96 C
ANISOU 2744 CG1 VAL A 275 3527 4250 2846 100 -30 262 C
ATOM 2745 CG2 VAL A 275 16.256 3.386 7.095 1.00 25.14 C
ANISOU 2745 CG2 VAL A 275 3159 3854 2538 182 -101 310 C
ATOM 2746 N LEU A 276 19.576 0.524 8.676 1.00 23.23 N
ANISOU 2746 N LEU A 276 2860 3614 2351 105 87 216 N
ATOM 2747 CA LEU A 276 20.358 -0.709 8.694 1.00 25.20 C
ANISOU 2747 CA LEU A 276 3098 3873 2606 88 133 183 C
ATOM 2748 C LEU A 276 20.021 -1.567 9.908 1.00 27.51 C
ANISOU 2748 C LEU A 276 3347 4160 2945 110 139 164 C
ATOM 2749 O LEU A 276 19.908 -2.794 9.796 1.00 26.87 O
ANISOU 2749 O LEU A 276 3259 4082 2867 100 152 139 O
ATOM 2750 CB LEU A 276 21.851 -0.384 8.667 1.00 24.04 C
ANISOU 2750 CB LEU A 276 2955 3721 2460 72 177 186 C
ATOM 2751 CG LEU A 276 22.796 -1.579 8.807 1.00 28.70 C
ANISOU 2751 CG LEU A 276 3523 4319 3062 72 226 152 C
ATOM 2752 CD1 LEU A 276 22.608 -2.559 7.657 1.00 28.07 C
ANISOU 2752 CD1 LEU A 276 3472 4257 2937 59 240 124 C
ATOM 2753 CD2 LEU A 276 24.241 -1.112 8.889 1.00 25.66 C
ANISOU 2753 CD2 LEU A 276 3122 3939 2688 59 265 160 C
ATOM 2754 N SER A 277 19.855 -0.944 11.079 1.00 25.27 N
ANISOU 2754 N SER A 277 3041 3866 2693 140 130 176 N
ATOM 2755 CA SER A 277 19.507 -1.710 12.271 1.00 22.40 C
ANISOU 2755 CA SER A 277 2643 3504 2363 160 139 167 C
ATOM 2756 C SER A 277 18.144 -2.374 12.129 1.00 26.23 C
ANISOU 2756 C SER A 277 3106 4010 2852 155 120 168 C
ATOM 2757 O SER A 277 17.906 -3.437 12.712 1.00 23.51 O
ANISOU 2757 O SER A 277 2739 3664 2529 149 135 161 O
ATOM 2758 CB SER A 277 19.536 -0.811 13.509 1.00 23.25 C
ANISOU 2758 CB SER A 277 2740 3604 2490 198 132 176 C
ATOM 2759 OG SER A 277 18.409 0.048 13.552 1.00 23.93 O
ANISOU 2759 OG SER A 277 2822 3698 2572 226 100 190 O
ATOM 2760 N HIS A 278 17.242 -1.772 11.351 1.00 20.51 N
ANISOU 2760 N HIS A 278 2384 3300 2108 154 82 180 N
ATOM 2761 CA HIS A 278 15.923 -2.360 11.152 1.00 20.32 C
ANISOU 2761 CA HIS A 278 2325 3303 2092 142 55 181 C
ATOM 2762 C HIS A 278 15.957 -3.535 10.184 1.00 27.37 C
ANISOU 2762 C HIS A 278 3237 4193 2970 93 51 157 C
ATOM 2763 O HIS A 278 15.125 -4.443 10.295 1.00 25.23 O
ANISOU 2763 O HIS A 278 2936 3931 2720 68 38 152 O
ATOM 2764 CB HIS A 278 14.945 -1.296 10.652 1.00 21.73 C
ANISOU 2764 CB HIS A 278 2495 3504 2258 166 6 202 C
ATOM 2765 CG HIS A 278 14.661 -0.219 11.653 1.00 24.16 C
ANISOU 2765 CG HIS A 278 2784 3811 2584 225 5 217 C
ATOM 2766 ND1 HIS A 278 14.002 0.946 11.326 1.00 26.24 N
ANISOU 2766 ND1 HIS A 278 3051 4079 2840 265 -38 235 N
ATOM 2767 CD2 HIS A 278 14.942 -0.132 12.975 1.00 27.53 C
ANISOU 2767 CD2 HIS A 278 3194 4232 3033 255 38 213 C
ATOM 2768 CE1 HIS A 278 13.892 1.705 12.401 1.00 27.36 C
ANISOU 2768 CE1 HIS A 278 3182 4214 3001 321 -28 236 C
ATOM 2769 NE2 HIS A 278 14.454 1.074 13.415 1.00 26.29 N
ANISOU 2769 NE2 HIS A 278 3035 4076 2880 314 18 222 N
ATOM 2770 N THR A 279 16.905 -3.543 9.239 1.00 22.60 N
ANISOU 2770 N THR A 279 2684 3575 2327 78 63 141 N
ATOM 2771 CA THR A 279 17.001 -4.645 8.286 1.00 29.94 C
ANISOU 2771 CA THR A 279 3646 4499 3233 41 61 107 C
ATOM 2772 C THR A 279 17.369 -5.958 8.959 1.00 28.42 C
ANISOU 2772 C THR A 279 3445 4276 3077 32 93 84 C
ATOM 2773 O THR A 279 17.164 -7.023 8.367 1.00 34.09 O
ANISOU 2773 O THR A 279 4187 4978 3789 1 81 52 O
ATOM 2774 CB THR A 279 18.029 -4.334 7.192 1.00 29.27 C
ANISOU 2774 CB THR A 279 3616 4415 3090 35 82 95 C
ATOM 2775 OG1 THR A 279 19.337 -4.225 7.770 1.00 32.92 O
ANISOU 2775 OG1 THR A 279 4076 4862 3570 53 136 94 O
ATOM 2776 CG2 THR A 279 17.682 -3.038 6.479 1.00 23.22 C
ANISOU 2776 CG2 THR A 279 2870 3670 2283 40 47 128 C
ATOM 2777 N ASN A 280 17.913 -5.907 10.176 1.00 24.45 N
ANISOU 2777 N ASN A 280 2919 3761 2611 59 126 98 N
ATOM 2778 CA ASN A 280 18.208 -7.137 10.901 1.00 26.70 C
ANISOU 2778 CA ASN A 280 3200 4012 2931 56 150 87 C
ATOM 2779 C ASN A 280 16.942 -7.945 11.163 1.00 27.22 C
ANISOU 2779 C ASN A 280 3242 4075 3026 20 124 95 C
ATOM 2780 O ASN A 280 17.004 -9.174 11.286 1.00 26.49 O
ANISOU 2780 O ASN A 280 3167 3942 2956 -2 130 81 O
ATOM 2781 CB ASN A 280 18.926 -6.810 12.210 1.00 27.20 C
ANISOU 2781 CB ASN A 280 3243 4071 3020 94 180 108 C
ATOM 2782 CG ASN A 280 19.288 -8.047 12.998 1.00 25.87 C
ANISOU 2782 CG ASN A 280 3078 3866 2884 97 201 105 C
ATOM 2783 OD1 ASN A 280 18.724 -8.307 14.059 1.00 32.14 O
ANISOU 2783 OD1 ASN A 280 3849 4661 3703 100 203 133 O
ATOM 2784 ND2 ASN A 280 20.225 -8.829 12.474 1.00 29.63 N
ANISOU 2784 ND2 ASN A 280 3588 4311 3358 102 219 73 N
ATOM 2785 N SER A 281 15.785 -7.285 11.229 1.00 23.61 N
ANISOU 2785 N SER A 281 2742 3658 2572 15 94 120 N
ATOM 2786 CA SER A 281 14.525 -8.002 11.397 1.00 28.34 C
ANISOU 2786 CA SER A 281 3301 4266 3202 -28 68 132 C
ATOM 2787 C SER A 281 14.068 -8.717 10.128 1.00 28.83 C
ANISOU 2787 C SER A 281 3390 4315 3248 -81 22 98 C
ATOM 2788 O SER A 281 13.022 -9.374 10.160 1.00 27.78 O
ANISOU 2788 O SER A 281 3222 4187 3146 -131 -8 106 O
ATOM 2789 CB SER A 281 13.434 -7.040 11.880 1.00 27.77 C
ANISOU 2789 CB SER A 281 3161 4251 3139 -7 52 168 C
ATOM 2790 OG SER A 281 13.812 -6.399 13.089 1.00 27.28 O
ANISOU 2790 OG SER A 281 3082 4198 3083 45 92 190 O
ATOM 2791 N VAL A 282 14.822 -8.610 9.033 1.00 29.51 N
ANISOU 2791 N VAL A 282 3538 4389 3286 -76 17 62 N
ATOM 2792 CA VAL A 282 14.489 -9.282 7.784 1.00 26.19 C
ANISOU 2792 CA VAL A 282 3159 3956 2835 -120 -27 20 C
ATOM 2793 C VAL A 282 15.418 -10.460 7.490 1.00 30.85 C
ANISOU 2793 C VAL A 282 3817 4484 3420 -127 -1 -29 C
ATOM 2794 O VAL A 282 15.012 -11.388 6.770 1.00 29.86 O
ANISOU 2794 O VAL A 282 3728 4329 3288 -172 -39 -70 O
ATOM 2795 CB VAL A 282 14.510 -8.284 6.603 1.00 28.39 C
ANISOU 2795 CB VAL A 282 3466 4276 3045 -106 -57 14 C
ATOM 2796 CG1 VAL A 282 13.931 -8.914 5.342 1.00 33.61 C
ANISOU 2796 CG1 VAL A 282 4168 4937 3666 -153 -118 -29 C
ATOM 2797 CG2 VAL A 282 13.781 -6.999 6.956 1.00 23.47 C
ANISOU 2797 CG2 VAL A 282 2786 3702 2430 -78 -79 63 C
ATOM 2798 N VAL A 283 16.640 -10.462 8.028 1.00 28.90 N
ANISOU 2798 N VAL A 283 3587 4216 3180 -81 58 -30 N
ATOM 2799 CA VAL A 283 17.664 -11.370 7.522 1.00 23.81 C
ANISOU 2799 CA VAL A 283 3006 3522 2518 -67 86 -82 C
ATOM 2800 C VAL A 283 17.538 -12.777 8.102 1.00 23.24 C
ANISOU 2800 C VAL A 283 2953 3378 2501 -88 83 -96 C
ATOM 2801 O VAL A 283 17.882 -13.754 7.427 1.00 24.64 O
ANISOU 2801 O VAL A 283 3193 3502 2665 -93 78 -152 O
ATOM 2802 CB VAL A 283 19.062 -10.785 7.786 1.00 26.43 C
ANISOU 2802 CB VAL A 283 3336 3868 2836 -8 146 -77 C
ATOM 2803 CG1 VAL A 283 19.200 -9.423 7.124 1.00 28.20 C
ANISOU 2803 CG1 VAL A 283 3555 4153 3008 1 147 -60 C
ATOM 2804 CG2 VAL A 283 19.329 -10.682 9.280 1.00 24.93 C
ANISOU 2804 CG2 VAL A 283 3100 3669 2703 18 171 -33 C
ATOM 2805 N ASN A 284 17.056 -12.919 9.339 1.00 28.37 N
ANISOU 2805 N ASN A 284 3554 4018 3207 -100 87 -45 N
ATOM 2806 CA ASN A 284 17.057 -14.237 9.973 1.00 27.64 C
ANISOU 2806 CA ASN A 284 3487 3849 3166 -119 89 -44 C
ATOM 2807 C ASN A 284 16.246 -15.287 9.218 1.00 27.27 C
ANISOU 2807 C ASN A 284 3482 3749 3130 -189 36 -82 C
ATOM 2808 O ASN A 284 16.735 -16.424 9.099 1.00 30.82 O
ANISOU 2808 O ASN A 284 3998 4115 3598 -187 37 -120 O
ATOM 2809 CB ASN A 284 16.573 -14.131 11.426 1.00 26.92 C
ANISOU 2809 CB ASN A 284 3338 3770 3122 -126 105 27 C
ATOM 2810 CG ASN A 284 17.545 -13.379 12.315 1.00 34.03 C
ANISOU 2810 CG ASN A 284 4216 4699 4015 -55 151 55 C
ATOM 2811 OD1 ASN A 284 18.708 -13.182 11.958 1.00 30.65 O
ANISOU 2811 OD1 ASN A 284 3814 4267 3563 -5 174 23 O
ATOM 2812 ND2 ASN A 284 17.075 -12.964 13.486 1.00 33.84 N
ANISOU 2812 ND2 ASN A 284 4140 4707 4008 -52 165 112 N
ATOM 2813 N PRO A 285 15.039 -15.009 8.708 1.00 23.27 N
ANISOU 2813 N PRO A 285 2941 3282 2617 -250 -16 -77 N
ATOM 2814 CA PRO A 285 14.344 -16.040 7.918 1.00 24.27 C
ANISOU 2814 CA PRO A 285 3113 3355 2754 -322 -77 -123 C
ATOM 2815 C PRO A 285 15.128 -16.502 6.701 1.00 25.01 C
ANISOU 2815 C PRO A 285 3305 3407 2791 -297 -86 -209 C
ATOM 2816 O PRO A 285 14.985 -17.660 6.288 1.00 25.61 O
ANISOU 2816 O PRO A 285 3448 3400 2883 -337 -121 -259 O
ATOM 2817 CB PRO A 285 13.034 -15.351 7.518 1.00 24.58 C
ANISOU 2817 CB PRO A 285 3083 3471 2786 -375 -134 -101 C
ATOM 2818 CG PRO A 285 12.808 -14.344 8.586 1.00 23.71 C
ANISOU 2818 CG PRO A 285 2882 3430 2695 -342 -95 -27 C
ATOM 2819 CD PRO A 285 14.172 -13.839 8.947 1.00 22.89 C
ANISOU 2819 CD PRO A 285 2808 3323 2564 -256 -29 -28 C
ATOM 2820 N PHE A 286 15.956 -15.634 6.115 1.00 24.25 N
ANISOU 2820 N PHE A 286 3222 3365 2628 -233 -52 -229 N
ATOM 2821 CA PHE A 286 16.769 -16.047 4.975 1.00 29.62 C
ANISOU 2821 CA PHE A 286 3991 4018 3244 -200 -44 -310 C
ATOM 2822 C PHE A 286 17.897 -16.974 5.408 1.00 29.79 C
ANISOU 2822 C PHE A 286 4062 3961 3296 -144 7 -340 C
ATOM 2823 O PHE A 286 18.263 -17.899 4.673 1.00 28.12 O
ANISOU 2823 O PHE A 286 3936 3687 3062 -133 -1 -416 O
ATOM 2824 CB PHE A 286 17.329 -14.821 4.254 1.00 26.11 C
ANISOU 2824 CB PHE A 286 3540 3661 2719 -153 -14 -310 C
ATOM 2825 CG PHE A 286 16.333 -14.136 3.363 1.00 35.55 C
ANISOU 2825 CG PHE A 286 4728 4919 3862 -197 -78 -307 C
ATOM 2826 CD1 PHE A 286 15.528 -13.120 3.851 1.00 32.07 C
ANISOU 2826 CD1 PHE A 286 4204 4539 3442 -214 -100 -238 C
ATOM 2827 CD2 PHE A 286 16.198 -14.515 2.038 1.00 34.16 C
ANISOU 2827 CD2 PHE A 286 4629 4739 3609 -215 -119 -377 C
ATOM 2828 CE1 PHE A 286 14.610 -12.492 3.032 1.00 35.69 C
ANISOU 2828 CE1 PHE A 286 4652 5054 3854 -244 -166 -232 C
ATOM 2829 CE2 PHE A 286 15.280 -13.891 1.214 1.00 40.55 C
ANISOU 2829 CE2 PHE A 286 5433 5608 4365 -252 -189 -371 C
ATOM 2830 CZ PHE A 286 14.485 -12.879 1.712 1.00 38.89 C
ANISOU 2830 CZ PHE A 286 5134 5458 4184 -266 -214 -296 C
ATOM 2831 N ILE A 287 18.463 -16.741 6.596 1.00 30.12 N
ANISOU 2831 N ILE A 287 4054 4005 3385 -103 56 -283 N
ATOM 2832 CA ILE A 287 19.513 -17.623 7.100 1.00 25.39 C
ANISOU 2832 CA ILE A 287 3494 3332 2821 -44 96 -302 C
ATOM 2833 C ILE A 287 18.962 -19.026 7.323 1.00 29.64 C
ANISOU 2833 C ILE A 287 4090 3756 3415 -91 53 -320 C
ATOM 2834 O ILE A 287 19.608 -20.026 6.983 1.00 33.95 O
ANISOU 2834 O ILE A 287 4716 4218 3966 -53 58 -381 O
ATOM 2835 CB ILE A 287 20.131 -17.043 8.387 1.00 31.90 C
ANISOU 2835 CB ILE A 287 4251 4188 3682 3 143 -232 C
ATOM 2836 CG1 ILE A 287 20.733 -15.663 8.116 1.00 31.88 C
ANISOU 2836 CG1 ILE A 287 4198 4285 3628 42 181 -219 C
ATOM 2837 CG2 ILE A 287 21.186 -17.984 8.948 1.00 28.74 C
ANISOU 2837 CG2 ILE A 287 3887 3713 3321 69 174 -246 C
ATOM 2838 CD1 ILE A 287 21.841 -15.666 7.082 1.00 38.31 C
ANISOU 2838 CD1 ILE A 287 5053 5116 4389 98 221 -283 C
ATOM 2839 N TYR A 288 17.755 -19.123 7.887 1.00 25.33 N
ANISOU 2839 N TYR A 288 3506 3204 2915 -175 11 -266 N
ATOM 2840 CA TYR A 288 17.140 -20.430 8.102 1.00 26.38 C
ANISOU 2840 CA TYR A 288 3691 3226 3107 -240 -34 -272 C
ATOM 2841 C TYR A 288 16.872 -21.135 6.777 1.00 31.24 C
ANISOU 2841 C TYR A 288 4395 3786 3690 -276 -90 -367 C
ATOM 2842 O TYR A 288 17.140 -22.334 6.634 1.00 29.44 O
ANISOU 2842 O TYR A 288 4258 3439 3490 -274 -108 -416 O
ATOM 2843 CB TYR A 288 15.841 -20.280 8.894 1.00 26.96 C
ANISOU 2843 CB TYR A 288 3688 3325 3230 -333 -62 -190 C
ATOM 2844 CG TYR A 288 15.973 -19.498 10.181 1.00 25.51 C
ANISOU 2844 CG TYR A 288 3420 3207 3065 -299 -10 -101 C
ATOM 2845 CD1 TYR A 288 17.104 -19.613 10.978 1.00 25.06 C
ANISOU 2845 CD1 TYR A 288 3380 3125 3018 -217 41 -81 C
ATOM 2846 CD2 TYR A 288 14.963 -18.639 10.597 1.00 24.90 C
ANISOU 2846 CD2 TYR A 288 3248 3222 2992 -343 -16 -41 C
ATOM 2847 CE1 TYR A 288 17.222 -18.896 12.156 1.00 33.18 C
ANISOU 2847 CE1 TYR A 288 4339 4213 4054 -186 81 -7 C
ATOM 2848 CE2 TYR A 288 15.075 -17.918 11.770 1.00 24.16 C
ANISOU 2848 CE2 TYR A 288 3087 3187 2905 -306 32 31 C
ATOM 2849 CZ TYR A 288 16.207 -18.049 12.546 1.00 29.06 C
ANISOU 2849 CZ TYR A 288 3734 3778 3530 -231 78 46 C
ATOM 2850 OH TYR A 288 16.323 -17.333 13.717 1.00 26.25 O
ANISOU 2850 OH TYR A 288 3320 3480 3173 -195 118 111 O
ATOM 2851 N ALA A 289 16.345 -20.401 5.794 1.00 28.16 N
ANISOU 2851 N ALA A 289 3987 3477 3237 -304 -121 -396 N
ATOM 2852 CA ALA A 289 15.993 -21.015 4.518 1.00 31.16 C
ANISOU 2852 CA ALA A 289 4452 3813 3572 -343 -185 -488 C
ATOM 2853 C ALA A 289 17.230 -21.505 3.778 1.00 32.51 C
ANISOU 2853 C ALA A 289 4724 3938 3689 -251 -146 -580 C
ATOM 2854 O ALA A 289 17.186 -22.536 3.099 1.00 30.80 O
ANISOU 2854 O ALA A 289 4610 3628 3465 -266 -189 -664 O
ATOM 2855 CB ALA A 289 15.206 -20.026 3.657 1.00 28.28 C
ANISOU 2855 CB ALA A 289 4045 3557 3142 -382 -229 -490 C
ATOM 2856 N TYR A 290 18.346 -20.787 3.902 1.00 32.81 N
ANISOU 2856 N TYR A 290 4734 4041 3692 -154 -66 -568 N
ATOM 2857 CA TYR A 290 19.545 -21.153 3.158 1.00 36.17 C
ANISOU 2857 CA TYR A 290 5235 4446 4061 -59 -17 -654 C
ATOM 2858 C TYR A 290 20.388 -22.202 3.873 1.00 36.27 C
ANISOU 2858 C TYR A 290 5291 4350 4141 6 15 -668 C
ATOM 2859 O TYR A 290 21.056 -23.002 3.210 1.00 29.94 O
ANISOU 2859 O TYR A 290 4581 3484 3313 68 27 -759 O
ATOM 2860 CB TYR A 290 20.395 -19.909 2.882 1.00 32.87 C
ANISOU 2860 CB TYR A 290 4760 4153 3576 8 56 -634 C
ATOM 2861 CG TYR A 290 19.995 -19.144 1.637 1.00 44.86 C
ANISOU 2861 CG TYR A 290 6294 5759 4990 -18 35 -664 C
ATOM 2862 CD1 TYR A 290 20.415 -19.559 0.379 1.00 45.19 C
ANISOU 2862 CD1 TYR A 290 6432 5797 4942 17 41 -763 C
ATOM 2863 CD2 TYR A 290 19.205 -18.003 1.718 1.00 45.72 C
ANISOU 2863 CD2 TYR A 290 6329 5957 5087 -72 7 -594 C
ATOM 2864 CE1 TYR A 290 20.055 -18.864 -0.763 1.00 51.36 C
ANISOU 2864 CE1 TYR A 290 7237 6662 5617 -7 19 -785 C
ATOM 2865 CE2 TYR A 290 18.840 -17.301 0.582 1.00 51.37 C
ANISOU 2865 CE2 TYR A 290 7065 6748 5705 -92 -19 -614 C
ATOM 2866 CZ TYR A 290 19.268 -17.737 -0.656 1.00 61.67 C
ANISOU 2866 CZ TYR A 290 8468 8050 6915 -62 -14 -706 C
ATOM 2867 OH TYR A 290 18.909 -17.045 -1.791 1.00 63.13 O
ANISOU 2867 OH TYR A 290 8682 8313 6991 -81 -43 -721 O
ATOM 2868 N ARG A 291 20.371 -22.230 5.207 1.00 30.20 N
ANISOU 2868 N ARG A 291 4463 3558 3454 1 27 -580 N
ATOM 2869 CA ARG A 291 21.320 -23.040 5.957 1.00 33.39 C
ANISOU 2869 CA ARG A 291 4897 3876 3916 81 62 -578 C
ATOM 2870 C ARG A 291 20.703 -24.158 6.785 1.00 34.56 C
ANISOU 2870 C ARG A 291 5088 3890 4152 24 12 -543 C
ATOM 2871 O ARG A 291 21.443 -25.036 7.243 1.00 37.50 O
ANISOU 2871 O ARG A 291 5515 4165 4570 92 26 -554 O
ATOM 2872 CB ARG A 291 22.163 -22.150 6.883 1.00 32.51 C
ANISOU 2872 CB ARG A 291 4686 3849 3815 148 127 -505 C
ATOM 2873 CG ARG A 291 23.109 -21.220 6.143 1.00 35.02 C
ANISOU 2873 CG ARG A 291 4968 4278 4058 219 189 -540 C
ATOM 2874 CD ARG A 291 24.206 -20.726 7.063 1.00 38.03 C
ANISOU 2874 CD ARG A 291 5274 4708 4470 298 247 -488 C
ATOM 2875 NE ARG A 291 24.962 -21.836 7.630 1.00 40.01 N
ANISOU 2875 NE ARG A 291 5567 4858 4779 375 254 -503 N
ATOM 2876 CZ ARG A 291 26.120 -22.275 7.157 1.00 42.61 C
ANISOU 2876 CZ ARG A 291 5920 5175 5094 480 299 -570 C
ATOM 2877 NH1 ARG A 291 26.703 -21.702 6.116 1.00 47.09 N
ANISOU 2877 NH1 ARG A 291 6473 5831 5587 517 349 -626 N
ATOM 2878 NH2 ARG A 291 26.709 -23.314 7.746 1.00 39.80 N
ANISOU 2878 NH2 ARG A 291 5605 4718 4799 553 294 -579 N
ATOM 2879 N ILE A 292 19.391 -24.161 6.996 1.00 29.29 N
ANISOU 2879 N ILE A 292 4399 3217 3514 -98 -45 -497 N
ATOM 2880 CA ILE A 292 18.728 -25.191 7.789 1.00 35.77 C
ANISOU 2880 CA ILE A 292 5255 3915 4420 -171 -89 -450 C
ATOM 2881 C ILE A 292 17.721 -25.886 6.883 1.00 32.56 C
ANISOU 2881 C ILE A 292 4919 3438 4016 -276 -171 -513 C
ATOM 2882 O ILE A 292 16.690 -25.302 6.525 1.00 36.24 O
ANISOU 2882 O ILE A 292 5326 3980 4461 -366 -210 -497 O
ATOM 2883 CB ILE A 292 18.052 -24.614 9.039 1.00 33.45 C
ANISOU 2883 CB ILE A 292 4856 3683 4169 -230 -77 -325 C
ATOM 2884 CG1 ILE A 292 19.052 -23.783 9.844 1.00 34.80 C
ANISOU 2884 CG1 ILE A 292 4959 3937 4325 -128 -5 -274 C
ATOM 2885 CG2 ILE A 292 17.503 -25.731 9.908 1.00 34.34 C
ANISOU 2885 CG2 ILE A 292 5012 3670 4367 -302 -109 -266 C
ATOM 2886 CD1 ILE A 292 18.489 -23.232 11.135 1.00 29.85 C
ANISOU 2886 CD1 ILE A 292 4242 3370 3730 -170 12 -159 C
ATOM 2887 N ARG A 293 18.019 -27.136 6.516 1.00 34.09 N
ANISOU 2887 N ARG A 293 5238 3480 4234 -260 -204 -586 N
ATOM 2888 CA ARG A 293 17.190 -27.851 5.551 1.00 44.11 C
ANISOU 2888 CA ARG A 293 6593 4669 5498 -353 -290 -667 C
ATOM 2889 C ARG A 293 15.775 -28.067 6.074 1.00 40.97 C
ANISOU 2889 C ARG A 293 6147 4250 5171 -514 -355 -588 C
ATOM 2890 O ARG A 293 14.806 -28.001 5.307 1.00 38.87 O
ANISOU 2890 O ARG A 293 5876 4007 4886 -614 -425 -625 O
ATOM 2891 CB ARG A 293 17.838 -29.190 5.194 1.00 42.03 C
ANISOU 2891 CB ARG A 293 6484 4231 5257 -297 -312 -760 C
ATOM 2892 CG ARG A 293 16.996 -30.054 4.268 1.00 48.00 C
ANISOU 2892 CG ARG A 293 7346 4878 6015 -398 -413 -850 C
ATOM 2893 CD ARG A 293 17.698 -31.352 3.895 1.00 56.50 C
ANISOU 2893 CD ARG A 293 8588 5772 7109 -327 -433 -953 C
ATOM 2894 NE ARG A 293 18.883 -31.127 3.074 1.00 69.60 N
ANISOU 2894 NE ARG A 293 10291 7477 8676 -169 -372 -1058 N
ATOM 2895 CZ ARG A 293 20.130 -31.281 3.498 1.00 73.91 C
ANISOU 2895 CZ ARG A 293 10847 8004 9232 -21 -296 -1059 C
ATOM 2896 NH1 ARG A 293 20.397 -31.679 4.731 1.00 79.49 N
ANISOU 2896 NH1 ARG A 293 11536 8637 10030 -2 -278 -965 N
ATOM 2897 NH2 ARG A 293 21.134 -31.034 2.661 1.00 81.20 N
ANISOU 2897 NH2 ARG A 293 11797 8988 10068 113 -236 -1156 N
ATOM 2898 N GLU A 294 15.632 -28.327 7.376 1.00 41.72 N
ANISOU 2898 N GLU A 294 6201 4305 5344 -543 -332 -478 N
ATOM 2899 CA GLU A 294 14.303 -28.557 7.932 1.00 39.83 C
ANISOU 2899 CA GLU A 294 5906 4053 5173 -698 -379 -394 C
ATOM 2900 C GLU A 294 13.433 -27.308 7.823 1.00 38.68 C
ANISOU 2900 C GLU A 294 5619 4086 4993 -752 -378 -350 C
ATOM 2901 O GLU A 294 12.219 -27.408 7.614 1.00 38.44 O
ANISOU 2901 O GLU A 294 5544 4069 4993 -884 -442 -334 O
ATOM 2902 CB GLU A 294 14.412 -29.018 9.385 1.00 34.94 C
ANISOU 2902 CB GLU A 294 5275 3371 4630 -706 -340 -277 C
ATOM 2903 CG GLU A 294 13.139 -29.653 9.923 1.00 41.56 C
ANISOU 2903 CG GLU A 294 6090 4149 5550 -874 -390 -197 C
ATOM 2904 CD GLU A 294 12.778 -30.938 9.200 1.00 50.36 C
ANISOU 2904 CD GLU A 294 7335 5087 6711 -961 -481 -273 C
ATOM 2905 OE1 GLU A 294 13.697 -31.723 8.885 1.00 63.76 O
ANISOU 2905 OE1 GLU A 294 9169 6649 8407 -874 -488 -349 O
ATOM 2906 OE2 GLU A 294 11.576 -31.163 8.943 1.00 46.74 O
ANISOU 2906 OE2 GLU A 294 6842 4624 6292 -1114 -548 -260 O
ATOM 2907 N PHE A 295 14.036 -26.123 7.959 1.00 31.97 N
ANISOU 2907 N PHE A 295 4693 3371 4082 -652 -310 -331 N
ATOM 2908 CA PHE A 295 13.282 -24.889 7.757 1.00 34.28 C
ANISOU 2908 CA PHE A 295 4864 3824 4336 -686 -312 -300 C
ATOM 2909 C PHE A 295 12.980 -24.665 6.281 1.00 38.60 C
ANISOU 2909 C PHE A 295 5446 4406 4816 -704 -374 -400 C
ATOM 2910 O PHE A 295 11.871 -24.249 5.924 1.00 35.27 O
ANISOU 2910 O PHE A 295 4953 4056 4393 -792 -430 -386 O
ATOM 2911 CB PHE A 295 14.050 -23.693 8.323 1.00 29.78 C
ANISOU 2911 CB PHE A 295 4218 3372 3724 -576 -227 -253 C
ATOM 2912 CG PHE A 295 13.700 -23.356 9.744 1.00 36.06 C
ANISOU 2912 CG PHE A 295 4921 4213 4568 -594 -182 -134 C
ATOM 2913 CD1 PHE A 295 12.505 -22.722 10.046 1.00 30.45 C
ANISOU 2913 CD1 PHE A 295 4098 3599 3873 -673 -196 -70 C
ATOM 2914 CD2 PHE A 295 14.575 -23.652 10.776 1.00 31.86 C
ANISOU 2914 CD2 PHE A 295 4412 3633 4059 -524 -126 -87 C
ATOM 2915 CE1 PHE A 295 12.185 -22.405 11.349 1.00 29.02 C
ANISOU 2915 CE1 PHE A 295 3835 3466 3725 -683 -147 34 C
ATOM 2916 CE2 PHE A 295 14.260 -23.335 12.082 1.00 36.58 C
ANISOU 2916 CE2 PHE A 295 4934 4278 4686 -538 -85 20 C
ATOM 2917 CZ PHE A 295 13.064 -22.711 12.369 1.00 34.20 C
ANISOU 2917 CZ PHE A 295 4526 4074 4394 -617 -91 78 C
ATOM 2918 N ARG A 296 13.955 -24.935 5.410 1.00 37.75 N
ANISOU 2918 N ARG A 296 5444 4254 4648 -618 -366 -500 N
ATOM 2919 CA ARG A 296 13.767 -24.696 3.983 1.00 36.88 C
ANISOU 2919 CA ARG A 296 5378 4183 4452 -624 -419 -598 C
ATOM 2920 C ARG A 296 12.667 -25.580 3.411 1.00 35.77 C
ANISOU 2920 C ARG A 296 5286 3961 4343 -756 -531 -644 C
ATOM 2921 O ARG A 296 11.829 -25.115 2.630 1.00 40.39 O
ANISOU 2921 O ARG A 296 5837 4623 4888 -818 -598 -666 O
ATOM 2922 CB ARG A 296 15.081 -24.927 3.241 1.00 41.45 C
ANISOU 2922 CB ARG A 296 6064 4726 4957 -501 -376 -696 C
ATOM 2923 CG ARG A 296 14.973 -24.795 1.734 1.00 45.08 C
ANISOU 2923 CG ARG A 296 6594 5220 5313 -500 -425 -804 C
ATOM 2924 CD ARG A 296 16.340 -24.852 1.071 1.00 49.18 C
ANISOU 2924 CD ARG A 296 7198 5735 5751 -365 -356 -890 C
ATOM 2925 NE ARG A 296 17.059 -26.083 1.372 1.00 46.12 N
ANISOU 2925 NE ARG A 296 6912 5198 5416 -313 -340 -940 N
ATOM 2926 CZ ARG A 296 18.060 -26.178 2.238 1.00 47.35 C
ANISOU 2926 CZ ARG A 296 7048 5329 5614 -219 -260 -900 C
ATOM 2927 NH1 ARG A 296 18.486 -25.127 2.920 1.00 45.39 N
ANISOU 2927 NH1 ARG A 296 6686 5195 5365 -173 -188 -812 N
ATOM 2928 NH2 ARG A 296 18.651 -27.356 2.420 1.00 54.41 N
ANISOU 2928 NH2 ARG A 296 8044 6076 6555 -167 -258 -950 N
ATOM 2929 N GLN A 297 12.653 -26.860 3.789 1.00 37.92 N
ANISOU 2929 N GLN A 297 5642 4075 4693 -802 -559 -656 N
ATOM 2930 CA GLN A 297 11.630 -27.768 3.282 1.00 37.54 C
ANISOU 2930 CA GLN A 297 5646 3933 4686 -940 -672 -700 C
ATOM 2931 C GLN A 297 10.252 -27.402 3.818 1.00 40.58 C
ANISOU 2931 C GLN A 297 5889 4394 5136 -1077 -714 -601 C
ATOM 2932 O GLN A 297 9.246 -27.549 3.114 1.00 38.23 O
ANISOU 2932 O GLN A 297 5579 4107 4840 -1187 -814 -636 O
ATOM 2933 CB GLN A 297 11.986 -29.210 3.642 1.00 41.36 C
ANISOU 2933 CB GLN A 297 6257 4214 5244 -955 -689 -728 C
ATOM 2934 CG GLN A 297 13.219 -29.740 2.927 1.00 53.30 C
ANISOU 2934 CG GLN A 297 7921 5638 6695 -824 -666 -850 C
ATOM 2935 CD GLN A 297 13.645 -31.106 3.430 1.00 62.15 C
ANISOU 2935 CD GLN A 297 9164 6552 7896 -818 -675 -865 C
ATOM 2936 OE1 GLN A 297 13.442 -31.441 4.597 1.00 63.88 O
ANISOU 2936 OE1 GLN A 297 9345 6718 8210 -864 -656 -756 O
ATOM 2937 NE2 GLN A 297 14.237 -31.903 2.549 1.00 55.31 N
ANISOU 2937 NE2 GLN A 297 8455 5569 6992 -756 -706 -999 N
ATOM 2938 N THR A 298 10.186 -26.926 5.062 1.00 36.91 N
ANISOU 2938 N THR A 298 5314 3988 4722 -1068 -640 -478 N
ATOM 2939 CA THR A 298 8.909 -26.480 5.606 1.00 35.82 C
ANISOU 2939 CA THR A 298 5026 3944 4639 -1181 -662 -382 C
ATOM 2940 C THR A 298 8.447 -25.195 4.931 1.00 38.95 C
ANISOU 2940 C THR A 298 5324 4511 4963 -1159 -681 -391 C
ATOM 2941 O THR A 298 7.247 -25.004 4.704 1.00 38.47 O
ANISOU 2941 O THR A 298 5172 4516 4930 -1264 -751 -368 O
ATOM 2942 CB THR A 298 9.019 -26.287 7.118 1.00 35.21 C
ANISOU 2942 CB THR A 298 4867 3890 4620 -1163 -570 -254 C
ATOM 2943 OG1 THR A 298 9.622 -27.447 7.703 1.00 35.30 O
ANISOU 2943 OG1 THR A 298 4988 3739 4686 -1161 -551 -245 O
ATOM 2944 CG2 THR A 298 7.641 -26.085 7.726 1.00 35.08 C
ANISOU 2944 CG2 THR A 298 4705 3953 4672 -1292 -590 -156 C
ATOM 2945 N PHE A 299 9.386 -24.305 4.596 1.00 33.59 N
ANISOU 2945 N PHE A 299 4662 3906 4195 -1024 -621 -420 N
ATOM 2946 CA PHE A 299 9.021 -23.091 3.874 1.00 37.16 C
ANISOU 2946 CA PHE A 299 5042 4505 4571 -997 -643 -429 C
ATOM 2947 C PHE A 299 8.399 -23.421 2.523 1.00 42.34 C
ANISOU 2947 C PHE A 299 5755 5150 5183 -1066 -760 -523 C
ATOM 2948 O PHE A 299 7.409 -22.800 2.122 1.00 40.72 O
ANISOU 2948 O PHE A 299 5459 5046 4966 -1120 -826 -504 O
ATOM 2949 CB PHE A 299 10.242 -22.190 3.695 1.00 39.74 C
ANISOU 2949 CB PHE A 299 5396 4893 4811 -849 -558 -446 C
ATOM 2950 CG PHE A 299 10.718 -21.546 4.967 1.00 34.20 C
ANISOU 2950 CG PHE A 299 4616 4239 4142 -782 -457 -351 C
ATOM 2951 CD1 PHE A 299 9.928 -21.553 6.106 1.00 31.91 C
ANISOU 2951 CD1 PHE A 299 4222 3968 3934 -846 -444 -254 C
ATOM 2952 CD2 PHE A 299 11.956 -20.929 5.020 1.00 29.42 C
ANISOU 2952 CD2 PHE A 299 4037 3662 3480 -659 -377 -360 C
ATOM 2953 CE1 PHE A 299 10.367 -20.960 7.273 1.00 29.31 C
ANISOU 2953 CE1 PHE A 299 3830 3684 3621 -780 -355 -174 C
ATOM 2954 CE2 PHE A 299 12.400 -20.334 6.183 1.00 29.45 C
ANISOU 2954 CE2 PHE A 299 3973 3707 3510 -601 -296 -280 C
ATOM 2955 CZ PHE A 299 11.604 -20.350 7.312 1.00 33.83 C
ANISOU 2955 CZ PHE A 299 4436 4278 4138 -659 -286 -189 C
ATOM 2956 N ARG A 300 8.962 -24.401 1.809 1.00 41.22 N
ANISOU 2956 N ARG A 300 5765 4885 5012 -1060 -793 -627 N
ATOM 2957 CA ARG A 300 8.389 -24.808 0.528 1.00 40.60 C
ANISOU 2957 CA ARG A 300 5758 4785 4883 -1128 -913 -727 C
ATOM 2958 C ARG A 300 6.981 -25.359 0.709 1.00 46.21 C
ANISOU 2958 C ARG A 300 6396 5473 5689 -1295 -1017 -694 C
ATOM 2959 O ARG A 300 6.065 -25.019 -0.050 1.00 49.76 O
ANISOU 2959 O ARG A 300 6798 5999 6110 -1361 -1116 -716 O
ATOM 2960 CB ARG A 300 9.279 -25.853 -0.149 1.00 44.99 C
ANISOU 2960 CB ARG A 300 6499 5198 5397 -1084 -923 -849 C
ATOM 2961 CG ARG A 300 10.691 -25.395 -0.474 1.00 54.09 C
ANISOU 2961 CG ARG A 300 7722 6379 6451 -922 -822 -894 C
ATOM 2962 CD ARG A 300 11.286 -26.257 -1.582 1.00 58.97 C
ANISOU 2962 CD ARG A 300 8518 6896 6993 -884 -858 -1040 C
ATOM 2963 NE ARG A 300 12.742 -26.178 -1.637 1.00 62.67 N
ANISOU 2963 NE ARG A 300 9054 7355 7401 -730 -746 -1078 N
ATOM 2964 CZ ARG A 300 13.560 -27.107 -1.161 1.00 59.72 C
ANISOU 2964 CZ ARG A 300 8763 6850 7078 -674 -699 -1107 C
ATOM 2965 NH1 ARG A 300 13.098 -28.208 -0.590 1.00 56.54 N
ANISOU 2965 NH1 ARG A 300 8399 6299 6784 -759 -752 -1099 N
ATOM 2966 NH2 ARG A 300 14.874 -26.930 -1.264 1.00 66.33 N
ANISOU 2966 NH2 ARG A 300 9641 7702 7858 -529 -597 -1141 N
ATOM 2967 N LYS A 301 6.794 -26.222 1.712 1.00 49.67 N
ANISOU 2967 N LYS A 301 6824 5807 6242 -1368 -999 -638 N
ATOM 2968 CA LYS A 301 5.484 -26.815 1.964 1.00 47.78 C
ANISOU 2968 CA LYS A 301 6508 5541 6104 -1540 -1088 -596 C
ATOM 2969 C LYS A 301 4.439 -25.745 2.255 1.00 48.82 C
ANISOU 2969 C LYS A 301 6444 5850 6255 -1579 -1096 -505 C
ATOM 2970 O LYS A 301 3.305 -25.823 1.767 1.00 61.10 O
ANISOU 2970 O LYS A 301 7929 7446 7839 -1696 -1205 -513 O
ATOM 2971 CB LYS A 301 5.584 -27.808 3.125 1.00 52.29 C
ANISOU 2971 CB LYS A 301 7100 5978 6788 -1598 -1042 -528 C
ATOM 2972 CG LYS A 301 4.254 -28.357 3.626 1.00 56.91 C
ANISOU 2972 CG LYS A 301 7583 6548 7493 -1783 -1107 -454 C
ATOM 2973 CD LYS A 301 3.681 -29.393 2.676 1.00 70.47 C
ANISOU 2973 CD LYS A 301 9396 8146 9234 -1916 -1251 -552 C
ATOM 2974 CE LYS A 301 2.369 -29.955 3.198 1.00 74.41 C
ANISOU 2974 CE LYS A 301 9782 8630 9861 -2114 -1315 -471 C
ATOM 2975 NZ LYS A 301 1.822 -31.007 2.298 1.00 76.54 N
ANISOU 2975 NZ LYS A 301 10151 8769 10162 -2256 -1466 -570 N
ATOM 2976 N ILE A 302 4.807 -24.730 3.038 1.00 48.72 N
ANISOU 2976 N ILE A 302 6340 5943 6228 -1477 -986 -421 N
ATOM 2977 CA ILE A 302 3.867 -23.664 3.369 1.00 48.76 C
ANISOU 2977 CA ILE A 302 6162 6114 6251 -1492 -984 -337 C
ATOM 2978 C ILE A 302 3.537 -22.835 2.134 1.00 53.55 C
ANISOU 2978 C ILE A 302 6756 6826 6765 -1461 -1066 -397 C
ATOM 2979 O ILE A 302 2.381 -22.453 1.914 1.00 54.06 O
ANISOU 2979 O ILE A 302 6695 6987 6856 -1533 -1144 -369 O
ATOM 2980 CB ILE A 302 4.441 -22.791 4.499 1.00 46.87 C
ANISOU 2980 CB ILE A 302 5852 5946 6009 -1380 -847 -246 C
ATOM 2981 CG1 ILE A 302 4.591 -23.612 5.779 1.00 42.26 C
ANISOU 2981 CG1 ILE A 302 5269 5272 5516 -1423 -776 -172 C
ATOM 2982 CG2 ILE A 302 3.563 -21.578 4.740 1.00 45.98 C
ANISOU 2982 CG2 ILE A 302 5567 6004 5900 -1367 -843 -175 C
ATOM 2983 CD1 ILE A 302 5.251 -22.856 6.902 1.00 35.47 C
ANISOU 2983 CD1 ILE A 302 4361 4470 4645 -1311 -648 -93 C
ATOM 2984 N ILE A 303 4.540 -22.556 1.303 1.00 55.93 N
ANISOU 2984 N ILE A 303 7184 7113 6955 -1353 -1052 -478 N
ATOM 2985 CA ILE A 303 4.358 -21.639 0.184 1.00 57.47 C
ANISOU 2985 CA ILE A 303 7376 7414 7045 -1306 -1114 -521 C
ATOM 2986 C ILE A 303 3.599 -22.308 -0.956 1.00 59.87 C
ANISOU 2986 C ILE A 303 7732 7687 7328 -1412 -1267 -608 C
ATOM 2987 O ILE A 303 2.660 -21.730 -1.515 1.00 61.35 O
ANISOU 2987 O ILE A 303 7832 7980 7496 -1449 -1360 -600 O
ATOM 2988 CB ILE A 303 5.725 -21.098 -0.277 1.00 51.69 C
ANISOU 2988 CB ILE A 303 6758 6684 6196 -1159 -1034 -567 C
ATOM 2989 CG1 ILE A 303 6.275 -20.112 0.756 1.00 50.34 C
ANISOU 2989 CG1 ILE A 303 6505 6582 6040 -1059 -907 -473 C
ATOM 2990 CG2 ILE A 303 5.614 -20.442 -1.643 1.00 57.44 C
ANISOU 2990 CG2 ILE A 303 7531 7492 6800 -1126 -1111 -628 C
ATOM 2991 CD1 ILE A 303 7.779 -19.969 0.726 1.00 47.74 C
ANISOU 2991 CD1 ILE A 303 6283 6214 5642 -937 -805 -506 C
ATOM 2992 N ARG A 304 3.983 -23.537 -1.313 1.00 60.49 N
ANISOU 2992 N ARG A 304 7956 7618 7410 -1459 -1303 -697 N
ATOM 2993 CA ARG A 304 3.395 -24.179 -2.487 1.00 64.16 C
ANISOU 2993 CA ARG A 304 8499 8042 7837 -1551 -1453 -800 C
ATOM 2994 C ARG A 304 1.929 -24.537 -2.271 1.00 71.17 C
ANISOU 2994 C ARG A 304 9253 8952 8836 -1717 -1565 -756 C
ATOM 2995 O ARG A 304 1.156 -24.578 -3.236 1.00 83.26 O
ANISOU 2995 O ARG A 304 10783 10522 10332 -1789 -1705 -814 O
ATOM 2996 CB ARG A 304 4.196 -25.426 -2.868 1.00 64.08 C
ANISOU 2996 CB ARG A 304 8686 7855 7808 -1552 -1460 -911 C
ATOM 2997 CG ARG A 304 4.051 -26.597 -1.907 1.00 65.38 C
ANISOU 2997 CG ARG A 304 8858 7871 8112 -1651 -1447 -879 C
ATOM 2998 CD ARG A 304 4.845 -27.804 -2.383 1.00 66.55 C
ANISOU 2998 CD ARG A 304 9216 7836 8236 -1638 -1465 -1000 C
ATOM 2999 N SER A 305 1.525 -24.796 -1.030 1.00 67.82 N
ANISOU 2999 N SER A 305 8715 8512 8543 -1782 -1507 -654 N
ATOM 3000 CA SER A 305 0.142 -25.137 -0.726 1.00 76.29 C
ANISOU 3000 CA SER A 305 9641 9615 9731 -1946 -1596 -600 C
ATOM 3001 C SER A 305 -0.719 -23.915 -0.439 1.00 78.54 C
ANISOU 3001 C SER A 305 9718 10094 10032 -1925 -1591 -505 C
ATOM 3002 O SER A 305 -1.919 -24.067 -0.184 1.00 95.64 O
ANISOU 3002 O SER A 305 11731 12314 12293 -2051 -1658 -453 O
ATOM 3003 CB SER A 305 0.083 -26.098 0.467 1.00 79.69 C
ANISOU 3003 CB SER A 305 10054 9932 10294 -2038 -1533 -530 C
ATOM 3004 OG SER A 305 0.488 -25.452 1.661 1.00 85.66 O
ANISOU 3004 OG SER A 305 10724 10749 11076 -1948 -1382 -421 O
TER 3005 SER A 305
HETATM 3006 C1 CLR A2401 36.495 7.696 21.249 1.00 33.31 C
HETATM 3007 C2 CLR A2401 36.574 9.198 21.202 1.00 29.33 C
HETATM 3008 C3 CLR A2401 37.674 9.621 20.211 1.00 36.77 C
HETATM 3009 C4 CLR A2401 37.435 9.005 18.817 1.00 29.34 C
HETATM 3010 C5 CLR A2401 37.445 7.505 18.952 1.00 29.16 C
HETATM 3011 C6 CLR A2401 37.431 6.914 17.550 1.00 32.49 C
HETATM 3012 C7 CLR A2401 37.293 5.422 17.626 1.00 27.92 C
HETATM 3013 C8 CLR A2401 36.125 5.064 18.541 1.00 25.23 C
HETATM 3014 C9 CLR A2401 36.193 5.643 19.954 1.00 28.57 C
HETATM 3015 C10 CLR A2401 36.249 7.149 19.836 1.00 32.52 C
HETATM 3016 C11 CLR A2401 34.955 5.266 20.809 1.00 31.22 C
HETATM 3017 C12 CLR A2401 34.834 3.762 20.954 1.00 32.04 C
HETATM 3018 C13 CLR A2401 34.954 3.114 19.578 1.00 31.83 C
HETATM 3019 C14 CLR A2401 36.182 3.587 18.798 1.00 33.10 C
HETATM 3020 C15 CLR A2401 36.116 2.834 17.481 1.00 33.80 C
HETATM 3021 C16 CLR A2401 35.641 1.457 17.987 1.00 33.63 C
HETATM 3022 C17 CLR A2401 35.139 1.575 19.477 1.00 39.35 C
HETATM 3023 C18 CLR A2401 33.695 3.536 18.797 1.00 28.62 C
HETATM 3024 C19 CLR A2401 34.875 7.568 19.256 1.00 27.14 C
HETATM 3025 C20 CLR A2401 33.956 0.618 19.820 1.00 45.94 C
HETATM 3026 C21 CLR A2401 33.891 0.207 21.320 1.00 41.04 C
HETATM 3027 C22 CLR A2401 33.999 -0.727 19.034 1.00 44.29 C
HETATM 3028 C23 CLR A2401 33.313 -1.968 19.643 1.00 43.73 C
HETATM 3029 C24 CLR A2401 34.268 -3.174 19.857 1.00 56.00 C
HETATM 3030 C25 CLR A2401 34.186 -4.305 18.806 1.00 49.11 C
HETATM 3031 C26 CLR A2401 32.772 -4.852 18.612 1.00 60.49 C
HETATM 3032 C27 CLR A2401 34.728 -3.866 17.447 1.00 60.54 C
HETATM 3033 O1 CLR A2401 37.590 11.026 20.177 1.00 38.78 O
HETATM 3034 C1 CLR A2402 31.380 10.341 13.264 1.00 33.79 C
HETATM 3035 C2 CLR A2402 31.239 11.835 13.223 1.00 35.44 C
HETATM 3036 C3 CLR A2402 32.624 12.457 12.962 1.00 44.09 C
HETATM 3037 C4 CLR A2402 33.248 11.921 11.658 1.00 41.52 C
HETATM 3038 C5 CLR A2402 33.387 10.423 11.750 1.00 39.98 C
HETATM 3039 C6 CLR A2402 34.137 9.943 10.506 1.00 48.41 C
HETATM 3040 C7 CLR A2402 34.262 8.448 10.548 1.00 41.92 C
HETATM 3041 C8 CLR A2402 32.878 7.839 10.827 1.00 41.75 C
HETATM 3042 C9 CLR A2402 32.130 8.348 12.064 1.00 33.42 C
HETATM 3043 C10 CLR A2402 31.978 9.844 11.941 1.00 35.65 C
HETATM 3044 C11 CLR A2402 30.714 7.726 12.174 1.00 33.80 C
HETATM 3045 C12 CLR A2402 30.792 6.220 12.300 1.00 31.91 C
HETATM 3046 C13 CLR A2402 31.689 5.676 11.195 1.00 37.10 C
HETATM 3047 C14 CLR A2402 33.046 6.381 11.144 1.00 44.74 C
HETATM 3048 C15 CLR A2402 33.782 5.700 10.013 1.00 50.54 C
HETATM 3049 C16 CLR A2402 33.356 4.240 10.266 1.00 47.86 C
HETATM 3050 C17 CLR A2402 32.127 4.190 11.237 1.00 40.26 C
HETATM 3051 C18 CLR A2402 30.953 5.950 9.868 1.00 36.73 C
HETATM 3052 C19 CLR A2402 31.017 10.053 10.748 1.00 39.47 C
HETATM 3053 C20 CLR A2402 31.098 3.082 10.878 1.00 44.48 C
HETATM 3054 C21 CLR A2402 30.176 2.721 12.062 1.00 41.55 C
HETATM 3055 C22 CLR A2402 31.720 1.718 10.416 1.00 50.74 C
HETATM 3056 C23 CLR A2402 31.354 0.438 11.209 1.00 44.35 C
HETATM 3057 C24 CLR A2402 32.081 -0.851 10.745 1.00 44.94 C
HETATM 3058 C25 CLR A2402 31.315 -2.163 11.018 1.00 36.35 C
HETATM 3059 C26 CLR A2402 30.887 -2.291 12.478 1.00 34.84 C
HETATM 3060 C27 CLR A2402 30.069 -2.284 10.142 1.00 49.83 C
HETATM 3061 O1 CLR A2402 32.361 13.833 12.860 1.00 42.55 O
HETATM 3062 C1 CLR A2403 1.221 10.131 21.924 1.00 36.49 C
HETATM 3063 C2 CLR A2403 1.700 11.537 22.172 1.00 34.55 C
HETATM 3064 C3 CLR A2403 1.334 11.943 23.616 1.00 37.69 C
HETATM 3065 C4 CLR A2403 1.940 10.959 24.633 1.00 32.60 C
HETATM 3066 C5 CLR A2403 1.364 9.588 24.382 1.00 41.74 C
HETATM 3067 C6 CLR A2403 1.811 8.676 25.520 1.00 35.30 C
HETATM 3068 C7 CLR A2403 1.283 7.294 25.286 1.00 40.19 C
HETATM 3069 C8 CLR A2403 1.604 6.854 23.845 1.00 38.46 C
HETATM 3070 C9 CLR A2403 1.213 7.802 22.704 1.00 38.49 C
HETATM 3071 C10 CLR A2403 1.809 9.165 22.973 1.00 38.53 C
HETATM 3072 C11 CLR A2403 1.738 7.278 21.336 1.00 36.15 C
HETATM 3073 C12 CLR A2403 1.068 5.965 20.992 1.00 37.35 C
HETATM 3074 C13 CLR A2403 1.196 5.026 22.189 1.00 38.86 C
HETATM 3075 C14 CLR A2403 0.754 5.665 23.513 1.00 40.03 C
HETATM 3076 C15 CLR A2403 0.964 4.583 24.551 1.00 39.53 C
HETATM 3077 C16 CLR A2403 0.447 3.368 23.756 1.00 41.06 C
HETATM 3078 C17 CLR A2403 0.362 3.713 22.222 1.00 41.40 C
HETATM 3079 C18 CLR A2403 2.693 4.703 22.303 1.00 33.93 C
HETATM 3080 C19 CLR A2403 3.329 8.957 22.804 1.00 36.02 C
HETATM 3081 C20 CLR A2403 0.740 2.520 21.294 1.00 35.76 C
HETATM 3082 C21 CLR A2403 0.249 2.689 19.829 1.00 30.43 C
HETATM 3083 C22 CLR A2403 0.164 1.144 21.761 1.00 38.34 C
HETATM 3084 C23 CLR A2403 -0.259 0.129 20.678 1.00 39.83 C
HETATM 3085 C24 CLR A2403 -1.058 -1.083 21.214 1.00 47.99 C
HETATM 3086 C25 CLR A2403 -0.715 -2.440 20.554 1.00 60.97 C
HETATM 3087 C26 CLR A2403 -1.428 -3.618 21.227 1.00 62.42 C
HETATM 3088 C27 CLR A2403 -1.034 -2.452 19.047 1.00 49.61 C
HETATM 3089 O1 CLR A2403 1.865 13.239 23.777 1.00 37.79 O
HETATM 3090 C29 8E2 A2404 22.310 16.097 15.024 1.00 35.75 C
HETATM 3091 C30 8E2 A2404 23.192 17.179 14.834 1.00 36.60 C
HETATM 3092 C31 8E2 A2404 23.785 17.446 13.574 1.00 43.97 C
HETATM 3093 C32 8E2 A2404 23.421 16.554 12.556 1.00 40.74 C
HETATM 3094 C34 8E2 A2404 24.104 19.812 13.079 1.00 65.65 C
HETATM 3095 C35 8E2 A2404 23.058 20.419 14.153 1.00 63.04 C
HETATM 3096 C36 8E2 A2404 19.423 2.036 19.351 1.00 21.46 C
HETATM 3097 C15 8E2 A2404 18.088 8.493 16.757 1.00 21.46 C
HETATM 3098 C20 8E2 A2404 19.704 4.565 18.547 1.00 21.46 C
HETATM 3099 C22 8E2 A2404 16.997 10.689 15.682 1.00 28.26 C
HETATM 3100 C23 8E2 A2404 17.818 10.952 14.379 1.00 30.25 C
HETATM 3101 C19 8E2 A2404 16.292 7.170 16.387 1.00 21.46 C
HETATM 3102 C18 8E2 A2404 20.204 8.069 17.759 1.00 21.46 C
HETATM 3103 C17 8E2 A2404 18.511 6.206 17.582 1.00 21.63 C
HETATM 3104 C25 8E2 A2404 19.831 13.980 13.136 1.00 29.69 C
HETATM 3105 C1 8E2 A2404 11.673 17.697 12.492 1.00 61.41 C
HETATM 3106 C16 8E2 A2404 17.624 7.159 16.943 1.00 21.46 C
HETATM 3107 C2 8E2 A2404 12.819 17.604 13.568 1.00 65.30 C
HETATM 3108 C21 8E2 A2404 20.075 3.206 19.075 1.00 21.46 C
HETATM 3109 C24 8E2 A2404 19.064 12.616 13.113 1.00 27.82 C
HETATM 3110 C26 8E2 A2404 20.388 13.650 15.426 1.00 27.98 C
HETATM 3111 C27 8E2 A2404 19.597 12.301 15.431 1.00 30.29 C
HETATM 3112 C28 8E2 A2404 21.934 15.188 14.016 1.00 34.04 C
HETATM 3113 C3 8E2 A2404 15.085 18.463 13.529 1.00 80.30 C
HETATM 3114 C33 8E2 A2404 22.541 15.477 12.759 1.00 29.58 C
HETATM 3115 C37 8E2 A2404 20.356 1.103 19.819 1.00 21.46 C
HETATM 3116 C38 8E2 A2404 21.513 1.724 19.803 1.00 23.62 C
HETATM 3117 C4 8E2 A2404 15.912 19.664 12.948 1.00 89.66 C
HETATM 3118 C5 8E2 A2404 17.813 18.199 12.719 1.00 87.56 C
HETATM 3119 C6 8E2 A2404 19.065 17.994 11.811 1.00 70.94 C
HETATM 3120 C7 8E2 A2404 20.062 20.174 11.950 1.00 85.06 C
HETATM 3121 C8 8E2 A2404 21.421 20.929 12.240 1.00 77.83 C
HETATM 3122 C9 8E2 A2404 11.346 17.217 10.165 1.00 61.18 C
HETATM 3123 N1 8E2 A2404 21.813 20.929 13.693 1.00 62.81 N
HETATM 3124 N10 8E2 A2404 21.003 13.997 14.090 1.00 38.47 N
HETATM 3125 N2 8E2 A2404 19.361 8.956 17.157 1.00 24.20 N
HETATM 3126 N3 8E2 A2404 19.811 6.688 17.986 1.00 22.41 N
HETATM 3127 N4 8E2 A2404 21.456 8.488 18.161 1.00 26.93 N
HETATM 3128 N5 8E2 A2404 17.062 9.241 16.126 1.00 26.37 N
HETATM 3129 N6 8E2 A2404 15.981 8.402 15.910 1.00 23.88 N
HETATM 3130 N7 8E2 A2404 18.454 4.886 17.932 1.00 26.02 N
HETATM 3131 N8 8E2 A2404 20.551 5.649 18.588 1.00 27.11 N
HETATM 3132 N9 8E2 A2404 18.480 12.317 14.448 1.00 32.38 N
HETATM 3133 O1 8E2 A2404 11.939 16.847 11.388 1.00 72.49 O
HETATM 3134 O2 8E2 A2404 13.690 18.724 13.492 1.00 82.41 O
HETATM 3135 O3 8E2 A2404 16.948 19.150 12.136 1.00101.54 O
HETATM 3136 O4 8E2 A2404 20.168 18.782 12.191 1.00 75.37 O
HETATM 3137 O7 8E2 A2404 24.656 18.526 13.397 1.00 48.71 O
HETATM 3138 O8 8E2 A2404 23.322 20.435 15.304 1.00 67.41 O
HETATM 3139 O9 8E2 A2404 21.461 3.037 19.355 1.00 21.46 O
HETATM 3140 C1 OLA A2405 19.140 -22.363 28.353 1.00 52.91 C
HETATM 3141 O1 OLA A2405 19.497 -22.333 27.156 1.00 44.27 O
HETATM 3142 O2 OLA A2405 18.298 -23.218 28.704 1.00 69.52 O
HETATM 3143 C2 OLA A2405 19.704 -21.385 29.358 1.00 42.27 C
HETATM 3144 C3 OLA A2405 19.614 -19.971 28.797 1.00 43.13 C
HETATM 3145 C4 OLA A2405 20.483 -18.992 29.579 1.00 47.25 C
HETATM 3146 C5 OLA A2405 20.589 -17.667 28.830 1.00 44.62 C
HETATM 3147 C6 OLA A2405 19.620 -16.624 29.373 1.00 43.82 C
HETATM 3148 C7 OLA A2405 20.165 -15.220 29.143 1.00 45.82 C
HETATM 3149 C1 OLA A2406 4.755 11.923 3.749 1.00 63.51 C
HETATM 3150 O1 OLA A2406 4.136 12.984 3.517 1.00 75.99 O
HETATM 3151 O2 OLA A2406 5.889 11.987 4.272 1.00 62.93 O
HETATM 3152 C2 OLA A2406 4.134 10.588 3.411 1.00 55.64 C
HETATM 3153 C3 OLA A2406 4.783 9.994 2.166 1.00 57.84 C
HETATM 3154 C4 OLA A2406 5.194 8.547 2.415 1.00 49.46 C
HETATM 3155 C5 OLA A2406 5.009 7.712 1.153 1.00 47.38 C
HETATM 3156 C6 OLA A2406 4.834 6.234 1.488 1.00 41.79 C
HETATM 3157 C7 OLA A2406 3.976 5.530 0.441 1.00 43.36 C
HETATM 3158 C8 OLA A2406 3.661 4.099 0.863 1.00 56.28 C
HETATM 3159 C9 OLA A2406 4.870 3.223 0.637 1.00 38.25 C
HETATM 3160 C1 OLA A2407 2.582 14.153 13.550 1.00 51.90 C
HETATM 3161 O1 OLA A2407 3.197 15.226 13.740 1.00 51.48 O
HETATM 3162 O2 OLA A2407 1.421 14.198 13.090 1.00 65.16 O
HETATM 3163 C2 OLA A2407 3.233 12.826 13.865 1.00 47.18 C
HETATM 3164 C3 OLA A2407 3.102 11.892 12.668 1.00 50.46 C
HETATM 3165 C4 OLA A2407 2.976 10.436 13.103 1.00 45.30 C
HETATM 3166 C5 OLA A2407 3.185 9.508 11.912 1.00 39.27 C
HETATM 3167 C6 OLA A2407 2.324 8.257 12.016 1.00 42.90 C
HETATM 3168 C7 OLA A2407 3.147 6.998 11.774 1.00 39.86 C
HETATM 3169 C8 OLA A2407 2.286 5.920 11.128 1.00 43.88 C
HETATM 3170 C9 OLA A2407 3.123 4.697 10.844 1.00 40.34 C
HETATM 3171 C10 OLA A2407 2.531 3.555 10.132 1.00 47.17 C
HETATM 3172 C11 OLA A2407 1.033 3.372 10.151 1.00 50.03 C
HETATM 3173 C12 OLA A2407 0.682 1.907 9.925 1.00 51.53 C
HETATM 3174 C13 OLA A2407 -0.100 1.368 11.117 1.00 59.18 C
HETATM 3175 C14 OLA A2407 -0.164 -0.155 11.106 1.00 62.14 C
HETATM 3176 C15 OLA A2407 1.018 -0.783 11.834 1.00 57.74 C
HETATM 3177 C16 OLA A2407 1.059 -2.287 11.587 1.00 59.93 C
HETATM 3178 C17 OLA A2407 -0.330 -2.904 11.718 1.00 60.10 C
HETATM 3179 C18 OLA A2407 -0.316 -4.379 11.333 1.00 51.49 C
HETATM 3180 C1 OLA A2408 -2.671 15.257 13.565 1.00 75.98 C
HETATM 3181 O1 OLA A2408 -3.757 14.928 13.042 1.00 73.90 O
HETATM 3182 O2 OLA A2408 -2.399 16.472 13.686 1.00 80.19 O
HETATM 3183 C2 OLA A2408 -1.700 14.208 14.049 1.00 68.19 C
HETATM 3184 C3 OLA A2408 -1.716 13.011 13.105 1.00 57.27 C
HETATM 3185 C4 OLA A2408 -1.676 11.706 13.891 1.00 45.90 C
HETATM 3186 C5 OLA A2408 -1.351 10.532 12.975 1.00 51.95 C
HETATM 3187 C6 OLA A2408 -2.118 9.285 13.395 1.00 48.72 C
HETATM 3188 C7 OLA A2408 -1.313 8.012 13.157 1.00 47.36 C
HETATM 3189 C8 OLA A2408 -2.256 6.823 13.006 1.00 46.94 C
HETATM 3190 C9 OLA A2408 -1.490 5.557 12.708 1.00 45.47 C
HETATM 3191 C10 OLA A2408 -2.224 4.292 12.555 1.00 53.58 C
HETATM 3192 C11 OLA A2408 -3.636 4.189 13.082 1.00 43.15 C
HETATM 3193 C12 OLA A2408 -3.790 2.914 13.901 1.00 41.86 C
HETATM 3194 C13 OLA A2408 -3.824 1.658 13.041 1.00 49.22 C
HETATM 3195 C14 OLA A2408 -4.471 0.520 13.823 1.00 43.77 C
HETATM 3196 C15 OLA A2408 -4.010 -0.838 13.308 1.00 61.69 C
HETATM 3197 C16 OLA A2408 -4.596 -1.968 14.146 1.00 56.78 C
HETATM 3198 C17 OLA A2408 -3.882 -3.283 13.860 1.00 66.83 C
HETATM 3199 C1 OLA A2409 -0.791 10.718 9.026 1.00 64.39 C
HETATM 3200 O1 OLA A2409 -1.904 11.207 8.731 1.00 67.90 O
HETATM 3201 O2 OLA A2409 0.194 11.480 9.137 1.00 61.44 O
HETATM 3202 C2 OLA A2409 -0.639 9.232 9.262 1.00 56.05 C
HETATM 3203 C3 OLA A2409 -1.890 8.494 8.799 1.00 53.85 C
HETATM 3204 C4 OLA A2409 -1.547 7.331 7.876 1.00 59.54 C
HETATM 3205 C5 OLA A2409 -2.798 6.549 7.491 1.00 61.57 C
HETATM 3206 C6 OLA A2409 -2.451 5.115 7.101 1.00 60.30 C
HETATM 3207 C7 OLA A2409 -3.521 4.133 7.568 1.00 61.61 C
HETATM 3208 C8 OLA A2409 -2.948 2.729 7.726 1.00 65.28 C
HETATM 3209 C9 OLA A2409 -3.838 1.931 8.649 1.00 62.45 C
HETATM 3210 C10 OLA A2409 -3.345 0.703 9.291 1.00 59.55 C
HETATM 3211 C11 OLA A2409 -2.658 -0.366 8.475 1.00 66.39 C
HETATM 3212 C1 OLA A2410 35.438 -25.111 13.043 1.00 55.13 C
HETATM 3213 O1 OLA A2410 35.221 -25.100 11.813 1.00 57.12 O
HETATM 3214 O2 OLA A2410 35.523 -26.208 13.638 1.00 58.67 O
HETATM 3215 C2 OLA A2410 35.606 -23.818 13.803 1.00 52.56 C
HETATM 3216 C3 OLA A2410 34.840 -22.695 13.114 1.00 44.58 C
HETATM 3217 C4 OLA A2410 35.687 -21.428 13.056 1.00 53.19 C
HETATM 3218 C5 OLA A2410 36.298 -21.116 14.418 1.00 49.95 C
HETATM 3219 C1 OLA A2411 14.198 13.449 7.627 1.00 67.21 C
HETATM 3220 O1 OLA A2411 14.316 14.413 6.839 1.00 67.20 O
HETATM 3221 O2 OLA A2411 13.564 13.611 8.693 1.00 68.80 O
HETATM 3222 C2 OLA A2411 14.813 12.111 7.292 1.00 54.06 C
HETATM 3223 C3 OLA A2411 16.217 12.337 6.743 1.00 55.28 C
HETATM 3224 C4 OLA A2411 16.322 11.920 5.281 1.00 54.34 C
HETATM 3225 C5 OLA A2411 16.701 10.450 5.140 1.00 53.30 C
HETATM 3226 C6 OLA A2411 17.521 10.237 3.873 1.00 53.13 C
HETATM 3227 C7 OLA A2411 18.351 8.967 3.974 1.00 57.11 C
HETATM 3228 C8 OLA A2411 17.590 7.800 3.362 1.00 53.88 C
HETATM 3229 C9 OLA A2411 17.844 6.547 4.162 1.00 52.86 C
HETATM 3230 C10 OLA A2411 18.090 5.295 3.434 1.00 50.87 C
HETATM 3231 C11 OLA A2411 17.956 5.304 1.930 1.00 59.72 C
HETATM 3232 C12 OLA A2411 17.974 3.883 1.383 1.00 51.09 C
HETATM 3233 C13 OLA A2411 19.051 3.023 2.032 1.00 47.83 C
HETATM 3234 C14 OLA A2411 18.444 1.722 2.545 1.00 54.42 C
HETATM 3235 C15 OLA A2411 19.511 0.771 3.078 1.00 63.73 C
HETATM 3236 C16 OLA A2411 19.018 -0.673 3.056 1.00 50.34 C
HETATM 3237 C17 OLA A2411 20.023 -1.604 3.724 1.00 58.54 C
HETATM 3238 C1 OLA A2412 3.414 16.088 -4.627 1.00 68.24 C
HETATM 3239 O1 OLA A2412 3.829 15.155 -5.348 1.00 66.81 O
HETATM 3240 O2 OLA A2412 2.841 17.060 -5.167 1.00 69.44 O
HETATM 3241 C2 OLA A2412 3.592 16.041 -3.128 1.00 64.14 C
HETATM 3242 C3 OLA A2412 4.828 15.221 -2.776 1.00 63.45 C
HETATM 3243 C4 OLA A2412 5.912 16.089 -2.148 1.00 62.08 C
HETATM 3244 C5 OLA A2412 6.997 15.236 -1.501 1.00 52.61 C
HETATM 3245 C6 OLA A2412 8.163 14.991 -2.451 1.00 43.45 C
HETATM 3246 C7 OLA A2412 8.446 13.499 -2.578 1.00 35.49 C
HETATM 3247 C8 OLA A2412 9.862 13.257 -3.083 1.00 37.59 C
HETATM 3248 C9 OLA A2412 10.118 11.772 -3.165 1.00 34.65 C
HETATM 3249 C10 OLA A2412 11.465 11.285 -3.495 1.00 43.43 C
HETATM 3250 C1 OLA A2413 42.532 -22.216 23.283 1.00 87.98 C
HETATM 3251 O1 OLA A2413 42.986 -22.667 22.210 1.00 88.67 O
HETATM 3252 O2 OLA A2413 42.276 -23.011 24.214 1.00 95.13 O
HETATM 3253 C2 OLA A2413 42.294 -20.735 23.456 1.00 87.55 C
HETATM 3254 C3 OLA A2413 41.800 -20.138 22.144 1.00 80.29 C
HETATM 3255 C4 OLA A2413 42.257 -18.693 21.991 1.00 72.06 C
HETATM 3256 C5 OLA A2413 41.882 -17.871 23.219 1.00 78.42 C
HETATM 3257 C6 OLA A2413 41.295 -16.521 22.821 1.00 76.85 C
HETATM 3258 C7 OLA A2413 42.396 -15.479 22.667 1.00 77.33 C
HETATM 3259 C8 OLA A2413 41.914 -14.091 23.069 1.00 75.80 C
HETATM 3260 C9 OLA A2413 40.980 -13.549 22.014 1.00 78.15 C
HETATM 3261 C10 OLA A2413 40.982 -12.110 21.708 1.00 72.73 C
HETATM 3262 C11 OLA A2413 41.404 -11.112 22.759 1.00 65.40 C
HETATM 3263 C1 OLA A2414 28.586 -15.515 5.737 1.00 89.15 C
HETATM 3264 O1 OLA A2414 27.705 -14.993 5.020 1.00 94.89 O
HETATM 3265 O2 OLA A2414 29.395 -16.314 5.217 1.00 91.28 O
HETATM 3266 C2 OLA A2414 28.671 -15.191 7.211 1.00 70.24 C
HETATM 3267 C3 OLA A2414 29.346 -13.838 7.408 1.00 74.32 C
HETATM 3268 C4 OLA A2414 28.594 -12.983 8.422 1.00 63.24 C
HETATM 3269 C5 OLA A2414 29.208 -11.592 8.522 1.00 62.40 C
HETATM 3270 C6 OLA A2414 29.281 -11.140 9.974 1.00 56.40 C
HETATM 3271 C7 OLA A2414 30.581 -10.402 10.266 1.00 55.06 C
HETATM 3272 C8 OLA A2414 30.313 -9.160 11.107 1.00 55.68 C
HETATM 3273 C9 OLA A2414 31.506 -8.888 11.990 1.00 54.62 C
HETATM 3274 C10 OLA A2414 31.333 -8.161 13.255 1.00 57.19 C
HETATM 3275 C1 OLA A2415 28.651 -21.867 30.423 1.00 80.82 C
HETATM 3276 O1 OLA A2415 28.353 -23.078 30.517 1.00 84.50 O
HETATM 3277 O2 OLA A2415 29.628 -21.430 31.070 1.00 91.53 O
HETATM 3278 C2 OLA A2415 27.847 -20.949 29.534 1.00 58.47 C
HETATM 3279 C3 OLA A2415 27.781 -19.559 30.155 1.00 67.42 C
HETATM 3280 C4 OLA A2415 28.489 -18.524 29.288 1.00 63.05 C
HETATM 3281 C5 OLA A2415 28.261 -17.109 29.809 1.00 53.71 C
HETATM 3282 C6 OLA A2415 26.850 -16.932 30.360 1.00 50.81 C
HETATM 3283 C7 OLA A2415 26.531 -15.459 30.601 1.00 53.04 C
HETATM 3284 C8 OLA A2415 25.449 -15.310 31.664 1.00 50.44 C
HETATM 3285 C9 OLA A2415 24.113 -15.687 31.070 1.00 60.45 C
HETATM 3286 C10 OLA A2415 23.174 -16.503 31.852 1.00 63.09 C
HETATM 3287 C11 OLA A2415 23.692 -17.718 32.589 1.00 67.27 C
HETATM 3288 C12 OLA A2415 22.539 -18.470 33.243 1.00 66.26 C
HETATM 3289 C13 OLA A2415 21.559 -17.507 33.900 1.00 69.81 C
HETATM 3290 C14 OLA A2415 21.593 -17.635 35.417 1.00 70.23 C
HETATM 3291 C15 OLA A2415 22.511 -16.583 36.028 1.00 58.10 C
HETATM 3292 C16 OLA A2415 21.858 -15.206 36.010 1.00 58.67 C
HETATM 3293 C17 OLA A2415 20.993 -14.994 37.248 1.00 59.03 C
HETATM 3294 C18 OLA A2415 20.078 -13.785 37.083 1.00 60.55 C
HETATM 3295 C1 OLA A2416 23.403 13.668 1.279 1.00 59.29 C
HETATM 3296 O1 OLA A2416 22.156 13.596 1.259 1.00 66.16 O
HETATM 3297 O2 OLA A2416 23.943 14.791 1.386 1.00 60.39 O
HETATM 3298 C2 OLA A2416 24.237 12.413 1.174 1.00 49.61 C
HETATM 3299 C3 OLA A2416 23.669 11.546 0.058 1.00 60.10 C
HETATM 3300 C4 OLA A2416 22.852 10.382 0.607 1.00 52.24 C
HETATM 3301 C5 OLA A2416 23.710 9.132 0.759 1.00 54.75 C
HETATM 3302 C6 OLA A2416 23.137 7.988 -0.069 1.00 58.60 C
HETATM 3303 C7 OLA A2416 22.046 7.252 0.699 1.00 48.67 C
HETATM 3304 C1 OLA A2417 1.914 -17.556 13.655 1.00 62.88 C
HETATM 3305 O1 OLA A2417 1.618 -17.612 12.442 1.00 56.66 O
HETATM 3306 O2 OLA A2417 1.901 -18.608 14.333 1.00 58.41 O
HETATM 3307 C2 OLA A2417 2.286 -16.235 14.283 1.00 55.64 C
HETATM 3308 C3 OLA A2417 1.620 -15.115 13.498 1.00 52.43 C
HETATM 3309 C4 OLA A2417 0.543 -14.418 14.319 1.00 70.10 C
HETATM 3310 C5 OLA A2417 0.964 -12.994 14.664 1.00 51.61 C
HETATM 3311 C6 OLA A2417 0.876 -12.099 13.433 1.00 56.85 C
HETATM 3312 C7 OLA A2417 0.117 -10.814 13.737 1.00 62.65 C
HETATM 3313 C8 OLA A2417 0.989 -9.834 14.511 1.00 49.61 C
HETATM 3314 C9 OLA A2417 0.318 -8.482 14.533 1.00 61.65 C
HETATM 3315 C1 OLA A2418 -2.055 12.726 26.145 1.00 52.65 C
HETATM 3316 O1 OLA A2418 -3.282 12.893 25.971 1.00 65.25 O
HETATM 3317 O2 OLA A2418 -1.298 13.721 26.139 1.00 58.15 O
HETATM 3318 C2 OLA A2418 -1.491 11.343 26.362 1.00 49.40 C
HETATM 3319 C3 OLA A2418 -2.196 10.342 25.453 1.00 47.70 C
HETATM 3320 C4 OLA A2418 -2.307 8.983 26.136 1.00 36.81 C
HETATM 3321 C5 OLA A2418 -2.440 7.858 25.118 1.00 32.70 C
HETATM 3322 C6 OLA A2418 -2.715 6.528 25.809 1.00 35.76 C
HETATM 3323 C7 OLA A2418 -3.626 5.639 24.968 1.00 36.92 C
HETATM 3324 C8 OLA A2418 -3.052 4.236 24.792 1.00 35.00 C
HETATM 3325 C9 OLA A2418 -3.979 3.244 25.457 1.00 45.45 C
HETATM 3326 C10 OLA A2418 -3.665 1.807 25.484 1.00 50.68 C
HETATM 3327 C11 OLA A2418 -3.305 1.082 24.209 1.00 47.32 C
HETATM 3328 C12 OLA A2418 -2.950 -0.366 24.526 1.00 59.31 C
HETATM 3329 C13 OLA A2418 -4.195 -1.212 24.772 1.00 58.69 C
HETATM 3330 C14 OLA A2418 -4.068 -2.574 24.096 1.00 63.61 C
HETATM 3331 C1 OLA A2419 2.230 6.662 29.407 1.00 73.66 C
HETATM 3332 O1 OLA A2419 2.230 7.893 29.621 1.00 69.97 O
HETATM 3333 O2 OLA A2419 1.318 5.958 29.895 1.00 73.69 O
HETATM 3334 C2 OLA A2419 3.315 6.028 28.571 1.00 55.33 C
HETATM 3335 C3 OLA A2419 3.442 4.564 28.973 1.00 60.41 C
HETATM 3336 C4 OLA A2419 3.015 3.637 27.843 1.00 50.36 C
HETATM 3337 C5 OLA A2419 2.504 2.310 28.392 1.00 56.96 C
HETATM 3338 C6 OLA A2419 1.002 2.174 28.176 1.00 65.40 C
HETATM 3339 C7 OLA A2419 0.721 1.327 26.940 1.00 66.27 C
HETATM 3340 C8 OLA A2419 0.647 -0.158 27.271 1.00 67.33 C
HETATM 3341 C9 OLA A2419 -0.282 -0.377 28.442 1.00 73.35 C
HETATM 3342 C10 OLA A2419 -0.644 -1.749 28.819 1.00 75.46 C
HETATM 3343 C11 OLA A2419 -1.214 -2.675 27.771 1.00 74.70 C
HETATM 3344 C12 OLA A2419 -1.050 -4.123 28.213 1.00 77.80 C
HETATM 3345 C13 OLA A2419 -1.948 -5.043 27.394 1.00 89.43 C
HETATM 3346 C14 OLA A2419 -1.286 -5.444 26.081 1.00 90.22 C
HETATM 3347 C15 OLA A2419 -2.323 -5.940 25.078 1.00 78.44 C
HETATM 3348 C1 OLA A2420 3.979 12.802 8.931 1.00 70.48 C
HETATM 3349 O1 OLA A2420 4.717 13.643 8.373 1.00 68.72 O
HETATM 3350 O2 OLA A2420 3.033 13.210 9.640 1.00 69.62 O
HETATM 3351 C2 OLA A2420 4.229 11.322 8.752 1.00 62.80 C
HETATM 3352 C3 OLA A2420 3.412 10.784 7.583 1.00 60.52 C
HETATM 3353 C4 OLA A2420 3.355 9.261 7.604 1.00 53.02 C
HETATM 3354 C5 OLA A2420 2.545 8.747 6.421 1.00 53.56 C
HETATM 3355 C6 OLA A2420 1.888 7.415 6.751 1.00 54.68 C
HETATM 3356 C7 OLA A2420 2.165 6.379 5.670 1.00 58.18 C
HETATM 3357 C8 OLA A2420 1.290 5.153 5.898 1.00 62.31 C
HETATM 3358 C9 OLA A2420 1.348 4.235 4.701 1.00 66.55 C
HETATM 3359 C10 OLA A2420 0.571 2.987 4.702 1.00 71.57 C
HETATM 3360 C11 OLA A2420 0.411 2.198 5.980 1.00 72.47 C
HETATM 3361 C12 OLA A2420 -0.408 0.941 5.710 1.00 76.30 C
HETATM 3362 C1 OLA A2421 4.693 -21.569 17.904 1.00 70.69 C
HETATM 3363 O1 OLA A2421 5.281 -21.122 16.894 1.00 54.67 O
HETATM 3364 O2 OLA A2421 4.741 -22.797 18.139 1.00 73.04 O
HETATM 3365 C2 OLA A2421 3.932 -20.640 18.822 1.00 65.45 C
HETATM 3366 C3 OLA A2421 4.390 -19.199 18.621 1.00 61.21 C
HETATM 3367 C4 OLA A2421 3.410 -18.435 17.736 1.00 62.25 C
HETATM 3368 C5 OLA A2421 3.901 -17.025 17.419 1.00 64.94 C
HETATM 3369 C6 OLA A2421 4.376 -16.291 18.667 1.00 56.05 C
HETATM 3370 C7 OLA A2421 3.398 -15.196 19.083 1.00 68.86 C
HETATM 3371 C8 OLA A2421 3.153 -14.179 17.973 1.00 59.33 C
HETATM 3372 C9 OLA A2421 4.460 -13.520 17.601 1.00 43.47 C
HETATM 3373 C10 OLA A2421 4.613 -12.056 17.607 1.00 47.44 C
HETATM 3374 C11 OLA A2421 3.424 -11.132 17.731 1.00 56.52 C
HETATM 3375 C12 OLA A2421 3.899 -9.691 17.560 1.00 46.23 C
HETATM 3376 C13 OLA A2421 3.033 -8.725 18.361 1.00 52.49 C
HETATM 3377 C14 OLA A2421 2.922 -7.372 17.668 1.00 35.08 C
HETATM 3378 C1 OLA A2422 31.336 13.513 7.242 1.00 65.12 C
HETATM 3379 O1 OLA A2422 31.277 14.742 7.019 1.00 73.52 O
HETATM 3380 O2 OLA A2422 31.664 13.120 8.382 1.00 61.49 O
HETATM 3381 C2 OLA A2422 31.009 12.524 6.148 1.00 65.14 C
HETATM 3382 C3 OLA A2422 31.746 11.209 6.384 1.00 62.85 C
HETATM 3383 C4 OLA A2422 30.770 10.044 6.494 1.00 59.82 C
HETATM 3384 C5 OLA A2422 31.509 8.711 6.512 1.00 48.67 C
HETATM 3385 C6 OLA A2422 30.559 7.558 6.207 1.00 53.56 C
HETATM 3386 C7 OLA A2422 31.288 6.415 5.513 1.00 55.62 C
HETATM 3387 C8 OLA A2422 30.327 5.332 5.031 1.00 55.94 C
HETATM 3388 C9 OLA A2422 29.159 5.941 4.291 1.00 58.62 C
HETATM 3389 C10 OLA A2422 28.165 5.070 3.640 1.00 53.47 C
HETATM 3390 C11 OLA A2422 28.620 3.835 2.896 1.00 56.53 C
HETATM 3391 C12 OLA A2422 27.436 3.163 2.208 1.00 49.34 C
HETATM 3392 C1 OLA A2423 8.663 -0.541 33.005 1.00 60.25 C
HETATM 3393 O1 OLA A2423 7.490 -0.146 33.175 1.00 70.79 O
HETATM 3394 O2 OLA A2423 9.604 0.248 33.242 1.00 53.56 O
HETATM 3395 C2 OLA A2423 8.938 -1.946 32.522 1.00 48.85 C
HETATM 3396 C3 OLA A2423 8.943 -2.901 33.709 1.00 47.94 C
HETATM 3397 C4 OLA A2423 7.710 -3.797 33.706 1.00 57.47 C
HETATM 3398 C5 OLA A2423 7.857 -4.945 32.713 1.00 50.31 C
HETATM 3399 C6 OLA A2423 6.527 -5.660 32.506 1.00 60.52 C
HETATM 3400 C7 OLA A2423 6.297 -5.992 31.037 1.00 55.11 C
HETATM 3401 C8 OLA A2423 6.488 -7.477 30.745 1.00 49.30 C
HETATM 3402 C9 OLA A2423 5.402 -7.914 29.789 1.00 62.21 C
HETATM 3403 C10 OLA A2423 5.195 -9.333 29.457 1.00 57.30 C
HETATM 3404 C11 OLA A2423 6.054 -10.016 28.420 1.00 56.00 C
HETATM 3405 C12 OLA A2423 5.607 -11.468 28.276 1.00 65.13 C
HETATM 3406 C13 OLA A2423 6.069 -12.066 26.952 1.00 52.63 C
HETATM 3407 C14 OLA A2423 5.355 -13.383 26.665 1.00 59.13 C
HETATM 3408 C15 OLA A2423 6.234 -14.568 27.046 1.00 53.95 C
HETATM 3409 C16 OLA A2423 5.613 -15.891 26.611 1.00 54.98 C
HETATM 3410 C17 OLA A2423 6.296 -17.058 27.313 1.00 54.10 C
HETATM 3411 C18 OLA A2423 5.799 -18.398 26.783 1.00 58.61 C
HETATM 3412 C1 OLA A2424 4.814 6.058 32.901 1.00 73.94 C
HETATM 3413 O1 OLA A2424 5.104 7.275 32.895 1.00 73.63 O
HETATM 3414 O2 OLA A2424 3.623 5.721 33.072 1.00 76.31 O
HETATM 3415 C2 OLA A2424 5.890 5.014 32.707 1.00 63.11 C
HETATM 3416 C3 OLA A2424 5.407 3.648 33.182 1.00 71.31 C
HETATM 3417 C4 OLA A2424 5.988 2.536 32.316 1.00 67.45 C
HETATM 3418 C5 OLA A2424 5.008 2.080 31.241 1.00 67.79 C
HETATM 3419 C6 OLA A2424 5.401 0.719 30.672 1.00 60.83 C
HETATM 3420 C7 OLA A2424 4.189 -0.200 30.579 1.00 64.17 C
HETATM 3421 C8 OLA A2424 4.566 -1.615 30.154 1.00 60.49 C
HETATM 3422 C9 OLA A2424 4.012 -1.865 28.772 1.00 63.02 C
HETATM 3423 C10 OLA A2424 3.340 -3.133 28.444 1.00 71.31 C
HETATM 3424 C11 OLA A2424 3.952 -4.458 28.834 1.00 65.59 C
HETATM 3425 C12 OLA A2424 3.013 -5.591 28.438 1.00 63.30 C
HETATM 3426 C1 OLA A2425 37.914 -20.398 25.844 1.00 87.40 C
HETATM 3427 O1 OLA A2425 38.383 -20.683 24.721 1.00 84.48 O
HETATM 3428 O2 OLA A2425 38.253 -21.084 26.833 1.00 74.68 O
HETATM 3429 C2 OLA A2425 36.952 -19.245 26.003 1.00 84.26 C
HETATM 3430 C3 OLA A2425 37.006 -18.364 24.760 1.00 73.86 C
HETATM 3431 C4 OLA A2425 36.962 -16.883 25.123 1.00 70.09 C
HETATM 3432 C5 OLA A2425 36.781 -16.035 23.870 1.00 66.23 C
HETATM 3433 C6 OLA A2425 37.220 -14.591 24.087 1.00 75.85 C
HETATM 3434 C7 OLA A2425 36.030 -13.639 24.016 1.00 62.02 C
HETATM 3435 C8 OLA A2425 35.634 -13.112 25.392 1.00 59.15 C
HETATM 3436 C9 OLA A2425 34.895 -14.175 26.171 1.00 63.06 C
HETATM 3437 C10 OLA A2425 34.026 -13.797 27.296 1.00 59.82 C
HETATM 3438 C1 OLA A2426 18.379 -13.272 -1.690 1.00 75.66 C
HETATM 3439 O1 OLA A2426 18.878 -12.921 -2.781 1.00 78.05 O
HETATM 3440 O2 OLA A2426 17.484 -14.144 -1.687 1.00 74.03 O
HETATM 3441 C2 OLA A2426 18.848 -12.651 -0.395 1.00 75.76 C
HETATM 3442 C3 OLA A2426 18.733 -11.133 -0.471 1.00 72.22 C
HETATM 3443 C4 OLA A2426 17.844 -10.611 0.653 1.00 65.04 C
HETATM 3444 C5 OLA A2426 18.478 -10.888 2.012 1.00 65.17 C
HETATM 3445 C6 OLA A2426 18.562 -9.627 2.865 1.00 55.76 C
HETATM 3446 C7 OLA A2426 17.211 -8.925 2.915 1.00 56.97 C
HETATM 3447 C8 OLA A2426 17.312 -7.495 3.432 1.00 50.48 C
HETATM 3448 C9 OLA A2426 17.416 -6.553 2.257 1.00 57.07 C
HETATM 3449 C10 OLA A2426 16.951 -5.163 2.377 1.00 52.78 C
HETATM 3450 C11 OLA A2426 15.553 -4.879 2.870 1.00 41.14 C
HETATM 3451 C12 OLA A2426 15.162 -3.465 2.459 1.00 37.45 C
HETATM 3452 C1 OLA A2427 30.850 -15.260 12.619 1.00 74.05 C
HETATM 3453 O1 OLA A2427 30.983 -14.356 11.766 1.00 82.70 O
HETATM 3454 O2 OLA A2427 30.314 -16.339 12.284 1.00 61.99 O
HETATM 3455 C2 OLA A2427 31.338 -15.056 14.034 1.00 68.23 C
HETATM 3456 C3 OLA A2427 31.615 -13.576 14.274 1.00 68.80 C
HETATM 3457 C4 OLA A2427 30.411 -12.889 14.905 1.00 65.80 C
HETATM 3458 C5 OLA A2427 30.014 -13.552 16.219 1.00 49.89 C
HETATM 3459 C6 OLA A2427 30.313 -12.673 17.431 1.00 58.86 C
HETATM 3460 C7 OLA A2427 30.243 -11.182 17.106 1.00 53.96 C
HETATM 3461 C8 OLA A2427 30.816 -10.344 18.245 1.00 49.03 C
HETATM 3462 C9 OLA A2427 31.046 -8.925 17.779 1.00 55.77 C
HETATM 3463 C1 OLA A2428 21.843 -12.751 3.541 1.00 75.45 C
HETATM 3464 O1 OLA A2428 20.978 -13.467 2.989 1.00 68.37 O
HETATM 3465 O2 OLA A2428 22.724 -13.295 4.243 1.00 79.88 O
HETATM 3466 C2 OLA A2428 21.829 -11.252 3.365 1.00 68.01 C
HETATM 3467 C3 OLA A2428 22.747 -10.600 4.393 1.00 61.06 C
HETATM 3468 C4 OLA A2428 22.810 -9.095 4.165 1.00 58.10 C
HETATM 3469 C5 OLA A2428 23.804 -8.416 5.101 1.00 60.95 C
HETATM 3470 C6 OLA A2428 23.301 -7.050 5.565 1.00 61.81 C
HETATM 3471 C7 OLA A2428 21.781 -7.017 5.705 1.00 56.21 C
HETATM 3472 C8 OLA A2428 21.212 -5.653 5.332 1.00 50.96 C
HETATM 3473 C9 OLA A2428 21.760 -5.215 3.994 1.00 53.08 C
HETATM 3474 C1 OLA A2429 32.250 7.477 33.551 1.00 52.84 C
HETATM 3475 O1 OLA A2429 31.300 7.986 32.919 1.00 56.97 O
HETATM 3476 O2 OLA A2429 33.251 8.183 33.794 1.00 65.58 O
HETATM 3477 C2 OLA A2429 32.194 6.041 34.018 1.00 47.02 C
HETATM 3478 C3 OLA A2429 31.895 5.100 32.858 1.00 47.09 C
HETATM 3479 C4 OLA A2429 32.195 3.654 33.234 1.00 48.46 C
HETATM 3480 C5 OLA A2429 32.188 2.762 31.999 1.00 50.54 C
HETATM 3481 C6 OLA A2429 31.662 1.364 32.310 1.00 51.28 C
HETATM 3482 C7 OLA A2429 30.864 0.811 31.133 1.00 38.58 C
HETATM 3483 C8 OLA A2429 29.986 -0.364 31.554 1.00 43.39 C
HETATM 3484 C9 OLA A2429 30.764 -1.653 31.422 1.00 51.56 C
HETATM 3485 C10 OLA A2429 30.082 -2.953 31.310 1.00 52.10 C
HETATM 3486 C11 OLA A2429 29.197 -3.490 32.414 1.00 53.46 C
HETATM 3487 C12 OLA A2429 28.974 -4.983 32.180 1.00 50.48 C
HETATM 3488 C13 OLA A2429 28.100 -5.617 33.258 1.00 46.85 C
HETATM 3489 C14 OLA A2429 26.998 -6.474 32.644 1.00 36.29 C
HETATM 3490 C1 OLA A2430 35.414 10.114 30.087 1.00 69.36 C
HETATM 3491 O1 OLA A2430 34.315 10.379 29.554 1.00 66.31 O
HETATM 3492 O2 OLA A2430 35.941 10.965 30.836 1.00 74.72 O
HETATM 3493 C2 OLA A2430 36.093 8.788 29.831 1.00 53.00 C
HETATM 3494 C3 OLA A2430 35.526 7.727 30.766 1.00 52.24 C
HETATM 3495 C4 OLA A2430 36.193 6.375 30.537 1.00 54.03 C
HETATM 3496 C5 OLA A2430 35.343 5.495 29.627 1.00 49.86 C
HETATM 3497 C6 OLA A2430 35.430 4.028 30.037 1.00 54.86 C
HETATM 3498 C7 OLA A2430 36.226 3.222 29.016 1.00 60.90 C
HETATM 3499 C8 OLA A2430 36.008 1.718 29.161 1.00 63.34 C
HETATM 3500 C9 OLA A2430 34.547 1.416 29.396 1.00 52.22 C
HETATM 3501 C10 OLA A2430 34.057 0.027 29.432 1.00 57.54 C
HETATM 3502 C11 OLA A2430 34.209 -0.879 28.229 1.00 59.78 C
HETATM 3503 C12 OLA A2430 33.493 -2.204 28.480 1.00 52.64 C
HETATM 3504 C13 OLA A2430 33.408 -3.044 27.210 1.00 49.40 C
HETATM 3505 C18 OLC A2431 15.364 -2.101 35.792 1.00 54.35 C
HETATM 3506 C10 OLC A2431 16.359 -9.201 39.650 1.00 52.42 C
HETATM 3507 C9 OLC A2431 15.127 -9.476 39.200 1.00 51.44 C
HETATM 3508 C17 OLC A2431 16.410 -2.553 34.768 1.00 45.63 C
HETATM 3509 C11 OLC A2431 16.943 -7.816 39.694 1.00 39.78 C
HETATM 3510 C8 OLC A2431 14.542 -10.862 39.153 1.00 54.80 C
HETATM 3511 C24 OLC A2431 8.629 -18.669 37.391 1.00 80.68 C
HETATM 3512 C16 OLC A2431 17.452 -3.500 35.379 1.00 47.28 C
HETATM 3513 C12 OLC A2431 16.579 -6.911 38.490 1.00 49.29 C
HETATM 3514 C7 OLC A2431 13.975 -11.290 37.778 1.00 59.68 C
HETATM 3515 C15 OLC A2431 16.788 -4.573 36.248 1.00 42.48 C
HETATM 3516 C13 OLC A2431 17.827 -6.304 37.818 1.00 49.67 C
HETATM 3517 C6 OLC A2431 12.532 -10.784 37.551 1.00 54.08 C
HETATM 3518 C14 OLC A2431 17.623 -5.855 36.359 1.00 44.45 C
HETATM 3519 C5 OLC A2431 11.838 -11.363 36.296 1.00 49.31 C
HETATM 3520 C4 OLC A2431 10.908 -12.560 36.607 1.00 44.28 C
HETATM 3521 C3 OLC A2431 9.438 -12.293 36.245 1.00 45.11 C
HETATM 3522 C2 OLC A2431 8.474 -13.317 36.881 1.00 67.06 C
HETATM 3523 C21 OLC A2431 8.193 -16.820 35.728 1.00 77.51 C
HETATM 3524 C1 OLC A2431 8.160 -14.451 35.938 1.00 77.23 C
HETATM 3525 C22 OLC A2431 9.136 -18.010 36.066 1.00 74.38 C
HETATM 3526 O19 OLC A2431 7.434 -14.409 34.960 1.00 72.75 O
HETATM 3527 O25 OLC A2431 8.228 -17.616 38.216 1.00 80.72 O
HETATM 3528 O23 OLC A2431 8.977 -18.909 35.010 1.00 72.11 O
HETATM 3529 O20 OLC A2431 8.777 -15.634 36.261 1.00 85.89 O
HETATM 3530 C10 OLC A2432 4.247 -6.847 22.373 1.00 65.53 C
HETATM 3531 C9 OLC A2432 5.380 -7.247 22.971 1.00 58.00 C
HETATM 3532 C11 OLC A2432 3.369 -5.739 22.903 1.00 64.90 C
HETATM 3533 C8 OLC A2432 6.274 -8.348 22.460 1.00 56.69 C
HETATM 3534 C24 OLC A2432 7.586 -21.677 23.654 1.00 76.11 C
HETATM 3535 C12 OLC A2432 1.842 -5.993 22.854 1.00 68.85 C
HETATM 3536 C7 OLC A2432 5.587 -9.686 22.094 1.00 60.53 C
HETATM 3537 C13 OLC A2432 1.470 -7.328 22.175 1.00 64.26 C
HETATM 3538 C6 OLC A2432 5.868 -10.808 23.125 1.00 58.29 C
HETATM 3539 C14 OLC A2432 0.811 -7.158 20.790 1.00 50.98 C
HETATM 3540 C5 OLC A2432 5.636 -12.242 22.589 1.00 58.63 C
HETATM 3541 C4 OLC A2432 6.622 -13.289 23.170 1.00 51.07 C
HETATM 3542 C3 OLC A2432 6.744 -14.560 22.305 1.00 49.26 C
HETATM 3543 C2 OLC A2432 7.425 -15.726 23.057 1.00 53.90 C
HETATM 3544 C21 OLC A2432 7.028 -19.298 23.053 1.00 60.99 C
HETATM 3545 C1 OLC A2432 7.218 -17.035 22.341 1.00 54.76 C
HETATM 3546 C22 OLC A2432 7.934 -20.510 22.685 1.00 60.90 C
HETATM 3547 O19 OLC A2432 6.595 -17.209 21.307 1.00 72.31 O
HETATM 3548 O25 OLC A2432 6.573 -22.395 23.014 1.00 86.82 O
HETATM 3549 O23 OLC A2432 7.550 -20.872 21.393 1.00 66.77 O
HETATM 3550 O20 OLC A2432 7.812 -18.114 22.950 1.00 52.37 O
HETATM 3551 C10 OLC A2433 1.194 2.168 15.508 1.00 45.09 C
HETATM 3552 C9 OLC A2433 1.269 3.494 15.317 1.00 37.23 C
HETATM 3553 C11 OLC A2433 0.158 1.280 14.871 1.00 47.92 C
HETATM 3554 C8 OLC A2433 2.312 4.369 15.962 1.00 32.33 C
HETATM 3555 C24 OLC A2433 -0.937 17.396 17.025 1.00 75.59 C
HETATM 3556 C12 OLC A2433 -0.271 0.049 15.703 1.00 46.72 C
HETATM 3557 C7 OLC A2433 1.777 5.447 16.930 1.00 37.51 C
HETATM 3558 C6 OLC A2433 1.786 6.854 16.297 1.00 35.18 C
HETATM 3559 C5 OLC A2433 1.779 8.015 17.310 1.00 35.09 C
HETATM 3560 C4 OLC A2433 0.861 9.176 16.868 1.00 47.32 C
HETATM 3561 C3 OLC A2433 1.321 10.550 17.378 1.00 45.36 C
HETATM 3562 C2 OLC A2433 0.505 11.693 16.751 1.00 54.87 C
HETATM 3563 C21 OLC A2433 -0.046 15.186 17.851 1.00 56.83 C
HETATM 3564 C1 OLC A2433 0.342 12.842 17.705 1.00 52.52 C
HETATM 3565 C22 OLC A2433 0.332 16.483 17.071 1.00 75.41 C
HETATM 3566 O19 OLC A2433 0.158 12.774 18.908 1.00 57.67 O
HETATM 3567 O25 OLC A2433 -1.188 17.643 15.673 1.00 69.49 O
HETATM 3568 O23 OLC A2433 1.322 17.107 17.837 1.00 62.82 O
HETATM 3569 O20 OLC A2433 0.410 14.070 17.097 1.00 52.52 O
HETATM 3570 C1 PEG A2434 12.563 -27.969 37.718 1.00 78.00 C
HETATM 3571 O1 PEG A2434 11.484 -28.182 36.801 1.00 82.58 O
HETATM 3572 C2 PEG A2434 12.245 -26.772 38.607 1.00 77.89 C
HETATM 3573 O2 PEG A2434 13.389 -25.925 38.691 1.00 74.29 O
HETATM 3574 C3 PEG A2434 13.774 -25.428 37.411 1.00 72.35 C
HETATM 3575 C4 PEG A2434 15.107 -24.699 37.529 1.00 71.57 C
HETATM 3576 O4 PEG A2434 16.144 -25.504 36.958 1.00 67.85 O
HETATM 3577 C1 PEG A2435 10.648 -23.981 35.783 1.00 75.59 C
HETATM 3578 O1 PEG A2435 10.313 -25.223 35.154 1.00 74.50 O
HETATM 3579 C2 PEG A2435 9.915 -22.843 35.082 1.00 70.36 C
HETATM 3580 O2 PEG A2435 10.700 -21.654 35.156 1.00 72.71 O
HETATM 3581 C3 PEG A2435 11.911 -21.772 34.414 1.00 57.91 C
HETATM 3582 C4 PEG A2435 12.981 -20.888 35.044 1.00 63.52 C
HETATM 3583 O4 PEG A2435 14.246 -21.558 34.991 1.00 67.44 O
HETATM 3584 O HOH A2501 28.960 -45.672 8.071 1.00 74.62 O
HETATM 3585 O HOH A2502 39.150 -61.118 11.608 1.00 79.02 O
HETATM 3586 O HOH A2503 25.587 -14.425 4.208 1.00 71.45 O
HETATM 3587 O HOH A2504 40.489 -50.507 21.602 1.00 75.46 O
HETATM 3588 O HOH A2505 25.866 -58.287 23.124 1.00 69.59 O
HETATM 3589 O HOH A2506 36.681 -64.976 20.894 1.00 60.22 O
HETATM 3590 O HOH A2507 30.963 -42.126 23.459 1.00 71.13 O
HETATM 3591 O HOH A2508 37.833 -42.478 24.457 1.00 59.53 O
HETATM 3592 O HOH A2509 34.506 -25.233 27.934 1.00 68.83 O
HETATM 3593 O HOH A2510 1.303 28.232 28.939 1.00 90.42 O
HETATM 3594 O HOH A2511 23.157 -17.566 19.110 1.00 30.10 O
HETATM 3595 O HOH A2512 42.784 -38.297 22.269 1.00 71.23 O
HETATM 3596 O HOH A2513 15.535 -11.150 11.162 1.00 26.32 O
HETATM 3597 O HOH A2514 14.220 -16.208 14.345 1.00 26.79 O
HETATM 3598 O HOH A2515 13.170 7.316 13.232 1.00 32.29 O
HETATM 3599 O HOH A2516 9.806 -29.725 37.809 1.00 72.91 O
HETATM 3600 O HOH A2517 19.275 -36.420 29.304 1.00 49.98 O
HETATM 3601 O HOH A2518 32.001 10.296 30.493 1.00 59.27 O
HETATM 3602 O HOH A2519 35.757 -63.605 12.043 1.00 80.24 O
HETATM 3603 O HOH A2520 13.979 -13.426 13.453 1.00 27.72 O
HETATM 3604 O HOH A2521 47.977 -72.877 22.278 1.00 52.54 O
HETATM 3605 O HOH A2522 29.712 17.941 17.728 1.00 49.79 O
HETATM 3606 O HOH A2523 10.515 9.041 34.841 1.00 39.09 O
HETATM 3607 O HOH A2524 13.978 -14.886 24.719 1.00 33.50 O
HETATM 3608 O HOH A2525 -4.305 11.939 8.088 1.00 60.01 O
HETATM 3609 O HOH A2526 24.659 9.910 17.700 1.00 25.95 O
HETATM 3610 O HOH A2527 15.659 14.661 33.422 1.00 52.49 O
HETATM 3611 O HOH A2528 20.823 10.038 22.994 1.00 28.68 O
HETATM 3612 O HOH A2529 11.773 2.416 16.887 1.00 24.78 O
HETATM 3613 O HOH A2530 14.076 2.458 15.589 1.00 31.53 O
HETATM 3614 O HOH A2531 16.762 -28.551 21.460 1.00 40.33 O
HETATM 3615 O HOH A2532 22.665 -25.330 9.537 1.00 41.12 O
HETATM 3616 O HOH A2533 2.971 10.394 29.305 1.00 59.02 O
HETATM 3617 O HOH A2534 28.644 14.886 23.391 1.00 43.78 O
HETATM 3618 O HOH A2535 19.939 -35.907 26.231 1.00 46.53 O
HETATM 3619 O HOH A2536 16.560 13.904 15.291 1.00 33.64 O
HETATM 3620 O HOH A2537 21.882 -17.713 16.652 1.00 29.87 O
HETATM 3621 O HOH A2538 -4.615 17.530 12.711 1.00 60.14 O
HETATM 3622 O HOH A2539 11.251 -30.996 21.559 1.00 56.03 O
HETATM 3623 O HOH A2540 39.071 -63.240 19.662 1.00 58.48 O
HETATM 3624 O HOH A2541 14.773 16.617 2.128 1.00 36.20 O
HETATM 3625 O HOH A2542 18.810 -25.202 37.137 1.00 71.92 O
HETATM 3626 O HOH A2543 16.749 -31.923 35.429 1.00 50.51 O
HETATM 3627 O HOH A2544 26.478 15.005 0.509 1.00 63.44 O
HETATM 3628 O HOH A2545 37.514 12.915 22.093 1.00 37.37 O
HETATM 3629 O HOH A2546 15.931 -4.948 13.895 1.00 21.46 O
HETATM 3630 O HOH A2547 15.607 15.728 4.856 1.00 66.90 O
HETATM 3631 O HOH A2548 0.689 25.307 19.561 1.00 70.94 O
HETATM 3632 O HOH A2549 16.279 23.325 29.832 1.00 47.45 O
HETATM 3633 O HOH A2550 20.261 -1.882 21.689 1.00 24.86 O
HETATM 3634 O HOH A2551 7.263 29.342 15.433 1.00 76.11 O
HETATM 3635 O HOH A2552 20.688 -11.530 12.860 1.00 23.46 O
HETATM 3636 O HOH A2553 29.764 14.508 25.417 1.00 42.86 O
HETATM 3637 O HOH A2554 23.275 0.545 12.468 1.00 21.46 O
HETATM 3638 O HOH A2555 33.956 -31.750 24.704 1.00 48.50 O
HETATM 3639 O HOH A2556 3.829 19.005 17.037 1.00 49.99 O
HETATM 3640 O HOH A2557 10.766 2.261 19.603 1.00 24.90 O
HETATM 3641 O HOH A2558 30.360 14.955 9.975 1.00 49.23 O
HETATM 3642 O HOH A2559 38.644 -48.056 20.300 1.00 75.41 O
HETATM 3643 O HOH A2560 13.395 -12.412 21.423 1.00 23.71 O
HETATM 3644 O HOH A2561 46.228 -57.258 31.061 1.00 70.98 O
HETATM 3645 O HOH A2562 28.622 8.634 32.696 1.00 46.74 O
HETATM 3646 O HOH A2563 21.612 -3.221 19.823 1.00 28.20 O
HETATM 3647 O HOH A2564 25.232 -26.968 17.208 1.00 30.72 O
HETATM 3648 O HOH A2565 16.942 25.736 5.293 1.00 78.34 O
HETATM 3649 O HOH A2566 13.203 -12.578 25.717 1.00 31.15 O
HETATM 3650 O HOH A2567 11.323 -30.189 0.235 1.00 62.36 O
HETATM 3651 O HOH A2568 14.843 -31.194 25.166 1.00 50.42 O
HETATM 3652 O HOH A2569 13.932 11.687 16.608 1.00 31.68 O
HETATM 3653 O HOH A2570 29.817 14.775 19.104 1.00 47.00 O
HETATM 3654 O HOH A2571 39.487 -32.321 15.102 1.00 50.28 O
HETATM 3655 O HOH A2572 11.530 -28.907 34.096 1.00 49.54 O
HETATM 3656 O HOH A2573 13.963 4.962 18.678 1.00 24.59 O
HETATM 3657 O HOH A2574 29.861 19.616 20.989 1.00 59.71 O
HETATM 3658 O HOH A2575 24.275 3.083 21.695 1.00 26.14 O
HETATM 3659 O HOH A2576 16.570 19.595 16.177 1.00 57.72 O
HETATM 3660 O HOH A2577 14.103 -33.449 33.255 1.00 58.97 O
HETATM 3661 O HOH A2578 0.235 -24.100 -5.862 1.00 74.43 O
HETATM 3662 O HOH A2579 23.553 16.709 8.835 1.00 37.98 O
HETATM 3663 O HOH A2580 13.267 18.372 22.269 1.00 31.26 O
HETATM 3664 O HOH A2581 18.607 -3.121 23.995 1.00 27.57 O
HETATM 3665 O HOH A2582 4.491 9.982 33.538 1.00 64.18 O
HETATM 3666 O HOH A2583 18.507 16.000 18.661 1.00 32.71 O
HETATM 3667 O HOH A2584 22.980 -28.386 16.751 1.00 35.83 O
HETATM 3668 O HOH A2585 28.857 -34.598 21.745 1.00 43.64 O
HETATM 3669 O HOH A2586 26.686 -33.848 21.149 1.00 47.35 O
HETATM 3670 O HOH A2587 25.834 -28.258 19.539 1.00 36.67 O
HETATM 3671 O HOH A2588 26.954 17.793 11.202 1.00 48.66 O
HETATM 3672 O HOH A2589 28.622 11.911 15.606 1.00 29.64 O
HETATM 3673 O HOH A2590 40.314 -28.644 20.721 1.00 55.14 O
HETATM 3674 O HOH A2591 21.730 12.577 23.534 1.00 30.28 O
HETATM 3675 O HOH A2592 8.518 -29.402 28.714 1.00 53.76 O
HETATM 3676 O HOH A2593 23.997 -33.355 15.319 1.00 46.87 O
HETATM 3677 O HOH A2594 16.797 -5.584 16.060 1.00 35.01 O
HETATM 3678 O HOH A2595 16.087 3.357 17.251 1.00 31.93 O
HETATM 3679 O HOH A2596 14.049 9.708 14.187 1.00 39.50 O
HETATM 3680 O HOH A2597 27.907 14.369 4.446 1.00 52.04 O
HETATM 3681 O HOH A2598 16.519 1.476 15.418 1.00 33.95 O
HETATM 3682 O HOH A2599 13.369 18.898 24.783 1.00 35.36 O
HETATM 3683 O HOH A2600 34.792 -61.149 28.258 1.00 61.89 O
HETATM 3684 O HOH A2601 17.339 -25.308 14.804 1.00 58.88 O
HETATM 3685 O HOH A2602 17.880 -29.055 9.098 1.00 39.02 O
HETATM 3686 O HOH A2603 12.094 -11.602 6.779 1.00 34.73 O
HETATM 3687 O HOH A2604 14.485 -30.064 22.387 1.00 40.61 O
HETATM 3688 O HOH A2605 36.741 -63.812 28.177 1.00 58.61 O
HETATM 3689 O HOH A2606 34.943 -38.171 21.300 1.00 47.31 O
HETATM 3690 O HOH A2607 10.862 -30.712 26.279 1.00 54.37 O
HETATM 3691 O HOH A2608 11.627 5.009 17.767 1.00 25.99 O
HETATM 3692 O HOH A2609 35.120 -64.427 18.047 1.00 56.58 O
HETATM 3693 O HOH A2610 13.971 16.869 26.544 1.00 41.02 O
HETATM 3694 O HOH A2611 22.278 13.177 26.083 1.00 29.73 O
HETATM 3695 O HOH A2612 4.421 -32.312 12.337 1.00 49.62 O
HETATM 3696 O HOH A2613 -4.598 15.179 10.189 1.00 76.80 O
HETATM 3697 O HOH A2614 18.710 -11.128 15.181 1.00 32.89 O
HETATM 3698 O HOH A2615 27.164 -44.686 24.331 1.00 70.58 O
HETATM 3699 O HOH A2616 3.023 -31.181 17.489 1.00 43.53 O
HETATM 3700 O HOH A2617 36.430 -40.743 22.247 1.00 49.13 O
HETATM 3701 O HOH A2618 17.345 13.586 17.857 1.00 25.45 O
HETATM 3702 O HOH A2619 8.663 -33.052 18.388 1.00 53.96 O
HETATM 3703 O HOH A2620 17.530 29.551 5.420 1.00 76.74 O
HETATM 3704 O HOH A2621 31.006 -24.154 31.426 1.00 83.74 O
HETATM 3705 O HOH A2622 21.110 16.091 18.651 1.00 44.89 O
HETATM 3706 O HOH A2623 27.023 -36.410 28.018 1.00 47.31 O
HETATM 3707 O HOH A2624 42.695 -68.408 18.521 1.00 68.39 O
HETATM 3708 O HOH A2625 21.365 -24.456 12.886 1.00 47.58 O
HETATM 3709 O HOH A2626 19.802 12.222 32.524 1.00 42.19 O
HETATM 3710 O HOH A2627 13.229 21.521 12.323 1.00 73.75 O
HETATM 3711 O HOH A2628 24.416 12.000 28.318 1.00 27.98 O
HETATM 3712 O HOH A2629 6.499 -24.867 19.593 1.00 68.84 O
HETATM 3713 O HOH A2630 22.409 13.332 29.366 1.00 34.57 O
HETATM 3714 O HOH A2631 30.778 13.518 16.711 1.00 43.92 O
HETATM 3715 O HOH A2632 36.515 -35.025 24.910 1.00 64.59 O
HETATM 3716 O HOH A2633 18.413 12.087 34.795 1.00 48.18 O
HETATM 3717 O HOH A2634 36.410 15.716 21.558 1.00 45.05 O
HETATM 3718 O HOH A2635 55.344 -55.792 18.823 1.00 58.44 O
HETATM 3719 O HOH A2636 11.699 11.182 34.849 1.00 44.45 O
HETATM 3720 O HOH A2637 41.403 -34.453 24.199 1.00 69.30 O
HETATM 3721 O HOH A2638 7.513 15.033 8.233 1.00 63.52 O
HETATM 3722 O HOH A2639 6.113 11.502 34.388 1.00 70.78 O
HETATM 3723 O HOH A2640 28.359 16.081 20.347 1.00 61.45 O
HETATM 3724 O HOH A2641 8.656 19.879 4.014 1.00 38.37 O
HETATM 3725 O HOH A2642 7.229 -22.146 32.265 1.00 54.50 O
HETATM 3726 O HOH A2643 46.527 -39.648 10.800 1.00 61.72 O
HETATM 3727 O HOH A2644 23.044 -29.491 10.752 1.00 51.45 O
HETATM 3728 O HOH A2645 14.186 12.997 35.102 1.00 45.06 O
HETATM 3729 O HOH A2646 22.134 11.846 32.431 1.00 40.01 O
HETATM 3730 O HOH A2647 28.191 19.342 15.267 1.00 50.38 O
HETATM 3731 O HOH A2648 33.230 -28.068 31.707 1.00 89.72 O
HETATM 3732 O HOH A2649 43.553 -63.948 32.043 1.00 63.55 O
HETATM 3733 O HOH A2650 20.589 -28.631 7.680 1.00 51.58 O
HETATM 3734 O HOH A2651 27.405 -18.550 4.088 1.00 72.33 O
HETATM 3735 O HOH A2652 22.960 -33.120 21.126 1.00 50.47 O
HETATM 3736 O HOH A2653 22.715 -29.783 5.999 1.00 68.31 O
HETATM 3737 O HOH A2654 21.302 -26.741 4.474 1.00 50.24 O
HETATM 3738 O HOH A2655 22.448 15.194 5.798 1.00 39.15 O
HETATM 3739 O HOH A2656 18.702 -33.637 21.910 1.00 56.30 O
HETATM 3740 O HOH A2657 36.006 21.742 18.621 1.00 61.74 O
HETATM 3741 O HOH A2658 16.394 -16.364 26.661 1.00 35.86 O
HETATM 3742 O HOH A2659 29.366 -38.038 31.328 1.00 63.42 O
HETATM 3743 O HOH A2660 -0.053 20.675 16.356 1.00 76.95 O
HETATM 3744 O HOH A2661 2.629 -29.191 -0.348 1.00 61.62 O
HETATM 3745 O HOH A2662 5.496 13.517 30.680 1.00 53.91 O
HETATM 3746 O HOH A2663 47.773 -75.492 27.571 1.00 49.81 O
HETATM 3747 O HOH A2664 -1.395 -22.684 -4.237 1.00 68.66 O
HETATM 3748 O HOH A2665 1.550 5.651 35.680 1.00 67.87 O
HETATM 3749 O HOH A2666 17.526 -34.840 34.518 1.00 60.50 O
HETATM 3750 O HOH A2667 34.893 -58.573 7.619 1.00 77.71 O
HETATM 3751 O HOH A2668 20.254 -31.475 20.603 1.00 45.27 O
HETATM 3752 O HOH A2669 37.461 -53.466 5.713 1.00 93.06 O
HETATM 3753 O HOH A2670 18.703 -27.451 17.245 1.00 54.59 O
HETATM 3754 O HOH A2671 28.088 10.797 32.061 1.00 38.37 O
HETATM 3755 O HOH A2672 -0.069 16.022 10.667 1.00 77.33 O
HETATM 3756 O HOH A2673 24.134 -40.031 17.509 1.00 66.91 O
HETATM 3757 O HOH A2674 45.318 -49.808 29.960 1.00 59.72 O
HETATM 3758 O HOH A2675 22.271 -31.684 7.591 1.00 63.35 O
HETATM 3759 O HOH A2676 44.170 -59.878 32.980 1.00 72.14 O
HETATM 3760 O HOH A2677 26.326 13.279 23.708 1.00 42.04 O
HETATM 3761 O HOH A2678 22.247 18.824 18.186 1.00 59.03 O
HETATM 3762 O HOH A2679 32.088 -17.078 27.297 1.00 54.39 O
HETATM 3763 O HOH A2680 13.671 5.724 15.696 1.00 34.15 O
HETATM 3764 O HOH A2681 32.146 -37.948 21.485 1.00 49.88 O
HETATM 3765 O HOH A2682 28.985 -38.403 18.871 1.00 53.10 O
HETATM 3766 O HOH A2683 19.755 18.884 15.752 1.00 60.88 O
HETATM 3767 O HOH A2684 24.865 18.676 9.840 1.00 47.76 O
HETATM 3768 O HOH A2685 29.345 -29.252 8.019 1.00 62.96 O
HETATM 3769 O HOH A2686 23.769 14.085 22.009 1.00 45.65 O
HETATM 3770 O HOH A2687 21.778 -53.356 12.199 1.00 92.47 O
HETATM 3771 O HOH A2688 31.386 -19.835 28.359 1.00 67.10 O
HETATM 3772 O HOH A2689 22.650 -32.656 18.632 1.00 63.88 O
HETATM 3773 O HOH A2690 2.323 -31.060 14.641 1.00 54.19 O
HETATM 3774 O HOH A2691 15.965 -27.173 13.090 1.00 53.36 O
HETATM 3775 O HOH A2692 41.782 -30.833 19.838 1.00 49.35 O
HETATM 3776 O HOH A2693 22.909 -30.808 14.950 1.00 51.02 O
HETATM 3777 O HOH A2694 17.849 17.105 16.173 1.00 54.92 O
HETATM 3778 O HOH A2695 21.143 -34.522 22.371 1.00 52.53 O
HETATM 3779 O HOH A2696 26.447 13.696 30.244 1.00 57.19 O
HETATM 3780 O HOH A2697 -0.726 21.368 24.560 1.00 73.70 O
HETATM 3781 O HOH A2698 18.567 -24.950 32.040 1.00 55.24 O
HETATM 3782 O HOH A2699 3.532 -1.561 8.919 1.00 54.23 O
HETATM 3783 O HOH A2700 28.268 -33.909 37.864 1.00 57.76 O
HETATM 3784 O HOH A2701 16.458 18.318 8.422 1.00 79.94 O
HETATM 3785 O HOH A2702 13.888 19.819 9.799 1.00 60.18 O
HETATM 3786 O HOH A2703 24.760 -30.385 7.606 1.00 62.35 O
HETATM 3787 O HOH A2704 5.963 -19.654 31.222 1.00 51.16 O
HETATM 3788 O HOH A2705 32.053 -38.807 26.049 1.00 67.75 O
HETATM 3789 O HOH A2706 32.504 -39.397 23.792 1.00 65.98 O
HETATM 3790 O HOH A2707 4.231 -19.603 -4.673 1.00 68.49 O
HETATM 3791 O HOH A2708 12.907 22.359 15.696 1.00 80.68 O
HETATM 3792 O HOH A2709 20.683 20.816 8.554 1.00 97.56 O
HETATM 3793 O HOH A2710 26.331 -42.341 20.977 1.00 70.65 O
HETATM 3794 O HOH A2711 21.284 -27.457 10.708 1.00 45.00 O
HETATM 3795 O HOH A2712 26.574 -39.969 18.702 1.00 65.25 O
HETATM 3796 O HOH A2713 -3.913 15.014 8.004 1.00 78.90 O
HETATM 3797 O HOH A2714 24.550 -17.957 3.696 1.00 53.59 O
HETATM 3798 O HOH A2715 25.696 13.573 26.256 1.00 34.53 O
HETATM 3799 O HOH A2716 20.868 -31.496 10.901 1.00 67.68 O
HETATM 3800 O HOH A2717 24.323 -19.844 2.290 1.00 57.78 O
HETATM 3801 O HOH A2718 2.791 11.933 32.011 1.00 70.87 O
HETATM 3802 O HOH A2719 26.398 2.769 8.123 1.00 36.55 O
HETATM 3803 O HOH A2720 10.239 -32.643 29.474 1.00 57.37 O
HETATM 3804 O HOH A2721 27.696 18.012 7.244 1.00 64.02 O
HETATM 3805 O HOH A2722 30.412 -39.568 33.184 1.00 88.07 O
HETATM 3806 O HOH A2723 1.259 21.992 14.944 1.00 77.29 O
HETATM 3807 O HOH A2724 4.399 -17.839 29.993 1.00 58.00 O
HETATM 3808 O HOH A2725 33.102 -40.931 30.637 1.00 69.89 O
HETATM 3809 O HOH A2726 19.524 -46.766 13.492 1.00 67.27 O
HETATM 3810 O HOH A2727 30.910 11.762 2.633 1.00 58.02 O
HETATM 3811 O HOH A2728 41.196 -53.521 4.295 1.00 69.27 O
HETATM 3812 O HOH A2729 1.769 -6.418 6.557 1.00 47.28 O
HETATM 3813 O HOH A2730 14.871 22.510 8.054 1.00 75.74 O
HETATM 3814 O HOH A2731 19.736 -27.464 12.448 1.00 53.13 O
CONECT 538 1204
CONECT 554 1110
CONECT 574 1248
CONECT 1110 554
CONECT 1204 538
CONECT 1248 574
CONECT 2618 2639
CONECT 2639 2618
CONECT 3006 3007 3015
CONECT 3007 3006 3008
CONECT 3008 3007 3009 3033
CONECT 3009 3008 3010
CONECT 3010 3009 3011 3015
CONECT 3011 3010 3012
CONECT 3012 3011 3013
CONECT 3013 3012 3014 3019
CONECT 3014 3013 3015 3016
CONECT 3015 3006 3010 3014 3024
CONECT 3016 3014 3017
CONECT 3017 3016 3018
CONECT 3018 3017 3019 3022 3023
CONECT 3019 3013 3018 3020
CONECT 3020 3019 3021
CONECT 3021 3020 3022
CONECT 3022 3018 3021 3025
CONECT 3023 3018
CONECT 3024 3015
CONECT 3025 3022 3026 3027
CONECT 3026 3025
CONECT 3027 3025 3028
CONECT 3028 3027 3029
CONECT 3029 3028 3030
CONECT 3030 3029 3031 3032
CONECT 3031 3030
CONECT 3032 3030
CONECT 3033 3008
CONECT 3034 3035 3043
CONECT 3035 3034 3036
CONECT 3036 3035 3037 3061
CONECT 3037 3036 3038
CONECT 3038 3037 3039 3043
CONECT 3039 3038 3040
CONECT 3040 3039 3041
CONECT 3041 3040 3042 3047
CONECT 3042 3041 3043 3044
CONECT 3043 3034 3038 3042 3052
CONECT 3044 3042 3045
CONECT 3045 3044 3046
CONECT 3046 3045 3047 3050 3051
CONECT 3047 3041 3046 3048
CONECT 3048 3047 3049
CONECT 3049 3048 3050
CONECT 3050 3046 3049 3053
CONECT 3051 3046
CONECT 3052 3043
CONECT 3053 3050 3054 3055
CONECT 3054 3053
CONECT 3055 3053 3056
CONECT 3056 3055 3057
CONECT 3057 3056 3058
CONECT 3058 3057 3059 3060
CONECT 3059 3058
CONECT 3060 3058
CONECT 3061 3036
CONECT 3062 3063 3071
CONECT 3063 3062 3064
CONECT 3064 3063 3065 3089
CONECT 3065 3064 3066
CONECT 3066 3065 3067 3071
CONECT 3067 3066 3068
CONECT 3068 3067 3069
CONECT 3069 3068 3070 3075
CONECT 3070 3069 3071 3072
CONECT 3071 3062 3066 3070 3080
CONECT 3072 3070 3073
CONECT 3073 3072 3074
CONECT 3074 3073 3075 3078 3079
CONECT 3075 3069 3074 3076
CONECT 3076 3075 3077
CONECT 3077 3076 3078
CONECT 3078 3074 3077 3081
CONECT 3079 3074
CONECT 3080 3071
CONECT 3081 3078 3082 3083
CONECT 3082 3081
CONECT 3083 3081 3084
CONECT 3084 3083 3085
CONECT 3085 3084 3086
CONECT 3086 3085 3087 3088
CONECT 3087 3086
CONECT 3088 3086
CONECT 3089 3064
CONECT 3090 3091 3112
CONECT 3091 3090 3092
CONECT 3092 3091 3093 3137
CONECT 3093 3092 3114
CONECT 3094 3095 3137
CONECT 3095 3094 3123 3138
CONECT 3096 3108 3115
CONECT 3097 3106 3125 3128
CONECT 3098 3108 3130 3131
CONECT 3099 3100 3128
CONECT 3100 3099 3132
CONECT 3101 3106 3129
CONECT 3102 3125 3126 3127
CONECT 3103 3106 3126 3130
CONECT 3104 3109 3124
CONECT 3105 3107 3133
CONECT 3106 3097 3101 3103
CONECT 3107 3105 3134
CONECT 3108 3096 3098 3139
CONECT 3109 3104 3132
CONECT 3110 3111 3124
CONECT 3111 3110 3132
CONECT 3112 3090 3114 3124
CONECT 3113 3117 3134
CONECT 3114 3093 3112
CONECT 3115 3096 3116
CONECT 3116 3115 3139
CONECT 3117 3113 3135
CONECT 3118 3119 3135
CONECT 3119 3118 3136
CONECT 3120 3121 3136
CONECT 3121 3120 3123
CONECT 3122 3133
CONECT 3123 3095 3121
CONECT 3124 3104 3110 3112
CONECT 3125 3097 3102
CONECT 3126 3102 3103 3131
CONECT 3127 3102
CONECT 3128 3097 3099 3129
CONECT 3129 3101 3128
CONECT 3130 3098 3103
CONECT 3131 3098 3126
CONECT 3132 3100 3109 3111
CONECT 3133 3105 3122
CONECT 3134 3107 3113
CONECT 3135 3117 3118
CONECT 3136 3119 3120
CONECT 3137 3092 3094
CONECT 3138 3095
CONECT 3139 3108 3116
CONECT 3140 3141 3142 3143
CONECT 3141 3140
CONECT 3142 3140
CONECT 3143 3140 3144
CONECT 3144 3143 3145
CONECT 3145 3144 3146
CONECT 3146 3145 3147
CONECT 3147 3146 3148
CONECT 3148 3147
CONECT 3149 3150 3151 3152
CONECT 3150 3149
CONECT 3151 3149
CONECT 3152 3149 3153
CONECT 3153 3152 3154
CONECT 3154 3153 3155
CONECT 3155 3154 3156
CONECT 3156 3155 3157
CONECT 3157 3156 3158
CONECT 3158 3157 3159
CONECT 3159 3158
CONECT 3160 3161 3162 3163
CONECT 3161 3160
CONECT 3162 3160
CONECT 3163 3160 3164
CONECT 3164 3163 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
CONECT 3180 3181 3182 3183
CONECT 3181 3180
CONECT 3182 3180
CONECT 3183 3180 3184
CONECT 3184 3183 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
CONECT 3199 3200 3201 3202
CONECT 3200 3199
CONECT 3201 3199
CONECT 3202 3199 3203
CONECT 3203 3202 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
CONECT 3212 3213 3214 3215
CONECT 3213 3212
CONECT 3214 3212
CONECT 3215 3212 3216
CONECT 3216 3215 3217
CONECT 3217 3216 3218
CONECT 3218 3217
CONECT 3219 3220 3221 3222
CONECT 3220 3219
CONECT 3221 3219
CONECT 3222 3219 3223
CONECT 3223 3222 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 3236
CONECT 3236 3235 3237
CONECT 3237 3236
CONECT 3238 3239 3240 3241
CONECT 3239 3238
CONECT 3240 3238
CONECT 3241 3238 3242
CONECT 3242 3241 3243
CONECT 3243 3242 3244
CONECT 3244 3243 3245
CONECT 3245 3244 3246
CONECT 3246 3245 3247
CONECT 3247 3246 3248
CONECT 3248 3247 3249
CONECT 3249 3248
CONECT 3250 3251 3252 3253
CONECT 3251 3250
CONECT 3252 3250
CONECT 3253 3250 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 3261
CONECT 3261 3260 3262
CONECT 3262 3261
CONECT 3263 3264 3265 3266
CONECT 3264 3263
CONECT 3265 3263
CONECT 3266 3263 3267
CONECT 3267 3266 3268
CONECT 3268 3267 3269
CONECT 3269 3268 3270
CONECT 3270 3269 3271
CONECT 3271 3270 3272
CONECT 3272 3271 3273
CONECT 3273 3272 3274
CONECT 3274 3273
CONECT 3275 3276 3277 3278
CONECT 3276 3275
CONECT 3277 3275
CONECT 3278 3275 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 3293
CONECT 3293 3292 3294
CONECT 3294 3293
CONECT 3295 3296 3297 3298
CONECT 3296 3295
CONECT 3297 3295
CONECT 3298 3295 3299
CONECT 3299 3298 3300
CONECT 3300 3299 3301
CONECT 3301 3300 3302
CONECT 3302 3301 3303
CONECT 3303 3302
CONECT 3304 3305 3306 3307
CONECT 3305 3304
CONECT 3306 3304
CONECT 3307 3304 3308
CONECT 3308 3307 3309
CONECT 3309 3308 3310
CONECT 3310 3309 3311
CONECT 3311 3310 3312
CONECT 3312 3311 3313
CONECT 3313 3312 3314
CONECT 3314 3313
CONECT 3315 3316 3317 3318
CONECT 3316 3315
CONECT 3317 3315
CONECT 3318 3315 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 3329
CONECT 3329 3328 3330
CONECT 3330 3329
CONECT 3331 3332 3333 3334
CONECT 3332 3331
CONECT 3333 3331
CONECT 3334 3331 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 3344
CONECT 3344 3343 3345
CONECT 3345 3344 3346
CONECT 3346 3345 3347
CONECT 3347 3346
CONECT 3348 3349 3350 3351
CONECT 3349 3348
CONECT 3350 3348
CONECT 3351 3348 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 3359
CONECT 3359 3358 3360
CONECT 3360 3359 3361
CONECT 3361 3360
CONECT 3362 3363 3364 3365
CONECT 3363 3362
CONECT 3364 3362
CONECT 3365 3362 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 3373
CONECT 3373 3372 3374
CONECT 3374 3373 3375
CONECT 3375 3374 3376
CONECT 3376 3375 3377
CONECT 3377 3376
CONECT 3378 3379 3380 3381
CONECT 3379 3378
CONECT 3380 3378
CONECT 3381 3378 3382
CONECT 3382 3381 3383
CONECT 3383 3382 3384
CONECT 3384 3383 3385
CONECT 3385 3384 3386
CONECT 3386 3385 3387
CONECT 3387 3386 3388
CONECT 3388 3387 3389
CONECT 3389 3388 3390
CONECT 3390 3389 3391
CONECT 3391 3390
CONECT 3392 3393 3394 3395
CONECT 3393 3392
CONECT 3394 3392
CONECT 3395 3392 3396
CONECT 3396 3395 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 3404
CONECT 3404 3403 3405
CONECT 3405 3404 3406
CONECT 3406 3405 3407
CONECT 3407 3406 3408
CONECT 3408 3407 3409
CONECT 3409 3408 3410
CONECT 3410 3409 3411
CONECT 3411 3410
CONECT 3412 3413 3414 3415
CONECT 3413 3412
CONECT 3414 3412
CONECT 3415 3412 3416
CONECT 3416 3415 3417
CONECT 3417 3416 3418
CONECT 3418 3417 3419
CONECT 3419 3418 3420
CONECT 3420 3419 3421
CONECT 3421 3420 3422
CONECT 3422 3421 3423
CONECT 3423 3422 3424
CONECT 3424 3423 3425
CONECT 3425 3424
CONECT 3426 3427 3428 3429
CONECT 3427 3426
CONECT 3428 3426
CONECT 3429 3426 3430
CONECT 3430 3429 3431
CONECT 3431 3430 3432
CONECT 3432 3431 3433
CONECT 3433 3432 3434
CONECT 3434 3433 3435
CONECT 3435 3434 3436
CONECT 3436 3435 3437
CONECT 3437 3436
CONECT 3438 3439 3440 3441
CONECT 3439 3438
CONECT 3440 3438
CONECT 3441 3438 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
CONECT 3452 3453 3454 3455
CONECT 3453 3452
CONECT 3454 3452
CONECT 3455 3452 3456
CONECT 3456 3455 3457
CONECT 3457 3456 3458
CONECT 3458 3457 3459
CONECT 3459 3458 3460
CONECT 3460 3459 3461
CONECT 3461 3460 3462
CONECT 3462 3461
CONECT 3463 3464 3465 3466
CONECT 3464 3463
CONECT 3465 3463
CONECT 3466 3463 3467
CONECT 3467 3466 3468
CONECT 3468 3467 3469
CONECT 3469 3468 3470
CONECT 3470 3469 3471
CONECT 3471 3470 3472
CONECT 3472 3471 3473
CONECT 3473 3472
CONECT 3474 3475 3476 3477
CONECT 3475 3474
CONECT 3476 3474
CONECT 3477 3474 3478
CONECT 3478 3477 3479
CONECT 3479 3478 3480
CONECT 3480 3479 3481
CONECT 3481 3480 3482
CONECT 3482 3481 3483
CONECT 3483 3482 3484
CONECT 3484 3483 3485
CONECT 3485 3484 3486
CONECT 3486 3485 3487
CONECT 3487 3486 3488
CONECT 3488 3487 3489
CONECT 3489 3488
CONECT 3490 3491 3492 3493
CONECT 3491 3490
CONECT 3492 3490
CONECT 3493 3490 3494
CONECT 3494 3493 3495
CONECT 3495 3494 3496
CONECT 3496 3495 3497
CONECT 3497 3496 3498
CONECT 3498 3497 3499
CONECT 3499 3498 3500
CONECT 3500 3499 3501
CONECT 3501 3500 3502
CONECT 3502 3501 3503
CONECT 3503 3502 3504
CONECT 3504 3503
CONECT 3505 3508
CONECT 3506 3507 3509
CONECT 3507 3506 3510
CONECT 3508 3505 3512
CONECT 3509 3506 3513
CONECT 3510 3507 3514
CONECT 3511 3525 3527
CONECT 3512 3508 3515
CONECT 3513 3509 3516
CONECT 3514 3510 3517
CONECT 3515 3512 3518
CONECT 3516 3513 3518
CONECT 3517 3514 3519
CONECT 3518 3515 3516
CONECT 3519 3517 3520
CONECT 3520 3519 3521
CONECT 3521 3520 3522
CONECT 3522 3521 3524
CONECT 3523 3525 3529
CONECT 3524 3522 3526 3529
CONECT 3525 3511 3523 3528
CONECT 3526 3524
CONECT 3527 3511
CONECT 3528 3525
CONECT 3529 3523 3524
CONECT 3530 3531 3532
CONECT 3531 3530 3533
CONECT 3532 3530 3535
CONECT 3533 3531 3536
CONECT 3534 3546 3548
CONECT 3535 3532 3537
CONECT 3536 3533 3538
CONECT 3537 3535 3539
CONECT 3538 3536 3540
CONECT 3539 3537
CONECT 3540 3538 3541
CONECT 3541 3540 3542
CONECT 3542 3541 3543
CONECT 3543 3542 3545
CONECT 3544 3546 3550
CONECT 3545 3543 3547 3550
CONECT 3546 3534 3544 3549
CONECT 3547 3545
CONECT 3548 3534
CONECT 3549 3546
CONECT 3550 3544 3545
CONECT 3551 3552 3553
CONECT 3552 3551 3554
CONECT 3553 3551 3556
CONECT 3554 3552 3557
CONECT 3555 3565 3567
CONECT 3556 3553
CONECT 3557 3554 3558
CONECT 3558 3557 3559
CONECT 3559 3558 3560
CONECT 3560 3559 3561
CONECT 3561 3560 3562
CONECT 3562 3561 3564
CONECT 3563 3565 3569
CONECT 3564 3562 3566 3569
CONECT 3565 3555 3563 3568
CONECT 3566 3564
CONECT 3567 3555
CONECT 3568 3565
CONECT 3569 3563 3564
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
CONECT 3577 3578 3579
CONECT 3578 3577
CONECT 3579 3577 3580
CONECT 3580 3579 3581
CONECT 3581 3580 3582
CONECT 3582 3581 3583
CONECT 3583 3582
MASTER 389 0 35 19 2 0 0 6 3813 1 586 35
END