HEADER MEMBRANE PROTEIN 07-SEP-20 7K15
TITLE CRYSTAL STRUCTURE OF THE HUMAN LEUKOTRIENE B4 RECEPTOR 1 IN COMPLEX
TITLE 2 WITH SELECTIVE ANTAGONIST MK-D-046
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUKOTRIENE B4 RECEPTOR 1,FLAVODOXIN,LEUKOTRIENE B4
COMPND 3 RECEPTOR 1;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: LTB4-R1,CHEMOATTRACTANT RECEPTOR-LIKE 1,G-PROTEIN COUPLED
COMPND 6 RECEPTOR 16,P2Y PURINOCEPTOR 7,P2Y7,LTB4-R1,CHEMOATTRACTANT RECEPTOR-
COMPND 7 LIKE 1,G-PROTEIN COUPLED RECEPTOR 16,P2Y PURINOCEPTOR 7,P2Y7;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, DESULFOVIBRIO VULGARIS (STRAIN
SOURCE 3 HILDENBOROUGH / ATCC 29579 / DSM 644 / NCIMB 8303);
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606, 882;
SOURCE 6 STRAIN: HILDENBOROUGH / ATCC 29579 / DSM 644 / NCIMB 8303;
SOURCE 7 GENE: LTB4R, BLT, BLT1, BLTR, CMKRL1, GPR16, P2RY7, DVU_2680;
SOURCE 8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS HUMAN LEUKOTRIENE B4 RECEPTOR 1, HBLT1, BLT1, BLTR1, LTB4, LTB4R,
KEYWDS 2 LT4R1, LTB4R1, MK-D-046, SELECTIVE ANTAGONIST, INFLAMMATION,
KEYWDS 3 INFLAMMATORY DISEASE, TYPE 2 DIABETES, G PROTEIN-COUPLED RECEPTOR,
KEYWDS 4 GPCR, FLAVODOXIN FUSION, MEMBRANE PROTEIN, LCP
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MICHAELIAN,G.W.HAN,V.CHEREZOV
REVDAT 2 02-JUN-21 7K15 1 JRNL
REVDAT 1 17-FEB-21 7K15 0
JRNL AUTH N.MICHAELIAN,A.SADYBEKOV,E.BESSERER-OFFROY,G.W.HAN,
JRNL AUTH 2 H.KRISHNAMURTHY,B.A.ZAMLYNNY,X.FRADERA,P.SILIPHAIVANH,
JRNL AUTH 3 J.PRESLAND,K.B.SPENCER,S.M.SOISSON,P.POPOV,P.SARRET,
JRNL AUTH 4 V.KATRITCH,V.CHEREZOV
JRNL TITL STRUCTURAL INSIGHTS ON LIGAND RECOGNITION AT THE HUMAN
JRNL TITL 2 LEUKOTRIENE B4 RECEPTOR 1.
JRNL REF NAT COMMUN V. 12 2971 2021
JRNL REFN ESSN 2041-1723
JRNL PMID 34016973
JRNL DOI 10.1038/S41467-021-23149-1
REMARK 2
REMARK 2 RESOLUTION. 2.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 78.8
REMARK 3 NUMBER OF REFLECTIONS : 13808
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170
REMARK 3 FREE R VALUE TEST SET COUNT : 714
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 34.3700 - 4.9200 0.99 3474 173 0.1967 0.2406
REMARK 3 2 4.9200 - 3.9100 0.98 3233 199 0.1894 0.2462
REMARK 3 3 3.9100 - 3.4100 0.87 2866 143 0.2304 0.2662
REMARK 3 4 3.4100 - 3.1000 0.67 2153 127 0.2671 0.3524
REMARK 3 5 3.1000 - 2.8800 0.42 1368 72 0.3170 0.3258
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 13 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0870 0.3740 7.8366
REMARK 3 T TENSOR
REMARK 3 T11: 1.2059 T22: 0.3858
REMARK 3 T33: 0.4876 T12: 0.3252
REMARK 3 T13: -0.0304 T23: -0.0853
REMARK 3 L TENSOR
REMARK 3 L11: 0.8011 L22: 0.1682
REMARK 3 L33: 0.1427 L12: -0.3472
REMARK 3 L13: 0.0964 L23: -0.0221
REMARK 3 S TENSOR
REMARK 3 S11: 0.7059 S12: 0.4546 S13: -0.1721
REMARK 3 S21: -0.4813 S22: -0.2133 S23: -0.1506
REMARK 3 S31: 0.2027 S32: 0.0487 S33: 1.2549
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9446 2.4685 24.4583
REMARK 3 T TENSOR
REMARK 3 T11: 0.4820 T22: 0.3603
REMARK 3 T33: 0.3409 T12: 0.0947
REMARK 3 T13: -0.0201 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.5664 L22: 0.3084
REMARK 3 L33: 0.0870 L12: -0.1381
REMARK 3 L13: -0.0040 L23: 0.1401
REMARK 3 S TENSOR
REMARK 3 S11: 0.1844 S12: -0.0072 S13: -0.1779
REMARK 3 S21: -0.3793 S22: -0.0524 S23: 0.3650
REMARK 3 S31: 0.0270 S32: -0.0002 S33: 0.0026
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 212 AND RESID 1002
REMARK 3 THROUGH 1150 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.1410 40.6879 26.9520
REMARK 3 T TENSOR
REMARK 3 T11: 0.2287 T22: 0.2860
REMARK 3 T33: 0.3572 T12: 0.0297
REMARK 3 T13: -0.0368 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.7490 L22: 0.6020
REMARK 3 L33: 0.9194 L12: -0.2860
REMARK 3 L13: -0.2504 L23: -0.3670
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: -0.0961 S13: -0.1953
REMARK 3 S21: -0.0954 S22: -0.0376 S23: 0.0755
REMARK 3 S31: 0.0089 S32: -0.0816 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 213 THROUGH 220 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6193 28.4314 22.9945
REMARK 3 T TENSOR
REMARK 3 T11: 0.4142 T22: 0.4001
REMARK 3 T33: 0.2755 T12: 0.1403
REMARK 3 T13: 0.1782 T23: -0.1330
REMARK 3 L TENSOR
REMARK 3 L11: 0.9966 L22: 0.0421
REMARK 3 L33: 0.1813 L12: -0.2036
REMARK 3 L13: 0.4242 L23: -0.0862
REMARK 3 S TENSOR
REMARK 3 S11: -0.0955 S12: 0.1096 S13: -0.0354
REMARK 3 S21: -0.2424 S22: -0.1902 S23: 0.0647
REMARK 3 S31: 0.1190 S32: 0.2199 S33: -0.3919
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 221 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7828 -0.5686 23.5822
REMARK 3 T TENSOR
REMARK 3 T11: 0.3916 T22: 0.2066
REMARK 3 T33: 0.6338 T12: 0.0923
REMARK 3 T13: -0.2422 T23: 0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 0.2636 L22: 0.9185
REMARK 3 L33: 0.9159 L12: 0.2263
REMARK 3 L13: -0.3860 L23: 0.1934
REMARK 3 S TENSOR
REMARK 3 S11: 0.1556 S12: 0.2023 S13: -0.4749
REMARK 3 S21: -0.1742 S22: 0.0364 S23: 0.1546
REMARK 3 S31: -0.0457 S32: 0.0488 S33: 0.6432
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 250 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5181 -13.8827 20.5906
REMARK 3 T TENSOR
REMARK 3 T11: 0.7751 T22: 0.4591
REMARK 3 T33: 0.5823 T12: 0.1234
REMARK 3 T13: -0.1929 T23: -0.0954
REMARK 3 L TENSOR
REMARK 3 L11: 0.1395 L22: 0.2227
REMARK 3 L33: 0.3862 L12: -0.1739
REMARK 3 L13: -0.2331 L23: 0.2960
REMARK 3 S TENSOR
REMARK 3 S11: 0.0268 S12: 0.1033 S13: -0.1563
REMARK 3 S21: 0.1704 S22: -0.4597 S23: 0.2653
REMARK 3 S31: 0.6952 S32: 0.0085 S33: -0.0763
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 277 THROUGH 318 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0399 21.7085 9.7402
REMARK 3 T TENSOR
REMARK 3 T11: 0.7510 T22: 0.8467
REMARK 3 T33: 0.4377 T12: 0.0770
REMARK 3 T13: -0.0540 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.0539 L22: 0.0227
REMARK 3 L33: 0.0630 L12: -0.0154
REMARK 3 L13: -0.0113 L23: -0.0325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0713 S12: 0.3240 S13: 0.0699
REMARK 3 S21: -0.1819 S22: 0.0068 S23: -0.2267
REMARK 3 S31: -0.2566 S32: 0.2498 S33: -0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7K15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-20.
REMARK 100 THE DEPOSITION ID IS D_1000251716.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 123
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 R CDTE 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14961
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.880
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.9
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : 0.24600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 50.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.83000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.600
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: 5X33, 1I1O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE TRIBASIC DIHYDRATE PH
REMARK 280 5.8, SODIUM ACETATE TRIHYDRATE, BENZAMIDINE HYDROCHLORIDE, PEG-
REMARK 280 400, MK-D-046, DMSO, LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,-Y,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 35.38500
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.74000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.38500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 63.74000
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN
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 -22
REMARK 465 LYS A -21
REMARK 465 THR A -20
REMARK 465 ILE A -19
REMARK 465 ILE A -18
REMARK 465 ALA A -17
REMARK 465 LEU A -16
REMARK 465 SER A -15
REMARK 465 TYR A -14
REMARK 465 ILE A -13
REMARK 465 PHE A -12
REMARK 465 CYS A -11
REMARK 465 LEU A -10
REMARK 465 VAL A -9
REMARK 465 PHE A -8
REMARK 465 ALA A -7
REMARK 465 ASP A -6
REMARK 465 TYR A -5
REMARK 465 LYS A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ASP A -1
REMARK 465 ASP A 0
REMARK 465 ALA A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 PRO A 9
REMARK 465 PRO A 10
REMARK 465 SER A 11
REMARK 465 LEU A 12
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 PHE A 16 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 45 CG CD CE NZ
REMARK 470 GLN A 48 CG CD OE1 NE2
REMARK 470 LYS A 49 CG CD CE NZ
REMARK 470 LYS A 162 CG CD CE NZ
REMARK 470 ARG A 171 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1042 CG CD OE1 OE2
REMARK 470 GLU A1118 CG CD OE1 OE2
REMARK 470 ARG A 214 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 217 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 252 CG CD OE1 NE2
REMARK 470 LEU A 258 CG CD1 CD2
REMARK 470 ARG A 294 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 LYS A 162 171.39 69.22
REMARK 500 PHE A 190 -61.94 -158.35
REMARK 500 CYS A1057 147.21 -172.19
REMARK 500 TRP A1060 24.07 -144.04
REMARK 500 ALA A 250 -58.08 -135.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLA A 2104
REMARK 610 OLC A 2105
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2102 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD1
REMARK 620 2 SER A 104 OG 87.3
REMARK 620 3 HOH A2205 O 127.0 126.7
REMARK 620 N 1 2
DBREF 7K15 A 5 212 UNP Q15722 LT4R1_HUMAN 5 212
DBREF 7K15 A 1002 1148 UNP P00323 FLAV_DESVH 2 148
DBREF 7K15 A 213 310 UNP Q15722 LT4R1_HUMAN 213 310
SEQADV 7K15 MET A -22 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 LYS A -21 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 THR A -20 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ILE A -19 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ILE A -18 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ALA A -17 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 LEU A -16 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 SER A -15 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 TYR A -14 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ILE A -13 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 PHE A -12 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 CYS A -11 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 LEU A -10 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 VAL A -9 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 PHE A -8 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ALA A -7 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ASP A -6 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 TYR A -5 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 LYS A -4 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ASP A -3 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ASP A -2 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ASP A -1 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ASP A 0 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ALA A 1 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 GLY A 2 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ARG A 3 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 ALA A 4 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 TRP A 106 UNP Q15722 LEU 106 ENGINEERED MUTATION
SEQADV 7K15 TYR A 116 UNP Q15722 SER 116 ENGINEERED MUTATION
SEQADV 7K15 ILE A 196 UNP Q15722 ALA 196 ENGINEERED MUTATION
SEQADV 7K15 ALA A 1002 UNP P00323 PRO 2 ENGINEERED MUTATION
SEQADV 7K15 TRP A 1098 UNP P00323 TYR 98 ENGINEERED MUTATION
SEQADV 7K15 ARG A 1149 UNP P00323 LINKER
SEQADV 7K15 ARG A 1150 UNP P00323 LINKER
SEQADV 7K15 PHE A 287 UNP Q15722 CYS 287 ENGINEERED MUTATION
SEQADV 7K15 ALA A 310 UNP Q15722 SER 310 ENGINEERED MUTATION
SEQADV 7K15 GLU A 311 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 PHE A 312 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 LEU A 313 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 GLU A 314 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 VAL A 315 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 LEU A 316 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 PHE A 317 UNP Q15722 EXPRESSION TAG
SEQADV 7K15 GLN A 318 UNP Q15722 EXPRESSION TAG
SEQRES 1 A 490 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU
SEQRES 2 A 490 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA GLY ARG
SEQRES 3 A 490 ALA SER SER ALA ALA PRO PRO SER LEU GLY VAL GLU PHE
SEQRES 4 A 490 ILE SER LEU LEU ALA ILE ILE LEU LEU SER VAL ALA LEU
SEQRES 5 A 490 ALA VAL GLY LEU PRO GLY ASN SER PHE VAL VAL TRP SER
SEQRES 6 A 490 ILE LEU LYS ARG MET GLN LYS ARG SER VAL THR ALA LEU
SEQRES 7 A 490 MET VAL LEU ASN LEU ALA LEU ALA ASP LEU ALA VAL LEU
SEQRES 8 A 490 LEU THR ALA PRO PHE PHE LEU HIS PHE LEU ALA GLN GLY
SEQRES 9 A 490 THR TRP SER PHE GLY LEU ALA GLY CYS ARG LEU CYS HIS
SEQRES 10 A 490 TYR VAL CYS GLY VAL SER MET TYR ALA SER VAL TRP LEU
SEQRES 11 A 490 ILE THR ALA MET SER LEU ASP ARG TYR LEU ALA VAL ALA
SEQRES 12 A 490 ARG PRO PHE VAL SER GLN LYS LEU ARG THR LYS ALA MET
SEQRES 13 A 490 ALA ARG ARG VAL LEU ALA GLY ILE TRP VAL LEU SER PHE
SEQRES 14 A 490 LEU LEU ALA THR PRO VAL LEU ALA TYR ARG THR VAL VAL
SEQRES 15 A 490 PRO TRP LYS THR ASN MET SER LEU CYS PHE PRO ARG TYR
SEQRES 16 A 490 PRO SER GLU GLY HIS ARG ALA PHE HIS LEU ILE PHE GLU
SEQRES 17 A 490 ALA VAL THR GLY PHE LEU LEU PRO PHE LEU ILE VAL VAL
SEQRES 18 A 490 ALA SER TYR SER ASP ILE GLY ARG ARG LEU GLN ALA ARG
SEQRES 19 A 490 ARG ALA LYS ALA LEU ILE VAL TYR GLY SER THR THR GLY
SEQRES 20 A 490 ASN THR GLU TYR THR ALA GLU THR ILE ALA ARG GLU LEU
SEQRES 21 A 490 ALA ASP ALA GLY TYR GLU VAL ASP SER ARG ASP ALA ALA
SEQRES 22 A 490 SER VAL GLU ALA GLY GLY LEU PHE GLU GLY PHE ASP LEU
SEQRES 23 A 490 VAL LEU LEU GLY CYS SER THR TRP GLY ASP ASP SER ILE
SEQRES 24 A 490 GLU LEU GLN ASP ASP PHE ILE PRO LEU PHE ASP SER LEU
SEQRES 25 A 490 GLU GLU THR GLY ALA GLN GLY ARG LYS VAL ALA CYS PHE
SEQRES 26 A 490 GLY CYS GLY ASP SER SER TRP GLU TYR PHE CYS GLY ALA
SEQRES 27 A 490 VAL ASP ALA ILE GLU GLU LYS LEU LYS ASN LEU GLY ALA
SEQRES 28 A 490 GLU ILE VAL GLN ASP GLY LEU ARG ILE ASP GLY ASP PRO
SEQRES 29 A 490 ARG ALA ALA ARG ASP ASP ILE VAL GLY TRP ALA HIS ASP
SEQRES 30 A 490 VAL ARG GLY ALA ILE ARG ARG PHE ARG ARG SER ARG ARG
SEQRES 31 A 490 THR GLY ARG LEU VAL VAL LEU ILE ILE LEU THR PHE ALA
SEQRES 32 A 490 ALA PHE TRP LEU PRO TYR HIS VAL VAL ASN LEU ALA GLU
SEQRES 33 A 490 ALA GLY ARG ALA LEU ALA GLY GLN ALA ALA GLY LEU GLY
SEQRES 34 A 490 LEU VAL GLY LYS ARG LEU SER LEU ALA ARG ASN VAL LEU
SEQRES 35 A 490 ILE ALA LEU ALA PHE LEU SER SER SER VAL ASN PRO VAL
SEQRES 36 A 490 LEU TYR ALA PHE ALA GLY GLY GLY LEU LEU ARG SER ALA
SEQRES 37 A 490 GLY VAL GLY PHE VAL ALA LYS LEU LEU GLU GLY THR GLY
SEQRES 38 A 490 ALA GLU PHE LEU GLU VAL LEU PHE GLN
HET VRJ A2101 35
HET NA A2102 1
HET FMN A2103 31
HET OLA A2104 12
HET OLC A2105 13
HET OLC A2106 25
HET 1PE A2107 16
HET 2PE A2108 28
HET P6G A2109 19
HETNAM VRJ N-(TERT-BUTYLSULFONYL)-4-FLUORO-2-{(3S,4R)-4-HYDROXY-3-
HETNAM 2 VRJ [(PYRIDIN-2-YL)METHYL]-3,4-DIHYDRO-2H-1-BENZOPYRAN-7-
HETNAM 3 VRJ YL}BENZAMIDE
HETNAM NA SODIUM ION
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM OLA OLEIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM 2PE NONAETHYLENE GLYCOL
HETNAM P6G HEXAETHYLENE GLYCOL
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
HETSYN 1PE PEG400
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 2 VRJ C26 H27 F N2 O5 S
FORMUL 3 NA NA 1+
FORMUL 4 FMN C17 H21 N4 O9 P
FORMUL 5 OLA C18 H34 O2
FORMUL 6 OLC 2(C21 H40 O4)
FORMUL 8 1PE C10 H22 O6
FORMUL 9 2PE C18 H38 O10
FORMUL 10 P6G C12 H26 O7
FORMUL 11 HOH *5(H2 O)
HELIX 1 AA1 GLY A 13 LYS A 45 1 33
HELIX 2 AA2 SER A 51 LEU A 69 1 19
HELIX 3 AA3 THR A 70 GLY A 81 1 12
HELIX 4 AA4 PHE A 85 ARG A 121 1 37
HELIX 5 AA5 ARG A 121 ARG A 129 1 9
HELIX 6 AA6 THR A 130 ALA A 149 1 20
HELIX 7 AA7 PRO A 151 TYR A 155 1 5
HELIX 8 AA8 SER A 174 PHE A 190 1 17
HELIX 9 AA9 PHE A 190 GLN A 209 1 20
HELIX 10 AB1 GLY A 1013 ALA A 1029 1 17
HELIX 11 AB2 ALA A 1039 VAL A 1041 5 3
HELIX 12 AB3 PHE A 1071 SER A 1077 1 7
HELIX 13 AB4 LEU A 1078 GLY A 1082 5 5
HELIX 14 AB5 CYS A 1102 LEU A 1115 1 14
HELIX 15 AB6 PRO A 1130 ALA A 1132 5 3
HELIX 16 AB7 ALA A 1133 ARG A 1149 1 17
HELIX 17 AB8 GLY A 220 ALA A 250 1 31
HELIX 18 AB9 VAL A 259 SER A 278 1 20
HELIX 19 AC1 SER A 279 LEU A 293 1 15
HELIX 20 AC2 ARG A 294 ALA A 296 5 3
HELIX 21 AC3 GLY A 297 GLU A 306 1 10
HELIX 22 AC4 GLY A 309 PHE A 317 1 9
SHEET 1 AA1 2 ARG A 156 PRO A 160 0
SHEET 2 AA1 2 SER A 166 PRO A 170 -1 O LEU A 167 N VAL A 159
SHEET 1 AA2 5 TYR A1031 ASP A1037 0
SHEET 2 AA2 5 ALA A1002 GLY A1009 1 N ILE A1006 O ASP A1034
SHEET 3 AA2 5 LEU A1052 CYS A1057 1 O LEU A1054 N LEU A1005
SHEET 4 AA2 5 LYS A1087 GLY A1094 1 O PHE A1091 N LEU A1055
SHEET 5 AA2 5 GLU A1118 ILE A1119 1 O GLU A1118 N VAL A1088
SHEET 1 AA3 5 TYR A1031 ASP A1037 0
SHEET 2 AA3 5 ALA A1002 GLY A1009 1 N ILE A1006 O ASP A1034
SHEET 3 AA3 5 LEU A1052 CYS A1057 1 O LEU A1054 N LEU A1005
SHEET 4 AA3 5 LYS A1087 GLY A1094 1 O PHE A1091 N LEU A1055
SHEET 5 AA3 5 LEU A1124 ASP A1127 1 O LEU A1124 N CYS A1090
SSBOND 1 CYS A 90 CYS A 168 1555 1555 2.03
LINK OD1 ASP A 64 NA NA A2102 1555 1555 2.36
LINK OG SER A 104 NA NA A2102 1555 1555 2.74
LINK NA NA A2102 O HOH A2205 1555 1555 2.46
CRYST1 70.770 82.670 127.480 90.00 90.00 90.00 P 21 2 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014130 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012096 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007844 0.00000
ATOM 1 N GLY A 13 -11.248 -19.073 8.541 1.00108.11 N
ANISOU 1 N GLY A 13 18231 10344 12502 2233 -4910 -1280 N
ATOM 2 CA GLY A 13 -10.284 -20.038 9.036 1.00119.09 C
ANISOU 2 CA GLY A 13 19538 11703 14008 2206 -5005 -1294 C
ATOM 3 C GLY A 13 -9.170 -19.389 9.832 1.00145.79 C
ANISOU 3 C GLY A 13 22929 15109 17357 2163 -4893 -1253 C
ATOM 4 O GLY A 13 -9.141 -18.168 9.973 1.00142.47 O
ANISOU 4 O GLY A 13 22585 14729 16819 2160 -4738 -1213 O
ATOM 5 N VAL A 14 -8.250 -20.205 10.352 1.00155.28 N
ANISOU 5 N VAL A 14 24053 16285 18660 2133 -4968 -1264 N
ATOM 6 CA VAL A 14 -7.133 -19.669 11.125 1.00150.29 C
ANISOU 6 CA VAL A 14 23425 15674 18006 2094 -4873 -1231 C
ATOM 7 C VAL A 14 -6.121 -18.991 10.204 1.00154.68 C
ANISOU 7 C VAL A 14 24060 16276 18434 2265 -4689 -1304 C
ATOM 8 O VAL A 14 -5.542 -17.954 10.551 1.00140.09 O
ANISOU 8 O VAL A 14 22216 14459 16552 2234 -4445 -1268 O
ATOM 9 CB VAL A 14 -6.487 -20.783 11.972 1.00144.86 C
ANISOU 9 CB VAL A 14 22611 14945 17485 2001 -4985 -1219 C
ATOM 10 CG1 VAL A 14 -5.169 -20.315 12.578 1.00135.00 C
ANISOU 10 CG1 VAL A 14 21336 13716 16241 1975 -4821 -1210 C
ATOM 11 CG2 VAL A 14 -7.441 -21.229 13.071 1.00134.66 C
ANISOU 11 CG2 VAL A 14 21195 13620 16349 1793 -5038 -1121 C
ATOM 12 N GLU A 15 -5.892 -19.560 9.017 1.00171.69 N
ANISOU 12 N GLU A 15 26268 18440 20528 2448 -4785 -1404 N
ATOM 13 CA GLU A 15 -5.070 -18.890 8.015 1.00155.94 C
ANISOU 13 CA GLU A 15 24345 16502 18402 2620 -4597 -1473 C
ATOM 14 C GLU A 15 -5.817 -17.737 7.354 1.00147.51 C
ANISOU 14 C GLU A 15 23379 15483 17187 2692 -4453 -1451 C
ATOM 15 O GLU A 15 -5.185 -16.771 6.910 1.00155.43 O
ANISOU 15 O GLU A 15 24427 16539 18090 2779 -4217 -1458 O
ATOM 16 CB GLU A 15 -4.593 -19.896 6.962 1.00166.31 C
ANISOU 16 CB GLU A 15 25674 17820 19697 2794 -4750 -1587 C
ATOM 17 CG GLU A 15 -3.567 -19.357 5.964 1.00165.28 C
ANISOU 17 CG GLU A 15 25598 17757 19442 2971 -4565 -1662 C
ATOM 18 CD GLU A 15 -4.208 -18.709 4.750 1.00174.17 C
ANISOU 18 CD GLU A 15 26833 18942 20403 3136 -4508 -1691 C
ATOM 19 OE1 GLU A 15 -5.381 -19.022 4.461 1.00182.87 O
ANISOU 19 OE1 GLU A 15 27968 20023 21492 3149 -4676 -1687 O
ATOM 20 OE2 GLU A 15 -3.542 -17.883 4.088 1.00173.31 O
ANISOU 20 OE2 GLU A 15 26771 18902 20177 3254 -4295 -1714 O
ATOM 21 N PHE A 16 -7.149 -17.813 7.281 1.00110.42 N
ANISOU 21 N PHE A 16 18713 10767 12474 2658 -4586 -1423 N
ATOM 22 CA PHE A 16 -7.922 -16.681 6.779 1.00114.18 C
ANISOU 22 CA PHE A 16 19281 11286 12815 2708 -4442 -1393 C
ATOM 23 C PHE A 16 -7.788 -15.479 7.706 1.00124.90 C
ANISOU 23 C PHE A 16 20617 12655 14183 2574 -4194 -1292 C
ATOM 24 O PHE A 16 -7.772 -14.329 7.249 1.00100.21 O
ANISOU 24 O PHE A 16 17556 9578 10940 2650 -3974 -1268 O
ATOM 25 CB PHE A 16 -9.390 -17.076 6.611 1.00108.55 C
ANISOU 25 CB PHE A 16 18572 10545 12127 2664 -4605 -1386 C
ATOM 26 N ILE A 17 -7.690 -15.729 9.015 1.00136.42 N
ANISOU 26 N ILE A 17 21978 14072 15782 2380 -4225 -1225 N
ATOM 27 CA ILE A 17 -7.383 -14.661 9.964 1.00115.12 C
ANISOU 27 CA ILE A 17 19243 11386 13113 2256 -3991 -1133 C
ATOM 28 C ILE A 17 -5.993 -14.098 9.692 1.00109.62 C
ANISOU 28 C ILE A 17 18550 10724 12377 2349 -3770 -1163 C
ATOM 29 O ILE A 17 -5.788 -12.878 9.695 1.00115.83 O
ANISOU 29 O ILE A 17 19364 11546 13101 2363 -3522 -1115 O
ATOM 30 CB ILE A 17 -7.516 -15.177 11.411 1.00118.68 C
ANISOU 30 CB ILE A 17 19577 11794 13724 2039 -4090 -1062 C
ATOM 31 CG1 ILE A 17 -8.963 -15.576 11.722 1.00121.11 C
ANISOU 31 CG1 ILE A 17 19874 12076 14066 1932 -4279 -1022 C
ATOM 32 CG2 ILE A 17 -7.017 -14.142 12.404 1.00112.12 C
ANISOU 32 CG2 ILE A 17 18694 10979 12929 1922 -3850 -975 C
ATOM 33 CD1 ILE A 17 -9.992 -14.528 11.352 1.00107.78 C
ANISOU 33 CD1 ILE A 17 18263 10415 12273 1943 -4164 -983 C
ATOM 34 N SER A 18 -5.019 -14.979 9.438 1.00111.64 N
ANISOU 34 N SER A 18 18773 10972 12673 2416 -3854 -1243 N
ATOM 35 CA SER A 18 -3.664 -14.530 9.130 1.00 95.84 C
ANISOU 35 CA SER A 18 16770 9007 10637 2505 -3654 -1282 C
ATOM 36 C SER A 18 -3.614 -13.746 7.826 1.00 99.51 C
ANISOU 36 C SER A 18 17336 9536 10936 2700 -3503 -1320 C
ATOM 37 O SER A 18 -2.745 -12.883 7.655 1.00 92.56 O
ANISOU 37 O SER A 18 16461 8698 10008 2754 -3264 -1314 O
ATOM 38 CB SER A 18 -2.716 -15.729 9.062 1.00108.00 C
ANISOU 38 CB SER A 18 18256 10528 12252 2540 -3797 -1366 C
ATOM 39 OG SER A 18 -1.424 -15.337 8.630 1.00 90.95 O
ANISOU 39 OG SER A 18 16099 8409 10049 2639 -3613 -1415 O
ATOM 40 N LEU A 19 -4.524 -14.039 6.892 1.00105.50 N
ANISOU 40 N LEU A 19 18170 10309 11607 2811 -3639 -1358 N
ATOM 41 CA LEU A 19 -4.599 -13.251 5.667 1.00114.92 C
ANISOU 41 CA LEU A 19 19458 11574 12632 2998 -3494 -1381 C
ATOM 42 C LEU A 19 -4.956 -11.803 5.976 1.00116.30 C
ANISOU 42 C LEU A 19 19662 11775 12753 2951 -3244 -1280 C
ATOM 43 O LEU A 19 -4.385 -10.874 5.392 1.00103.38 O
ANISOU 43 O LEU A 19 18060 10200 11020 3062 -3011 -1272 O
ATOM 44 CB LEU A 19 -5.619 -13.864 4.705 1.00114.81 C
ANISOU 44 CB LEU A 19 19513 11568 12541 3114 -3703 -1436 C
ATOM 45 CG LEU A 19 -5.773 -13.171 3.348 1.00102.04 C
ANISOU 45 CG LEU A 19 17994 10035 10741 3326 -3581 -1465 C
ATOM 46 CD1 LEU A 19 -4.464 -13.208 2.568 1.00107.14 C
ANISOU 46 CD1 LEU A 19 18636 10742 11332 3480 -3471 -1535 C
ATOM 47 CD2 LEU A 19 -6.905 -13.793 2.539 1.00 99.37 C
ANISOU 47 CD2 LEU A 19 17717 9699 10340 3420 -3805 -1514 C
ATOM 48 N LEU A 20 -5.899 -11.590 6.895 1.00112.85 N
ANISOU 48 N LEU A 20 19203 11295 12381 2785 -3284 -1198 N
ATOM 49 CA LEU A 20 -6.174 -10.235 7.356 1.00 99.19 C
ANISOU 49 CA LEU A 20 17482 9584 10624 2719 -3045 -1094 C
ATOM 50 C LEU A 20 -4.958 -9.631 8.041 1.00 92.20 C
ANISOU 50 C LEU A 20 16529 8702 9801 2657 -2829 -1061 C
ATOM 51 O LEU A 20 -4.738 -8.420 7.959 1.00 82.23 O
ANISOU 51 O LEU A 20 15285 7478 8480 2685 -2575 -1004 O
ATOM 52 CB LEU A 20 -7.374 -10.233 8.304 1.00114.75 C
ANISOU 52 CB LEU A 20 19424 11509 12668 2537 -3146 -1013 C
ATOM 53 CG LEU A 20 -8.705 -10.721 7.730 1.00121.71 C
ANISOU 53 CG LEU A 20 20366 12383 13495 2572 -3348 -1038 C
ATOM 54 CD1 LEU A 20 -9.749 -10.848 8.828 1.00110.29 C
ANISOU 54 CD1 LEU A 20 18862 10892 12152 2363 -3453 -961 C
ATOM 55 CD2 LEU A 20 -9.188 -9.784 6.633 1.00120.25 C
ANISOU 55 CD2 LEU A 20 20286 12261 13142 2734 -3203 -1031 C
ATOM 56 N ALA A 21 -4.149 -10.457 8.707 1.00 90.85 N
ANISOU 56 N ALA A 21 16276 8493 9750 2575 -2923 -1097 N
ATOM 57 CA ALA A 21 -3.003 -9.932 9.439 1.00 93.61 C
ANISOU 57 CA ALA A 21 16553 8843 10170 2505 -2729 -1071 C
ATOM 58 C ALA A 21 -1.932 -9.409 8.489 1.00 87.52 C
ANISOU 58 C ALA A 21 15816 8133 9307 2674 -2535 -1121 C
ATOM 59 O ALA A 21 -1.402 -8.308 8.682 1.00 88.43 O
ANISOU 59 O ALA A 21 15916 8274 9409 2666 -2281 -1070 O
ATOM 60 CB ALA A 21 -2.430 -11.008 10.363 1.00 68.24 C
ANISOU 60 CB ALA A 21 13244 5581 7105 2382 -2889 -1098 C
ATOM 61 N ILE A 22 -1.607 -10.178 7.449 1.00 78.57 N
ANISOU 61 N ILE A 22 14720 7025 8110 2828 -2648 -1218 N
ATOM 62 CA ILE A 22 -0.517 -9.783 6.563 1.00 84.12 C
ANISOU 62 CA ILE A 22 15439 7792 8731 2985 -2474 -1267 C
ATOM 63 C ILE A 22 -0.876 -8.512 5.801 1.00 86.47 C
ANISOU 63 C ILE A 22 15807 8156 8890 3096 -2252 -1213 C
ATOM 64 O ILE A 22 -0.019 -7.652 5.570 1.00 62.08 O
ANISOU 64 O ILE A 22 12706 5116 5767 3151 -2011 -1193 O
ATOM 65 CB ILE A 22 -0.140 -10.943 5.619 1.00105.09 C
ANISOU 65 CB ILE A 22 18114 10465 11350 3125 -2660 -1382 C
ATOM 66 CG1 ILE A 22 1.087 -10.581 4.777 1.00 95.31 C
ANISOU 66 CG1 ILE A 22 16877 9298 10037 3275 -2479 -1430 C
ATOM 67 CG2 ILE A 22 -1.311 -11.335 4.726 1.00111.90 C
ANISOU 67 CG2 ILE A 22 19059 11343 12116 3231 -2832 -1410 C
ATOM 68 CD1 ILE A 22 1.554 -11.700 3.873 1.00 74.71 C
ANISOU 68 CD1 ILE A 22 14279 6712 7395 3413 -2651 -1543 C
ATOM 69 N ILE A 23 -2.148 -8.352 5.423 1.00 93.20 N
ANISOU 69 N ILE A 23 16731 9015 9667 3126 -2326 -1182 N
ATOM 70 CA ILE A 23 -2.538 -7.142 4.707 1.00 86.73 C
ANISOU 70 CA ILE A 23 15978 8263 8714 3233 -2114 -1122 C
ATOM 71 C ILE A 23 -2.575 -5.950 5.655 1.00 87.33 C
ANISOU 71 C ILE A 23 16015 8323 8842 3098 -1892 -1010 C
ATOM 72 O ILE A 23 -2.135 -4.850 5.302 1.00 83.53 O
ANISOU 72 O ILE A 23 15541 7898 8298 3166 -1634 -961 O
ATOM 73 CB ILE A 23 -3.882 -7.342 3.977 1.00 82.96 C
ANISOU 73 CB ILE A 23 15588 7801 8134 3315 -2261 -1127 C
ATOM 74 CG1 ILE A 23 -5.003 -7.700 4.957 1.00 92.10 C
ANISOU 74 CG1 ILE A 23 16730 8879 9383 3138 -2435 -1083 C
ATOM 75 CG2 ILE A 23 -3.746 -8.412 2.906 1.00 80.72 C
ANISOU 75 CG2 ILE A 23 15339 7546 7786 3474 -2455 -1241 C
ATOM 76 CD1 ILE A 23 -6.373 -7.822 4.319 1.00 80.61 C
ANISOU 76 CD1 ILE A 23 15358 7436 7835 3202 -2571 -1083 C
ATOM 77 N LEU A 24 -3.078 -6.151 6.878 1.00 87.60 N
ANISOU 77 N LEU A 24 16001 8285 8998 2905 -1986 -963 N
ATOM 78 CA LEU A 24 -3.140 -5.059 7.846 1.00 60.51 C
ANISOU 78 CA LEU A 24 12525 4840 5626 2769 -1789 -858 C
ATOM 79 C LEU A 24 -1.745 -4.578 8.225 1.00 71.57 C
ANISOU 79 C LEU A 24 13854 6251 7087 2747 -1586 -860 C
ATOM 80 O LEU A 24 -1.499 -3.369 8.314 1.00 71.84 O
ANISOU 80 O LEU A 24 13877 6317 7102 2746 -1333 -790 O
ATOM 81 CB LEU A 24 -3.913 -5.501 9.088 1.00 61.81 C
ANISOU 81 CB LEU A 24 12638 4934 5912 2565 -1952 -812 C
ATOM 82 CG LEU A 24 -5.437 -5.574 8.973 1.00 70.71 C
ANISOU 82 CG LEU A 24 13821 6052 6994 2540 -2088 -771 C
ATOM 83 CD1 LEU A 24 -6.019 -6.327 10.159 1.00 70.92 C
ANISOU 83 CD1 LEU A 24 13776 6016 7155 2341 -2291 -744 C
ATOM 84 CD2 LEU A 24 -6.039 -4.182 8.873 1.00 64.60 C
ANISOU 84 CD2 LEU A 24 13084 5317 6146 2550 -1864 -670 C
ATOM 85 N LEU A 25 -0.815 -5.507 8.452 1.00 67.88 N
ANISOU 85 N LEU A 25 13332 5760 6698 2729 -1693 -938 N
ATOM 86 CA LEU A 25 0.563 -5.106 8.710 1.00 69.38 C
ANISOU 86 CA LEU A 25 13454 5966 6942 2722 -1507 -951 C
ATOM 87 C LEU A 25 1.180 -4.450 7.484 1.00 89.77 C
ANISOU 87 C LEU A 25 16078 8629 9401 2910 -1314 -968 C
ATOM 88 O LEU A 25 1.951 -3.491 7.608 1.00 90.92 O
ANISOU 88 O LEU A 25 16182 8804 9559 2907 -1069 -928 O
ATOM 89 CB LEU A 25 1.397 -6.310 9.140 1.00 70.20 C
ANISOU 89 CB LEU A 25 13494 6031 7149 2673 -1674 -1034 C
ATOM 90 CG LEU A 25 1.558 -6.525 10.644 1.00 64.97 C
ANISOU 90 CG LEU A 25 12736 5305 6643 2467 -1719 -1000 C
ATOM 91 CD1 LEU A 25 0.320 -7.174 11.235 1.00 80.79 C
ANISOU 91 CD1 LEU A 25 14745 7260 8691 2354 -1948 -967 C
ATOM 92 CD2 LEU A 25 2.803 -7.349 10.930 1.00 70.23 C
ANISOU 92 CD2 LEU A 25 13331 5956 7396 2451 -1775 -1077 C
ATOM 93 N SER A 26 0.857 -4.955 6.291 1.00 94.85 N
ANISOU 93 N SER A 26 16796 9316 9927 3073 -1422 -1024 N
ATOM 94 CA SER A 26 1.438 -4.393 5.079 1.00 86.80 C
ANISOU 94 CA SER A 26 15809 8386 8784 3257 -1248 -1036 C
ATOM 95 C SER A 26 0.859 -3.015 4.783 1.00 80.30 C
ANISOU 95 C SER A 26 15023 7611 7874 3294 -1021 -931 C
ATOM 96 O SER A 26 1.604 -2.073 4.489 1.00 86.23 O
ANISOU 96 O SER A 26 15746 8417 8599 3345 -773 -890 O
ATOM 97 CB SER A 26 1.225 -5.340 3.899 1.00 72.52 C
ANISOU 97 CB SER A 26 14065 6617 6873 3422 -1436 -1126 C
ATOM 98 OG SER A 26 1.946 -4.903 2.760 1.00 82.87 O
ANISOU 98 OG SER A 26 15391 8021 8074 3598 -1277 -1141 O
ATOM 99 N VAL A 27 -0.468 -2.871 4.868 1.00 79.78 N
ANISOU 99 N VAL A 27 15016 7527 7769 3264 -1100 -882 N
ATOM 100 CA VAL A 27 -1.074 -1.566 4.604 1.00 90.66 C
ANISOU 100 CA VAL A 27 16429 8951 9065 3297 -887 -778 C
ATOM 101 C VAL A 27 -0.627 -0.553 5.649 1.00 83.80 C
ANISOU 101 C VAL A 27 15484 8057 8300 3153 -668 -694 C
ATOM 102 O VAL A 27 -0.389 0.618 5.332 1.00 88.74 O
ANISOU 102 O VAL A 27 16101 8738 8878 3201 -413 -620 O
ATOM 103 CB VAL A 27 -2.611 -1.669 4.522 1.00 77.12 C
ANISOU 103 CB VAL A 27 14791 7219 7293 3287 -1029 -745 C
ATOM 104 CG1 VAL A 27 -3.231 -1.974 5.878 1.00 78.81 C
ANISOU 104 CG1 VAL A 27 14965 7340 7639 3076 -1161 -715 C
ATOM 105 CG2 VAL A 27 -3.194 -0.381 3.957 1.00 75.86 C
ANISOU 105 CG2 VAL A 27 14678 7126 7020 3366 -808 -646 C
ATOM 106 N ALA A 28 -0.481 -0.986 6.903 1.00 68.62 N
ANISOU 106 N ALA A 28 13496 6054 6521 2975 -763 -702 N
ATOM 107 CA ALA A 28 0.045 -0.088 7.924 1.00 75.63 C
ANISOU 107 CA ALA A 28 14301 6921 7515 2839 -566 -635 C
ATOM 108 C ALA A 28 1.474 0.319 7.596 1.00 77.03 C
ANISOU 108 C ALA A 28 14422 7143 7705 2905 -371 -659 C
ATOM 109 O ALA A 28 1.853 1.481 7.767 1.00 86.86 O
ANISOU 109 O ALA A 28 15624 8414 8965 2883 -121 -587 O
ATOM 110 CB ALA A 28 -0.030 -0.744 9.301 1.00 79.17 C
ANISOU 110 CB ALA A 28 14683 7285 8112 2643 -724 -646 C
ATOM 111 N LEU A 29 2.278 -0.627 7.108 1.00 74.21 N
ANISOU 111 N LEU A 29 14058 6795 7344 2983 -483 -758 N
ATOM 112 CA LEU A 29 3.634 -0.298 6.685 1.00 75.87 C
ANISOU 112 CA LEU A 29 14215 7054 7558 3056 -309 -783 C
ATOM 113 C LEU A 29 3.628 0.686 5.523 1.00 78.92 C
ANISOU 113 C LEU A 29 14640 7534 7813 3212 -100 -726 C
ATOM 114 O LEU A 29 4.481 1.579 5.451 1.00 70.94 O
ANISOU 114 O LEU A 29 13569 6562 6821 3223 135 -683 O
ATOM 115 CB LEU A 29 4.381 -1.572 6.298 1.00 68.75 C
ANISOU 115 CB LEU A 29 13308 6149 6666 3121 -489 -901 C
ATOM 116 CG LEU A 29 5.315 -2.161 7.350 1.00 61.56 C
ANISOU 116 CG LEU A 29 12307 5177 5907 2989 -548 -952 C
ATOM 117 CD1 LEU A 29 5.806 -3.521 6.902 1.00 71.05 C
ANISOU 117 CD1 LEU A 29 13517 6374 7105 3058 -760 -1065 C
ATOM 118 CD2 LEU A 29 6.482 -1.219 7.580 1.00 75.68 C
ANISOU 118 CD2 LEU A 29 14013 6993 7750 2967 -286 -922 C
ATOM 119 N ALA A 30 2.672 0.539 4.604 1.00 87.72 N
ANISOU 119 N ALA A 30 15846 8688 8795 3333 -183 -721 N
ATOM 120 CA ALA A 30 2.631 1.396 3.423 1.00 80.98 C
ANISOU 120 CA ALA A 30 15028 7933 7807 3492 0 -663 C
ATOM 121 C ALA A 30 2.149 2.799 3.761 1.00 86.40 C
ANISOU 121 C ALA A 30 15701 8631 8495 3432 231 -534 C
ATOM 122 O ALA A 30 2.632 3.779 3.183 1.00 92.07 O
ANISOU 122 O ALA A 30 16392 9421 9171 3505 465 -467 O
ATOM 123 CB ALA A 30 1.735 0.773 2.353 1.00 79.19 C
ANISOU 123 CB ALA A 30 14902 7748 7438 3641 -170 -701 C
ATOM 124 N VAL A 31 1.193 2.921 4.677 1.00 89.49 N
ANISOU 124 N VAL A 31 16106 8958 8938 3299 169 -493 N
ATOM 125 CA VAL A 31 0.711 4.245 5.042 1.00 85.65 C
ANISOU 125 CA VAL A 31 15603 8482 8459 3236 385 -371 C
ATOM 126 C VAL A 31 1.493 4.806 6.224 1.00 87.02 C
ANISOU 126 C VAL A 31 15669 8608 8785 3074 524 -343 C
ATOM 127 O VAL A 31 1.612 6.027 6.366 1.00 95.33 O
ANISOU 127 O VAL A 31 16678 9688 9855 3044 763 -249 O
ATOM 128 CB VAL A 31 -0.799 4.199 5.333 1.00 78.04 C
ANISOU 128 CB VAL A 31 14710 7483 7459 3186 261 -332 C
ATOM 129 CG1 VAL A 31 -1.092 3.335 6.544 1.00 74.31 C
ANISOU 129 CG1 VAL A 31 14214 6912 7109 3016 45 -378 C
ATOM 130 CG2 VAL A 31 -1.354 5.598 5.522 1.00 54.57 C
ANISOU 130 CG2 VAL A 31 11728 4534 4472 3147 491 -203 C
ATOM 131 N GLY A 32 2.060 3.939 7.056 1.00 78.03 N
ANISOU 131 N GLY A 32 14483 7405 7760 2971 381 -422 N
ATOM 132 CA GLY A 32 2.705 4.386 8.271 1.00 82.71 C
ANISOU 132 CA GLY A 32 14974 7951 8501 2809 485 -401 C
ATOM 133 C GLY A 32 4.120 4.882 8.081 1.00 75.42 C
ANISOU 133 C GLY A 32 13968 7067 7622 2841 680 -410 C
ATOM 134 O GLY A 32 4.439 6.017 8.442 1.00 89.07 O
ANISOU 134 O GLY A 32 15631 8810 9403 2783 905 -335 O
ATOM 135 N LEU A 33 4.979 4.033 7.519 1.00 74.75 N
ANISOU 135 N LEU A 33 13881 6999 7523 2928 592 -501 N
ATOM 136 CA LEU A 33 6.389 4.392 7.399 1.00 81.37 C
ANISOU 136 CA LEU A 33 14634 7869 8415 2948 756 -518 C
ATOM 137 C LEU A 33 6.617 5.639 6.550 1.00 79.94 C
ANISOU 137 C LEU A 33 14440 7770 8166 3043 1017 -426 C
ATOM 138 O LEU A 33 7.431 6.487 6.958 1.00 76.39 O
ANISOU 138 O LEU A 33 13897 7326 7802 2979 1213 -384 O
ATOM 139 CB LEU A 33 7.185 3.198 6.860 1.00 62.76 C
ANISOU 139 CB LEU A 33 12286 5520 6042 3036 600 -633 C
ATOM 140 CG LEU A 33 8.549 2.989 7.524 1.00 75.18 C
ANISOU 140 CG LEU A 33 13755 7066 7743 2959 640 -690 C
ATOM 141 CD1 LEU A 33 8.563 1.715 8.365 1.00 61.96 C
ANISOU 141 CD1 LEU A 33 12073 5315 6154 2863 391 -779 C
ATOM 142 CD2 LEU A 33 9.671 2.982 6.495 1.00 68.26 C
ANISOU 142 CD2 LEU A 33 12858 6260 6819 3097 734 -724 C
ATOM 143 N PRO A 34 5.973 5.818 5.391 1.00 78.10 N
ANISOU 143 N PRO A 34 14286 7602 7787 3190 1032 -388 N
ATOM 144 CA PRO A 34 6.111 7.111 4.697 1.00 61.76 C
ANISOU 144 CA PRO A 34 12192 5606 5667 3258 1288 -278 C
ATOM 145 C PRO A 34 5.568 8.270 5.509 1.00 70.15 C
ANISOU 145 C PRO A 34 13217 6644 6795 3132 1449 -170 C
ATOM 146 O PRO A 34 6.226 9.312 5.620 1.00 81.98 O
ANISOU 146 O PRO A 34 14631 8163 8354 3096 1670 -100 O
ATOM 147 CB PRO A 34 5.321 6.891 3.399 1.00 69.48 C
ANISOU 147 CB PRO A 34 13273 6652 6474 3433 1222 -265 C
ATOM 148 CG PRO A 34 5.348 5.419 3.184 1.00 79.03 C
ANISOU 148 CG PRO A 34 14536 7840 7651 3487 958 -394 C
ATOM 149 CD PRO A 34 5.241 4.842 4.566 1.00 81.40 C
ANISOU 149 CD PRO A 34 14809 8038 8083 3311 819 -446 C
ATOM 150 N GLY A 35 4.383 8.113 6.092 1.00 73.39 N
ANISOU 150 N GLY A 35 13682 7006 7198 3059 1337 -156 N
ATOM 151 CA GLY A 35 3.757 9.190 6.831 1.00 74.01 C
ANISOU 151 CA GLY A 35 13730 7064 7328 2944 1480 -54 C
ATOM 152 C GLY A 35 4.492 9.566 8.100 1.00 74.81 C
ANISOU 152 C GLY A 35 13719 7112 7594 2775 1564 -57 C
ATOM 153 O GLY A 35 4.827 10.735 8.306 1.00 71.40 O
ANISOU 153 O GLY A 35 13212 6699 7218 2727 1787 26 O
ATOM 154 N ASN A 36 4.756 8.578 8.958 1.00 69.04 N
ANISOU 154 N ASN A 36 12970 6316 6947 2683 1382 -151 N
ATOM 155 CA ASN A 36 5.379 8.875 10.244 1.00 75.15 C
ANISOU 155 CA ASN A 36 13636 7040 7878 2518 1442 -158 C
ATOM 156 C ASN A 36 6.761 9.489 10.050 1.00 75.98 C
ANISOU 156 C ASN A 36 13643 7181 8043 2536 1636 -154 C
ATOM 157 O ASN A 36 7.162 10.391 10.794 1.00 85.40 O
ANISOU 157 O ASN A 36 14742 8365 9340 2428 1797 -107 O
ATOM 158 CB ASN A 36 5.460 7.611 11.102 1.00 52.58 C
ANISOU 158 CB ASN A 36 10774 4110 5092 2428 1198 -257 C
ATOM 159 CG ASN A 36 4.124 7.244 11.714 1.00 73.83 C
ANISOU 159 CG ASN A 36 13524 6753 7775 2344 1031 -237 C
ATOM 160 OD1 ASN A 36 3.653 7.894 12.651 1.00 67.66 O
ANISOU 160 OD1 ASN A 36 12699 5946 7062 2214 1095 -176 O
ATOM 161 ND2 ASN A 36 3.497 6.202 11.178 1.00 80.46 N
ANISOU 161 ND2 ASN A 36 14457 7583 8533 2418 811 -286 N
ATOM 162 N SER A 37 7.501 9.029 9.041 1.00 66.52 N
ANISOU 162 N SER A 37 12463 6028 6784 2671 1621 -203 N
ATOM 163 CA SER A 37 8.850 9.543 8.846 1.00 72.16 C
ANISOU 163 CA SER A 37 13083 6775 7560 2687 1789 -202 C
ATOM 164 C SER A 37 8.847 10.883 8.114 1.00 78.32 C
ANISOU 164 C SER A 37 13840 7618 8299 2745 2032 -80 C
ATOM 165 O SER A 37 9.756 11.698 8.316 1.00 66.92 O
ANISOU 165 O SER A 37 12297 6186 6945 2699 2208 -43 O
ATOM 166 CB SER A 37 9.700 8.510 8.104 1.00 84.39 C
ANISOU 166 CB SER A 37 14651 8347 9067 2800 1675 -302 C
ATOM 167 OG SER A 37 11.074 8.707 8.397 1.00 91.64 O
ANISOU 167 OG SER A 37 15464 9267 10089 2761 1777 -333 O
ATOM 168 N PHE A 38 7.843 11.131 7.268 1.00 75.86 N
ANISOU 168 N PHE A 38 13616 7347 7860 2844 2039 -14 N
ATOM 169 CA PHE A 38 7.666 12.470 6.713 1.00 73.48 C
ANISOU 169 CA PHE A 38 13290 7095 7533 2878 2264 118 C
ATOM 170 C PHE A 38 7.435 13.484 7.825 1.00 77.18 C
ANISOU 170 C PHE A 38 13683 7523 8120 2715 2397 190 C
ATOM 171 O PHE A 38 7.914 14.622 7.752 1.00 73.47 O
ANISOU 171 O PHE A 38 13133 7072 7711 2689 2602 278 O
ATOM 172 CB PHE A 38 6.508 12.475 5.714 1.00 65.73 C
ANISOU 172 CB PHE A 38 12419 6160 6394 3006 2224 172 C
ATOM 173 CG PHE A 38 6.081 13.850 5.277 1.00 61.23 C
ANISOU 173 CG PHE A 38 11830 5628 5805 3023 2435 320 C
ATOM 174 CD1 PHE A 38 7.004 14.761 4.783 1.00 74.26 C
ANISOU 174 CD1 PHE A 38 13399 7317 7502 3051 2630 392 C
ATOM 175 CD2 PHE A 38 4.749 14.222 5.341 1.00 64.00 C
ANISOU 175 CD2 PHE A 38 12245 5975 6097 3012 2429 390 C
ATOM 176 CE1 PHE A 38 6.605 16.021 4.383 1.00 80.36 C
ANISOU 176 CE1 PHE A 38 14148 8113 8272 3062 2810 533 C
ATOM 177 CE2 PHE A 38 4.346 15.474 4.940 1.00 85.19 C
ANISOU 177 CE2 PHE A 38 14907 8688 8771 3027 2615 529 C
ATOM 178 CZ PHE A 38 5.274 16.376 4.461 1.00 65.00 C
ANISOU 178 CZ PHE A 38 12265 6161 6271 3051 2801 602 C
ATOM 179 N VAL A 39 6.723 13.077 8.875 1.00 73.84 N
ANISOU 179 N VAL A 39 13278 7039 7738 2601 2275 154 N
ATOM 180 CA VAL A 39 6.548 13.939 10.039 1.00 60.36 C
ANISOU 180 CA VAL A 39 11492 5294 6149 2438 2383 207 C
ATOM 181 C VAL A 39 7.890 14.191 10.710 1.00 60.20 C
ANISOU 181 C VAL A 39 11345 5257 6272 2349 2472 171 C
ATOM 182 O VAL A 39 8.246 15.333 11.026 1.00 66.40 O
ANISOU 182 O VAL A 39 12040 6046 7142 2280 2662 246 O
ATOM 183 CB VAL A 39 5.537 13.308 11.010 1.00 56.48 C
ANISOU 183 CB VAL A 39 11047 4745 5669 2337 2206 167 C
ATOM 184 CG1 VAL A 39 5.420 14.140 12.277 1.00 53.90 C
ANISOU 184 CG1 VAL A 39 10628 4383 5468 2166 2309 211 C
ATOM 185 CG2 VAL A 39 4.187 13.164 10.335 1.00 69.80 C
ANISOU 185 CG2 VAL A 39 12855 6449 7215 2423 2129 210 C
ATOM 186 N VAL A 40 8.668 13.127 10.910 1.00 56.68 N
ANISOU 186 N VAL A 40 10891 4790 5857 2353 2331 56 N
ATOM 187 CA VAL A 40 9.941 13.255 11.607 1.00 54.37 C
ANISOU 187 CA VAL A 40 10480 4480 5700 2268 2393 10 C
ATOM 188 C VAL A 40 10.907 14.129 10.818 1.00 71.94 C
ANISOU 188 C VAL A 40 12641 6755 7938 2334 2593 68 C
ATOM 189 O VAL A 40 11.610 14.968 11.393 1.00 73.69 O
ANISOU 189 O VAL A 40 12754 6968 8277 2242 2737 99 O
ATOM 190 CB VAL A 40 10.526 11.860 11.887 1.00 50.90 C
ANISOU 190 CB VAL A 40 10051 4007 5279 2271 2188 -124 C
ATOM 191 CG1 VAL A 40 11.876 11.982 12.574 1.00 64.68 C
ANISOU 191 CG1 VAL A 40 11675 5739 7160 2191 2253 -173 C
ATOM 192 CG2 VAL A 40 9.569 11.062 12.744 1.00 67.90 C
ANISOU 192 CG2 VAL A 40 12257 6103 7439 2188 1987 -166 C
ATOM 193 N TRP A 41 10.955 13.961 9.494 1.00 87.49 N
ANISOU 193 N TRP A 41 14674 8777 9790 2493 2599 85 N
ATOM 194 CA TRP A 41 11.871 14.764 8.689 1.00 89.04 C
ANISOU 194 CA TRP A 41 14812 9020 9998 2560 2777 146 C
ATOM 195 C TRP A 41 11.493 16.241 8.729 1.00 95.90 C
ANISOU 195 C TRP A 41 15633 9894 10910 2508 2979 286 C
ATOM 196 O TRP A 41 12.369 17.113 8.764 1.00104.71 O
ANISOU 196 O TRP A 41 16652 11011 12120 2470 3136 334 O
ATOM 197 CB TRP A 41 11.895 14.251 7.249 1.00 85.76 C
ANISOU 197 CB TRP A 41 14479 8666 9439 2746 2730 138 C
ATOM 198 CG TRP A 41 12.584 15.170 6.283 1.00 99.29 C
ANISOU 198 CG TRP A 41 16147 10433 11146 2827 2914 227 C
ATOM 199 CD1 TRP A 41 13.921 15.223 6.005 1.00103.75 C
ANISOU 199 CD1 TRP A 41 16639 11017 11765 2852 2982 200 C
ATOM 200 CD2 TRP A 41 11.964 16.163 5.458 1.00112.87 C
ANISOU 200 CD2 TRP A 41 17890 12191 12803 2894 3046 361 C
ATOM 201 NE1 TRP A 41 14.170 16.191 5.061 1.00101.43 N
ANISOU 201 NE1 TRP A 41 16322 10768 11448 2929 3147 310 N
ATOM 202 CE2 TRP A 41 12.985 16.782 4.709 1.00106.52 C
ANISOU 202 CE2 TRP A 41 17025 11425 12025 2955 3187 412 C
ATOM 203 CE3 TRP A 41 10.644 16.590 5.282 1.00106.06 C
ANISOU 203 CE3 TRP A 41 17095 11332 11870 2907 3055 446 C
ATOM 204 CZ2 TRP A 41 12.726 17.805 3.798 1.00 95.11 C
ANISOU 204 CZ2 TRP A 41 15581 10016 10542 3029 3330 545 C
ATOM 205 CZ3 TRP A 41 10.390 17.605 4.379 1.00 96.00 C
ANISOU 205 CZ3 TRP A 41 15821 10097 10557 2981 3200 576 C
ATOM 206 CH2 TRP A 41 11.425 18.201 3.649 1.00 93.88 C
ANISOU 206 CH2 TRP A 41 15489 9861 10321 3041 3333 626 C
ATOM 207 N SER A 42 10.196 16.545 8.743 1.00 86.02 N
ANISOU 207 N SER A 42 14447 8639 9598 2501 2971 352 N
ATOM 208 CA SER A 42 9.738 17.927 8.721 1.00 80.84 C
ANISOU 208 CA SER A 42 13753 7982 8980 2459 3151 489 C
ATOM 209 C SER A 42 9.835 18.607 10.084 1.00 83.39 C
ANISOU 209 C SER A 42 13977 8252 9455 2277 3225 502 C
ATOM 210 O SER A 42 9.524 19.800 10.188 1.00109.98 O
ANISOU 210 O SER A 42 17300 11608 12879 2225 3373 612 O
ATOM 211 CB SER A 42 8.299 17.984 8.210 1.00 75.68 C
ANISOU 211 CB SER A 42 13206 7346 8201 2524 3112 554 C
ATOM 212 OG SER A 42 7.459 17.152 8.987 1.00 90.47 O
ANISOU 212 OG SER A 42 15140 9187 10047 2465 2946 482 O
ATOM 213 N ILE A 43 10.241 17.879 11.120 1.00 77.70 N
ANISOU 213 N ILE A 43 13220 7498 8806 2182 3118 394 N
ATOM 214 CA ILE A 43 10.524 18.453 12.426 1.00 71.26 C
ANISOU 214 CA ILE A 43 12297 6640 8139 2015 3182 391 C
ATOM 215 C ILE A 43 12.022 18.558 12.671 1.00 91.90 C
ANISOU 215 C ILE A 43 14803 9249 10866 1980 3243 343 C
ATOM 216 O ILE A 43 12.500 19.577 13.169 1.00100.70 O
ANISOU 216 O ILE A 43 15815 10345 12099 1887 3384 394 O
ATOM 217 CB ILE A 43 9.841 17.629 13.540 1.00 77.01 C
ANISOU 217 CB ILE A 43 13052 7330 8876 1920 3015 310 C
ATOM 218 CG1 ILE A 43 8.326 17.606 13.343 1.00 69.00 C
ANISOU 218 CG1 ILE A 43 12142 6319 7756 1946 2960 363 C
ATOM 219 CG2 ILE A 43 10.190 18.190 14.907 1.00 77.73 C
ANISOU 219 CG2 ILE A 43 13025 7389 9120 1751 3077 300 C
ATOM 220 CD1 ILE A 43 7.624 16.668 14.292 1.00 72.87 C
ANISOU 220 CD1 ILE A 43 12673 6769 8244 1868 2767 285 C
ATOM 221 N LEU A 44 12.779 17.511 12.328 1.00 77.69 N
ANISOU 221 N LEU A 44 13024 7462 9032 2052 3131 243 N
ATOM 222 CA LEU A 44 14.228 17.563 12.488 1.00 83.24 C
ANISOU 222 CA LEU A 44 13629 8164 9833 2029 3184 195 C
ATOM 223 C LEU A 44 14.852 18.477 11.447 1.00 88.85 C
ANISOU 223 C LEU A 44 14309 8907 10541 2110 3353 286 C
ATOM 224 O LEU A 44 15.586 19.411 11.783 1.00103.56 O
ANISOU 224 O LEU A 44 16070 10755 12524 2037 3491 329 O
ATOM 225 CB LEU A 44 14.837 16.162 12.377 1.00 84.47 C
ANISOU 225 CB LEU A 44 13819 8323 9952 2089 3012 64 C
ATOM 226 CG LEU A 44 14.305 15.091 13.318 1.00 78.68 C
ANISOU 226 CG LEU A 44 13122 7548 9223 2021 2813 -31 C
ATOM 227 CD1 LEU A 44 14.987 13.790 12.973 1.00 63.23 C
ANISOU 227 CD1 LEU A 44 11200 5594 7232 2099 2655 -148 C
ATOM 228 CD2 LEU A 44 14.553 15.484 14.764 1.00 65.21 C
ANISOU 228 CD2 LEU A 44 11312 5804 7662 1851 2841 -49 C
ATOM 229 N LYS A 45 14.557 18.231 10.171 1.00 77.12 N
ANISOU 229 N LYS A 45 12259 9450 7592 1428 673 -258 N
ATOM 230 CA LYS A 45 15.260 18.924 9.099 1.00101.69 C
ANISOU 230 CA LYS A 45 15422 12547 10667 1438 700 -236 C
ATOM 231 C LYS A 45 14.629 20.275 8.768 1.00101.13 C
ANISOU 231 C LYS A 45 15411 12440 10574 1474 730 -202 C
ATOM 232 O LYS A 45 15.336 21.277 8.624 1.00 98.06 O
ANISOU 232 O LYS A 45 14998 12057 10204 1442 814 -178 O
ATOM 233 CB LYS A 45 15.310 18.029 7.851 1.00109.78 C
ANISOU 233 CB LYS A 45 16548 13545 11618 1498 600 -253 C
ATOM 234 N ARG A 46 13.303 20.322 8.641 1.00103.16 N
ANISOU 234 N ARG A 46 15748 12657 10791 1540 656 -203 N
ATOM 235 CA ARG A 46 12.658 21.533 8.142 1.00127.17 C
ANISOU 235 CA ARG A 46 18865 15657 13795 1587 668 -170 C
ATOM 236 C ARG A 46 12.515 22.588 9.236 1.00121.50 C
ANISOU 236 C ARG A 46 18061 14955 13149 1539 775 -153 C
ATOM 237 O ARG A 46 12.897 23.747 9.042 1.00122.09 O
ANISOU 237 O ARG A 46 18132 15021 13233 1525 855 -122 O
ATOM 238 CB ARG A 46 11.296 21.187 7.532 1.00133.32 C
ANISOU 238 CB ARG A 46 19765 16387 14502 1679 532 -180 C
ATOM 239 CG ARG A 46 10.942 22.005 6.293 1.00129.52 C
ANISOU 239 CG ARG A 46 19408 15859 13944 1749 496 -148 C
ATOM 240 CD ARG A 46 10.312 23.347 6.645 1.00144.62 C
ANISOU 240 CD ARG A 46 21332 17751 15866 1759 558 -115 C
ATOM 241 NE ARG A 46 8.935 23.194 7.105 1.00138.42 N
ANISOU 241 NE ARG A 46 20475 16932 15186 1755 451 -111 N
ATOM 242 CZ ARG A 46 8.118 24.206 7.376 1.00119.42 C
ANISOU 242 CZ ARG A 46 18020 14494 12862 1746 455 -75 C
ATOM 243 NH1 ARG A 46 6.880 23.966 7.788 1.00113.09 N
ANISOU 243 NH1 ARG A 46 17132 13660 12177 1734 348 -73 N
ATOM 244 NH2 ARG A 46 8.536 25.456 7.233 1.00125.32 N
ANISOU 244 NH2 ARG A 46 18801 15236 13577 1749 568 -43 N
ATOM 245 N MET A 47 11.970 22.209 10.390 1.00131.04 N
ANISOU 245 N MET A 47 19194 16186 14409 1514 779 -174 N
ATOM 246 CA MET A 47 11.749 23.151 11.484 1.00136.25 C
ANISOU 246 CA MET A 47 19762 16864 15142 1469 878 -163 C
ATOM 247 C MET A 47 13.045 23.343 12.260 1.00140.07 C
ANISOU 247 C MET A 47 20103 17406 15711 1369 981 -163 C
ATOM 248 O MET A 47 13.492 22.437 12.972 1.00138.02 O
ANISOU 248 O MET A 47 19757 17191 15493 1321 979 -187 O
ATOM 249 CB MET A 47 10.635 22.655 12.401 1.00139.47 C
ANISOU 249 CB MET A 47 20119 17274 15602 1472 829 -181 C
ATOM 250 CG MET A 47 9.244 22.827 11.827 1.00134.19 C
ANISOU 250 CG MET A 47 19464 16537 14986 1508 692 -155 C
ATOM 251 SD MET A 47 7.975 22.155 12.910 1.00133.48 S
ANISOU 251 SD MET A 47 19219 16441 15057 1462 595 -157 S
ATOM 252 CE MET A 47 8.260 23.096 14.402 1.00 96.51 C
ANISOU 252 CE MET A 47 14397 11811 10460 1387 755 -153 C
ATOM 253 N GLN A 48 13.649 24.526 12.128 1.00139.32 N
ANISOU 253 N GLN A 48 19983 17310 15643 1339 1064 -138 N
ATOM 254 CA GLN A 48 14.839 24.831 12.912 1.00139.58 C
ANISOU 254 CA GLN A 48 19876 17398 15760 1244 1149 -145 C
ATOM 255 C GLN A 48 14.500 25.021 14.384 1.00151.34 C
ANISOU 255 C GLN A 48 21235 18928 17338 1188 1200 -159 C
ATOM 256 O GLN A 48 15.357 24.808 15.249 1.00142.22 O
ANISOU 256 O GLN A 48 19952 17832 16252 1109 1237 -178 O
ATOM 257 CB GLN A 48 15.529 26.078 12.359 1.00119.40 C
ANISOU 257 CB GLN A 48 17332 14825 13208 1231 1215 -119 C
ATOM 258 N LYS A 49 13.265 25.412 14.684 1.00142.83 N
ANISOU 258 N LYS A 49 20187 17823 16260 1230 1198 -152 N
ATOM 259 CA LYS A 49 12.798 25.612 16.050 1.00136.19 C
ANISOU 259 CA LYS A 49 19225 17018 15502 1185 1247 -165 C
ATOM 260 C LYS A 49 11.820 24.499 16.401 1.00130.17 C
ANISOU 260 C LYS A 49 18488 16254 14718 1226 1180 -184 C
ATOM 261 O LYS A 49 10.744 24.405 15.802 1.00132.83 O
ANISOU 261 O LYS A 49 18936 16538 14996 1307 1114 -182 O
ATOM 262 CB LYS A 49 12.135 26.981 16.203 1.00118.87 C
ANISOU 262 CB LYS A 49 17033 14795 13338 1200 1308 -146 C
ATOM 263 N ARG A 50 12.194 23.660 17.364 1.00115.95 N
ANISOU 263 N ARG A 50 16578 14510 12968 1169 1186 -205 N
ATOM 264 CA ARG A 50 11.340 22.561 17.814 1.00108.16 C
ANISOU 264 CA ARG A 50 15602 13527 11969 1203 1130 -224 C
ATOM 265 C ARG A 50 10.505 23.057 18.989 1.00 96.45 C
ANISOU 265 C ARG A 50 13996 12061 10589 1168 1166 -219 C
ATOM 266 O ARG A 50 10.998 23.167 20.114 1.00112.32 O
ANISOU 266 O ARG A 50 15889 14135 12653 1105 1251 -231 O
ATOM 267 CB ARG A 50 12.176 21.342 18.191 1.00102.48 C
ANISOU 267 CB ARG A 50 14822 12855 11262 1157 1107 -241 C
ATOM 268 CG ARG A 50 12.848 20.647 17.010 1.00101.60 C
ANISOU 268 CG ARG A 50 14805 12719 11077 1186 1039 -245 C
ATOM 269 CD ARG A 50 13.379 19.269 17.397 1.00116.35 C
ANISOU 269 CD ARG A 50 16630 14625 12954 1159 1004 -266 C
ATOM 270 NE ARG A 50 14.555 19.336 18.262 1.00110.62 N
ANISOU 270 NE ARG A 50 15761 13967 12303 1064 1073 -271 N
ATOM 271 CZ ARG A 50 15.123 18.278 18.834 1.00101.39 C
ANISOU 271 CZ ARG A 50 14527 12841 11156 1027 1061 -288 C
ATOM 272 NH1 ARG A 50 16.193 18.430 19.603 1.00 85.53 N
ANISOU 272 NH1 ARG A 50 12391 10894 9212 943 1113 -296 N
ATOM 273 NH2 ARG A 50 14.619 17.066 18.643 1.00 93.92 N
ANISOU 273 NH2 ARG A 50 13644 11875 10165 1076 989 -300 N
ATOM 274 N SER A 51 9.233 23.355 18.730 1.00 75.34 N
ANISOU 274 N SER A 51 11308 9330 7987 1183 1069 -193 N
ATOM 275 CA SER A 51 8.337 23.841 19.766 1.00 54.54 C
ANISOU 275 CA SER A 51 8538 6705 5478 1139 1078 -183 C
ATOM 276 C SER A 51 7.874 22.692 20.658 1.00 53.90 C
ANISOU 276 C SER A 51 8353 6655 5472 1103 1019 -188 C
ATOM 277 O SER A 51 8.140 21.516 20.397 1.00 57.38 O
ANISOU 277 O SER A 51 8830 7099 5875 1115 957 -198 O
ATOM 278 CB SER A 51 7.131 24.547 19.148 1.00 71.44 C
ANISOU 278 CB SER A 51 10701 8771 7672 1170 992 -154 C
ATOM 279 OG SER A 51 6.356 23.648 18.374 1.00 78.51 O
ANISOU 279 OG SER A 51 11650 9613 8569 1208 836 -145 O
ATOM 280 N VAL A 52 7.162 23.050 21.729 1.00 52.73 N
ANISOU 280 N VAL A 52 8072 6529 5434 1058 1040 -182 N
ATOM 281 CA VAL A 52 6.675 22.038 22.663 1.00 63.09 C
ANISOU 281 CA VAL A 52 9275 7873 6825 1020 993 -181 C
ATOM 282 C VAL A 52 5.720 21.081 21.961 1.00 60.16 C
ANISOU 282 C VAL A 52 8940 7435 6482 1052 827 -167 C
ATOM 283 O VAL A 52 5.785 19.861 22.155 1.00 69.78 O
ANISOU 283 O VAL A 52 10140 8667 7706 1044 773 -172 O
ATOM 284 CB VAL A 52 6.015 22.708 23.882 1.00 50.38 C
ANISOU 284 CB VAL A 52 7518 6297 5328 970 1046 -175 C
ATOM 285 CG1 VAL A 52 5.417 21.654 24.808 1.00 35.20 C
ANISOU 285 CG1 VAL A 52 5483 4403 3489 933 992 -168 C
ATOM 286 CG2 VAL A 52 7.029 23.573 24.622 1.00 34.05 C
ANISOU 286 CG2 VAL A 52 5408 4299 3230 939 1210 -197 C
ATOM 287 N THR A 53 4.827 21.616 21.128 1.00 53.10 N
ANISOU 287 N THR A 53 8097 6469 5609 1089 744 -151 N
ATOM 288 CA THR A 53 3.906 20.754 20.398 1.00 46.52 C
ANISOU 288 CA THR A 53 7302 5571 4804 1123 582 -142 C
ATOM 289 C THR A 53 4.652 19.887 19.390 1.00 56.80 C
ANISOU 289 C THR A 53 8730 6858 5995 1168 534 -157 C
ATOM 290 O THR A 53 4.365 18.691 19.261 1.00 60.03 O
ANISOU 290 O THR A 53 9136 7251 6421 1174 435 -163 O
ATOM 291 CB THR A 53 2.833 21.597 19.708 1.00 38.16 C
ANISOU 291 CB THR A 53 6273 4440 3786 1157 508 -123 C
ATOM 292 OG1 THR A 53 2.355 22.597 20.617 1.00 65.27 O
ANISOU 292 OG1 THR A 53 9598 7892 7308 1117 579 -114 O
ATOM 293 CG2 THR A 53 1.664 20.725 19.286 1.00 54.32 C
ANISOU 293 CG2 THR A 53 8315 6426 5898 1179 342 -117 C
ATOM 294 N ALA A 54 5.630 20.464 18.686 1.00 60.45 N
ANISOU 294 N ALA A 54 9299 7326 6342 1197 606 -165 N
ATOM 295 CA ALA A 54 6.399 19.697 17.709 1.00 58.72 C
ANISOU 295 CA ALA A 54 9203 7097 6011 1241 569 -182 C
ATOM 296 C ALA A 54 7.201 18.588 18.379 1.00 58.21 C
ANISOU 296 C ALA A 54 9096 7090 5931 1209 603 -204 C
ATOM 297 O ALA A 54 7.332 17.488 17.829 1.00 55.50 O
ANISOU 297 O ALA A 54 8806 6729 5551 1234 518 -218 O
ATOM 298 CB ALA A 54 7.325 20.623 16.923 1.00 61.18 C
ANISOU 298 CB ALA A 54 9629 7409 6206 1274 657 -184 C
ATOM 299 N LEU A 55 7.760 18.862 19.560 1.00 53.57 N
ANISOU 299 N LEU A 55 8413 6572 5371 1155 726 -208 N
ATOM 300 CA LEU A 55 8.465 17.820 20.298 1.00 52.62 C
ANISOU 300 CA LEU A 55 8240 6508 5244 1123 758 -225 C
ATOM 301 C LEU A 55 7.537 16.660 20.627 1.00 51.65 C
ANISOU 301 C LEU A 55 8048 6362 5213 1110 636 -215 C
ATOM 302 O LEU A 55 7.941 15.493 20.564 1.00 44.65 O
ANISOU 302 O LEU A 55 7177 5485 4304 1114 595 -228 O
ATOM 303 CB LEU A 55 9.073 18.398 21.574 1.00 61.98 C
ANISOU 303 CB LEU A 55 9323 7773 6454 1067 906 -229 C
ATOM 304 CG LEU A 55 10.464 19.016 21.452 1.00 50.95 C
ANISOU 304 CG LEU A 55 7985 6421 4953 1070 1042 -252 C
ATOM 305 CD1 LEU A 55 10.769 19.842 22.686 1.00 57.47 C
ANISOU 305 CD1 LEU A 55 8699 7315 5823 1018 1176 -257 C
ATOM 306 CD2 LEU A 55 11.510 17.927 21.261 1.00 47.58 C
ANISOU 306 CD2 LEU A 55 7609 6023 4445 1079 1046 -276 C
ATOM 307 N MET A 56 6.285 16.960 20.971 1.00 58.64 N
ANISOU 307 N MET A 56 8857 7218 6208 1096 578 -193 N
ATOM 308 CA MET A 56 5.329 15.897 21.253 1.00 55.93 C
ANISOU 308 CA MET A 56 8445 6847 5960 1085 460 -182 C
ATOM 309 C MET A 56 4.961 15.133 19.986 1.00 51.53 C
ANISOU 309 C MET A 56 7992 6216 5371 1141 316 -192 C
ATOM 310 O MET A 56 4.863 13.900 20.005 1.00 49.67 O
ANISOU 310 O MET A 56 7742 5970 5160 1140 239 -198 O
ATOM 311 CB MET A 56 4.083 16.481 21.915 1.00 61.29 C
ANISOU 311 CB MET A 56 9015 7510 6763 1056 438 -159 C
ATOM 312 CG MET A 56 3.040 15.443 22.286 1.00 79.62 C
ANISOU 312 CG MET A 56 11254 9802 9195 1039 324 -145 C
ATOM 313 SD MET A 56 3.638 14.234 23.483 1.00104.30 S
ANISOU 313 SD MET A 56 14282 12999 12350 988 371 -143 S
ATOM 314 CE MET A 56 4.065 15.295 24.862 1.00 75.45 C
ANISOU 314 CE MET A 56 10518 9437 8715 931 541 -136 C
ATOM 315 N VAL A 57 4.761 15.844 18.875 1.00 48.12 N
ANISOU 315 N VAL A 57 7665 5734 4883 1191 278 -193 N
ATOM 316 CA VAL A 57 4.436 15.180 17.615 1.00 50.33 C
ANISOU 316 CA VAL A 57 8050 5950 5124 1250 142 -206 C
ATOM 317 C VAL A 57 5.599 14.312 17.152 1.00 59.72 C
ANISOU 317 C VAL A 57 9322 7162 6208 1270 155 -233 C
ATOM 318 O VAL A 57 5.399 13.222 16.601 1.00 59.43 O
ANISOU 318 O VAL A 57 9320 7091 6171 1297 43 -250 O
ATOM 319 CB VAL A 57 4.051 16.220 16.547 1.00 49.07 C
ANISOU 319 CB VAL A 57 7988 5740 4917 1302 111 -198 C
ATOM 320 CG1 VAL A 57 3.715 15.533 15.231 1.00 52.60 C
ANISOU 320 CG1 VAL A 57 8545 6125 5316 1367 -33 -214 C
ATOM 321 CG2 VAL A 57 2.883 17.053 17.024 1.00 46.95 C
ANISOU 321 CG2 VAL A 57 7633 5446 4759 1282 95 -173 C
ATOM 322 N LEU A 58 6.830 14.782 17.366 1.00 53.23 N
ANISOU 322 N LEU A 58 8529 6398 5300 1258 291 -242 N
ATOM 323 CA LEU A 58 8.003 14.017 16.956 1.00 48.56 C
ANISOU 323 CA LEU A 58 8013 5831 4605 1276 314 -271 C
ATOM 324 C LEU A 58 8.071 12.684 17.690 1.00 50.87 C
ANISOU 324 C LEU A 58 8226 6146 4957 1244 280 -279 C
ATOM 325 O LEU A 58 8.227 11.626 17.069 1.00 40.26 O
ANISOU 325 O LEU A 58 6937 4777 3583 1273 193 -300 O
ATOM 326 CB LEU A 58 9.269 14.831 17.211 1.00 47.32 C
ANISOU 326 CB LEU A 58 7883 5736 4362 1261 476 -278 C
ATOM 327 CG LEU A 58 10.602 14.179 16.843 1.00 45.29 C
ANISOU 327 CG LEU A 58 7703 5512 3995 1277 521 -310 C
ATOM 328 CD1 LEU A 58 10.924 14.428 15.381 1.00 69.30 C
ANISOU 328 CD1 LEU A 58 10898 8514 6920 1342 486 -324 C
ATOM 329 CD2 LEU A 58 11.729 14.675 17.741 1.00 48.84 C
ANISOU 329 CD2 LEU A 58 8106 6039 4413 1234 686 -317 C
ATOM 330 N ASN A 59 7.943 12.719 19.020 1.00 47.31 N
ANISOU 330 N ASN A 59 7643 5741 4590 1184 346 -261 N
ATOM 331 CA ASN A 59 8.056 11.499 19.813 1.00 46.20 C
ANISOU 331 CA ASN A 59 7422 5627 4506 1150 326 -262 C
ATOM 332 C ASN A 59 6.916 10.531 19.516 1.00 52.39 C
ANISOU 332 C ASN A 59 8182 6344 5379 1164 168 -256 C
ATOM 333 O ASN A 59 7.132 9.316 19.435 1.00 54.13 O
ANISOU 333 O ASN A 59 8406 6556 5606 1168 107 -269 O
ATOM 334 CB ASN A 59 8.100 11.845 21.301 1.00 36.71 C
ANISOU 334 CB ASN A 59 6084 4493 3374 1086 433 -241 C
ATOM 335 CG ASN A 59 9.455 12.380 21.735 1.00 46.31 C
ANISOU 335 CG ASN A 59 7310 5783 4502 1069 587 -256 C
ATOM 336 OD1 ASN A 59 10.246 11.668 22.353 1.00 48.14 O
ANISOU 336 OD1 ASN A 59 7507 6067 4718 1045 636 -265 O
ATOM 337 ND2 ASN A 59 9.728 13.641 21.412 1.00 48.01 N
ANISOU 337 ND2 ASN A 59 7573 6004 4663 1080 665 -260 N
ATOM 338 N LEU A 60 5.695 11.046 19.356 1.00 54.29 N
ANISOU 338 N LEU A 60 8396 6536 5696 1170 97 -237 N
ATOM 339 CA LEU A 60 4.586 10.188 18.951 1.00 50.20 C
ANISOU 339 CA LEU A 60 7863 5948 5261 1189 -59 -237 C
ATOM 340 C LEU A 60 4.841 9.554 17.594 1.00 58.33 C
ANISOU 340 C LEU A 60 9024 6930 6210 1251 -158 -270 C
ATOM 341 O LEU A 60 4.433 8.412 17.355 1.00 64.35 O
ANISOU 341 O LEU A 60 9777 7652 7021 1263 -271 -282 O
ATOM 342 CB LEU A 60 3.285 10.984 18.926 1.00 43.81 C
ANISOU 342 CB LEU A 60 7014 5096 4538 1189 -112 -215 C
ATOM 343 CG LEU A 60 2.535 11.029 20.253 1.00 58.47 C
ANISOU 343 CG LEU A 60 8714 6975 6526 1128 -84 -185 C
ATOM 344 CD1 LEU A 60 1.493 12.135 20.244 1.00 51.45 C
ANISOU 344 CD1 LEU A 60 7794 6056 5698 1129 -100 -167 C
ATOM 345 CD2 LEU A 60 1.888 9.677 20.536 1.00 37.39 C
ANISOU 345 CD2 LEU A 60 5976 4274 3956 1114 -190 -180 C
ATOM 346 N ALA A 61 5.524 10.269 16.700 1.00 60.74 N
ANISOU 346 N ALA A 61 9449 7239 6391 1293 -117 -286 N
ATOM 347 CA ALA A 61 5.894 9.682 15.419 1.00 54.08 C
ANISOU 347 CA ALA A 61 8733 6360 5455 1354 -199 -320 C
ATOM 348 C ALA A 61 7.037 8.692 15.583 1.00 54.85 C
ANISOU 348 C ALA A 61 8846 6497 5498 1346 -160 -346 C
ATOM 349 O ALA A 61 7.056 7.645 14.927 1.00 54.02 O
ANISOU 349 O ALA A 61 8787 6357 5379 1378 -261 -374 O
ATOM 350 CB ALA A 61 6.270 10.779 14.427 1.00 44.83 C
ANISOU 350 CB ALA A 61 7683 5182 4166 1401 -161 -325 C
ATOM 351 N LEU A 62 8.003 9.005 16.452 1.00 62.58 N
ANISOU 351 N LEU A 62 9784 7547 6447 1304 -17 -338 N
ATOM 352 CA LEU A 62 9.111 8.084 16.686 1.00 55.04 C
ANISOU 352 CA LEU A 62 8837 6632 5444 1294 25 -362 C
ATOM 353 C LEU A 62 8.618 6.772 17.279 1.00 49.14 C
ANISOU 353 C LEU A 62 7999 5868 4804 1268 -58 -357 C
ATOM 354 O LEU A 62 9.109 5.696 16.918 1.00 60.17 O
ANISOU 354 O LEU A 62 9432 7256 6175 1286 -107 -385 O
ATOM 355 CB LEU A 62 10.147 8.729 17.606 1.00 48.20 C
ANISOU 355 CB LEU A 62 7930 5846 4537 1252 194 -354 C
ATOM 356 CG LEU A 62 11.007 9.840 17.008 1.00 60.17 C
ANISOU 356 CG LEU A 62 9545 7387 5930 1276 294 -366 C
ATOM 357 CD1 LEU A 62 11.727 10.595 18.111 1.00 59.75 C
ANISOU 357 CD1 LEU A 62 9420 7408 5873 1226 454 -354 C
ATOM 358 CD2 LEU A 62 12.003 9.265 16.011 1.00 45.52 C
ANISOU 358 CD2 LEU A 62 7811 5529 3955 1322 281 -405 C
ATOM 359 N ALA A 63 7.650 6.841 18.195 1.00 51.74 N
ANISOU 359 N ALA A 63 8207 6192 5258 1226 -73 -322 N
ATOM 360 CA ALA A 63 7.073 5.624 18.754 1.00 61.82 C
ANISOU 360 CA ALA A 63 9394 7447 6648 1201 -155 -312 C
ATOM 361 C ALA A 63 6.373 4.814 17.672 1.00 64.09 C
ANISOU 361 C ALA A 63 9740 7652 6958 1250 -319 -337 C
ATOM 362 O ALA A 63 6.595 3.605 17.538 1.00 58.54 O
ANISOU 362 O ALA A 63 9039 6931 6273 1257 -382 -357 O
ATOM 363 CB ALA A 63 6.099 5.972 19.880 1.00 35.11 C
ANISOU 363 CB ALA A 63 5874 4073 3393 1149 -137 -269 C
ATOM 364 N ASP A 64 5.528 5.474 16.880 1.00 58.96 N
ANISOU 364 N ASP A 64 9139 6952 6311 1286 -390 -340 N
ATOM 365 CA ASP A 64 4.822 4.775 15.816 1.00 60.56 C
ANISOU 365 CA ASP A 64 9399 7079 6533 1336 -550 -368 C
ATOM 366 C ASP A 64 5.782 4.246 14.754 1.00 57.63 C
ANISOU 366 C ASP A 64 9154 6704 6038 1388 -574 -415 C
ATOM 367 O ASP A 64 5.522 3.197 14.156 1.00 64.45 O
ANISOU 367 O ASP A 64 10042 7519 6925 1418 -694 -446 O
ATOM 368 CB ASP A 64 3.770 5.702 15.196 1.00 77.29 C
ANISOU 368 CB ASP A 64 11547 9150 8670 1367 -613 -360 C
ATOM 369 CG ASP A 64 2.620 6.004 16.150 1.00 81.88 C
ANISOU 369 CG ASP A 64 11996 9719 9394 1320 -623 -320 C
ATOM 370 OD1 ASP A 64 2.451 5.249 17.129 1.00 88.93 O
ANISOU 370 OD1 ASP A 64 12780 10624 10384 1272 -617 -302 O
ATOM 371 OD2 ASP A 64 1.872 6.979 15.914 1.00 64.17 O
ANISOU 371 OD2 ASP A 64 9760 7454 7168 1332 -638 -307 O
ATOM 372 N LEU A 65 6.905 4.931 14.524 1.00 46.44 N
ANISOU 372 N LEU A 65 7815 5338 4492 1399 -461 -424 N
ATOM 373 CA LEU A 65 7.829 4.477 13.491 1.00 47.62 C
ANISOU 373 CA LEU A 65 8087 5487 4518 1449 -479 -469 C
ATOM 374 C LEU A 65 8.585 3.229 13.922 1.00 54.08 C
ANISOU 374 C LEU A 65 8873 6327 5348 1430 -473 -489 C
ATOM 375 O LEU A 65 8.903 2.379 13.083 1.00 51.32 O
ANISOU 375 O LEU A 65 8596 5951 4954 1471 -550 -532 O
ATOM 376 CB LEU A 65 8.811 5.593 13.136 1.00 45.20 C
ANISOU 376 CB LEU A 65 7871 5229 4075 1465 -355 -471 C
ATOM 377 CG LEU A 65 9.602 5.419 11.839 1.00 61.48 C
ANISOU 377 CG LEU A 65 10079 7285 5996 1528 -378 -516 C
ATOM 378 CD1 LEU A 65 8.711 5.642 10.623 1.00 69.65 C
ANISOU 378 CD1 LEU A 65 11196 8257 7010 1590 -505 -528 C
ATOM 379 CD2 LEU A 65 10.792 6.361 11.818 1.00 60.14 C
ANISOU 379 CD2 LEU A 65 9970 7175 5704 1526 -225 -513 C
ATOM 380 N ALA A 66 8.875 3.101 15.218 1.00 53.84 N
ANISOU 380 N ALA A 66 8735 6344 5379 1368 -382 -459 N
ATOM 381 CA ALA A 66 9.669 1.976 15.698 1.00 35.60 C
ANISOU 381 CA ALA A 66 6391 4059 3077 1348 -364 -473 C
ATOM 382 C ALA A 66 8.899 0.667 15.600 1.00 52.06 C
ANISOU 382 C ALA A 66 8430 6080 5269 1353 -506 -483 C
ATOM 383 O ALA A 66 9.465 -0.366 15.223 1.00 49.61 O
ANISOU 383 O ALA A 66 8154 5759 4936 1373 -551 -518 O
ATOM 384 CB ALA A 66 10.111 2.229 17.137 1.00 46.90 C
ANISOU 384 CB ALA A 66 7714 5560 4546 1282 -232 -435 C
ATOM 385 N VAL A 67 7.608 0.685 15.940 1.00 59.41 N
ANISOU 385 N VAL A 67 9280 6969 6325 1335 -580 -454 N
ATOM 386 CA VAL A 67 6.820 -0.539 15.861 1.00 54.57 C
ANISOU 386 CA VAL A 67 8617 6291 5826 1338 -716 -463 C
ATOM 387 C VAL A 67 6.616 -0.951 14.409 1.00 60.49 C
ANISOU 387 C VAL A 67 9478 6980 6526 1408 -847 -518 C
ATOM 388 O VAL A 67 6.518 -2.145 14.100 1.00 70.58 O
ANISOU 388 O VAL A 67 10752 8215 7852 1424 -946 -547 O
ATOM 389 CB VAL A 67 5.482 -0.362 16.608 1.00 34.26 C
ANISOU 389 CB VAL A 67 5927 3690 3401 1300 -756 -418 C
ATOM 390 CG1 VAL A 67 4.727 0.829 16.074 1.00 70.23 C
ANISOU 390 CG1 VAL A 67 10522 8225 7936 1324 -774 -412 C
ATOM 391 CG2 VAL A 67 4.639 -1.614 16.493 1.00 52.05 C
ANISOU 391 CG2 VAL A 67 8127 5871 5778 1304 -898 -428 C
ATOM 392 N LEU A 68 6.578 0.018 13.492 1.00 52.40 N
ANISOU 392 N LEU A 68 8554 5951 5404 1452 -848 -533 N
ATOM 393 CA LEU A 68 6.445 -0.323 12.081 1.00 52.64 C
ANISOU 393 CA LEU A 68 8697 5933 5372 1523 -967 -587 C
ATOM 394 C LEU A 68 7.733 -0.914 11.519 1.00 60.14 C
ANISOU 394 C LEU A 68 9736 6910 6206 1552 -939 -633 C
ATOM 395 O LEU A 68 7.681 -1.706 10.572 1.00 58.86 O
ANISOU 395 O LEU A 68 9636 6705 6024 1601 -1051 -684 O
ATOM 396 CB LEU A 68 6.022 0.907 11.283 1.00 52.30 C
ANISOU 396 CB LEU A 68 8736 5880 5257 1563 -974 -584 C
ATOM 397 CG LEU A 68 4.570 1.336 11.495 1.00 51.13 C
ANISOU 397 CG LEU A 68 8517 5685 5226 1553 -1047 -554 C
ATOM 398 CD1 LEU A 68 4.353 2.718 10.922 1.00 74.01 C
ANISOU 398 CD1 LEU A 68 11488 8588 8044 1583 -1016 -540 C
ATOM 399 CD2 LEU A 68 3.604 0.339 10.866 1.00 53.16 C
ANISOU 399 CD2 LEU A 68 8765 5864 5568 1586 -1223 -588 C
ATOM 400 N LEU A 69 8.889 -0.560 12.089 1.00 56.14 N
ANISOU 400 N LEU A 69 9233 6473 5625 1523 -794 -620 N
ATOM 401 CA LEU A 69 10.156 -1.134 11.643 1.00 35.30 C
ANISOU 401 CA LEU A 69 6669 3863 2881 1546 -760 -664 C
ATOM 402 C LEU A 69 10.323 -2.594 12.044 1.00 49.12 C
ANISOU 402 C LEU A 69 8357 5594 4713 1529 -815 -682 C
ATOM 403 O LEU A 69 11.328 -3.209 11.675 1.00 54.79 O
ANISOU 403 O LEU A 69 9132 6330 5357 1549 -800 -723 O
ATOM 404 CB LEU A 69 11.331 -0.324 12.189 1.00 34.52 C
ANISOU 404 CB LEU A 69 6585 3844 2688 1519 -586 -646 C
ATOM 405 CG LEU A 69 11.518 1.067 11.580 1.00 54.47 C
ANISOU 405 CG LEU A 69 9202 6392 5102 1546 -518 -640 C
ATOM 406 CD1 LEU A 69 12.677 1.805 12.234 1.00 33.77 C
ANISOU 406 CD1 LEU A 69 6578 3848 2405 1512 -344 -624 C
ATOM 407 CD2 LEU A 69 11.731 0.949 10.083 1.00 54.44 C
ANISOU 407 CD2 LEU A 69 9337 6360 4985 1620 -595 -691 C
ATOM 408 N THR A 70 9.377 -3.162 12.792 1.00 51.46 N
ANISOU 408 N THR A 70 8537 5854 5162 1492 -877 -651 N
ATOM 409 CA THR A 70 9.417 -4.574 13.133 1.00 35.49 C
ANISOU 409 CA THR A 70 6451 3802 3230 1477 -941 -665 C
ATOM 410 C THR A 70 8.355 -5.388 12.421 1.00 54.27 C
ANISOU 410 C THR A 70 8827 6094 5698 1511 -1114 -696 C
ATOM 411 O THR A 70 8.497 -6.610 12.326 1.00 71.57 O
ANISOU 411 O THR A 70 11000 8252 7941 1518 -1185 -726 O
ATOM 412 CB THR A 70 9.249 -4.761 14.641 1.00 36.42 C
ANISOU 412 CB THR A 70 6428 3947 3463 1405 -872 -603 C
ATOM 413 OG1 THR A 70 7.930 -4.353 15.026 1.00 48.87 O
ANISOU 413 OG1 THR A 70 7928 5490 5151 1383 -918 -563 O
ATOM 414 CG2 THR A 70 10.259 -3.919 15.368 1.00 47.33 C
ANISOU 414 CG2 THR A 70 7808 5417 4760 1373 -703 -576 C
ATOM 415 N ALA A 71 7.300 -4.743 11.933 1.00 67.05 N
ANISOU 415 N ALA A 71 10462 7675 7340 1534 -1184 -691 N
ATOM 416 CA ALA A 71 6.299 -5.438 11.131 1.00 69.08 C
ANISOU 416 CA ALA A 71 10726 7851 7671 1574 -1353 -729 C
ATOM 417 C ALA A 71 6.884 -6.235 9.968 1.00 77.14 C
ANISOU 417 C ALA A 71 11849 8850 8611 1635 -1434 -805 C
ATOM 418 O ALA A 71 6.374 -7.338 9.703 1.00 67.21 O
ANISOU 418 O ALA A 71 10560 7530 7447 1649 -1558 -838 O
ATOM 419 CB ALA A 71 5.261 -4.426 10.627 1.00 78.38 C
ANISOU 419 CB ALA A 71 11931 9003 8849 1599 -1403 -718 C
ATOM 420 N PRO A 72 7.914 -5.767 9.243 1.00 68.10 N
ANISOU 420 N PRO A 72 10823 7750 7301 1673 -1372 -836 N
ATOM 421 CA PRO A 72 8.519 -6.635 8.215 1.00 72.36 C
ANISOU 421 CA PRO A 72 11451 8272 7770 1728 -1445 -911 C
ATOM 422 C PRO A 72 9.014 -7.966 8.755 1.00 62.29 C
ANISOU 422 C PRO A 72 10111 6987 6571 1701 -1458 -926 C
ATOM 423 O PRO A 72 8.931 -8.982 8.054 1.00 73.66 O
ANISOU 423 O PRO A 72 11574 8378 8033 1739 -1574 -986 O
ATOM 424 CB PRO A 72 9.673 -5.779 7.667 1.00 68.47 C
ANISOU 424 CB PRO A 72 11078 7846 7092 1756 -1335 -924 C
ATOM 425 CG PRO A 72 9.867 -4.682 8.669 1.00 58.51 C
ANISOU 425 CG PRO A 72 9768 6640 5823 1702 -1187 -855 C
ATOM 426 CD PRO A 72 8.505 -4.419 9.202 1.00 41.19 C
ANISOU 426 CD PRO A 72 7481 4405 3765 1674 -1244 -811 C
ATOM 427 N PHE A 73 9.532 -7.990 9.984 1.00 62.86 N
ANISOU 427 N PHE A 73 10099 7102 6683 1639 -1343 -876 N
ATOM 428 CA PHE A 73 9.949 -9.255 10.581 1.00 64.54 C
ANISOU 428 CA PHE A 73 10241 7303 6978 1611 -1354 -882 C
ATOM 429 C PHE A 73 8.751 -10.152 10.865 1.00 54.49 C
ANISOU 429 C PHE A 73 8868 5952 5885 1595 -1481 -873 C
ATOM 430 O PHE A 73 8.831 -11.375 10.704 1.00 74.57 O
ANISOU 430 O PHE A 73 11389 8451 8493 1605 -1562 -909 O
ATOM 431 CB PHE A 73 10.743 -8.994 11.860 1.00 59.29 C
ANISOU 431 CB PHE A 73 9509 6708 6311 1549 -1199 -825 C
ATOM 432 CG PHE A 73 12.010 -8.217 11.637 1.00 67.48 C
ANISOU 432 CG PHE A 73 10637 7820 7182 1561 -1070 -838 C
ATOM 433 CD1 PHE A 73 12.820 -8.485 10.547 1.00 79.66 C
ANISOU 433 CD1 PHE A 73 12296 9367 8605 1616 -1093 -907 C
ATOM 434 CD2 PHE A 73 12.383 -7.210 12.511 1.00 55.55 C
ANISOU 434 CD2 PHE A 73 9095 6377 5636 1518 -926 -785 C
ATOM 435 CE1 PHE A 73 13.986 -7.770 10.338 1.00 78.41 C
ANISOU 435 CE1 PHE A 73 12220 9277 8296 1627 -972 -919 C
ATOM 436 CE2 PHE A 73 13.547 -6.492 12.308 1.00 75.24 C
ANISOU 436 CE2 PHE A 73 11668 8937 7983 1528 -807 -799 C
ATOM 437 CZ PHE A 73 14.350 -6.773 11.221 1.00 65.92 C
ANISOU 437 CZ PHE A 73 10603 7757 6685 1582 -828 -864 C
ATOM 438 N PHE A 74 7.631 -9.565 11.285 1.00 53.56 N
ANISOU 438 N PHE A 74 8685 5813 5853 1571 -1499 -825 N
ATOM 439 CA PHE A 74 6.415 -10.331 11.520 1.00 60.55 C
ANISOU 439 CA PHE A 74 9474 6622 6912 1556 -1620 -816 C
ATOM 440 C PHE A 74 5.672 -10.662 10.233 1.00 81.83 C
ANISOU 440 C PHE A 74 12232 9246 9614 1621 -1782 -884 C
ATOM 441 O PHE A 74 4.745 -11.478 10.265 1.00 80.89 O
ANISOU 441 O PHE A 74 12041 9054 9638 1617 -1898 -893 O
ATOM 442 CB PHE A 74 5.488 -9.577 12.476 1.00 75.70 C
ANISOU 442 CB PHE A 74 11295 8546 8922 1505 -1577 -742 C
ATOM 443 CG PHE A 74 6.108 -9.287 13.817 1.00 76.16 C
ANISOU 443 CG PHE A 74 11278 8674 8986 1440 -1426 -675 C
ATOM 444 CD1 PHE A 74 6.376 -10.315 14.708 1.00 61.79 C
ANISOU 444 CD1 PHE A 74 9366 6852 7262 1398 -1409 -650 C
ATOM 445 CD2 PHE A 74 6.419 -7.989 14.188 1.00 49.60 C
ANISOU 445 CD2 PHE A 74 7933 5379 5534 1422 -1300 -639 C
ATOM 446 CE1 PHE A 74 6.947 -10.053 15.941 1.00 56.94 C
ANISOU 446 CE1 PHE A 74 8682 6306 6648 1341 -1272 -589 C
ATOM 447 CE2 PHE A 74 6.990 -7.721 15.417 1.00 56.45 C
ANISOU 447 CE2 PHE A 74 8729 6314 6406 1365 -1163 -583 C
ATOM 448 CZ PHE A 74 7.254 -8.754 16.295 1.00 57.61 C
ANISOU 448 CZ PHE A 74 8785 6461 6641 1325 -1150 -558 C
ATOM 449 N LEU A 75 6.049 -10.048 9.110 1.00 84.97 N
ANISOU 449 N LEU A 75 12761 9663 9862 1681 -1791 -931 N
ATOM 450 CA LEU A 75 5.543 -10.490 7.815 1.00 70.43 C
ANISOU 450 CA LEU A 75 10989 7762 8007 1750 -1944 -1006 C
ATOM 451 C LEU A 75 6.272 -11.739 7.338 1.00 77.89 C
ANISOU 451 C LEU A 75 11963 8688 8941 1777 -1999 -1073 C
ATOM 452 O LEU A 75 5.640 -12.678 6.842 1.00 76.06 O
ANISOU 452 O LEU A 75 11711 8386 8802 1804 -2140 -1122 O
ATOM 453 CB LEU A 75 5.685 -9.371 6.788 1.00 60.71 C
ANISOU 453 CB LEU A 75 9889 6564 6616 1806 -1932 -1029 C
ATOM 454 CG LEU A 75 4.824 -8.130 7.004 1.00 77.31 C
ANISOU 454 CG LEU A 75 11975 8671 8727 1794 -1907 -976 C
ATOM 455 CD1 LEU A 75 5.198 -7.074 5.982 1.00 77.10 C
ANISOU 455 CD1 LEU A 75 12086 8682 8526 1851 -1879 -996 C
ATOM 456 CD2 LEU A 75 3.340 -8.469 6.915 1.00 63.58 C
ANISOU 456 CD2 LEU A 75 10166 6854 7140 1799 -2050 -980 C
ATOM 457 N HIS A 76 7.601 -11.762 7.488 1.00 95.05 N
ANISOU 457 N HIS A 76 14183 10923 11008 1771 -1890 -1077 N
ATOM 458 CA HIS A 76 8.374 -12.955 7.157 1.00 87.35 C
ANISOU 458 CA HIS A 76 13227 9934 10028 1791 -1929 -1137 C
ATOM 459 C HIS A 76 7.909 -14.148 7.978 1.00 82.29 C
ANISOU 459 C HIS A 76 12456 9236 9574 1747 -1985 -1119 C
ATOM 460 O HIS A 76 7.866 -15.278 7.477 1.00 95.98 O
ANISOU 460 O HIS A 76 14188 10916 11366 1774 -2094 -1179 O
ATOM 461 CB HIS A 76 9.864 -12.689 7.384 1.00 80.74 C
ANISOU 461 CB HIS A 76 12444 9176 9056 1780 -1784 -1133 C
ATOM 462 CG HIS A 76 10.751 -13.847 7.045 1.00 97.85 C
ANISOU 462 CG HIS A 76 14636 11336 11208 1801 -1814 -1196 C
ATOM 463 ND1 HIS A 76 11.522 -13.884 5.904 1.00102.52 N
ANISOU 463 ND1 HIS A 76 15352 11948 11655 1863 -1830 -1270 N
ATOM 464 CD2 HIS A 76 10.994 -15.006 7.701 1.00 95.36 C
ANISOU 464 CD2 HIS A 76 14236 10994 11004 1769 -1829 -1194 C
ATOM 465 CE1 HIS A 76 12.199 -15.018 5.869 1.00105.12 C
ANISOU 465 CE1 HIS A 76 15670 12263 12009 1868 -1856 -1316 C
ATOM 466 NE2 HIS A 76 11.896 -15.717 6.948 1.00 95.52 N
ANISOU 466 NE2 HIS A 76 14329 11017 10948 1812 -1856 -1269 N
ATOM 467 N PHE A 77 7.551 -13.915 9.244 1.00 60.21 N
ANISOU 467 N PHE A 77 9549 6451 6877 1679 -1912 -1036 N
ATOM 468 CA PHE A 77 7.021 -14.989 10.077 1.00 81.97 C
ANISOU 468 CA PHE A 77 12176 9152 9817 1635 -1962 -1007 C
ATOM 469 C PHE A 77 5.693 -15.498 9.530 1.00 91.21 C
ANISOU 469 C PHE A 77 13312 10230 11115 1659 -2127 -1040 C
ATOM 470 O PHE A 77 5.492 -16.710 9.385 1.00 96.76 O
ANISOU 470 O PHE A 77 13972 10869 11925 1667 -2226 -1077 O
ATOM 471 CB PHE A 77 6.861 -14.507 11.519 1.00 72.60 C
ANISOU 471 CB PHE A 77 10882 8004 8698 1560 -1845 -909 C
ATOM 472 CG PHE A 77 6.254 -15.532 12.437 1.00 71.90 C
ANISOU 472 CG PHE A 77 10656 7861 8799 1512 -1887 -868 C
ATOM 473 CD1 PHE A 77 7.049 -16.483 13.053 1.00 76.43 C
ANISOU 473 CD1 PHE A 77 11185 8444 9413 1485 -1848 -857 C
ATOM 474 CD2 PHE A 77 4.890 -15.542 12.685 1.00 75.39 C
ANISOU 474 CD2 PHE A 77 11016 8245 9385 1493 -1966 -839 C
ATOM 475 CE1 PHE A 77 6.497 -17.424 13.895 1.00 78.22 C
ANISOU 475 CE1 PHE A 77 11286 8620 9815 1441 -1884 -814 C
ATOM 476 CE2 PHE A 77 4.334 -16.481 13.525 1.00 85.66 C
ANISOU 476 CE2 PHE A 77 12189 9494 10862 1448 -2001 -799 C
ATOM 477 CZ PHE A 77 5.138 -17.422 14.131 1.00100.32 C
ANISOU 477 CZ PHE A 77 14003 11360 12754 1422 -1959 -784 C
ATOM 478 N LEU A 78 4.765 -14.584 9.228 1.00 79.10 N
ANISOU 478 N LEU A 78 11792 8687 9575 1673 -2159 -1028 N
ATOM 479 CA LEU A 78 3.491 -14.998 8.650 1.00 75.35 C
ANISOU 479 CA LEU A 78 11289 8126 9215 1700 -2319 -1064 C
ATOM 480 C LEU A 78 3.689 -15.663 7.294 1.00 85.47 C
ANISOU 480 C LEU A 78 12664 9371 10440 1775 -2442 -1167 C
ATOM 481 O LEU A 78 2.919 -16.557 6.925 1.00 99.52 O
ANISOU 481 O LEU A 78 14400 11070 12342 1794 -2582 -1212 O
ATOM 482 CB LEU A 78 2.548 -13.797 8.519 1.00 83.81 C
ANISOU 482 CB LEU A 78 12369 9201 10272 1706 -2325 -1035 C
ATOM 483 CG LEU A 78 2.061 -13.144 9.820 1.00 71.15 C
ANISOU 483 CG LEU A 78 10660 7622 8750 1634 -2228 -938 C
ATOM 484 CD1 LEU A 78 1.576 -11.715 9.589 1.00 59.81 C
ANISOU 484 CD1 LEU A 78 9270 6217 7239 1647 -2194 -914 C
ATOM 485 CD2 LEU A 78 0.971 -13.976 10.483 1.00 74.03 C
ANISOU 485 CD2 LEU A 78 10888 7913 9329 1594 -2308 -912 C
ATOM 486 N ALA A 79 4.714 -15.255 6.542 1.00105.74 N
ANISOU 486 N ALA A 79 15356 11996 12826 1820 -2394 -1209 N
ATOM 487 CA ALA A 79 4.882 -15.782 5.192 1.00112.70 C
ANISOU 487 CA ALA A 79 16334 12850 13638 1896 -2509 -1310 C
ATOM 488 C ALA A 79 5.472 -17.187 5.225 1.00113.78 C
ANISOU 488 C ALA A 79 16440 12954 13839 1895 -2551 -1356 C
ATOM 489 O ALA A 79 4.829 -18.155 4.800 1.00 97.44 O
ANISOU 489 O ALA A 79 14333 10807 11882 1918 -2691 -1411 O
ATOM 490 CB ALA A 79 5.751 -14.836 4.360 1.00104.18 C
ANISOU 490 CB ALA A 79 15400 11844 12341 1944 -2440 -1335 C
ATOM 491 N GLN A 80 6.702 -17.321 5.734 1.00106.36 N
ANISOU 491 N GLN A 80 15511 12071 12832 1869 -2431 -1337 N
ATOM 492 CA GLN A 80 7.354 -18.625 5.797 1.00 73.95 C
ANISOU 492 CA GLN A 80 11378 7938 8781 1867 -2461 -1379 C
ATOM 493 C GLN A 80 6.718 -19.561 6.821 1.00 80.43 C
ANISOU 493 C GLN A 80 12050 8695 9815 1810 -2496 -1333 C
ATOM 494 O GLN A 80 6.903 -20.778 6.721 1.00 67.24 O
ANISOU 494 O GLN A 80 10345 6973 8229 1816 -2567 -1377 O
ATOM 495 CB GLN A 80 8.842 -18.455 6.113 1.00 78.14 C
ANISOU 495 CB GLN A 80 11958 8549 9183 1853 -2317 -1367 C
ATOM 496 CG GLN A 80 9.735 -18.279 4.892 1.00 76.46 C
ANISOU 496 CG GLN A 80 11889 8376 8788 1922 -2321 -1450 C
ATOM 497 CD GLN A 80 9.738 -16.863 4.345 1.00106.88 C
ANISOU 497 CD GLN A 80 15841 12285 12482 1950 -2264 -1438 C
ATOM 498 OE1 GLN A 80 8.980 -16.001 4.795 1.00109.75 O
ANISOU 498 OE1 GLN A 80 16169 12653 12876 1924 -2236 -1374 O
ATOM 499 NE2 GLN A 80 10.604 -16.615 3.367 1.00115.16 N
ANISOU 499 NE2 GLN A 80 17016 13378 13361 2006 -2246 -1498 N
ATOM 500 N GLY A 81 5.983 -19.033 7.798 1.00 76.10 N
ANISOU 500 N GLY A 81 11413 8148 9356 1754 -2447 -1246 N
ATOM 501 CA GLY A 81 5.418 -19.862 8.846 1.00 74.09 C
ANISOU 501 CA GLY A 81 11015 7839 9296 1696 -2465 -1192 C
ATOM 502 C GLY A 81 6.353 -20.198 9.988 1.00 74.49 C
ANISOU 502 C GLY A 81 11007 7934 9360 1639 -2338 -1129 C
ATOM 503 O GLY A 81 5.988 -21.010 10.845 1.00 64.46 O
ANISOU 503 O GLY A 81 9621 6619 8251 1593 -2352 -1085 O
ATOM 504 N THR A 82 7.541 -19.596 10.035 1.00 94.08 N
ANISOU 504 N THR A 82 13565 10503 11680 1642 -2214 -1124 N
ATOM 505 CA THR A 82 8.528 -19.912 11.061 1.00 75.74 C
ANISOU 505 CA THR A 82 11194 8227 9356 1595 -2094 -1073 C
ATOM 506 C THR A 82 9.379 -18.680 11.342 1.00 67.71 C
ANISOU 506 C THR A 82 10240 7314 8173 1583 -1939 -1038 C
ATOM 507 O THR A 82 9.502 -17.782 10.505 1.00 65.85 O
ANISOU 507 O THR A 82 10110 7111 7801 1625 -1930 -1074 O
ATOM 508 CB THR A 82 9.414 -21.091 10.637 1.00 68.20 C
ANISOU 508 CB THR A 82 10266 7250 8398 1622 -2135 -1139 C
ATOM 509 OG1 THR A 82 10.500 -21.233 11.560 1.00 80.37 O
ANISOU 509 OG1 THR A 82 11778 8850 9907 1582 -2007 -1092 O
ATOM 510 CG2 THR A 82 9.970 -20.856 9.239 1.00 64.71 C
ANISOU 510 CG2 THR A 82 9966 6824 7796 1695 -2177 -1237 C
ATOM 511 N TRP A 83 9.971 -18.649 12.537 1.00 68.38 N
ANISOU 511 N TRP A 83 10258 7450 8273 1527 -1816 -967 N
ATOM 512 CA TRP A 83 10.827 -17.545 12.955 1.00 53.53 C
ANISOU 512 CA TRP A 83 8421 5668 6249 1510 -1661 -932 C
ATOM 513 C TRP A 83 12.280 -17.878 12.640 1.00 58.30 C
ANISOU 513 C TRP A 83 9099 6317 6734 1533 -1602 -980 C
ATOM 514 O TRP A 83 12.776 -18.942 13.024 1.00 59.52 O
ANISOU 514 O TRP A 83 9207 6454 6954 1520 -1611 -984 O
ATOM 515 CB TRP A 83 10.662 -17.267 14.449 1.00 49.04 C
ANISOU 515 CB TRP A 83 7737 5137 5758 1438 -1556 -832 C
ATOM 516 CG TRP A 83 11.364 -16.032 14.900 1.00 57.78 C
ANISOU 516 CG TRP A 83 8879 6343 6733 1419 -1403 -796 C
ATOM 517 CD1 TRP A 83 12.575 -15.955 15.521 1.00 53.40 C
ANISOU 517 CD1 TRP A 83 8327 5862 6101 1397 -1278 -778 C
ATOM 518 CD2 TRP A 83 10.899 -14.688 14.757 1.00 49.19 C
ANISOU 518 CD2 TRP A 83 7826 5287 5576 1421 -1361 -776 C
ATOM 519 NE1 TRP A 83 12.892 -14.644 15.778 1.00 51.69 N
ANISOU 519 NE1 TRP A 83 8144 5722 5775 1385 -1159 -750 N
ATOM 520 CE2 TRP A 83 11.878 -13.845 15.317 1.00 54.98 C
ANISOU 520 CE2 TRP A 83 8581 6114 6195 1398 -1206 -748 C
ATOM 521 CE3 TRP A 83 9.747 -14.114 14.210 1.00 46.79 C
ANISOU 521 CE3 TRP A 83 7536 4942 5300 1440 -1439 -781 C
ATOM 522 CZ2 TRP A 83 11.742 -12.460 15.347 1.00 54.10 C
ANISOU 522 CZ2 TRP A 83 8503 6053 6001 1394 -1128 -724 C
ATOM 523 CZ3 TRP A 83 9.613 -12.738 14.240 1.00 60.12 C
ANISOU 523 CZ3 TRP A 83 9259 6681 6904 1436 -1362 -755 C
ATOM 524 CH2 TRP A 83 10.605 -11.927 14.804 1.00 58.94 C
ANISOU 524 CH2 TRP A 83 9129 6621 6644 1413 -1207 -727 C
ATOM 525 N SER A 84 12.965 -16.967 11.945 1.00 51.67 N
ANISOU 525 N SER A 84 8375 5535 5722 1567 -1542 -1016 N
ATOM 526 CA SER A 84 14.322 -17.229 11.477 1.00 75.23 C
ANISOU 526 CA SER A 84 11442 8561 8583 1596 -1493 -1073 C
ATOM 527 C SER A 84 15.321 -16.186 11.965 1.00 68.70 C
ANISOU 527 C SER A 84 10650 7831 7621 1575 -1325 -1040 C
ATOM 528 O SER A 84 16.419 -16.078 11.410 1.00 94.45 O
ANISOU 528 O SER A 84 14001 11135 10750 1605 -1275 -1090 O
ATOM 529 CB SER A 84 14.352 -17.315 9.949 1.00 80.20 C
ANISOU 529 CB SER A 84 12191 9161 9122 1670 -1592 -1168 C
ATOM 530 OG SER A 84 13.894 -16.112 9.360 1.00105.52 O
ANISOU 530 OG SER A 84 15469 12389 12236 1695 -1583 -1167 O
ATOM 531 N PHE A 85 14.976 -15.426 13.000 1.00 65.42 N
ANISOU 531 N PHE A 85 10164 7454 7240 1523 -1237 -959 N
ATOM 532 CA PHE A 85 15.828 -14.350 13.484 1.00 74.71 C
ANISOU 532 CA PHE A 85 11368 8722 8297 1502 -1080 -928 C
ATOM 533 C PHE A 85 16.415 -14.624 14.861 1.00 77.25 C
ANISOU 533 C PHE A 85 11592 9092 8668 1444 -975 -868 C
ATOM 534 O PHE A 85 17.124 -13.767 15.400 1.00 87.15 O
ANISOU 534 O PHE A 85 12854 10425 9836 1422 -841 -841 O
ATOM 535 CB PHE A 85 15.043 -13.034 13.490 1.00 59.49 C
ANISOU 535 CB PHE A 85 9450 6812 6343 1494 -1049 -890 C
ATOM 536 CG PHE A 85 14.352 -12.747 12.186 1.00 66.87 C
ANISOU 536 CG PHE A 85 10473 7698 7236 1551 -1158 -941 C
ATOM 537 CD1 PHE A 85 15.047 -12.185 11.128 1.00 58.23 C
ANISOU 537 CD1 PHE A 85 9509 6634 5982 1602 -1135 -997 C
ATOM 538 CD2 PHE A 85 13.011 -13.053 12.012 1.00 73.29 C
ANISOU 538 CD2 PHE A 85 11238 8437 8171 1556 -1284 -934 C
ATOM 539 CE1 PHE A 85 14.418 -11.926 9.924 1.00 51.00 C
ANISOU 539 CE1 PHE A 85 8676 5678 5023 1658 -1236 -1043 C
ATOM 540 CE2 PHE A 85 12.376 -12.796 10.810 1.00 75.36 C
ANISOU 540 CE2 PHE A 85 11582 8658 8395 1611 -1388 -984 C
ATOM 541 CZ PHE A 85 13.081 -12.232 9.765 1.00 58.23 C
ANISOU 541 CZ PHE A 85 9544 6522 6060 1663 -1364 -1037 C
ATOM 542 N GLY A 86 16.148 -15.792 15.441 1.00 57.57 N
ANISOU 542 N GLY A 86 9008 6555 6313 1421 -1034 -847 N
ATOM 543 CA GLY A 86 16.778 -16.186 16.683 1.00 86.21 C
ANISOU 543 CA GLY A 86 12547 10225 9982 1373 -943 -794 C
ATOM 544 C GLY A 86 16.035 -15.714 17.916 1.00 55.91 C
ANISOU 544 C GLY A 86 8598 6411 6234 1315 -888 -702 C
ATOM 545 O GLY A 86 15.021 -15.014 17.859 1.00 47.72 O
ANISOU 545 O GLY A 86 7546 5356 5227 1309 -913 -677 O
ATOM 546 N LEU A 87 16.573 -16.126 19.068 1.00 55.14 N
ANISOU 546 N LEU A 87 8417 6354 6178 1273 -810 -651 N
ATOM 547 CA LEU A 87 15.987 -15.749 20.350 1.00 47.42 C
ANISOU 547 CA LEU A 87 7327 5409 5281 1216 -747 -562 C
ATOM 548 C LEU A 87 16.072 -14.244 20.572 1.00 64.74 C
ANISOU 548 C LEU A 87 9546 7678 7372 1204 -636 -543 C
ATOM 549 O LEU A 87 15.096 -13.608 20.984 1.00 66.52 O
ANISOU 549 O LEU A 87 9720 7903 7654 1178 -633 -496 O
ATOM 550 CB LEU A 87 16.688 -16.498 21.484 1.00 66.11 C
ANISOU 550 CB LEU A 87 9610 7815 7695 1180 -682 -516 C
ATOM 551 CG LEU A 87 16.322 -16.069 22.906 1.00 66.08 C
ANISOU 551 CG LEU A 87 9493 7866 7750 1122 -593 -423 C
ATOM 552 CD1 LEU A 87 14.905 -16.498 23.236 1.00 53.18 C
ANISOU 552 CD1 LEU A 87 7766 6162 6277 1098 -683 -372 C
ATOM 553 CD2 LEU A 87 17.318 -16.623 23.923 1.00 63.97 C
ANISOU 553 CD2 LEU A 87 9167 7657 7480 1096 -507 -388 C
ATOM 554 N ALA A 88 17.239 -13.656 20.299 1.00 77.08 N
ANISOU 554 N ALA A 88 11191 9307 8790 1221 -542 -581 N
ATOM 555 CA ALA A 88 17.412 -12.220 20.487 1.00 53.80 C
ANISOU 555 CA ALA A 88 8269 6428 5743 1210 -430 -567 C
ATOM 556 C ALA A 88 16.502 -11.416 19.567 1.00 49.20 C
ANISOU 556 C ALA A 88 7748 5806 5139 1237 -492 -588 C
ATOM 557 O ALA A 88 16.020 -10.346 19.954 1.00 61.03 O
ANISOU 557 O ALA A 88 9223 7336 6629 1215 -434 -551 O
ATOM 558 CB ALA A 88 18.873 -11.840 20.264 1.00 53.53 C
ANISOU 558 CB ALA A 88 8314 6464 5562 1227 -326 -612 C
ATOM 559 N GLY A 89 16.241 -11.918 18.359 1.00 58.94 N
ANISOU 559 N GLY A 89 9059 6970 6366 1286 -610 -646 N
ATOM 560 CA GLY A 89 15.329 -11.219 17.468 1.00 57.10 C
ANISOU 560 CA GLY A 89 8883 6697 6117 1316 -679 -665 C
ATOM 561 C GLY A 89 13.898 -11.254 17.969 1.00 46.38 C
ANISOU 561 C GLY A 89 7429 5290 4902 1287 -747 -612 C
ATOM 562 O GLY A 89 13.219 -10.225 18.020 1.00 44.25 O
ANISOU 562 O GLY A 89 7155 5031 4626 1279 -725 -586 O
ATOM 563 N CYS A 90 13.419 -12.443 18.341 1.00 57.29 N
ANISOU 563 N CYS A 90 8730 6617 6419 1271 -829 -594 N
ATOM 564 CA CYS A 90 12.084 -12.562 18.917 1.00 53.60 C
ANISOU 564 CA CYS A 90 8160 6105 6101 1239 -888 -540 C
ATOM 565 C CYS A 90 11.973 -11.790 20.226 1.00 55.39 C
ANISOU 565 C CYS A 90 8296 6401 6348 1182 -767 -463 C
ATOM 566 O CYS A 90 10.898 -11.274 20.554 1.00 64.62 O
ANISOU 566 O CYS A 90 9408 7554 7590 1160 -784 -423 O
ATOM 567 CB CYS A 90 11.741 -14.042 19.112 1.00 54.74 C
ANISOU 567 CB CYS A 90 8233 6179 6385 1232 -987 -535 C
ATOM 568 SG CYS A 90 10.261 -14.431 20.090 1.00 71.05 S
ANISOU 568 SG CYS A 90 10148 8195 8654 1181 -1042 -456 S
ATOM 569 N ARG A 91 13.070 -11.684 20.978 1.00 48.92 N
ANISOU 569 N ARG A 91 7461 5661 5464 1159 -644 -445 N
ATOM 570 CA ARG A 91 13.060 -10.859 22.182 1.00 46.43 C
ANISOU 570 CA ARG A 91 7068 5422 5152 1109 -522 -380 C
ATOM 571 C ARG A 91 12.934 -9.383 21.825 1.00 47.80 C
ANISOU 571 C ARG A 91 7301 5632 5231 1119 -463 -391 C
ATOM 572 O ARG A 91 12.010 -8.697 22.278 1.00 61.95 O
ANISOU 572 O ARG A 91 9034 7425 7078 1093 -454 -349 O
ATOM 573 CB ARG A 91 14.328 -11.101 23.006 1.00 47.74 C
ANISOU 573 CB ARG A 91 7209 5666 5264 1087 -408 -366 C
ATOM 574 CG ARG A 91 14.365 -12.414 23.769 1.00 51.14 C
ANISOU 574 CG ARG A 91 7548 6076 5805 1062 -439 -329 C
ATOM 575 CD ARG A 91 15.315 -12.305 24.950 1.00 33.06 C
ANISOU 575 CD ARG A 91 5202 3882 3478 1027 -305 -289 C
ATOM 576 NE ARG A 91 15.789 -13.601 25.425 1.00 46.13 N
ANISOU 576 NE ARG A 91 6807 5525 5196 1018 -326 -272 N
ATOM 577 CZ ARG A 91 15.066 -14.444 26.154 1.00 58.04 C
ANISOU 577 CZ ARG A 91 8210 6997 6846 988 -374 -212 C
ATOM 578 NH1 ARG A 91 15.589 -15.595 26.547 1.00 65.11 N
ANISOU 578 NH1 ARG A 91 9067 7882 7790 984 -388 -197 N
ATOM 579 NH2 ARG A 91 13.818 -14.143 26.481 1.00 74.13 N
ANISOU 579 NH2 ARG A 91 10181 9008 8979 964 -408 -166 N
ATOM 580 N LEU A 92 13.853 -8.882 20.994 1.00 44.31 N
ANISOU 580 N LEU A 92 6974 5216 4647 1156 -424 -447 N
ATOM 581 CA LEU A 92 13.932 -7.448 20.730 1.00 42.48 C
ANISOU 581 CA LEU A 92 6798 5026 4316 1164 -347 -454 C
ATOM 582 C LEU A 92 12.689 -6.942 20.006 1.00 45.04 C
ANISOU 582 C LEU A 92 7148 5288 4677 1185 -441 -457 C
ATOM 583 O LEU A 92 12.137 -5.898 20.364 1.00 58.35 O
ANISOU 583 O LEU A 92 8805 6997 6369 1165 -393 -425 O
ATOM 584 CB LEU A 92 15.192 -7.134 19.922 1.00 43.15 C
ANISOU 584 CB LEU A 92 7005 5146 4246 1202 -292 -513 C
ATOM 585 CG LEU A 92 15.291 -5.713 19.379 1.00 50.58 C
ANISOU 585 CG LEU A 92 8025 6115 5078 1221 -228 -528 C
ATOM 586 CD1 LEU A 92 16.435 -4.999 20.062 1.00 50.16 C
ANISOU 586 CD1 LEU A 92 7968 6156 4936 1196 -68 -522 C
ATOM 587 CD2 LEU A 92 15.483 -5.750 17.870 1.00 74.10 C
ANISOU 587 CD2 LEU A 92 11138 9050 7967 1284 -302 -594 C
ATOM 588 N CYS A 93 12.222 -7.681 18.996 1.00 41.73 N
ANISOU 588 N CYS A 93 6778 4789 4287 1226 -578 -499 N
ATOM 589 CA CYS A 93 11.115 -7.196 18.172 1.00 49.74 C
ANISOU 589 CA CYS A 93 7830 5744 5323 1255 -673 -512 C
ATOM 590 C CYS A 93 9.841 -7.010 18.988 1.00 57.83 C
ANISOU 590 C CYS A 93 8740 6748 6485 1214 -697 -452 C
ATOM 591 O CYS A 93 9.055 -6.092 18.724 1.00 64.86 O
ANISOU 591 O CYS A 93 9642 7625 7377 1220 -712 -443 O
ATOM 592 CB CYS A 93 10.866 -8.148 17.006 1.00 34.15 C
ANISOU 592 CB CYS A 93 5921 3692 3364 1307 -819 -571 C
ATOM 593 SG CYS A 93 12.176 -8.165 15.759 1.00 81.25 S
ANISOU 593 SG CYS A 93 12042 9676 9154 1368 -806 -650 S
ATOM 594 N HIS A 94 9.608 -7.879 19.971 1.00 66.57 N
ANISOU 594 N HIS A 94 9735 7850 7711 1172 -703 -409 N
ATOM 595 CA HIS A 94 8.465 -7.713 20.858 1.00 49.13 C
ANISOU 595 CA HIS A 94 7408 5628 5631 1127 -712 -348 C
ATOM 596 C HIS A 94 8.705 -6.665 21.935 1.00 51.79 C
ANISOU 596 C HIS A 94 7687 6052 5937 1082 -567 -299 C
ATOM 597 O HIS A 94 7.735 -6.128 22.481 1.00 62.89 O
ANISOU 597 O HIS A 94 9020 7456 7421 1053 -564 -257 O
ATOM 598 CB HIS A 94 8.100 -9.050 21.507 1.00 51.56 C
ANISOU 598 CB HIS A 94 7615 5896 6081 1099 -772 -317 C
ATOM 599 CG HIS A 94 7.265 -9.932 20.635 1.00 56.51 C
ANISOU 599 CG HIS A 94 8256 6420 6796 1131 -934 -352 C
ATOM 600 ND1 HIS A 94 6.023 -9.557 20.171 1.00 64.58 N
ANISOU 600 ND1 HIS A 94 9271 7384 7882 1144 -1023 -356 N
ATOM 601 CD2 HIS A 94 7.490 -11.172 20.144 1.00 64.15 C
ANISOU 601 CD2 HIS A 94 9241 7332 7801 1155 -1024 -388 C
ATOM 602 CE1 HIS A 94 5.519 -10.529 19.432 1.00 59.46 C
ANISOU 602 CE1 HIS A 94 8635 6649 7306 1174 -1162 -394 C
ATOM 603 NE2 HIS A 94 6.391 -11.520 19.398 1.00 61.58 N
ANISOU 603 NE2 HIS A 94 8918 6917 7561 1181 -1165 -415 N
ATOM 604 N TYR A 95 9.965 -6.354 22.245 1.00 41.69 N
ANISOU 604 N TYR A 95 6441 4851 4549 1077 -449 -306 N
ATOM 605 CA TYR A 95 10.246 -5.363 23.276 1.00 37.47 C
ANISOU 605 CA TYR A 95 5850 4402 3983 1036 -309 -266 C
ATOM 606 C TYR A 95 10.073 -3.944 22.751 1.00 39.37 C
ANISOU 606 C TYR A 95 6156 4659 4145 1053 -270 -282 C
ATOM 607 O TYR A 95 9.597 -3.065 23.477 1.00 50.29 O
ANISOU 607 O TYR A 95 7474 6077 5556 1020 -205 -244 O
ATOM 608 CB TYR A 95 11.657 -5.561 23.828 1.00 46.94 C
ANISOU 608 CB TYR A 95 7054 5679 5101 1024 -198 -270 C
ATOM 609 CG TYR A 95 12.023 -4.573 24.910 1.00 44.78 C
ANISOU 609 CG TYR A 95 6721 5500 4794 983 -53 -235 C
ATOM 610 CD1 TYR A 95 11.399 -4.611 26.149 1.00 47.78 C
ANISOU 610 CD1 TYR A 95 6971 5909 5275 933 -20 -172 C
ATOM 611 CD2 TYR A 95 12.991 -3.604 24.692 1.00 36.47 C
ANISOU 611 CD2 TYR A 95 5739 4507 3609 995 53 -266 C
ATOM 612 CE1 TYR A 95 11.728 -3.710 27.139 1.00 45.65 C
ANISOU 612 CE1 TYR A 95 6644 5728 4973 898 111 -145 C
ATOM 613 CE2 TYR A 95 13.328 -2.699 25.676 1.00 35.14 C
ANISOU 613 CE2 TYR A 95 5514 4424 3414 959 183 -239 C
ATOM 614 CZ TYR A 95 12.694 -2.756 26.898 1.00 48.57 C
ANISOU 614 CZ TYR A 95 7086 6155 5214 911 211 -180 C
ATOM 615 OH TYR A 95 13.026 -1.853 27.883 1.00 70.01 O
ANISOU 615 OH TYR A 95 9741 8959 7901 877 340 -159 O
ATOM 616 N VAL A 96 10.458 -3.699 21.496 1.00 48.30 N
ANISOU 616 N VAL A 96 7414 5762 5174 1106 -306 -338 N
ATOM 617 CA VAL A 96 10.251 -2.381 20.911 1.00 55.72 C
ANISOU 617 CA VAL A 96 8421 6708 6041 1127 -277 -351 C
ATOM 618 C VAL A 96 8.792 -2.161 20.536 1.00 50.40 C
ANISOU 618 C VAL A 96 7726 5964 5457 1136 -385 -338 C
ATOM 619 O VAL A 96 8.365 -1.013 20.366 1.00 54.84 O
ANISOU 619 O VAL A 96 8308 6533 5994 1140 -357 -331 O
ATOM 620 CB VAL A 96 11.164 -2.182 19.689 1.00 39.75 C
ANISOU 620 CB VAL A 96 6544 4683 3876 1182 -275 -410 C
ATOM 621 CG1 VAL A 96 12.624 -2.178 20.117 1.00 30.94 C
ANISOU 621 CG1 VAL A 96 5445 3643 2666 1170 -150 -422 C
ATOM 622 CG2 VAL A 96 10.916 -3.277 18.683 1.00 48.75 C
ANISOU 622 CG2 VAL A 96 7740 5747 5035 1226 -418 -452 C
ATOM 623 N CYS A 97 8.011 -3.234 20.395 1.00 42.62 N
ANISOU 623 N CYS A 97 6701 4910 4582 1140 -510 -337 N
ATOM 624 CA CYS A 97 6.571 -3.071 20.242 1.00 44.82 C
ANISOU 624 CA CYS A 97 6936 5126 4966 1140 -607 -321 C
ATOM 625 C CYS A 97 5.930 -2.660 21.560 1.00 51.29 C
ANISOU 625 C CYS A 97 7624 5981 5884 1080 -543 -258 C
ATOM 626 O CYS A 97 5.080 -1.763 21.592 1.00 36.25 O
ANISOU 626 O CYS A 97 5697 4066 4011 1074 -546 -241 O
ATOM 627 CB CYS A 97 5.943 -4.362 19.722 1.00 51.66 C
ANISOU 627 CB CYS A 97 7794 5907 5927 1161 -758 -341 C
ATOM 628 SG CYS A 97 6.281 -4.710 17.984 1.00 57.61 S
ANISOU 628 SG CYS A 97 8703 6605 6581 1241 -868 -422 S
ATOM 629 N GLY A 98 6.340 -3.296 22.659 1.00 59.95 N
ANISOU 629 N GLY A 98 8631 7121 7027 1036 -482 -222 N
ATOM 630 CA GLY A 98 5.754 -2.981 23.951 1.00 62.92 C
ANISOU 630 CA GLY A 98 8877 7535 7495 979 -419 -162 C
ATOM 631 C GLY A 98 6.030 -1.557 24.397 1.00 60.12 C
ANISOU 631 C GLY A 98 8520 7254 7068 962 -293 -150 C
ATOM 632 O GLY A 98 5.142 -0.881 24.922 1.00 65.83 O
ANISOU 632 O GLY A 98 9172 7983 7859 935 -279 -118 O
ATOM 633 N VAL A 99 7.261 -1.080 24.195 1.00 63.97 N
ANISOU 633 N VAL A 99 9084 7799 7422 976 -199 -177 N
ATOM 634 CA VAL A 99 7.568 0.294 24.578 1.00 60.97 C
ANISOU 634 CA VAL A 99 8705 7486 6975 962 -78 -171 C
ATOM 635 C VAL A 99 6.826 1.279 23.683 1.00 72.57 C
ANISOU 635 C VAL A 99 10239 8909 8427 993 -125 -189 C
ATOM 636 O VAL A 99 6.496 2.390 24.115 1.00 82.10 O
ANISOU 636 O VAL A 99 11410 10147 9638 973 -58 -170 O
ATOM 637 CB VAL A 99 9.089 0.543 24.557 1.00 54.82 C
ANISOU 637 CB VAL A 99 7992 6776 6062 970 35 -199 C
ATOM 638 CG1 VAL A 99 9.791 -0.386 25.534 1.00 69.23 C
ANISOU 638 CG1 VAL A 99 9745 8651 7907 938 85 -178 C
ATOM 639 CG2 VAL A 99 9.647 0.373 23.159 1.00 55.31 C
ANISOU 639 CG2 VAL A 99 8197 6795 6025 1028 -22 -254 C
ATOM 640 N SER A 100 6.544 0.898 22.434 1.00 50.52 N
ANISOU 640 N SER A 100 7538 6040 5616 1044 -243 -225 N
ATOM 641 CA SER A 100 5.758 1.765 21.564 1.00 32.38 C
ANISOU 641 CA SER A 100 5300 3695 3308 1077 -301 -239 C
ATOM 642 C SER A 100 4.333 1.918 22.078 1.00 47.88 C
ANISOU 642 C SER A 100 7160 5622 5409 1049 -357 -202 C
ATOM 643 O SER A 100 3.727 2.985 21.924 1.00 63.38 O
ANISOU 643 O SER A 100 9128 7578 7375 1054 -349 -196 O
ATOM 644 CB SER A 100 5.755 1.216 20.138 1.00 54.25 C
ANISOU 644 CB SER A 100 8188 6396 6030 1139 -422 -287 C
ATOM 645 OG SER A 100 4.972 2.032 19.284 1.00 74.23 O
ANISOU 645 OG SER A 100 10776 8880 8549 1175 -483 -298 O
ATOM 646 N MET A 101 3.790 0.868 22.691 1.00 45.37 N
ANISOU 646 N MET A 101 6748 5282 5210 1021 -414 -178 N
ATOM 647 CA MET A 101 2.466 0.954 23.292 1.00 45.57 C
ANISOU 647 CA MET A 101 6664 5278 5374 989 -459 -140 C
ATOM 648 C MET A 101 2.476 1.881 24.501 1.00 46.72 C
ANISOU 648 C MET A 101 6718 5502 5533 938 -328 -100 C
ATOM 649 O MET A 101 1.750 2.880 24.538 1.00 62.89 O
ANISOU 649 O MET A 101 8746 7545 7607 934 -319 -91 O
ATOM 650 CB MET A 101 1.983 -0.442 23.684 1.00 44.95 C
ANISOU 650 CB MET A 101 6505 5158 5417 969 -541 -121 C
ATOM 651 CG MET A 101 0.619 -0.458 24.343 1.00 41.99 C
ANISOU 651 CG MET A 101 6010 4751 5192 934 -587 -81 C
ATOM 652 SD MET A 101 0.469 -1.833 25.496 1.00 51.25 S
ANISOU 652 SD MET A 101 7051 5929 6492 883 -591 -32 S
ATOM 653 CE MET A 101 1.070 -3.192 24.495 1.00 84.26 C
ANISOU 653 CE MET A 101 11321 10049 10647 928 -694 -77 C
ATOM 654 N TYR A 102 3.316 1.574 25.496 1.00 37.27 N
ANISOU 654 N TYR A 102 5464 4379 4317 901 -225 -78 N
ATOM 655 CA TYR A 102 3.339 2.367 26.722 1.00 42.81 C
ANISOU 655 CA TYR A 102 6069 5160 5035 852 -101 -42 C
ATOM 656 C TYR A 102 3.713 3.819 26.458 1.00 44.93 C
ANISOU 656 C TYR A 102 6396 5467 5209 865 -16 -63 C
ATOM 657 O TYR A 102 3.227 4.717 27.153 1.00 57.22 O
ANISOU 657 O TYR A 102 7880 7057 6803 835 46 -41 O
ATOM 658 CB TYR A 102 4.304 1.757 27.739 1.00 52.51 C
ANISOU 658 CB TYR A 102 7241 6466 6244 818 -8 -21 C
ATOM 659 CG TYR A 102 3.831 0.455 28.345 1.00 48.92 C
ANISOU 659 CG TYR A 102 6696 5988 5905 792 -69 17 C
ATOM 660 CD1 TYR A 102 2.894 0.438 29.373 1.00 52.06 C
ANISOU 660 CD1 TYR A 102 6963 6399 6420 747 -60 67 C
ATOM 661 CD2 TYR A 102 4.331 -0.757 27.897 1.00 63.81 C
ANISOU 661 CD2 TYR A 102 8625 7839 7783 813 -132 2 C
ATOM 662 CE1 TYR A 102 2.467 -0.757 29.929 1.00 56.19 C
ANISOU 662 CE1 TYR A 102 7401 6898 7050 722 -112 106 C
ATOM 663 CE2 TYR A 102 3.911 -1.951 28.444 1.00 72.02 C
ANISOU 663 CE2 TYR A 102 9581 8852 8933 789 -186 38 C
ATOM 664 CZ TYR A 102 2.982 -1.948 29.459 1.00 67.68 C
ANISOU 664 CZ TYR A 102 8903 8315 8499 743 -175 92 C
ATOM 665 OH TYR A 102 2.573 -3.148 29.994 1.00 79.79 O
ANISOU 665 OH TYR A 102 10352 9819 10143 720 -226 132 O
ATOM 666 N ALA A 103 4.570 4.078 25.471 1.00 30.81 N
ANISOU 666 N ALA A 103 4736 3672 3300 909 -7 -104 N
ATOM 667 CA ALA A 103 4.919 5.462 25.173 1.00 39.62 C
ANISOU 667 CA ALA A 103 5909 4817 4328 922 74 -121 C
ATOM 668 C ALA A 103 3.738 6.197 24.552 1.00 55.12 C
ANISOU 668 C ALA A 103 7889 6716 6339 943 -3 -121 C
ATOM 669 O ALA A 103 3.346 7.271 25.025 1.00 39.60 O
ANISOU 669 O ALA A 103 5875 4776 4395 922 59 -107 O
ATOM 670 CB ALA A 103 6.138 5.520 24.256 1.00 39.36 C
ANISOU 670 CB ALA A 103 6010 4792 4154 964 103 -163 C
ATOM 671 N SER A 104 3.145 5.622 23.501 1.00 56.56 N
ANISOU 671 N SER A 104 8135 6814 6542 984 -141 -140 N
ATOM 672 CA SER A 104 2.054 6.298 22.806 1.00 53.80 C
ANISOU 672 CA SER A 104 7811 6401 6231 1011 -223 -143 C
ATOM 673 C SER A 104 0.877 6.572 23.731 1.00 53.46 C
ANISOU 673 C SER A 104 7635 6355 6322 967 -230 -106 C
ATOM 674 O SER A 104 0.218 7.611 23.604 1.00 50.29 O
ANISOU 674 O SER A 104 7229 5939 5939 972 -227 -102 O
ATOM 675 CB SER A 104 1.597 5.471 21.605 1.00 49.65 C
ANISOU 675 CB SER A 104 7363 5788 5712 1062 -378 -172 C
ATOM 676 OG SER A 104 2.634 5.329 20.652 1.00 47.39 O
ANISOU 676 OG SER A 104 7207 5505 5296 1108 -374 -209 O
ATOM 677 N VAL A 105 0.601 5.666 24.670 1.00 39.35 N
ANISOU 677 N VAL A 105 5738 4581 4630 925 -237 -78 N
ATOM 678 CA VAL A 105 -0.551 5.869 25.539 1.00 45.80 C
ANISOU 678 CA VAL A 105 6428 5396 5579 884 -246 -43 C
ATOM 679 C VAL A 105 -0.253 6.915 26.606 1.00 31.11 C
ANISOU 679 C VAL A 105 4495 3621 3702 842 -100 -22 C
ATOM 680 O VAL A 105 -1.159 7.631 27.046 1.00 44.82 O
ANISOU 680 O VAL A 105 6158 5356 5514 820 -93 -5 O
ATOM 681 CB VAL A 105 -1.005 4.536 26.160 1.00 47.02 C
ANISOU 681 CB VAL A 105 6489 5532 5845 854 -304 -16 C
ATOM 682 CG1 VAL A 105 -0.019 4.061 27.219 1.00 31.32 C
ANISOU 682 CG1 VAL A 105 4444 3628 3829 815 -194 7 C
ATOM 683 CG2 VAL A 105 -2.414 4.671 26.732 1.00 32.23 C
ANISOU 683 CG2 VAL A 105 4500 3629 4117 823 -350 15 C
ATOM 684 N TRP A 106 0.998 7.040 27.039 1.00 36.57 N
ANISOU 684 N TRP A 106 5204 4390 4300 830 17 -27 N
ATOM 685 CA TRP A 106 1.318 8.074 28.010 1.00 48.06 C
ANISOU 685 CA TRP A 106 6594 5929 5737 793 155 -15 C
ATOM 686 C TRP A 106 1.638 9.409 27.361 1.00 42.10 C
ANISOU 686 C TRP A 106 5924 5176 4896 821 206 -42 C
ATOM 687 O TRP A 106 1.491 10.447 28.014 1.00 60.65 O
ANISOU 687 O TRP A 106 8214 7571 7260 795 292 -35 O
ATOM 688 CB TRP A 106 2.478 7.632 28.907 1.00 29.36 C
ANISOU 688 CB TRP A 106 4189 3649 3317 764 264 -7 C
ATOM 689 CG TRP A 106 2.041 6.629 29.921 1.00 40.04 C
ANISOU 689 CG TRP A 106 5423 5021 4771 722 248 33 C
ATOM 690 CD1 TRP A 106 2.342 5.300 29.945 1.00 35.83 C
ANISOU 690 CD1 TRP A 106 4887 4473 4253 723 198 43 C
ATOM 691 CD2 TRP A 106 1.187 6.867 31.045 1.00 38.61 C
ANISOU 691 CD2 TRP A 106 5103 4872 4693 675 279 70 C
ATOM 692 NE1 TRP A 106 1.741 4.697 31.022 1.00 38.94 N
ANISOU 692 NE1 TRP A 106 5153 4888 4753 679 199 89 N
ATOM 693 CE2 TRP A 106 1.025 5.638 31.714 1.00 45.32 C
ANISOU 693 CE2 TRP A 106 5877 5729 5616 649 249 106 C
ATOM 694 CE3 TRP A 106 0.548 8.001 31.555 1.00 33.55 C
ANISOU 694 CE3 TRP A 106 4397 4258 4093 653 330 77 C
ATOM 695 CZ2 TRP A 106 0.256 5.511 32.868 1.00 53.89 C
ANISOU 695 CZ2 TRP A 106 6822 6847 6806 602 272 150 C
ATOM 696 CZ3 TRP A 106 -0.218 7.872 32.702 1.00 47.25 C
ANISOU 696 CZ3 TRP A 106 5993 6026 5932 606 351 116 C
ATOM 697 CH2 TRP A 106 -0.358 6.637 33.343 1.00 54.61 C
ANISOU 697 CH2 TRP A 106 6852 6966 6930 581 323 153 C
ATOM 698 N LEU A 107 2.052 9.414 26.093 1.00 34.77 N
ANISOU 698 N LEU A 107 5131 4200 3881 874 154 -73 N
ATOM 699 CA LEU A 107 2.251 10.683 25.406 1.00 30.16 C
ANISOU 699 CA LEU A 107 4629 3608 3222 904 194 -93 C
ATOM 700 C LEU A 107 0.917 11.353 25.106 1.00 41.52 C
ANISOU 700 C LEU A 107 6046 4987 4744 913 119 -83 C
ATOM 701 O LEU A 107 0.782 12.573 25.256 1.00 59.36 O
ANISOU 701 O LEU A 107 8294 7263 6997 907 185 -82 O
ATOM 702 CB LEU A 107 3.058 10.472 24.125 1.00 37.10 C
ANISOU 702 CB LEU A 107 5660 4455 3982 959 159 -126 C
ATOM 703 CG LEU A 107 4.545 10.139 24.289 1.00 48.37 C
ANISOU 703 CG LEU A 107 7130 5946 5304 956 255 -143 C
ATOM 704 CD1 LEU A 107 5.117 9.576 22.998 1.00 46.15 C
ANISOU 704 CD1 LEU A 107 6987 5620 4929 1011 186 -174 C
ATOM 705 CD2 LEU A 107 5.334 11.360 24.728 1.00 50.32 C
ANISOU 705 CD2 LEU A 107 7376 6261 5484 940 404 -149 C
ATOM 706 N ILE A 108 -0.085 10.575 24.691 1.00 43.49 N
ANISOU 706 N ILE A 108 6285 5164 5076 927 -19 -78 N
ATOM 707 CA ILE A 108 -1.406 11.159 24.486 1.00 50.79 C
ANISOU 707 CA ILE A 108 7175 6032 6089 933 -92 -69 C
ATOM 708 C ILE A 108 -2.030 11.531 25.824 1.00 42.85 C
ANISOU 708 C ILE A 108 6019 5072 5189 874 -29 -40 C
ATOM 709 O ILE A 108 -2.805 12.492 25.910 1.00 51.91 O
ANISOU 709 O ILE A 108 7132 6205 6388 870 -26 -35 O
ATOM 710 CB ILE A 108 -2.306 10.211 23.670 1.00 39.97 C
ANISOU 710 CB ILE A 108 5832 4572 4782 966 -260 -77 C
ATOM 711 CG1 ILE A 108 -2.573 8.909 24.427 1.00 52.46 C
ANISOU 711 CG1 ILE A 108 7317 6157 6457 929 -296 -57 C
ATOM 712 CG2 ILE A 108 -1.672 9.915 22.319 1.00 39.67 C
ANISOU 712 CG2 ILE A 108 5946 4495 4632 1028 -320 -110 C
ATOM 713 CD1 ILE A 108 -3.908 8.874 25.149 1.00 47.43 C
ANISOU 713 CD1 ILE A 108 6551 5497 5972 893 -341 -30 C
ATOM 714 N THR A 109 -1.704 10.791 26.888 1.00 43.06 N
ANISOU 714 N THR A 109 5955 5156 5250 829 24 -20 N
ATOM 715 CA THR A 109 -2.095 11.223 28.224 1.00 40.05 C
ANISOU 715 CA THR A 109 5434 4836 4946 773 108 6 C
ATOM 716 C THR A 109 -1.454 12.560 28.572 1.00 41.82 C
ANISOU 716 C THR A 109 5663 5126 5102 764 242 -6 C
ATOM 717 O THR A 109 -2.077 13.395 29.235 1.00 50.07 O
ANISOU 717 O THR A 109 6622 6193 6211 736 286 4 O
ATOM 718 CB THR A 109 -1.721 10.162 29.261 1.00 30.69 C
ANISOU 718 CB THR A 109 4161 3707 3792 731 147 31 C
ATOM 719 OG1 THR A 109 -2.332 8.914 28.913 1.00 42.15 O
ANISOU 719 OG1 THR A 109 5607 5091 5315 740 20 42 O
ATOM 720 CG2 THR A 109 -2.197 10.572 30.645 1.00 30.07 C
ANISOU 720 CG2 THR A 109 3935 3694 3795 675 228 60 C
ATOM 721 N ALA A 110 -0.221 12.789 28.115 1.00 43.00 N
ANISOU 721 N ALA A 110 5910 5303 5125 787 307 -29 N
ATOM 722 CA ALA A 110 0.424 14.075 28.351 1.00 46.96 C
ANISOU 722 CA ALA A 110 6423 5858 5562 781 433 -43 C
ATOM 723 C ALA A 110 -0.294 15.194 27.609 1.00 50.37 C
ANISOU 723 C ALA A 110 6899 6231 6007 810 396 -51 C
ATOM 724 O ALA A 110 -0.558 16.256 28.185 1.00 58.58 O
ANISOU 724 O ALA A 110 7876 7301 7080 787 470 -50 O
ATOM 725 CB ALA A 110 1.893 14.009 27.938 1.00 35.48 C
ANISOU 725 CB ALA A 110 5069 4440 3973 802 503 -67 C
ATOM 726 N MET A 111 -0.629 14.971 26.337 1.00 40.63 N
ANISOU 726 N MET A 111 5772 4914 4750 861 282 -61 N
ATOM 727 CA MET A 111 -1.341 15.991 25.575 1.00 44.28 C
ANISOU 727 CA MET A 111 6282 5316 5224 893 238 -65 C
ATOM 728 C MET A 111 -2.660 16.358 26.240 1.00 53.24 C
ANISOU 728 C MET A 111 7298 6437 6496 863 206 -47 C
ATOM 729 O MET A 111 -3.049 17.532 26.260 1.00 54.87 O
ANISOU 729 O MET A 111 7489 6636 6722 864 241 -48 O
ATOM 730 CB MET A 111 -1.583 15.508 24.148 1.00 51.75 C
ANISOU 730 CB MET A 111 7353 6177 6131 954 105 -77 C
ATOM 731 CG MET A 111 -0.316 15.243 23.375 1.00 56.57 C
ANISOU 731 CG MET A 111 8091 6800 6603 989 134 -97 C
ATOM 732 SD MET A 111 -0.625 15.106 21.608 1.00 74.86 S
ANISOU 732 SD MET A 111 10564 9021 8858 1069 -7 -114 S
ATOM 733 CE MET A 111 -1.792 13.752 21.584 1.00 81.70 C
ANISOU 733 CE MET A 111 11372 9828 9843 1067 -169 -110 C
ATOM 734 N SER A 112 -3.362 15.369 26.795 1.00 41.72 N
ANISOU 734 N SER A 112 5749 4969 5132 836 142 -30 N
ATOM 735 CA SER A 112 -4.618 15.666 27.471 1.00 36.76 C
ANISOU 735 CA SER A 112 5001 4329 4638 805 114 -13 C
ATOM 736 C SER A 112 -4.385 16.392 28.789 1.00 47.43 C
ANISOU 736 C SER A 112 6238 5770 6013 752 254 -6 C
ATOM 737 O SER A 112 -5.194 17.241 29.178 1.00 71.22 O
ANISOU 737 O SER A 112 9180 8780 9102 735 267 -3 O
ATOM 738 CB SER A 112 -5.407 14.379 27.699 1.00 36.20 C
ANISOU 738 CB SER A 112 4865 4224 4665 790 10 4 C
ATOM 739 OG SER A 112 -4.671 13.481 28.504 1.00 52.79 O
ANISOU 739 OG SER A 112 6918 6389 6750 756 69 17 O
ATOM 740 N LEU A 113 -3.293 16.077 29.488 1.00 52.66 N
ANISOU 740 N LEU A 113 6882 6514 6613 726 357 -6 N
ATOM 741 CA LEU A 113 -2.994 16.777 30.731 1.00 40.05 C
ANISOU 741 CA LEU A 113 5180 5009 5029 679 493 -4 C
ATOM 742 C LEU A 113 -2.505 18.193 30.472 1.00 37.85 C
ANISOU 742 C LEU A 113 4948 4745 4688 693 580 -28 C
ATOM 743 O LEU A 113 -2.771 19.094 31.275 1.00 53.74 O
ANISOU 743 O LEU A 113 6871 6801 6747 663 658 -32 O
ATOM 744 CB LEU A 113 -1.963 15.994 31.541 1.00 54.91 C
ANISOU 744 CB LEU A 113 7027 6975 6861 650 573 2 C
ATOM 745 CG LEU A 113 -2.534 14.836 32.357 1.00 49.30 C
ANISOU 745 CG LEU A 113 6213 6280 6241 615 531 34 C
ATOM 746 CD1 LEU A 113 -1.420 13.926 32.838 1.00 52.47 C
ANISOU 746 CD1 LEU A 113 6615 6746 6576 601 587 40 C
ATOM 747 CD2 LEU A 113 -3.341 15.367 33.534 1.00 48.06 C
ANISOU 747 CD2 LEU A 113 5908 6170 6183 568 582 50 C
ATOM 748 N ASP A 114 -1.793 18.413 29.367 1.00 41.87 N
ANISOU 748 N ASP A 114 5595 5218 5094 739 570 -46 N
ATOM 749 CA ASP A 114 -1.399 19.773 29.017 1.00 45.04 C
ANISOU 749 CA ASP A 114 6049 5622 5444 756 645 -64 C
ATOM 750 C ASP A 114 -2.610 20.635 28.672 1.00 52.72 C
ANISOU 750 C ASP A 114 7004 6529 6499 769 584 -60 C
ATOM 751 O ASP A 114 -2.605 21.844 28.935 1.00 63.38 O
ANISOU 751 O ASP A 114 8326 7897 7858 760 662 -70 O
ATOM 752 CB ASP A 114 -0.401 19.746 27.858 1.00 46.64 C
ANISOU 752 CB ASP A 114 6407 5797 5519 804 643 -80 C
ATOM 753 CG ASP A 114 -0.085 21.131 27.320 1.00 76.60 C
ANISOU 753 CG ASP A 114 10267 9576 9263 828 706 -93 C
ATOM 754 OD1 ASP A 114 0.322 22.010 28.113 1.00 67.56 O
ANISOU 754 OD1 ASP A 114 9057 8491 8120 798 828 -105 O
ATOM 755 OD2 ASP A 114 -0.233 21.336 26.096 1.00 80.92 O
ANISOU 755 OD2 ASP A 114 10929 10050 9767 879 633 -93 O
ATOM 756 N ARG A 115 -3.662 20.035 28.109 1.00 41.58 N
ANISOU 756 N ARG A 115 5603 5042 5153 789 444 -47 N
ATOM 757 CA ARG A 115 -4.840 20.811 27.741 1.00 44.24 C
ANISOU 757 CA ARG A 115 5925 5314 5570 805 377 -43 C
ATOM 758 C ARG A 115 -5.691 21.150 28.957 1.00 39.30 C
ANISOU 758 C ARG A 115 5141 4726 5067 753 412 -36 C
ATOM 759 O ARG A 115 -6.204 22.270 29.061 1.00 49.65 O
ANISOU 759 O ARG A 115 6417 6025 6423 751 439 -41 O
ATOM 760 CB ARG A 115 -5.671 20.056 26.704 1.00 48.21 C
ANISOU 760 CB ARG A 115 6492 5724 6101 847 212 -37 C
ATOM 761 CG ARG A 115 -6.816 20.875 26.123 1.00 70.45 C
ANISOU 761 CG ARG A 115 9315 8466 8986 874 133 -36 C
ATOM 762 CD ARG A 115 -7.386 20.211 24.882 1.00103.60 C
ANISOU 762 CD ARG A 115 13608 12574 13179 928 -25 -36 C
ATOM 763 NE ARG A 115 -6.328 19.775 23.974 1.00113.59 N
ANISOU 763 NE ARG A 115 15012 13835 14313 969 -30 -46 N
ATOM 764 CZ ARG A 115 -5.694 20.575 23.122 1.00117.17 C
ANISOU 764 CZ ARG A 115 15581 14274 14663 1010 3 -53 C
ATOM 765 NH1 ARG A 115 -6.005 21.863 23.056 1.00131.90 N
ANISOU 765 NH1 ARG A 115 17443 16125 16546 1017 43 -50 N
ATOM 766 NH2 ARG A 115 -4.743 20.087 22.338 1.00 91.06 N
ANISOU 766 NH2 ARG A 115 12393 10966 11239 1045 -1 -62 N
ATOM 767 N TYR A 116 -5.866 20.196 29.875 1.00 33.58 N
ANISOU 767 N TYR A 116 4318 4045 4397 712 413 -21 N
ATOM 768 CA TYR A 116 -6.575 20.494 31.115 1.00 30.67 C
ANISOU 768 CA TYR A 116 3794 3725 4135 661 461 -14 C
ATOM 769 C TYR A 116 -5.873 21.602 31.887 1.00 49.76 C
ANISOU 769 C TYR A 116 6166 6223 6517 635 612 -32 C
ATOM 770 O TYR A 116 -6.526 22.520 32.398 1.00 47.73 O
ANISOU 770 O TYR A 116 5826 5975 6333 615 646 -39 O
ATOM 771 CB TYR A 116 -6.695 19.234 31.975 1.00 35.86 C
ANISOU 771 CB TYR A 116 4362 4423 4839 622 449 9 C
ATOM 772 CG TYR A 116 -7.145 19.506 33.399 1.00 40.95 C
ANISOU 772 CG TYR A 116 4847 5143 5570 565 527 18 C
ATOM 773 CD1 TYR A 116 -8.488 19.693 33.704 1.00 44.39 C
ANISOU 773 CD1 TYR A 116 5189 5545 6133 549 469 27 C
ATOM 774 CD2 TYR A 116 -6.224 19.576 34.437 1.00 36.79 C
ANISOU 774 CD2 TYR A 116 4260 4723 4995 530 659 14 C
ATOM 775 CE1 TYR A 116 -8.900 19.947 35.003 1.00 45.76 C
ANISOU 775 CE1 TYR A 116 5216 5791 6381 498 543 34 C
ATOM 776 CE2 TYR A 116 -6.627 19.830 35.737 1.00 46.28 C
ANISOU 776 CE2 TYR A 116 5317 5999 6269 481 731 21 C
ATOM 777 CZ TYR A 116 -7.965 20.012 36.015 1.00 50.48 C
ANISOU 777 CZ TYR A 116 5758 6497 6925 464 674 31 C
ATOM 778 OH TYR A 116 -8.363 20.259 37.311 1.00 89.90 O
ANISOU 778 OH TYR A 116 10605 11567 11986 416 748 36 O
ATOM 779 N LEU A 117 -4.541 21.538 31.971 1.00 32.14 N
ANISOU 779 N LEU A 117 3985 4049 4176 635 704 -43 N
ATOM 780 CA LEU A 117 -3.793 22.571 32.679 1.00 30.49 C
ANISOU 780 CA LEU A 117 3735 3918 3932 612 849 -66 C
ATOM 781 C LEU A 117 -3.949 23.929 32.004 1.00 53.87 C
ANISOU 781 C LEU A 117 6750 6830 6887 640 864 -83 C
ATOM 782 O LEU A 117 -4.008 24.963 32.680 1.00 49.74 O
ANISOU 782 O LEU A 117 6151 6348 6398 616 952 -100 O
ATOM 783 CB LEU A 117 -2.319 22.182 32.762 1.00 34.85 C
ANISOU 783 CB LEU A 117 4343 4532 4365 613 934 -77 C
ATOM 784 CG LEU A 117 -1.457 23.011 33.717 1.00 36.71 C
ANISOU 784 CG LEU A 117 4515 4866 4568 582 1091 -103 C
ATOM 785 CD1 LEU A 117 -1.887 22.785 35.155 1.00 51.67 C
ANISOU 785 CD1 LEU A 117 6250 6842 6541 529 1138 -96 C
ATOM 786 CD2 LEU A 117 0.018 22.689 33.540 1.00 46.13 C
ANISOU 786 CD2 LEU A 117 5787 6102 5637 592 1162 -118 C
ATOM 787 N ALA A 118 -4.033 23.943 30.670 1.00 51.71 N
ANISOU 787 N ALA A 118 6608 6470 6571 692 776 -79 N
ATOM 788 CA ALA A 118 -4.149 25.201 29.941 1.00 30.14 C
ANISOU 788 CA ALA A 118 3939 3686 3827 724 785 -89 C
ATOM 789 C ALA A 118 -5.466 25.912 30.227 1.00 32.55 C
ANISOU 789 C ALA A 118 4155 3956 4256 713 745 -87 C
ATOM 790 O ALA A 118 -5.521 27.146 30.184 1.00 63.13 O
ANISOU 790 O ALA A 118 8024 7820 8143 718 799 -99 O
ATOM 791 CB ALA A 118 -4.001 24.954 28.441 1.00 33.89 C
ANISOU 791 CB ALA A 118 4574 4078 4227 785 691 -82 C
ATOM 792 N VAL A 119 -6.529 25.164 30.518 1.00 34.13 N
ANISOU 792 N VAL A 119 4283 4135 4551 698 652 -71 N
ATOM 793 CA VAL A 119 -7.841 25.764 30.733 1.00 39.25 C
ANISOU 793 CA VAL A 119 4848 4745 5322 689 603 -69 C
ATOM 794 C VAL A 119 -8.105 25.939 32.223 1.00 45.55 C
ANISOU 794 C VAL A 119 5481 5627 6199 628 690 -76 C
ATOM 795 O VAL A 119 -8.786 26.886 32.634 1.00 51.47 O
ANISOU 795 O VAL A 119 6152 6375 7028 614 714 -87 O
ATOM 796 CB VAL A 119 -8.949 24.927 30.066 1.00 31.78 C
ANISOU 796 CB VAL A 119 3922 3715 4440 713 441 -51 C
ATOM 797 CG1 VAL A 119 -8.711 24.846 28.567 1.00 50.55 C
ANISOU 797 CG1 VAL A 119 6462 6011 6734 777 354 -48 C
ATOM 798 CG2 VAL A 119 -9.007 23.539 30.661 1.00 44.08 C
ANISOU 798 CG2 VAL A 119 5421 5307 6022 683 410 -35 C
ATOM 799 N ALA A 120 -7.561 25.037 33.045 1.00 39.55 N
ANISOU 799 N ALA A 120 4668 4944 5416 594 737 -69 N
ATOM 800 CA ALA A 120 -7.811 25.098 34.481 1.00 36.98 C
ANISOU 800 CA ALA A 120 4186 4706 5160 538 817 -73 C
ATOM 801 C ALA A 120 -6.932 26.142 35.158 1.00 41.21 C
ANISOU 801 C ALA A 120 4685 5322 5650 518 968 -103 C
ATOM 802 O ALA A 120 -7.426 26.977 35.923 1.00 60.44 O
ANISOU 802 O ALA A 120 7014 7791 8159 491 1023 -120 O
ATOM 803 CB ALA A 120 -7.595 23.724 35.111 1.00 34.28 C
ANISOU 803 CB ALA A 120 3797 4414 4812 511 809 -50 C
ATOM 804 N ARG A 121 -5.625 26.106 34.897 1.00 29.25 N
ANISOU 804 N ARG A 121 3255 3840 4020 532 1036 -114 N
ATOM 805 CA ARG A 121 -4.671 27.060 35.461 1.00 30.97 C
ANISOU 805 CA ARG A 121 3448 4131 4188 516 1180 -147 C
ATOM 806 C ARG A 121 -3.840 27.640 34.328 1.00 34.26 C
ANISOU 806 C ARG A 121 4010 4497 4509 561 1194 -158 C
ATOM 807 O ARG A 121 -2.730 27.165 34.054 1.00 52.09 O
ANISOU 807 O ARG A 121 6347 6780 6664 572 1230 -161 O
ATOM 808 CB ARG A 121 -3.776 26.402 36.508 1.00 42.20 C
ANISOU 808 CB ARG A 121 4808 5664 5561 480 1272 -152 C
ATOM 809 CG ARG A 121 -4.138 26.745 37.946 1.00 70.84 C
ANISOU 809 CG ARG A 121 8270 9383 9261 430 1352 -165 C
ATOM 810 CD ARG A 121 -4.244 28.253 38.142 1.00 52.20 C
ANISOU 810 CD ARG A 121 5869 7029 6936 426 1428 -203 C
ATOM 811 NE ARG A 121 -4.357 28.624 39.551 1.00 28.24 N
ANISOU 811 NE ARG A 121 2682 4098 3952 380 1523 -225 N
ATOM 812 CZ ARG A 121 -5.492 28.592 40.244 1.00 56.09 C
ANISOU 812 CZ ARG A 121 6090 7636 7585 353 1492 -217 C
ATOM 813 NH1 ARG A 121 -6.617 28.197 39.659 1.00 50.67 N
ANISOU 813 NH1 ARG A 121 5420 6862 6971 366 1368 -187 N
ATOM 814 NH2 ARG A 121 -5.504 28.952 41.523 1.00 49.04 N
ANISOU 814 NH2 ARG A 121 5061 6844 6727 313 1586 -241 N
ATOM 815 N PRO A 122 -4.344 28.671 33.646 1.00 33.21 N
ANISOU 815 N PRO A 122 3917 4294 4409 587 1169 -164 N
ATOM 816 CA PRO A 122 -3.603 29.216 32.496 1.00 37.46 C
ANISOU 816 CA PRO A 122 4599 4777 4856 632 1178 -168 C
ATOM 817 C PRO A 122 -2.252 29.808 32.867 1.00 52.85 C
ANISOU 817 C PRO A 122 6559 6797 6725 621 1324 -198 C
ATOM 818 O PRO A 122 -1.305 29.710 32.075 1.00 38.09 O
ANISOU 818 O PRO A 122 4810 4910 4753 651 1340 -197 O
ATOM 819 CB PRO A 122 -4.562 30.279 31.938 1.00 35.28 C
ANISOU 819 CB PRO A 122 4332 4421 4653 655 1129 -166 C
ATOM 820 CG PRO A 122 -5.919 29.864 32.431 1.00 33.22 C
ANISOU 820 CG PRO A 122 3966 4145 4511 634 1043 -153 C
ATOM 821 CD PRO A 122 -5.667 29.292 33.798 1.00 39.60 C
ANISOU 821 CD PRO A 122 4649 5060 5339 580 1117 -162 C
ATOM 822 N PHE A 123 -2.123 30.410 34.053 1.00 59.42 N
ANISOU 822 N PHE A 123 7266 7710 7601 578 1431 -226 N
ATOM 823 CA PHE A 123 -0.835 30.970 34.444 1.00 43.66 C
ANISOU 823 CA PHE A 123 5273 5783 5534 567 1570 -260 C
ATOM 824 C PHE A 123 0.190 29.879 34.719 1.00 41.94 C
ANISOU 824 C PHE A 123 5079 5632 5226 558 1601 -259 C
ATOM 825 O PHE A 123 1.388 30.086 34.493 1.00 53.41 O
ANISOU 825 O PHE A 123 6597 7108 6587 568 1681 -278 O
ATOM 826 CB PHE A 123 -0.994 31.862 35.672 1.00 40.34 C
ANISOU 826 CB PHE A 123 4706 5435 5185 525 1672 -296 C
ATOM 827 CG PHE A 123 0.298 32.420 36.177 1.00 49.77 C
ANISOU 827 CG PHE A 123 5888 6706 6316 511 1815 -337 C
ATOM 828 CD1 PHE A 123 0.835 33.566 35.620 1.00 54.45 C
ANISOU 828 CD1 PHE A 123 6544 7265 6882 524 1847 -355 C
ATOM 829 CD2 PHE A 123 0.985 31.793 37.202 1.00 56.34 C
ANISOU 829 CD2 PHE A 123 6657 7650 7097 458 1779 -342 C
ATOM 830 CE1 PHE A 123 2.024 34.081 36.078 1.00 57.25 C
ANISOU 830 CE1 PHE A 123 6891 7695 7167 477 1808 -375 C
ATOM 831 CE2 PHE A 123 2.177 32.302 37.665 1.00 57.88 C
ANISOU 831 CE2 PHE A 123 6852 7924 7216 422 1736 -362 C
ATOM 832 CZ PHE A 123 2.698 33.448 37.104 1.00 78.09 C
ANISOU 832 CZ PHE A 123 9466 10448 9757 432 1750 -378 C
ATOM 833 N VAL A 124 -0.257 28.725 35.219 1.00 51.79 N
ANISOU 833 N VAL A 124 6272 6907 6500 539 1541 -237 N
ATOM 834 CA VAL A 124 0.652 27.614 35.481 1.00 33.59 C
ANISOU 834 CA VAL A 124 3987 4661 4116 531 1562 -232 C
ATOM 835 C VAL A 124 1.054 26.929 34.182 1.00 38.29 C
ANISOU 835 C VAL A 124 4737 5182 4629 576 1482 -211 C
ATOM 836 O VAL A 124 2.199 26.490 34.029 1.00 45.50 O
ANISOU 836 O VAL A 124 5713 6129 5446 584 1528 -221 O
ATOM 837 CB VAL A 124 0.008 26.623 36.466 1.00 37.57 C
ANISOU 837 CB VAL A 124 4376 5216 4682 495 1526 -210 C
ATOM 838 CG1 VAL A 124 0.893 25.404 36.649 1.00 38.05 C
ANISOU 838 CG1 VAL A 124 4465 5326 4665 492 1534 -199 C
ATOM 839 CG2 VAL A 124 -0.265 27.301 37.803 1.00 44.11 C
ANISOU 839 CG2 VAL A 124 5050 6130 5578 451 1618 -234 C
ATOM 840 N SER A 125 0.124 26.818 33.231 1.00 35.27 N
ANISOU 840 N SER A 125 4416 4701 4282 608 1359 -186 N
ATOM 841 CA SER A 125 0.476 26.279 31.922 1.00 28.09 C
ANISOU 841 CA SER A 125 3659 3721 3292 655 1281 -171 C
ATOM 842 C SER A 125 1.511 27.158 31.240 1.00 38.40 C
ANISOU 842 C SER A 125 5067 5016 4508 682 1360 -192 C
ATOM 843 O SER A 125 2.526 26.665 30.739 1.00 60.89 O
ANISOU 843 O SER A 125 8008 7872 7255 702 1379 -196 O
ATOM 844 CB SER A 125 -0.769 26.147 31.051 1.00 34.91 C
ANISOU 844 CB SER A 125 4564 4484 4217 686 1138 -145 C
ATOM 845 OG SER A 125 -0.445 25.539 29.813 1.00 64.77 O
ANISOU 845 OG SER A 125 8488 8203 7918 733 1057 -134 O
ATOM 846 N GLN A 126 1.277 28.472 31.229 1.00 52.63 N
ANISOU 846 N GLN A 126 6850 6800 6348 683 1412 -205 N
ATOM 847 CA GLN A 126 2.254 29.399 30.664 1.00 44.91 C
ANISOU 847 CA GLN A 126 5957 5813 5295 705 1499 -224 C
ATOM 848 C GLN A 126 3.605 29.280 31.359 1.00 39.25 C
ANISOU 848 C GLN A 126 5218 5190 4507 680 1626 -254 C
ATOM 849 O GLN A 126 4.649 29.509 30.736 1.00 30.02 O
ANISOU 849 O GLN A 126 4147 4015 3245 703 1681 -266 O
ATOM 850 CB GLN A 126 1.718 30.830 30.761 1.00 43.18 C
ANISOU 850 CB GLN A 126 5693 5565 5147 702 1540 -234 C
ATOM 851 CG GLN A 126 2.580 31.893 30.107 1.00 28.43 C
ANISOU 851 CG GLN A 126 3913 3673 3217 727 1625 -248 C
ATOM 852 CD GLN A 126 1.983 33.280 30.249 1.00 54.97 C
ANISOU 852 CD GLN A 126 7220 7003 6662 723 1661 -257 C
ATOM 853 OE1 GLN A 126 2.308 34.016 31.181 1.00 42.18 O
ANISOU 853 OE1 GLN A 126 5504 5444 5080 688 1773 -292 O
ATOM 854 NE2 GLN A 126 1.098 33.641 29.325 1.00 51.34 N
ANISOU 854 NE2 GLN A 126 6822 6448 6235 759 1566 -228 N
ATOM 855 N LYS A 127 3.608 28.896 32.637 1.00 50.12 N
ANISOU 855 N LYS A 127 6466 6654 5923 635 1674 -268 N
ATOM 856 CA LYS A 127 4.847 28.823 33.401 1.00 45.05 C
ANISOU 856 CA LYS A 127 5779 6108 5229 592 1744 -298 C
ATOM 857 C LYS A 127 5.598 27.522 33.144 1.00 41.53 C
ANISOU 857 C LYS A 127 5397 5680 4701 600 1709 -288 C
ATOM 858 O LYS A 127 6.833 27.521 33.089 1.00 58.54 O
ANISOU 858 O LYS A 127 7568 7874 6801 562 1673 -307 O
ATOM 859 CB LYS A 127 4.543 28.983 34.894 1.00 48.75 C
ANISOU 859 CB LYS A 127 6076 6670 5776 521 1728 -314 C
ATOM 860 CG LYS A 127 5.769 29.129 35.781 1.00 76.55 C
ANISOU 860 CG LYS A 127 9525 10300 9259 453 1671 -343 C
ATOM 861 CD LYS A 127 5.390 29.185 37.259 1.00 78.01 C
ANISOU 861 CD LYS A 127 9561 10585 9495 407 1641 -349 C
ATOM 862 CE LYS A 127 4.883 27.835 37.759 1.00 59.00 C
ANISOU 862 CE LYS A 127 7113 8202 7102 401 1636 -326 C
ATOM 863 NZ LYS A 127 4.507 27.869 39.201 1.00 58.08 N
ANISOU 863 NZ LYS A 127 6859 8187 7023 361 1602 -322 N
ATOM 864 N LEU A 128 4.879 26.410 32.969 1.00 61.82 N
ANISOU 864 N LEU A 128 7986 8222 7283 626 1649 -256 N
ATOM 865 CA LEU A 128 5.500 25.095 32.858 1.00 61.77 C
ANISOU 865 CA LEU A 128 8024 8236 7210 632 1616 -246 C
ATOM 866 C LEU A 128 5.530 24.531 31.444 1.00 60.99 C
ANISOU 866 C LEU A 128 8074 8049 7051 681 1513 -227 C
ATOM 867 O LEU A 128 6.128 23.472 31.236 1.00 74.66 O
ANISOU 867 O LEU A 128 9855 9792 8722 690 1486 -222 O
ATOM 868 CB LEU A 128 4.785 24.090 33.773 1.00 31.54 C
ANISOU 868 CB LEU A 128 4087 4447 3451 599 1564 -223 C
ATOM 869 CG LEU A 128 4.804 24.406 35.266 1.00 39.66 C
ANISOU 869 CG LEU A 128 4963 5577 4529 550 1661 -239 C
ATOM 870 CD1 LEU A 128 4.142 23.288 36.058 1.00 45.66 C
ANISOU 870 CD1 LEU A 128 5629 6371 5348 523 1604 -208 C
ATOM 871 CD2 LEU A 128 6.228 24.644 35.744 1.00 64.52 C
ANISOU 871 CD2 LEU A 128 8086 8805 7625 484 1630 -279 C
ATOM 872 N ARG A 129 4.898 25.185 30.473 1.00 48.85 N
ANISOU 872 N ARG A 129 6607 6424 5529 714 1453 -216 N
ATOM 873 CA ARG A 129 4.910 24.686 29.099 1.00 43.71 C
ANISOU 873 CA ARG A 129 6100 5693 4817 765 1353 -199 C
ATOM 874 C ARG A 129 6.119 25.274 28.369 1.00 44.54 C
ANISOU 874 C ARG A 129 6317 5794 4813 792 1434 -219 C
ATOM 875 O ARG A 129 6.017 26.140 27.498 1.00 63.90 O
ANISOU 875 O ARG A 129 8848 8185 7244 825 1429 -215 O
ATOM 876 CB ARG A 129 3.596 25.013 28.400 1.00 49.58 C
ANISOU 876 CB ARG A 129 6865 6345 5629 790 1239 -175 C
ATOM 877 CG ARG A 129 3.442 24.441 27.002 1.00 36.31 C
ANISOU 877 CG ARG A 129 5323 4581 3892 845 1120 -159 C
ATOM 878 CD ARG A 129 2.045 24.689 26.461 1.00 37.11 C
ANISOU 878 CD ARG A 129 5426 4600 4074 867 1001 -137 C
ATOM 879 NE ARG A 129 2.011 24.573 25.008 1.00 62.44 N
ANISOU 879 NE ARG A 129 8781 7729 7215 927 910 -127 N
ATOM 880 CZ ARG A 129 1.863 23.426 24.354 1.00 59.86 C
ANISOU 880 CZ ARG A 129 8517 7366 6860 954 800 -120 C
ATOM 881 NH1 ARG A 129 1.732 22.293 25.026 1.00 70.19 N
ANISOU 881 NH1 ARG A 129 9755 8709 8207 925 766 -119 N
ATOM 882 NH2 ARG A 129 1.850 23.413 23.029 1.00 65.75 N
ANISOU 882 NH2 ARG A 129 9397 8046 7540 1011 722 -114 N
ATOM 883 N THR A 130 7.290 24.783 28.762 1.00 45.21 N
ANISOU 883 N THR A 130 6405 5947 4827 779 1511 -240 N
ATOM 884 CA THR A 130 8.562 25.152 28.159 1.00 50.75 C
ANISOU 884 CA THR A 130 7196 6654 5433 790 1573 -260 C
ATOM 885 C THR A 130 9.155 23.955 27.428 1.00 50.62 C
ANISOU 885 C THR A 130 7283 6624 5328 821 1517 -257 C
ATOM 886 O THR A 130 8.752 22.808 27.636 1.00 59.89 O
ANISOU 886 O THR A 130 8438 7801 6517 823 1448 -244 O
ATOM 887 CB THR A 130 9.551 25.659 29.219 1.00 63.80 C
ANISOU 887 CB THR A 130 8697 8395 7150 683 1579 -285 C
ATOM 888 OG1 THR A 130 9.686 24.684 30.264 1.00 51.00 O
ANISOU 888 OG1 THR A 130 6976 6846 5554 640 1562 -291 O
ATOM 889 CG2 THR A 130 9.073 26.975 29.816 1.00 51.26 C
ANISOU 889 CG2 THR A 130 7018 6818 5639 654 1620 -295 C
ATOM 890 N LYS A 131 10.125 24.235 26.556 1.00 47.39 N
ANISOU 890 N LYS A 131 6946 6194 4868 815 1495 -262 N
ATOM 891 CA LYS A 131 10.810 23.147 25.865 1.00 45.60 C
ANISOU 891 CA LYS A 131 6803 5957 4566 835 1441 -263 C
ATOM 892 C LYS A 131 11.630 22.300 26.832 1.00 49.51 C
ANISOU 892 C LYS A 131 7186 6532 5095 763 1430 -277 C
ATOM 893 O LYS A 131 11.862 21.114 26.569 1.00 49.09 O
ANISOU 893 O LYS A 131 7182 6477 4995 786 1389 -276 O
ATOM 894 CB LYS A 131 11.695 23.706 24.749 1.00 55.35 C
ANISOU 894 CB LYS A 131 8122 7156 5751 840 1426 -263 C
ATOM 895 CG LYS A 131 10.932 24.103 23.487 1.00 70.70 C
ANISOU 895 CG LYS A 131 10226 9012 7625 932 1409 -246 C
ATOM 896 CD LYS A 131 11.590 25.280 22.767 1.00 76.11 C
ANISOU 896 CD LYS A 131 10944 9671 8303 920 1433 -239 C
ATOM 897 CE LYS A 131 13.025 24.973 22.365 1.00 71.66 C
ANISOU 897 CE LYS A 131 10376 9134 7719 877 1412 -247 C
ATOM 898 NZ LYS A 131 13.108 23.875 21.364 1.00 95.44 N
ANISOU 898 NZ LYS A 131 13512 12110 10642 934 1345 -243 N
ATOM 899 N ALA A 132 12.061 22.884 27.955 1.00 50.98 N
ANISOU 899 N ALA A 132 7223 6790 5357 682 1458 -294 N
ATOM 900 CA ALA A 132 12.799 22.126 28.961 1.00 32.31 C
ANISOU 900 CA ALA A 132 4748 4506 3022 617 1440 -311 C
ATOM 901 C ALA A 132 11.888 21.149 29.689 1.00 45.03 C
ANISOU 901 C ALA A 132 6325 6133 4650 634 1445 -294 C
ATOM 902 O ALA A 132 12.198 19.956 29.796 1.00 58.88 O
ANISOU 902 O ALA A 132 8089 7904 6378 637 1418 -291 O
ATOM 903 CB ALA A 132 13.458 23.076 29.959 1.00 25.10 C
ANISOU 903 CB ALA A 132 3693 3670 2172 536 1450 -340 C
ATOM 904 N MET A 133 10.766 21.645 30.217 1.00 45.01 N
ANISOU 904 N MET A 133 6275 6128 4697 647 1482 -282 N
ATOM 905 CA MET A 133 9.793 20.757 30.840 1.00 44.45 C
ANISOU 905 CA MET A 133 6171 6069 4650 674 1493 -258 C
ATOM 906 C MET A 133 9.333 19.685 29.865 1.00 52.73 C
ANISOU 906 C MET A 133 7342 7049 5643 749 1428 -237 C
ATOM 907 O MET A 133 9.122 18.529 30.254 1.00 49.56 O
ANISOU 907 O MET A 133 6900 6662 5270 736 1369 -220 O
ATOM 908 CB MET A 133 8.607 21.564 31.359 1.00 32.35 C
ANISOU 908 CB MET A 133 4572 4532 3188 683 1540 -247 C
ATOM 909 CG MET A 133 8.674 21.861 32.843 1.00 56.96 C
ANISOU 909 CG MET A 133 7514 7739 6391 595 1553 -260 C
ATOM 910 SD MET A 133 8.499 20.359 33.822 1.00 99.01 S
ANISOU 910 SD MET A 133 12761 13123 11736 579 1543 -236 S
ATOM 911 CE MET A 133 6.863 19.824 33.325 1.00 63.20 C
ANISOU 911 CE MET A 133 8243 8502 7268 624 1452 -189 C
ATOM 912 N ALA A 134 9.197 20.044 28.586 1.00 37.87 N
ANISOU 912 N ALA A 134 5580 5087 3721 793 1373 -236 N
ATOM 913 CA ALA A 134 8.849 19.057 27.573 1.00 29.89 C
ANISOU 913 CA ALA A 134 4661 4006 2691 831 1240 -221 C
ATOM 914 C ALA A 134 9.896 17.953 27.509 1.00 40.01 C
ANISOU 914 C ALA A 134 5986 5320 3897 836 1248 -235 C
ATOM 915 O ALA A 134 9.582 16.770 27.678 1.00 44.82 O
ANISOU 915 O ALA A 134 6568 5922 4538 831 1167 -220 O
ATOM 916 CB ALA A 134 8.689 19.737 26.214 1.00 33.24 C
ANISOU 916 CB ALA A 134 5212 4350 3068 880 1197 -221 C
ATOM 917 N ARG A 135 11.161 18.328 27.291 1.00 45.35 N
ANISOU 917 N ARG A 135 6716 6029 4485 839 1337 -263 N
ATOM 918 CA ARG A 135 12.229 17.336 27.196 1.00 38.47 C
ANISOU 918 CA ARG A 135 5849 5182 3586 812 1301 -273 C
ATOM 919 C ARG A 135 12.351 16.502 28.464 1.00 33.85 C
ANISOU 919 C ARG A 135 5144 4667 3050 766 1316 -268 C
ATOM 920 O ARG A 135 12.797 15.351 28.407 1.00 39.87 O
ANISOU 920 O ARG A 135 5930 5437 3782 774 1284 -269 O
ATOM 921 CB ARG A 135 13.558 18.023 26.886 1.00 53.02 C
ANISOU 921 CB ARG A 135 7665 7044 5437 750 1302 -293 C
ATOM 922 CG ARG A 135 13.884 18.046 25.408 1.00 65.94 C
ANISOU 922 CG ARG A 135 9442 8614 6998 801 1262 -295 C
ATOM 923 CD ARG A 135 14.449 19.381 24.983 1.00 47.19 C
ANISOU 923 CD ARG A 135 7059 6232 4638 771 1288 -299 C
ATOM 924 NE ARG A 135 14.659 19.425 23.540 1.00 60.95 N
ANISOU 924 NE ARG A 135 8940 7911 6308 825 1252 -295 N
ATOM 925 CZ ARG A 135 14.904 20.536 22.856 1.00 67.96 C
ANISOU 925 CZ ARG A 135 9864 8770 7187 828 1271 -289 C
ATOM 926 NH1 ARG A 135 14.968 21.701 23.486 1.00 65.25 N
ANISOU 926 NH1 ARG A 135 9430 8455 6907 781 1324 -291 N
ATOM 927 NH2 ARG A 135 15.079 20.483 21.542 1.00 72.22 N
ANISOU 927 NH2 ARG A 135 10530 9254 7657 879 1235 -282 N
ATOM 928 N ARG A 136 11.961 17.055 29.612 1.00 33.66 N
ANISOU 928 N ARG A 136 4992 4695 3104 717 1363 -262 N
ATOM 929 CA ARG A 136 11.994 16.273 30.841 1.00 33.94 C
ANISOU 929 CA ARG A 136 4912 4798 3185 674 1375 -253 C
ATOM 930 C ARG A 136 10.875 15.236 30.864 1.00 47.35 C
ANISOU 930 C ARG A 136 6627 6466 4897 727 1334 -217 C
ATOM 931 O ARG A 136 11.123 14.054 31.130 1.00 42.77 O
ANISOU 931 O ARG A 136 6032 5904 4317 722 1298 -206 O
ATOM 932 CB ARG A 136 11.919 17.197 32.056 1.00 44.45 C
ANISOU 932 CB ARG A 136 6092 6196 4601 595 1410 -262 C
ATOM 933 CG ARG A 136 13.255 17.371 32.764 1.00 45.79 C
ANISOU 933 CG ARG A 136 6166 6439 4794 502 1390 -300 C
ATOM 934 CD ARG A 136 13.157 18.338 33.927 1.00 69.56 C
ANISOU 934 CD ARG A 136 9039 9519 7871 434 1405 -321 C
ATOM 935 NE ARG A 136 13.296 19.724 33.494 1.00 76.28 N
ANISOU 935 NE ARG A 136 9898 10357 8729 430 1411 -341 N
ATOM 936 CZ ARG A 136 14.460 20.358 33.401 1.00 89.80 C
ANISOU 936 CZ ARG A 136 11585 12104 10431 391 1386 -375 C
ATOM 937 NH1 ARG A 136 15.585 19.726 33.711 1.00 86.21 N
ANISOU 937 NH1 ARG A 136 11094 11701 9960 353 1352 -397 N
ATOM 938 NH2 ARG A 136 14.502 21.621 32.998 1.00 79.59 N
ANISOU 938 NH2 ARG A 136 10301 10795 9146 396 1397 -384 N
ATOM 939 N VAL A 137 9.637 15.649 30.571 1.00 38.44 N
ANISOU 939 N VAL A 137 5484 5277 3844 732 1261 -196 N
ATOM 940 CA VAL A 137 8.535 14.690 30.599 1.00 30.64 C
ANISOU 940 CA VAL A 137 4456 4242 2942 728 1137 -161 C
ATOM 941 C VAL A 137 8.648 13.707 29.441 1.00 41.88 C
ANISOU 941 C VAL A 137 5993 5594 4324 770 1027 -163 C
ATOM 942 O VAL A 137 8.327 12.521 29.587 1.00 52.38 O
ANISOU 942 O VAL A 137 7296 6909 5697 765 948 -143 O
ATOM 943 CB VAL A 137 7.171 15.409 30.604 1.00 38.26 C
ANISOU 943 CB VAL A 137 5371 5162 4003 721 1086 -143 C
ATOM 944 CG1 VAL A 137 7.056 16.335 31.803 1.00 50.98 C
ANISOU 944 CG1 VAL A 137 6863 6849 5660 678 1195 -144 C
ATOM 945 CG2 VAL A 137 6.946 16.177 29.316 1.00 51.69 C
ANISOU 945 CG2 VAL A 137 7188 6784 5668 765 1042 -155 C
ATOM 946 N LEU A 138 9.107 14.175 28.276 1.00 38.16 N
ANISOU 946 N LEU A 138 5651 5079 3771 812 1020 -187 N
ATOM 947 CA LEU A 138 9.280 13.283 27.132 1.00 27.67 C
ANISOU 947 CA LEU A 138 4434 3687 2391 856 920 -195 C
ATOM 948 C LEU A 138 10.301 12.197 27.439 1.00 39.71 C
ANISOU 948 C LEU A 138 5962 5257 3868 849 944 -206 C
ATOM 949 O LEU A 138 10.022 11.002 27.288 1.00 45.62 O
ANISOU 949 O LEU A 138 6711 5974 4648 856 849 -194 O
ATOM 950 CB LEU A 138 9.698 14.085 25.902 1.00 33.74 C
ANISOU 950 CB LEU A 138 5337 4413 3069 901 929 -219 C
ATOM 951 CG LEU A 138 8.630 15.004 25.308 1.00 49.26 C
ANISOU 951 CG LEU A 138 7325 6315 5077 921 874 -206 C
ATOM 952 CD1 LEU A 138 9.257 15.985 24.335 1.00 47.18 C
ANISOU 952 CD1 LEU A 138 7180 6032 4716 958 923 -226 C
ATOM 953 CD2 LEU A 138 7.550 14.186 24.627 1.00 53.57 C
ANISOU 953 CD2 LEU A 138 7895 6780 5679 947 714 -191 C
ATOM 954 N ALA A 139 11.496 12.597 27.878 1.00 51.22 N
ANISOU 954 N ALA A 139 7421 6788 5253 837 1071 -229 N
ATOM 955 CA ALA A 139 12.475 11.619 28.334 1.00 49.07 C
ANISOU 955 CA ALA A 139 7136 6568 4942 827 1104 -239 C
ATOM 956 C ALA A 139 11.955 10.829 29.528 1.00 44.99 C
ANISOU 956 C ALA A 139 6487 6089 4517 786 1087 -205 C
ATOM 957 O ALA A 139 12.257 9.638 29.660 1.00 45.69 O
ANISOU 957 O ALA A 139 6571 6182 4608 785 1046 -198 O
ATOM 958 CB ALA A 139 13.788 12.317 28.678 1.00 58.01 C
ANISOU 958 CB ALA A 139 8251 7767 6024 792 1215 -268 C
ATOM 959 N GLY A 140 11.156 11.460 30.390 1.00 37.69 N
ANISOU 959 N GLY A 140 5457 5191 3673 751 1117 -182 N
ATOM 960 CA GLY A 140 10.578 10.731 31.506 1.00 52.36 C
ANISOU 960 CA GLY A 140 7189 7084 5620 713 1099 -145 C
ATOM 961 C GLY A 140 9.597 9.667 31.054 1.00 49.94 C
ANISOU 961 C GLY A 140 6887 6698 5389 724 954 -116 C
ATOM 962 O GLY A 140 9.586 8.551 31.578 1.00 34.42 O
ANISOU 962 O GLY A 140 4869 4746 3463 709 921 -92 O
ATOM 963 N ILE A 141 8.757 9.999 30.072 1.00 41.30 N
ANISOU 963 N ILE A 141 5854 5518 4318 753 864 -118 N
ATOM 964 CA ILE A 141 7.827 9.014 29.529 1.00 41.55 C
ANISOU 964 CA ILE A 141 5898 5468 4421 768 719 -99 C
ATOM 965 C ILE A 141 8.590 7.888 28.844 1.00 40.84 C
ANISOU 965 C ILE A 141 5893 5352 4271 798 667 -116 C
ATOM 966 O ILE A 141 8.204 6.716 28.928 1.00 37.87 O
ANISOU 966 O ILE A 141 5487 4945 3956 794 582 -96 O
ATOM 967 CB ILE A 141 6.828 9.700 28.577 1.00 37.16 C
ANISOU 967 CB ILE A 141 5396 4830 3892 797 637 -103 C
ATOM 968 CG1 ILE A 141 5.810 10.510 29.374 1.00 27.79 C
ANISOU 968 CG1 ILE A 141 4100 3658 2799 763 661 -79 C
ATOM 969 CG2 ILE A 141 6.108 8.694 27.713 1.00 39.00 C
ANISOU 969 CG2 ILE A 141 5675 4973 4171 827 484 -99 C
ATOM 970 CD1 ILE A 141 4.912 11.346 28.514 1.00 28.23 C
ANISOU 970 CD1 ILE A 141 4205 3642 2878 790 597 -85 C
ATOM 971 N TRP A 142 9.701 8.218 28.179 1.00 46.14 N
ANISOU 971 N TRP A 142 6669 6037 4826 827 720 -154 N
ATOM 972 CA TRP A 142 10.489 7.191 27.502 1.00 45.60 C
ANISOU 972 CA TRP A 142 6684 5947 4695 856 675 -176 C
ATOM 973 C TRP A 142 11.128 6.233 28.498 1.00 44.58 C
ANISOU 973 C TRP A 142 6480 5879 4579 826 718 -162 C
ATOM 974 O TRP A 142 11.073 5.011 28.320 1.00 46.43 O
ANISOU 974 O TRP A 142 6719 6079 4844 834 635 -155 O
ATOM 975 CB TRP A 142 11.555 7.837 26.620 1.00 38.34 C
ANISOU 975 CB TRP A 142 5887 5034 3646 892 734 -219 C
ATOM 976 CG TRP A 142 11.044 8.206 25.273 1.00 45.58 C
ANISOU 976 CG TRP A 142 6913 5869 4536 939 648 -235 C
ATOM 977 CD1 TRP A 142 10.985 9.456 24.732 1.00 42.66 C
ANISOU 977 CD1 TRP A 142 6601 5488 4121 957 687 -246 C
ATOM 978 CD2 TRP A 142 10.498 7.315 24.290 1.00 37.21 C
ANISOU 978 CD2 TRP A 142 5917 4728 3494 976 505 -241 C
ATOM 979 NE1 TRP A 142 10.442 9.399 23.470 1.00 48.65 N
ANISOU 979 NE1 TRP A 142 7457 6165 4863 1005 577 -256 N
ATOM 980 CE2 TRP A 142 10.136 8.096 23.176 1.00 28.83 C
ANISOU 980 CE2 TRP A 142 4953 3613 2390 1018 463 -256 C
ATOM 981 CE3 TRP A 142 10.284 5.934 24.245 1.00 29.04 C
ANISOU 981 CE3 TRP A 142 4866 3660 2509 980 407 -237 C
ATOM 982 CZ2 TRP A 142 9.574 7.543 22.030 1.00 29.49 C
ANISOU 982 CZ2 TRP A 142 5117 3615 2475 1063 327 -269 C
ATOM 983 CZ3 TRP A 142 9.723 5.387 23.108 1.00 29.32 C
ANISOU 983 CZ3 TRP A 142 4979 3611 2551 1023 273 -252 C
ATOM 984 CH2 TRP A 142 9.377 6.189 22.015 1.00 37.47 C
ANISOU 984 CH2 TRP A 142 6106 4596 3535 1065 233 -269 C
ATOM 985 N VAL A 143 11.747 6.768 29.553 1.00 48.54 N
ANISOU 985 N VAL A 143 6911 6473 5060 792 845 -158 N
ATOM 986 CA VAL A 143 12.339 5.906 30.571 1.00 37.42 C
ANISOU 986 CA VAL A 143 5426 5130 3664 764 889 -141 C
ATOM 987 C VAL A 143 11.258 5.087 31.263 1.00 46.82 C
ANISOU 987 C VAL A 143 6510 6301 4978 736 815 -90 C
ATOM 988 O VAL A 143 11.440 3.893 31.529 1.00 37.63 O
ANISOU 988 O VAL A 143 5321 5134 3842 731 774 -72 O
ATOM 989 CB VAL A 143 13.149 6.741 31.579 1.00 35.27 C
ANISOU 989 CB VAL A 143 5093 4962 3344 735 1040 -151 C
ATOM 990 CG1 VAL A 143 13.689 5.850 32.683 1.00 51.39 C
ANISOU 990 CG1 VAL A 143 7050 7075 5402 707 1082 -129 C
ATOM 991 CG2 VAL A 143 14.288 7.462 30.879 1.00 44.42 C
ANISOU 991 CG2 VAL A 143 6357 6136 4384 762 1115 -202 C
ATOM 992 N LEU A 144 10.112 5.712 31.550 1.00 57.98 N
ANISOU 992 N LEU A 144 7860 7698 6471 717 796 -66 N
ATOM 993 CA LEU A 144 9.002 4.990 32.167 1.00 38.43 C
ANISOU 993 CA LEU A 144 5283 5199 4120 691 725 -17 C
ATOM 994 C LEU A 144 8.492 3.877 31.259 1.00 56.10 C
ANISOU 994 C LEU A 144 7574 7338 6402 718 580 -14 C
ATOM 995 O LEU A 144 8.100 2.807 31.739 1.00 49.30 O
ANISOU 995 O LEU A 144 6647 6464 5622 701 527 22 O
ATOM 996 CB LEU A 144 7.878 5.967 32.510 1.00 50.41 C
ANISOU 996 CB LEU A 144 6733 6712 5709 670 730 0 C
ATOM 997 CG LEU A 144 6.567 5.458 33.118 1.00 78.21 C
ANISOU 997 CG LEU A 144 10144 10205 9366 641 660 50 C
ATOM 998 CD1 LEU A 144 6.083 6.436 34.178 1.00 95.00 C
ANISOU 998 CD1 LEU A 144 12163 12399 11535 602 747 68 C
ATOM 999 CD2 LEU A 144 5.487 5.270 32.052 1.00 35.75 C
ANISOU 999 CD2 LEU A 144 4819 4715 4050 669 521 46 C
ATOM 1000 N SER A 145 8.496 4.106 29.943 1.00 59.96 N
ANISOU 1000 N SER A 145 8183 7758 6840 763 516 -52 N
ATOM 1001 CA SER A 145 7.993 3.094 29.017 1.00 53.16 C
ANISOU 1001 CA SER A 145 7376 6803 6020 794 374 -57 C
ATOM 1002 C SER A 145 8.930 1.897 28.940 1.00 46.66 C
ANISOU 1002 C SER A 145 6584 5986 5161 804 361 -67 C
ATOM 1003 O SER A 145 8.477 0.746 28.970 1.00 55.35 O
ANISOU 1003 O SER A 145 7650 7040 6340 801 272 -46 O
ATOM 1004 CB SER A 145 7.790 3.700 27.630 1.00 37.62 C
ANISOU 1004 CB SER A 145 5530 4767 3997 842 312 -97 C
ATOM 1005 OG SER A 145 6.792 4.703 27.646 1.00 49.13 O
ANISOU 1005 OG SER A 145 6957 6207 5504 835 305 -85 O
ATOM 1006 N PHE A 146 10.237 2.149 28.839 1.00 57.67 N
ANISOU 1006 N PHE A 146 8039 7434 6439 816 450 -99 N
ATOM 1007 CA PHE A 146 11.196 1.061 28.677 1.00 51.92 C
ANISOU 1007 CA PHE A 146 7349 6711 5668 830 439 -115 C
ATOM 1008 C PHE A 146 11.115 0.074 29.832 1.00 46.12 C
ANISOU 1008 C PHE A 146 6499 6009 5015 792 445 -67 C
ATOM 1009 O PHE A 146 11.111 -1.143 29.621 1.00 57.84 O
ANISOU 1009 O PHE A 146 7987 7449 6541 802 365 -62 O
ATOM 1010 CB PHE A 146 12.613 1.619 28.553 1.00 55.06 C
ANISOU 1010 CB PHE A 146 7815 7173 5933 843 551 -155 C
ATOM 1011 CG PHE A 146 13.006 1.973 27.146 1.00 63.20 C
ANISOU 1011 CG PHE A 146 8988 8155 6870 893 518 -207 C
ATOM 1012 CD1 PHE A 146 13.374 0.986 26.248 1.00 64.29 C
ANISOU 1012 CD1 PHE A 146 9208 8241 6979 930 434 -236 C
ATOM 1013 CD2 PHE A 146 13.023 3.293 26.726 1.00 68.34 C
ANISOU 1013 CD2 PHE A 146 9690 8814 7461 905 573 -226 C
ATOM 1014 CE1 PHE A 146 13.741 1.309 24.953 1.00 58.57 C
ANISOU 1014 CE1 PHE A 146 8615 7478 6163 978 405 -283 C
ATOM 1015 CE2 PHE A 146 13.389 3.620 25.434 1.00 55.06 C
ANISOU 1015 CE2 PHE A 146 8140 7091 5689 953 545 -268 C
ATOM 1016 CZ PHE A 146 13.747 2.627 24.547 1.00 50.38 C
ANISOU 1016 CZ PHE A 146 7629 6450 5064 990 462 -297 C
ATOM 1017 N LEU A 147 11.048 0.576 31.065 1.00 48.80 N
ANISOU 1017 N LEU A 147 6733 6426 5381 750 541 -33 N
ATOM 1018 CA LEU A 147 11.037 -0.324 32.210 1.00 45.56 C
ANISOU 1018 CA LEU A 147 6214 6057 5039 714 557 17 C
ATOM 1019 C LEU A 147 9.662 -0.921 32.492 1.00 55.28 C
ANISOU 1019 C LEU A 147 7362 7231 6412 694 462 66 C
ATOM 1020 O LEU A 147 9.556 -1.794 33.360 1.00 71.69 O
ANISOU 1020 O LEU A 147 9352 9330 8558 667 461 113 O
ATOM 1021 CB LEU A 147 11.570 0.397 33.455 1.00 46.55 C
ANISOU 1021 CB LEU A 147 6258 6299 5131 679 699 33 C
ATOM 1022 CG LEU A 147 10.904 1.694 33.915 1.00 64.98 C
ANISOU 1022 CG LEU A 147 8538 8667 7484 656 758 40 C
ATOM 1023 CD1 LEU A 147 9.795 1.429 34.933 1.00 66.15 C
ANISOU 1023 CD1 LEU A 147 8553 8827 7754 616 740 102 C
ATOM 1024 CD2 LEU A 147 11.943 2.647 34.481 1.00 63.07 C
ANISOU 1024 CD2 LEU A 147 8290 8526 7146 647 901 14 C
ATOM 1025 N LEU A 148 8.614 -0.488 31.786 1.00 51.73 N
ANISOU 1025 N LEU A 148 6937 6709 6009 707 382 58 N
ATOM 1026 CA LEU A 148 7.307 -1.124 31.917 1.00 56.49 C
ANISOU 1026 CA LEU A 148 7469 7245 6750 692 281 98 C
ATOM 1027 C LEU A 148 7.105 -2.259 30.921 1.00 49.77 C
ANISOU 1027 C LEU A 148 6681 6295 5935 725 146 81 C
ATOM 1028 O LEU A 148 6.195 -3.076 31.111 1.00 58.81 O
ANISOU 1028 O LEU A 148 7760 7385 7200 711 62 116 O
ATOM 1029 CB LEU A 148 6.176 -0.100 31.745 1.00 51.24 C
ANISOU 1029 CB LEU A 148 6784 6552 6132 687 259 100 C
ATOM 1030 CG LEU A 148 5.846 0.793 32.946 1.00 51.23 C
ANISOU 1030 CG LEU A 148 6675 6632 6158 644 362 134 C
ATOM 1031 CD1 LEU A 148 4.499 1.474 32.770 1.00 44.30 C
ANISOU 1031 CD1 LEU A 148 5763 5705 5363 638 309 142 C
ATOM 1032 CD2 LEU A 148 5.875 0.002 34.240 1.00 66.33 C
ANISOU 1032 CD2 LEU A 148 8468 8602 8134 602 404 190 C
ATOM 1033 N ALA A 149 7.932 -2.334 29.877 1.00 48.38 N
ANISOU 1033 N ALA A 149 6627 6095 5661 769 125 26 N
ATOM 1034 CA ALA A 149 7.836 -3.397 28.887 1.00 55.24 C
ANISOU 1034 CA ALA A 149 7561 6874 6553 804 0 0 C
ATOM 1035 C ALA A 149 8.902 -4.473 29.049 1.00 48.99 C
ANISOU 1035 C ALA A 149 6782 6102 5730 809 14 -4 C
ATOM 1036 O ALA A 149 8.905 -5.444 28.283 1.00 56.97 O
ANISOU 1036 O ALA A 149 7841 7041 6763 837 -88 -28 O
ATOM 1037 CB ALA A 149 7.916 -2.818 27.471 1.00 37.65 C
ANISOU 1037 CB ALA A 149 5467 4597 4243 856 -52 -61 C
ATOM 1038 N THR A 150 9.810 -4.322 30.014 1.00 47.68 N
ANISOU 1038 N THR A 150 6574 6031 5513 783 135 15 N
ATOM 1039 CA THR A 150 10.811 -5.356 30.249 1.00 43.56 C
ANISOU 1039 CA THR A 150 6055 5529 4965 786 149 14 C
ATOM 1040 C THR A 150 10.229 -6.749 30.491 1.00 43.51 C
ANISOU 1040 C THR A 150 5982 5462 5085 775 54 53 C
ATOM 1041 O THR A 150 10.894 -7.720 30.089 1.00 60.22 O
ANISOU 1041 O THR A 150 8143 7552 7187 796 13 32 O
ATOM 1042 CB THR A 150 11.732 -4.927 31.398 1.00 54.64 C
ANISOU 1042 CB THR A 150 7403 7049 6307 756 295 35 C
ATOM 1043 OG1 THR A 150 10.934 -4.279 32.411 1.00 75.76 O
ANISOU 1043 OG1 THR A 150 9972 9770 9045 715 346 85 O
ATOM 1044 CG2 THR A 150 12.778 -3.945 30.897 1.00 29.37 C
ANISOU 1044 CG2 THR A 150 4298 3897 2963 780 380 -22 C
ATOM 1045 N PRO A 151 9.023 -6.936 31.104 1.00 46.28 N
ANISOU 1045 N PRO A 151 6231 5787 5566 743 14 109 N
ATOM 1046 CA PRO A 151 8.519 -8.306 31.266 1.00 48.42 C
ANISOU 1046 CA PRO A 151 6444 5992 5960 734 -78 145 C
ATOM 1047 C PRO A 151 8.426 -9.101 29.975 1.00 48.31 C
ANISOU 1047 C PRO A 151 6518 5876 5963 778 -209 93 C
ATOM 1048 O PRO A 151 8.410 -10.332 30.020 1.00 57.02 O
ANISOU 1048 O PRO A 151 7592 6930 7142 778 -274 109 O
ATOM 1049 CB PRO A 151 7.130 -8.103 31.886 1.00 47.02 C
ANISOU 1049 CB PRO A 151 6160 5795 5908 698 -104 199 C
ATOM 1050 CG PRO A 151 7.253 -6.893 32.699 1.00 57.70 C
ANISOU 1050 CG PRO A 151 7472 7246 7205 671 20 217 C
ATOM 1051 CD PRO A 151 8.294 -6.010 31.998 1.00 56.48 C
ANISOU 1051 CD PRO A 151 7433 7130 6896 704 80 151 C
ATOM 1052 N VAL A 152 8.373 -8.432 28.824 1.00 50.31 N
ANISOU 1052 N VAL A 152 6876 6094 6146 817 -250 32 N
ATOM 1053 CA VAL A 152 8.275 -9.183 27.579 1.00 49.60 C
ANISOU 1053 CA VAL A 152 6870 5910 6067 862 -377 -21 C
ATOM 1054 C VAL A 152 9.617 -9.804 27.205 1.00 48.58 C
ANISOU 1054 C VAL A 152 6815 5798 5846 889 -357 -61 C
ATOM 1055 O VAL A 152 9.654 -10.865 26.573 1.00 55.96 O
ANISOU 1055 O VAL A 152 7779 6662 6820 914 -455 -88 O
ATOM 1056 CB VAL A 152 7.728 -8.297 26.448 1.00 40.45 C
ANISOU 1056 CB VAL A 152 5799 4707 4862 898 -433 -71 C
ATOM 1057 CG1 VAL A 152 8.807 -7.379 25.907 1.00 43.52 C
ANISOU 1057 CG1 VAL A 152 6297 5153 5086 927 -351 -120 C
ATOM 1058 CG2 VAL A 152 7.175 -9.162 25.341 1.00 65.45 C
ANISOU 1058 CG2 VAL A 152 9014 7765 8087 937 -587 -112 C
ATOM 1059 N LEU A 153 10.733 -9.174 27.587 1.00 60.30 N
ANISOU 1059 N LEU A 153 8326 7375 7212 884 -233 -69 N
ATOM 1060 CA LEU A 153 12.053 -9.701 27.251 1.00 53.11 C
ANISOU 1060 CA LEU A 153 7485 6486 6210 909 -206 -110 C
ATOM 1061 C LEU A 153 12.334 -11.044 27.905 1.00 54.79 C
ANISOU 1061 C LEU A 153 7627 6688 6501 892 -227 -75 C
ATOM 1062 O LEU A 153 13.294 -11.716 27.514 1.00 66.25 O
ANISOU 1062 O LEU A 153 9134 8135 7901 916 -234 -112 O
ATOM 1063 CB LEU A 153 13.142 -8.709 27.655 1.00 36.28 C
ANISOU 1063 CB LEU A 153 5382 4458 3946 903 -61 -122 C
ATOM 1064 CG LEU A 153 13.463 -7.587 26.675 1.00 34.90 C
ANISOU 1064 CG LEU A 153 5321 4290 3648 937 -36 -181 C
ATOM 1065 CD1 LEU A 153 14.517 -6.663 27.263 1.00 29.05 C
ANISOU 1065 CD1 LEU A 153 4586 3654 2796 923 115 -185 C
ATOM 1066 CD2 LEU A 153 13.935 -8.171 25.352 1.00 43.84 C
ANISOU 1066 CD2 LEU A 153 6570 5362 4725 989 -119 -248 C
ATOM 1067 N ALA A 154 11.532 -11.446 28.891 1.00 59.03 N
ANISOU 1067 N ALA A 154 8044 7221 7162 851 -234 -3 N
ATOM 1068 CA ALA A 154 11.707 -12.725 29.558 1.00 54.49 C
ANISOU 1068 CA ALA A 154 7396 6634 6675 833 -254 40 C
ATOM 1069 C ALA A 154 10.595 -13.722 29.268 1.00 59.52 C
ANISOU 1069 C ALA A 154 7988 7161 7464 832 -389 59 C
ATOM 1070 O ALA A 154 10.834 -14.930 29.363 1.00 69.06 O
ANISOU 1070 O ALA A 154 9171 8330 8737 834 -437 71 O
ATOM 1071 CB ALA A 154 11.812 -12.518 31.077 1.00 41.25 C
ANISOU 1071 CB ALA A 154 5606 5048 5019 783 -142 117 C
ATOM 1072 N TYR A 155 9.402 -13.253 28.903 1.00 56.72 N
ANISOU 1072 N TYR A 155 7624 6757 7172 831 -452 59 N
ATOM 1073 CA TYR A 155 8.269 -14.123 28.620 1.00 45.09 C
ANISOU 1073 CA TYR A 155 6104 5179 5850 830 -582 72 C
ATOM 1074 C TYR A 155 8.194 -14.561 27.165 1.00 51.58 C
ANISOU 1074 C TYR A 155 7027 5909 6663 882 -707 -8 C
ATOM 1075 O TYR A 155 7.360 -15.409 26.834 1.00 75.19 O
ANISOU 1075 O TYR A 155 9984 8806 9778 887 -823 -8 O
ATOM 1076 CB TYR A 155 6.958 -13.429 29.006 1.00 45.77 C
ANISOU 1076 CB TYR A 155 6118 5255 6018 801 -590 113 C
ATOM 1077 CG TYR A 155 6.763 -13.258 30.496 1.00 46.96 C
ANISOU 1077 CG TYR A 155 6145 5479 6219 746 -491 200 C
ATOM 1078 CD1 TYR A 155 7.364 -14.125 31.400 1.00 52.49 C
ANISOU 1078 CD1 TYR A 155 6781 6214 6948 723 -444 251 C
ATOM 1079 CD2 TYR A 155 5.977 -12.229 31.000 1.00 64.70 C
ANISOU 1079 CD2 TYR A 155 8340 7763 8482 719 -444 230 C
ATOM 1080 CE1 TYR A 155 7.187 -13.972 32.765 1.00 74.95 C
ANISOU 1080 CE1 TYR A 155 9513 9131 9833 675 -353 332 C
ATOM 1081 CE2 TYR A 155 5.793 -12.068 32.364 1.00 75.80 C
ANISOU 1081 CE2 TYR A 155 9631 9240 9929 670 -353 307 C
ATOM 1082 CZ TYR A 155 6.400 -12.942 33.242 1.00 74.11 C
ANISOU 1082 CZ TYR A 155 9356 9063 9739 649 -307 358 C
ATOM 1083 OH TYR A 155 6.219 -12.783 34.598 1.00 56.83 O
ANISOU 1083 OH TYR A 155 7055 6951 7586 603 -216 436 O
ATOM 1084 N ARG A 156 9.025 -14.006 26.291 1.00 53.17 N
ANISOU 1084 N ARG A 156 7348 6134 6721 923 -687 -77 N
ATOM 1085 CA ARG A 156 9.064 -14.413 24.896 1.00 71.64 C
ANISOU 1085 CA ARG A 156 9789 8397 9034 977 -800 -157 C
ATOM 1086 C ARG A 156 10.203 -15.395 24.669 1.00 75.78 C
ANISOU 1086 C ARG A 156 10354 8920 9520 998 -804 -189 C
ATOM 1087 O ARG A 156 11.258 -15.309 25.303 1.00 67.78 O
ANISOU 1087 O ARG A 156 9338 7985 8432 984 -697 -173 O
ATOM 1088 CB ARG A 156 9.227 -13.203 23.974 1.00 59.09 C
ANISOU 1088 CB ARG A 156 8311 6830 7309 1012 -781 -214 C
ATOM 1089 CG ARG A 156 7.985 -12.335 23.869 1.00 64.35 C
ANISOU 1089 CG ARG A 156 8954 7472 8022 1005 -814 -198 C
ATOM 1090 CD ARG A 156 6.900 -13.013 23.047 1.00 72.79 C
ANISOU 1090 CD ARG A 156 10025 8430 9202 1030 -973 -227 C
ATOM 1091 NE ARG A 156 5.612 -12.334 23.157 1.00 62.38 N
ANISOU 1091 NE ARG A 156 8658 7087 7958 1014 -1006 -200 N
ATOM 1092 CZ ARG A 156 4.593 -12.536 22.328 1.00 61.23 C
ANISOU 1092 CZ ARG A 156 8527 6853 7886 1041 -1137 -233 C
ATOM 1093 NH1 ARG A 156 3.452 -11.881 22.499 1.00 76.31 N
ANISOU 1093 NH1 ARG A 156 10387 8743 9862 1025 -1159 -207 N
ATOM 1094 NH2 ARG A 156 4.719 -13.386 21.320 1.00 73.04 N
ANISOU 1094 NH2 ARG A 156 10086 8280 9386 1086 -1247 -295 N
ATOM 1095 N THR A 157 9.978 -16.334 23.756 1.00 77.44 N
ANISOU 1095 N THR A 157 10600 9038 9783 1032 -931 -239 N
ATOM 1096 CA THR A 157 10.967 -17.359 23.460 1.00 93.03 C
ANISOU 1096 CA THR A 157 12611 10999 11737 1055 -952 -276 C
ATOM 1097 C THR A 157 10.599 -18.024 22.146 1.00 83.10 C
ANISOU 1097 C THR A 157 11420 9643 10510 1105 -1099 -353 C
ATOM 1098 O THR A 157 9.424 -18.075 21.769 1.00 98.11 O
ANISOU 1098 O THR A 157 13299 11474 12505 1109 -1197 -356 O
ATOM 1099 CB THR A 157 11.048 -18.407 24.579 1.00102.15 C
ANISOU 1099 CB THR A 157 13653 12151 13008 1015 -934 -207 C
ATOM 1100 OG1 THR A 157 12.093 -19.345 24.292 1.00 97.80 O
ANISOU 1100 OG1 THR A 157 13141 11590 12429 1038 -948 -245 O
ATOM 1101 CG2 THR A 157 9.732 -19.149 24.717 1.00 90.97 C
ANISOU 1101 CG2 THR A 157 12148 10642 11776 997 -1043 -171 C
ATOM 1102 N VAL A 158 11.616 -18.527 21.453 1.00 64.70 N
ANISOU 1102 N VAL A 158 9172 7311 8100 1143 -1113 -418 N
ATOM 1103 CA VAL A 158 11.420 -19.284 20.223 1.00 71.84 C
ANISOU 1103 CA VAL A 158 10140 8128 9030 1193 -1251 -498 C
ATOM 1104 C VAL A 158 11.433 -20.762 20.592 1.00 60.09 C
ANISOU 1104 C VAL A 158 8575 6577 7678 1180 -1313 -482 C
ATOM 1105 O VAL A 158 12.454 -21.289 21.039 1.00 60.44 O
ANISOU 1105 O VAL A 158 8612 6657 7696 1173 -1254 -473 O
ATOM 1106 CB VAL A 158 12.497 -18.957 19.184 1.00 59.10 C
ANISOU 1106 CB VAL A 158 8662 6546 7247 1244 -1233 -583 C
ATOM 1107 CG1 VAL A 158 12.162 -19.603 17.850 1.00 72.20 C
ANISOU 1107 CG1 VAL A 158 10390 8119 8925 1300 -1379 -669 C
ATOM 1108 CG2 VAL A 158 12.649 -17.453 19.031 1.00 73.96 C
ANISOU 1108 CG2 VAL A 158 10609 8501 8989 1249 -1142 -583 C
ATOM 1109 N VAL A 159 10.299 -21.431 20.418 1.00 66.39 N
ANISOU 1109 N VAL A 159 9314 7281 8629 1178 -1433 -477 N
ATOM 1110 CA VAL A 159 10.161 -22.847 20.730 1.00 68.83 C
ANISOU 1110 CA VAL A 159 9545 7518 9089 1166 -1503 -460 C
ATOM 1111 C VAL A 159 9.797 -23.585 19.445 1.00 77.26 C
ANISOU 1111 C VAL A 159 10667 8488 10201 1218 -1657 -552 C
ATOM 1112 O VAL A 159 8.810 -23.238 18.789 1.00 79.45 O
ANISOU 1112 O VAL A 159 10961 8717 10510 1237 -1741 -582 O
ATOM 1113 CB VAL A 159 9.118 -23.110 21.831 1.00 66.62 C
ANISOU 1113 CB VAL A 159 9127 7211 8976 1111 -1503 -363 C
ATOM 1114 CG1 VAL A 159 9.651 -22.641 23.178 1.00 83.61 C
ANISOU 1114 CG1 VAL A 159 11217 9461 11089 1061 -1352 -274 C
ATOM 1115 CG2 VAL A 159 7.797 -22.416 21.524 1.00 85.59 C
ANISOU 1115 CG2 VAL A 159 11515 9576 11427 1109 -1561 -362 C
ATOM 1116 N PRO A 160 10.577 -24.579 19.023 1.00 75.25 N
ANISOU 1116 N PRO A 160 10442 8202 9947 1245 -1698 -604 N
ATOM 1117 CA PRO A 160 10.194 -25.362 17.840 1.00 78.16 C
ANISOU 1117 CA PRO A 160 10851 8474 10370 1294 -1850 -694 C
ATOM 1118 C PRO A 160 8.947 -26.191 18.116 1.00 76.51 C
ANISOU 1118 C PRO A 160 10533 8165 10374 1271 -1955 -662 C
ATOM 1119 O PRO A 160 8.848 -26.878 19.136 1.00 82.85 O
ANISOU 1119 O PRO A 160 11228 8950 11299 1226 -1929 -586 O
ATOM 1120 CB PRO A 160 11.418 -26.249 17.584 1.00 67.58 C
ANISOU 1120 CB PRO A 160 9550 7136 8990 1318 -1847 -744 C
ATOM 1121 CG PRO A 160 12.540 -25.574 18.292 1.00 59.46 C
ANISOU 1121 CG PRO A 160 8546 6219 7827 1297 -1691 -702 C
ATOM 1122 CD PRO A 160 11.931 -24.916 19.492 1.00 63.98 C
ANISOU 1122 CD PRO A 160 9028 6835 8447 1239 -1606 -595 C
ATOM 1123 N TRP A 161 7.993 -26.114 17.192 1.00 76.28 N
ANISOU 1123 N TRP A 161 10530 8069 10385 1303 -2074 -720 N
ATOM 1124 CA TRP A 161 6.748 -26.870 17.266 1.00 90.04 C
ANISOU 1124 CA TRP A 161 12176 9706 12327 1289 -2189 -705 C
ATOM 1125 C TRP A 161 6.346 -27.249 15.848 1.00109.54 C
ANISOU 1125 C TRP A 161 14715 12100 14806 1351 -2340 -820 C
ATOM 1126 O TRP A 161 6.225 -26.371 14.988 1.00124.63 O
ANISOU 1126 O TRP A 161 16719 14037 16596 1391 -2359 -875 O
ATOM 1127 CB TRP A 161 5.652 -26.054 17.960 1.00 90.14 C
ANISOU 1127 CB TRP A 161 12117 9731 12399 1246 -2156 -627 C
ATOM 1128 CG TRP A 161 4.268 -26.582 17.749 1.00110.44 C
ANISOU 1128 CG TRP A 161 14614 12196 15152 1243 -2286 -634 C
ATOM 1129 CD1 TRP A 161 3.658 -27.591 18.439 1.00125.77 C
ANISOU 1129 CD1 TRP A 161 16432 14064 17291 1205 -2327 -580 C
ATOM 1130 CD2 TRP A 161 3.312 -26.120 16.785 1.00123.69 C
ANISOU 1130 CD2 TRP A 161 16333 13829 16833 1280 -2390 -696 C
ATOM 1131 NE1 TRP A 161 2.385 -27.789 17.959 1.00150.12 N
ANISOU 1131 NE1 TRP A 161 19477 17057 20504 1215 -2451 -609 N
ATOM 1132 CE2 TRP A 161 2.148 -26.898 16.944 1.00135.44 C
ANISOU 1132 CE2 TRP A 161 17717 15215 18529 1261 -2494 -682 C
ATOM 1133 CE3 TRP A 161 3.330 -25.127 15.800 1.00102.55 C
ANISOU 1133 CE3 TRP A 161 13772 11188 14006 1328 -2407 -762 C
ATOM 1134 CZ2 TRP A 161 1.013 -26.714 16.156 1.00107.41 C
ANISOU 1134 CZ2 TRP A 161 14173 11599 15038 1289 -2614 -735 C
ATOM 1135 CZ3 TRP A 161 2.201 -24.945 15.019 1.00 97.74 C
ANISOU 1135 CZ3 TRP A 161 13170 10514 13452 1357 -2527 -812 C
ATOM 1136 CH2 TRP A 161 1.060 -25.735 15.202 1.00 94.80 C
ANISOU 1136 CH2 TRP A 161 12690 10041 13287 1338 -2630 -800 C
ATOM 1137 N LYS A 162 6.152 -28.553 15.615 1.00 88.98 N
ANISOU 1137 N LYS A 162 12062 9401 12346 1361 -2447 -855 N
ATOM 1138 CA LYS A 162 5.952 -29.156 14.295 1.00 92.11 C
ANISOU 1138 CA LYS A 162 12517 9722 12758 1423 -2594 -973 C
ATOM 1139 C LYS A 162 7.231 -29.102 13.464 1.00101.53 C
ANISOU 1139 C LYS A 162 13835 10966 13773 1475 -2572 -1056 C
ATOM 1140 O LYS A 162 8.209 -28.459 13.860 1.00116.83 O
ANISOU 1140 O LYS A 162 15820 13000 15568 1463 -2443 -1024 O
ATOM 1141 CB LYS A 162 4.794 -28.493 13.542 1.00 87.67 C
ANISOU 1141 CB LYS A 162 11981 9127 12201 1450 -2684 -1013 C
ATOM 1142 N THR A 163 7.236 -29.772 12.313 1.00109.31 N
ANISOU 1142 N THR A 163 14874 11891 14767 1532 -2698 -1167 N
ATOM 1143 CA THR A 163 8.471 -29.942 11.556 1.00125.21 C
ANISOU 1143 CA THR A 163 16995 13945 16636 1579 -2685 -1249 C
ATOM 1144 C THR A 163 8.902 -28.620 10.925 1.00124.65 C
ANISOU 1144 C THR A 163 17050 13966 16344 1613 -2621 -1278 C
ATOM 1145 O THR A 163 8.092 -27.915 10.312 1.00130.51 O
ANISOU 1145 O THR A 163 17830 14701 17055 1638 -2675 -1303 O
ATOM 1146 CB THR A 163 8.301 -31.038 10.494 1.00131.83 C
ANISOU 1146 CB THR A 163 17849 14691 17549 1633 -2842 -1362 C
ATOM 1147 OG1 THR A 163 9.533 -31.234 9.787 1.00121.49 O
ANISOU 1147 OG1 THR A 163 16639 13422 16098 1678 -2825 -1443 O
ATOM 1148 CG2 THR A 163 7.180 -30.705 9.505 1.00135.93 C
ANISOU 1148 CG2 THR A 163 18400 15162 18084 1675 -2968 -1428 C
ATOM 1149 N ASN A 164 10.181 -28.273 11.112 1.00106.97 N
ANISOU 1149 N ASN A 164 14873 11814 13958 1612 -2502 -1272 N
ATOM 1150 CA ASN A 164 10.788 -27.050 10.590 1.00109.30 C
ANISOU 1150 CA ASN A 164 15288 12201 14038 1641 -2421 -1295 C
ATOM 1151 C ASN A 164 9.898 -25.829 10.795 1.00110.10 C
ANISOU 1151 C ASN A 164 15387 12332 14114 1623 -2389 -1240 C
ATOM 1152 O ASN A 164 9.775 -24.981 9.905 1.00 84.94 O
ANISOU 1152 O ASN A 164 12298 9173 10802 1666 -2406 -1287 O
ATOM 1153 CB ASN A 164 11.126 -27.216 9.107 1.00107.29 C
ANISOU 1153 CB ASN A 164 15151 11935 13679 1717 -2512 -1421 C
ATOM 1154 CG ASN A 164 12.364 -28.063 8.886 1.00112.33 C
ANISOU 1154 CG ASN A 164 15823 12582 14275 1738 -2498 -1477 C
ATOM 1155 OD1 ASN A 164 12.327 -29.285 9.033 1.00128.50 O
ANISOU 1155 OD1 ASN A 164 17803 14559 16463 1733 -2569 -1495 O
ATOM 1156 ND2 ASN A 164 13.469 -27.418 8.531 1.00101.99 N
ANISOU 1156 ND2 ASN A 164 14617 11358 12775 1761 -2405 -1504 N
ATOM 1157 N MET A 165 9.275 -25.739 11.965 1.00121.69 N
ANISOU 1157 N MET A 165 16743 13793 15700 1560 -2343 -1139 N
ATOM 1158 CA MET A 165 8.356 -24.655 12.283 1.00101.77 C
ANISOU 1158 CA MET A 165 14200 11292 13177 1537 -2314 -1081 C
ATOM 1159 C MET A 165 8.673 -24.175 13.689 1.00101.45 C
ANISOU 1159 C MET A 165 14088 11319 13139 1471 -2164 -970 C
ATOM 1160 O MET A 165 8.541 -24.936 14.652 1.00 88.78 O
ANISOU 1160 O MET A 165 12374 9686 11671 1424 -2151 -908 O
ATOM 1161 CB MET A 165 6.899 -25.120 12.168 1.00100.83 C
ANISOU 1161 CB MET A 165 14001 11074 13238 1534 -2447 -1082 C
ATOM 1162 CG MET A 165 5.854 -24.070 12.524 1.00107.94 C
ANISOU 1162 CG MET A 165 14869 11988 14158 1508 -2426 -1024 C
ATOM 1163 SD MET A 165 4.170 -24.562 12.071 1.00108.31 S
ANISOU 1163 SD MET A 165 14845 11915 14392 1520 -2601 -1052 S
ATOM 1164 CE MET A 165 4.288 -24.589 10.283 1.00 64.41 C
ANISOU 1164 CE MET A 165 9424 6331 8717 1614 -2728 -1193 C
ATOM 1165 N SER A 166 9.121 -22.930 13.801 1.00 95.58 N
ANISOU 1165 N SER A 166 13406 10667 12243 1467 -2051 -947 N
ATOM 1166 CA SER A 166 9.457 -22.331 15.083 1.00 80.29 C
ANISOU 1166 CA SER A 166 11411 8806 10289 1408 -1904 -849 C
ATOM 1167 C SER A 166 8.556 -21.132 15.324 1.00 78.30 C
ANISOU 1167 C SER A 166 11144 8579 10026 1389 -1872 -802 C
ATOM 1168 O SER A 166 8.249 -20.377 14.396 1.00 79.07 O
ANISOU 1168 O SER A 166 11327 8679 10037 1430 -1911 -851 O
ATOM 1169 CB SER A 166 10.928 -21.913 15.128 1.00 78.14 C
ANISOU 1169 CB SER A 166 11217 8627 9847 1416 -1780 -862 C
ATOM 1170 OG SER A 166 11.769 -23.018 14.850 1.00 93.45 O
ANISOU 1170 OG SER A 166 13172 10542 11794 1437 -1813 -912 O
ATOM 1171 N LEU A 167 8.130 -20.962 16.573 1.00 84.05 N
ANISOU 1171 N LEU A 167 11764 9327 10844 1328 -1803 -707 N
ATOM 1172 CA LEU A 167 7.159 -19.941 16.936 1.00 74.68 C
ANISOU 1172 CA LEU A 167 10541 8156 9678 1303 -1779 -656 C
ATOM 1173 C LEU A 167 7.760 -18.973 17.942 1.00 79.62 C
ANISOU 1173 C LEU A 167 11150 8886 10215 1261 -1613 -586 C
ATOM 1174 O LEU A 167 8.273 -19.389 18.986 1.00 58.46 O
ANISOU 1174 O LEU A 167 8398 6240 7572 1219 -1533 -528 O
ATOM 1175 CB LEU A 167 5.892 -20.570 17.519 1.00 43.68 C
ANISOU 1175 CB LEU A 167 6488 4152 5955 1267 -1854 -607 C
ATOM 1176 CG LEU A 167 5.120 -21.551 16.637 1.00 57.94 C
ANISOU 1176 CG LEU A 167 8288 5845 7879 1302 -2024 -671 C
ATOM 1177 CD1 LEU A 167 3.898 -22.066 17.374 1.00 73.33 C
ANISOU 1177 CD1 LEU A 167 10102 7727 10032 1258 -2077 -610 C
ATOM 1178 CD2 LEU A 167 4.719 -20.910 15.313 1.00 82.04 C
ANISOU 1178 CD2 LEU A 167 11448 8880 10846 1362 -2109 -753 C
ATOM 1179 N CYS A 168 7.695 -17.682 17.621 1.00 89.39 N
ANISOU 1179 N CYS A 168 12453 10174 11336 1274 -1563 -593 N
ATOM 1180 CA CYS A 168 7.971 -16.617 18.585 1.00 63.88 C
ANISOU 1180 CA CYS A 168 9194 7035 8044 1232 -1417 -526 C
ATOM 1181 C CYS A 168 6.723 -16.451 19.445 1.00 58.15 C
ANISOU 1181 C CYS A 168 8350 6286 7460 1184 -1427 -453 C
ATOM 1182 O CYS A 168 5.900 -15.559 19.237 1.00 78.11 O
ANISOU 1182 O CYS A 168 10884 8809 9985 1187 -1441 -448 O
ATOM 1183 CB CYS A 168 8.344 -15.327 17.864 1.00 55.73 C
ANISOU 1183 CB CYS A 168 8277 6057 6843 1265 -1365 -563 C
ATOM 1184 SG CYS A 168 8.689 -13.900 18.916 1.00 80.08 S
ANISOU 1184 SG CYS A 168 11334 9251 9842 1219 -1188 -494 S
ATOM 1185 N PHE A 169 6.580 -17.350 20.425 1.00 53.01 N
ANISOU 1185 N PHE A 169 7586 5617 6938 1141 -1420 -395 N
ATOM 1186 CA PHE A 169 5.417 -17.530 21.279 1.00 53.60 C
ANISOU 1186 CA PHE A 169 7535 5658 7175 1094 -1441 -324 C
ATOM 1187 C PHE A 169 5.708 -17.023 22.686 1.00 54.94 C
ANISOU 1187 C PHE A 169 7623 5916 7335 1037 -1296 -236 C
ATOM 1188 O PHE A 169 6.850 -17.118 23.150 1.00 77.34 O
ANISOU 1188 O PHE A 169 10474 8819 10091 1028 -1201 -224 O
ATOM 1189 CB PHE A 169 5.031 -19.016 21.331 1.00 90.85 C
ANISOU 1189 CB PHE A 169 12181 10283 12053 1089 -1545 -322 C
ATOM 1190 CG PHE A 169 3.644 -19.281 21.863 1.00 80.40 C
ANISOU 1190 CG PHE A 169 10742 8898 10909 1053 -1604 -269 C
ATOM 1191 CD1 PHE A 169 2.543 -19.266 21.016 1.00 63.76 C
ANISOU 1191 CD1 PHE A 169 8646 6709 8872 1080 -1731 -314 C
ATOM 1192 CD2 PHE A 169 3.446 -19.580 23.202 1.00 73.91 C
ANISOU 1192 CD2 PHE A 169 9797 8099 10185 994 -1534 -175 C
ATOM 1193 CE1 PHE A 169 1.272 -19.523 21.503 1.00 79.05 C
ANISOU 1193 CE1 PHE A 169 10472 8586 10978 1047 -1785 -268 C
ATOM 1194 CE2 PHE A 169 2.181 -19.837 23.693 1.00 82.00 C
ANISOU 1194 CE2 PHE A 169 10713 9067 11376 960 -1585 -125 C
ATOM 1195 CZ PHE A 169 1.091 -19.809 22.843 1.00 85.03 C
ANISOU 1195 CZ PHE A 169 11108 9367 11834 985 -1710 -173 C
ATOM 1196 N PRO A 170 4.708 -16.477 23.388 1.00 55.63 N
ANISOU 1196 N PRO A 170 7626 6010 7502 998 -1275 -177 N
ATOM 1197 CA PRO A 170 4.908 -16.062 24.782 1.00 58.16 C
ANISOU 1197 CA PRO A 170 7859 6415 7826 943 -1142 -92 C
ATOM 1198 C PRO A 170 4.794 -17.249 25.728 1.00 56.94 C
ANISOU 1198 C PRO A 170 7590 6236 7808 904 -1146 -27 C
ATOM 1199 O PRO A 170 3.707 -17.788 25.947 1.00 80.07 O
ANISOU 1199 O PRO A 170 10435 9095 10893 884 -1221 5 O
ATOM 1200 CB PRO A 170 3.782 -15.042 25.003 1.00 49.10 C
ANISOU 1200 CB PRO A 170 6670 5272 6715 923 -1136 -64 C
ATOM 1201 CG PRO A 170 2.706 -15.468 24.073 1.00 62.81 C
ANISOU 1201 CG PRO A 170 8415 6899 8551 951 -1289 -107 C
ATOM 1202 CD PRO A 170 3.389 -16.068 22.872 1.00 81.82 C
ANISOU 1202 CD PRO A 170 10933 9264 10892 1008 -1368 -192 C
ATOM 1203 N ARG A 171 5.928 -17.656 26.293 1.00 44.86 N
ANISOU 1203 N ARG A 171 6057 4763 6223 894 -1065 -6 N
ATOM 1204 CA ARG A 171 5.964 -18.733 27.274 1.00 54.19 C
ANISOU 1204 CA ARG A 171 7134 5935 7521 857 -1053 63 C
ATOM 1205 C ARG A 171 6.156 -18.133 28.660 1.00 46.45 C
ANISOU 1205 C ARG A 171 6073 5058 6517 808 -912 148 C
ATOM 1206 O ARG A 171 7.162 -17.464 28.924 1.00 56.23 O
ANISOU 1206 O ARG A 171 7356 6391 7617 810 -804 141 O
ATOM 1207 CB ARG A 171 7.073 -19.736 26.959 1.00 47.65 C
ANISOU 1207 CB ARG A 171 6352 5092 6660 883 -1069 29 C
ATOM 1208 N TYR A 172 5.203 -18.374 29.524 1.00 51.60 N
ANISOU 1208 N TYR A 172 6608 5694 7305 765 -914 223 N
ATOM 1209 CA TYR A 172 5.197 -17.918 30.898 1.00 42.68 C
ANISOU 1209 CA TYR A 172 5385 4656 6176 715 -793 309 C
ATOM 1210 C TYR A 172 5.522 -19.068 31.839 1.00 68.17 C
ANISOU 1210 C TYR A 172 8526 7886 9489 688 -769 381 C
ATOM 1211 O TYR A 172 5.320 -20.238 31.502 1.00 76.50 O
ANISOU 1211 O TYR A 172 9564 8850 10651 697 -865 378 O
ATOM 1212 CB TYR A 172 3.826 -17.326 31.248 1.00 45.71 C
ANISOU 1212 CB TYR A 172 5692 5022 6653 685 -807 348 C
ATOM 1213 CG TYR A 172 3.376 -16.215 30.325 1.00 51.38 C
ANISOU 1213 CG TYR A 172 6489 5729 7304 713 -839 282 C
ATOM 1214 CD1 TYR A 172 2.736 -16.498 29.123 1.00 70.78 C
ANISOU 1214 CD1 TYR A 172 9001 8081 9810 750 -975 218 C
ATOM 1215 CD2 TYR A 172 3.584 -14.885 30.658 1.00 58.11 C
ANISOU 1215 CD2 TYR A 172 7359 6674 8046 704 -735 284 C
ATOM 1216 CE1 TYR A 172 2.324 -15.485 28.273 1.00 54.18 C
ANISOU 1216 CE1 TYR A 172 6973 5970 7644 778 -1006 161 C
ATOM 1217 CE2 TYR A 172 3.175 -13.862 29.813 1.00 60.45 C
ANISOU 1217 CE2 TYR A 172 7729 6957 8283 730 -764 228 C
ATOM 1218 CZ TYR A 172 2.546 -14.169 28.624 1.00 53.61 C
ANISOU 1218 CZ TYR A 172 6918 5988 7463 767 -900 169 C
ATOM 1219 OH TYR A 172 2.139 -13.155 27.790 1.00 77.24 O
ANISOU 1219 OH TYR A 172 9984 8970 10395 796 -929 117 O
ATOM 1220 N PRO A 173 6.040 -18.768 33.033 1.00 52.75 N
ANISOU 1220 N PRO A 173 6514 6038 7490 655 -643 447 N
ATOM 1221 CA PRO A 173 6.270 -19.840 34.013 1.00 38.51 C
ANISOU 1221 CA PRO A 173 4619 4241 5772 627 -618 527 C
ATOM 1222 C PRO A 173 4.989 -20.482 34.511 1.00 45.57 C
ANISOU 1222 C PRO A 173 5399 5065 6852 592 -676 598 C
ATOM 1223 O PRO A 173 5.002 -21.665 34.872 1.00 47.73 O
ANISOU 1223 O PRO A 173 5613 5290 7231 581 -710 646 O
ATOM 1224 CB PRO A 173 7.016 -19.124 35.150 1.00 38.61 C
ANISOU 1224 CB PRO A 173 4599 4393 5678 602 -466 576 C
ATOM 1225 CG PRO A 173 7.584 -17.886 34.522 1.00 54.33 C
ANISOU 1225 CG PRO A 173 6693 6441 7508 628 -419 499 C
ATOM 1226 CD PRO A 173 6.591 -17.480 33.481 1.00 55.90 C
ANISOU 1226 CD PRO A 173 6937 6557 7747 647 -518 445 C
ATOM 1227 N SER A 174 3.885 -19.741 34.539 1.00 42.92 N
ANISOU 1227 N SER A 174 5026 4718 6562 574 -689 606 N
ATOM 1228 CA SER A 174 2.613 -20.259 35.023 1.00 53.83 C
ANISOU 1228 CA SER A 174 6295 6035 8121 539 -739 672 C
ATOM 1229 C SER A 174 1.501 -19.362 34.500 1.00 64.97 C
ANISOU 1229 C SER A 174 7714 7413 9558 540 -785 637 C
ATOM 1230 O SER A 174 1.750 -18.272 33.981 1.00 77.43 O
ANISOU 1230 O SER A 174 9373 9034 11011 562 -758 577 O
ATOM 1231 CB SER A 174 2.583 -20.333 36.553 1.00 58.77 C
ANISOU 1231 CB SER A 174 6804 6745 8782 490 -630 783 C
ATOM 1232 OG SER A 174 2.628 -19.037 37.123 1.00 58.75 O
ANISOU 1232 OG SER A 174 6793 6853 8677 473 -522 793 O
ATOM 1233 N GLU A 175 0.262 -19.839 34.646 1.00 72.36 N
ANISOU 1233 N GLU A 175 8564 8269 10662 517 -856 675 N
ATOM 1234 CA GLU A 175 -0.882 -19.030 34.239 1.00 71.45 C
ANISOU 1234 CA GLU A 175 8441 8119 10587 515 -903 647 C
ATOM 1235 C GLU A 175 -1.069 -17.830 35.158 1.00 63.31 C
ANISOU 1235 C GLU A 175 7363 7199 9494 482 -783 691 C
ATOM 1236 O GLU A 175 -1.656 -16.821 34.747 1.00 52.11 O
ANISOU 1236 O GLU A 175 5971 5782 8046 489 -794 652 O
ATOM 1237 CB GLU A 175 -2.148 -19.885 34.201 1.00 83.02 C
ANISOU 1237 CB GLU A 175 9819 9470 12255 496 -1007 677 C
ATOM 1238 CG GLU A 175 -2.150 -20.940 33.099 1.00 88.09 C
ANISOU 1238 CG GLU A 175 10513 9991 12967 534 -1145 614 C
ATOM 1239 CD GLU A 175 -2.208 -20.340 31.702 1.00 93.34 C
ANISOU 1239 CD GLU A 175 11297 10614 13553 586 -1230 503 C
ATOM 1240 OE1 GLU A 175 -3.090 -19.492 31.449 1.00 85.54 O
ANISOU 1240 OE1 GLU A 175 10306 9617 12577 585 -1252 483 O
ATOM 1241 OE2 GLU A 175 -1.367 -20.715 30.857 1.00 90.85 O
ANISOU 1241 OE2 GLU A 175 11079 10277 13163 629 -1273 436 O
ATOM 1242 N GLY A 176 -0.580 -17.917 36.398 1.00 69.18 N
ANISOU 1242 N GLY A 176 8034 8034 10215 447 -669 770 N
ATOM 1243 CA GLY A 176 -0.584 -16.748 37.261 1.00 46.38 C
ANISOU 1243 CA GLY A 176 5109 5264 7250 420 -548 802 C
ATOM 1244 C GLY A 176 0.303 -15.641 36.729 1.00 56.20 C
ANISOU 1244 C GLY A 176 6466 6578 8312 452 -494 728 C
ATOM 1245 O GLY A 176 -0.062 -14.464 36.775 1.00 66.15 O
ANISOU 1245 O GLY A 176 7729 7883 9521 446 -451 710 O
ATOM 1246 N HIS A 177 1.476 -16.005 36.203 1.00 54.94 N
ANISOU 1246 N HIS A 177 6396 6423 8054 486 -495 684 N
ATOM 1247 CA HIS A 177 2.334 -15.019 35.552 1.00 64.89 C
ANISOU 1247 CA HIS A 177 7772 7737 9147 520 -453 608 C
ATOM 1248 C HIS A 177 1.688 -14.472 34.282 1.00 69.54 C
ANISOU 1248 C HIS A 177 8441 8248 9733 553 -550 530 C
ATOM 1249 O HIS A 177 1.826 -13.281 33.974 1.00 60.27 O
ANISOU 1249 O HIS A 177 7324 7121 8453 566 -506 488 O
ATOM 1250 CB HIS A 177 3.699 -15.634 35.240 1.00 65.05 C
ANISOU 1250 CB HIS A 177 7868 7773 9075 549 -440 577 C
ATOM 1251 CG HIS A 177 4.592 -15.765 36.436 1.00 66.86 C
ANISOU 1251 CG HIS A 177 8044 8109 9251 524 -319 637 C
ATOM 1252 ND1 HIS A 177 4.293 -16.585 37.502 1.00 68.42 N
ANISOU 1252 ND1 HIS A 177 8127 8315 9554 487 -298 729 N
ATOM 1253 CD2 HIS A 177 5.779 -15.181 36.731 1.00 59.14 C
ANISOU 1253 CD2 HIS A 177 7110 7235 8124 532 -213 619 C
ATOM 1254 CE1 HIS A 177 5.256 -16.500 38.403 1.00 53.36 C
ANISOU 1254 CE1 HIS A 177 6197 6515 7562 476 -186 765 C
ATOM 1255 NE2 HIS A 177 6.169 -15.654 37.960 1.00 50.73 N
ANISOU 1255 NE2 HIS A 177 5959 6242 7076 502 -134 697 N
ATOM 1256 N ARG A 178 0.986 -15.325 33.528 1.00 70.74 N
ANISOU 1256 N ARG A 178 8597 8281 10001 569 -683 509 N
ATOM 1257 CA AARG A 178 0.307 -14.859 32.322 0.50 63.59 C
ANISOU 1257 CA AARG A 178 7763 7300 9099 603 -784 435 C
ATOM 1258 CA BARG A 178 0.313 -14.854 32.322 0.50 69.06 C
ANISOU 1258 CA BARG A 178 8456 7993 9790 603 -783 435 C
ATOM 1259 C ARG A 178 -0.827 -13.904 32.668 1.00 64.62 C
ANISOU 1259 C ARG A 178 7833 7441 9279 577 -769 458 C
ATOM 1260 O ARG A 178 -1.062 -12.921 31.955 1.00 74.78 O
ANISOU 1260 O ARG A 178 9187 8726 10500 602 -786 403 O
ATOM 1261 CB AARG A 178 -0.212 -16.054 31.517 0.50 60.45 C
ANISOU 1261 CB AARG A 178 7371 6773 8823 625 -930 408 C
ATOM 1262 CB BARG A 178 -0.211 -16.035 31.502 0.50 58.07 C
ANISOU 1262 CB BARG A 178 7072 6472 8520 625 -931 407 C
ATOM 1263 CG AARG A 178 -1.007 -15.684 30.278 0.50 59.91 C
ANISOU 1263 CG AARG A 178 7369 6622 8773 662 -1047 333 C
ATOM 1264 CG BARG A 178 -0.816 -15.611 30.180 0.50 59.70 C
ANISOU 1264 CG BARG A 178 7361 6602 8718 668 -1041 324 C
ATOM 1265 CD AARG A 178 -1.361 -16.910 29.445 0.50 59.69 C
ANISOU 1265 CD AARG A 178 7354 6472 8855 689 -1191 296 C
ATOM 1266 CD BARG A 178 -1.604 -16.721 29.505 0.50 60.87 C
ANISOU 1266 CD BARG A 178 7491 6622 9015 684 -1190 301 C
ATOM 1267 NE AARG A 178 -2.361 -16.610 28.422 0.50 74.06 N
ANISOU 1267 NE AARG A 178 9210 8209 10722 718 -1309 235 N
ATOM 1268 NE BARG A 178 -2.338 -16.208 28.351 0.50 73.49 N
ANISOU 1268 NE BARG A 178 9155 8155 10612 722 -1293 227 N
ATOM 1269 CZ AARG A 178 -3.650 -16.923 28.520 0.50 70.50 C
ANISOU 1269 CZ AARG A 178 8673 7682 10433 699 -1387 257 C
ATOM 1270 CZ BARG A 178 -1.824 -16.090 27.130 0.50 65.68 C
ANISOU 1270 CZ BARG A 178 8292 7142 9522 778 -1353 141 C
ATOM 1271 NH1AARG A 178 -4.103 -17.552 29.597 0.50 66.94 N
ANISOU 1271 NH1AARG A 178 8095 7226 10113 648 -1357 340 N
ATOM 1272 NH1BARG A 178 -0.570 -16.452 26.901 0.50 60.55 N
ANISOU 1272 NH1BARG A 178 7715 6525 8767 800 -1319 115 N
ATOM 1273 NH2AARG A 178 -4.487 -16.613 27.540 0.50 68.13 N
ANISOU 1273 NH2AARG A 178 8412 7311 10163 730 -1495 195 N
ATOM 1274 NH2BARG A 178 -2.564 -15.610 26.139 0.50 53.34 N
ANISOU 1274 NH2BARG A 178 6782 5522 7962 812 -1447 81 N
ATOM 1275 N ALA A 179 -1.540 -14.176 33.761 1.00 55.62 N
ANISOU 1275 N ALA A 179 6564 6314 8255 529 -736 539 N
ATOM 1276 CA ALA A 179 -2.621 -13.289 34.176 1.00 47.89 C
ANISOU 1276 CA ALA A 179 5516 5350 7329 501 -716 562 C
ATOM 1277 C ALA A 179 -2.079 -11.959 34.682 1.00 52.74 C
ANISOU 1277 C ALA A 179 6149 6085 7806 492 -586 561 C
ATOM 1278 O ALA A 179 -2.630 -10.896 34.368 1.00 64.91 O
ANISOU 1278 O ALA A 179 7710 7631 9322 498 -587 531 O
ATOM 1279 CB ALA A 179 -3.470 -13.969 35.247 1.00 53.75 C
ANISOU 1279 CB ALA A 179 6114 6079 8229 450 -708 652 C
ATOM 1280 N PHE A 180 -1.004 -11.997 35.473 1.00 45.73 N
ANISOU 1280 N PHE A 180 5252 5294 6830 479 -475 594 N
ATOM 1281 CA PHE A 180 -0.411 -10.761 35.969 1.00 38.38 C
ANISOU 1281 CA PHE A 180 4336 4479 5768 471 -349 588 C
ATOM 1282 C PHE A 180 0.064 -9.888 34.819 1.00 43.88 C
ANISOU 1282 C PHE A 180 5166 5168 6338 517 -367 500 C
ATOM 1283 O PHE A 180 -0.214 -8.685 34.783 1.00 63.27 O
ANISOU 1283 O PHE A 180 7634 7661 8745 516 -325 479 O
ATOM 1284 CB PHE A 180 0.748 -11.062 36.919 1.00 55.22 C
ANISOU 1284 CB PHE A 180 6444 6712 7826 456 -238 629 C
ATOM 1285 CG PHE A 180 1.553 -9.845 37.287 1.00 59.83 C
ANISOU 1285 CG PHE A 180 7060 7413 8262 456 -113 608 C
ATOM 1286 CD1 PHE A 180 1.056 -8.911 38.184 1.00 61.68 C
ANISOU 1286 CD1 PHE A 180 7213 7722 8500 421 -28 641 C
ATOM 1287 CD2 PHE A 180 2.802 -9.628 36.726 1.00 66.68 C
ANISOU 1287 CD2 PHE A 180 8035 8312 8989 490 -80 551 C
ATOM 1288 CE1 PHE A 180 1.789 -7.788 38.517 1.00 59.79 C
ANISOU 1288 CE1 PHE A 180 7000 7587 8132 422 85 617 C
ATOM 1289 CE2 PHE A 180 3.540 -8.503 37.057 1.00 60.31 C
ANISOU 1289 CE2 PHE A 180 7255 7609 8053 489 35 529 C
ATOM 1290 CZ PHE A 180 3.033 -7.585 37.954 1.00 61.14 C
ANISOU 1290 CZ PHE A 180 7278 7787 8168 455 116 561 C
ATOM 1291 N HIS A 181 0.777 -10.484 33.862 1.00 50.61 N
ANISOU 1291 N HIS A 181 6118 5971 7139 558 -429 448 N
ATOM 1292 CA HIS A 181 1.278 -9.715 32.728 1.00 62.50 C
ANISOU 1292 CA HIS A 181 7756 7470 8522 604 -445 367 C
ATOM 1293 C HIS A 181 0.140 -9.044 31.966 1.00 62.22 C
ANISOU 1293 C HIS A 181 7742 7368 8533 620 -527 333 C
ATOM 1294 O HIS A 181 0.226 -7.857 31.627 1.00 76.25 O
ANISOU 1294 O HIS A 181 9574 9179 10219 634 -487 298 O
ATOM 1295 CB HIS A 181 2.093 -10.618 31.805 1.00 60.08 C
ANISOU 1295 CB HIS A 181 7544 7111 8171 646 -513 318 C
ATOM 1296 CG HIS A 181 2.782 -9.885 30.698 1.00 42.51 C
ANISOU 1296 CG HIS A 181 5457 4891 5805 694 -516 239 C
ATOM 1297 ND1 HIS A 181 2.149 -9.549 29.521 1.00 78.77 N
ANISOU 1297 ND1 HIS A 181 10124 9407 10400 731 -616 183 N
ATOM 1298 CD2 HIS A 181 4.048 -9.418 30.592 1.00 53.46 C
ANISOU 1298 CD2 HIS A 181 6920 6349 7042 711 -429 208 C
ATOM 1299 CE1 HIS A 181 2.995 -8.906 28.737 1.00 75.40 C
ANISOU 1299 CE1 HIS A 181 9813 9005 9828 769 -590 124 C
ATOM 1300 NE2 HIS A 181 4.154 -8.814 29.362 1.00 77.82 N
ANISOU 1300 NE2 HIS A 181 10124 9400 10044 757 -476 137 N
ATOM 1301 N LEU A 182 -0.949 -9.775 31.717 1.00 49.87 N
ANISOU 1301 N LEU A 182 6129 5708 7113 616 -641 344 N
ATOM 1302 CA LEU A 182 -2.032 -9.227 30.905 1.00 62.44 C
ANISOU 1302 CA LEU A 182 7744 7228 8752 636 -733 306 C
ATOM 1303 C LEU A 182 -2.789 -8.127 31.641 1.00 56.52 C
ANISOU 1303 C LEU A 182 6919 6528 8028 601 -666 340 C
ATOM 1304 O LEU A 182 -3.173 -7.122 31.031 1.00 58.19 O
ANISOU 1304 O LEU A 182 7181 6729 8197 623 -683 299 O
ATOM 1305 CB LEU A 182 -2.984 -10.341 30.471 1.00 66.78 C
ANISOU 1305 CB LEU A 182 8256 7661 9458 640 -873 306 C
ATOM 1306 CG LEU A 182 -2.362 -11.380 29.534 1.00 58.30 C
ANISOU 1306 CG LEU A 182 7264 6521 8364 682 -961 258 C
ATOM 1307 CD1 LEU A 182 -3.386 -12.400 29.059 1.00 45.62 C
ANISOU 1307 CD1 LEU A 182 5618 4796 6920 688 -1105 250 C
ATOM 1308 CD2 LEU A 182 -1.688 -10.697 28.354 1.00 72.12 C
ANISOU 1308 CD2 LEU A 182 9162 8277 9965 737 -977 177 C
ATOM 1309 N ILE A 183 -3.026 -8.296 32.945 1.00 51.77 N
ANISOU 1309 N ILE A 183 6195 5981 7494 550 -589 413 N
ATOM 1310 CA ILE A 183 -3.710 -7.238 33.683 1.00 50.26 C
ANISOU 1310 CA ILE A 183 5928 5844 7323 517 -520 442 C
ATOM 1311 C ILE A 183 -2.763 -6.077 33.940 1.00 48.75 C
ANISOU 1311 C ILE A 183 5786 5760 6978 520 -394 423 C
ATOM 1312 O ILE A 183 -3.192 -4.919 33.995 1.00 59.22 O
ANISOU 1312 O ILE A 183 7106 7115 8282 515 -358 411 O
ATOM 1313 CB ILE A 183 -4.323 -7.779 34.991 1.00 41.43 C
ANISOU 1313 CB ILE A 183 4660 4752 6329 461 -479 526 C
ATOM 1314 CG1 ILE A 183 -3.241 -8.263 35.962 1.00 65.24 C
ANISOU 1314 CG1 ILE A 183 7643 7857 9287 439 -373 574 C
ATOM 1315 CG2 ILE A 183 -5.296 -8.904 34.687 1.00 46.91 C
ANISOU 1315 CG2 ILE A 183 5306 5331 7185 458 -606 541 C
ATOM 1316 CD1 ILE A 183 -2.962 -7.313 37.114 1.00 60.97 C
ANISOU 1316 CD1 ILE A 183 7039 7443 8683 405 -229 609 C
ATOM 1317 N PHE A 184 -1.468 -6.355 34.091 1.00 38.50 N
ANISOU 1317 N PHE A 184 4534 4520 5573 528 -327 419 N
ATOM 1318 CA PHE A 184 -0.498 -5.275 34.210 1.00 39.90 C
ANISOU 1318 CA PHE A 184 4766 4791 5601 536 -214 392 C
ATOM 1319 C PHE A 184 -0.414 -4.500 32.904 1.00 48.09 C
ANISOU 1319 C PHE A 184 5931 5785 6557 584 -264 318 C
ATOM 1320 O PHE A 184 -0.440 -3.263 32.896 1.00 63.15 O
ANISOU 1320 O PHE A 184 7857 7735 8402 586 -205 299 O
ATOM 1321 CB PHE A 184 0.865 -5.841 34.609 1.00 45.10 C
ANISOU 1321 CB PHE A 184 5449 5515 6174 537 -141 401 C
ATOM 1322 CG PHE A 184 1.945 -4.813 34.713 1.00 39.52 C
ANISOU 1322 CG PHE A 184 4799 4903 5315 546 -25 369 C
ATOM 1323 CD1 PHE A 184 2.069 -4.031 35.847 1.00 44.73 C
ANISOU 1323 CD1 PHE A 184 5380 5667 5948 511 98 401 C
ATOM 1324 CD2 PHE A 184 2.853 -4.643 33.683 1.00 56.76 C
ANISOU 1324 CD2 PHE A 184 7113 7071 7382 591 -38 306 C
ATOM 1325 CE1 PHE A 184 3.071 -3.089 35.943 1.00 59.93 C
ANISOU 1325 CE1 PHE A 184 7355 7676 7739 519 204 368 C
ATOM 1326 CE2 PHE A 184 3.854 -3.704 33.775 1.00 41.26 C
ANISOU 1326 CE2 PHE A 184 5201 5192 5285 598 71 276 C
ATOM 1327 CZ PHE A 184 3.963 -2.926 34.905 1.00 44.04 C
ANISOU 1327 CZ PHE A 184 5473 5644 5618 562 191 306 C
ATOM 1328 N GLU A 185 -0.341 -5.219 31.783 1.00 45.32 N
ANISOU 1328 N GLU A 185 5666 5347 6208 625 -375 277 N
ATOM 1329 CA GLU A 185 -0.366 -4.568 30.480 1.00 49.14 C
ANISOU 1329 CA GLU A 185 6269 5782 6620 674 -436 210 C
ATOM 1330 C GLU A 185 -1.651 -3.772 30.286 1.00 53.20 C
ANISOU 1330 C GLU A 185 6752 6256 7207 671 -484 208 C
ATOM 1331 O GLU A 185 -1.617 -2.647 29.777 1.00 71.01 O
ANISOU 1331 O GLU A 185 9073 8525 9385 693 -462 173 O
ATOM 1332 CB GLU A 185 -0.191 -5.617 29.385 1.00 53.63 C
ANISOU 1332 CB GLU A 185 6919 6263 7195 717 -557 168 C
ATOM 1333 CG GLU A 185 -0.027 -5.069 27.991 1.00 61.38 C
ANISOU 1333 CG GLU A 185 8037 7202 8085 774 -618 97 C
ATOM 1334 CD GLU A 185 0.269 -6.158 26.987 1.00 75.10 C
ANISOU 1334 CD GLU A 185 9851 8864 9821 816 -728 54 C
ATOM 1335 OE1 GLU A 185 0.735 -7.239 27.405 1.00 73.18 O
ANISOU 1335 OE1 GLU A 185 9572 8621 9611 802 -727 75 O
ATOM 1336 OE2 GLU A 185 0.029 -5.937 25.784 1.00 89.28 O
ANISOU 1336 OE2 GLU A 185 11741 10602 11581 864 -816 -1 O
ATOM 1337 N ALA A 186 -2.792 -4.318 30.720 1.00 49.98 N
ANISOU 1337 N ALA A 186 6242 5799 6950 643 -546 246 N
ATOM 1338 CA ALA A 186 -4.054 -3.602 30.549 1.00 56.04 C
ANISOU 1338 CA ALA A 186 6973 6525 7795 640 -596 243 C
ATOM 1339 C ALA A 186 -4.114 -2.349 31.419 1.00 52.36 C
ANISOU 1339 C ALA A 186 6451 6147 7295 608 -474 266 C
ATOM 1340 O ALA A 186 -4.554 -1.291 30.957 1.00 52.90 O
ANISOU 1340 O ALA A 186 6555 6206 7339 624 -482 237 O
ATOM 1341 CB ALA A 186 -5.237 -4.519 30.856 1.00 49.29 C
ANISOU 1341 CB ALA A 186 6015 5598 7116 615 -686 278 C
ATOM 1342 N VAL A 187 -3.676 -2.441 32.675 1.00 45.87 N
ANISOU 1342 N VAL A 187 5543 5415 6472 564 -362 316 N
ATOM 1343 CA VAL A 187 -3.823 -1.318 33.599 1.00 41.95 C
ANISOU 1343 CA VAL A 187 4976 5004 5958 530 -248 338 C
ATOM 1344 C VAL A 187 -2.791 -0.235 33.308 1.00 36.89 C
ANISOU 1344 C VAL A 187 4427 4429 5162 553 -159 297 C
ATOM 1345 O VAL A 187 -3.135 0.931 33.088 1.00 44.58 O
ANISOU 1345 O VAL A 187 5418 5410 6110 560 -138 274 O
ATOM 1346 CB VAL A 187 -3.735 -1.805 35.057 1.00 46.62 C
ANISOU 1346 CB VAL A 187 5441 5672 6601 477 -161 406 C
ATOM 1347 CG1 VAL A 187 -3.637 -0.625 36.021 1.00 59.23 C
ANISOU 1347 CG1 VAL A 187 6975 7374 8154 447 -30 420 C
ATOM 1348 CG2 VAL A 187 -4.936 -2.671 35.393 1.00 32.80 C
ANISOU 1348 CG2 VAL A 187 3588 3856 5017 451 -242 451 C
ATOM 1349 N THR A 188 -1.509 -0.599 33.314 1.00 43.07 N
ANISOU 1349 N THR A 188 5266 5258 5842 564 -104 287 N
ATOM 1350 CA THR A 188 -0.464 0.401 33.118 1.00 36.46 C
ANISOU 1350 CA THR A 188 4507 4486 4859 581 -8 250 C
ATOM 1351 C THR A 188 -0.386 0.861 31.671 1.00 43.93 C
ANISOU 1351 C THR A 188 5589 5365 5738 635 -80 189 C
ATOM 1352 O THR A 188 0.067 1.979 31.401 1.00 60.20 O
ANISOU 1352 O THR A 188 7708 7462 7704 650 -15 159 O
ATOM 1353 CB THR A 188 0.888 -0.153 33.559 1.00 58.22 C
ANISOU 1353 CB THR A 188 7280 7311 7528 578 71 255 C
ATOM 1354 OG1 THR A 188 1.226 -1.283 32.748 1.00 59.69 O
ANISOU 1354 OG1 THR A 188 7537 7429 7712 609 -22 238 O
ATOM 1355 CG2 THR A 188 0.831 -0.578 35.018 1.00 43.91 C
ANISOU 1355 CG2 THR A 188 5334 5573 5776 527 146 318 C
ATOM 1356 N GLY A 189 -0.811 0.024 30.732 1.00 49.58 N
ANISOU 1356 N GLY A 189 6355 5983 6499 666 -212 171 N
ATOM 1357 CA GLY A 189 -0.746 0.383 29.332 1.00 50.11 C
ANISOU 1357 CA GLY A 189 6552 5988 6498 721 -287 115 C
ATOM 1358 C GLY A 189 -2.022 0.915 28.727 1.00 39.28 C
ANISOU 1358 C GLY A 189 5182 4543 5199 737 -380 103 C
ATOM 1359 O GLY A 189 -2.046 1.211 27.528 1.00 32.55 O
ANISOU 1359 O GLY A 189 4438 3637 4293 786 -450 57 O
ATOM 1360 N PHE A 190 -3.097 1.040 29.503 1.00 35.26 N
ANISOU 1360 N PHE A 190 4554 4031 4811 698 -384 141 N
ATOM 1361 CA PHE A 190 -4.317 1.628 28.966 1.00 46.18 C
ANISOU 1361 CA PHE A 190 5934 5348 6265 713 -468 127 C
ATOM 1362 C PHE A 190 -5.232 2.172 30.058 1.00 54.74 C
ANISOU 1362 C PHE A 190 6885 6465 7450 663 -418 169 C
ATOM 1363 O PHE A 190 -5.505 3.376 30.092 1.00 47.93 O
ANISOU 1363 O PHE A 190 6022 5626 6565 663 -374 159 O
ATOM 1364 CB PHE A 190 -5.077 0.611 28.114 1.00 46.03 C
ANISOU 1364 CB PHE A 190 5936 5220 6333 741 -627 110 C
ATOM 1365 CG PHE A 190 -6.149 1.229 27.265 1.00 60.23 C
ANISOU 1365 CG PHE A 190 7766 6946 8175 771 -726 82 C
ATOM 1366 CD1 PHE A 190 -5.846 1.747 26.017 1.00 63.87 C
ANISOU 1366 CD1 PHE A 190 8360 7373 8534 829 -772 31 C
ATOM 1367 CD2 PHE A 190 -7.454 1.311 27.723 1.00 42.18 C
ANISOU 1367 CD2 PHE A 190 5373 4625 6029 744 -770 106 C
ATOM 1368 CE1 PHE A 190 -6.828 2.326 25.235 1.00 69.25 C
ANISOU 1368 CE1 PHE A 190 9070 7989 9251 861 -864 7 C
ATOM 1369 CE2 PHE A 190 -8.438 1.888 26.946 1.00 43.37 C
ANISOU 1369 CE2 PHE A 190 5550 4708 6220 774 -862 78 C
ATOM 1370 CZ PHE A 190 -8.126 2.396 25.701 1.00 65.15 C
ANISOU 1370 CZ PHE A 190 8444 7434 8874 833 -911 29 C
ATOM 1371 N LEU A 191 -5.709 1.299 30.949 1.00 46.51 N
ANISOU 1371 N LEU A 191 5727 5425 6519 621 -425 215 N
ATOM 1372 CA LEU A 191 -6.721 1.696 31.926 1.00 43.12 C
ANISOU 1372 CA LEU A 191 5166 5017 6201 576 -394 254 C
ATOM 1373 C LEU A 191 -6.268 2.902 32.743 1.00 42.02 C
ANISOU 1373 C LEU A 191 4994 4982 5990 551 -250 262 C
ATOM 1374 O LEU A 191 -6.931 3.945 32.754 1.00 47.91 O
ANISOU 1374 O LEU A 191 5718 5728 6759 548 -238 252 O
ATOM 1375 CB LEU A 191 -7.058 0.514 32.837 1.00 54.06 C
ANISOU 1375 CB LEU A 191 6439 6404 7699 534 -401 309 C
ATOM 1376 CG LEU A 191 -7.683 -0.691 32.126 1.00 83.26 C
ANISOU 1376 CG LEU A 191 10148 9993 11496 553 -547 303 C
ATOM 1377 CD1 LEU A 191 -7.853 -1.862 33.087 1.00 97.19 C
ANISOU 1377 CD1 LEU A 191 11802 11765 13363 510 -538 363 C
ATOM 1378 CD2 LEU A 191 -9.015 -0.315 31.481 1.00 53.44 C
ANISOU 1378 CD2 LEU A 191 6361 6128 7814 568 -656 280 C
ATOM 1379 N LEU A 192 -5.131 2.784 33.425 1.00 43.04 N
ANISOU 1379 N LEU A 192 5119 5200 6036 534 -139 277 N
ATOM 1380 CA LEU A 192 -4.645 3.901 34.232 1.00 42.51 C
ANISOU 1380 CA LEU A 192 5016 5235 5901 510 0 279 C
ATOM 1381 C LEU A 192 -4.367 5.153 33.409 1.00 40.32 C
ANISOU 1381 C LEU A 192 4837 4952 5530 546 17 229 C
ATOM 1382 O LEU A 192 -4.846 6.234 33.797 1.00 34.83 O
ANISOU 1382 O LEU A 192 4093 4286 4853 530 68 227 O
ATOM 1383 CB LEU A 192 -3.414 3.466 35.028 1.00 42.69 C
ANISOU 1383 CB LEU A 192 5023 5351 5846 491 105 299 C
ATOM 1384 CG LEU A 192 -2.655 4.618 35.676 1.00 38.71 C
ANISOU 1384 CG LEU A 192 4508 4953 5248 477 249 287 C
ATOM 1385 CD1 LEU A 192 -3.498 5.278 36.757 1.00 55.72 C
ANISOU 1385 CD1 LEU A 192 6531 7159 7482 434 307 316 C
ATOM 1386 CD2 LEU A 192 -1.344 4.114 36.240 1.00 73.67 C
ANISOU 1386 CD2 LEU A 192 8943 9462 9587 469 337 296 C
ATOM 1387 N PRO A 193 -3.630 5.102 32.289 1.00 45.10 N
ANISOU 1387 N PRO A 193 5579 5521 6038 593 -20 189 N
ATOM 1388 CA PRO A 193 -3.428 6.345 31.521 1.00 55.50 C
ANISOU 1388 CA PRO A 193 6986 6830 7270 627 0 147 C
ATOM 1389 C PRO A 193 -4.708 6.912 30.933 1.00 42.76 C
ANISOU 1389 C PRO A 193 5370 5140 5736 643 -92 137 C
ATOM 1390 O PRO A 193 -4.914 8.131 30.979 1.00 52.29 O
ANISOU 1390 O PRO A 193 6575 6367 6927 642 -42 125 O
ATOM 1391 CB PRO A 193 -2.427 5.931 30.430 1.00 37.13 C
ANISOU 1391 CB PRO A 193 4801 4475 4831 675 -34 111 C
ATOM 1392 CG PRO A 193 -2.523 4.460 30.350 1.00 36.60 C
ANISOU 1392 CG PRO A 193 4721 4364 4820 675 -119 127 C
ATOM 1393 CD PRO A 193 -2.842 3.990 31.727 1.00 33.57 C
ANISOU 1393 CD PRO A 193 4194 4034 4527 619 -66 179 C
ATOM 1394 N PHE A 194 -5.584 6.067 30.385 1.00 40.25 N
ANISOU 1394 N PHE A 194 5050 4733 5509 657 -226 139 N
ATOM 1395 CA PHE A 194 -6.815 6.579 29.792 1.00 37.53 C
ANISOU 1395 CA PHE A 194 4705 4313 5242 675 -321 126 C
ATOM 1396 C PHE A 194 -7.829 7.012 30.839 1.00 46.26 C
ANISOU 1396 C PHE A 194 5670 5443 6465 627 -288 158 C
ATOM 1397 O PHE A 194 -8.708 7.825 30.533 1.00 34.91 O
ANISOU 1397 O PHE A 194 4223 3967 5074 637 -326 145 O
ATOM 1398 CB PHE A 194 -7.439 5.538 28.866 1.00 41.13 C
ANISOU 1398 CB PHE A 194 5201 4666 5762 707 -478 113 C
ATOM 1399 CG PHE A 194 -7.311 5.879 27.415 1.00 51.05 C
ANISOU 1399 CG PHE A 194 6599 5859 6937 772 -559 65 C
ATOM 1400 CD1 PHE A 194 -6.173 5.530 26.707 1.00 68.14 C
ANISOU 1400 CD1 PHE A 194 8881 8031 8980 807 -553 39 C
ATOM 1401 CD2 PHE A 194 -8.321 6.562 26.761 1.00 44.84 C
ANISOU 1401 CD2 PHE A 194 5829 5010 6197 798 -639 47 C
ATOM 1402 CE1 PHE A 194 -6.049 5.849 25.369 1.00 48.73 C
ANISOU 1402 CE1 PHE A 194 6554 5519 6442 868 -625 -2 C
ATOM 1403 CE2 PHE A 194 -8.204 6.883 25.424 1.00 59.68 C
ANISOU 1403 CE2 PHE A 194 7842 6835 7998 860 -714 7 C
ATOM 1404 CZ PHE A 194 -7.065 6.525 24.726 1.00 61.43 C
ANISOU 1404 CZ PHE A 194 8180 7067 8094 895 -706 -17 C
ATOM 1405 N LEU A 195 -7.740 6.486 32.059 1.00 40.48 N
ANISOU 1405 N LEU A 195 4825 4774 5781 577 -218 199 N
ATOM 1406 CA LEU A 195 -8.569 7.028 33.126 1.00 47.58 C
ANISOU 1406 CA LEU A 195 5591 5713 6774 530 -165 227 C
ATOM 1407 C LEU A 195 -8.187 8.470 33.428 1.00 49.33 C
ANISOU 1407 C LEU A 195 5816 6003 6922 526 -53 209 C
ATOM 1408 O LEU A 195 -9.055 9.285 33.762 1.00 39.97 O
ANISOU 1408 O LEU A 195 4563 4818 5805 509 -43 210 O
ATOM 1409 CB LEU A 195 -8.446 6.155 34.371 1.00 56.67 C
ANISOU 1409 CB LEU A 195 6628 6926 7978 480 -106 278 C
ATOM 1410 CG LEU A 195 -9.481 6.343 35.475 1.00 50.68 C
ANISOU 1410 CG LEU A 195 5718 6197 7342 430 -75 315 C
ATOM 1411 CD1 LEU A 195 -9.757 5.005 36.130 1.00 32.70 C
ANISOU 1411 CD1 LEU A 195 3356 3914 5155 398 -102 365 C
ATOM 1412 CD2 LEU A 195 -8.978 7.347 36.498 1.00 46.68 C
ANISOU 1412 CD2 LEU A 195 5154 5806 6778 399 75 319 C
ATOM 1413 N ILE A 196 -6.899 8.801 33.301 1.00 51.32 N
ANISOU 1413 N ILE A 196 6147 6311 7040 540 32 190 N
ATOM 1414 CA ILE A 196 -6.460 10.184 33.446 1.00 46.63 C
ANISOU 1414 CA ILE A 196 5571 5773 6373 541 134 167 C
ATOM 1415 C ILE A 196 -6.948 11.021 32.273 1.00 36.54 C
ANISOU 1415 C ILE A 196 4384 4417 5084 586 61 133 C
ATOM 1416 O ILE A 196 -7.235 12.213 32.428 1.00 52.47 O
ANISOU 1416 O ILE A 196 6380 6453 7106 582 110 121 O
ATOM 1417 CB ILE A 196 -4.926 10.241 33.583 1.00 46.16 C
ANISOU 1417 CB ILE A 196 5573 5789 6176 546 240 154 C
ATOM 1418 CG1 ILE A 196 -4.443 9.291 34.677 1.00 30.09 C
ANISOU 1418 CG1 ILE A 196 3454 3826 4152 507 299 190 C
ATOM 1419 CG2 ILE A 196 -4.459 11.651 33.897 1.00 30.69 C
ANISOU 1419 CG2 ILE A 196 3612 3894 4152 541 357 131 C
ATOM 1420 CD1 ILE A 196 -2.939 9.254 34.808 1.00 29.51 C
ANISOU 1420 CD1 ILE A 196 3439 3825 3949 513 395 176 C
ATOM 1421 N VAL A 197 -7.064 10.417 31.089 1.00 41.65 N
ANISOU 1421 N VAL A 197 5131 4977 5717 631 -59 116 N
ATOM 1422 CA VAL A 197 -7.474 11.166 29.904 1.00 39.16 C
ANISOU 1422 CA VAL A 197 4912 4589 5380 680 -133 85 C
ATOM 1423 C VAL A 197 -8.956 11.511 29.972 1.00 38.39 C
ANISOU 1423 C VAL A 197 4736 4437 5414 672 -207 92 C
ATOM 1424 O VAL A 197 -9.353 12.655 29.727 1.00 41.18 O
ANISOU 1424 O VAL A 197 5102 4778 5769 684 -197 77 O
ATOM 1425 CB VAL A 197 -7.141 10.378 28.626 1.00 32.51 C
ANISOU 1425 CB VAL A 197 4199 3676 4480 733 -240 63 C
ATOM 1426 CG1 VAL A 197 -7.664 11.110 27.413 1.00 33.00 C
ANISOU 1426 CG1 VAL A 197 4354 3661 4522 786 -325 35 C
ATOM 1427 CG2 VAL A 197 -5.645 10.168 28.515 1.00 46.27 C
ANISOU 1427 CG2 VAL A 197 6021 5472 6085 744 -160 52 C
ATOM 1428 N VAL A 198 -9.799 10.530 30.301 1.00 45.80 N
ANISOU 1428 N VAL A 198 5593 5339 6468 650 -284 114 N
ATOM 1429 CA VAL A 198 -11.239 10.781 30.319 1.00 54.75 C
ANISOU 1429 CA VAL A 198 6653 6415 7734 643 -364 118 C
ATOM 1430 C VAL A 198 -11.592 11.783 31.407 1.00 44.74 C
ANISOU 1430 C VAL A 198 5273 5214 6512 599 -259 131 C
ATOM 1431 O VAL A 198 -12.482 12.624 31.231 1.00 54.00 O
ANISOU 1431 O VAL A 198 6421 6351 7744 605 -291 119 O
ATOM 1432 CB VAL A 198 -12.021 9.465 30.486 1.00 34.09 C
ANISOU 1432 CB VAL A 198 3967 3747 5238 626 -462 139 C
ATOM 1433 CG1 VAL A 198 -11.766 8.556 29.309 1.00 40.23 C
ANISOU 1433 CG1 VAL A 198 4858 4451 5978 675 -577 117 C
ATOM 1434 CG2 VAL A 198 -11.641 8.782 31.784 1.00 65.23 C
ANISOU 1434 CG2 VAL A 198 7806 7770 9210 571 -371 180 C
ATOM 1435 N ALA A 199 -10.899 11.719 32.545 1.00 32.74 N
ANISOU 1435 N ALA A 199 3683 3793 4964 555 -134 153 N
ATOM 1436 CA ALA A 199 -11.152 12.678 33.612 1.00 50.89 C
ANISOU 1436 CA ALA A 199 5874 6165 7298 514 -28 161 C
ATOM 1437 C ALA A 199 -10.787 14.088 33.170 1.00 63.33 C
ANISOU 1437 C ALA A 199 7517 7750 8796 539 27 128 C
ATOM 1438 O ALA A 199 -11.502 15.050 33.478 1.00 64.82 O
ANISOU 1438 O ALA A 199 7643 7941 9043 527 48 121 O
ATOM 1439 CB ALA A 199 -10.380 12.281 34.866 1.00 54.12 C
ANISOU 1439 CB ALA A 199 6203 6681 7678 468 94 189 C
ATOM 1440 N SER A 200 -9.691 14.226 32.417 1.00 61.60 N
ANISOU 1440 N SER A 200 7424 7533 8447 576 48 107 N
ATOM 1441 CA SER A 200 -9.293 15.539 31.919 1.00 41.58 C
ANISOU 1441 CA SER A 200 4962 5001 5836 603 100 78 C
ATOM 1442 C SER A 200 -10.342 16.101 30.972 1.00 39.47 C
ANISOU 1442 C SER A 200 4735 4638 5623 640 -10 63 C
ATOM 1443 O SER A 200 -10.839 17.216 31.170 1.00 53.91 O
ANISOU 1443 O SER A 200 6524 6471 7490 634 23 54 O
ATOM 1444 CB SER A 200 -7.931 15.456 31.225 1.00 31.48 C
ANISOU 1444 CB SER A 200 3815 3735 4409 637 136 61 C
ATOM 1445 OG SER A 200 -6.952 14.874 32.068 1.00 44.06 O
ANISOU 1445 OG SER A 200 5373 5415 5952 605 230 74 O
ATOM 1446 N TYR A 201 -10.704 15.336 29.942 1.00 32.94 N
ANISOU 1446 N TYR A 201 3985 3725 4805 679 -143 59 N
ATOM 1447 CA TYR A 201 -11.633 15.855 28.945 1.00 49.09 C
ANISOU 1447 CA TYR A 201 6081 5679 6890 722 -254 42 C
ATOM 1448 C TYR A 201 -13.061 15.959 29.465 1.00 48.10 C
ANISOU 1448 C TYR A 201 5834 5524 6920 695 -307 52 C
ATOM 1449 O TYR A 201 -13.841 16.746 28.923 1.00 47.72 O
ANISOU 1449 O TYR A 201 5800 5419 6911 720 -364 38 O
ATOM 1450 CB TYR A 201 -11.577 15.002 27.673 1.00 34.02 C
ANISOU 1450 CB TYR A 201 4293 3693 4942 776 -383 29 C
ATOM 1451 CG TYR A 201 -10.491 15.445 26.701 1.00 40.72 C
ANISOU 1451 CG TYR A 201 5293 4541 5639 824 -357 9 C
ATOM 1452 CD1 TYR A 201 -10.675 16.557 25.889 1.00 47.43 C
ANISOU 1452 CD1 TYR A 201 6220 5352 6451 866 -374 -6 C
ATOM 1453 CD2 TYR A 201 -9.287 14.757 26.599 1.00 52.71 C
ANISOU 1453 CD2 TYR A 201 6877 6097 7053 829 -314 7 C
ATOM 1454 CE1 TYR A 201 -9.696 16.974 25.008 1.00 68.12 C
ANISOU 1454 CE1 TYR A 201 8976 7972 8934 910 -346 -21 C
ATOM 1455 CE2 TYR A 201 -8.304 15.166 25.718 1.00 69.00 C
ANISOU 1455 CE2 TYR A 201 9076 8161 8981 873 -287 -11 C
ATOM 1456 CZ TYR A 201 -8.514 16.276 24.923 1.00 75.95 C
ANISOU 1456 CZ TYR A 201 10029 9002 9824 913 -302 -24 C
ATOM 1457 OH TYR A 201 -7.541 16.694 24.038 1.00 64.46 O
ANISOU 1457 OH TYR A 201 8711 7548 8234 956 -272 -39 O
ATOM 1458 N SER A 202 -13.423 15.204 30.505 1.00 64.71 N
ANISOU 1458 N SER A 202 7814 7663 9111 644 -288 77 N
ATOM 1459 CA SER A 202 -14.744 15.392 31.098 1.00 60.61 C
ANISOU 1459 CA SER A 202 7169 7124 8737 614 -322 86 C
ATOM 1460 C SER A 202 -14.825 16.733 31.806 1.00 59.19 C
ANISOU 1460 C SER A 202 6923 7001 8566 589 -214 80 C
ATOM 1461 O SER A 202 -15.840 17.431 31.714 1.00 73.26 O
ANISOU 1461 O SER A 202 8662 8741 10432 593 -257 70 O
ATOM 1462 CB SER A 202 -15.074 14.262 32.071 1.00 53.08 C
ANISOU 1462 CB SER A 202 6097 6197 7872 564 -320 119 C
ATOM 1463 OG SER A 202 -14.179 14.253 33.170 1.00 68.19 O
ANISOU 1463 OG SER A 202 7955 8220 9734 522 -179 138 O
ATOM 1464 N ASP A 203 -13.757 17.112 32.509 1.00 55.04 N
ANISOU 1464 N ASP A 203 6387 6570 7954 565 -75 82 N
ATOM 1465 CA ASP A 203 -13.733 18.401 33.187 1.00 49.56 C
ANISOU 1465 CA ASP A 203 5632 5935 7264 543 34 70 C
ATOM 1466 C ASP A 203 -13.647 19.544 32.183 1.00 38.91 C
ANISOU 1466 C ASP A 203 4388 4536 5861 591 17 43 C
ATOM 1467 O ASP A 203 -14.258 20.599 32.381 1.00 59.86 O
ANISOU 1467 O ASP A 203 6990 7183 8569 585 38 30 O
ATOM 1468 CB ASP A 203 -12.564 18.446 34.166 1.00 55.76 C
ANISOU 1468 CB ASP A 203 6383 6834 7969 508 183 76 C
ATOM 1469 CG ASP A 203 -12.871 19.265 35.399 1.00 81.26 C
ANISOU 1469 CG ASP A 203 9477 10142 11256 461 289 74 C
ATOM 1470 OD1 ASP A 203 -13.718 18.832 36.214 1.00 92.87 O
ANISOU 1470 OD1 ASP A 203 10825 11629 12833 422 276 94 O
ATOM 1471 OD2 ASP A 203 -12.254 20.341 35.551 1.00 64.26 O
ANISOU 1471 OD2 ASP A 203 7339 8035 9042 462 386 51 O
ATOM 1472 N ILE A 204 -12.905 19.345 31.092 1.00 50.82 N
ANISOU 1472 N ILE A 204 6041 6006 7263 639 -22 34 N
ATOM 1473 CA ILE A 204 -12.834 20.360 30.044 1.00 33.39 C
ANISOU 1473 CA ILE A 204 3941 3745 4999 689 -46 13 C
ATOM 1474 C ILE A 204 -14.207 20.570 29.417 1.00 41.55 C
ANISOU 1474 C ILE A 204 4966 4684 6135 715 -176 9 C
ATOM 1475 O ILE A 204 -14.614 21.705 29.141 1.00 59.83 O
ANISOU 1475 O ILE A 204 7290 6972 8469 732 -173 -4 O
ATOM 1476 CB ILE A 204 -11.780 19.967 28.991 1.00 41.88 C
ANISOU 1476 CB ILE A 204 5173 4800 5939 736 -67 7 C
ATOM 1477 CG1 ILE A 204 -10.370 20.010 29.600 1.00 35.84 C
ANISOU 1477 CG1 ILE A 204 4418 4129 5070 713 75 6 C
ATOM 1478 CG2 ILE A 204 -11.863 20.887 27.783 1.00 47.05 C
ANISOU 1478 CG2 ILE A 204 5945 5387 6544 795 -115 -8 C
ATOM 1479 CD1 ILE A 204 -9.334 19.281 28.782 1.00 43.72 C
ANISOU 1479 CD1 ILE A 204 5546 5119 5948 748 55 2 C
ATOM 1480 N GLY A 205 -14.949 19.478 29.193 1.00 44.42 N
ANISOU 1480 N GLY A 205 5310 4995 6571 718 -294 17 N
ATOM 1481 CA GLY A 205 -16.294 19.569 28.649 1.00 47.33 C
ANISOU 1481 CA GLY A 205 5660 5275 7046 741 -424 10 C
ATOM 1482 C GLY A 205 -17.346 19.968 29.656 1.00 53.36 C
ANISOU 1482 C GLY A 205 6270 6056 7950 694 -402 15 C
ATOM 1483 O GLY A 205 -18.366 20.548 29.270 1.00 62.08 O
ANISOU 1483 O GLY A 205 7358 7098 9132 714 -477 3 O
ATOM 1484 N ARG A 206 -17.110 19.696 30.939 1.00 48.41 N
ANISOU 1484 N ARG A 206 5529 5514 7351 635 -300 31 N
ATOM 1485 CA ARG A 206 -18.019 20.120 31.991 1.00 39.37 C
ANISOU 1485 CA ARG A 206 4232 4398 6328 587 -262 35 C
ATOM 1486 C ARG A 206 -17.906 21.605 32.290 1.00 39.54 C
ANISOU 1486 C ARG A 206 4232 4455 6335 583 -168 16 C
ATOM 1487 O ARG A 206 -18.770 22.141 32.983 1.00 51.97 O
ANISOU 1487 O ARG A 206 5691 6041 8015 553 -150 12 O
ATOM 1488 CB ARG A 206 -17.758 19.296 33.256 1.00 51.07 C
ANISOU 1488 CB ARG A 206 5603 5965 7837 528 -183 61 C
ATOM 1489 CG ARG A 206 -18.831 19.405 34.327 1.00 51.37 C
ANISOU 1489 CG ARG A 206 5477 6028 8014 478 -165 70 C
ATOM 1490 CD ARG A 206 -19.084 18.072 34.992 1.00 55.88 C
ANISOU 1490 CD ARG A 206 5966 6616 8649 440 -184 103 C
ATOM 1491 NE ARG A 206 -20.086 18.227 36.034 1.00 88.58 N
ANISOU 1491 NE ARG A 206 9950 10786 12919 392 -158 113 N
ATOM 1492 CZ ARG A 206 -21.390 18.329 35.803 1.00 86.91 C
ANISOU 1492 CZ ARG A 206 9687 10502 12834 395 -254 105 C
ATOM 1493 NH1 ARG A 206 -21.860 18.282 34.563 1.00 84.90 N
ANISOU 1493 NH1 ARG A 206 9524 10142 12593 446 -386 86 N
ATOM 1494 NH2 ARG A 206 -22.223 18.482 36.816 1.00 89.24 N
ANISOU 1494 NH2 ARG A 206 9835 10832 13240 349 -217 114 N
ATOM 1495 N ARG A 207 -16.871 22.277 31.787 1.00 56.30 N
ANISOU 1495 N ARG A 207 6462 6595 8335 612 -107 5 N
ATOM 1496 CA ARG A 207 -16.745 23.723 31.923 1.00 43.32 C
ANISOU 1496 CA ARG A 207 4811 4972 6679 614 -25 -15 C
ATOM 1497 C ARG A 207 -17.468 24.455 30.799 1.00 44.32 C
ANISOU 1497 C ARG A 207 5011 4998 6830 667 -126 -28 C
ATOM 1498 O ARG A 207 -18.207 25.413 31.049 1.00 63.65 O
ANISOU 1498 O ARG A 207 7392 7433 9358 660 -117 -40 O
ATOM 1499 CB ARG A 207 -15.267 24.125 31.950 1.00 49.35 C
ANISOU 1499 CB ARG A 207 5648 5799 7302 618 96 -21 C
ATOM 1500 CG ARG A 207 -14.485 23.631 33.161 1.00 58.78 C
ANISOU 1500 CG ARG A 207 6763 7104 8468 566 214 -12 C
ATOM 1501 CD ARG A 207 -12.995 23.878 32.978 1.00 52.01 C
ANISOU 1501 CD ARG A 207 5998 6297 7466 579 313 -20 C
ATOM 1502 NE ARG A 207 -12.492 24.900 33.888 1.00 43.74 N
ANISOU 1502 NE ARG A 207 4881 5333 6406 547 456 -39 N
ATOM 1503 CZ ARG A 207 -11.841 24.636 35.015 1.00 54.69 C
ANISOU 1503 CZ ARG A 207 6187 6823 7769 503 566 -38 C
ATOM 1504 NH1 ARG A 207 -11.608 23.377 35.368 1.00 41.97 N
ANISOU 1504 NH1 ARG A 207 4558 5243 6146 485 549 -14 N
ATOM 1505 NH2 ARG A 207 -11.417 25.630 35.786 1.00 60.62 N
ANISOU 1505 NH2 ARG A 207 6876 7647 8510 478 691 -61 N
ATOM 1506 N LEU A 208 -17.265 24.007 29.557 1.00 43.77 N
ANISOU 1506 N LEU A 208 5077 4860 6693 722 -224 -26 N
ATOM 1507 CA LEU A 208 -17.913 24.627 28.407 1.00 42.23 C
ANISOU 1507 CA LEU A 208 4964 4571 6511 779 -329 -35 C
ATOM 1508 C LEU A 208 -19.415 24.387 28.384 1.00 55.18 C
ANISOU 1508 C LEU A 208 6524 6145 8296 778 -449 -39 C
ATOM 1509 O LEU A 208 -20.141 25.162 27.752 1.00 57.21 O
ANISOU 1509 O LEU A 208 6806 6337 8595 813 -516 -49 O
ATOM 1510 CB LEU A 208 -17.284 24.101 27.115 1.00 49.91 C
ANISOU 1510 CB LEU A 208 6100 5496 7368 838 -404 -33 C
ATOM 1511 CG LEU A 208 -15.789 24.346 26.906 1.00 56.61 C
ANISOU 1511 CG LEU A 208 7049 6395 8065 849 -299 -31 C
ATOM 1512 CD1 LEU A 208 -15.152 23.158 26.201 1.00 50.63 C
ANISOU 1512 CD1 LEU A 208 6393 5623 7219 877 -359 -27 C
ATOM 1513 CD2 LEU A 208 -15.556 25.631 26.114 1.00 52.51 C
ANISOU 1513 CD2 LEU A 208 6624 5842 7487 894 -279 -37 C
ATOM 1514 N GLN A 209 -19.895 23.345 29.060 1.00 70.33 N
ANISOU 1514 N GLN A 209 7893 8829 10002 1220 722 1426 N
ATOM 1515 CA GLN A 209 -21.312 23.022 29.023 1.00 50.33 C
ANISOU 1515 CA GLN A 209 5436 6184 7504 1170 695 1331 C
ATOM 1516 C GLN A 209 -22.125 24.180 29.588 1.00 48.72 C
ANISOU 1516 C GLN A 209 5197 6051 7263 1064 599 1258 C
ATOM 1517 O GLN A 209 -21.612 25.041 30.310 1.00 58.15 O
ANISOU 1517 O GLN A 209 6301 7382 8409 1030 558 1296 O
ATOM 1518 CB GLN A 209 -21.593 21.726 29.796 1.00 62.90 C
ANISOU 1518 CB GLN A 209 7024 7725 9151 1209 749 1405 C
ATOM 1519 CG GLN A 209 -21.340 21.789 31.297 1.00 65.27 C
ANISOU 1519 CG GLN A 209 7207 8162 9432 1198 736 1508 C
ATOM 1520 CD GLN A 209 -22.517 22.337 32.061 1.00 60.67 C
ANISOU 1520 CD GLN A 209 6606 7604 8839 1104 661 1444 C
ATOM 1521 OE1 GLN A 209 -23.628 21.813 31.973 1.00112.84 O
ANISOU 1521 OE1 GLN A 209 13276 14103 15494 1077 661 1388 O
ATOM 1522 NE2 GLN A 209 -22.287 23.411 32.803 1.00 67.74 N
ANISOU 1522 NE2 GLN A 209 7418 8645 9673 1052 597 1452 N
ATOM 1523 N ALA A 210 -23.410 24.195 29.242 1.00 49.73 N
ANISOU 1523 N ALA A 210 5398 6084 7413 1011 563 1151 N
ATOM 1524 CA ALA A 210 -24.324 25.220 29.729 1.00 61.31 C
ANISOU 1524 CA ALA A 210 6843 7603 8849 918 479 1077 C
ATOM 1525 C ALA A 210 -25.740 24.687 29.603 1.00 49.16 C
ANISOU 1525 C ALA A 210 5370 5951 7357 881 465 1002 C
ATOM 1526 O ALA A 210 -26.104 24.137 28.559 1.00 50.35 O
ANISOU 1526 O ALA A 210 5612 5976 7542 900 486 941 O
ATOM 1527 CB ALA A 210 -24.168 26.536 28.951 1.00 75.15 C
ANISOU 1527 CB ALA A 210 8613 9390 10551 880 428 999 C
ATOM 1528 N ARG A 211 -26.524 24.834 30.669 1.00 61.63 N
ANISOU 1528 N ARG A 211 6903 7577 8938 830 429 1007 N
ATOM 1529 CA ARG A 211 -27.927 24.453 30.623 1.00 45.75 C
ANISOU 1529 CA ARG A 211 4939 5473 6971 785 408 939 C
ATOM 1530 C ARG A 211 -28.647 25.247 29.540 1.00 48.34 C
ANISOU 1530 C ARG A 211 5336 5751 7281 738 353 809 C
ATOM 1531 O ARG A 211 -28.292 26.388 29.237 1.00 74.02 O
ANISOU 1531 O ARG A 211 8579 9070 10476 720 315 773 O
ATOM 1532 CB ARG A 211 -28.587 24.699 31.983 1.00 48.82 C
ANISOU 1532 CB ARG A 211 5255 5944 7349 739 376 971 C
ATOM 1533 CG ARG A 211 -29.981 24.117 32.113 1.00 77.00 C
ANISOU 1533 CG ARG A 211 8854 9425 10976 699 368 930 C
ATOM 1534 CD ARG A 211 -30.800 24.825 33.185 1.00 87.66 C
ANISOU 1534 CD ARG A 211 10146 10865 12296 643 318 925 C
ATOM 1535 NE ARG A 211 -31.248 26.154 32.767 1.00 63.22 N
ANISOU 1535 NE ARG A 211 7065 7808 9146 591 248 826 N
ATOM 1536 CZ ARG A 211 -30.740 27.295 33.224 1.00 65.03 C
ANISOU 1536 CZ ARG A 211 7251 8154 9303 576 210 828 C
ATOM 1537 NH1 ARG A 211 -29.765 27.278 34.122 1.00 76.28 N
ANISOU 1537 NH1 ARG A 211 8607 9679 10695 605 229 920 N
ATOM 1538 NH2 ARG A 211 -31.212 28.456 32.790 1.00 35.45 N
ANISOU 1538 NH2 ARG A 211 3529 4425 5515 531 154 737 N
ATOM 1539 N ARG A 212 -29.664 24.630 28.947 1.00 51.03 N
ANISOU 1539 N ARG A 212 5746 5973 7671 719 350 741 N
ATOM 1540 CA ARG A 212 -30.466 25.318 27.944 1.00 50.79 C
ANISOU 1540 CA ARG A 212 5777 5897 7622 676 295 620 C
ATOM 1541 C ARG A 212 -31.235 26.469 28.585 1.00 39.03 C
ANISOU 1541 C ARG A 212 4241 4497 6093 610 227 583 C
ATOM 1542 O ARG A 212 -31.735 26.350 29.706 1.00 57.66 O
ANISOU 1542 O ARG A 212 6542 6901 8466 583 220 625 O
ATOM 1543 CB ARG A 212 -31.424 24.336 27.278 1.00 48.99 C
ANISOU 1543 CB ARG A 212 5626 5530 7458 662 301 559 C
ATOM 1544 CG ARG A 212 -31.764 24.681 25.848 1.00 59.80 C
ANISOU 1544 CG ARG A 212 7083 6832 8808 656 269 447 C
ATOM 1545 CD ARG A 212 -31.866 23.430 24.996 1.00 44.98 C
ANISOU 1545 CD ARG A 212 5294 4811 6984 686 310 418 C
ATOM 1546 NE ARG A 212 -32.290 23.745 23.637 1.00 86.24 N
ANISOU 1546 NE ARG A 212 10607 9977 12185 677 273 304 N
ATOM 1547 CZ ARG A 212 -32.398 22.851 22.662 1.00 87.33 C
ANISOU 1547 CZ ARG A 212 10839 9991 12351 701 295 252 C
ATOM 1548 NH1 ARG A 212 -32.109 21.577 22.894 1.00 83.89 N
ANISOU 1548 NH1 ARG A 212 10427 9469 11976 734 360 304 N
ATOM 1549 NH2 ARG A 212 -32.794 23.231 21.455 1.00103.74 N
ANISOU 1549 NH2 ARG A 212 12991 12031 14394 694 254 148 N
ATOM 1550 N ALA A1002 -31.315 27.592 27.874 1.00 50.98 N
ANISOU 1550 N ALA A1002 5780 6035 7556 589 181 507 N
ATOM 1551 CA ALA A1002 -31.955 28.783 28.419 1.00 36.26 C
ANISOU 1551 CA ALA A1002 3878 4252 5647 534 121 471 C
ATOM 1552 C ALA A1002 -33.470 28.622 28.480 1.00 52.83 C
ANISOU 1552 C ALA A1002 5991 6303 7777 486 85 412 C
ATOM 1553 O ALA A1002 -34.084 28.004 27.603 1.00 68.95 O
ANISOU 1553 O ALA A1002 8093 8245 9858 482 84 357 O
ATOM 1554 CB ALA A1002 -31.604 30.005 27.577 1.00 38.32 C
ANISOU 1554 CB ALA A1002 4169 4542 5850 530 90 411 C
ATOM 1555 N LYS A1003 -34.077 29.193 29.518 1.00 39.51 N
ANISOU 1555 N LYS A1003 4248 4693 6071 448 56 425 N
ATOM 1556 CA LYS A1003 -35.519 29.133 29.722 1.00 33.49 C
ANISOU 1556 CA LYS A1003 3483 3906 5337 403 23 383 C
ATOM 1557 C LYS A1003 -36.110 30.535 29.666 1.00 39.72 C
ANISOU 1557 C LYS A1003 4271 4755 6066 371 -33 318 C
ATOM 1558 O LYS A1003 -35.614 31.452 30.329 1.00 54.45 O
ANISOU 1558 O LYS A1003 6100 6711 7875 369 -43 340 O
ATOM 1559 CB LYS A1003 -35.860 28.462 31.057 1.00 47.78 C
ANISOU 1559 CB LYS A1003 5228 5746 7180 396 47 463 C
ATOM 1560 CG LYS A1003 -36.086 26.964 30.941 1.00 51.24 C
ANISOU 1560 CG LYS A1003 5682 6083 7703 406 91 497 C
ATOM 1561 CD LYS A1003 -36.295 26.294 32.295 1.00 56.10 C
ANISOU 1561 CD LYS A1003 6230 6734 8352 407 125 593 C
ATOM 1562 CE LYS A1003 -34.975 26.028 33.004 1.00 79.73 C
ANISOU 1562 CE LYS A1003 9183 9787 11322 460 172 692 C
ATOM 1563 NZ LYS A1003 -34.740 26.960 34.140 1.00 81.95 N
ANISOU 1563 NZ LYS A1003 9397 10207 11532 456 150 730 N
ATOM 1564 N ALA A1004 -37.173 30.692 28.884 1.00 27.53 N
ANISOU 1564 N ALA A1004 2766 3160 4535 345 -68 239 N
ATOM 1565 CA ALA A1004 -37.839 31.972 28.712 1.00 26.50 C
ANISOU 1565 CA ALA A1004 2640 3076 4352 322 -117 177 C
ATOM 1566 C ALA A1004 -39.337 31.807 28.925 1.00 39.86 C
ANISOU 1566 C ALA A1004 4314 4754 6076 285 -146 150 C
ATOM 1567 O ALA A1004 -39.917 30.767 28.604 1.00 46.65 O
ANISOU 1567 O ALA A1004 5185 5541 7000 271 -141 143 O
ATOM 1568 CB ALA A1004 -37.569 32.566 27.324 1.00 45.31 C
ANISOU 1568 CB ALA A1004 5090 5422 6702 337 -136 104 C
ATOM 1569 N LEU A1005 -39.955 32.850 29.473 1.00 42.68 N
ANISOU 1569 N LEU A1005 4645 5183 6389 269 -174 135 N
ATOM 1570 CA LEU A1005 -41.380 32.872 29.766 1.00 28.59 C
ANISOU 1570 CA LEU A1005 2832 3405 4626 239 -200 117 C
ATOM 1571 C LEU A1005 -42.029 34.002 28.985 1.00 28.30 C
ANISOU 1571 C LEU A1005 2827 3381 4543 235 -244 40 C
ATOM 1572 O LEU A1005 -41.531 35.133 28.991 1.00 28.18 O
ANISOU 1572 O LEU A1005 2829 3415 4464 250 -251 23 O
ATOM 1573 CB LEU A1005 -41.632 33.054 31.266 1.00 41.41 C
ANISOU 1573 CB LEU A1005 4389 5109 6237 235 -186 182 C
ATOM 1574 CG LEU A1005 -43.085 33.247 31.708 1.00 31.12 C
ANISOU 1574 CG LEU A1005 3047 3830 4945 211 -206 175 C
ATOM 1575 CD1 LEU A1005 -43.895 31.988 31.471 1.00 38.89 C
ANISOU 1575 CD1 LEU A1005 4015 4744 6019 184 -202 186 C
ATOM 1576 CD2 LEU A1005 -43.157 33.663 33.170 1.00 46.10 C
ANISOU 1576 CD2 LEU A1005 4891 5819 6806 220 -189 234 C
ATOM 1577 N ILE A1006 -43.138 33.696 28.321 1.00 33.25 N
ANISOU 1577 N ILE A1006 3462 3967 5204 213 -274 -5 N
ATOM 1578 CA ILE A1006 -43.883 34.665 27.529 1.00 35.14 C
ANISOU 1578 CA ILE A1006 3728 4220 5403 213 -317 -75 C
ATOM 1579 C ILE A1006 -45.319 34.631 28.031 1.00 39.46 C
ANISOU 1579 C ILE A1006 4221 4796 5976 186 -338 -69 C
ATOM 1580 O ILE A1006 -46.092 33.741 27.661 1.00 43.75 O
ANISOU 1580 O ILE A1006 4752 5292 6581 156 -354 -80 O
ATOM 1581 CB ILE A1006 -43.813 34.373 26.027 1.00 33.87 C
ANISOU 1581 CB ILE A1006 3631 3989 5249 218 -339 -141 C
ATOM 1582 CG1 ILE A1006 -42.366 34.417 25.547 1.00 36.34 C
ANISOU 1582 CG1 ILE A1006 3993 4278 5535 252 -310 -137 C
ATOM 1583 CG2 ILE A1006 -44.637 35.380 25.246 1.00 28.95 C
ANISOU 1583 CG2 ILE A1006 3028 3390 4581 223 -383 -204 C
ATOM 1584 CD1 ILE A1006 -42.232 34.181 24.073 1.00 46.06 C
ANISOU 1584 CD1 ILE A1006 5293 5445 6762 267 -326 -200 C
ATOM 1585 N VAL A1007 -45.678 35.590 28.877 1.00 40.58 N
ANISOU 1585 N VAL A1007 4332 5015 6074 196 -337 -50 N
ATOM 1586 CA VAL A1007 -47.048 35.761 29.346 1.00 36.80 C
ANISOU 1586 CA VAL A1007 3801 4576 5607 181 -354 -42 C
ATOM 1587 C VAL A1007 -47.672 36.891 28.547 1.00 33.05 C
ANISOU 1587 C VAL A1007 3353 4123 5080 198 -390 -103 C
ATOM 1588 O VAL A1007 -47.165 38.018 28.557 1.00 39.90 O
ANISOU 1588 O VAL A1007 4256 5024 5881 227 -385 -121 O
ATOM 1589 CB VAL A1007 -47.097 36.059 30.851 1.00 25.91 C
ANISOU 1589 CB VAL A1007 2371 3269 4207 192 -322 23 C
ATOM 1590 CG1 VAL A1007 -48.522 36.372 31.276 1.00 24.98 C
ANISOU 1590 CG1 VAL A1007 2201 3198 4093 187 -335 33 C
ATOM 1591 CG2 VAL A1007 -46.536 34.882 31.642 1.00 30.35 C
ANISOU 1591 CG2 VAL A1007 2899 3812 4820 180 -285 93 C
ATOM 1592 N TYR A1008 -48.772 36.598 27.858 1.00 36.69 N
ANISOU 1592 N TYR A1008 3799 4568 5574 178 -426 -134 N
ATOM 1593 CA TYR A1008 -49.439 37.572 27.010 1.00 33.83 C
ANISOU 1593 CA TYR A1008 3459 4229 5165 198 -462 -189 C
ATOM 1594 C TYR A1008 -50.874 37.787 27.469 1.00 40.25 C
ANISOU 1594 C TYR A1008 4205 5097 5990 191 -478 -169 C
ATOM 1595 O TYR A1008 -51.505 36.894 28.042 1.00 38.48 O
ANISOU 1595 O TYR A1008 3918 4872 5829 156 -474 -127 O
ATOM 1596 CB TYR A1008 -49.428 37.132 25.538 1.00 37.96 C
ANISOU 1596 CB TYR A1008 4029 4691 5701 188 -500 -252 C
ATOM 1597 CG TYR A1008 -50.091 35.798 25.278 1.00 42.04 C
ANISOU 1597 CG TYR A1008 4514 5160 6299 137 -523 -254 C
ATOM 1598 CD1 TYR A1008 -49.375 34.616 25.389 1.00 55.26 C
ANISOU 1598 CD1 TYR A1008 6201 6766 8029 113 -499 -236 C
ATOM 1599 CD2 TYR A1008 -51.430 35.721 24.906 1.00 46.21 C
ANISOU 1599 CD2 TYR A1008 4999 5709 6849 111 -568 -274 C
ATOM 1600 CE1 TYR A1008 -49.973 33.390 25.149 1.00 62.45 C
ANISOU 1600 CE1 TYR A1008 7090 7620 9018 62 -518 -241 C
ATOM 1601 CE2 TYR A1008 -52.037 34.499 24.665 1.00 57.33 C
ANISOU 1601 CE2 TYR A1008 6377 7069 8336 54 -593 -279 C
ATOM 1602 CZ TYR A1008 -51.302 33.337 24.789 1.00 56.30 C
ANISOU 1602 CZ TYR A1008 6269 6861 8263 28 -567 -265 C
ATOM 1603 OH TYR A1008 -51.891 32.117 24.551 1.00 59.14 O
ANISOU 1603 OH TYR A1008 6606 7160 8704 -33 -589 -273 O
ATOM 1604 N GLY A1009 -51.380 38.989 27.211 1.00 31.18 N
ANISOU 1604 N GLY A1009 3069 3997 4781 227 -491 -194 N
ATOM 1605 CA GLY A1009 -52.779 39.295 27.428 1.00 42.57 C
ANISOU 1605 CA GLY A1009 4450 5496 6228 230 -508 -178 C
ATOM 1606 C GLY A1009 -53.418 39.848 26.171 1.00 41.19 C
ANISOU 1606 C GLY A1009 4298 5329 6025 247 -554 -234 C
ATOM 1607 O GLY A1009 -53.214 41.017 25.831 1.00 53.74 O
ANISOU 1607 O GLY A1009 5934 6939 7544 296 -549 -259 O
ATOM 1608 N SER A1010 -54.181 39.022 25.462 1.00 26.15 N
ANISOU 1608 N SER A1010 2359 3406 4171 207 -599 -254 N
ATOM 1609 CA SER A1010 -54.760 39.420 24.188 1.00 47.88 C
ANISOU 1609 CA SER A1010 5130 6169 6894 221 -651 -309 C
ATOM 1610 C SER A1010 -56.267 39.211 24.212 1.00 65.76 C
ANISOU 1610 C SER A1010 7306 8488 9193 198 -687 -290 C
ATOM 1611 O SER A1010 -56.757 38.200 24.725 1.00 74.10 O
ANISOU 1611 O SER A1010 8296 9533 10324 143 -691 -256 O
ATOM 1612 CB SER A1010 -54.137 38.640 23.027 1.00 52.38 C
ANISOU 1612 CB SER A1010 5758 6665 7481 194 -682 -367 C
ATOM 1613 OG SER A1010 -54.429 39.263 21.790 1.00 54.04 O
ANISOU 1613 OG SER A1010 6006 6890 7637 225 -724 -423 O
ATOM 1614 N THR A1011 -56.992 40.183 23.660 1.00 50.85 N
ANISOU 1614 N THR A1011 5413 6658 7251 242 -711 -306 N
ATOM 1615 CA THR A1011 -58.437 40.114 23.495 1.00 42.44 C
ANISOU 1615 CA THR A1011 4261 5657 6208 229 -752 -290 C
ATOM 1616 C THR A1011 -58.842 39.794 22.065 1.00 42.76 C
ANISOU 1616 C THR A1011 4313 5689 6246 206 -826 -353 C
ATOM 1617 O THR A1011 -59.786 39.027 21.849 1.00 61.68 O
ANISOU 1617 O THR A1011 6636 8101 8698 150 -875 -352 O
ATOM 1618 CB THR A1011 -59.086 41.437 23.921 1.00 44.82 C
ANISOU 1618 CB THR A1011 4540 6041 6448 302 -726 -255 C
ATOM 1619 OG1 THR A1011 -58.772 41.707 25.292 1.00 42.14 O
ANISOU 1619 OG1 THR A1011 4192 5712 6106 322 -661 -200 O
ATOM 1620 CG2 THR A1011 -60.600 41.364 23.763 1.00 64.51 C
ANISOU 1620 CG2 THR A1011 6934 8612 8966 293 -767 -229 C
ATOM 1621 N THR A1012 -58.145 40.367 21.082 1.00 57.31 N
ANISOU 1621 N THR A1012 6244 7508 8024 248 -836 -408 N
ATOM 1622 CA THR A1012 -58.431 40.123 19.674 1.00 53.64 C
ANISOU 1622 CA THR A1012 5802 7038 7540 237 -904 -473 C
ATOM 1623 C THR A1012 -57.430 39.186 19.006 1.00 66.40 C
ANISOU 1623 C THR A1012 7492 8559 9176 200 -917 -529 C
ATOM 1624 O THR A1012 -57.616 38.848 17.833 1.00 58.92 O
ANISOU 1624 O THR A1012 6573 7601 8214 186 -975 -589 O
ATOM 1625 CB THR A1012 -58.470 41.445 18.895 1.00 43.66 C
ANISOU 1625 CB THR A1012 4584 5821 6182 322 -908 -493 C
ATOM 1626 OG1 THR A1012 -57.176 42.060 18.925 1.00 68.47 O
ANISOU 1626 OG1 THR A1012 7820 8916 9279 367 -854 -502 O
ATOM 1627 CG2 THR A1012 -59.498 42.398 19.493 1.00 42.24 C
ANISOU 1627 CG2 THR A1012 4336 5734 5978 369 -892 -438 C
ATOM 1628 N GLY A1013 -56.375 38.771 19.707 1.00 62.35 N
ANISOU 1628 N GLY A1013 7014 7982 8692 187 -863 -509 N
ATOM 1629 CA GLY A1013 -55.416 37.839 19.154 1.00 64.97 C
ANISOU 1629 CA GLY A1013 7415 8224 9047 158 -865 -553 C
ATOM 1630 C GLY A1013 -54.197 38.456 18.501 1.00 76.35 C
ANISOU 1630 C GLY A1013 8957 9634 10420 217 -838 -584 C
ATOM 1631 O GLY A1013 -53.348 37.711 17.992 1.00 72.93 O
ANISOU 1631 O GLY A1013 8584 9126 10000 203 -834 -618 O
ATOM 1632 N ASN A1014 -54.078 39.787 18.493 1.00 87.25 N
ANISOU 1632 N ASN A1014 10357 11063 11730 284 -814 -571 N
ATOM 1633 CA ASN A1014 -52.901 40.421 17.906 1.00 67.09 C
ANISOU 1633 CA ASN A1014 7894 8479 9116 337 -783 -593 C
ATOM 1634 C ASN A1014 -51.670 40.205 18.781 1.00 52.13 C
ANISOU 1634 C ASN A1014 6024 6537 7246 329 -721 -558 C
ATOM 1635 O ASN A1014 -50.611 39.795 18.290 1.00 53.67 O
ANISOU 1635 O ASN A1014 6281 6674 7438 334 -704 -579 O
ATOM 1636 CB ASN A1014 -53.154 41.915 17.690 1.00 61.54 C
ANISOU 1636 CB ASN A1014 7207 7836 8339 406 -771 -585 C
ATOM 1637 CG ASN A1014 -54.369 42.189 16.816 1.00 62.86 C
ANISOU 1637 CG ASN A1014 7346 8063 8476 424 -832 -612 C
ATOM 1638 OD1 ASN A1014 -55.255 42.958 17.191 1.00 95.44 O
ANISOU 1638 OD1 ASN A1014 11423 12257 12583 451 -832 -581 O
ATOM 1639 ND2 ASN A1014 -54.413 41.564 15.644 1.00 72.41 N
ANISOU 1639 ND2 ASN A1014 8588 9250 9676 412 -883 -668 N
ATOM 1640 N THR A1015 -51.789 40.489 20.083 1.00 53.66 N
ANISOU 1640 N THR A1015 6168 6762 7460 322 -685 -502 N
ATOM 1641 CA THR A1015 -50.687 40.229 21.007 1.00 70.07 C
ANISOU 1641 CA THR A1015 8257 8806 9559 311 -632 -465 C
ATOM 1642 C THR A1015 -50.377 38.739 21.092 1.00 54.30 C
ANISOU 1642 C THR A1015 6250 6747 7634 259 -635 -463 C
ATOM 1643 O THR A1015 -49.213 38.352 21.245 1.00 38.06 O
ANISOU 1643 O THR A1015 4230 4645 5587 261 -599 -451 O
ATOM 1644 CB THR A1015 -51.020 40.796 22.392 1.00 55.08 C
ANISOU 1644 CB THR A1015 6305 6961 7662 315 -599 -409 C
ATOM 1645 OG1 THR A1015 -51.198 42.215 22.295 1.00 67.47 O
ANISOU 1645 OG1 THR A1015 7898 8574 9162 368 -589 -414 O
ATOM 1646 CG2 THR A1015 -49.907 40.500 23.402 1.00 24.45 C
ANISOU 1646 CG2 THR A1015 2430 3058 3800 302 -550 -368 C
ATOM 1647 N GLU A1016 -51.399 37.889 20.975 1.00 51.64 N
ANISOU 1647 N GLU A1016 5865 6407 7350 213 -675 -472 N
ATOM 1648 CA GLU A1016 -51.152 36.454 20.967 1.00 32.99 C
ANISOU 1648 CA GLU A1016 3502 3973 5059 162 -677 -475 C
ATOM 1649 C GLU A1016 -50.327 36.038 19.757 1.00 44.50 C
ANISOU 1649 C GLU A1016 5047 5364 6498 176 -687 -533 C
ATOM 1650 O GLU A1016 -49.519 35.108 19.851 1.00 57.73 O
ANISOU 1650 O GLU A1016 6751 6972 8213 161 -659 -526 O
ATOM 1651 CB GLU A1016 -52.477 35.702 21.005 1.00 41.23 C
ANISOU 1651 CB GLU A1016 4477 5025 6165 104 -723 -478 C
ATOM 1652 CG GLU A1016 -52.329 34.200 21.052 1.00 51.86 C
ANISOU 1652 CG GLU A1016 5822 6288 7594 44 -724 -480 C
ATOM 1653 CD GLU A1016 -53.643 33.508 21.318 1.00 56.50 C
ANISOU 1653 CD GLU A1016 6328 6887 8252 -23 -762 -468 C
ATOM 1654 OE1 GLU A1016 -53.620 32.321 21.703 1.00 51.81 O
ANISOU 1654 OE1 GLU A1016 5717 6229 7740 -76 -750 -448 O
ATOM 1655 OE2 GLU A1016 -54.699 34.156 21.151 1.00 79.60 O
ANISOU 1655 OE2 GLU A1016 9203 9886 11155 -21 -802 -473 O
ATOM 1656 N TYR A1017 -50.499 36.719 18.621 1.00 52.83 N
ANISOU 1656 N TYR A1017 6146 6438 7489 212 -721 -587 N
ATOM 1657 CA TYR A1017 -49.661 36.433 17.459 1.00 48.20 C
ANISOU 1657 CA TYR A1017 5648 5795 6872 238 -724 -639 C
ATOM 1658 C TYR A1017 -48.214 36.835 17.711 1.00 54.43 C
ANISOU 1658 C TYR A1017 6483 6564 7633 282 -659 -607 C
ATOM 1659 O TYR A1017 -47.290 36.074 17.400 1.00 62.25 O
ANISOU 1659 O TYR A1017 7522 7489 8640 286 -634 -615 O
ATOM 1660 CB TYR A1017 -50.206 37.147 16.220 1.00 47.78 C
ANISOU 1660 CB TYR A1017 5628 5779 6749 274 -773 -696 C
ATOM 1661 CG TYR A1017 -49.433 36.858 14.946 1.00 42.35 C
ANISOU 1661 CG TYR A1017 5033 5039 6020 307 -778 -752 C
ATOM 1662 CD1 TYR A1017 -49.715 35.732 14.181 1.00 64.58 C
ANISOU 1662 CD1 TYR A1017 7878 7799 8860 272 -821 -810 C
ATOM 1663 CD2 TYR A1017 -48.428 37.712 14.506 1.00 40.23 C
ANISOU 1663 CD2 TYR A1017 4825 4774 5688 374 -738 -746 C
ATOM 1664 CE1 TYR A1017 -49.014 35.462 13.016 1.00 71.40 C
ANISOU 1664 CE1 TYR A1017 8835 8617 9679 309 -822 -864 C
ATOM 1665 CE2 TYR A1017 -47.721 37.449 13.344 1.00 54.90 C
ANISOU 1665 CE2 TYR A1017 6767 6588 7505 411 -736 -792 C
ATOM 1666 CZ TYR A1017 -48.018 36.323 12.602 1.00 69.39 C
ANISOU 1666 CZ TYR A1017 8635 8372 9359 383 -777 -851 C
ATOM 1667 OH TYR A1017 -47.318 36.057 11.445 1.00 74.14 O
ANISOU 1667 OH TYR A1017 9327 8930 9913 427 -773 -898 O
ATOM 1668 N THR A1018 -47.996 38.028 18.275 1.00 55.00 N
ANISOU 1668 N THR A1018 6542 6692 7665 315 -631 -572 N
ATOM 1669 CA THR A1018 -46.634 38.481 18.547 1.00 56.42 C
ANISOU 1669 CA THR A1018 6758 6860 7821 347 -575 -540 C
ATOM 1670 C THR A1018 -45.957 37.600 19.588 1.00 43.26 C
ANISOU 1670 C THR A1018 5062 5162 6212 317 -535 -489 C
ATOM 1671 O THR A1018 -44.751 37.341 19.505 1.00 45.09 O
ANISOU 1671 O THR A1018 5331 5359 6443 335 -496 -473 O
ATOM 1672 CB THR A1018 -46.639 39.937 19.015 1.00 55.76 C
ANISOU 1672 CB THR A1018 6665 6837 7686 378 -557 -516 C
ATOM 1673 OG1 THR A1018 -47.487 40.070 20.161 1.00 68.28 O
ANISOU 1673 OG1 THR A1018 8179 8468 9297 351 -560 -482 O
ATOM 1674 CG2 THR A1018 -47.139 40.849 17.916 1.00 55.26 C
ANISOU 1674 CG2 THR A1018 6637 6799 7560 421 -585 -559 C
ATOM 1675 N ALA A1019 -46.715 37.140 20.586 1.00 52.94 N
ANISOU 1675 N ALA A1019 6220 6406 7489 275 -541 -457 N
ATOM 1676 CA ALA A1019 -46.146 36.246 21.587 1.00 40.13 C
ANISOU 1676 CA ALA A1019 4567 4757 5923 250 -502 -402 C
ATOM 1677 C ALA A1019 -45.723 34.925 20.960 1.00 45.27 C
ANISOU 1677 C ALA A1019 5257 5325 6620 236 -499 -422 C
ATOM 1678 O ALA A1019 -44.666 34.381 21.296 1.00 62.78 O
ANISOU 1678 O ALA A1019 7489 7508 8857 246 -454 -386 O
ATOM 1679 CB ALA A1019 -47.150 36.012 22.716 1.00 34.94 C
ANISOU 1679 CB ALA A1019 3829 4138 5310 211 -508 -361 C
ATOM 1680 N GLU A1020 -46.528 34.402 20.035 1.00 36.88 N
ANISOU 1680 N GLU A1020 4214 4228 5572 215 -546 -481 N
ATOM 1681 CA GLU A1020 -46.207 33.122 19.418 1.00 42.58 C
ANISOU 1681 CA GLU A1020 4982 4860 6337 200 -545 -509 C
ATOM 1682 C GLU A1020 -45.077 33.239 18.406 1.00 43.93 C
ANISOU 1682 C GLU A1020 5239 4994 6458 254 -523 -540 C
ATOM 1683 O GLU A1020 -44.366 32.258 18.166 1.00 53.55 O
ANISOU 1683 O GLU A1020 6500 6139 7707 260 -493 -540 O
ATOM 1684 CB GLU A1020 -47.451 32.535 18.757 1.00 51.52 C
ANISOU 1684 CB GLU A1020 6108 5969 7499 152 -609 -569 C
ATOM 1685 CG GLU A1020 -48.506 32.093 19.752 1.00 63.51 C
ANISOU 1685 CG GLU A1020 7538 7507 9087 91 -622 -530 C
ATOM 1686 CD GLU A1020 -49.824 31.748 19.092 1.00 79.14 C
ANISOU 1686 CD GLU A1020 9497 9484 11088 41 -694 -586 C
ATOM 1687 OE1 GLU A1020 -49.972 32.013 17.878 1.00 84.84 O
ANISOU 1687 OE1 GLU A1020 10272 10204 11758 58 -739 -658 O
ATOM 1688 OE2 GLU A1020 -50.713 31.213 19.789 1.00 71.95 O
ANISOU 1688 OE2 GLU A1020 8514 8578 10246 -17 -707 -556 O
ATOM 1689 N THR A1021 -44.895 34.414 17.804 1.00 46.43 N
ANISOU 1689 N THR A1021 5584 5359 6700 299 -532 -561 N
ATOM 1690 CA THR A1021 -43.796 34.577 16.859 1.00 42.88 C
ANISOU 1690 CA THR A1021 5211 4879 6202 355 -504 -581 C
ATOM 1691 C THR A1021 -42.466 34.758 17.580 1.00 45.57 C
ANISOU 1691 C THR A1021 5545 5226 6545 381 -438 -512 C
ATOM 1692 O THR A1021 -41.445 34.215 17.144 1.00 56.61 O
ANISOU 1692 O THR A1021 6990 6575 7942 413 -400 -505 O
ATOM 1693 CB THR A1021 -44.067 35.752 15.919 1.00 28.39 C
ANISOU 1693 CB THR A1021 3409 3091 4288 395 -533 -623 C
ATOM 1694 OG1 THR A1021 -44.443 36.900 16.684 1.00 57.43 O
ANISOU 1694 OG1 THR A1021 7033 6842 7946 392 -534 -589 O
ATOM 1695 CG2 THR A1021 -45.188 35.406 14.947 1.00 36.99 C
ANISOU 1695 CG2 THR A1021 4518 4169 5366 378 -601 -697 C
ATOM 1696 N ILE A1022 -42.451 35.509 18.685 1.00 36.98 N
ANISOU 1696 N ILE A1022 4397 4200 5454 369 -424 -460 N
ATOM 1697 CA ILE A1022 -41.220 35.597 19.457 1.00 42.83 C
ANISOU 1697 CA ILE A1022 5121 4952 6200 384 -369 -394 C
ATOM 1698 C ILE A1022 -40.961 34.303 20.210 1.00 45.47 C
ANISOU 1698 C ILE A1022 5428 5246 6603 360 -341 -349 C
ATOM 1699 O ILE A1022 -39.810 34.009 20.550 1.00 67.03 O
ANISOU 1699 O ILE A1022 8159 7968 9342 382 -292 -298 O
ATOM 1700 CB ILE A1022 -41.230 36.793 20.427 1.00 37.47 C
ANISOU 1700 CB ILE A1022 4394 4350 5492 376 -364 -357 C
ATOM 1701 CG1 ILE A1022 -42.301 36.630 21.498 1.00 63.14 C
ANISOU 1701 CG1 ILE A1022 7578 7634 8779 333 -384 -338 C
ATOM 1702 CG2 ILE A1022 -41.452 38.089 19.685 1.00 39.74 C
ANISOU 1702 CG2 ILE A1022 4714 4670 5714 404 -384 -396 C
ATOM 1703 CD1 ILE A1022 -42.321 37.785 22.471 1.00 69.51 C
ANISOU 1703 CD1 ILE A1022 8347 8513 9551 331 -377 -307 C
ATOM 1704 N ALA A1023 -42.001 33.511 20.475 1.00 34.28 N
ANISOU 1704 N ALA A1023 3983 3803 5238 317 -368 -362 N
ATOM 1705 CA ALA A1023 -41.783 32.186 21.044 1.00 39.60 C
ANISOU 1705 CA ALA A1023 4642 4422 5983 297 -337 -322 C
ATOM 1706 C ALA A1023 -41.122 31.259 20.031 1.00 51.14 C
ANISOU 1706 C ALA A1023 6180 5795 7456 326 -316 -352 C
ATOM 1707 O ALA A1023 -40.263 30.447 20.393 1.00 65.70 O
ANISOU 1707 O ALA A1023 8029 7600 9335 343 -265 -302 O
ATOM 1708 CB ALA A1023 -43.106 31.596 21.533 1.00 47.74 C
ANISOU 1708 CB ALA A1023 5624 5443 7072 239 -370 -328 C
ATOM 1709 N ARG A1024 -41.503 31.370 18.756 1.00 46.81 N
ANISOU 1709 N ARG A1024 5693 5217 6874 337 -354 -431 N
ATOM 1710 CA ARG A1024 -40.841 30.582 17.723 1.00 53.77 C
ANISOU 1710 CA ARG A1024 6659 6018 7753 373 -333 -466 C
ATOM 1711 C ARG A1024 -39.443 31.110 17.425 1.00 66.23 C
ANISOU 1711 C ARG A1024 8269 7616 9281 441 -281 -432 C
ATOM 1712 O ARG A1024 -38.541 30.321 17.123 1.00 80.85 O
ANISOU 1712 O ARG A1024 10165 9408 11146 479 -233 -415 O
ATOM 1713 CB ARG A1024 -41.688 30.561 16.451 1.00 61.20 C
ANISOU 1713 CB ARG A1024 7659 6931 8664 366 -393 -564 C
ATOM 1714 CG ARG A1024 -42.965 29.743 16.570 1.00 79.73 C
ANISOU 1714 CG ARG A1024 9984 9240 11071 295 -443 -602 C
ATOM 1715 CD ARG A1024 -42.674 28.253 16.484 1.00 99.23 C
ANISOU 1715 CD ARG A1024 12498 11599 13606 283 -413 -607 C
ATOM 1716 NE ARG A1024 -43.780 27.445 16.991 1.00109.74 N
ANISOU 1716 NE ARG A1024 13786 12895 15016 204 -446 -615 N
ATOM 1717 CZ ARG A1024 -43.878 27.023 18.248 1.00116.66 C
ANISOU 1717 CZ ARG A1024 14591 13774 15961 171 -415 -538 C
ATOM 1718 NH1 ARG A1024 -42.933 27.332 19.128 1.00108.13 N
ANISOU 1718 NH1 ARG A1024 13475 12734 14874 210 -354 -453 N
ATOM 1719 NH2 ARG A1024 -44.917 26.290 18.627 1.00 93.58 N
ANISOU 1719 NH2 ARG A1024 11628 10816 13111 98 -444 -544 N
ATOM 1720 N GLU A1025 -39.237 32.430 17.505 1.00 49.87 N
ANISOU 1720 N GLU A1025 6174 5622 7153 457 -287 -419 N
ATOM 1721 CA GLU A1025 -37.903 32.982 17.278 1.00 39.79 C
ANISOU 1721 CA GLU A1025 4917 4367 5836 513 -238 -380 C
ATOM 1722 C GLU A1025 -36.934 32.518 18.357 1.00 53.60 C
ANISOU 1722 C GLU A1025 6617 6125 7624 516 -182 -291 C
ATOM 1723 O GLU A1025 -35.807 32.104 18.060 1.00 69.04 O
ANISOU 1723 O GLU A1025 8601 8055 9578 563 -131 -256 O
ATOM 1724 CB GLU A1025 -37.956 34.511 17.228 1.00 26.99 C
ANISOU 1724 CB GLU A1025 3277 2822 4154 519 -256 -383 C
ATOM 1725 CG GLU A1025 -36.802 35.169 16.454 1.00 59.35 C
ANISOU 1725 CG GLU A1025 7418 6931 8201 578 -218 -370 C
ATOM 1726 CD GLU A1025 -35.467 35.150 17.198 1.00 72.57 C
ANISOU 1726 CD GLU A1025 9055 8629 9890 592 -160 -285 C
ATOM 1727 OE1 GLU A1025 -35.477 35.102 18.446 1.00 75.74 O
ANISOU 1727 OE1 GLU A1025 9388 9065 10324 554 -158 -236 O
ATOM 1728 OE2 GLU A1025 -34.406 35.188 16.531 1.00 37.45 O
ANISOU 1728 OE2 GLU A1025 4641 4170 5419 644 -118 -264 O
ATOM 1729 N LEU A1026 -37.356 32.585 19.621 1.00 41.18 N
ANISOU 1729 N LEU A1026 4970 4595 6083 470 -191 -249 N
ATOM 1730 CA LEU A1026 -36.487 32.157 20.712 1.00 43.51 C
ANISOU 1730 CA LEU A1026 5213 4910 6410 474 -143 -161 C
ATOM 1731 C LEU A1026 -36.203 30.663 20.631 1.00 48.07 C
ANISOU 1731 C LEU A1026 5816 5404 7044 490 -105 -141 C
ATOM 1732 O LEU A1026 -35.058 30.226 20.798 1.00 58.47 O
ANISOU 1732 O LEU A1026 7132 6715 8369 531 -49 -80 O
ATOM 1733 CB LEU A1026 -37.121 32.503 22.058 1.00 38.31 C
ANISOU 1733 CB LEU A1026 4475 4315 5767 426 -162 -126 C
ATOM 1734 CG LEU A1026 -37.367 33.968 22.416 1.00 28.65 C
ANISOU 1734 CG LEU A1026 3221 3174 4490 410 -192 -135 C
ATOM 1735 CD1 LEU A1026 -38.299 34.023 23.602 1.00 41.68 C
ANISOU 1735 CD1 LEU A1026 4807 4866 6162 365 -213 -114 C
ATOM 1736 CD2 LEU A1026 -36.077 34.687 22.733 1.00 25.39 C
ANISOU 1736 CD2 LEU A1026 2791 2815 4041 432 -160 -84 C
ATOM 1737 N ALA A1027 -37.240 29.863 20.368 1.00 53.86 N
ANISOU 1737 N ALA A1027 6572 6071 7819 457 -133 -191 N
ATOM 1738 CA ALA A1027 -37.087 28.412 20.401 1.00 48.30 C
ANISOU 1738 CA ALA A1027 5896 5278 7180 463 -96 -172 C
ATOM 1739 C ALA A1027 -36.117 27.928 19.329 1.00 49.27 C
ANISOU 1739 C ALA A1027 6101 5336 7283 529 -53 -188 C
ATOM 1740 O ALA A1027 -35.335 26.999 19.566 1.00 64.15 O
ANISOU 1740 O ALA A1027 7997 7174 9204 564 7 -132 O
ATOM 1741 CB ALA A1027 -38.449 27.740 20.240 1.00 31.56 C
ANISOU 1741 CB ALA A1027 3786 3097 5108 405 -141 -232 C
ATOM 1742 N ASP A1028 -36.149 28.548 18.145 1.00 57.89 N
ANISOU 1742 N ASP A1028 7253 6427 8316 554 -80 -257 N
ATOM 1743 CA ASP A1028 -35.217 28.184 17.082 1.00 51.73 C
ANISOU 1743 CA ASP A1028 6555 5594 7506 625 -36 -271 C
ATOM 1744 C ASP A1028 -33.773 28.497 17.449 1.00 58.77 C
ANISOU 1744 C ASP A1028 7415 6536 8379 681 29 -180 C
ATOM 1745 O ASP A1028 -32.855 27.951 16.828 1.00 63.79 O
ANISOU 1745 O ASP A1028 8104 7126 9007 747 84 -163 O
ATOM 1746 CB ASP A1028 -35.583 28.904 15.782 1.00 55.16 C
ANISOU 1746 CB ASP A1028 7054 6032 7873 643 -79 -359 C
ATOM 1747 CG ASP A1028 -36.941 28.492 15.244 1.00 75.87 C
ANISOU 1747 CG ASP A1028 9714 8604 10508 593 -146 -454 C
ATOM 1748 OD1 ASP A1028 -37.635 27.695 15.911 1.00 74.30 O
ANISOU 1748 OD1 ASP A1028 9487 8366 10377 537 -159 -450 O
ATOM 1749 OD2 ASP A1028 -37.315 28.966 14.149 1.00 85.11 O
ANISOU 1749 OD2 ASP A1028 10941 9777 11621 608 -185 -529 O
ATOM 1750 N ALA A1029 -33.551 29.366 18.436 1.00 53.41 N
ANISOU 1750 N ALA A1029 6651 5952 7692 657 23 -121 N
ATOM 1751 CA ALA A1029 -32.215 29.702 18.899 1.00 34.15 C
ANISOU 1751 CA ALA A1029 4167 3573 5238 696 75 -32 C
ATOM 1752 C ALA A1029 -31.823 28.928 20.153 1.00 35.42 C
ANISOU 1752 C ALA A1029 4262 3745 5452 690 113 58 C
ATOM 1753 O ALA A1029 -30.937 29.366 20.895 1.00 52.62 O
ANISOU 1753 O ALA A1029 6373 6001 7618 699 137 137 O
ATOM 1754 CB ALA A1029 -32.108 31.207 19.144 1.00 46.24 C
ANISOU 1754 CB ALA A1029 5650 5201 6718 673 45 -26 C
ATOM 1755 N GLY A1030 -32.464 27.791 20.405 1.00 40.98 N
ANISOU 1755 N GLY A1030 4981 4374 6214 672 118 49 N
ATOM 1756 CA GLY A1030 -32.086 26.946 21.521 1.00 45.41 C
ANISOU 1756 CA GLY A1030 5488 4937 6829 676 162 140 C
ATOM 1757 C GLY A1030 -32.631 27.378 22.863 1.00 53.97 C
ANISOU 1757 C GLY A1030 6481 6101 7925 617 131 179 C
ATOM 1758 O GLY A1030 -31.934 27.261 23.879 1.00 69.19 O
ANISOU 1758 O GLY A1030 8342 8087 9861 630 165 271 O
ATOM 1759 N TYR A1031 -33.857 27.885 22.898 1.00 58.51 N
ANISOU 1759 N TYR A1031 7050 6684 8496 558 69 114 N
ATOM 1760 CA TYR A1031 -34.521 28.262 24.135 1.00 49.69 C
ANISOU 1760 CA TYR A1031 5854 5637 7390 506 41 144 C
ATOM 1761 C TYR A1031 -35.614 27.255 24.465 1.00 55.73 C
ANISOU 1761 C TYR A1031 6618 6334 8224 466 33 134 C
ATOM 1762 O TYR A1031 -36.108 26.531 23.597 1.00 56.30 O
ANISOU 1762 O TYR A1031 6755 6308 8327 461 27 74 O
ATOM 1763 CB TYR A1031 -35.137 29.662 24.034 1.00 39.93 C
ANISOU 1763 CB TYR A1031 4604 4470 6098 471 -19 88 C
ATOM 1764 CG TYR A1031 -34.219 30.814 24.390 1.00 39.78 C
ANISOU 1764 CG TYR A1031 4548 4547 6020 484 -16 124 C
ATOM 1765 CD1 TYR A1031 -33.197 31.207 23.538 1.00 31.65 C
ANISOU 1765 CD1 TYR A1031 3554 3518 4953 528 5 122 C
ATOM 1766 CD2 TYR A1031 -34.407 31.536 25.562 1.00 37.71 C
ANISOU 1766 CD2 TYR A1031 4216 4373 5737 451 -36 157 C
ATOM 1767 CE1 TYR A1031 -32.374 32.270 23.854 1.00 47.16 C
ANISOU 1767 CE1 TYR A1031 5482 5567 6871 530 6 154 C
ATOM 1768 CE2 TYR A1031 -33.591 32.602 25.885 1.00 25.67 C
ANISOU 1768 CE2 TYR A1031 2662 2931 4161 454 -38 182 C
ATOM 1769 CZ TYR A1031 -32.576 32.965 25.027 1.00 27.00 C
ANISOU 1769 CZ TYR A1031 2863 3096 4301 489 -18 181 C
ATOM 1770 OH TYR A1031 -31.755 34.024 25.342 1.00 46.57 O
ANISOU 1770 OH TYR A1031 5308 5652 6733 483 -22 207 O
ATOM 1771 N GLU A1032 -35.987 27.223 25.738 1.00 53.42 N
ANISOU 1771 N GLU A1032 6249 6094 7953 436 33 192 N
ATOM 1772 CA GLU A1032 -37.129 26.453 26.219 1.00 36.01 C
ANISOU 1772 CA GLU A1032 4024 3844 5814 389 23 192 C
ATOM 1773 C GLU A1032 -38.208 27.473 26.575 1.00 42.20 C
ANISOU 1773 C GLU A1032 4767 4700 6569 339 -38 154 C
ATOM 1774 O GLU A1032 -38.291 27.953 27.705 1.00 54.52 O
ANISOU 1774 O GLU A1032 6258 6346 8113 329 -38 207 O
ATOM 1775 CB GLU A1032 -36.751 25.566 27.404 1.00 34.88 C
ANISOU 1775 CB GLU A1032 3827 3706 5719 403 78 298 C
ATOM 1776 CG GLU A1032 -35.800 24.440 27.039 1.00 40.40 C
ANISOU 1776 CG GLU A1032 4572 4323 6455 457 145 339 C
ATOM 1777 CD GLU A1032 -35.520 23.493 28.190 1.00 51.29 C
ANISOU 1777 CD GLU A1032 5899 5701 7887 474 203 449 C
ATOM 1778 OE1 GLU A1032 -35.621 23.917 29.360 1.00 60.07 O
ANISOU 1778 OE1 GLU A1032 6931 6910 8981 462 198 510 O
ATOM 1779 OE2 GLU A1032 -35.203 22.316 27.923 1.00 66.46 O
ANISOU 1779 OE2 GLU A1032 7864 7523 9865 504 257 475 O
ATOM 1780 N VAL A1033 -39.028 27.802 25.594 1.00 41.65 N
ANISOU 1780 N VAL A1033 4740 4597 6489 314 -87 62 N
ATOM 1781 CA VAL A1033 -40.022 28.858 25.729 1.00 43.21 C
ANISOU 1781 CA VAL A1033 4907 4861 6652 278 -143 20 C
ATOM 1782 C VAL A1033 -41.261 28.310 26.424 1.00 34.90 C
ANISOU 1782 C VAL A1033 3803 3798 5660 226 -158 36 C
ATOM 1783 O VAL A1033 -41.661 27.160 26.210 1.00 38.22 O
ANISOU 1783 O VAL A1033 4241 4131 6151 203 -148 32 O
ATOM 1784 CB VAL A1033 -40.352 29.447 24.345 1.00 40.13 C
ANISOU 1784 CB VAL A1033 4581 4446 6220 280 -189 -77 C
ATOM 1785 CG1 VAL A1033 -41.250 30.665 24.471 1.00 35.90 C
ANISOU 1785 CG1 VAL A1033 4014 3986 5639 257 -240 -112 C
ATOM 1786 CG2 VAL A1033 -39.063 29.808 23.618 1.00 42.11 C
ANISOU 1786 CG2 VAL A1033 4884 4695 6421 336 -163 -82 C
ATOM 1787 N ASP A1034 -41.870 29.138 27.272 1.00 51.24 N
ANISOU 1787 N ASP A1034 5811 5956 7702 208 -179 55 N
ATOM 1788 CA ASP A1034 -43.099 28.796 27.988 1.00 51.72 C
ANISOU 1788 CA ASP A1034 5814 6026 7813 163 -192 77 C
ATOM 1789 C ASP A1034 -44.116 29.900 27.696 1.00 56.95 C
ANISOU 1789 C ASP A1034 6463 6744 8431 143 -249 18 C
ATOM 1790 O ASP A1034 -44.053 30.979 28.293 1.00 59.40 O
ANISOU 1790 O ASP A1034 6746 7143 8682 160 -253 33 O
ATOM 1791 CB ASP A1034 -42.829 28.650 29.486 1.00 43.53 C
ANISOU 1791 CB ASP A1034 4707 5050 6783 173 -150 176 C
ATOM 1792 CG ASP A1034 -43.918 27.871 30.214 1.00 61.73 C
ANISOU 1792 CG ASP A1034 6955 7340 9161 133 -142 219 C
ATOM 1793 OD1 ASP A1034 -45.111 28.055 29.895 1.00 81.23 O
ANISOU 1793 OD1 ASP A1034 9409 9806 11647 93 -184 174 O
ATOM 1794 OD2 ASP A1034 -43.577 27.071 31.114 1.00 67.82 O
ANISOU 1794 OD2 ASP A1034 7692 8104 9973 142 -92 303 O
ATOM 1795 N SER A1035 -45.044 29.633 26.774 1.00 64.32 N
ANISOU 1795 N SER A1035 7418 7627 9392 110 -292 -48 N
ATOM 1796 CA SER A1035 -46.046 30.606 26.345 1.00 62.94 C
ANISOU 1796 CA SER A1035 7233 7503 9178 96 -347 -104 C
ATOM 1797 C SER A1035 -47.344 30.368 27.111 1.00 61.76 C
ANISOU 1797 C SER A1035 7006 7383 9078 52 -360 -71 C
ATOM 1798 O SER A1035 -47.926 29.279 27.032 1.00 63.72 O
ANISOU 1798 O SER A1035 7239 7567 9405 8 -364 -67 O
ATOM 1799 CB SER A1035 -46.284 30.514 24.835 1.00 63.02 C
ANISOU 1799 CB SER A1035 7310 7455 9180 89 -392 -195 C
ATOM 1800 OG SER A1035 -47.197 31.503 24.381 1.00 73.52 O
ANISOU 1800 OG SER A1035 8629 8841 10465 85 -444 -244 O
ATOM 1801 N ARG A1036 -47.798 31.388 27.843 1.00 28.81 N
ANISOU 1801 N ARG A1036 2786 3303 4859 66 -365 -48 N
ATOM 1802 CA ARG A1036 -48.972 31.294 28.701 1.00 37.59 C
ANISOU 1802 CA ARG A1036 3817 4459 6007 37 -368 -4 C
ATOM 1803 C ARG A1036 -49.872 32.504 28.512 1.00 48.92 C
ANISOU 1803 C ARG A1036 5233 5968 7385 47 -407 -39 C
ATOM 1804 O ARG A1036 -49.393 33.639 28.439 1.00 45.81 O
ANISOU 1804 O ARG A1036 4871 5622 6912 89 -407 -60 O
ATOM 1805 CB ARG A1036 -48.589 31.205 30.181 1.00 29.68 C
ANISOU 1805 CB ARG A1036 2765 3507 5005 55 -314 88 C
ATOM 1806 CG ARG A1036 -47.686 30.049 30.533 1.00 33.25 C
ANISOU 1806 CG ARG A1036 3227 3897 5509 55 -266 140 C
ATOM 1807 CD ARG A1036 -47.445 29.977 32.034 1.00 35.37 C
ANISOU 1807 CD ARG A1036 3438 4228 5773 76 -217 235 C
ATOM 1808 NE ARG A1036 -46.232 29.224 32.344 1.00 77.17 N
ANISOU 1808 NE ARG A1036 8751 9487 11084 98 -170 285 N
ATOM 1809 CZ ARG A1036 -45.770 29.025 33.574 1.00 56.02 C
ANISOU 1809 CZ ARG A1036 6030 6858 8397 123 -124 371 C
ATOM 1810 NH1 ARG A1036 -46.424 29.522 34.614 1.00 54.88 N
ANISOU 1810 NH1 ARG A1036 5827 6799 8227 128 -118 415 N
ATOM 1811 NH2 ARG A1036 -44.654 28.333 33.763 1.00 35.97 N
ANISOU 1811 NH2 ARG A1036 3507 4289 5872 148 -83 418 N
ATOM 1812 N ASP A1037 -51.178 32.256 28.458 1.00 53.08 N
ANISOU 1812 N ASP A1037 5705 6506 7957 9 -437 -39 N
ATOM 1813 CA ASP A1037 -52.152 33.335 28.471 1.00 29.73 C
ANISOU 1813 CA ASP A1037 2714 3630 4953 25 -465 -53 C
ATOM 1814 C ASP A1037 -52.281 33.872 29.887 1.00 40.16 C
ANISOU 1814 C ASP A1037 3982 5029 6246 54 -422 21 C
ATOM 1815 O ASP A1037 -52.307 33.104 30.851 1.00 53.71 O
ANISOU 1815 O ASP A1037 5650 6743 8013 38 -385 90 O
ATOM 1816 CB ASP A1037 -53.505 32.842 27.966 1.00 44.72 C
ANISOU 1816 CB ASP A1037 4560 5521 6910 -27 -512 -70 C
ATOM 1817 CG ASP A1037 -54.379 33.963 27.453 1.00 64.08 C
ANISOU 1817 CG ASP A1037 7000 8044 9305 -4 -554 -107 C
ATOM 1818 OD1 ASP A1037 -54.647 34.914 28.220 1.00 65.26 O
ANISOU 1818 OD1 ASP A1037 7120 8272 9405 38 -531 -71 O
ATOM 1819 OD2 ASP A1037 -54.784 33.899 26.272 1.00 71.28 O
ANISOU 1819 OD2 ASP A1037 7933 8932 10217 -24 -609 -173 O
ATOM 1820 N ALA A1038 -52.357 35.198 30.013 1.00 42.33 N
ANISOU 1820 N ALA A1038 4271 5374 6440 100 -425 5 N
ATOM 1821 CA ALA A1038 -52.389 35.823 31.330 1.00 26.32 C
ANISOU 1821 CA ALA A1038 2210 3421 4370 135 -384 63 C
ATOM 1822 C ALA A1038 -53.625 35.450 32.142 1.00 48.14 C
ANISOU 1822 C ALA A1038 4882 6229 7180 119 -372 126 C
ATOM 1823 O ALA A1038 -53.663 35.739 33.344 1.00 46.16 O
ANISOU 1823 O ALA A1038 4599 6037 6902 148 -331 185 O
ATOM 1824 CB ALA A1038 -52.305 37.344 31.186 1.00 40.11 C
ANISOU 1824 CB ALA A1038 3999 5219 6021 186 -391 24 C
ATOM 1825 N ALA A1039 -54.630 34.824 31.529 1.00 38.85 N
ANISOU 1825 N ALA A1039 3661 5029 6070 75 -406 117 N
ATOM 1826 CA ALA A1039 -55.840 34.431 32.242 1.00 50.34 C
ANISOU 1826 CA ALA A1039 5021 6527 7579 54 -395 183 C
ATOM 1827 C ALA A1039 -55.718 33.072 32.918 1.00 60.19 C
ANISOU 1827 C ALA A1039 6225 7728 8915 11 -361 250 C
ATOM 1828 O ALA A1039 -56.662 32.644 33.592 1.00 77.05 O
ANISOU 1828 O ALA A1039 8276 9895 11104 -9 -344 316 O
ATOM 1829 CB ALA A1039 -57.034 34.419 31.285 1.00 56.58 C
ANISOU 1829 CB ALA A1039 5773 7323 8402 20 -452 146 C
ATOM 1830 N SER A1040 -54.583 32.391 32.757 1.00 56.76 N
ANISOU 1830 N SER A1040 5846 7221 8501 0 -347 239 N
ATOM 1831 CA SER A1040 -54.358 31.066 33.320 1.00 54.52 C
ANISOU 1831 CA SER A1040 5532 6881 8302 -36 -309 303 C
ATOM 1832 C SER A1040 -53.058 31.017 34.116 1.00 60.88 C
ANISOU 1832 C SER A1040 6372 7690 9069 6 -258 343 C
ATOM 1833 O SER A1040 -52.392 29.978 34.170 1.00 62.55 O
ANISOU 1833 O SER A1040 6599 7832 9336 -12 -232 370 O
ATOM 1834 CB SER A1040 -54.351 30.006 32.218 1.00 53.64 C
ANISOU 1834 CB SER A1040 5450 6661 8272 -98 -343 254 C
ATOM 1835 OG SER A1040 -53.318 30.246 31.274 1.00 56.56 O
ANISOU 1835 OG SER A1040 5912 6982 8594 -80 -363 178 O
ATOM 1836 N VAL A1041 -52.676 32.132 34.735 1.00 41.86 N
ANISOU 1836 N VAL A1041 3977 5361 6564 63 -243 348 N
ATOM 1837 CA VAL A1041 -51.424 32.221 35.473 1.00 36.42 C
ANISOU 1837 CA VAL A1041 3320 4691 5828 101 -204 380 C
ATOM 1838 C VAL A1041 -51.685 32.821 36.848 1.00 66.78 C
ANISOU 1838 C VAL A1041 7120 8636 9616 143 -168 445 C
ATOM 1839 O VAL A1041 -52.561 33.675 37.026 1.00 70.97 O
ANISOU 1839 O VAL A1041 7629 9229 10108 162 -178 435 O
ATOM 1840 CB VAL A1041 -50.364 33.050 34.714 1.00 39.89 C
ANISOU 1840 CB VAL A1041 3843 5120 6194 125 -229 305 C
ATOM 1841 CG1 VAL A1041 -49.970 32.359 33.424 1.00 62.95 C
ANISOU 1841 CG1 VAL A1041 6813 7942 9164 93 -255 249 C
ATOM 1842 CG2 VAL A1041 -50.883 34.457 34.427 1.00 53.96 C
ANISOU 1842 CG2 VAL A1041 5643 6960 7899 151 -259 251 C
ATOM 1843 N GLU A1042 -50.913 32.359 37.829 1.00 70.61 N
ANISOU 1843 N GLU A1042 7594 9139 10094 164 -124 512 N
ATOM 1844 CA GLU A1042 -50.926 32.904 39.179 1.00 38.59 C
ANISOU 1844 CA GLU A1042 3510 5182 5971 210 -88 570 C
ATOM 1845 C GLU A1042 -49.633 33.673 39.421 1.00 46.82 C
ANISOU 1845 C GLU A1042 4610 6259 6919 244 -91 542 C
ATOM 1846 O GLU A1042 -48.548 33.212 39.056 1.00 66.48 O
ANISOU 1846 O GLU A1042 7134 8703 9422 236 -90 535 O
ATOM 1847 CB GLU A1042 -51.085 31.795 40.223 1.00 39.26 C
ANISOU 1847 CB GLU A1042 3529 5275 6114 210 -35 678 C
ATOM 1848 N ALA A1043 -49.759 34.852 40.037 1.00 57.91 N
ANISOU 1848 N ALA A1043 6027 7745 8230 282 -92 527 N
ATOM 1849 CA ALA A1043 -48.608 35.733 40.222 1.00 49.01 C
ANISOU 1849 CA ALA A1043 4958 6653 7012 305 -102 489 C
ATOM 1850 C ALA A1043 -47.554 35.119 41.138 1.00 56.33 C
ANISOU 1850 C ALA A1043 5869 7609 7925 318 -71 555 C
ATOM 1851 O ALA A1043 -46.352 35.312 40.917 1.00 57.49 O
ANISOU 1851 O ALA A1043 6055 7749 8038 316 -84 531 O
ATOM 1852 CB ALA A1043 -49.075 37.075 40.776 1.00 48.46 C
ANISOU 1852 CB ALA A1043 4907 6659 6848 341 -105 460 C
ATOM 1853 N GLY A1044 -47.978 34.364 42.150 1.00 77.04 N
ANISOU 1853 N GLY A1044 8430 10267 10574 332 -30 645 N
ATOM 1854 CA GLY A1044 -47.071 33.747 43.103 1.00 67.51 C
ANISOU 1854 CA GLY A1044 7200 9100 9351 353 3 721 C
ATOM 1855 C GLY A1044 -46.007 32.847 42.505 1.00 70.85 C
ANISOU 1855 C GLY A1044 7637 9453 9829 334 5 732 C
ATOM 1856 O GLY A1044 -46.326 31.797 41.941 1.00 68.07 O
ANISOU 1856 O GLY A1044 7269 9019 9577 308 19 754 O
ATOM 1857 N GLY A1045 -44.741 33.246 42.641 1.00 90.38 N
ANISOU 1857 N GLY A1045 10141 11960 12239 346 -6 718 N
ATOM 1858 CA GLY A1045 -43.624 32.515 42.065 1.00 71.64 C
ANISOU 1858 CA GLY A1045 7784 9531 9907 338 -2 729 C
ATOM 1859 C GLY A1045 -43.731 32.254 40.580 1.00 77.05 C
ANISOU 1859 C GLY A1045 8509 10105 10660 304 -24 664 C
ATOM 1860 O GLY A1045 -43.270 31.210 40.110 1.00 94.54 O
ANISOU 1860 O GLY A1045 10726 12250 12946 298 -3 691 O
ATOM 1861 N LEU A1046 -44.328 33.175 39.822 1.00 50.48 N
ANISOU 1861 N LEU A1046 5180 6725 7274 287 -62 578 N
ATOM 1862 CA LEU A1046 -44.545 32.926 38.399 1.00 57.45 C
ANISOU 1862 CA LEU A1046 6101 7509 8216 258 -86 514 C
ATOM 1863 C LEU A1046 -43.234 32.951 37.624 1.00 43.22 C
ANISOU 1863 C LEU A1046 4349 5671 6403 260 -95 482 C
ATOM 1864 O LEU A1046 -42.977 32.076 36.788 1.00 43.33 O
ANISOU 1864 O LEU A1046 4381 5599 6483 249 -88 477 O
ATOM 1865 CB LEU A1046 -45.517 33.950 37.828 1.00 50.75 C
ANISOU 1865 CB LEU A1046 5275 6666 7341 248 -124 438 C
ATOM 1866 CG LEU A1046 -45.736 33.857 36.323 1.00 38.68 C
ANISOU 1866 CG LEU A1046 3791 5051 5856 222 -156 364 C
ATOM 1867 CD1 LEU A1046 -46.396 32.537 35.986 1.00 50.49 C
ANISOU 1867 CD1 LEU A1046 5257 6472 7455 192 -145 392 C
ATOM 1868 CD2 LEU A1046 -46.584 35.020 35.850 1.00 47.66 C
ANISOU 1868 CD2 LEU A1046 4948 6210 6949 223 -192 296 C
ATOM 1869 N PHE A1047 -42.397 33.955 37.880 1.00 50.99 N
ANISOU 1869 N PHE A1047 5355 6717 7304 274 -110 460 N
ATOM 1870 CA PHE A1047 -41.148 34.118 37.148 1.00 46.20 C
ANISOU 1870 CA PHE A1047 4788 6085 6681 276 -119 433 C
ATOM 1871 C PHE A1047 -40.038 33.211 37.658 1.00 50.62 C
ANISOU 1871 C PHE A1047 5319 6656 7257 295 -84 513 C
ATOM 1872 O PHE A1047 -39.025 33.055 36.966 1.00 48.22 O
ANISOU 1872 O PHE A1047 5042 6319 6960 301 -81 505 O
ATOM 1873 CB PHE A1047 -40.682 35.574 37.217 1.00 46.24 C
ANISOU 1873 CB PHE A1047 4825 6149 6595 276 -149 381 C
ATOM 1874 CG PHE A1047 -41.638 36.559 36.592 1.00 55.16 C
ANISOU 1874 CG PHE A1047 5991 7262 7704 266 -180 302 C
ATOM 1875 CD1 PHE A1047 -42.688 36.131 35.794 1.00 49.54 C
ANISOU 1875 CD1 PHE A1047 5285 6486 7051 255 -187 274 C
ATOM 1876 CD2 PHE A1047 -41.472 37.920 36.795 1.00 49.69 C
ANISOU 1876 CD2 PHE A1047 5330 6619 6932 267 -201 256 C
ATOM 1877 CE1 PHE A1047 -43.559 37.038 35.226 1.00 48.13 C
ANISOU 1877 CE1 PHE A1047 5135 6302 6850 252 -215 209 C
ATOM 1878 CE2 PHE A1047 -42.338 38.830 36.228 1.00 38.53 C
ANISOU 1878 CE2 PHE A1047 3951 5190 5498 266 -223 190 C
ATOM 1879 CZ PHE A1047 -43.383 38.389 35.442 1.00 36.97 C
ANISOU 1879 CZ PHE A1047 3753 4938 5358 262 -230 170 C
ATOM 1880 N GLU A1048 -40.203 32.616 38.836 1.00 63.01 N
ANISOU 1880 N GLU A1048 6834 8275 8832 311 -53 594 N
ATOM 1881 CA GLU A1048 -39.156 31.796 39.429 1.00 37.83 C
ANISOU 1881 CA GLU A1048 3612 5111 5651 337 -17 680 C
ATOM 1882 C GLU A1048 -38.812 30.622 38.522 1.00 32.47 C
ANISOU 1882 C GLU A1048 2953 4327 5059 342 11 697 C
ATOM 1883 O GLU A1048 -39.660 29.769 38.245 1.00 57.11 O
ANISOU 1883 O GLU A1048 6071 7370 8257 330 29 705 O
ATOM 1884 CB GLU A1048 -39.599 31.294 40.804 1.00 45.93 C
ANISOU 1884 CB GLU A1048 4578 6202 6673 358 14 768 C
ATOM 1885 CG GLU A1048 -39.650 32.361 41.895 1.00 77.63 C
ANISOU 1885 CG GLU A1048 8575 10336 10586 366 -6 766 C
ATOM 1886 CD GLU A1048 -38.272 32.847 42.318 1.00100.46 C
ANISOU 1886 CD GLU A1048 11461 13307 13401 378 -21 780 C
ATOM 1887 OE1 GLU A1048 -38.046 34.076 42.327 1.00 96.39 O
ANISOU 1887 OE1 GLU A1048 10975 12839 12811 362 -61 714 O
ATOM 1888 OE2 GLU A1048 -37.413 31.999 42.643 1.00103.42 O
ANISOU 1888 OE2 GLU A1048 11803 13698 13795 403 9 858 O
ATOM 1889 N GLY A1049 -37.563 30.582 38.067 1.00 48.17 N
ANISOU 1889 N GLY A1049 4958 6309 7033 358 16 702 N
ATOM 1890 CA GLY A1049 -37.060 29.505 37.239 1.00 42.11 C
ANISOU 1890 CA GLY A1049 4216 5446 6337 374 49 721 C
ATOM 1891 C GLY A1049 -36.698 29.912 35.829 1.00 52.78 C
ANISOU 1891 C GLY A1049 5631 6733 7689 365 26 638 C
ATOM 1892 O GLY A1049 -36.057 29.124 35.120 1.00 56.54 O
ANISOU 1892 O GLY A1049 6135 7138 8208 387 56 652 O
ATOM 1893 N PHE A1050 -37.072 31.111 35.399 1.00 48.78 N
ANISOU 1893 N PHE A1050 5154 6248 7134 340 -21 556 N
ATOM 1894 CA PHE A1050 -36.864 31.556 34.030 1.00 42.50 C
ANISOU 1894 CA PHE A1050 4420 5392 6335 334 -43 476 C
ATOM 1895 C PHE A1050 -35.759 32.600 33.989 1.00 33.93 C
ANISOU 1895 C PHE A1050 3340 4372 5178 340 -59 465 C
ATOM 1896 O PHE A1050 -35.769 33.551 34.777 1.00 34.93 O
ANISOU 1896 O PHE A1050 3444 4586 5244 326 -83 461 O
ATOM 1897 CB PHE A1050 -38.158 32.123 33.442 1.00 47.53 C
ANISOU 1897 CB PHE A1050 5088 5995 6974 303 -82 393 C
ATOM 1898 CG PHE A1050 -39.274 31.119 33.351 1.00 48.71 C
ANISOU 1898 CG PHE A1050 5231 6076 7201 287 -73 397 C
ATOM 1899 CD1 PHE A1050 -39.390 30.289 32.246 1.00 34.85 C
ANISOU 1899 CD1 PHE A1050 3521 4215 5505 284 -67 364 C
ATOM 1900 CD2 PHE A1050 -40.203 31.003 34.370 1.00 59.11 C
ANISOU 1900 CD2 PHE A1050 6496 7434 8528 273 -70 434 C
ATOM 1901 CE1 PHE A1050 -40.412 29.365 32.161 1.00 30.48 C
ANISOU 1901 CE1 PHE A1050 2961 3595 5026 258 -63 365 C
ATOM 1902 CE2 PHE A1050 -41.232 30.079 34.289 1.00 47.28 C
ANISOU 1902 CE2 PHE A1050 4985 5872 7107 251 -61 444 C
ATOM 1903 CZ PHE A1050 -41.335 29.261 33.183 1.00 26.64 C
ANISOU 1903 CZ PHE A1050 2416 3150 4557 239 -60 407 C
ATOM 1904 N ASP A1051 -34.809 32.414 33.070 1.00 48.39 N
ANISOU 1904 N ASP A1051 5203 6163 7019 360 -44 460 N
ATOM 1905 CA ASP A1051 -33.729 33.382 32.916 1.00 42.15 C
ANISOU 1905 CA ASP A1051 4415 5430 6170 362 -58 452 C
ATOM 1906 C ASP A1051 -34.232 34.668 32.280 1.00 51.72 C
ANISOU 1906 C ASP A1051 5671 6639 7342 334 -100 362 C
ATOM 1907 O ASP A1051 -33.752 35.759 32.611 1.00 40.64 O
ANISOU 1907 O ASP A1051 4260 5301 5881 317 -122 349 O
ATOM 1908 CB ASP A1051 -32.607 32.782 32.072 1.00 44.12 C
ANISOU 1908 CB ASP A1051 4683 5636 6445 398 -23 480 C
ATOM 1909 CG ASP A1051 -32.256 31.366 32.493 1.00 59.74 C
ANISOU 1909 CG ASP A1051 6632 7590 8475 434 28 565 C
ATOM 1910 OD1 ASP A1051 -32.184 31.100 33.714 1.00 47.59 O
ANISOU 1910 OD1 ASP A1051 5033 6120 6929 436 38 634 O
ATOM 1911 OD2 ASP A1051 -32.053 30.516 31.598 1.00 55.76 O
ANISOU 1911 OD2 ASP A1051 6169 6998 8019 464 61 564 O
ATOM 1912 N LEU A1052 -35.195 34.555 31.365 1.00 37.88 N
ANISOU 1912 N LEU A1052 3966 4809 5618 330 -112 298 N
ATOM 1913 CA LEU A1052 -35.772 35.688 30.659 1.00 27.24 C
ANISOU 1913 CA LEU A1052 2663 3452 4236 313 -149 216 C
ATOM 1914 C LEU A1052 -37.282 35.646 30.808 1.00 26.90 C
ANISOU 1914 C LEU A1052 2619 3390 4210 295 -171 181 C
ATOM 1915 O LEU A1052 -37.885 34.569 30.796 1.00 52.40 O
ANISOU 1915 O LEU A1052 5839 6573 7497 295 -158 198 O
ATOM 1916 CB LEU A1052 -35.399 35.668 29.172 1.00 32.20 C
ANISOU 1916 CB LEU A1052 3352 4010 4874 332 -145 172 C
ATOM 1917 CG LEU A1052 -35.991 36.769 28.290 1.00 31.93 C
ANISOU 1917 CG LEU A1052 3368 3959 4805 324 -178 91 C
ATOM 1918 CD1 LEU A1052 -35.428 38.136 28.671 1.00 30.27 C
ANISOU 1918 CD1 LEU A1052 3153 3813 4534 309 -191 84 C
ATOM 1919 CD2 LEU A1052 -35.758 36.466 26.820 1.00 23.46 C
ANISOU 1919 CD2 LEU A1052 2356 2812 3747 351 -171 52 C
ATOM 1920 N VAL A1053 -37.895 36.814 30.958 1.00 23.53 N
ANISOU 1920 N VAL A1053 2202 3001 3736 280 -201 136 N
ATOM 1921 CA VAL A1053 -39.346 36.924 31.048 1.00 31.39 C
ANISOU 1921 CA VAL A1053 3194 3990 4742 268 -221 103 C
ATOM 1922 C VAL A1053 -39.805 37.998 30.072 1.00 30.80 C
ANISOU 1922 C VAL A1053 3171 3897 4633 269 -251 27 C
ATOM 1923 O VAL A1053 -39.295 39.123 30.092 1.00 34.43 O
ANISOU 1923 O VAL A1053 3652 4390 5038 269 -258 7 O
ATOM 1924 CB VAL A1053 -39.813 37.247 32.480 1.00 32.63 C
ANISOU 1924 CB VAL A1053 3302 4223 4870 259 -221 139 C
ATOM 1925 CG1 VAL A1053 -41.323 37.365 32.527 1.00 31.36 C
ANISOU 1925 CG1 VAL A1053 3133 4059 4723 252 -238 113 C
ATOM 1926 CG2 VAL A1053 -39.335 36.178 33.448 1.00 35.69 C
ANISOU 1926 CG2 VAL A1053 3638 4635 5289 265 -189 222 C
ATOM 1927 N LEU A1054 -40.758 37.650 29.213 1.00 23.29 N
ANISOU 1927 N LEU A1054 2241 2895 3715 268 -268 -14 N
ATOM 1928 CA LEU A1054 -41.308 38.573 28.228 1.00 23.08 C
ANISOU 1928 CA LEU A1054 2261 2854 3657 275 -296 -82 C
ATOM 1929 C LEU A1054 -42.790 38.752 28.518 1.00 35.82 C
ANISOU 1929 C LEU A1054 3847 4487 5274 266 -318 -98 C
ATOM 1930 O LEU A1054 -43.569 37.802 28.391 1.00 51.69 O
ANISOU 1930 O LEU A1054 5834 6467 7339 252 -326 -93 O
ATOM 1931 CB LEU A1054 -41.091 38.054 26.811 1.00 25.47 C
ANISOU 1931 CB LEU A1054 2610 3084 3981 288 -301 -120 C
ATOM 1932 CG LEU A1054 -39.644 37.809 26.390 1.00 23.14 C
ANISOU 1932 CG LEU A1054 2342 2767 3684 306 -273 -100 C
ATOM 1933 CD1 LEU A1054 -39.623 37.073 25.064 1.00 23.37 C
ANISOU 1933 CD1 LEU A1054 2419 2721 3739 323 -276 -136 C
ATOM 1934 CD2 LEU A1054 -38.887 39.122 26.286 1.00 31.50 C
ANISOU 1934 CD2 LEU A1054 3424 3861 4682 315 -271 -111 C
ATOM 1935 N LEU A1055 -43.182 39.963 28.904 1.00 40.18 N
ANISOU 1935 N LEU A1055 4405 5088 5773 274 -327 -115 N
ATOM 1936 CA LEU A1055 -44.576 40.276 29.187 1.00 33.91 C
ANISOU 1936 CA LEU A1055 3585 4322 4977 275 -343 -125 C
ATOM 1937 C LEU A1055 -45.170 41.064 28.031 1.00 28.36 C
ANISOU 1937 C LEU A1055 2925 3602 4248 293 -369 -186 C
ATOM 1938 O LEU A1055 -44.617 42.091 27.625 1.00 39.28 O
ANISOU 1938 O LEU A1055 4356 4985 5581 311 -367 -214 O
ATOM 1939 CB LEU A1055 -44.713 41.072 30.484 1.00 23.10 C
ANISOU 1939 CB LEU A1055 2194 3021 3562 281 -329 -100 C
ATOM 1940 CG LEU A1055 -44.177 40.380 31.733 1.00 23.26 C
ANISOU 1940 CG LEU A1055 2168 3074 3595 269 -304 -36 C
ATOM 1941 CD1 LEU A1055 -44.348 41.272 32.957 1.00 28.39 C
ANISOU 1941 CD1 LEU A1055 2807 3795 4186 280 -294 -21 C
ATOM 1942 CD2 LEU A1055 -44.872 39.052 31.923 1.00 31.41 C
ANISOU 1942 CD2 LEU A1055 3148 4088 4700 255 -298 4 C
ATOM 1943 N GLY A1056 -46.296 40.586 27.511 1.00 36.93 N
ANISOU 1943 N GLY A1056 3991 4674 5367 288 -395 -203 N
ATOM 1944 CA GLY A1056 -47.020 41.279 26.465 1.00 33.17 C
ANISOU 1944 CA GLY A1056 3545 4195 4864 309 -423 -254 C
ATOM 1945 C GLY A1056 -48.423 41.634 26.919 1.00 32.85 C
ANISOU 1945 C GLY A1056 3458 4204 4820 315 -436 -245 C
ATOM 1946 O GLY A1056 -49.037 40.916 27.711 1.00 27.48 O
ANISOU 1946 O GLY A1056 2717 3542 4182 293 -432 -206 O
ATOM 1947 N CYS A1057 -48.930 42.749 26.401 1.00 28.87 N
ANISOU 1947 N CYS A1057 2983 3721 4267 349 -447 -277 N
ATOM 1948 CA CYS A1057 -50.250 43.230 26.784 1.00 32.12 C
ANISOU 1948 CA CYS A1057 3352 4185 4667 367 -455 -266 C
ATOM 1949 C CYS A1057 -50.625 44.399 25.892 1.00 42.71 C
ANISOU 1949 C CYS A1057 4738 5536 5953 413 -466 -305 C
ATOM 1950 O CYS A1057 -49.763 45.177 25.473 1.00 42.32 O
ANISOU 1950 O CYS A1057 4754 5463 5861 434 -453 -329 O
ATOM 1951 CB CYS A1057 -50.285 43.655 28.255 1.00 30.22 C
ANISOU 1951 CB CYS A1057 3086 3991 4405 376 -419 -222 C
ATOM 1952 SG CYS A1057 -51.844 44.369 28.786 1.00 40.27 S
ANISOU 1952 SG CYS A1057 4313 5333 5654 413 -415 -202 S
ATOM 1953 N SER A1058 -51.917 44.518 25.614 1.00 32.95 N
ANISOU 1953 N SER A1058 3463 4337 4720 429 -490 -305 N
ATOM 1954 CA SER A1058 -52.441 45.596 24.794 1.00 42.14 C
ANISOU 1954 CA SER A1058 4660 5519 5831 480 -501 -333 C
ATOM 1955 C SER A1058 -53.130 46.638 25.664 1.00 45.53 C
ANISOU 1955 C SER A1058 5078 6002 6221 523 -470 -306 C
ATOM 1956 O SER A1058 -53.532 46.371 26.799 1.00 54.03 O
ANISOU 1956 O SER A1058 6103 7112 7315 513 -451 -266 O
ATOM 1957 CB SER A1058 -53.425 45.054 23.759 1.00 44.61 C
ANISOU 1957 CB SER A1058 4938 5845 6168 474 -553 -353 C
ATOM 1958 OG SER A1058 -54.381 44.215 24.383 1.00 36.47 O
ANISOU 1958 OG SER A1058 3819 4846 5191 439 -567 -318 O
ATOM 1959 N THR A1059 -53.259 47.838 25.113 1.00 44.20 N
ANISOU 1959 N THR A1059 4960 5839 5995 578 -460 -327 N
ATOM 1960 CA THR A1059 -53.958 48.915 25.792 1.00 39.73 C
ANISOU 1960 CA THR A1059 4395 5316 5385 631 -428 -306 C
ATOM 1961 C THR A1059 -55.421 48.912 25.372 1.00 43.88 C
ANISOU 1961 C THR A1059 4859 5898 5915 663 -453 -290 C
ATOM 1962 O THR A1059 -55.747 48.625 24.216 1.00 38.15 O
ANISOU 1962 O THR A1059 4125 5172 5198 662 -496 -312 O
ATOM 1963 CB THR A1059 -53.308 50.260 25.478 1.00 35.43 C
ANISOU 1963 CB THR A1059 3942 4740 4778 675 -397 -332 C
ATOM 1964 OG1 THR A1059 -51.884 50.109 25.502 1.00 38.19 O
ANISOU 1964 OG1 THR A1059 4342 5036 5134 636 -387 -351 O
ATOM 1965 CG2 THR A1059 -53.716 51.292 26.517 1.00 37.18 C
ANISOU 1965 CG2 THR A1059 4181 4990 4957 720 -351 -313 C
ATOM 1966 N TRP A1060 -56.305 49.226 26.322 1.00 37.63 N
ANISOU 1966 N TRP A1060 4022 5160 5115 692 -427 -249 N
ATOM 1967 CA TRP A1060 -57.734 49.093 26.068 1.00 56.91 C
ANISOU 1967 CA TRP A1060 6385 7667 7570 716 -450 -220 C
ATOM 1968 C TRP A1060 -58.576 50.178 26.732 1.00 58.16 C
ANISOU 1968 C TRP A1060 6538 7879 7681 793 -405 -185 C
ATOM 1969 O TRP A1060 -59.770 49.958 26.968 1.00 75.15 O
ANISOU 1969 O TRP A1060 8606 10097 9852 810 -412 -142 O
ATOM 1970 CB TRP A1060 -58.229 47.722 26.516 1.00 32.96 C
ANISOU 1970 CB TRP A1060 3255 4656 4612 652 -477 -188 C
ATOM 1971 CG TRP A1060 -58.141 46.714 25.449 1.00 31.96 C
ANISOU 1971 CG TRP A1060 3110 4501 4532 596 -537 -220 C
ATOM 1972 CD1 TRP A1060 -57.030 46.041 25.055 1.00 34.70 C
ANISOU 1972 CD1 TRP A1060 3502 4779 4902 547 -551 -256 C
ATOM 1973 CD2 TRP A1060 -59.206 46.269 24.606 1.00 42.92 C
ANISOU 1973 CD2 TRP A1060 4432 5929 5946 585 -592 -221 C
ATOM 1974 NE1 TRP A1060 -57.334 45.194 24.020 1.00 60.64 N
ANISOU 1974 NE1 TRP A1060 6763 8053 8224 508 -609 -284 N
ATOM 1975 CE2 TRP A1060 -58.666 45.313 23.727 1.00 57.58 C
ANISOU 1975 CE2 TRP A1060 6306 7732 7839 526 -640 -266 C
ATOM 1976 CE3 TRP A1060 -60.566 46.580 24.513 1.00 50.92 C
ANISOU 1976 CE3 TRP A1060 5372 7022 6955 620 -607 -187 C
ATOM 1977 CZ2 TRP A1060 -59.434 44.666 22.765 1.00 69.10 C
ANISOU 1977 CZ2 TRP A1060 7717 9212 9327 495 -706 -286 C
ATOM 1978 CZ3 TRP A1060 -61.331 45.930 23.561 1.00 69.41 C
ANISOU 1978 CZ3 TRP A1060 7654 9391 9327 586 -675 -201 C
ATOM 1979 CH2 TRP A1060 -60.762 44.986 22.698 1.00102.78 C
ANISOU 1979 CH2 TRP A1060 11904 13559 13587 522 -726 -254 C
ATOM 1980 N GLY A1061 -57.999 51.341 27.026 1.00 38.59 N
ANISOU 1980 N GLY A1061 4149 5371 5143 840 -358 -202 N
ATOM 1981 CA GLY A1061 -58.743 52.371 27.721 1.00 61.15 C
ANISOU 1981 CA GLY A1061 7014 8269 7952 917 -308 -172 C
ATOM 1982 C GLY A1061 -59.712 53.090 26.797 1.00 58.24 C
ANISOU 1982 C GLY A1061 6638 7939 7554 990 -314 -163 C
ATOM 1983 O GLY A1061 -59.399 53.392 25.646 1.00 63.84 O
ANISOU 1983 O GLY A1061 7391 8619 8247 1000 -337 -196 O
ATOM 1984 N ASP A1062 -60.913 53.353 27.317 1.00 45.10 N
ANISOU 1984 N ASP A1062 4912 6346 5879 1046 -291 -111 N
ATOM 1985 CA ASP A1062 -61.889 54.139 26.569 1.00 61.10 C
ANISOU 1985 CA ASP A1062 6927 8419 7871 1129 -288 -91 C
ATOM 1986 C ASP A1062 -61.427 55.587 26.440 1.00 59.66 C
ANISOU 1986 C ASP A1062 6863 8187 7618 1204 -233 -115 C
ATOM 1987 O ASP A1062 -61.121 56.062 25.341 1.00 53.25 O
ANISOU 1987 O ASP A1062 6103 7344 6784 1226 -247 -143 O
ATOM 1988 CB ASP A1062 -63.258 54.046 27.253 1.00 58.24 C
ANISOU 1988 CB ASP A1062 6463 8148 7516 1173 -270 -22 C
ATOM 1989 CG ASP A1062 -64.326 54.857 26.546 1.00 44.97 C
ANISOU 1989 CG ASP A1062 4759 6529 5798 1267 -264 10 C
ATOM 1990 OD1 ASP A1062 -64.700 54.502 25.408 1.00 88.89 O
ANISOU 1990 OD1 ASP A1062 10276 12122 11378 1254 -324 4 O
ATOM 1991 OD2 ASP A1062 -64.803 55.845 27.142 1.00 47.00 O
ANISOU 1991 OD2 ASP A1062 5045 6807 6007 1358 -198 42 O
ATOM 1992 N ASP A1063 -61.360 56.303 27.563 1.00 42.01 N
ANISOU 1992 N ASP A1063 4676 5940 5346 1244 -168 -104 N
ATOM 1993 CA ASP A1063 -60.738 57.620 27.636 1.00 42.31 C
ANISOU 1993 CA ASP A1063 4841 5911 5325 1297 -113 -136 C
ATOM 1994 C ASP A1063 -59.490 57.569 28.513 1.00 61.44 C
ANISOU 1994 C ASP A1063 7332 8267 7745 1233 -96 -176 C
ATOM 1995 O ASP A1063 -59.183 58.520 29.235 1.00 85.49 O
ANISOU 1995 O ASP A1063 10464 11276 10743 1269 -41 -191 O
ATOM 1996 CB ASP A1063 -61.730 58.657 28.163 1.00 55.41 C
ANISOU 1996 CB ASP A1063 6514 7607 6932 1408 -47 -95 C
ATOM 1997 CG ASP A1063 -61.232 60.091 28.008 1.00 76.39 C
ANISOU 1997 CG ASP A1063 9307 10189 9530 1471 11 -127 C
ATOM 1998 OD1 ASP A1063 -60.267 60.325 27.247 1.00 86.41 O
ANISOU 1998 OD1 ASP A1063 10646 11387 10800 1436 -5 -172 O
ATOM 1999 OD2 ASP A1063 -61.806 60.985 28.665 1.00 90.77 O
ANISOU 1999 OD2 ASP A1063 11167 12019 11305 1556 76 -104 O
ATOM 2000 N SER A1064 -58.759 56.462 28.463 1.00 50.94 N
ANISOU 2000 N SER A1064 5967 6922 6465 1139 -144 -193 N
ATOM 2001 CA SER A1064 -57.658 56.247 29.388 1.00 46.17 C
ANISOU 2001 CA SER A1064 5405 6276 5862 1077 -133 -219 C
ATOM 2002 C SER A1064 -56.685 55.255 28.770 1.00 58.30 C
ANISOU 2002 C SER A1064 6925 7776 7449 988 -186 -246 C
ATOM 2003 O SER A1064 -56.842 54.823 27.626 1.00 48.55 O
ANISOU 2003 O SER A1064 5661 6543 6241 977 -228 -251 O
ATOM 2004 CB SER A1064 -58.177 55.750 30.740 1.00 60.47 C
ANISOU 2004 CB SER A1064 7155 8143 7678 1075 -113 -180 C
ATOM 2005 OG SER A1064 -59.083 54.672 30.563 1.00 58.69 O
ANISOU 2005 OG SER A1064 6810 7982 7507 1057 -149 -134 O
ATOM 2006 N ILE A1065 -55.658 54.908 29.540 1.00 59.47 N
ANISOU 2006 N ILE A1065 7096 7895 7604 927 -183 -263 N
ATOM 2007 CA ILE A1065 -54.784 53.796 29.190 1.00 47.54 C
ANISOU 2007 CA ILE A1065 5557 6361 6146 845 -227 -275 C
ATOM 2008 C ILE A1065 -55.065 52.642 30.139 1.00 54.92 C
ANISOU 2008 C ILE A1065 6405 7341 7120 805 -237 -237 C
ATOM 2009 O ILE A1065 -54.544 52.602 31.256 1.00 49.58 O
ANISOU 2009 O ILE A1065 5741 6667 6429 784 -215 -231 O
ATOM 2010 CB ILE A1065 -53.301 54.201 29.219 1.00 41.74 C
ANISOU 2010 CB ILE A1065 4906 5560 5395 805 -218 -316 C
ATOM 2011 CG1 ILE A1065 -52.978 55.044 30.453 1.00 73.15 C
ANISOU 2011 CG1 ILE A1065 8941 9532 9322 817 -175 -325 C
ATOM 2012 CG2 ILE A1065 -52.940 54.981 27.971 1.00 67.41 C
ANISOU 2012 CG2 ILE A1065 8225 8760 8628 829 -219 -347 C
ATOM 2013 CD1 ILE A1065 -51.501 55.273 30.645 1.00 72.54 C
ANISOU 2013 CD1 ILE A1065 8926 9401 9236 761 -175 -360 C
ATOM 2014 N GLU A1066 -55.924 51.721 29.721 1.00 65.00 N
ANISOU 2014 N GLU A1066 7594 8655 8446 794 -270 -208 N
ATOM 2015 CA GLU A1066 -56.260 50.556 30.523 1.00 58.95 C
ANISOU 2015 CA GLU A1066 6741 7928 7731 753 -278 -165 C
ATOM 2016 C GLU A1066 -55.577 49.312 29.971 1.00 47.49 C
ANISOU 2016 C GLU A1066 5262 6440 6342 677 -322 -176 C
ATOM 2017 O GLU A1066 -55.226 49.232 28.791 1.00 43.32 O
ANISOU 2017 O GLU A1066 4761 5875 5825 663 -354 -212 O
ATOM 2018 CB GLU A1066 -57.773 50.341 30.569 1.00 52.80 C
ANISOU 2018 CB GLU A1066 5872 7218 6970 788 -281 -117 C
ATOM 2019 CG GLU A1066 -58.550 51.536 31.084 1.00 61.82 C
ANISOU 2019 CG GLU A1066 7038 8400 8050 875 -232 -98 C
ATOM 2020 CD GLU A1066 -58.162 51.937 32.493 1.00 77.46 C
ANISOU 2020 CD GLU A1066 9057 10387 9989 892 -181 -88 C
ATOM 2021 OE1 GLU A1066 -57.665 51.078 33.254 1.00 81.71 O
ANISOU 2021 OE1 GLU A1066 9564 10927 10554 839 -184 -71 O
ATOM 2022 OE2 GLU A1066 -58.363 53.118 32.845 1.00 82.42 O
ANISOU 2022 OE2 GLU A1066 9748 11017 10551 960 -137 -96 O
ATOM 2023 N LEU A1067 -55.387 48.335 30.850 1.00 43.82 N
ANISOU 2023 N LEU A1067 4746 5987 5917 632 -318 -143 N
ATOM 2024 CA LEU A1067 -54.735 47.096 30.463 1.00 46.50 C
ANISOU 2024 CA LEU A1067 5061 6289 6319 564 -350 -147 C
ATOM 2025 C LEU A1067 -55.744 46.099 29.912 1.00 49.33 C
ANISOU 2025 C LEU A1067 5335 6664 6743 538 -387 -126 C
ATOM 2026 O LEU A1067 -56.953 46.198 30.144 1.00 42.60 O
ANISOU 2026 O LEU A1067 4422 5868 5897 564 -385 -92 O
ATOM 2027 CB LEU A1067 -54.003 46.474 31.646 1.00 36.67 C
ANISOU 2027 CB LEU A1067 3801 5045 5087 530 -327 -117 C
ATOM 2028 CG LEU A1067 -52.836 47.277 32.202 1.00 42.11 C
ANISOU 2028 CG LEU A1067 4568 5716 5717 538 -301 -140 C
ATOM 2029 CD1 LEU A1067 -52.333 46.606 33.455 1.00 24.56 C
ANISOU 2029 CD1 LEU A1067 2314 3515 3503 511 -281 -100 C
ATOM 2030 CD2 LEU A1067 -51.731 47.389 31.171 1.00 29.86 C
ANISOU 2030 CD2 LEU A1067 3078 4102 4165 513 -322 -188 C
ATOM 2031 N GLN A1068 -55.222 45.126 29.173 1.00 40.39 N
ANISOU 2031 N GLN A1068 4202 5484 5662 484 -422 -148 N
ATOM 2032 CA GLN A1068 -56.054 44.049 28.667 1.00 34.49 C
ANISOU 2032 CA GLN A1068 3380 4741 4985 443 -462 -136 C
ATOM 2033 C GLN A1068 -56.681 43.296 29.833 1.00 46.16 C
ANISOU 2033 C GLN A1068 4772 6256 6510 421 -441 -69 C
ATOM 2034 O GLN A1068 -56.093 43.181 30.911 1.00 47.15 O
ANISOU 2034 O GLN A1068 4902 6384 6628 419 -402 -38 O
ATOM 2035 CB GLN A1068 -55.224 43.111 27.790 1.00 26.65 C
ANISOU 2035 CB GLN A1068 2416 3678 4033 391 -495 -174 C
ATOM 2036 CG GLN A1068 -56.042 42.214 26.884 1.00 35.98 C
ANISOU 2036 CG GLN A1068 3547 4851 5272 350 -548 -188 C
ATOM 2037 CD GLN A1068 -56.435 40.917 27.556 1.00 53.96 C
ANISOU 2037 CD GLN A1068 5746 7123 7632 291 -549 -142 C
ATOM 2038 OE1 GLN A1068 -55.893 40.559 28.602 1.00 50.59 O
ANISOU 2038 OE1 GLN A1068 5312 6689 7222 281 -508 -101 O
ATOM 2039 NE2 GLN A1068 -57.382 40.203 26.959 1.00 53.37 N
ANISOU 2039 NE2 GLN A1068 5613 7053 7612 251 -595 -146 N
ATOM 2040 N ASP A1069 -57.895 42.793 29.607 1.00 55.89 N
ANISOU 2040 N ASP A1069 5922 7524 7791 404 -467 -43 N
ATOM 2041 CA ASP A1069 -58.700 42.241 30.694 1.00 46.41 C
ANISOU 2041 CA ASP A1069 4631 6371 6633 393 -441 31 C
ATOM 2042 C ASP A1069 -57.968 41.122 31.429 1.00 56.62 C
ANISOU 2042 C ASP A1069 5910 7623 7980 342 -421 62 C
ATOM 2043 O ASP A1069 -57.884 41.128 32.663 1.00 58.80 O
ANISOU 2043 O ASP A1069 6166 7931 8245 360 -374 115 O
ATOM 2044 CB ASP A1069 -60.037 41.746 30.140 1.00 58.52 C
ANISOU 2044 CB ASP A1069 6073 7940 8222 367 -483 50 C
ATOM 2045 CG ASP A1069 -60.863 42.862 29.521 1.00 59.05 C
ANISOU 2045 CG ASP A1069 6140 8063 8233 429 -497 34 C
ATOM 2046 OD1 ASP A1069 -60.415 44.031 29.539 1.00 55.09 O
ANISOU 2046 OD1 ASP A1069 5715 7565 7652 494 -470 10 O
ATOM 2047 OD2 ASP A1069 -61.966 42.566 29.016 1.00 67.72 O
ANISOU 2047 OD2 ASP A1069 7160 9202 9368 412 -536 49 O
ATOM 2048 N ASP A1070 -57.431 40.148 30.688 1.00 73.81 N
ANISOU 2048 N ASP A1070 8102 9731 10212 283 -455 30 N
ATOM 2049 CA ASP A1070 -56.778 39.007 31.328 1.00 47.35 C
ANISOU 2049 CA ASP A1070 4735 6336 6919 237 -433 66 C
ATOM 2050 C ASP A1070 -55.491 39.412 32.031 1.00 44.36 C
ANISOU 2050 C ASP A1070 4421 5948 6486 265 -392 67 C
ATOM 2051 O ASP A1070 -55.068 38.741 32.977 1.00 43.21 O
ANISOU 2051 O ASP A1070 4253 5800 6367 251 -358 118 O
ATOM 2052 CB ASP A1070 -56.480 37.918 30.299 1.00 39.16 C
ANISOU 2052 CB ASP A1070 3711 5218 5948 174 -475 26 C
ATOM 2053 CG ASP A1070 -57.716 37.477 29.540 1.00 79.09 C
ANISOU 2053 CG ASP A1070 8706 10284 11059 135 -525 16 C
ATOM 2054 OD1 ASP A1070 -58.816 37.482 30.136 1.00 77.69 O
ANISOU 2054 OD1 ASP A1070 8444 10169 10907 136 -517 71 O
ATOM 2055 OD2 ASP A1070 -57.585 37.122 28.346 1.00 70.85 O
ANISOU 2055 OD2 ASP A1070 7698 9190 10032 104 -574 -47 O
ATOM 2056 N PHE A1071 -54.854 40.494 31.586 1.00 44.90 N
ANISOU 2056 N PHE A1071 4568 6012 6479 303 -396 14 N
ATOM 2057 CA PHE A1071 -53.574 40.890 32.152 1.00 25.46 C
ANISOU 2057 CA PHE A1071 2165 3539 3967 320 -366 10 C
ATOM 2058 C PHE A1071 -53.720 41.683 33.441 1.00 32.83 C
ANISOU 2058 C PHE A1071 3092 4539 4841 364 -324 47 C
ATOM 2059 O PHE A1071 -52.779 41.706 34.243 1.00 46.54 O
ANISOU 2059 O PHE A1071 4854 6281 6550 366 -298 62 O
ATOM 2060 CB PHE A1071 -52.785 41.707 31.128 1.00 24.96 C
ANISOU 2060 CB PHE A1071 2189 3441 3855 336 -385 -60 C
ATOM 2061 CG PHE A1071 -51.303 41.667 31.334 1.00 34.12 C
ANISOU 2061 CG PHE A1071 3402 4567 4995 327 -369 -69 C
ATOM 2062 CD1 PHE A1071 -50.688 42.537 32.219 1.00 38.97 C
ANISOU 2062 CD1 PHE A1071 4048 5214 5544 353 -339 -62 C
ATOM 2063 CD2 PHE A1071 -50.521 40.759 30.640 1.00 34.04 C
ANISOU 2063 CD2 PHE A1071 3409 4495 5029 293 -383 -83 C
ATOM 2064 CE1 PHE A1071 -49.323 42.496 32.416 1.00 32.88 C
ANISOU 2064 CE1 PHE A1071 3315 4421 4756 340 -328 -66 C
ATOM 2065 CE2 PHE A1071 -49.151 40.717 30.829 1.00 32.05 C
ANISOU 2065 CE2 PHE A1071 3198 4220 4760 289 -365 -83 C
ATOM 2066 CZ PHE A1071 -48.554 41.588 31.718 1.00 34.92 C
ANISOU 2066 CZ PHE A1071 3583 4624 5062 310 -340 -72 C
ATOM 2067 N ILE A1072 -54.874 42.318 33.663 1.00 50.12 N
ANISOU 2067 N ILE A1072 5251 6784 7009 402 -316 62 N
ATOM 2068 CA ILE A1072 -55.042 43.167 34.848 1.00 40.77 C
ANISOU 2068 CA ILE A1072 4073 5661 5757 453 -273 90 C
ATOM 2069 C ILE A1072 -54.758 42.427 36.149 1.00 46.52 C
ANISOU 2069 C ILE A1072 4760 6416 6500 442 -238 155 C
ATOM 2070 O ILE A1072 -54.003 42.959 36.984 1.00 52.26 O
ANISOU 2070 O ILE A1072 5531 7164 7163 465 -212 154 O
ATOM 2071 CB ILE A1072 -56.435 43.817 34.840 1.00 32.76 C
ANISOU 2071 CB ILE A1072 3021 4702 4725 501 -266 107 C
ATOM 2072 CG1 ILE A1072 -56.589 44.745 33.635 1.00 32.11 C
ANISOU 2072 CG1 ILE A1072 2992 4599 4609 526 -294 45 C
ATOM 2073 CG2 ILE A1072 -56.667 44.573 36.138 1.00 30.18 C
ANISOU 2073 CG2 ILE A1072 2701 4437 4330 559 -215 141 C
ATOM 2074 CD1 ILE A1072 -57.996 45.258 33.439 1.00 49.40 C
ANISOU 2074 CD1 ILE A1072 5135 6845 6791 572 -293 66 C
ATOM 2075 N PRO A1073 -55.311 41.233 36.408 1.00 47.93 N
ANISOU 2075 N PRO A1073 4856 6597 6758 409 -234 214 N
ATOM 2076 CA PRO A1073 -55.021 40.574 37.693 1.00 39.54 C
ANISOU 2076 CA PRO A1073 3755 5564 5703 408 -194 283 C
ATOM 2077 C PRO A1073 -53.546 40.287 37.915 1.00 41.36 C
ANISOU 2077 C PRO A1073 4035 5762 5918 388 -191 271 C
ATOM 2078 O PRO A1073 -53.079 40.360 39.060 1.00 53.58 O
ANISOU 2078 O PRO A1073 5584 7353 7421 410 -158 308 O
ATOM 2079 CB PRO A1073 -55.844 39.280 37.619 1.00 40.46 C
ANISOU 2079 CB PRO A1073 3780 5668 5925 364 -196 342 C
ATOM 2080 CG PRO A1073 -56.061 39.052 36.165 1.00 55.69 C
ANISOU 2080 CG PRO A1073 5719 7538 7903 323 -249 284 C
ATOM 2081 CD PRO A1073 -56.231 40.418 35.591 1.00 51.31 C
ANISOU 2081 CD PRO A1073 5221 7003 7272 369 -265 223 C
ATOM 2082 N LEU A1074 -52.793 39.974 36.859 1.00 35.10 N
ANISOU 2082 N LEU A1074 3282 4899 5156 351 -224 222 N
ATOM 2083 CA LEU A1074 -51.357 39.769 37.019 1.00 31.59 C
ANISOU 2083 CA LEU A1074 2881 4428 4693 337 -220 214 C
ATOM 2084 C LEU A1074 -50.661 41.070 37.393 1.00 40.07 C
ANISOU 2084 C LEU A1074 4022 5535 5667 371 -215 174 C
ATOM 2085 O LEU A1074 -49.823 41.100 38.303 1.00 46.78 O
ANISOU 2085 O LEU A1074 4881 6415 6476 376 -197 197 O
ATOM 2086 CB LEU A1074 -50.759 39.188 35.736 1.00 41.26 C
ANISOU 2086 CB LEU A1074 4136 5572 5970 298 -252 171 C
ATOM 2087 CG LEU A1074 -49.235 39.025 35.695 1.00 35.98 C
ANISOU 2087 CG LEU A1074 3512 4873 5284 288 -249 160 C
ATOM 2088 CD1 LEU A1074 -48.778 37.887 36.598 1.00 33.96 C
ANISOU 2088 CD1 LEU A1074 3211 4624 5070 276 -218 235 C
ATOM 2089 CD2 LEU A1074 -48.753 38.809 34.269 1.00 27.67 C
ANISOU 2089 CD2 LEU A1074 2505 3746 4263 266 -279 104 C
ATOM 2090 N PHE A1075 -51.002 42.156 36.696 1.00 51.44 N
ANISOU 2090 N PHE A1075 5510 6969 7067 392 -233 115 N
ATOM 2091 CA PHE A1075 -50.351 43.442 36.925 1.00 39.59 C
ANISOU 2091 CA PHE A1075 4083 5483 5478 417 -229 69 C
ATOM 2092 C PHE A1075 -50.518 43.896 38.367 1.00 37.50 C
ANISOU 2092 C PHE A1075 3811 5290 5149 451 -196 103 C
ATOM 2093 O PHE A1075 -49.554 44.341 39.002 1.00 38.67 O
ANISOU 2093 O PHE A1075 3999 5455 5238 450 -191 90 O
ATOM 2094 CB PHE A1075 -50.927 44.472 35.952 1.00 37.77 C
ANISOU 2094 CB PHE A1075 3897 5233 5222 442 -245 12 C
ATOM 2095 CG PHE A1075 -50.285 45.828 36.030 1.00 44.92 C
ANISOU 2095 CG PHE A1075 4886 6136 6046 463 -240 -40 C
ATOM 2096 CD1 PHE A1075 -49.202 46.142 35.227 1.00 42.80 C
ANISOU 2096 CD1 PHE A1075 4675 5817 5771 439 -259 -86 C
ATOM 2097 CD2 PHE A1075 -50.792 46.804 36.877 1.00 51.50 C
ANISOU 2097 CD2 PHE A1075 5742 7015 6810 509 -214 -41 C
ATOM 2098 CE1 PHE A1075 -48.619 47.396 35.284 1.00 60.02 C
ANISOU 2098 CE1 PHE A1075 6931 7989 7884 452 -254 -132 C
ATOM 2099 CE2 PHE A1075 -50.213 48.056 36.939 1.00 34.56 C
ANISOU 2099 CE2 PHE A1075 3681 4857 4594 524 -208 -93 C
ATOM 2100 CZ PHE A1075 -49.126 48.354 36.140 1.00 49.78 C
ANISOU 2100 CZ PHE A1075 5662 6731 6522 491 -229 -138 C
ATOM 2101 N ASP A1076 -51.733 43.776 38.907 1.00 46.94 N
ANISOU 2101 N ASP A1076 4954 6530 6352 482 -173 147 N
ATOM 2102 CA ASP A1076 -51.998 44.230 40.265 1.00 62.06 C
ANISOU 2102 CA ASP A1076 6866 8516 8199 525 -137 179 C
ATOM 2103 C ASP A1076 -51.206 43.444 41.301 1.00 53.88 C
ANISOU 2103 C ASP A1076 5802 7512 7159 510 -121 231 C
ATOM 2104 O ASP A1076 -50.981 43.950 42.405 1.00 47.77 O
ANISOU 2104 O ASP A1076 5049 6795 6308 540 -100 240 O
ATOM 2105 CB ASP A1076 -53.498 44.147 40.566 1.00 55.63 C
ANISOU 2105 CB ASP A1076 5989 7745 7402 564 -111 227 C
ATOM 2106 CG ASP A1076 -54.305 45.201 39.816 1.00 64.29 C
ANISOU 2106 CG ASP A1076 7120 8834 8473 601 -118 181 C
ATOM 2107 OD1 ASP A1076 -53.691 46.028 39.105 1.00 45.97 O
ANISOU 2107 OD1 ASP A1076 4877 6471 6119 597 -139 112 O
ATOM 2108 OD2 ASP A1076 -55.549 45.205 39.939 1.00 53.69 O
ANISOU 2108 OD2 ASP A1076 5723 7529 7146 636 -99 221 O
ATOM 2109 N SER A1077 -50.775 42.225 40.972 1.00 52.66 N
ANISOU 2109 N SER A1077 5603 7322 7084 466 -131 265 N
ATOM 2110 CA SER A1077 -49.969 41.406 41.870 1.00 42.09 C
ANISOU 2110 CA SER A1077 4235 6010 5746 455 -114 321 C
ATOM 2111 C SER A1077 -48.613 41.074 41.253 1.00 48.60 C
ANISOU 2111 C SER A1077 5090 6786 6591 414 -140 294 C
ATOM 2112 O SER A1077 -48.062 40.000 41.489 1.00 55.29 O
ANISOU 2112 O SER A1077 5899 7625 7484 395 -131 347 O
ATOM 2113 CB SER A1077 -50.715 40.130 42.259 1.00 46.83 C
ANISOU 2113 CB SER A1077 4747 6619 6426 450 -87 408 C
ATOM 2114 OG SER A1077 -51.979 40.432 42.828 1.00 66.22 O
ANISOU 2114 OG SER A1077 7166 9127 8866 490 -60 441 O
ATOM 2115 N LEU A1078 -48.063 41.994 40.461 1.00 57.28 N
ANISOU 2115 N LEU A1078 6259 7851 7656 404 -168 218 N
ATOM 2116 CA LEU A1078 -46.800 41.742 39.780 1.00 46.99 C
ANISOU 2116 CA LEU A1078 4982 6500 6372 368 -190 194 C
ATOM 2117 C LEU A1078 -45.610 41.686 40.731 1.00 50.68 C
ANISOU 2117 C LEU A1078 5450 7017 6790 363 -185 220 C
ATOM 2118 O LEU A1078 -44.531 41.256 40.312 1.00 57.99 O
ANISOU 2118 O LEU A1078 6380 7914 7740 337 -196 222 O
ATOM 2119 CB LEU A1078 -46.571 42.818 38.715 1.00 41.14 C
ANISOU 2119 CB LEU A1078 4312 5714 5604 363 -217 111 C
ATOM 2120 CG LEU A1078 -45.564 42.534 37.604 1.00 24.16 C
ANISOU 2120 CG LEU A1078 2188 3500 3491 331 -238 83 C
ATOM 2121 CD1 LEU A1078 -46.030 41.382 36.741 1.00 24.15 C
ANISOU 2121 CD1 LEU A1078 2151 3443 3580 316 -242 101 C
ATOM 2122 CD2 LEU A1078 -45.370 43.785 36.778 1.00 23.86 C
ANISOU 2122 CD2 LEU A1078 2222 3431 3412 333 -256 9 C
ATOM 2123 N GLU A1079 -45.769 42.110 41.988 1.00 34.04 N
ANISOU 2123 N GLU A1079 3338 4985 4612 390 -169 242 N
ATOM 2124 CA GLU A1079 -44.661 42.028 42.934 1.00 39.93 C
ANISOU 2124 CA GLU A1079 4079 5789 5305 385 -169 269 C
ATOM 2125 C GLU A1079 -44.400 40.595 43.391 1.00 51.80 C
ANISOU 2125 C GLU A1079 5511 7308 6864 385 -147 360 C
ATOM 2126 O GLU A1079 -43.243 40.232 43.634 1.00 41.89 O
ANISOU 2126 O GLU A1079 4245 6073 5599 370 -153 384 O
ATOM 2127 CB GLU A1079 -44.924 42.934 44.142 1.00 52.95 C
ANISOU 2127 CB GLU A1079 5752 7517 6851 417 -161 259 C
ATOM 2128 CG GLU A1079 -46.124 42.553 45.006 1.00 60.49 C
ANISOU 2128 CG GLU A1079 6660 8520 7803 462 -123 318 C
ATOM 2129 CD GLU A1079 -47.444 43.072 44.460 1.00 80.55 C
ANISOU 2129 CD GLU A1079 9214 11030 10362 486 -113 289 C
ATOM 2130 OE1 GLU A1079 -47.453 43.620 43.337 1.00 92.71 O
ANISOU 2130 OE1 GLU A1079 10797 12506 11924 467 -136 225 O
ATOM 2131 OE2 GLU A1079 -48.475 42.935 45.157 1.00 54.81 O
ANISOU 2131 OE2 GLU A1079 5919 7814 7094 527 -80 334 O
ATOM 2132 N GLU A1080 -45.446 39.769 43.501 1.00 46.97 N
ANISOU 2132 N GLU A1080 4846 6686 6313 400 -119 413 N
ATOM 2133 CA GLU A1080 -45.282 38.380 43.919 1.00 33.70 C
ANISOU 2133 CA GLU A1080 3100 5009 4695 400 -90 504 C
ATOM 2134 C GLU A1080 -44.614 37.516 42.861 1.00 48.14 C
ANISOU 2134 C GLU A1080 4928 6756 6609 367 -99 504 C
ATOM 2135 O GLU A1080 -44.290 36.358 43.145 1.00 67.34 O
ANISOU 2135 O GLU A1080 7314 9179 9092 368 -73 578 O
ATOM 2136 CB GLU A1080 -46.634 37.762 44.277 1.00 55.91 C
ANISOU 2136 CB GLU A1080 5858 7826 7559 419 -56 561 C
ATOM 2137 CG GLU A1080 -47.408 38.474 45.371 1.00 57.15 C
ANISOU 2137 CG GLU A1080 6010 8068 7637 464 -36 576 C
ATOM 2138 CD GLU A1080 -48.721 37.777 45.677 1.00 84.77 C
ANISOU 2138 CD GLU A1080 9442 11571 11197 481 2 645 C
ATOM 2139 OE1 GLU A1080 -48.690 36.576 46.027 1.00 81.18 O
ANISOU 2139 OE1 GLU A1080 8928 11110 10806 476 32 728 O
ATOM 2140 OE2 GLU A1080 -49.783 38.423 45.550 1.00 73.35 O
ANISOU 2140 OE2 GLU A1080 7999 10133 9738 499 4 619 O
ATOM 2141 N THR A1081 -44.413 38.043 41.653 1.00 51.12 N
ANISOU 2141 N THR A1081 5356 7070 6999 343 -130 427 N
ATOM 2142 CA THR A1081 -43.807 37.263 40.580 1.00 47.67 C
ANISOU 2142 CA THR A1081 4926 6552 6635 318 -136 422 C
ATOM 2143 C THR A1081 -42.327 36.990 40.812 1.00 54.26 C
ANISOU 2143 C THR A1081 5760 7407 7450 316 -134 450 C
ATOM 2144 O THR A1081 -41.806 36.002 40.286 1.00 51.73 O
ANISOU 2144 O THR A1081 5428 7032 7194 309 -122 480 O
ATOM 2145 CB THR A1081 -43.994 37.989 39.246 1.00 39.64 C
ANISOU 2145 CB THR A1081 3965 5472 5624 301 -169 333 C
ATOM 2146 OG1 THR A1081 -43.420 39.301 39.330 1.00 41.62 O
ANISOU 2146 OG1 THR A1081 4266 5759 5790 303 -190 278 O
ATOM 2147 CG2 THR A1081 -45.477 38.125 38.910 1.00 61.44 C
ANISOU 2147 CG2 THR A1081 6717 8215 8415 304 -173 313 C
ATOM 2148 N GLY A1082 -41.647 37.825 41.587 1.00 44.50 N
ANISOU 2148 N GLY A1082 4536 6247 6125 322 -147 442 N
ATOM 2149 CA GLY A1082 -40.217 37.696 41.733 1.00 35.06 C
ANISOU 2149 CA GLY A1082 3336 5079 4906 316 -152 465 C
ATOM 2150 C GLY A1082 -39.426 38.385 40.652 1.00 49.43 C
ANISOU 2150 C GLY A1082 5207 6855 6720 291 -181 397 C
ATOM 2151 O GLY A1082 -38.375 37.874 40.247 1.00 53.20 O
ANISOU 2151 O GLY A1082 5676 7316 7223 285 -177 422 O
ATOM 2152 N ALA A1083 -39.893 39.542 40.176 1.00 47.99 N
ANISOU 2152 N ALA A1083 5077 6655 6503 280 -205 317 N
ATOM 2153 CA ALA A1083 -39.239 40.241 39.079 1.00 38.96 C
ANISOU 2153 CA ALA A1083 3984 5463 5356 258 -228 254 C
ATOM 2154 C ALA A1083 -37.930 40.895 39.489 1.00 43.60 C
ANISOU 2154 C ALA A1083 4578 6105 5883 238 -246 250 C
ATOM 2155 O ALA A1083 -37.151 41.277 38.608 1.00 49.36 O
ANISOU 2155 O ALA A1083 5337 6798 6620 219 -259 218 O
ATOM 2156 CB ALA A1083 -40.177 41.298 38.505 1.00 35.29 C
ANISOU 2156 CB ALA A1083 3572 4964 4871 258 -243 178 C
ATOM 2157 N GLN A1084 -37.672 41.030 40.788 1.00 43.91 N
ANISOU 2157 N GLN A1084 4589 6233 5862 241 -249 283 N
ATOM 2158 CA GLN A1084 -36.482 41.728 41.248 1.00 52.78 C
ANISOU 2158 CA GLN A1084 5716 7417 6921 213 -276 273 C
ATOM 2159 C GLN A1084 -35.226 41.060 40.708 1.00 37.97 C
ANISOU 2159 C GLN A1084 3809 5532 5086 203 -272 317 C
ATOM 2160 O GLN A1084 -35.027 39.854 40.882 1.00 44.67 O
ANISOU 2160 O GLN A1084 4606 6386 5979 228 -246 392 O
ATOM 2161 CB GLN A1084 -36.453 41.767 42.775 1.00 43.61 C
ANISOU 2161 CB GLN A1084 4522 6360 5687 224 -280 309 C
ATOM 2162 CG GLN A1084 -35.322 42.618 43.326 1.00 47.17 C
ANISOU 2162 CG GLN A1084 4980 6880 6061 187 -317 287 C
ATOM 2163 CD GLN A1084 -35.359 42.741 44.836 1.00 68.32 C
ANISOU 2163 CD GLN A1084 7637 9667 8655 199 -326 312 C
ATOM 2164 OE1 GLN A1084 -35.235 43.838 45.382 1.00 96.70 O
ANISOU 2164 OE1 GLN A1084 11272 13300 12168 175 -356 253 O
ATOM 2165 NE2 GLN A1084 -35.517 41.613 45.521 1.00 70.12 N
ANISOU 2165 NE2 GLN A1084 7803 9941 8898 238 -298 399 N
ATOM 2166 N GLY A1085 -34.389 41.846 40.036 1.00 34.81 N
ANISOU 2166 N GLY A1085 3439 5113 4673 171 -294 273 N
ATOM 2167 CA GLY A1085 -33.159 41.328 39.475 1.00 42.54 C
ANISOU 2167 CA GLY A1085 4389 6087 5688 164 -288 315 C
ATOM 2168 C GLY A1085 -33.326 40.339 38.344 1.00 44.14 C
ANISOU 2168 C GLY A1085 4594 6202 5975 192 -256 336 C
ATOM 2169 O GLY A1085 -32.395 39.582 38.057 1.00 53.15 O
ANISOU 2169 O GLY A1085 5701 7343 7150 204 -238 391 O
ATOM 2170 N ARG A1086 -34.479 40.322 37.679 1.00 36.81 N
ANISOU 2170 N ARG A1086 3705 5199 5080 205 -248 292 N
ATOM 2171 CA ARG A1086 -34.739 39.377 36.602 1.00 33.15 C
ANISOU 2171 CA ARG A1086 3252 4649 4693 227 -223 300 C
ATOM 2172 C ARG A1086 -34.719 40.082 35.252 1.00 26.75 C
ANISOU 2172 C ARG A1086 2502 3768 3892 218 -234 232 C
ATOM 2173 O ARG A1086 -35.160 41.229 35.132 1.00 33.40 O
ANISOU 2173 O ARG A1086 3386 4609 4696 202 -255 169 O
ATOM 2174 CB ARG A1086 -36.080 38.672 36.799 1.00 26.61 C
ANISOU 2174 CB ARG A1086 2416 3791 3903 246 -209 308 C
ATOM 2175 CG ARG A1086 -36.198 37.390 36.005 1.00 44.23 C
ANISOU 2175 CG ARG A1086 4644 5945 6217 266 -181 336 C
ATOM 2176 CD ARG A1086 -37.308 36.523 36.543 1.00 34.97 C
ANISOU 2176 CD ARG A1086 3442 4761 5085 276 -163 369 C
ATOM 2177 NE ARG A1086 -37.135 36.232 37.964 1.00 63.34 N
ANISOU 2177 NE ARG A1086 6979 8439 8649 287 -150 440 N
ATOM 2178 CZ ARG A1086 -36.538 35.143 38.438 1.00 57.49 C
ANISOU 2178 CZ ARG A1086 6193 7711 7939 307 -118 523 C
ATOM 2179 NH1 ARG A1086 -36.049 34.236 37.603 1.00 50.93 N
ANISOU 2179 NH1 ARG A1086 5371 6808 7171 320 -93 544 N
ATOM 2180 NH2 ARG A1086 -36.428 34.960 39.746 1.00 67.29 N
ANISOU 2180 NH2 ARG A1086 7385 9039 9145 321 -107 587 N
ATOM 2181 N LYS A1087 -34.203 39.388 34.239 1.00 30.94 N
ANISOU 2181 N LYS A1087 3041 4242 4473 235 -214 246 N
ATOM 2182 CA LYS A1087 -34.154 39.939 32.891 1.00 34.39 C
ANISOU 2182 CA LYS A1087 3535 4613 4919 235 -219 188 C
ATOM 2183 C LYS A1087 -35.551 39.930 32.284 1.00 42.98 C
ANISOU 2183 C LYS A1087 4661 5640 6028 245 -227 134 C
ATOM 2184 O LYS A1087 -36.186 38.873 32.180 1.00 33.01 O
ANISOU 2184 O LYS A1087 3386 4342 4815 260 -214 152 O
ATOM 2185 CB LYS A1087 -33.191 39.132 32.021 1.00 37.02 C
ANISOU 2185 CB LYS A1087 3867 4905 5294 259 -191 223 C
ATOM 2186 CG LYS A1087 -31.882 38.751 32.700 1.00 37.89 C
ANISOU 2186 CG LYS A1087 3920 5080 5396 260 -176 300 C
ATOM 2187 CD LYS A1087 -30.977 39.955 32.902 1.00 55.44 C
ANISOU 2187 CD LYS A1087 6137 7360 7567 225 -199 289 C
ATOM 2188 CE LYS A1087 -29.743 39.571 33.692 1.00 51.09 C
ANISOU 2188 CE LYS A1087 5517 6889 7005 223 -191 369 C
ATOM 2189 NZ LYS A1087 -29.034 38.431 33.050 1.00 59.75 N
ANISOU 2189 NZ LYS A1087 6597 7954 8153 267 -149 429 N
ATOM 2190 N VAL A1088 -36.037 41.103 31.887 1.00 37.19 N
ANISOU 2190 N VAL A1088 3973 4897 5259 235 -248 70 N
ATOM 2191 CA VAL A1088 -37.388 41.239 31.357 1.00 26.94 C
ANISOU 2191 CA VAL A1088 2705 3558 3972 246 -259 21 C
ATOM 2192 C VAL A1088 -37.369 42.186 30.165 1.00 29.00 C
ANISOU 2192 C VAL A1088 3028 3777 4215 251 -269 -38 C
ATOM 2193 O VAL A1088 -36.487 43.041 30.040 1.00 33.58 O
ANISOU 2193 O VAL A1088 3627 4369 4763 239 -269 -47 O
ATOM 2194 CB VAL A1088 -38.381 41.748 32.423 1.00 34.13 C
ANISOU 2194 CB VAL A1088 3600 4517 4850 239 -270 14 C
ATOM 2195 CG1 VAL A1088 -38.470 40.779 33.595 1.00 36.03 C
ANISOU 2195 CG1 VAL A1088 3780 4802 5109 240 -257 79 C
ATOM 2196 CG2 VAL A1088 -37.980 43.131 32.897 1.00 54.25 C
ANISOU 2196 CG2 VAL A1088 6174 7106 7332 223 -283 -15 C
ATOM 2197 N ALA A1089 -38.353 42.018 29.283 1.00 28.64 N
ANISOU 2197 N ALA A1089 3010 3683 4191 269 -278 -77 N
ATOM 2198 CA ALA A1089 -38.558 42.910 28.148 1.00 31.10 C
ANISOU 2198 CA ALA A1089 3379 3959 4480 283 -287 -132 C
ATOM 2199 C ALA A1089 -40.021 42.818 27.751 1.00 43.53 C
ANISOU 2199 C ALA A1089 4961 5513 6065 297 -306 -167 C
ATOM 2200 O ALA A1089 -40.579 41.719 27.700 1.00 43.49 O
ANISOU 2200 O ALA A1089 4930 5490 6105 296 -309 -154 O
ATOM 2201 CB ALA A1089 -37.654 42.540 26.970 1.00 43.60 C
ANISOU 2201 CB ALA A1089 4990 5494 6081 299 -273 -132 C
ATOM 2202 N CYS A1090 -40.648 43.960 27.497 1.00 48.68 N
ANISOU 2202 N CYS A1090 5647 6171 6678 308 -317 -208 N
ATOM 2203 CA CYS A1090 -42.084 43.989 27.277 1.00 28.05 C
ANISOU 2203 CA CYS A1090 3031 3557 4069 323 -335 -233 C
ATOM 2204 C CYS A1090 -42.416 44.191 25.807 1.00 34.01 C
ANISOU 2204 C CYS A1090 3830 4270 4821 349 -349 -277 C
ATOM 2205 O CYS A1090 -41.625 44.731 25.030 1.00 57.97 O
ANISOU 2205 O CYS A1090 6912 7281 7835 362 -340 -293 O
ATOM 2206 CB CYS A1090 -42.740 45.091 28.100 1.00 22.28 C
ANISOU 2206 CB CYS A1090 2303 2870 3294 329 -335 -243 C
ATOM 2207 SG CYS A1090 -42.514 44.883 29.865 1.00 46.93 S
ANISOU 2207 SG CYS A1090 5375 6052 6406 306 -322 -195 S
ATOM 2208 N PHE A1091 -43.607 43.740 25.441 1.00 29.13 N
ANISOU 2208 N PHE A1091 3196 3647 4223 357 -372 -294 N
ATOM 2209 CA PHE A1091 -44.137 43.891 24.101 1.00 27.17 C
ANISOU 2209 CA PHE A1091 2984 3372 3966 382 -394 -337 C
ATOM 2210 C PHE A1091 -45.643 44.075 24.215 1.00 37.43 C
ANISOU 2210 C PHE A1091 4255 4703 5264 391 -419 -349 C
ATOM 2211 O PHE A1091 -46.222 43.971 25.300 1.00 43.31 O
ANISOU 2211 O PHE A1091 4951 5484 6020 377 -414 -321 O
ATOM 2212 CB PHE A1091 -43.765 42.692 23.223 1.00 29.17 C
ANISOU 2212 CB PHE A1091 3248 3577 4260 377 -402 -346 C
ATOM 2213 CG PHE A1091 -44.347 41.391 23.694 1.00 37.57 C
ANISOU 2213 CG PHE A1091 4260 4633 5382 347 -414 -327 C
ATOM 2214 CD1 PHE A1091 -43.753 40.682 24.726 1.00 35.29 C
ANISOU 2214 CD1 PHE A1091 3934 4349 5127 323 -390 -278 C
ATOM 2215 CD2 PHE A1091 -45.487 40.874 23.101 1.00 26.76 C
ANISOU 2215 CD2 PHE A1091 2878 3254 4036 341 -450 -356 C
ATOM 2216 CE1 PHE A1091 -44.289 39.485 25.163 1.00 40.93 C
ANISOU 2216 CE1 PHE A1091 4602 5050 5899 296 -394 -255 C
ATOM 2217 CE2 PHE A1091 -46.026 39.676 23.531 1.00 36.96 C
ANISOU 2217 CE2 PHE A1091 4122 4532 5389 306 -460 -337 C
ATOM 2218 CZ PHE A1091 -45.427 38.980 24.563 1.00 38.96 C
ANISOU 2218 CZ PHE A1091 4342 4782 5679 285 -428 -285 C
ATOM 2219 N GLY A1092 -46.280 44.361 23.097 1.00 30.39 N
ANISOU 2219 N GLY A1092 3389 3803 4355 418 -443 -386 N
ATOM 2220 CA GLY A1092 -47.711 44.569 23.101 1.00 49.74 C
ANISOU 2220 CA GLY A1092 5806 6291 6803 429 -468 -394 C
ATOM 2221 C GLY A1092 -48.149 45.363 21.900 1.00 47.58 C
ANISOU 2221 C GLY A1092 5575 6018 6485 474 -486 -431 C
ATOM 2222 O GLY A1092 -47.364 46.063 21.257 1.00 55.92 O
ANISOU 2222 O GLY A1092 6691 7052 7505 500 -469 -446 O
ATOM 2223 N CYS A1093 -49.436 45.248 21.592 1.00 53.09 N
ANISOU 2223 N CYS A1093 6236 6747 7187 482 -521 -441 N
ATOM 2224 CA CYS A1093 -50.017 45.897 20.430 1.00 58.69 C
ANISOU 2224 CA CYS A1093 6975 7470 7853 528 -544 -472 C
ATOM 2225 C CYS A1093 -50.926 47.041 20.860 1.00 63.30 C
ANISOU 2225 C CYS A1093 7544 8106 8399 569 -532 -456 C
ATOM 2226 O CYS A1093 -51.493 47.037 21.959 1.00 65.26 O
ANISOU 2226 O CYS A1093 7742 8388 8664 557 -521 -424 O
ATOM 2227 CB CYS A1093 -50.808 44.904 19.577 1.00 47.81 C
ANISOU 2227 CB CYS A1093 5568 6095 6503 509 -600 -500 C
ATOM 2228 SG CYS A1093 -49.887 43.415 19.136 1.00 65.77 S
ANISOU 2228 SG CYS A1093 7862 8300 8826 462 -611 -521 S
ATOM 2229 N GLY A1094 -51.053 48.015 19.978 1.00 38.98 N
ANISOU 2229 N GLY A1094 4512 5032 5268 624 -531 -473 N
ATOM 2230 CA GLY A1094 -51.899 49.173 20.201 1.00 46.59 C
ANISOU 2230 CA GLY A1094 5473 6038 6189 677 -514 -458 C
ATOM 2231 C GLY A1094 -52.295 49.752 18.875 1.00 52.34 C
ANISOU 2231 C GLY A1094 6235 6779 6872 733 -533 -479 C
ATOM 2232 O GLY A1094 -52.384 49.035 17.874 1.00 60.93 O
ANISOU 2232 O GLY A1094 7321 7863 7965 725 -576 -507 O
ATOM 2233 N ASP A1095 -52.525 51.062 18.859 1.00 44.54 N
ANISOU 2233 N ASP A1095 5284 5803 5835 795 -499 -467 N
ATOM 2234 CA ASP A1095 -52.900 51.757 17.633 1.00 51.70 C
ANISOU 2234 CA ASP A1095 6226 6727 6692 861 -508 -478 C
ATOM 2235 C ASP A1095 -52.476 53.211 17.767 1.00 51.06 C
ANISOU 2235 C ASP A1095 6216 6618 6567 915 -447 -464 C
ATOM 2236 O ASP A1095 -52.876 53.883 18.722 1.00 65.50 O
ANISOU 2236 O ASP A1095 8038 8460 8388 931 -414 -442 O
ATOM 2237 CB ASP A1095 -54.407 51.646 17.379 1.00 62.68 C
ANISOU 2237 CB ASP A1095 7549 8193 8074 890 -550 -467 C
ATOM 2238 CG ASP A1095 -54.799 52.086 15.983 1.00 76.20 C
ANISOU 2238 CG ASP A1095 9286 9931 9734 953 -575 -481 C
ATOM 2239 OD1 ASP A1095 -54.318 51.469 15.009 1.00 74.86 O
ANISOU 2239 OD1 ASP A1095 9142 9742 9561 938 -608 -514 O
ATOM 2240 OD2 ASP A1095 -55.599 53.038 15.862 1.00 59.41 O
ANISOU 2240 OD2 ASP A1095 7157 7850 7567 1023 -559 -456 O
ATOM 2241 N SER A1096 -51.670 53.692 16.813 1.00 52.56 N
ANISOU 2241 N SER A1096 6475 6768 6727 942 -430 -477 N
ATOM 2242 CA SER A1096 -51.140 55.053 16.878 1.00 50.16 C
ANISOU 2242 CA SER A1096 6245 6424 6389 985 -369 -464 C
ATOM 2243 C SER A1096 -52.233 56.115 16.916 1.00 67.39 C
ANISOU 2243 C SER A1096 8431 8644 8532 1061 -347 -442 C
ATOM 2244 O SER A1096 -51.963 57.249 17.327 1.00 58.43 O
ANISOU 2244 O SER A1096 7352 7472 7376 1090 -291 -430 O
ATOM 2245 CB SER A1096 -50.223 55.325 15.683 1.00 44.42 C
ANISOU 2245 CB SER A1096 5583 5655 5638 1009 -355 -475 C
ATOM 2246 OG SER A1096 -49.115 54.445 15.667 1.00 72.41 O
ANISOU 2246 OG SER A1096 9131 9164 9219 947 -363 -489 O
ATOM 2247 N SER A1097 -53.454 55.780 16.492 1.00 77.72 N
ANISOU 2247 N SER A1097 9679 10021 9828 1094 -390 -435 N
ATOM 2248 CA SER A1097 -54.531 56.764 16.496 1.00 60.47 C
ANISOU 2248 CA SER A1097 7491 7881 7604 1175 -368 -405 C
ATOM 2249 C SER A1097 -54.850 57.240 17.906 1.00 52.34 C
ANISOU 2249 C SER A1097 6452 6850 6585 1173 -326 -384 C
ATOM 2250 O SER A1097 -55.293 58.379 18.089 1.00 71.51 O
ANISOU 2250 O SER A1097 8916 9278 8978 1243 -278 -361 O
ATOM 2251 CB SER A1097 -55.778 56.176 15.837 1.00 57.37 C
ANISOU 2251 CB SER A1097 7020 7575 7202 1201 -430 -399 C
ATOM 2252 OG SER A1097 -55.471 55.601 14.578 1.00 61.35 O
ANISOU 2252 OG SER A1097 7535 8081 7694 1196 -476 -426 O
ATOM 2253 N TRP A1098 -54.626 56.395 18.908 1.00 52.51 N
ANISOU 2253 N TRP A1098 6430 6870 6652 1098 -340 -391 N
ATOM 2254 CA TRP A1098 -54.915 56.756 20.287 1.00 65.82 C
ANISOU 2254 CA TRP A1098 8105 8561 8343 1095 -303 -373 C
ATOM 2255 C TRP A1098 -53.841 57.687 20.838 1.00 59.83 C
ANISOU 2255 C TRP A1098 7439 7726 7569 1087 -245 -386 C
ATOM 2256 O TRP A1098 -52.709 57.730 20.351 1.00 74.22 O
ANISOU 2256 O TRP A1098 9313 9491 9396 1056 -240 -407 O
ATOM 2257 CB TRP A1098 -55.037 55.503 21.152 1.00 62.84 C
ANISOU 2257 CB TRP A1098 7649 8212 8017 1020 -337 -370 C
ATOM 2258 CG TRP A1098 -56.215 54.663 20.773 1.00 61.14 C
ANISOU 2258 CG TRP A1098 7337 8070 7821 1022 -392 -355 C
ATOM 2259 CD1 TRP A1098 -56.277 53.745 19.764 1.00 60.98 C
ANISOU 2259 CD1 TRP A1098 7284 8064 7821 993 -452 -374 C
ATOM 2260 CD2 TRP A1098 -57.509 54.675 21.385 1.00 64.35 C
ANISOU 2260 CD2 TRP A1098 7671 8550 8230 1053 -392 -316 C
ATOM 2261 NE1 TRP A1098 -57.528 53.181 19.715 1.00 64.22 N
ANISOU 2261 NE1 TRP A1098 7602 8550 8248 995 -495 -354 N
ATOM 2262 CE2 TRP A1098 -58.304 53.736 20.698 1.00 59.41 C
ANISOU 2262 CE2 TRP A1098 6961 7980 7631 1033 -457 -313 C
ATOM 2263 CE3 TRP A1098 -58.072 55.388 22.448 1.00 78.81 C
ANISOU 2263 CE3 TRP A1098 9499 10405 10042 1097 -341 -283 C
ATOM 2264 CZ2 TRP A1098 -59.632 53.489 21.041 1.00 64.80 C
ANISOU 2264 CZ2 TRP A1098 7548 8745 8327 1050 -475 -273 C
ATOM 2265 CZ3 TRP A1098 -59.392 55.142 22.788 1.00 91.73 C
ANISOU 2265 CZ3 TRP A1098 11043 12123 11688 1124 -353 -241 C
ATOM 2266 CH2 TRP A1098 -60.156 54.199 22.086 1.00 85.65 C
ANISOU 2266 CH2 TRP A1098 10182 11412 10950 1099 -420 -233 C
ATOM 2267 N GLU A1099 -54.217 58.440 21.877 1.00 46.70 N
ANISOU 2267 N GLU A1099 5794 6063 5886 1115 -200 -372 N
ATOM 2268 CA GLU A1099 -53.345 59.498 22.381 1.00 42.83 C
ANISOU 2268 CA GLU A1099 5399 5500 5375 1114 -144 -388 C
ATOM 2269 C GLU A1099 -52.032 58.934 22.915 1.00 57.15 C
ANISOU 2269 C GLU A1099 7223 7271 7220 1019 -155 -414 C
ATOM 2270 O GLU A1099 -50.972 59.546 22.743 1.00 82.84 O
ANISOU 2270 O GLU A1099 10549 10459 10469 998 -129 -432 O
ATOM 2271 CB GLU A1099 -54.072 60.305 23.461 1.00 75.49 C
ANISOU 2271 CB GLU A1099 9554 9648 9481 1162 -96 -374 C
ATOM 2272 CG GLU A1099 -53.296 61.511 23.993 1.00 88.89 C
ANISOU 2272 CG GLU A1099 11359 11263 11150 1164 -37 -397 C
ATOM 2273 CD GLU A1099 -54.061 62.291 25.058 1.00 80.57 C
ANISOU 2273 CD GLU A1099 10332 10219 10060 1220 12 -387 C
ATOM 2274 OE1 GLU A1099 -55.309 62.214 25.081 1.00 60.15 O
ANISOU 2274 OE1 GLU A1099 7692 7700 7461 1287 14 -352 O
ATOM 2275 OE2 GLU A1099 -53.411 62.981 25.874 1.00 74.24 O
ANISOU 2275 OE2 GLU A1099 9607 9360 9242 1196 49 -415 O
ATOM 2276 N TYR A1100 -52.076 57.763 23.547 1.00 54.70 N
ANISOU 2276 N TYR A1100 6838 6999 6945 962 -191 -410 N
ATOM 2277 CA TYR A1100 -50.893 57.154 24.155 1.00 49.29 C
ANISOU 2277 CA TYR A1100 6152 6286 6289 878 -201 -425 C
ATOM 2278 C TYR A1100 -50.678 55.772 23.546 1.00 40.86 C
ANISOU 2278 C TYR A1100 5022 5237 5267 833 -253 -424 C
ATOM 2279 O TYR A1100 -51.281 54.787 23.983 1.00 28.84 O
ANISOU 2279 O TYR A1100 3424 3762 3773 811 -282 -409 O
ATOM 2280 CB TYR A1100 -51.037 57.090 25.670 1.00 52.44 C
ANISOU 2280 CB TYR A1100 6532 6708 6684 856 -186 -418 C
ATOM 2281 CG TYR A1100 -51.082 58.458 26.307 1.00 54.36 C
ANISOU 2281 CG TYR A1100 6854 6920 6879 894 -134 -430 C
ATOM 2282 CD1 TYR A1100 -49.970 59.288 26.286 1.00 48.75 C
ANISOU 2282 CD1 TYR A1100 6228 6140 6155 868 -108 -457 C
ATOM 2283 CD2 TYR A1100 -52.238 58.925 26.917 1.00 62.24 C
ANISOU 2283 CD2 TYR A1100 7844 7957 7847 958 -107 -412 C
ATOM 2284 CE1 TYR A1100 -50.004 60.544 26.859 1.00 62.76 C
ANISOU 2284 CE1 TYR A1100 8082 7875 7887 898 -60 -474 C
ATOM 2285 CE2 TYR A1100 -52.282 60.181 27.494 1.00 62.76 C
ANISOU 2285 CE2 TYR A1100 7993 7986 7866 998 -54 -426 C
ATOM 2286 CZ TYR A1100 -51.162 60.986 27.461 1.00 64.73 C
ANISOU 2286 CZ TYR A1100 8332 8159 8104 965 -32 -460 C
ATOM 2287 OH TYR A1100 -51.198 62.237 28.033 1.00 82.10 O
ANISOU 2287 OH TYR A1100 10623 10312 10259 1000 20 -480 O
ATOM 2288 N PHE A1101 -49.804 55.708 22.547 1.00 57.34 N
ANISOU 2288 N PHE A1101 7143 7282 7359 820 -260 -439 N
ATOM 2289 CA PHE A1101 -49.557 54.473 21.815 1.00 35.29 C
ANISOU 2289 CA PHE A1101 4309 4498 4604 787 -304 -443 C
ATOM 2290 C PHE A1101 -48.925 53.432 22.727 1.00 48.76 C
ANISOU 2290 C PHE A1101 5970 6205 6350 714 -317 -438 C
ATOM 2291 O PHE A1101 -47.833 53.646 23.266 1.00 66.46 O
ANISOU 2291 O PHE A1101 8242 8416 8595 676 -296 -440 O
ATOM 2292 CB PHE A1101 -48.655 54.757 20.620 1.00 39.30 C
ANISOU 2292 CB PHE A1101 4873 4959 5101 797 -297 -457 C
ATOM 2293 CG PHE A1101 -48.236 53.532 19.874 1.00 32.51 C
ANISOU 2293 CG PHE A1101 3984 4096 4271 766 -335 -466 C
ATOM 2294 CD1 PHE A1101 -49.180 52.657 19.368 1.00 48.79 C
ANISOU 2294 CD1 PHE A1101 5994 6198 6345 775 -381 -471 C
ATOM 2295 CD2 PHE A1101 -46.898 53.266 19.660 1.00 44.13 C
ANISOU 2295 CD2 PHE A1101 5483 5525 5759 730 -323 -469 C
ATOM 2296 CE1 PHE A1101 -48.793 51.532 18.671 1.00 51.65 C
ANISOU 2296 CE1 PHE A1101 6342 6549 6734 747 -414 -486 C
ATOM 2297 CE2 PHE A1101 -46.505 52.146 18.962 1.00 50.43 C
ANISOU 2297 CE2 PHE A1101 6264 6316 6582 710 -351 -477 C
ATOM 2298 CZ PHE A1101 -47.453 51.275 18.468 1.00 51.88 C
ANISOU 2298 CZ PHE A1101 6405 6531 6776 718 -397 -489 C
ATOM 2299 N CYS A1102 -49.611 52.302 22.889 1.00 46.88 N
ANISOU 2299 N CYS A1102 5659 6006 6147 694 -353 -427 N
ATOM 2300 CA CYS A1102 -49.148 51.199 23.732 1.00 58.23 C
ANISOU 2300 CA CYS A1102 7049 7448 7629 632 -364 -414 C
ATOM 2301 C CYS A1102 -48.820 51.676 25.144 1.00 35.17 C
ANISOU 2301 C CYS A1102 4133 4535 4693 615 -332 -400 C
ATOM 2302 O CYS A1102 -47.778 51.346 25.713 1.00 37.70 O
ANISOU 2302 O CYS A1102 4456 4840 5027 569 -325 -396 O
ATOM 2303 CB CYS A1102 -47.945 50.492 23.102 1.00 43.11 C
ANISOU 2303 CB CYS A1102 5151 5490 5739 596 -373 -425 C
ATOM 2304 SG CYS A1102 -48.346 49.487 21.663 1.00 52.76 S
ANISOU 2304 SG CYS A1102 6356 6706 6984 603 -419 -444 S
ATOM 2305 N GLY A1103 -49.724 52.477 25.709 1.00 23.93 N
ANISOU 2305 N GLY A1103 2713 3141 3237 656 -312 -393 N
ATOM 2306 CA GLY A1103 -49.582 52.875 27.097 1.00 36.36 C
ANISOU 2306 CA GLY A1103 4292 4730 4791 646 -285 -383 C
ATOM 2307 C GLY A1103 -49.503 51.705 28.052 1.00 41.27 C
ANISOU 2307 C GLY A1103 4846 5385 5450 599 -298 -356 C
ATOM 2308 O GLY A1103 -48.914 51.833 29.131 1.00 31.76 O
ANISOU 2308 O GLY A1103 3649 4187 4230 574 -281 -350 O
ATOM 2309 N ALA A1104 -50.069 50.558 27.673 1.00 38.50 N
ANISOU 2309 N ALA A1104 4428 5053 5147 585 -328 -339 N
ATOM 2310 CA ALA A1104 -49.950 49.364 28.499 1.00 26.63 C
ANISOU 2310 CA ALA A1104 2861 3571 3687 540 -337 -307 C
ATOM 2311 C ALA A1104 -48.499 48.922 28.611 1.00 41.06 C
ANISOU 2311 C ALA A1104 4707 5364 5529 492 -336 -310 C
ATOM 2312 O ALA A1104 -48.031 48.579 29.702 1.00 38.92 O
ANISOU 2312 O ALA A1104 4414 5114 5260 465 -324 -286 O
ATOM 2313 CB ALA A1104 -50.813 48.244 27.922 1.00 37.83 C
ANISOU 2313 CB ALA A1104 4211 5002 5159 528 -370 -293 C
ATOM 2314 N VAL A1105 -47.772 48.918 27.489 1.00 40.66 N
ANISOU 2314 N VAL A1105 4695 5268 5485 486 -347 -336 N
ATOM 2315 CA VAL A1105 -46.362 48.536 27.512 1.00 27.21 C
ANISOU 2315 CA VAL A1105 3008 3536 3796 447 -343 -333 C
ATOM 2316 C VAL A1105 -45.571 49.473 28.414 1.00 31.53 C
ANISOU 2316 C VAL A1105 3591 4088 4300 436 -318 -335 C
ATOM 2317 O VAL A1105 -44.649 49.048 29.118 1.00 50.28 O
ANISOU 2317 O VAL A1105 5949 6473 6684 398 -314 -316 O
ATOM 2318 CB VAL A1105 -45.792 48.515 26.081 1.00 29.95 C
ANISOU 2318 CB VAL A1105 3395 3836 4151 454 -352 -358 C
ATOM 2319 CG1 VAL A1105 -44.335 48.089 26.089 1.00 32.24 C
ANISOU 2319 CG1 VAL A1105 3693 4099 4456 419 -343 -347 C
ATOM 2320 CG2 VAL A1105 -46.623 47.601 25.190 1.00 48.16 C
ANISOU 2320 CG2 VAL A1105 5671 6137 6492 463 -383 -365 C
ATOM 2321 N ASP A1106 -45.922 50.761 28.413 1.00 40.21 N
ANISOU 2321 N ASP A1106 4742 5184 5353 468 -302 -359 N
ATOM 2322 CA ASP A1106 -45.219 51.722 29.258 1.00 38.01 C
ANISOU 2322 CA ASP A1106 4507 4903 5031 452 -281 -370 C
ATOM 2323 C ASP A1106 -45.489 51.453 30.735 1.00 41.36 C
ANISOU 2323 C ASP A1106 4894 5380 5441 441 -276 -348 C
ATOM 2324 O ASP A1106 -44.562 51.443 31.554 1.00 24.72 O
ANISOU 2324 O ASP A1106 2787 3286 3320 402 -274 -343 O
ATOM 2325 CB ASP A1106 -45.628 53.150 28.885 1.00 41.54 C
ANISOU 2325 CB ASP A1106 5026 5324 5435 494 -259 -402 C
ATOM 2326 CG ASP A1106 -45.498 53.431 27.387 1.00 58.51 C
ANISOU 2326 CG ASP A1106 7210 7428 7593 517 -261 -417 C
ATOM 2327 OD1 ASP A1106 -44.630 52.814 26.728 1.00 53.59 O
ANISOU 2327 OD1 ASP A1106 6578 6783 7000 489 -273 -412 O
ATOM 2328 OD2 ASP A1106 -46.267 54.272 26.867 1.00 54.27 O
ANISOU 2328 OD2 ASP A1106 6710 6880 7030 569 -248 -431 O
ATOM 2329 N ALA A1107 -46.757 51.218 31.090 1.00 33.82 N
ANISOU 2329 N ALA A1107 3902 4461 4487 475 -273 -331 N
ATOM 2330 CA ALA A1107 -47.109 50.990 32.490 1.00 39.47 C
ANISOU 2330 CA ALA A1107 4583 5231 5184 475 -262 -305 C
ATOM 2331 C ALA A1107 -46.485 49.707 33.022 1.00 47.86 C
ANISOU 2331 C ALA A1107 5582 6316 6286 431 -274 -266 C
ATOM 2332 O ALA A1107 -46.032 49.658 34.173 1.00 57.40 O
ANISOU 2332 O ALA A1107 6781 7561 7468 414 -267 -250 O
ATOM 2333 CB ALA A1107 -48.627 50.949 32.650 1.00 23.71 C
ANISOU 2333 CB ALA A1107 2550 3271 3188 524 -253 -285 C
ATOM 2334 N ILE A1108 -46.454 48.659 32.200 1.00 46.29 N
ANISOU 2334 N ILE A1108 5344 6097 6147 415 -293 -251 N
ATOM 2335 CA ILE A1108 -45.849 47.401 32.622 1.00 34.77 C
ANISOU 2335 CA ILE A1108 3831 4650 4732 379 -298 -211 C
ATOM 2336 C ILE A1108 -44.351 47.575 32.820 1.00 28.37 C
ANISOU 2336 C ILE A1108 3046 3829 3903 345 -298 -215 C
ATOM 2337 O ILE A1108 -43.790 47.157 33.840 1.00 54.41 O
ANISOU 2337 O ILE A1108 6314 7166 7194 324 -294 -182 O
ATOM 2338 CB ILE A1108 -46.163 46.296 31.602 1.00 40.63 C
ANISOU 2338 CB ILE A1108 4539 5358 5541 372 -316 -202 C
ATOM 2339 CG1 ILE A1108 -47.673 46.067 31.544 1.00 30.92 C
ANISOU 2339 CG1 ILE A1108 3269 4150 4331 396 -322 -191 C
ATOM 2340 CG2 ILE A1108 -45.428 45.015 31.955 1.00 32.33 C
ANISOU 2340 CG2 ILE A1108 3443 4306 4537 338 -316 -160 C
ATOM 2341 CD1 ILE A1108 -48.111 45.330 30.329 1.00 23.21 C
ANISOU 2341 CD1 ILE A1108 2276 3136 3407 390 -348 -204 C
ATOM 2342 N GLU A1109 -43.682 48.198 31.849 1.00 29.94 N
ANISOU 2342 N GLU A1109 3297 3983 4096 340 -302 -250 N
ATOM 2343 CA GLU A1109 -42.253 48.459 31.983 1.00 33.56 C
ANISOU 2343 CA GLU A1109 3776 4435 4540 304 -302 -251 C
ATOM 2344 C GLU A1109 -41.954 49.350 33.180 1.00 40.92 C
ANISOU 2344 C GLU A1109 4730 5405 5413 290 -296 -261 C
ATOM 2345 O GLU A1109 -40.911 49.193 33.824 1.00 36.11 O
ANISOU 2345 O GLU A1109 4105 4823 4793 254 -302 -244 O
ATOM 2346 CB GLU A1109 -41.711 49.095 30.705 1.00 28.78 C
ANISOU 2346 CB GLU A1109 3225 3774 3937 306 -302 -284 C
ATOM 2347 CG GLU A1109 -40.981 48.120 29.811 1.00 40.04 C
ANISOU 2347 CG GLU A1109 4630 5171 5412 296 -306 -264 C
ATOM 2348 CD GLU A1109 -40.677 48.683 28.436 1.00 58.15 C
ANISOU 2348 CD GLU A1109 6976 7412 7706 312 -303 -294 C
ATOM 2349 OE1 GLU A1109 -41.105 49.820 28.137 1.00 36.13 O
ANISOU 2349 OE1 GLU A1109 4238 4607 4884 332 -297 -327 O
ATOM 2350 OE2 GLU A1109 -40.006 47.976 27.653 1.00 76.44 O
ANISOU 2350 OE2 GLU A1109 9285 9703 10055 309 -302 -280 O
ATOM 2351 N GLU A1110 -42.852 50.285 33.501 1.00 39.65 N
ANISOU 2351 N GLU A1110 4607 5249 5210 320 -286 -290 N
ATOM 2352 CA GLU A1110 -42.623 51.137 34.663 1.00 36.85 C
ANISOU 2352 CA GLU A1110 4284 4927 4792 309 -280 -307 C
ATOM 2353 C GLU A1110 -42.692 50.336 35.960 1.00 44.29 C
ANISOU 2353 C GLU A1110 5167 5938 5723 304 -282 -265 C
ATOM 2354 O GLU A1110 -41.874 50.542 36.864 1.00 40.79 O
ANISOU 2354 O GLU A1110 4727 5531 5240 272 -289 -265 O
ATOM 2355 CB GLU A1110 -43.628 52.285 34.686 1.00 35.31 C
ANISOU 2355 CB GLU A1110 4147 4716 4553 354 -262 -345 C
ATOM 2356 CG GLU A1110 -43.385 53.283 35.807 1.00 31.26 C
ANISOU 2356 CG GLU A1110 3686 4223 3969 344 -254 -376 C
ATOM 2357 CD GLU A1110 -44.553 54.228 36.005 1.00 70.58 C
ANISOU 2357 CD GLU A1110 8718 9194 8906 403 -226 -402 C
ATOM 2358 OE1 GLU A1110 -45.494 54.195 35.181 1.00 62.26 O
ANISOU 2358 OE1 GLU A1110 7658 8121 7878 449 -216 -395 O
ATOM 2359 OE2 GLU A1110 -44.533 54.999 36.989 1.00 83.76 O
ANISOU 2359 OE2 GLU A1110 10435 10880 10512 405 -216 -429 O
ATOM 2360 N LYS A1111 -43.650 49.411 36.068 1.00 34.07 N
ANISOU 2360 N LYS A1111 3816 4666 4463 332 -275 -226 N
ATOM 2361 CA LYS A1111 -43.759 48.609 37.283 1.00 23.92 C
ANISOU 2361 CA LYS A1111 2473 3446 3171 332 -270 -176 C
ATOM 2362 C LYS A1111 -42.585 47.647 37.409 1.00 39.16 C
ANISOU 2362 C LYS A1111 4357 5389 5132 293 -282 -137 C
ATOM 2363 O LYS A1111 -42.001 47.509 38.489 1.00 52.25 O
ANISOU 2363 O LYS A1111 5995 7103 6754 278 -284 -113 O
ATOM 2364 CB LYS A1111 -45.086 47.851 37.302 1.00 28.60 C
ANISOU 2364 CB LYS A1111 3012 4053 3802 368 -256 -139 C
ATOM 2365 CG LYS A1111 -45.618 47.529 38.697 1.00 24.39 C
ANISOU 2365 CG LYS A1111 2438 3591 3238 390 -238 -95 C
ATOM 2366 CD LYS A1111 -47.071 47.067 38.618 1.00 25.49 C
ANISOU 2366 CD LYS A1111 2531 3740 3413 428 -221 -63 C
ATOM 2367 CE LYS A1111 -47.761 47.061 39.974 1.00 38.78 C
ANISOU 2367 CE LYS A1111 4187 5495 5053 463 -194 -24 C
ATOM 2368 NZ LYS A1111 -47.166 46.070 40.911 1.00 43.50 N
ANISOU 2368 NZ LYS A1111 4730 6139 5658 445 -189 35 N
ATOM 2369 N LEU A1112 -42.221 46.976 36.310 1.00 33.95 N
ANISOU 2369 N LEU A1112 3683 4681 4535 280 -288 -128 N
ATOM 2370 CA LEU A1112 -41.080 46.064 36.339 1.00 39.56 C
ANISOU 2370 CA LEU A1112 4353 5400 5277 251 -293 -87 C
ATOM 2371 C LEU A1112 -39.806 46.785 36.760 1.00 39.57 C
ANISOU 2371 C LEU A1112 4379 5426 5231 216 -306 -102 C
ATOM 2372 O LEU A1112 -39.009 46.252 37.541 1.00 39.83 O
ANISOU 2372 O LEU A1112 4369 5510 5254 198 -309 -60 O
ATOM 2373 CB LEU A1112 -40.892 45.410 34.970 1.00 29.11 C
ANISOU 2373 CB LEU A1112 3029 4011 4020 250 -295 -88 C
ATOM 2374 CG LEU A1112 -41.905 44.342 34.559 1.00 31.43 C
ANISOU 2374 CG LEU A1112 3285 4281 4375 269 -290 -65 C
ATOM 2375 CD1 LEU A1112 -41.622 43.842 33.160 1.00 22.84 C
ANISOU 2375 CD1 LEU A1112 2213 3126 3339 267 -295 -79 C
ATOM 2376 CD2 LEU A1112 -41.865 43.195 35.542 1.00 40.28 C
ANISOU 2376 CD2 LEU A1112 4341 5443 5522 267 -277 3 C
ATOM 2377 N LYS A1113 -39.598 48.001 36.251 1.00 38.71 N
ANISOU 2377 N LYS A1113 4335 5283 5092 205 -312 -159 N
ATOM 2378 CA LYS A1113 -38.450 48.798 36.668 1.00 33.58 C
ANISOU 2378 CA LYS A1113 3710 4653 4398 162 -327 -179 C
ATOM 2379 C LYS A1113 -38.516 49.104 38.158 1.00 39.91 C
ANISOU 2379 C LYS A1113 4506 5526 5131 156 -334 -178 C
ATOM 2380 O LYS A1113 -37.522 48.958 38.879 1.00 47.73 O
ANISOU 2380 O LYS A1113 5468 6571 6097 122 -351 -157 O
ATOM 2381 CB LYS A1113 -38.389 50.092 35.854 1.00 28.96 C
ANISOU 2381 CB LYS A1113 3201 4006 3796 154 -327 -241 C
ATOM 2382 CG LYS A1113 -37.177 50.966 36.138 1.00 43.46 C
ANISOU 2382 CG LYS A1113 5065 5850 5597 99 -343 -265 C
ATOM 2383 CD LYS A1113 -37.118 52.172 35.196 1.00 64.28 C
ANISOU 2383 CD LYS A1113 7778 8414 8231 91 -335 -318 C
ATOM 2384 CE LYS A1113 -37.687 53.444 35.830 1.00 53.68 C
ANISOU 2384 CE LYS A1113 6508 7061 6826 94 -331 -376 C
ATOM 2385 NZ LYS A1113 -39.163 53.415 36.043 1.00 60.80 N
ANISOU 2385 NZ LYS A1113 7423 7965 7713 157 -312 -383 N
ATOM 2386 N ASN A1114 -39.690 49.522 38.640 1.00 36.86 N
ANISOU 2386 N ASN A1114 4145 5148 4711 193 -321 -199 N
ATOM 2387 CA ASN A1114 -39.838 49.864 40.049 1.00 35.67 C
ANISOU 2387 CA ASN A1114 4000 5065 4487 197 -323 -202 C
ATOM 2388 C ASN A1114 -39.739 48.644 40.954 1.00 40.72 C
ANISOU 2388 C ASN A1114 4560 5778 5133 206 -321 -130 C
ATOM 2389 O ASN A1114 -39.484 48.798 42.152 1.00 54.64 O
ANISOU 2389 O ASN A1114 6318 7612 6831 201 -330 -124 O
ATOM 2390 CB ASN A1114 -41.166 50.586 40.276 1.00 39.37 C
ANISOU 2390 CB ASN A1114 4517 5522 4919 247 -301 -236 C
ATOM 2391 CG ASN A1114 -41.224 51.934 39.574 1.00 50.22 C
ANISOU 2391 CG ASN A1114 5979 6828 6274 242 -299 -306 C
ATOM 2392 OD1 ASN A1114 -40.239 52.674 39.542 1.00 59.78 O
ANISOU 2392 OD1 ASN A1114 7232 8022 7461 194 -316 -344 O
ATOM 2393 ND2 ASN A1114 -42.381 52.260 39.009 1.00 45.44 N
ANISOU 2393 ND2 ASN A1114 5399 6184 5680 292 -275 -321 N
ATOM 2394 N LEU A1115 -39.927 47.444 40.410 1.00 39.83 N
ANISOU 2394 N LEU A1115 4389 5649 5095 220 -309 -76 N
ATOM 2395 CA LEU A1115 -39.785 46.209 41.166 1.00 29.02 C
ANISOU 2395 CA LEU A1115 2944 4338 3744 230 -301 0 C
ATOM 2396 C LEU A1115 -38.376 45.632 41.091 1.00 39.51 C
ANISOU 2396 C LEU A1115 4235 5687 5092 195 -316 37 C
ATOM 2397 O LEU A1115 -38.148 44.520 41.579 1.00 49.34 O
ANISOU 2397 O LEU A1115 5415 6971 6361 207 -305 108 O
ATOM 2398 CB LEU A1115 -40.803 45.177 40.677 1.00 34.07 C
ANISOU 2398 CB LEU A1115 3543 4944 4458 263 -277 41 C
ATOM 2399 CG LEU A1115 -42.275 45.526 40.914 1.00 31.65 C
ANISOU 2399 CG LEU A1115 3249 4638 4137 303 -258 27 C
ATOM 2400 CD1 LEU A1115 -43.189 44.527 40.223 1.00 29.85 C
ANISOU 2400 CD1 LEU A1115 2978 4369 3994 321 -243 62 C
ATOM 2401 CD2 LEU A1115 -42.586 45.597 42.401 1.00 31.30 C
ANISOU 2401 CD2 LEU A1115 3189 4679 4026 328 -245 56 C
ATOM 2402 N GLY A1116 -37.431 46.357 40.501 1.00 46.96 N
ANISOU 2402 N GLY A1116 5212 6603 6027 156 -337 -3 N
ATOM 2403 CA GLY A1116 -36.054 45.914 40.437 1.00 42.49 C
ANISOU 2403 CA GLY A1116 4606 6064 5476 124 -350 35 C
ATOM 2404 C GLY A1116 -35.708 45.011 39.276 1.00 38.02 C
ANISOU 2404 C GLY A1116 4015 5439 4993 131 -334 68 C
ATOM 2405 O GLY A1116 -34.622 44.416 39.278 1.00 35.18 O
ANISOU 2405 O GLY A1116 3610 5107 4652 118 -336 117 O
ATOM 2406 N ALA A1117 -36.589 44.885 38.289 1.00 39.56 N
ANISOU 2406 N ALA A1117 4236 5558 5236 155 -319 44 N
ATOM 2407 CA ALA A1117 -36.307 44.045 37.138 1.00 37.30 C
ANISOU 2407 CA ALA A1117 3938 5212 5024 164 -305 67 C
ATOM 2408 C ALA A1117 -35.345 44.743 36.187 1.00 47.13 C
ANISOU 2408 C ALA A1117 5218 6420 6270 138 -314 35 C
ATOM 2409 O ALA A1117 -35.376 45.967 36.013 1.00 43.26 O
ANISOU 2409 O ALA A1117 4781 5915 5743 118 -327 -23 O
ATOM 2410 CB ALA A1117 -37.595 43.684 36.402 1.00 29.06 C
ANISOU 2410 CB ALA A1117 2912 4106 4025 194 -292 48 C
ATOM 2411 N GLU A1118 -34.481 43.945 35.568 1.00 39.97 N
ANISOU 2411 N GLU A1118 4283 5496 5410 141 -302 77 N
ATOM 2412 CA GLU A1118 -33.502 44.450 34.611 1.00 34.51 C
ANISOU 2412 CA GLU A1118 3614 4771 4727 122 -303 61 C
ATOM 2413 C GLU A1118 -34.151 44.430 33.234 1.00 50.21 C
ANISOU 2413 C GLU A1118 5650 6672 6754 149 -291 23 C
ATOM 2414 O GLU A1118 -34.246 43.382 32.592 1.00 43.08 O
ANISOU 2414 O GLU A1118 4735 5731 5902 177 -272 49 O
ATOM 2415 CB GLU A1118 -32.225 43.620 34.652 1.00 48.47 C
ANISOU 2415 CB GLU A1118 5325 6572 6519 120 -293 131 C
ATOM 2416 N ILE A1119 -34.618 45.592 32.784 1.00 43.95 N
ANISOU 2416 N ILE A1119 4917 5847 5936 142 -300 -39 N
ATOM 2417 CA ILE A1119 -35.219 45.719 31.458 1.00 32.97 C
ANISOU 2417 CA ILE A1119 3575 4383 4571 170 -291 -77 C
ATOM 2418 C ILE A1119 -34.102 45.678 30.419 1.00 38.52 C
ANISOU 2418 C ILE A1119 4286 5053 5296 169 -278 -63 C
ATOM 2419 O ILE A1119 -33.272 46.588 30.347 1.00 60.68 O
ANISOU 2419 O ILE A1119 7108 7867 8081 140 -280 -71 O
ATOM 2420 CB ILE A1119 -36.041 47.004 31.335 1.00 40.03 C
ANISOU 2420 CB ILE A1119 4528 5256 5426 171 -299 -139 C
ATOM 2421 CG1 ILE A1119 -37.034 47.112 32.495 1.00 38.95 C
ANISOU 2421 CG1 ILE A1119 4379 5161 5259 176 -308 -146 C
ATOM 2422 CG2 ILE A1119 -36.754 47.043 29.995 1.00 52.59 C
ANISOU 2422 CG2 ILE A1119 6160 6781 7040 207 -293 -171 C
ATOM 2423 CD1 ILE A1119 -37.829 48.406 32.485 1.00 22.82 C
ANISOU 2423 CD1 ILE A1119 2397 3101 3174 184 -310 -202 C
ATOM 2424 N VAL A1120 -34.085 44.625 29.602 1.00 37.36 N
ANISOU 2424 N VAL A1120 4132 4869 5195 201 -261 -42 N
ATOM 2425 CA VAL A1120 -32.976 44.412 28.679 1.00 46.97 C
ANISOU 2425 CA VAL A1120 5353 6062 6433 211 -241 -18 C
ATOM 2426 C VAL A1120 -33.195 45.046 27.311 1.00 46.21 C
ANISOU 2426 C VAL A1120 5320 5904 6335 233 -234 -63 C
ATOM 2427 O VAL A1120 -32.222 45.245 26.569 1.00 61.60 O
ANISOU 2427 O VAL A1120 7279 7838 8289 238 -216 -47 O
ATOM 2428 CB VAL A1120 -32.700 42.909 28.498 1.00 29.88 C
ANISOU 2428 CB VAL A1120 3154 3885 4315 240 -220 32 C
ATOM 2429 CG1 VAL A1120 -32.177 42.303 29.791 1.00 33.77 C
ANISOU 2429 CG1 VAL A1120 3578 4444 4807 223 -220 93 C
ATOM 2430 CG2 VAL A1120 -33.961 42.205 28.049 1.00 23.82 C
ANISOU 2430 CG2 VAL A1120 2409 3068 3574 268 -224 2 C
ATOM 2431 N GLN A1121 -34.435 45.359 26.951 1.00 38.79 N
ANISOU 2431 N GLN A1121 4419 4933 5385 251 -247 -113 N
ATOM 2432 CA GLN A1121 -34.726 45.930 25.647 1.00 43.03 C
ANISOU 2432 CA GLN A1121 5016 5419 5915 280 -241 -153 C
ATOM 2433 C GLN A1121 -35.914 46.866 25.766 1.00 43.07 C
ANISOU 2433 C GLN A1121 5056 5420 5890 284 -258 -203 C
ATOM 2434 O GLN A1121 -36.804 46.662 26.596 1.00 49.42 O
ANISOU 2434 O GLN A1121 5838 6249 6691 278 -273 -209 O
ATOM 2435 CB GLN A1121 -35.023 44.850 24.601 1.00 43.55 C
ANISOU 2435 CB GLN A1121 5094 5440 6012 322 -234 -157 C
ATOM 2436 CG GLN A1121 -33.790 44.299 23.918 1.00 40.74 C
ANISOU 2436 CG GLN A1121 4736 5068 5676 339 -205 -119 C
ATOM 2437 CD GLN A1121 -33.213 45.265 22.915 1.00 53.10 C
ANISOU 2437 CD GLN A1121 6346 6610 7219 353 -188 -131 C
ATOM 2438 OE1 GLN A1121 -32.355 46.085 23.247 1.00 78.82 O
ANISOU 2438 OE1 GLN A1121 9593 9892 10463 324 -179 -110 O
ATOM 2439 NE2 GLN A1121 -33.687 45.181 21.676 1.00 51.42 N
ANISOU 2439 NE2 GLN A1121 6184 6352 7000 398 -185 -165 N
ATOM 2440 N ASP A1122 -35.922 47.892 24.924 1.00 43.42 N
ANISOU 2440 N ASP A1122 5153 5432 5911 298 -250 -233 N
ATOM 2441 CA ASP A1122 -37.058 48.796 24.885 1.00 45.90 C
ANISOU 2441 CA ASP A1122 5506 5739 6197 314 -260 -276 C
ATOM 2442 C ASP A1122 -38.287 48.059 24.373 1.00 49.07 C
ANISOU 2442 C ASP A1122 5905 6129 6611 351 -276 -296 C
ATOM 2443 O ASP A1122 -38.191 47.183 23.509 1.00 47.56 O
ANISOU 2443 O ASP A1122 5714 5913 6444 372 -277 -292 O
ATOM 2444 CB ASP A1122 -36.753 50.002 24.003 1.00 48.99 C
ANISOU 2444 CB ASP A1122 5957 6094 6564 328 -242 -296 C
ATOM 2445 CG ASP A1122 -37.810 51.078 24.114 1.00 49.29 C
ANISOU 2445 CG ASP A1122 6037 6124 6568 346 -246 -334 C
ATOM 2446 OD1 ASP A1122 -38.090 51.520 25.250 1.00 45.65 O
ANISOU 2446 OD1 ASP A1122 5567 5689 6088 320 -252 -342 O
ATOM 2447 OD2 ASP A1122 -38.362 51.480 23.066 1.00 50.02 O
ANISOU 2447 OD2 ASP A1122 6171 6187 6648 391 -240 -355 O
ATOM 2448 N GLY A1123 -39.444 48.415 24.924 1.00 48.12 N
ANISOU 2448 N GLY A1123 5782 6027 6473 357 -290 -316 N
ATOM 2449 CA GLY A1123 -40.686 47.726 24.640 1.00 42.33 C
ANISOU 2449 CA GLY A1123 5032 5295 5756 381 -310 -329 C
ATOM 2450 C GLY A1123 -41.026 47.616 23.172 1.00 40.41 C
ANISOU 2450 C GLY A1123 4823 5017 5513 420 -318 -355 C
ATOM 2451 O GLY A1123 -40.849 48.570 22.408 1.00 45.82 O
ANISOU 2451 O GLY A1123 5559 5682 6169 445 -306 -373 O
ATOM 2452 N LEU A1124 -41.506 46.444 22.767 1.00 24.46 N
ANISOU 2452 N LEU A1124 2780 2988 3526 425 -337 -358 N
ATOM 2453 CA LEU A1124 -41.953 46.230 21.396 1.00 34.70 C
ANISOU 2453 CA LEU A1124 4109 4258 4818 460 -353 -390 C
ATOM 2454 C LEU A1124 -43.393 46.712 21.280 1.00 44.73 C
ANISOU 2454 C LEU A1124 5376 5552 6068 482 -378 -415 C
ATOM 2455 O LEU A1124 -44.306 46.107 21.851 1.00 53.55 O
ANISOU 2455 O LEU A1124 6445 6692 7210 466 -399 -411 O
ATOM 2456 CB LEU A1124 -41.831 44.759 21.015 1.00 33.97 C
ANISOU 2456 CB LEU A1124 3999 4140 4768 451 -365 -388 C
ATOM 2457 CG LEU A1124 -42.298 44.437 19.599 1.00 22.60 C
ANISOU 2457 CG LEU A1124 2597 2673 3319 485 -387 -428 C
ATOM 2458 CD1 LEU A1124 -41.425 45.146 18.583 1.00 22.57 C
ANISOU 2458 CD1 LEU A1124 2652 2648 3277 522 -363 -435 C
ATOM 2459 CD2 LEU A1124 -42.277 42.940 19.387 1.00 36.58 C
ANISOU 2459 CD2 LEU A1124 4352 4412 5134 468 -400 -431 C
ATOM 2460 N ARG A1125 -43.600 47.803 20.556 1.00 27.39 N
ANISOU 2460 N ARG A1125 3225 3352 3828 521 -372 -435 N
ATOM 2461 CA ARG A1125 -44.910 48.434 20.443 1.00 38.87 C
ANISOU 2461 CA ARG A1125 4677 4834 5256 552 -389 -451 C
ATOM 2462 C ARG A1125 -45.377 48.307 18.996 1.00 33.07 C
ANISOU 2462 C ARG A1125 3970 4091 4503 593 -413 -480 C
ATOM 2463 O ARG A1125 -44.919 49.042 18.117 1.00 54.78 O
ANISOU 2463 O ARG A1125 6774 6822 7218 631 -396 -489 O
ATOM 2464 CB ARG A1125 -44.839 49.886 20.911 1.00 34.72 C
ANISOU 2464 CB ARG A1125 4185 4314 4692 570 -358 -446 C
ATOM 2465 CG ARG A1125 -44.448 50.021 22.379 1.00 34.54 C
ANISOU 2465 CG ARG A1125 4138 4306 4679 528 -341 -424 C
ATOM 2466 CD ARG A1125 -44.150 51.458 22.768 1.00 29.39 C
ANISOU 2466 CD ARG A1125 3534 3645 3988 538 -309 -428 C
ATOM 2467 NE ARG A1125 -43.823 51.577 24.187 1.00 32.18 N
ANISOU 2467 NE ARG A1125 3867 4018 4341 498 -298 -414 N
ATOM 2468 CZ ARG A1125 -42.639 51.271 24.709 1.00 37.93 C
ANISOU 2468 CZ ARG A1125 4585 4741 5085 452 -291 -398 C
ATOM 2469 NH1 ARG A1125 -42.426 51.411 26.012 1.00 33.86 N
ANISOU 2469 NH1 ARG A1125 4052 4253 4562 419 -286 -387 N
ATOM 2470 NH2 ARG A1125 -41.666 50.823 23.926 1.00 42.22 N
ANISOU 2470 NH2 ARG A1125 5135 5258 5648 442 -289 -390 N
ATOM 2471 N ILE A1126 -46.289 47.368 18.758 1.00 28.43 N
ANISOU 2471 N ILE A1126 3345 3519 3939 585 -455 -495 N
ATOM 2472 CA ILE A1126 -46.794 47.073 17.422 1.00 38.72 C
ANISOU 2472 CA ILE A1126 4668 4821 5222 616 -489 -529 C
ATOM 2473 C ILE A1126 -48.000 47.957 17.140 1.00 50.89 C
ANISOU 2473 C ILE A1126 6203 6407 6725 659 -506 -536 C
ATOM 2474 O ILE A1126 -48.931 48.033 17.951 1.00 64.97 O
ANISOU 2474 O ILE A1126 7935 8229 8521 648 -517 -521 O
ATOM 2475 CB ILE A1126 -47.162 45.585 17.291 1.00 45.13 C
ANISOU 2475 CB ILE A1126 5443 5623 6081 577 -529 -546 C
ATOM 2476 CG1 ILE A1126 -45.916 44.712 17.436 1.00 32.48 C
ANISOU 2476 CG1 ILE A1126 3856 3972 4514 548 -505 -536 C
ATOM 2477 CG2 ILE A1126 -47.843 45.316 15.958 1.00 52.46 C
ANISOU 2477 CG2 ILE A1126 6391 6557 6983 605 -575 -589 C
ATOM 2478 CD1 ILE A1126 -44.871 44.976 16.377 1.00 64.25 C
ANISOU 2478 CD1 ILE A1126 7947 7961 8503 586 -482 -547 C
ATOM 2479 N ASP A1127 -47.989 48.619 15.987 1.00 52.75 N
ANISOU 2479 N ASP A1127 6490 6642 6911 714 -506 -553 N
ATOM 2480 CA ASP A1127 -49.096 49.457 15.547 1.00 45.02 C
ANISOU 2480 CA ASP A1127 5508 5709 5889 767 -521 -555 C
ATOM 2481 C ASP A1127 -49.937 48.674 14.545 1.00 50.34 C
ANISOU 2481 C ASP A1127 6162 6411 6554 775 -583 -588 C
ATOM 2482 O ASP A1127 -49.426 48.232 13.510 1.00 49.11 O
ANISOU 2482 O ASP A1127 6048 6231 6382 787 -597 -616 O
ATOM 2483 CB ASP A1127 -48.583 50.755 14.924 1.00 54.33 C
ANISOU 2483 CB ASP A1127 6756 6872 7014 828 -478 -547 C
ATOM 2484 CG ASP A1127 -49.701 51.727 14.579 1.00 79.74 C
ANISOU 2484 CG ASP A1127 9973 10136 10186 892 -483 -539 C
ATOM 2485 OD1 ASP A1127 -50.868 51.466 14.943 1.00 86.84 O
ANISOU 2485 OD1 ASP A1127 10813 11087 11096 887 -517 -537 O
ATOM 2486 OD2 ASP A1127 -49.408 52.763 13.942 1.00 73.32 O
ANISOU 2486 OD2 ASP A1127 9218 9310 9329 949 -449 -530 O
ATOM 2487 N GLY A1128 -51.218 48.498 14.857 1.00 55.60 N
ANISOU 2487 N GLY A1128 6763 7130 7231 767 -621 -585 N
ATOM 2488 CA GLY A1128 -52.102 47.848 13.914 1.00 58.12 C
ANISOU 2488 CA GLY A1128 7057 7485 7540 769 -688 -618 C
ATOM 2489 C GLY A1128 -51.866 46.350 13.835 1.00 52.13 C
ANISOU 2489 C GLY A1128 6282 6692 6834 702 -724 -649 C
ATOM 2490 O GLY A1128 -51.469 45.697 14.805 1.00 61.39 O
ANISOU 2490 O GLY A1128 7428 7832 8064 647 -706 -633 O
ATOM 2491 N ASP A1129 -52.115 45.805 12.651 1.00 61.83 N
ANISOU 2491 N ASP A1129 7530 7924 8037 710 -775 -694 N
ATOM 2492 CA ASP A1129 -52.028 44.366 12.451 1.00 60.94 C
ANISOU 2492 CA ASP A1129 7410 7774 7971 648 -816 -732 C
ATOM 2493 C ASP A1129 -50.592 43.896 12.669 1.00 67.52 C
ANISOU 2493 C ASP A1129 8295 8529 8830 632 -766 -729 C
ATOM 2494 O ASP A1129 -49.666 44.429 12.039 1.00 70.08 O
ANISOU 2494 O ASP A1129 8689 8830 9110 681 -730 -731 O
ATOM 2495 CB ASP A1129 -52.513 44.009 11.046 1.00 70.77 C
ANISOU 2495 CB ASP A1129 8680 9039 9169 667 -880 -788 C
ATOM 2496 CG ASP A1129 -52.618 42.513 10.818 1.00 66.91 C
ANISOU 2496 CG ASP A1129 8184 8509 8729 598 -929 -836 C
ATOM 2497 OD1 ASP A1129 -53.208 41.811 11.667 1.00 42.25 O
ANISOU 2497 OD1 ASP A1129 4991 5386 5676 530 -949 -824 O
ATOM 2498 OD2 ASP A1129 -52.130 42.047 9.768 1.00 87.69 O
ANISOU 2498 OD2 ASP A1129 10884 11108 11328 614 -947 -886 O
ATOM 2499 N PRO A1130 -50.364 42.919 13.553 1.00 60.19 N
ANISOU 2499 N PRO A1130 7333 7563 7973 567 -759 -717 N
ATOM 2500 CA PRO A1130 -48.981 42.507 13.842 1.00 66.09 C
ANISOU 2500 CA PRO A1130 8122 8246 8744 557 -707 -703 C
ATOM 2501 C PRO A1130 -48.320 41.768 12.693 1.00 70.79 C
ANISOU 2501 C PRO A1130 8785 8790 9321 572 -717 -749 C
ATOM 2502 O PRO A1130 -47.144 42.021 12.399 1.00 70.92 O
ANISOU 2502 O PRO A1130 8857 8773 9315 607 -669 -738 O
ATOM 2503 CB PRO A1130 -49.141 41.615 15.081 1.00 54.33 C
ANISOU 2503 CB PRO A1130 6569 6739 7334 489 -702 -675 C
ATOM 2504 CG PRO A1130 -50.526 41.081 14.977 1.00 58.09 C
ANISOU 2504 CG PRO A1130 6987 7248 7835 453 -766 -697 C
ATOM 2505 CD PRO A1130 -51.348 42.175 14.356 1.00 55.99 C
ANISOU 2505 CD PRO A1130 6718 7050 7504 504 -792 -707 C
ATOM 2506 N ARG A1131 -49.038 40.860 12.030 1.00 58.20 N
ANISOU 2506 N ARG A1131 7189 7189 7736 546 -777 -800 N
ATOM 2507 CA ARG A1131 -48.449 40.140 10.910 1.00 68.60 C
ANISOU 2507 CA ARG A1131 8582 8456 9029 564 -787 -851 C
ATOM 2508 C ARG A1131 -48.012 41.081 9.797 1.00 70.04 C
ANISOU 2508 C ARG A1131 8831 8659 9122 646 -773 -864 C
ATOM 2509 O ARG A1131 -47.142 40.715 8.998 1.00 84.50 O
ANISOU 2509 O ARG A1131 10734 10446 10926 679 -753 -887 O
ATOM 2510 CB ARG A1131 -49.436 39.103 10.374 1.00 65.95 C
ANISOU 2510 CB ARG A1131 8233 8114 8712 516 -864 -912 C
ATOM 2511 CG ARG A1131 -50.878 39.364 10.770 1.00 67.99 C
ANISOU 2511 CG ARG A1131 8405 8442 8985 481 -919 -907 C
ATOM 2512 CD ARG A1131 -51.400 38.293 11.708 1.00 72.51 C
ANISOU 2512 CD ARG A1131 8911 8987 9653 394 -937 -896 C
ATOM 2513 NE ARG A1131 -52.730 38.616 12.218 1.00 66.49 N
ANISOU 2513 NE ARG A1131 8056 8299 8910 364 -978 -875 N
ATOM 2514 CZ ARG A1131 -53.474 37.783 12.939 1.00 70.77 C
ANISOU 2514 CZ ARG A1131 8524 8834 9529 288 -1004 -864 C
ATOM 2515 NH1 ARG A1131 -54.673 38.160 13.363 1.00 77.90 N
ANISOU 2515 NH1 ARG A1131 9339 9813 10445 270 -1037 -837 N
ATOM 2516 NH2 ARG A1131 -53.022 36.570 13.230 1.00 71.82 N
ANISOU 2516 NH2 ARG A1131 8672 8885 9730 233 -992 -873 N
ATOM 2517 N ALA A1132 -48.588 42.286 9.733 1.00 66.63 N
ANISOU 2517 N ALA A1132 8379 8292 8645 685 -778 -844 N
ATOM 2518 CA ALA A1132 -48.123 43.298 8.794 1.00 81.59 C
ANISOU 2518 CA ALA A1132 10336 10206 10460 767 -751 -841 C
ATOM 2519 C ALA A1132 -46.711 43.773 9.122 1.00 85.31 C
ANISOU 2519 C ALA A1132 10844 10635 10936 791 -670 -795 C
ATOM 2520 O ALA A1132 -46.016 44.279 8.233 1.00 90.65 O
ANISOU 2520 O ALA A1132 11582 11303 11556 854 -639 -793 O
ATOM 2521 CB ALA A1132 -49.085 44.487 8.782 1.00 70.74 C
ANISOU 2521 CB ALA A1132 8927 8906 9045 803 -767 -821 C
ATOM 2522 N ALA A1133 -46.268 43.617 10.377 1.00 60.47 N
ANISOU 2522 N ALA A1133 7656 7465 7853 742 -634 -754 N
ATOM 2523 CA ALA A1133 -44.899 43.928 10.781 1.00 53.92 C
ANISOU 2523 CA ALA A1133 6851 6600 7036 752 -564 -709 C
ATOM 2524 C ALA A1133 -44.316 42.720 11.527 1.00 75.69 C
ANISOU 2524 C ALA A1133 9586 9309 9862 697 -551 -699 C
ATOM 2525 O ALA A1133 -44.072 42.780 12.733 1.00 70.04 O
ANISOU 2525 O ALA A1133 8824 8595 9192 657 -526 -658 O
ATOM 2526 CB ALA A1133 -44.848 45.194 11.645 1.00 61.52 C
ANISOU 2526 CB ALA A1133 7786 7591 7997 754 -528 -661 C
ATOM 2527 N ARG A1134 -44.108 41.619 10.801 1.00 85.56 N
ANISOU 2527 N ARG A1134 10875 10518 11117 698 -567 -738 N
ATOM 2528 CA ARG A1134 -43.520 40.397 11.349 1.00 55.97 C
ANISOU 2528 CA ARG A1134 7119 6716 7432 657 -549 -729 C
ATOM 2529 C ARG A1134 -42.008 40.459 11.494 1.00 54.50 C
ANISOU 2529 C ARG A1134 6959 6499 7250 683 -478 -682 C
ATOM 2530 O ARG A1134 -41.463 39.842 12.414 1.00 68.25 O
ANISOU 2530 O ARG A1134 8668 8216 9048 647 -450 -645 O
ATOM 2531 CB ARG A1134 -43.857 39.195 10.468 1.00 60.17 C
ANISOU 2531 CB ARG A1134 7693 7205 7964 652 -590 -793 C
ATOM 2532 CG ARG A1134 -43.807 37.871 11.208 1.00 58.40 C
ANISOU 2532 CG ARG A1134 7443 6928 7820 593 -589 -789 C
ATOM 2533 CD ARG A1134 -43.879 36.693 10.263 1.00 68.65 C
ANISOU 2533 CD ARG A1134 8803 8166 9117 594 -616 -854 C
ATOM 2534 NE ARG A1134 -42.597 36.455 9.610 1.00 69.09 N
ANISOU 2534 NE ARG A1134 8932 8176 9144 653 -560 -848 N
ATOM 2535 CZ ARG A1134 -41.672 35.625 10.078 1.00 95.35 C
ANISOU 2535 CZ ARG A1134 12267 11445 12518 648 -508 -814 C
ATOM 2536 NH1 ARG A1134 -40.531 35.461 9.422 1.00 91.75 N
ANISOU 2536 NH1 ARG A1134 11876 10955 12032 711 -455 -804 N
ATOM 2537 NH2 ARG A1134 -41.889 34.957 11.204 1.00 83.75 N
ANISOU 2537 NH2 ARG A1134 10739 9955 11128 587 -505 -784 N
ATOM 2538 N ASP A1135 -41.318 41.181 10.610 1.00 68.58 N
ANISOU 2538 N ASP A1135 8796 8287 8976 745 -447 -677 N
ATOM 2539 CA ASP A1135 -39.869 41.297 10.731 1.00 70.68 C
ANISOU 2539 CA ASP A1135 9077 8530 9248 768 -379 -624 C
ATOM 2540 C ASP A1135 -39.483 42.096 11.965 1.00 61.95 C
ANISOU 2540 C ASP A1135 7914 7453 8171 734 -349 -565 C
ATOM 2541 O ASP A1135 -38.522 41.749 12.659 1.00 58.23 O
ANISOU 2541 O ASP A1135 7419 6968 7739 715 -310 -518 O
ATOM 2542 CB ASP A1135 -39.279 41.940 9.476 1.00 87.60 C
ANISOU 2542 CB ASP A1135 11286 10674 11322 844 -350 -627 C
ATOM 2543 CG ASP A1135 -39.426 41.063 8.244 1.00 75.86 C
ANISOU 2543 CG ASP A1135 9867 9156 9799 886 -371 -686 C
ATOM 2544 OD1 ASP A1135 -39.336 39.821 8.376 1.00 74.90 O
ANISOU 2544 OD1 ASP A1135 9752 8989 9715 863 -377 -706 O
ATOM 2545 OD2 ASP A1135 -39.621 41.616 7.140 1.00 81.26 O
ANISOU 2545 OD2 ASP A1135 10601 9860 10414 944 -379 -711 O
ATOM 2546 N ASP A1136 -40.217 43.173 12.251 1.00 57.81 N
ANISOU 2546 N ASP A1136 7368 6971 7626 727 -368 -566 N
ATOM 2547 CA ASP A1136 -39.931 43.949 13.450 1.00 50.81 C
ANISOU 2547 CA ASP A1136 6435 6109 6763 692 -345 -519 C
ATOM 2548 C ASP A1136 -40.112 43.109 14.706 1.00 56.47 C
ANISOU 2548 C ASP A1136 7091 6826 7540 631 -356 -502 C
ATOM 2549 O ASP A1136 -39.467 43.370 15.728 1.00 54.87 O
ANISOU 2549 O ASP A1136 6852 6635 7361 602 -328 -457 O
ATOM 2550 CB ASP A1136 -40.823 45.190 13.498 1.00 49.66 C
ANISOU 2550 CB ASP A1136 6286 6002 6582 702 -362 -529 C
ATOM 2551 CG ASP A1136 -40.673 46.059 12.266 1.00 74.86 C
ANISOU 2551 CG ASP A1136 9536 9194 9712 767 -347 -538 C
ATOM 2552 OD1 ASP A1136 -39.543 46.163 11.744 1.00 88.46 O
ANISOU 2552 OD1 ASP A1136 11292 10894 11423 795 -303 -514 O
ATOM 2553 OD2 ASP A1136 -41.685 46.634 11.817 1.00 72.52 O
ANISOU 2553 OD2 ASP A1136 9250 8925 9380 793 -377 -564 O
ATOM 2554 N ILE A1137 -40.969 42.091 14.645 1.00 63.29 N
ANISOU 2554 N ILE A1137 7941 7676 8429 611 -396 -536 N
ATOM 2555 CA ILE A1137 -41.192 41.225 15.799 1.00 53.31 C
ANISOU 2555 CA ILE A1137 6621 6409 7226 557 -403 -515 C
ATOM 2556 C ILE A1137 -40.030 40.258 15.977 1.00 46.46 C
ANISOU 2556 C ILE A1137 5759 5501 6395 555 -363 -482 C
ATOM 2557 O ILE A1137 -39.336 40.277 17.000 1.00 63.49 O
ANISOU 2557 O ILE A1137 7874 7671 8577 532 -332 -430 O
ATOM 2558 CB ILE A1137 -42.523 40.466 15.657 1.00 52.98 C
ANISOU 2558 CB ILE A1137 6561 6363 7207 531 -458 -558 C
ATOM 2559 CG1 ILE A1137 -43.697 41.429 15.521 1.00 56.08 C
ANISOU 2559 CG1 ILE A1137 6938 6805 7563 538 -496 -581 C
ATOM 2560 CG2 ILE A1137 -42.753 39.598 16.858 1.00 36.01 C
ANISOU 2560 CG2 ILE A1137 4351 4208 5123 477 -458 -528 C
ATOM 2561 CD1 ILE A1137 -44.979 40.735 15.119 1.00 56.34 C
ANISOU 2561 CD1 ILE A1137 6955 6842 7611 516 -556 -627 C
ATOM 2562 N VAL A1138 -39.802 39.394 14.982 1.00 48.45 N
ANISOU 2562 N VAL A1138 6060 5704 6644 582 -363 -513 N
ATOM 2563 CA VAL A1138 -38.713 38.423 15.049 1.00 63.47 C
ANISOU 2563 CA VAL A1138 7974 7563 8578 592 -319 -481 C
ATOM 2564 C VAL A1138 -37.338 39.073 15.057 1.00 58.05 C
ANISOU 2564 C VAL A1138 7294 6892 7871 624 -264 -428 C
ATOM 2565 O VAL A1138 -36.342 38.392 15.328 1.00 58.25 O
ANISOU 2565 O VAL A1138 7312 6897 7924 632 -222 -384 O
ATOM 2566 CB VAL A1138 -38.799 37.420 13.880 1.00 48.86 C
ANISOU 2566 CB VAL A1138 6191 5653 6721 622 -329 -533 C
ATOM 2567 CG1 VAL A1138 -40.140 36.702 13.899 1.00 47.94 C
ANISOU 2567 CG1 VAL A1138 6064 5519 6634 578 -388 -586 C
ATOM 2568 CG2 VAL A1138 -38.586 38.130 12.550 1.00 68.29 C
ANISOU 2568 CG2 VAL A1138 8718 8119 9110 683 -327 -566 C
ATOM 2569 N GLY A1139 -37.254 40.366 14.756 1.00 61.53 N
ANISOU 2569 N GLY A1139 7745 7369 8266 642 -261 -427 N
ATOM 2570 CA GLY A1139 -36.013 41.098 14.899 1.00 47.85 C
ANISOU 2570 CA GLY A1139 6006 5654 6521 657 -212 -372 C
ATOM 2571 C GLY A1139 -35.848 41.629 16.306 1.00 49.41 C
ANISOU 2571 C GLY A1139 6137 5894 6743 604 -209 -328 C
ATOM 2572 O GLY A1139 -34.737 41.664 16.841 1.00 51.78 O
ANISOU 2572 O GLY A1139 6408 6209 7058 595 -173 -273 O
ATOM 2573 N TRP A1140 -36.959 42.051 16.915 1.00 56.55 N
ANISOU 2573 N TRP A1140 7016 6823 7646 571 -248 -353 N
ATOM 2574 CA TRP A1140 -36.925 42.457 18.316 1.00 33.56 C
ANISOU 2574 CA TRP A1140 4047 3953 4753 523 -248 -318 C
ATOM 2575 C TRP A1140 -36.541 41.287 19.212 1.00 44.04 C
ANISOU 2575 C TRP A1140 5327 5276 6129 497 -237 -279 C
ATOM 2576 O TRP A1140 -35.823 41.465 20.202 1.00 47.58 O
ANISOU 2576 O TRP A1140 5732 5758 6589 471 -219 -230 O
ATOM 2577 CB TRP A1140 -38.282 43.035 18.728 1.00 50.99 C
ANISOU 2577 CB TRP A1140 6240 6185 6948 504 -288 -352 C
ATOM 2578 CG TRP A1140 -38.373 43.455 20.177 1.00 47.04 C
ANISOU 2578 CG TRP A1140 5687 5727 6458 461 -289 -322 C
ATOM 2579 CD1 TRP A1140 -37.966 44.642 20.715 1.00 35.07 C
ANISOU 2579 CD1 TRP A1140 4170 4240 4916 447 -276 -308 C
ATOM 2580 CD2 TRP A1140 -38.916 42.691 21.262 1.00 35.64 C
ANISOU 2580 CD2 TRP A1140 4191 4301 5051 426 -303 -306 C
ATOM 2581 NE1 TRP A1140 -38.214 44.661 22.066 1.00 22.95 N
ANISOU 2581 NE1 TRP A1140 2587 2741 3392 409 -283 -287 N
ATOM 2582 CE2 TRP A1140 -38.798 43.476 22.427 1.00 28.88 C
ANISOU 2582 CE2 TRP A1140 3303 3489 4181 399 -298 -282 C
ATOM 2583 CE3 TRP A1140 -39.484 41.415 21.363 1.00 39.14 C
ANISOU 2583 CE3 TRP A1140 4611 4723 5538 416 -317 -307 C
ATOM 2584 CZ2 TRP A1140 -39.228 43.029 23.676 1.00 40.45 C
ANISOU 2584 CZ2 TRP A1140 4715 4987 5669 369 -305 -257 C
ATOM 2585 CZ3 TRP A1140 -39.909 40.972 22.604 1.00 32.68 C
ANISOU 2585 CZ3 TRP A1140 3735 3932 4749 382 -322 -278 C
ATOM 2586 CH2 TRP A1140 -39.779 41.777 23.744 1.00 38.29 C
ANISOU 2586 CH2 TRP A1140 4415 4694 5439 362 -315 -251 C
ATOM 2587 N ALA A1141 -36.995 40.076 18.872 1.00 48.73 N
ANISOU 2587 N ALA A1141 5931 5831 6754 503 -248 -298 N
ATOM 2588 CA ALA A1141 -36.643 38.904 19.667 1.00 38.60 C
ANISOU 2588 CA ALA A1141 4608 4535 5521 485 -231 -256 C
ATOM 2589 C ALA A1141 -35.168 38.546 19.523 1.00 42.52 C
ANISOU 2589 C ALA A1141 5108 5023 6025 513 -181 -204 C
ATOM 2590 O ALA A1141 -34.557 38.041 20.472 1.00 57.10 O
ANISOU 2590 O ALA A1141 6906 6888 7900 498 -158 -146 O
ATOM 2591 CB ALA A1141 -37.521 37.718 19.271 1.00 32.61 C
ANISOU 2591 CB ALA A1141 3867 3725 4798 481 -254 -294 C
ATOM 2592 N HIS A1142 -34.582 38.796 18.349 1.00 41.89 N
ANISOU 2592 N HIS A1142 5082 4919 5914 558 -161 -218 N
ATOM 2593 CA HIS A1142 -33.158 38.539 18.157 1.00 32.21 C
ANISOU 2593 CA HIS A1142 3856 3691 4692 591 -108 -162 C
ATOM 2594 C HIS A1142 -32.317 39.428 19.063 1.00 45.12 C
ANISOU 2594 C HIS A1142 5433 5389 6320 562 -94 -105 C
ATOM 2595 O HIS A1142 -31.405 38.950 19.748 1.00 58.72 O
ANISOU 2595 O HIS A1142 7109 7134 8066 558 -65 -41 O
ATOM 2596 CB HIS A1142 -32.786 38.754 16.688 1.00 54.73 C
ANISOU 2596 CB HIS A1142 6777 6511 7507 650 -88 -189 C
ATOM 2597 CG HIS A1142 -31.311 38.835 16.437 1.00 47.82 C
ANISOU 2597 CG HIS A1142 5896 5647 6626 686 -31 -125 C
ATOM 2598 ND1 HIS A1142 -30.658 40.031 16.230 1.00 36.03 N
ANISOU 2598 ND1 HIS A1142 4396 4190 5103 688 -15 -101 N
ATOM 2599 CD2 HIS A1142 -30.366 37.870 16.347 1.00 48.93 C
ANISOU 2599 CD2 HIS A1142 6034 5767 6790 723 16 -76 C
ATOM 2600 CE1 HIS A1142 -29.372 39.800 16.031 1.00 50.15 C
ANISOU 2600 CE1 HIS A1142 6171 5985 6898 721 37 -38 C
ATOM 2601 NE2 HIS A1142 -29.169 38.496 16.097 1.00 56.01 N
ANISOU 2601 NE2 HIS A1142 6915 6695 7669 747 58 -21 N
ATOM 2602 N ASP A1143 -32.616 40.731 19.081 1.00 39.07 N
ANISOU 2602 N ASP A1143 4672 4653 5521 542 -114 -128 N
ATOM 2603 CA ASP A1143 -31.849 41.662 19.902 1.00 42.46 C
ANISOU 2603 CA ASP A1143 5056 5137 5941 506 -106 -84 C
ATOM 2604 C ASP A1143 -32.026 41.381 21.390 1.00 44.59 C
ANISOU 2604 C ASP A1143 5260 5448 6232 458 -123 -56 C
ATOM 2605 O ASP A1143 -31.113 41.645 22.183 1.00 44.96 O
ANISOU 2605 O ASP A1143 5259 5544 6281 432 -111 -5 O
ATOM 2606 CB ASP A1143 -32.257 43.101 19.579 1.00 51.44 C
ANISOU 2606 CB ASP A1143 6224 6283 7040 496 -122 -122 C
ATOM 2607 CG ASP A1143 -31.888 43.513 18.164 1.00 75.52 C
ANISOU 2607 CG ASP A1143 9331 9301 10063 547 -97 -134 C
ATOM 2608 OD1 ASP A1143 -32.321 42.838 17.208 1.00 55.63 O
ANISOU 2608 OD1 ASP A1143 6857 6741 7538 592 -98 -167 O
ATOM 2609 OD2 ASP A1143 -31.170 44.523 18.005 1.00120.76 O
ANISOU 2609 OD2 ASP A1143 15062 15045 15776 540 -77 -111 O
ATOM 2610 N VAL A1144 -33.188 40.856 21.790 1.00 49.39 N
ANISOU 2610 N VAL A1144 5865 6046 6856 445 -152 -87 N
ATOM 2611 CA VAL A1144 -33.392 40.486 23.188 1.00 42.80 C
ANISOU 2611 CA VAL A1144 4970 5251 6041 408 -163 -55 C
ATOM 2612 C VAL A1144 -32.475 39.333 23.571 1.00 50.99 C
ANISOU 2612 C VAL A1144 5970 6291 7113 421 -130 11 C
ATOM 2613 O VAL A1144 -31.869 39.334 24.650 1.00 60.39 O
ANISOU 2613 O VAL A1144 7102 7537 8305 398 -124 64 O
ATOM 2614 CB VAL A1144 -34.871 40.143 23.446 1.00 32.52 C
ANISOU 2614 CB VAL A1144 3670 3934 4752 395 -196 -97 C
ATOM 2615 CG1 VAL A1144 -35.046 39.546 24.833 1.00 40.46 C
ANISOU 2615 CG1 VAL A1144 4613 4977 5782 367 -198 -53 C
ATOM 2616 CG2 VAL A1144 -35.732 41.380 23.306 1.00 40.20 C
ANISOU 2616 CG2 VAL A1144 4667 4921 5685 385 -225 -148 C
ATOM 2617 N ARG A1145 -32.355 38.332 22.696 1.00 42.79 N
ANISOU 2617 N ARG A1145 4965 5194 6100 463 -107 8 N
ATOM 2618 CA ARG A1145 -31.429 37.235 22.950 1.00 54.86 C
ANISOU 2618 CA ARG A1145 6466 6717 7661 487 -66 74 C
ATOM 2619 C ARG A1145 -30.005 37.749 23.098 1.00 53.89 C
ANISOU 2619 C ARG A1145 6308 6645 7521 494 -37 135 C
ATOM 2620 O ARG A1145 -29.328 37.459 24.092 1.00 76.49 O
ANISOU 2620 O ARG A1145 9107 9561 10395 481 -24 202 O
ATOM 2621 CB ARG A1145 -31.514 36.203 21.829 1.00 63.11 C
ANISOU 2621 CB ARG A1145 7571 7680 8729 536 -43 51 C
ATOM 2622 CG ARG A1145 -32.748 35.339 21.908 1.00 34.71 C
ANISOU 2622 CG ARG A1145 3990 4032 5165 521 -67 10 C
ATOM 2623 CD ARG A1145 -32.679 34.184 20.931 1.00 42.10 C
ANISOU 2623 CD ARG A1145 4985 4882 6127 565 -41 -9 C
ATOM 2624 NE ARG A1145 -32.809 34.611 19.542 1.00 34.30 N
ANISOU 2624 NE ARG A1145 4071 3860 5102 596 -50 -73 N
ATOM 2625 CZ ARG A1145 -31.785 34.792 18.716 1.00 56.15 C
ANISOU 2625 CZ ARG A1145 6872 6621 7843 648 -12 -56 C
ATOM 2626 NH1 ARG A1145 -30.545 34.579 19.135 1.00 63.51 N
ANISOU 2626 NH1 ARG A1145 7764 7581 8785 671 37 25 N
ATOM 2627 NH2 ARG A1145 -32.003 35.183 17.468 1.00 62.89 N
ANISOU 2627 NH2 ARG A1145 7792 7445 8657 679 -21 -114 N
ATOM 2628 N GLY A1146 -29.534 38.525 22.120 1.00 36.30 N
ANISOU 2628 N GLY A1146 4117 4409 5265 513 -27 117 N
ATOM 2629 CA GLY A1146 -28.200 39.091 22.202 1.00 54.79 C
ANISOU 2629 CA GLY A1146 6422 6801 7595 512 -1 177 C
ATOM 2630 C GLY A1146 -27.994 40.005 23.392 1.00 57.22 C
ANISOU 2630 C GLY A1146 6671 7185 7887 449 -30 196 C
ATOM 2631 O GLY A1146 -26.848 40.284 23.761 1.00 48.74 O
ANISOU 2631 O GLY A1146 5545 6166 6809 436 -14 257 O
ATOM 2632 N ALA A1147 -29.076 40.478 24.007 1.00 42.80 N
ANISOU 2632 N ALA A1147 4849 5366 6047 410 -72 147 N
ATOM 2633 CA ALA A1147 -28.943 41.306 25.194 1.00 31.81 C
ANISOU 2633 CA ALA A1147 3410 4044 4633 352 -99 158 C
ATOM 2634 C ALA A1147 -28.695 40.486 26.453 1.00 49.59 C
ANISOU 2634 C ALA A1147 5593 6348 6899 340 -100 216 C
ATOM 2635 O ALA A1147 -28.270 41.052 27.464 1.00 73.86 O
ANISOU 2635 O ALA A1147 8619 9493 9951 297 -119 240 O
ATOM 2636 CB ALA A1147 -30.189 42.176 25.376 1.00 44.34 C
ANISOU 2636 CB ALA A1147 5033 5620 6194 324 -138 86 C
ATOM 2637 N ILE A1148 -28.938 39.175 26.421 1.00 39.58 N
ANISOU 2637 N ILE A1148 4322 5049 5668 377 -79 240 N
ATOM 2638 CA ILE A1148 -28.711 38.337 27.595 1.00 57.80 C
ANISOU 2638 CA ILE A1148 6565 7404 7991 373 -72 304 C
ATOM 2639 C ILE A1148 -27.846 37.134 27.236 1.00 42.91 C
ANISOU 2639 C ILE A1148 4663 5498 6142 426 -22 372 C
ATOM 2640 O ILE A1148 -27.669 36.219 28.049 1.00 39.32 O
ANISOU 2640 O ILE A1148 4162 5069 5709 439 -5 432 O
ATOM 2641 CB ILE A1148 -30.042 37.880 28.216 1.00 48.14 C
ANISOU 2641 CB ILE A1148 5346 6164 6781 362 -93 276 C
ATOM 2642 CG1 ILE A1148 -30.893 37.151 27.178 1.00 40.76 C
ANISOU 2642 CG1 ILE A1148 4471 5134 5881 393 -83 230 C
ATOM 2643 CG2 ILE A1148 -30.788 39.060 28.801 1.00 39.61 C
ANISOU 2643 CG2 ILE A1148 4271 5120 5660 316 -136 224 C
ATOM 2644 CD1 ILE A1148 -32.044 36.384 27.783 1.00 33.10 C
ANISOU 2644 CD1 ILE A1148 3491 4144 4940 384 -94 223 C
ATOM 2645 N ARG A1149 -27.296 37.136 26.025 1.00 40.51 N
ANISOU 2645 N ARG A1149 4400 5149 5842 464 7 366 N
ATOM 2646 CA ARG A1149 -26.573 35.978 25.513 1.00 42.30 C
ANISOU 2646 CA ARG A1149 4630 5341 6102 527 61 421 C
ATOM 2647 C ARG A1149 -25.326 35.703 26.347 1.00 48.60 C
ANISOU 2647 C ARG A1149 5342 6221 6901 534 85 523 C
ATOM 2648 O ARG A1149 -24.540 36.611 26.629 1.00 44.56 O
ANISOU 2648 O ARG A1149 4785 5783 6363 502 71 548 O
ATOM 2649 CB ARG A1149 -26.198 36.213 24.049 1.00 55.06 C
ANISOU 2649 CB ARG A1149 6307 6902 7710 568 87 394 C
ATOM 2650 CG ARG A1149 -25.775 34.975 23.278 1.00 64.60 C
ANISOU 2650 CG ARG A1149 7551 8047 8949 643 144 424 C
ATOM 2651 CD ARG A1149 -25.726 35.262 21.781 1.00 76.92 C
ANISOU 2651 CD ARG A1149 9189 9546 10491 684 161 375 C
ATOM 2652 NE ARG A1149 -27.016 35.727 21.274 1.00 89.82 N
ANISOU 2652 NE ARG A1149 10887 11133 12110 658 116 275 N
ATOM 2653 CZ ARG A1149 -27.222 36.173 20.038 1.00 96.90 C
ANISOU 2653 CZ ARG A1149 11853 11986 12980 685 116 219 C
ATOM 2654 NH1 ARG A1149 -26.219 36.223 19.170 1.00118.70 N
ANISOU 2654 NH1 ARG A1149 14632 14741 15727 739 163 252 N
ATOM 2655 NH2 ARG A1149 -28.432 36.575 19.669 1.00 59.41 N
ANISOU 2655 NH2 ARG A1149 7153 7205 8217 662 71 134 N
ATOM 2656 N ARG A1150 -25.150 34.444 26.741 1.00 34.03 N
ANISOU 2656 N ARG A1150 3474 4365 5090 575 121 583 N
ATOM 2657 CA ARG A1150 -23.978 34.057 27.510 1.00 37.88 C
ANISOU 2657 CA ARG A1150 3878 4935 5580 593 148 689 C
ATOM 2658 C ARG A1150 -22.709 34.278 26.693 1.00 43.10 C
ANISOU 2658 C ARG A1150 4528 5613 6236 631 187 735 C
ATOM 2659 O ARG A1150 -22.748 34.466 25.474 1.00 64.86 O
ANISOU 2659 O ARG A1150 7351 8302 8991 658 204 690 O
ATOM 2660 CB ARG A1150 -24.091 32.599 27.947 1.00 48.87 C
ANISOU 2660 CB ARG A1150 5260 6296 7014 642 190 746 C
ATOM 2661 CG ARG A1150 -25.134 32.391 29.022 1.00 61.72 C
ANISOU 2661 CG ARG A1150 6870 7934 8646 603 157 731 C
ATOM 2662 CD ARG A1150 -25.479 30.931 29.196 1.00 54.73 C
ANISOU 2662 CD ARG A1150 5998 6983 7813 650 202 770 C
ATOM 2663 NE ARG A1150 -26.124 30.374 28.013 1.00 77.10 N
ANISOU 2663 NE ARG A1150 8924 9689 10680 676 222 704 N
ATOM 2664 CZ ARG A1150 -26.862 29.270 28.026 1.00 61.28 C
ANISOU 2664 CZ ARG A1150 6956 7601 8727 693 244 698 C
ATOM 2665 NH1 ARG A1150 -27.051 28.617 29.165 1.00 35.44 N
ANISOU 2665 NH1 ARG A1150 3631 4358 5477 691 256 761 N
ATOM 2666 NH2 ARG A1150 -27.416 28.825 26.906 1.00 60.44 N
ANISOU 2666 NH2 ARG A1150 6938 7382 8646 710 254 629 N
ATOM 2667 N PHE A 213 -21.568 34.267 27.382 1.00 28.60 N
ANISOU 2667 N PHE A 213 3991 3629 3248 850 955 -1350 N
ATOM 2668 CA PHE A 213 -20.311 34.559 26.707 1.00 45.32 C
ANISOU 2668 CA PHE A 213 6103 5784 5333 873 1006 -1327 C
ATOM 2669 C PHE A 213 -20.023 33.508 25.643 1.00 38.97 C
ANISOU 2669 C PHE A 213 5369 4947 4491 885 1081 -1282 C
ATOM 2670 O PHE A 213 -20.249 32.312 25.848 1.00 50.11 O
ANISOU 2670 O PHE A 213 6810 6331 5899 896 1112 -1227 O
ATOM 2671 CB PHE A 213 -19.158 34.636 27.718 1.00 44.56 C
ANISOU 2671 CB PHE A 213 5936 5756 5239 888 1057 -1275 C
ATOM 2672 CG PHE A 213 -18.665 33.298 28.201 1.00 33.81 C
ANISOU 2672 CG PHE A 213 4590 4390 3868 901 1149 -1184 C
ATOM 2673 CD1 PHE A 213 -17.633 32.645 27.547 1.00 30.28 C
ANISOU 2673 CD1 PHE A 213 4136 3947 3423 867 1234 -1142 C
ATOM 2674 CD2 PHE A 213 -19.213 32.708 29.327 1.00 43.86 C
ANISOU 2674 CD2 PHE A 213 5848 5661 5156 908 1141 -1161 C
ATOM 2675 CE1 PHE A 213 -17.172 31.422 27.991 1.00 36.00 C
ANISOU 2675 CE1 PHE A 213 4775 4686 4215 778 1294 -1152 C
ATOM 2676 CE2 PHE A 213 -18.751 31.483 29.779 1.00 52.91 C
ANISOU 2676 CE2 PHE A 213 6999 6812 6292 926 1198 -1071 C
ATOM 2677 CZ PHE A 213 -17.730 30.840 29.110 1.00 33.21 C
ANISOU 2677 CZ PHE A 213 4514 4290 3815 881 1291 -1027 C
ATOM 2678 N ARG A 214 -19.541 33.965 24.488 1.00 38.81 N
ANISOU 2678 N ARG A 214 5355 4942 4448 880 1092 -1309 N
ATOM 2679 CA ARG A 214 -19.178 33.056 23.409 1.00 27.87 C
ANISOU 2679 CA ARG A 214 3978 3552 3059 846 1155 -1304 C
ATOM 2680 C ARG A 214 -18.037 32.152 23.848 1.00 40.79 C
ANISOU 2680 C ARG A 214 5489 5286 4723 813 1207 -1305 C
ATOM 2681 O ARG A 214 -16.908 32.617 24.039 1.00 46.88 O
ANISOU 2681 O ARG A 214 6216 6146 5451 854 1224 -1274 O
ATOM 2682 CB ARG A 214 -18.784 33.833 22.152 1.00 27.88 C
ANISOU 2682 CB ARG A 214 3977 3607 3009 870 1133 -1353 C
ATOM 2683 N ARG A 215 -18.331 30.864 24.019 1.00 52.76 N
ANISOU 2683 N ARG A 215 6938 6829 6280 785 1190 -1344 N
ATOM 2684 CA ARG A 215 -17.306 29.890 24.358 1.00 43.83 C
ANISOU 2684 CA ARG A 215 5739 5805 5109 836 1201 -1317 C
ATOM 2685 C ARG A 215 -16.198 29.896 23.309 1.00 65.04 C
ANISOU 2685 C ARG A 215 8467 8532 7713 887 1263 -1273 C
ATOM 2686 O ARG A 215 -16.398 30.288 22.155 1.00 78.34 O
ANISOU 2686 O ARG A 215 10208 10197 9362 902 1263 -1292 O
ATOM 2687 CB ARG A 215 -17.911 28.489 24.469 1.00 45.64 C
ANISOU 2687 CB ARG A 215 5940 6045 5359 853 1161 -1349 C
ATOM 2688 CG ARG A 215 -18.315 28.077 25.878 1.00 37.67 C
ANISOU 2688 CG ARG A 215 4868 5074 4371 869 1105 -1344 C
ATOM 2689 CD ARG A 215 -19.462 28.910 26.424 1.00 35.21 C
ANISOU 2689 CD ARG A 215 4623 4778 3977 1006 955 -1297 C
ATOM 2690 NE ARG A 215 -19.929 28.403 27.713 1.00 45.61 N
ANISOU 2690 NE ARG A 215 6085 5999 5245 1095 1009 -1134 N
ATOM 2691 CZ ARG A 215 -20.848 29.000 28.468 1.00 59.02 C
ANISOU 2691 CZ ARG A 215 7888 7537 7001 1025 1095 -1091 C
ATOM 2692 NH1 ARG A 215 -21.209 28.460 29.625 1.00 62.83 N
ANISOU 2692 NH1 ARG A 215 8327 8043 7504 1028 1097 -1080 N
ATOM 2693 NH2 ARG A 215 -21.403 30.139 28.072 1.00 41.15 N
ANISOU 2693 NH2 ARG A 215 5653 5208 4772 960 1090 -1151 N
ATOM 2694 N SER A 216 -15.013 29.461 23.731 1.00 64.19 N
ANISOU 2694 N SER A 216 8330 8486 7574 912 1318 -1210 N
ATOM 2695 CA SER A 216 -13.866 29.427 22.836 1.00 59.52 C
ANISOU 2695 CA SER A 216 7776 7934 6906 953 1363 -1126 C
ATOM 2696 C SER A 216 -14.167 28.563 21.621 1.00 59.96 C
ANISOU 2696 C SER A 216 7875 7968 6938 971 1367 -1159 C
ATOM 2697 O SER A 216 -14.596 27.412 21.747 1.00 83.42 O
ANISOU 2697 O SER A 216 10830 10918 9948 964 1363 -1204 O
ATOM 2698 CB SER A 216 -12.633 28.895 23.568 1.00 79.24 C
ANISOU 2698 CB SER A 216 10235 10482 9389 961 1407 -1040 C
ATOM 2699 OG SER A 216 -12.807 27.540 23.942 1.00 87.76 O
ANISOU 2699 OG SER A 216 11291 11550 10502 955 1414 -1066 O
ATOM 2700 N ARG A 217 -13.961 29.133 20.438 1.00 54.95 N
ANISOU 2700 N ARG A 217 7294 7346 6239 1000 1372 -1137 N
ATOM 2701 CA ARG A 217 -14.127 28.399 19.195 1.00 72.34 C
ANISOU 2701 CA ARG A 217 9538 9538 8409 1022 1381 -1164 C
ATOM 2702 C ARG A 217 -12.931 27.510 18.867 1.00 70.26 C
ANISOU 2702 C ARG A 217 9273 9323 8098 1057 1434 -1094 C
ATOM 2703 O ARG A 217 -12.967 26.807 17.853 1.00 67.22 O
ANISOU 2703 O ARG A 217 8920 8936 7686 1081 1445 -1117 O
ATOM 2704 CB ARG A 217 -14.389 29.377 18.045 1.00 81.16 C
ANISOU 2704 CB ARG A 217 10711 10660 9466 1045 1360 -1166 C
ATOM 2705 N ARG A 218 -11.882 27.510 19.697 1.00 75.91 N
ANISOU 2705 N ARG A 218 9954 10082 8806 1060 1466 -1014 N
ATOM 2706 CA ARG A 218 -10.721 26.640 19.485 1.00 80.32 C
ANISOU 2706 CA ARG A 218 10508 10682 9327 1088 1513 -949 C
ATOM 2707 C ARG A 218 -10.860 25.399 20.365 1.00 70.98 C
ANISOU 2707 C ARG A 218 9289 9469 8211 1070 1518 -982 C
ATOM 2708 O ARG A 218 -10.325 25.315 21.470 1.00 71.95 O
ANISOU 2708 O ARG A 218 9370 9608 8358 1054 1530 -937 O
ATOM 2709 CB ARG A 218 -9.412 27.381 19.757 1.00 75.45 C
ANISOU 2709 CB ARG A 218 9875 10134 8658 1104 1542 -834 C
ATOM 2710 CG ARG A 218 -9.347 28.170 21.055 1.00 88.27 C
ANISOU 2710 CG ARG A 218 11456 11760 10324 1073 1529 -808 C
ATOM 2711 CD ARG A 218 -7.908 28.555 21.361 1.00 93.86 C
ANISOU 2711 CD ARG A 218 12140 12534 10989 1089 1562 -690 C
ATOM 2712 NE ARG A 218 -7.364 29.491 20.379 1.00 72.70 N
ANISOU 2712 NE ARG A 218 9484 9911 8228 1129 1570 -621 N
ATOM 2713 CZ ARG A 218 -6.103 29.913 20.370 1.00 83.47 C
ANISOU 2713 CZ ARG A 218 10829 11344 9543 1149 1595 -509 C
ATOM 2714 NH1 ARG A 218 -5.694 30.772 19.446 1.00 67.63 N
ANISOU 2714 NH1 ARG A 218 8837 9399 7459 1188 1598 -442 N
ATOM 2715 NH2 ARG A 218 -5.248 29.473 21.283 1.00 86.62 N
ANISOU 2715 NH2 ARG A 218 11190 11754 9969 1131 1615 -460 N
ATOM 2716 N THR A 219 -11.589 24.416 19.848 1.00 71.55 N
ANISOU 2716 N THR A 219 9375 9499 8310 1076 1508 -1059 N
ATOM 2717 CA THR A 219 -11.733 23.119 20.494 1.00 76.04 C
ANISOU 2717 CA THR A 219 9915 10042 8935 1075 1513 -1088 C
ATOM 2718 C THR A 219 -10.749 22.135 19.872 1.00 80.94 C
ANISOU 2718 C THR A 219 10551 10685 9517 1116 1557 -1053 C
ATOM 2719 O THR A 219 -10.683 22.008 18.645 1.00 95.53 O
ANISOU 2719 O THR A 219 12437 12538 11321 1145 1566 -1071 O
ATOM 2720 CB THR A 219 -13.167 22.601 20.357 1.00 80.37 C
ANISOU 2720 CB THR A 219 10464 10529 9544 1064 1469 -1195 C
ATOM 2721 OG1 THR A 219 -13.493 22.470 18.969 1.00 93.51 O
ANISOU 2721 OG1 THR A 219 12174 12176 11180 1084 1466 -1241 O
ATOM 2722 CG2 THR A 219 -14.146 23.572 21.010 1.00 59.84 C
ANISOU 2722 CG2 THR A 219 7845 7911 6982 1025 1420 -1233 C
ATOM 2723 N GLY A 220 -9.989 21.443 20.716 1.00 70.79 N
ANISOU 2723 N GLY A 220 9235 9414 8249 1119 1584 -1005 N
ATOM 2724 CA GLY A 220 -8.980 20.524 20.230 1.00 71.59 C
ANISOU 2724 CA GLY A 220 9347 9537 8317 1157 1625 -971 C
ATOM 2725 C GLY A 220 -9.541 19.316 19.507 1.00 81.96 C
ANISOU 2725 C GLY A 220 10678 10806 9655 1187 1623 -1052 C
ATOM 2726 O GLY A 220 -9.575 18.217 20.067 1.00 73.78 O
ANISOU 2726 O GLY A 220 9623 9743 8668 1198 1631 -1070 O
ATOM 2727 N ARG A 221 -9.978 19.500 18.256 1.00 68.08 N
ANISOU 2727 N ARG A 221 10460 7200 8209 1064 -1023 826 N
ATOM 2728 CA ARG A 221 -10.528 18.376 17.504 1.00 61.86 C
ANISOU 2728 CA ARG A 221 9558 6404 7543 1126 -1203 771 C
ATOM 2729 C ARG A 221 -9.441 17.402 17.069 1.00 66.40 C
ANISOU 2729 C ARG A 221 10139 6949 8140 1116 -1306 665 C
ATOM 2730 O ARG A 221 -9.715 16.210 16.891 1.00 76.27 O
ANISOU 2730 O ARG A 221 11240 8189 9549 1133 -1445 619 O
ATOM 2731 CB ARG A 221 -11.311 18.876 16.288 1.00 66.76 C
ANISOU 2731 CB ARG A 221 10260 7041 8066 1211 -1249 755 C
ATOM 2732 CG ARG A 221 -12.690 19.411 16.625 1.00 83.48 C
ANISOU 2732 CG ARG A 221 12287 9190 10242 1237 -1204 850 C
ATOM 2733 CD ARG A 221 -13.796 18.603 15.955 1.00 94.05 C
ANISOU 2733 CD ARG A 221 13493 10543 11699 1302 -1357 832 C
ATOM 2734 NE ARG A 221 -13.699 17.170 16.230 1.00109.94 N
ANISOU 2734 NE ARG A 221 15343 12542 13888 1275 -1470 785 N
ATOM 2735 CZ ARG A 221 -14.184 16.575 17.317 1.00 93.52 C
ANISOU 2735 CZ ARG A 221 13090 10466 11976 1232 -1448 838 C
ATOM 2736 NH1 ARG A 221 -14.800 17.289 18.251 1.00 89.35 N
ANISOU 2736 NH1 ARG A 221 12528 9952 11468 1216 -1322 944 N
ATOM 2737 NH2 ARG A 221 -14.049 15.264 17.475 1.00 76.65 N
ANISOU 2737 NH2 ARG A 221 10822 8318 9985 1205 -1545 783 N
ATOM 2738 N LEU A 222 -8.209 17.878 16.890 1.00 70.90 N
ANISOU 2738 N LEU A 222 10817 7555 8568 1046 -1194 593 N
ATOM 2739 CA LEU A 222 -7.153 16.992 16.417 1.00 67.57 C
ANISOU 2739 CA LEU A 222 10332 7164 8176 996 -1235 455 C
ATOM 2740 C LEU A 222 -6.717 16.018 17.504 1.00 56.53 C
ANISOU 2740 C LEU A 222 8766 5758 6957 939 -1264 463 C
ATOM 2741 O LEU A 222 -6.542 14.823 17.238 1.00 58.39 O
ANISOU 2741 O LEU A 222 8871 5990 7324 943 -1377 387 O
ATOM 2742 CB LEU A 222 -5.966 17.810 15.917 1.00 71.66 C
ANISOU 2742 CB LEU A 222 11011 7726 8491 935 -1099 372 C
ATOM 2743 CG LEU A 222 -4.792 16.989 15.382 1.00 62.21 C
ANISOU 2743 CG LEU A 222 9759 6565 7314 882 -1124 222 C
ATOM 2744 CD1 LEU A 222 -5.257 16.007 14.319 1.00 32.53 C
ANISOU 2744 CD1 LEU A 222 5931 2795 3635 945 -1282 140 C
ATOM 2745 CD2 LEU A 222 -3.713 17.904 14.834 1.00 67.43 C
ANISOU 2745 CD2 LEU A 222 10589 7267 7763 821 -980 141 C
ATOM 2746 N VAL A 223 -6.548 16.503 18.735 1.00 44.69 N
ANISOU 2746 N VAL A 223 7269 4249 5461 887 -1164 557 N
ATOM 2747 CA VAL A 223 -6.078 15.631 19.807 1.00 55.72 C
ANISOU 2747 CA VAL A 223 8520 5639 7014 831 -1188 570 C
ATOM 2748 C VAL A 223 -7.153 14.620 20.194 1.00 58.46 C
ANISOU 2748 C VAL A 223 8711 5933 7570 883 -1325 628 C
ATOM 2749 O VAL A 223 -6.851 13.455 20.477 1.00 55.30 O
ANISOU 2749 O VAL A 223 8170 5520 7320 867 -1409 587 O
ATOM 2750 CB VAL A 223 -5.616 16.464 21.014 1.00 60.19 C
ANISOU 2750 CB VAL A 223 9144 6211 7514 754 -1043 656 C
ATOM 2751 CG1 VAL A 223 -5.162 15.554 22.146 1.00 42.18 C
ANISOU 2751 CG1 VAL A 223 6715 3921 5390 700 -1077 677 C
ATOM 2752 CG2 VAL A 223 -4.488 17.379 20.601 1.00 63.91 C
ANISOU 2752 CG2 VAL A 223 9761 6738 7784 692 -909 584 C
ATOM 2753 N VAL A 224 -8.421 15.037 20.211 1.00 48.56 N
ANISOU 2753 N VAL A 224 7463 4658 6328 939 -1333 714 N
ATOM 2754 CA VAL A 224 -9.477 14.075 20.492 1.00 51.56 C
ANISOU 2754 CA VAL A 224 7646 5053 6890 947 -1400 730 C
ATOM 2755 C VAL A 224 -9.608 13.064 19.362 1.00 69.25 C
ANISOU 2755 C VAL A 224 9831 7282 9200 998 -1559 626 C
ATOM 2756 O VAL A 224 -10.094 11.951 19.586 1.00 69.96 O
ANISOU 2756 O VAL A 224 9760 7375 9448 986 -1628 608 O
ATOM 2757 CB VAL A 224 -10.822 14.778 20.757 1.00 40.30 C
ANISOU 2757 CB VAL A 224 6197 3658 5456 969 -1323 821 C
ATOM 2758 CG1 VAL A 224 -10.672 15.784 21.876 1.00 57.10 C
ANISOU 2758 CG1 VAL A 224 8378 5796 7520 916 -1157 916 C
ATOM 2759 CG2 VAL A 224 -11.337 15.447 19.500 1.00 73.13 C
ANISOU 2759 CG2 VAL A 224 10463 7825 9497 1044 -1357 799 C
ATOM 2760 N LEU A 225 -9.178 13.417 18.149 1.00 52.45 N
ANISOU 2760 N LEU A 225 7845 5140 6945 1052 -1612 554 N
ATOM 2761 CA LEU A 225 -9.107 12.422 17.085 1.00 54.14 C
ANISOU 2761 CA LEU A 225 8001 5357 7215 1081 -1743 435 C
ATOM 2762 C LEU A 225 -7.976 11.434 17.340 1.00 51.31 C
ANISOU 2762 C LEU A 225 7550 5003 6942 1020 -1755 347 C
ATOM 2763 O LEU A 225 -8.155 10.220 17.183 1.00 46.63 O
ANISOU 2763 O LEU A 225 6830 4384 6502 1032 -1871 296 O
ATOM 2764 CB LEU A 225 -8.932 13.108 15.730 1.00 52.50 C
ANISOU 2764 CB LEU A 225 7942 5186 6819 1112 -1727 357 C
ATOM 2765 CG LEU A 225 -10.188 13.643 15.036 1.00 62.86 C
ANISOU 2765 CG LEU A 225 9314 6493 8078 1198 -1787 407 C
ATOM 2766 CD1 LEU A 225 -9.811 14.435 13.792 1.00 58.88 C
ANISOU 2766 CD1 LEU A 225 8985 6024 7361 1218 -1747 333 C
ATOM 2767 CD2 LEU A 225 -11.137 12.508 14.681 1.00 62.21 C
ANISOU 2767 CD2 LEU A 225 9078 6395 8162 1237 -1948 382 C
ATOM 2768 N ILE A 226 -6.809 11.937 17.746 1.00 45.15 N
ANISOU 2768 N ILE A 226 6832 4256 6068 955 -1634 328 N
ATOM 2769 CA ILE A 226 -5.679 11.067 18.063 1.00 33.45 C
ANISOU 2769 CA ILE A 226 5259 2785 4667 901 -1639 251 C
ATOM 2770 C ILE A 226 -6.025 10.143 19.220 1.00 47.02 C
ANISOU 2770 C ILE A 226 6824 4455 6587 893 -1701 324 C
ATOM 2771 O ILE A 226 -5.669 8.958 19.221 1.00 55.54 O
ANISOU 2771 O ILE A 226 7787 5515 7801 889 -1781 260 O
ATOM 2772 CB ILE A 226 -4.435 11.915 18.377 1.00 34.01 C
ANISOU 2772 CB ILE A 226 5422 2907 4591 829 -1491 229 C
ATOM 2773 CG1 ILE A 226 -4.057 12.763 17.168 1.00 49.17 C
ANISOU 2773 CG1 ILE A 226 7502 4870 6312 832 -1426 145 C
ATOM 2774 CG2 ILE A 226 -3.272 11.036 18.799 1.00 48.68 C
ANISOU 2774 CG2 ILE A 226 7173 4782 6540 778 -1498 159 C
ATOM 2775 CD1 ILE A 226 -2.993 13.780 17.471 1.00 50.89 C
ANISOU 2775 CD1 ILE A 226 7831 5137 6369 758 -1266 134 C
ATOM 2776 N ILE A 227 -6.726 10.667 20.222 1.00 44.99 N
ANISOU 2776 N ILE A 227 6573 4171 6352 890 -1659 458 N
ATOM 2777 CA ILE A 227 -7.051 9.860 21.390 1.00 40.16 C
ANISOU 2777 CA ILE A 227 5813 3546 5899 851 -1665 519 C
ATOM 2778 C ILE A 227 -8.123 8.832 21.051 1.00 50.06 C
ANISOU 2778 C ILE A 227 6937 4806 7277 868 -1744 489 C
ATOM 2779 O ILE A 227 -8.018 7.660 21.433 1.00 39.88 O
ANISOU 2779 O ILE A 227 5524 3507 6121 840 -1789 457 O
ATOM 2780 CB ILE A 227 -7.471 10.773 22.552 1.00 34.92 C
ANISOU 2780 CB ILE A 227 5178 2907 5183 804 -1527 641 C
ATOM 2781 CG1 ILE A 227 -6.275 11.610 23.003 1.00 43.21 C
ANISOU 2781 CG1 ILE A 227 6350 3945 6122 767 -1454 666 C
ATOM 2782 CG2 ILE A 227 -8.009 9.957 23.704 1.00 39.54 C
ANISOU 2782 CG2 ILE A 227 5616 3506 5901 757 -1503 688 C
ATOM 2783 CD1 ILE A 227 -6.583 12.547 24.132 1.00 50.08 C
ANISOU 2783 CD1 ILE A 227 7260 4839 6929 714 -1310 779 C
ATOM 2784 N LEU A 228 -9.158 9.245 20.315 1.00 51.57 N
ANISOU 2784 N LEU A 228 7163 5011 7422 912 -1763 497 N
ATOM 2785 CA LEU A 228 -10.246 8.328 19.985 1.00 37.60 C
ANISOU 2785 CA LEU A 228 5278 3244 5763 924 -1841 472 C
ATOM 2786 C LEU A 228 -9.761 7.189 19.096 1.00 54.97 C
ANISOU 2786 C LEU A 228 7431 5415 8040 942 -1970 350 C
ATOM 2787 O LEU A 228 -10.098 6.022 19.327 1.00 57.18 O
ANISOU 2787 O LEU A 228 7589 5681 8456 915 -2019 323 O
ATOM 2788 CB LEU A 228 -11.388 9.086 19.311 1.00 61.67 C
ANISOU 2788 CB LEU A 228 8379 6316 8739 975 -1844 504 C
ATOM 2789 CG LEU A 228 -12.360 9.842 20.220 1.00 65.19 C
ANISOU 2789 CG LEU A 228 8814 6789 9168 962 -1730 621 C
ATOM 2790 CD1 LEU A 228 -13.313 10.690 19.387 1.00 68.69 C
ANISOU 2790 CD1 LEU A 228 9321 7254 9524 1028 -1738 646 C
ATOM 2791 CD2 LEU A 228 -13.131 8.883 21.116 1.00 46.37 C
ANISOU 2791 CD2 LEU A 228 6285 4403 6933 919 -1729 647 C
ATOM 2792 N THR A 229 -8.969 7.508 18.068 1.00 48.40 N
ANISOU 2792 N THR A 229 6705 4568 7119 990 -2022 273 N
ATOM 2793 CA THR A 229 -8.452 6.463 17.187 1.00 58.63 C
ANISOU 2793 CA THR A 229 7963 5831 8485 1015 -2139 148 C
ATOM 2794 C THR A 229 -7.549 5.501 17.948 1.00 51.26 C
ANISOU 2794 C THR A 229 6929 4877 7671 970 -2133 121 C
ATOM 2795 O THR A 229 -7.652 4.279 17.791 1.00 51.28 O
ANISOU 2795 O THR A 229 6827 4858 7800 960 -2203 59 O
ATOM 2796 CB THR A 229 -7.697 7.082 16.016 1.00 59.06 C
ANISOU 2796 CB THR A 229 8153 5910 8375 1040 -2128 54 C
ATOM 2797 OG1 THR A 229 -6.667 7.940 16.518 1.00 62.67 O
ANISOU 2797 OG1 THR A 229 8691 6407 8714 993 -1991 70 O
ATOM 2798 CG2 THR A 229 -8.648 7.877 15.138 1.00 62.36 C
ANISOU 2798 CG2 THR A 229 8670 6348 8677 1093 -2153 72 C
ATOM 2799 N PHE A 230 -6.647 6.037 18.773 1.00 44.99 N
ANISOU 2799 N PHE A 230 6170 4087 6836 943 -2050 166 N
ATOM 2800 CA PHE A 230 -5.834 5.175 19.621 1.00 46.02 C
ANISOU 2800 CA PHE A 230 6201 4206 7078 900 -2041 155 C
ATOM 2801 C PHE A 230 -6.713 4.307 20.511 1.00 53.28 C
ANISOU 2801 C PHE A 230 6994 5134 8117 847 -2026 210 C
ATOM 2802 O PHE A 230 -6.447 3.113 20.683 1.00 63.63 O
ANISOU 2802 O PHE A 230 8208 6422 9546 830 -2070 162 O
ATOM 2803 CB PHE A 230 -4.874 6.013 20.467 1.00 40.44 C
ANISOU 2803 CB PHE A 230 5554 3518 6294 867 -1944 210 C
ATOM 2804 CG PHE A 230 -3.867 5.197 21.232 1.00 53.35 C
ANISOU 2804 CG PHE A 230 7096 5146 8030 835 -1947 191 C
ATOM 2805 CD1 PHE A 230 -4.165 4.701 22.492 1.00 57.73 C
ANISOU 2805 CD1 PHE A 230 7558 5706 8670 782 -1911 272 C
ATOM 2806 CD2 PHE A 230 -2.618 4.931 20.693 1.00 73.84 C
ANISOU 2806 CD2 PHE A 230 9685 7784 10587 819 -1926 71 C
ATOM 2807 CE1 PHE A 230 -3.239 3.951 23.197 1.00 57.53 C
ANISOU 2807 CE1 PHE A 230 7454 5676 8730 758 -1918 259 C
ATOM 2808 CE2 PHE A 230 -1.688 4.183 21.393 1.00 63.24 C
ANISOU 2808 CE2 PHE A 230 8250 6438 9341 799 -1933 56 C
ATOM 2809 CZ PHE A 230 -1.998 3.694 22.647 1.00 50.00 C
ANISOU 2809 CZ PHE A 230 6497 4711 7792 792 -1964 162 C
ATOM 2810 N ALA A 231 -7.776 4.888 21.072 1.00 46.67 N
ANISOU 2810 N ALA A 231 6164 4322 7248 826 -1961 307 N
ATOM 2811 CA ALA A 231 -8.695 4.106 21.890 1.00 50.67 C
ANISOU 2811 CA ALA A 231 6566 4826 7859 781 -1948 352 C
ATOM 2812 C ALA A 231 -9.433 3.056 21.071 1.00 59.39 C
ANISOU 2812 C ALA A 231 7603 5904 9060 798 -2052 279 C
ATOM 2813 O ALA A 231 -9.724 1.969 21.582 1.00 68.98 O
ANISOU 2813 O ALA A 231 8726 7094 10390 761 -2072 272 O
ATOM 2814 CB ALA A 231 -9.696 5.024 22.589 1.00 36.91 C
ANISOU 2814 CB ALA A 231 4851 3114 6061 766 -1855 460 C
ATOM 2815 N ALA A 232 -9.737 3.350 19.805 1.00 55.00 N
ANISOU 2815 N ALA A 232 7098 5347 8452 852 -2122 222 N
ATOM 2816 CA ALA A 232 -10.504 2.406 18.999 1.00 45.86 C
ANISOU 2816 CA ALA A 232 5881 4163 7380 865 -2228 153 C
ATOM 2817 C ALA A 232 -9.725 1.123 18.748 1.00 52.06 C
ANISOU 2817 C ALA A 232 6606 4903 8271 858 -2297 56 C
ATOM 2818 O ALA A 232 -10.318 0.043 18.656 1.00 51.62 O
ANISOU 2818 O ALA A 232 6471 4814 8329 839 -2358 22 O
ATOM 2819 CB ALA A 232 -10.910 3.052 17.675 1.00 50.90 C
ANISOU 2819 CB ALA A 232 6601 4814 7926 929 -2294 110 C
ATOM 2820 N PHE A 233 -8.401 1.215 18.640 1.00 52.84 N
ANISOU 2820 N PHE A 233 6739 4997 8339 874 -2288 10 N
ATOM 2821 CA PHE A 233 -7.591 0.037 18.361 1.00 57.80 C
ANISOU 2821 CA PHE A 233 7311 5584 9068 878 -2348 -86 C
ATOM 2822 C PHE A 233 -7.124 -0.679 19.620 1.00 73.98 C
ANISOU 2822 C PHE A 233 9281 7624 11204 824 -2294 -43 C
ATOM 2823 O PHE A 233 -6.970 -1.906 19.603 1.00 81.82 O
ANISOU 2823 O PHE A 233 10202 8575 12310 813 -2340 -98 O
ATOM 2824 CB PHE A 233 -6.368 0.418 17.523 1.00 55.36 C
ANISOU 2824 CB PHE A 233 7073 5268 8693 933 -2374 -175 C
ATOM 2825 CG PHE A 233 -6.691 0.789 16.104 1.00 63.57 C
ANISOU 2825 CG PHE A 233 8194 6299 9660 995 -2455 -252 C
ATOM 2826 CD1 PHE A 233 -7.002 -0.188 15.173 1.00 70.03 C
ANISOU 2826 CD1 PHE A 233 8975 7077 10555 1018 -2560 -352 C
ATOM 2827 CD2 PHE A 233 -6.665 2.113 15.695 1.00 63.65 C
ANISOU 2827 CD2 PHE A 233 8328 6346 9509 1023 -2417 -228 C
ATOM 2828 CE1 PHE A 233 -7.294 0.148 13.864 1.00 84.38 C
ANISOU 2828 CE1 PHE A 233 10875 8910 12276 1054 -2616 -429 C
ATOM 2829 CE2 PHE A 233 -6.953 2.456 14.387 1.00 70.59 C
ANISOU 2829 CE2 PHE A 233 9292 7256 10272 1044 -2447 -306 C
ATOM 2830 CZ PHE A 233 -7.270 1.471 13.470 1.00 84.19 C
ANISOU 2830 CZ PHE A 233 10975 8950 12065 1059 -2549 -406 C
ATOM 2831 N TRP A 234 -6.897 0.050 20.710 1.00 65.70 N
ANISOU 2831 N TRP A 234 8251 6610 10103 793 -2198 54 N
ATOM 2832 CA TRP A 234 -6.272 -0.526 21.893 1.00 44.32 C
ANISOU 2832 CA TRP A 234 5485 3898 7458 749 -2152 93 C
ATOM 2833 C TRP A 234 -7.259 -0.933 22.973 1.00 60.66 C
ANISOU 2833 C TRP A 234 7502 5963 9583 694 -2111 177 C
ATOM 2834 O TRP A 234 -6.968 -1.863 23.731 1.00 75.76 O
ANISOU 2834 O TRP A 234 9355 7853 11580 663 -2108 184 O
ATOM 2835 CB TRP A 234 -5.252 0.455 22.476 1.00 49.05 C
ANISOU 2835 CB TRP A 234 6137 4532 7970 748 -2082 139 C
ATOM 2836 CG TRP A 234 -4.041 0.566 21.619 1.00 60.04 C
ANISOU 2836 CG TRP A 234 7559 5915 9339 799 -2125 43 C
ATOM 2837 CD1 TRP A 234 -3.741 1.567 20.742 1.00 64.45 C
ANISOU 2837 CD1 TRP A 234 8215 6482 9792 846 -2134 7 C
ATOM 2838 CD2 TRP A 234 -2.974 -0.380 21.531 1.00 57.70 C
ANISOU 2838 CD2 TRP A 234 7200 5595 9129 815 -2165 -37 C
ATOM 2839 NE1 TRP A 234 -2.542 1.310 20.123 1.00 49.99 N
ANISOU 2839 NE1 TRP A 234 6384 4631 7979 890 -2175 -97 N
ATOM 2840 CE2 TRP A 234 -2.051 0.119 20.590 1.00 60.36 C
ANISOU 2840 CE2 TRP A 234 7591 5928 9414 873 -2193 -126 C
ATOM 2841 CE3 TRP A 234 -2.706 -1.599 22.160 1.00 57.43 C
ANISOU 2841 CE3 TRP A 234 7074 5538 9209 790 -2176 -43 C
ATOM 2842 CZ2 TRP A 234 -0.879 -0.557 20.266 1.00 66.01 C
ANISOU 2842 CZ2 TRP A 234 8258 6623 10198 908 -2228 -226 C
ATOM 2843 CZ3 TRP A 234 -1.543 -2.270 21.837 1.00 49.46 C
ANISOU 2843 CZ3 TRP A 234 6020 4510 8262 825 -2212 -133 C
ATOM 2844 CH2 TRP A 234 -0.644 -1.747 20.899 1.00 67.32 C
ANISOU 2844 CH2 TRP A 234 8323 6774 10479 883 -2236 -225 C
ATOM 2845 N LEU A 235 -8.410 -0.268 23.072 1.00 60.35 N
ANISOU 2845 N LEU A 235 7487 5944 9500 685 -2080 239 N
ATOM 2846 CA LEU A 235 -9.430 -0.720 24.018 1.00 59.76 C
ANISOU 2846 CA LEU A 235 7358 5857 9490 638 -2050 305 C
ATOM 2847 C LEU A 235 -9.870 -2.155 23.753 1.00 54.62 C
ANISOU 2847 C LEU A 235 6630 5149 8972 625 -2130 245 C
ATOM 2848 O LEU A 235 -9.928 -2.944 24.713 1.00 55.01 O
ANISOU 2848 O LEU A 235 6631 5174 9098 584 -2112 275 O
ATOM 2849 CB LEU A 235 -10.622 0.243 24.006 1.00 50.68 C
ANISOU 2849 CB LEU A 235 6242 4736 8279 642 -2010 369 C
ATOM 2850 CG LEU A 235 -11.826 -0.152 24.869 1.00 50.50 C
ANISOU 2850 CG LEU A 235 6163 4698 8326 600 -1984 429 C
ATOM 2851 CD1 LEU A 235 -11.473 -0.179 26.348 1.00 45.72 C
ANISOU 2851 CD1 LEU A 235 5550 4100 7724 551 -1899 502 C
ATOM 2852 CD2 LEU A 235 -12.994 0.785 24.618 1.00 40.48 C
ANISOU 2852 CD2 LEU A 235 4921 3455 7003 621 -1959 476 C
ATOM 2853 N PRO A 236 -10.180 -2.568 22.518 1.00 72.20 N
ANISOU 2853 N PRO A 236 8850 7349 11232 660 -2223 160 N
ATOM 2854 CA PRO A 236 -10.531 -3.981 22.311 1.00 61.25 C
ANISOU 2854 CA PRO A 236 7393 5900 9980 645 -2299 101 C
ATOM 2855 C PRO A 236 -9.364 -4.925 22.529 1.00 55.38 C
ANISOU 2855 C PRO A 236 6621 5126 9297 643 -2312 52 C
ATOM 2856 O PRO A 236 -9.577 -6.077 22.924 1.00 67.99 O
ANISOU 2856 O PRO A 236 8160 6672 11003 615 -2338 41 O
ATOM 2857 CB PRO A 236 -11.021 -4.012 20.858 1.00 71.88 C
ANISOU 2857 CB PRO A 236 8752 7231 11327 688 -2397 17 C
ATOM 2858 CG PRO A 236 -10.325 -2.871 20.209 1.00 64.83 C
ANISOU 2858 CG PRO A 236 7941 6386 10305 735 -2380 2 C
ATOM 2859 CD PRO A 236 -10.274 -1.801 21.261 1.00 60.59 C
ANISOU 2859 CD PRO A 236 7440 5901 9682 713 -2267 113 C
ATOM 2860 N TYR A 237 -8.133 -4.475 22.287 1.00 62.06 N
ANISOU 2860 N TYR A 237 7503 5997 10080 674 -2295 23 N
ATOM 2861 CA TYR A 237 -6.987 -5.345 22.514 1.00 54.12 C
ANISOU 2861 CA TYR A 237 6463 4966 9135 679 -2305 -22 C
ATOM 2862 C TYR A 237 -6.768 -5.610 23.996 1.00 69.73 C
ANISOU 2862 C TYR A 237 8412 6948 11135 633 -2237 65 C
ATOM 2863 O TYR A 237 -6.334 -6.703 24.371 1.00 82.87 O
ANISOU 2863 O TYR A 237 10029 8573 12885 626 -2256 44 O
ATOM 2864 CB TYR A 237 -5.735 -4.732 21.890 1.00 60.53 C
ANISOU 2864 CB TYR A 237 7316 5804 9878 727 -2305 -78 C
ATOM 2865 CG TYR A 237 -4.451 -5.438 22.263 1.00 69.68 C
ANISOU 2865 CG TYR A 237 8435 6949 11091 737 -2300 -112 C
ATOM 2866 CD1 TYR A 237 -4.027 -6.563 21.568 1.00 67.03 C
ANISOU 2866 CD1 TYR A 237 8058 6562 10849 767 -2365 -213 C
ATOM 2867 CD2 TYR A 237 -3.659 -4.975 23.306 1.00 68.37 C
ANISOU 2867 CD2 TYR A 237 8273 6820 10886 721 -2233 -43 C
ATOM 2868 CE1 TYR A 237 -2.853 -7.209 21.905 1.00 67.77 C
ANISOU 2868 CE1 TYR A 237 8112 6644 10994 783 -2358 -244 C
ATOM 2869 CE2 TYR A 237 -2.488 -5.616 23.651 1.00 62.22 C
ANISOU 2869 CE2 TYR A 237 7451 6030 10158 735 -2236 -73 C
ATOM 2870 CZ TYR A 237 -2.088 -6.730 22.947 1.00 62.32 C
ANISOU 2870 CZ TYR A 237 7421 5995 10263 769 -2296 -172 C
ATOM 2871 OH TYR A 237 -0.919 -7.370 23.286 1.00 74.16 O
ANISOU 2871 OH TYR A 237 8874 7486 11817 790 -2295 -201 O
ATOM 2872 N HIS A 238 -7.060 -4.636 24.853 1.00 63.60 N
ANISOU 2872 N HIS A 238 7668 6217 10280 606 -2160 161 N
ATOM 2873 CA HIS A 238 -6.801 -4.811 26.275 1.00 60.46 C
ANISOU 2873 CA HIS A 238 7253 5826 9893 564 -2099 241 C
ATOM 2874 C HIS A 238 -7.945 -5.484 27.014 1.00 63.29 C
ANISOU 2874 C HIS A 238 7574 6151 10323 519 -2093 289 C
ATOM 2875 O HIS A 238 -7.733 -5.974 28.129 1.00 68.36 O
ANISOU 2875 O HIS A 238 8195 6782 10996 489 -2062 338 O
ATOM 2876 CB HIS A 238 -6.483 -3.465 26.928 1.00 48.05 C
ANISOU 2876 CB HIS A 238 5737 4314 8205 554 -2017 319 C
ATOM 2877 CG HIS A 238 -5.122 -2.943 26.589 1.00 54.69 C
ANISOU 2877 CG HIS A 238 6606 5182 8992 587 -2017 285 C
ATOM 2878 ND1 HIS A 238 -3.980 -3.370 27.232 1.00 58.70 N
ANISOU 2878 ND1 HIS A 238 7087 5688 9527 586 -2013 286 N
ATOM 2879 CD2 HIS A 238 -4.717 -2.039 25.666 1.00 65.01 C
ANISOU 2879 CD2 HIS A 238 7964 6514 10222 627 -2025 246 C
ATOM 2880 CE1 HIS A 238 -2.932 -2.748 26.724 1.00 48.68 C
ANISOU 2880 CE1 HIS A 238 5844 4445 8209 621 -2019 247 C
ATOM 2881 NE2 HIS A 238 -3.352 -1.935 25.772 1.00 67.85 N
ANISOU 2881 NE2 HIS A 238 8323 6886 10570 646 -2026 221 N
ATOM 2882 N VAL A 239 -9.142 -5.531 26.431 1.00 51.68 N
ANISOU 2882 N VAL A 239 6092 4661 8881 517 -2128 275 N
ATOM 2883 CA VAL A 239 -10.225 -6.248 27.091 1.00 65.19 C
ANISOU 2883 CA VAL A 239 7759 6333 10677 475 -2131 312 C
ATOM 2884 C VAL A 239 -10.119 -7.742 26.824 1.00 60.49 C
ANISOU 2884 C VAL A 239 7110 5668 10206 475 -2205 246 C
ATOM 2885 O VAL A 239 -10.438 -8.561 27.694 1.00 66.05 O
ANISOU 2885 O VAL A 239 7780 6334 10983 441 -2198 280 O
ATOM 2886 CB VAL A 239 -11.592 -5.684 26.667 1.00 69.27 C
ANISOU 2886 CB VAL A 239 8277 6856 11186 472 -2139 329 C
ATOM 2887 CG1 VAL A 239 -11.738 -4.247 27.143 1.00 45.73 C
ANISOU 2887 CG1 VAL A 239 5350 3940 8085 471 -2051 407 C
ATOM 2888 CG2 VAL A 239 -11.767 -5.775 25.166 1.00 57.43 C
ANISOU 2888 CG2 VAL A 239 6780 5342 9701 514 -2227 239 C
ATOM 2889 N VAL A 240 -9.664 -8.131 25.630 1.00 57.84 N
ANISOU 2889 N VAL A 240 6770 5309 9895 516 -2276 150 N
ATOM 2890 CA VAL A 240 -9.401 -9.547 25.404 1.00 69.33 C
ANISOU 2890 CA VAL A 240 8180 6697 11466 521 -2338 85 C
ATOM 2891 C VAL A 240 -8.232 -9.997 26.264 1.00 63.45 C
ANISOU 2891 C VAL A 240 7431 5953 10725 523 -2300 108 C
ATOM 2892 O VAL A 240 -8.146 -11.171 26.641 1.00 79.29 O
ANISOU 2892 O VAL A 240 9401 7905 12823 515 -2323 97 O
ATOM 2893 CB VAL A 240 -9.163 -9.844 23.910 1.00 73.06 C
ANISOU 2893 CB VAL A 240 8652 7143 11964 568 -2423 -29 C
ATOM 2894 CG1 VAL A 240 -10.370 -9.426 23.082 1.00 61.72 C
ANISOU 2894 CG1 VAL A 240 7222 5705 10526 569 -2472 -49 C
ATOM 2895 CG2 VAL A 240 -7.906 -9.160 23.411 1.00 75.84 C
ANISOU 2895 CG2 VAL A 240 9045 7541 12231 613 -2405 -67 C
ATOM 2896 N ASN A 241 -7.322 -9.079 26.600 1.00 54.75 N
ANISOU 2896 N ASN A 241 6366 4911 9526 535 -2244 140 N
ATOM 2897 CA ASN A 241 -6.309 -9.386 27.603 1.00 62.69 C
ANISOU 2897 CA ASN A 241 7366 5923 10531 532 -2207 179 C
ATOM 2898 C ASN A 241 -6.959 -9.650 28.954 1.00 73.53 C
ANISOU 2898 C ASN A 241 8730 7285 11923 482 -2163 271 C
ATOM 2899 O ASN A 241 -6.659 -10.648 29.619 1.00 81.89 O
ANISOU 2899 O ASN A 241 9763 8305 13047 476 -2171 282 O
ATOM 2900 CB ASN A 241 -5.298 -8.242 27.707 1.00 74.51 C
ANISOU 2900 CB ASN A 241 8902 7487 11923 550 -2161 199 C
ATOM 2901 CG ASN A 241 -4.369 -8.173 26.512 1.00 85.92 C
ANISOU 2901 CG ASN A 241 10349 8936 13362 606 -2204 101 C
ATOM 2902 OD1 ASN A 241 -4.636 -8.769 25.467 1.00 96.22 O
ANISOU 2902 OD1 ASN A 241 11637 10200 14722 631 -2267 18 O
ATOM 2903 ND2 ASN A 241 -3.269 -7.441 26.659 1.00 60.44 N
ANISOU 2903 ND2 ASN A 241 7141 5754 10068 627 -2175 108 N
ATOM 2904 N LEU A 242 -7.867 -8.764 29.370 1.00 65.13 N
ANISOU 2904 N LEU A 242 7688 6254 10803 449 -2116 336 N
ATOM 2905 CA LEU A 242 -8.581 -8.974 30.623 1.00 63.30 C
ANISOU 2905 CA LEU A 242 7449 6012 10592 402 -2073 417 C
ATOM 2906 C LEU A 242 -9.478 -10.202 30.558 1.00 55.86 C
ANISOU 2906 C LEU A 242 6459 4996 9769 386 -2124 393 C
ATOM 2907 O LEU A 242 -9.666 -10.884 31.571 1.00 60.04 O
ANISOU 2907 O LEU A 242 6974 5496 10344 360 -2107 439 O
ATOM 2908 CB LEU A 242 -9.400 -7.733 30.973 1.00 47.87 C
ANISOU 2908 CB LEU A 242 5526 4106 8556 377 -2010 483 C
ATOM 2909 CG LEU A 242 -8.586 -6.477 31.279 1.00 49.01 C
ANISOU 2909 CG LEU A 242 5724 4319 8579 385 -1947 522 C
ATOM 2910 CD1 LEU A 242 -9.506 -5.282 31.367 1.00 56.38 C
ANISOU 2910 CD1 LEU A 242 6691 5292 9438 370 -1890 574 C
ATOM 2911 CD2 LEU A 242 -7.804 -6.648 32.568 1.00 44.30 C
ANISOU 2911 CD2 LEU A 242 5136 3730 7965 365 -1907 579 C
ATOM 2912 N ALA A 243 -10.038 -10.500 29.384 1.00 52.63 N
ANISOU 2912 N ALA A 243 6027 4556 9414 402 -2190 322 N
ATOM 2913 CA ALA A 243 -10.883 -11.682 29.256 1.00 60.51 C
ANISOU 2913 CA ALA A 243 6975 5478 10536 385 -2247 294 C
ATOM 2914 C ALA A 243 -10.055 -12.960 29.317 1.00 74.46 C
ANISOU 2914 C ALA A 243 8722 7192 12377 406 -2282 253 C
ATOM 2915 O ALA A 243 -10.470 -13.945 29.939 1.00 84.76 O
ANISOU 2915 O ALA A 243 10000 8441 13763 385 -2291 273 O
ATOM 2916 CB ALA A 243 -11.685 -11.616 27.958 1.00 65.70 C
ANISOU 2916 CB ALA A 243 7615 6116 11232 398 -2317 225 C
ATOM 2917 N GLU A 244 -8.881 -12.965 28.679 1.00 77.56 N
ANISOU 2917 N GLU A 244 9128 7598 12743 451 -2300 195 N
ATOM 2918 CA GLU A 244 -7.993 -14.117 28.795 1.00 81.69 C
ANISOU 2918 CA GLU A 244 9633 8073 13331 478 -2324 161 C
ATOM 2919 C GLU A 244 -7.417 -14.237 30.197 1.00 78.27 C
ANISOU 2919 C GLU A 244 9214 7654 12871 466 -2267 243 C
ATOM 2920 O GLU A 244 -7.093 -15.344 30.641 1.00 92.55 O
ANISOU 2920 O GLU A 244 11008 9410 14748 477 -2281 243 O
ATOM 2921 CB GLU A 244 -6.861 -14.029 27.771 1.00 70.69 C
ANISOU 2921 CB GLU A 244 8246 6695 11919 533 -2353 77 C
ATOM 2922 CG GLU A 244 -7.293 -14.281 26.337 1.00106.95 C
ANISOU 2922 CG GLU A 244 12824 11253 16560 555 -2426 -23 C
ATOM 2923 CD GLU A 244 -6.114 -14.490 25.404 1.00116.13 C
ANISOU 2923 CD GLU A 244 13986 12413 17726 614 -2456 -115 C
ATOM 2924 OE1 GLU A 244 -6.331 -14.970 24.271 1.00134.49 O
ANISOU 2924 OE1 GLU A 244 16297 14696 20106 637 -2520 -208 O
ATOM 2925 OE2 GLU A 244 -4.971 -14.181 25.805 1.00101.08 O
ANISOU 2925 OE2 GLU A 244 12091 10544 15770 637 -2417 -98 O
ATOM 2926 N ALA A 245 -7.281 -13.114 30.905 1.00 68.00 N
ANISOU 2926 N ALA A 245 7946 6420 11470 446 -2205 313 N
ATOM 2927 CA ALA A 245 -6.769 -13.152 32.269 1.00 81.54 C
ANISOU 2927 CA ALA A 245 9678 8149 13154 432 -2156 392 C
ATOM 2928 C ALA A 245 -7.828 -13.657 33.244 1.00 89.03 C
ANISOU 2928 C ALA A 245 10622 9061 14146 388 -2136 454 C
ATOM 2929 O ALA A 245 -7.541 -14.503 34.097 1.00 83.46 O
ANISOU 2929 O ALA A 245 9916 8317 13477 389 -2132 486 O
ATOM 2930 CB ALA A 245 -6.267 -11.766 32.682 1.00 68.82 C
ANISOU 2930 CB ALA A 245 8106 6618 11424 424 -2098 442 C
ATOM 2931 N GLY A 246 -9.057 -13.146 33.133 1.00 79.21 N
ANISOU 2931 N GLY A 246 9372 7824 12898 353 -2123 473 N
ATOM 2932 CA GLY A 246 -10.131 -13.644 33.978 1.00 52.16 C
ANISOU 2932 CA GLY A 246 5934 4360 9525 313 -2105 524 C
ATOM 2933 C GLY A 246 -10.333 -15.138 33.825 1.00 70.61 C
ANISOU 2933 C GLY A 246 8237 6610 11980 323 -2160 485 C
ATOM 2934 O GLY A 246 -10.562 -15.849 34.807 1.00 80.64 O
ANISOU 2934 O GLY A 246 9512 7841 13287 307 -2140 532 O
ATOM 2935 N ARG A 247 -10.246 -15.634 32.590 1.00 80.97 N
ANISOU 2935 N ARG A 247 9522 7889 13353 351 -2226 398 N
ATOM 2936 CA ARG A 247 -10.256 -17.074 32.366 1.00 84.28 C
ANISOU 2936 CA ARG A 247 9915 8224 13884 368 -2277 353 C
ATOM 2937 C ARG A 247 -9.072 -17.739 33.054 1.00 87.23 C
ANISOU 2937 C ARG A 247 10311 8581 14250 401 -2261 372 C
ATOM 2938 O ARG A 247 -9.244 -18.654 33.867 1.00105.05 O
ANISOU 2938 O ARG A 247 12574 10784 16557 395 -2252 408 O
ATOM 2939 CB ARG A 247 -10.239 -17.371 30.869 1.00 99.62 C
ANISOU 2939 CB ARG A 247 11831 10139 15882 397 -2349 250 C
ATOM 2940 CG ARG A 247 -11.610 -17.485 30.231 1.00106.50 C
ANISOU 2940 CG ARG A 247 12663 10974 16827 368 -2396 219 C
ATOM 2941 CD ARG A 247 -11.550 -18.341 28.971 1.00136.84 C
ANISOU 2941 CD ARG A 247 16478 14756 20758 399 -2478 114 C
ATOM 2942 NE ARG A 247 -10.949 -17.648 27.832 1.00154.34 N
ANISOU 2942 NE ARG A 247 18707 17015 22919 434 -2506 45 N
ATOM 2943 CZ ARG A 247 -9.669 -17.740 27.477 1.00144.56 C
ANISOU 2943 CZ ARG A 247 17488 15791 21648 481 -2504 3 C
ATOM 2944 NH1 ARG A 247 -8.830 -18.495 28.174 1.00138.36 N
ANISOU 2944 NH1 ARG A 247 16709 14981 20879 501 -2479 25 N
ATOM 2945 NH2 ARG A 247 -9.228 -17.073 26.419 1.00125.52 N
ANISOU 2945 NH2 ARG A 247 15090 13416 19187 511 -2529 -61 N
ATOM 2946 N ALA A 248 -7.856 -17.277 32.748 1.00 78.11 N
ANISOU 2946 N ALA A 248 9172 7472 13036 438 -2258 350 N
ATOM 2947 CA ALA A 248 -6.659 -17.907 33.297 1.00 81.50 C
ANISOU 2947 CA ALA A 248 9614 7885 13467 478 -2254 361 C
ATOM 2948 C ALA A 248 -6.613 -17.828 34.817 1.00 94.77 C
ANISOU 2948 C ALA A 248 11326 9577 15103 454 -2202 460 C
ATOM 2949 O ALA A 248 -5.986 -18.677 35.461 1.00109.06 O
ANISOU 2949 O ALA A 248 13149 11348 16941 482 -2205 482 O
ATOM 2950 CB ALA A 248 -5.407 -17.265 32.698 1.00 81.91 C
ANISOU 2950 CB ALA A 248 9669 7992 13462 520 -2258 320 C
ATOM 2951 N LEU A 249 -7.266 -16.825 35.413 1.00 88.52 N
ANISOU 2951 N LEU A 249 10554 8837 14244 407 -2154 521 N
ATOM 2952 CA LEU A 249 -7.245 -16.693 36.867 1.00 83.74 C
ANISOU 2952 CA LEU A 249 9984 8243 13591 383 -2103 612 C
ATOM 2953 C LEU A 249 -8.046 -17.786 37.560 1.00 83.53 C
ANISOU 2953 C LEU A 249 9961 8140 13636 367 -2102 642 C
ATOM 2954 O LEU A 249 -7.819 -18.047 38.746 1.00 78.91 O
ANISOU 2954 O LEU A 249 9412 7543 13027 363 -2071 707 O
ATOM 2955 CB LEU A 249 -7.780 -15.321 37.281 1.00 95.81 C
ANISOU 2955 CB LEU A 249 11533 9843 15028 339 -2047 664 C
ATOM 2956 CG LEU A 249 -6.824 -14.137 37.143 1.00 75.42 C
ANISOU 2956 CG LEU A 249 8969 7339 12347 351 -2026 668 C
ATOM 2957 CD1 LEU A 249 -7.599 -12.833 37.099 1.00 58.05 C
ANISOU 2957 CD1 LEU A 249 6783 5197 10074 313 -1977 696 C
ATOM 2958 CD2 LEU A 249 -5.808 -14.120 38.277 1.00 90.44 C
ANISOU 2958 CD2 LEU A 249 10903 9259 14202 360 -2005 726 C
ATOM 2959 N ALA A 250 -8.978 -18.421 36.855 1.00111.05 N
ANISOU 2959 N ALA A 250 17400 11325 13467 -154 -735 -782 N
ATOM 2960 CA ALA A 250 -9.772 -19.483 37.457 1.00123.95 C
ANISOU 2960 CA ALA A 250 19235 12771 15089 -294 -575 -899 C
ATOM 2961 C ALA A 250 -9.893 -20.667 36.504 1.00129.31 C
ANISOU 2961 C ALA A 250 20045 13352 15735 -237 -511 -963 C
ATOM 2962 O ALA A 250 -9.489 -21.783 36.844 1.00153.74 O
ANISOU 2962 O ALA A 250 23367 16318 18730 -189 -410 -903 O
ATOM 2963 CB ALA A 250 -11.151 -18.954 37.862 1.00116.35 C
ANISOU 2963 CB ALA A 250 18174 11785 14250 -524 -538 -1095 C
ATOM 2964 N GLY A 251 -10.431 -20.434 35.303 1.00114.69 N
ANISOU 2964 N GLY A 251 18055 11561 13963 -237 -569 -1082 N
ATOM 2965 CA GLY A 251 -10.624 -21.525 34.362 1.00121.11 C
ANISOU 2965 CA GLY A 251 18980 12284 14752 -192 -510 -1158 C
ATOM 2966 C GLY A 251 -9.331 -22.115 33.830 1.00136.95 C
ANISOU 2966 C GLY A 251 21086 14308 16642 33 -543 -978 C
ATOM 2967 O GLY A 251 -9.312 -23.267 33.385 1.00120.28 O
ANISOU 2967 O GLY A 251 19140 12084 14478 76 -461 -1005 O
ATOM 2968 N GLN A 252 -8.244 -21.338 33.860 1.00143.24 N
ANISOU 2968 N GLN A 252 21783 15243 17398 179 -661 -796 N
ATOM 2969 CA GLN A 252 -6.910 -21.744 33.417 1.00138.15 C
ANISOU 2969 CA GLN A 252 21212 14636 16641 402 -708 -609 C
ATOM 2970 C GLN A 252 -6.846 -22.083 31.931 1.00136.17 C
ANISOU 2970 C GLN A 252 20919 14420 16401 513 -756 -649 C
ATOM 2971 O GLN A 252 -5.917 -22.769 31.493 1.00136.11 O
ANISOU 2971 O GLN A 252 21021 14398 16297 680 -759 -527 O
ATOM 2972 CB GLN A 252 -6.377 -22.922 34.243 1.00128.59 C
ANISOU 2972 CB GLN A 252 20274 13277 15308 439 -587 -516 C
ATOM 2973 N ALA A 253 -7.802 -21.606 31.140 1.00125.03 N
ANISOU 2973 N ALA A 253 19349 13056 15102 427 -795 -815 N
ATOM 2974 CA ALA A 253 -7.794 -21.854 29.707 1.00116.97 C
ANISOU 2974 CA ALA A 253 18272 12076 14096 529 -846 -861 C
ATOM 2975 C ALA A 253 -6.841 -20.897 28.999 1.00136.27 C
ANISOU 2975 C ALA A 253 20540 14703 16534 703 -1005 -720 C
ATOM 2976 O ALA A 253 -6.678 -19.738 29.394 1.00142.65 O
ANISOU 2976 O ALA A 253 21189 15628 17382 688 -1089 -668 O
ATOM 2977 CB ALA A 253 -9.201 -21.710 29.128 1.00117.35 C
ANISOU 2977 CB ALA A 253 18217 12108 14264 374 -828 -1100 C
ATOM 2978 N ALA A 254 -6.205 -21.398 27.942 1.00118.02 N
ANISOU 2978 N ALA A 254 18259 12412 14170 869 -1041 -660 N
ATOM 2979 CA ALA A 254 -5.269 -20.605 27.157 1.00107.36 C
ANISOU 2979 CA ALA A 254 16756 11228 12810 1045 -1184 -528 C
ATOM 2980 C ALA A 254 -5.222 -21.162 25.744 1.00126.22 C
ANISOU 2980 C ALA A 254 19147 13621 15191 1157 -1208 -570 C
ATOM 2981 O ALA A 254 -5.009 -22.364 25.556 1.00123.73 O
ANISOU 2981 O ALA A 254 19018 13191 14802 1209 -1127 -560 O
ATOM 2982 CB ALA A 254 -3.869 -20.609 27.782 1.00 83.96 C
ANISOU 2982 CB ALA A 254 13867 8298 9735 1191 -1210 -298 C
ATOM 2983 N GLY A 255 -5.428 -20.292 24.758 1.00149.37 N
ANISOU 2983 N GLY A 255 21874 16683 18197 1195 -1319 -618 N
ATOM 2984 CA GLY A 255 -5.426 -20.702 23.369 1.00137.98 C
ANISOU 2984 CA GLY A 255 20411 15260 16755 1302 -1353 -664 C
ATOM 2985 C GLY A 255 -6.595 -21.560 22.940 1.00132.83 C
ANISOU 2985 C GLY A 255 19833 14489 16148 1184 -1260 -874 C
ATOM 2986 O GLY A 255 -6.649 -21.955 21.770 1.00122.22 O
ANISOU 2986 O GLY A 255 18477 13156 14806 1268 -1284 -924 O
ATOM 2987 N LEU A 256 -7.529 -21.861 23.837 1.00144.10 N
ANISOU 2987 N LEU A 256 21335 15805 17613 993 -1154 -1000 N
ATOM 2988 CA LEU A 256 -8.672 -22.722 23.540 1.00138.13 C
ANISOU 2988 CA LEU A 256 20659 14924 16900 865 -1051 -1208 C
ATOM 2989 C LEU A 256 -9.771 -22.426 24.559 1.00121.72 C
ANISOU 2989 C LEU A 256 18563 12786 14898 638 -979 -1350 C
ATOM 2990 O LEU A 256 -9.667 -21.488 25.357 1.00112.69 O
ANISOU 2990 O LEU A 256 17326 11710 13779 589 -1023 -1291 O
ATOM 2991 CB LEU A 256 -8.260 -24.200 23.528 1.00115.11 C
ANISOU 2991 CB LEU A 256 17991 11860 13885 925 -940 -1167 C
ATOM 2992 CG LEU A 256 -7.545 -24.796 24.749 1.00101.52 C
ANISOU 2992 CG LEU A 256 16471 10039 12063 935 -853 -1022 C
ATOM 2993 CD1 LEU A 256 -8.533 -25.283 25.801 1.00 94.80 C
ANISOU 2993 CD1 LEU A 256 15739 9039 11241 724 -712 -1156 C
ATOM 2994 CD2 LEU A 256 -6.600 -25.918 24.336 1.00 91.85 C
ANISOU 2994 CD2 LEU A 256 15432 8747 10722 1101 -815 -901 C
ATOM 2995 N GLY A 257 -10.829 -23.234 24.528 1.00111.12 N
ANISOU 2995 N GLY A 257 17311 11317 13594 498 -867 -1540 N
ATOM 2996 CA GLY A 257 -11.971 -23.058 25.401 1.00 95.32 C
ANISOU 2996 CA GLY A 257 15300 9249 11670 275 -789 -1699 C
ATOM 2997 C GLY A 257 -13.279 -23.173 24.646 1.00111.77 C
ANISOU 2997 C GLY A 257 17301 11314 13853 156 -766 -1948 C
ATOM 2998 O GLY A 257 -13.392 -23.936 23.681 1.00110.39 O
ANISOU 2998 O GLY A 257 17177 11102 13666 215 -745 -2016 O
ATOM 2999 N LEU A 258 -14.288 -22.428 25.090 1.00142.48 N
ANISOU 2999 N LEU A 258 21063 15230 17842 -14 -769 -2090 N
ATOM 3000 CA LEU A 258 -15.548 -22.316 24.367 1.00135.18 C
ANISOU 3000 CA LEU A 258 20022 14319 17022 -125 -769 -2330 C
ATOM 3001 C LEU A 258 -15.714 -20.923 23.776 1.00136.75 C
ANISOU 3001 C LEU A 258 19958 14702 17298 -90 -922 -2349 C
ATOM 3002 O LEU A 258 -15.791 -20.764 22.553 1.00122.79 O
ANISOU 3002 O LEU A 258 18083 13017 15554 4 -1001 -2401 O
ATOM 3003 CB LEU A 258 -16.726 -22.663 25.288 1.00120.38 C
ANISOU 3003 CB LEU A 258 18216 12317 15206 -362 -636 -2512 C
ATOM 3004 N VAL A 259 -15.786 -19.903 24.627 1.00142.55 N
ANISOU 3004 N VAL A 259 20590 15501 18072 -165 -963 -2309 N
ATOM 3005 CA VAL A 259 -15.569 -18.544 24.154 1.00122.80 C
ANISOU 3005 CA VAL A 259 17860 13181 15617 -90 -1117 -2258 C
ATOM 3006 C VAL A 259 -14.078 -18.297 23.926 1.00112.45 C
ANISOU 3006 C VAL A 259 16555 11953 14217 124 -1204 -2006 C
ATOM 3007 O VAL A 259 -13.704 -17.492 23.065 1.00112.74 O
ANISOU 3007 O VAL A 259 16432 12132 14271 249 -1330 -1954 O
ATOM 3008 CB VAL A 259 -16.185 -17.545 25.149 1.00118.15 C
ANISOU 3008 CB VAL A 259 17158 12630 15104 -249 -1127 -2308 C
ATOM 3009 CG1 VAL A 259 -15.879 -16.116 24.743 1.00110.64 C
ANISOU 3009 CG1 VAL A 259 15980 11863 14195 -167 -1281 -2237 C
ATOM 3010 CG2 VAL A 259 -17.689 -17.758 25.235 1.00113.55 C
ANISOU 3010 CG2 VAL A 259 16552 11977 14614 -453 -1049 -2570 C
ATOM 3011 N GLY A 260 -13.209 -19.005 24.656 1.00 95.92 N
ANISOU 3011 N GLY A 260 14647 9771 12025 175 -1137 -1851 N
ATOM 3012 CA GLY A 260 -11.777 -18.842 24.464 1.00 97.32 C
ANISOU 3012 CA GLY A 260 14839 10024 12114 378 -1214 -1615 C
ATOM 3013 C GLY A 260 -11.313 -19.183 23.061 1.00112.41 C
ANISOU 3013 C GLY A 260 16732 11984 13994 552 -1275 -1590 C
ATOM 3014 O GLY A 260 -10.326 -18.622 22.575 1.00103.42 O
ANISOU 3014 O GLY A 260 15514 10963 12819 720 -1381 -1432 O
ATOM 3015 N LYS A 261 -12.006 -20.112 22.394 1.00116.34 N
ANISOU 3015 N LYS A 261 17305 12393 14505 515 -1206 -1745 N
ATOM 3016 CA LYS A 261 -11.709 -20.385 20.991 1.00 91.97 C
ANISOU 3016 CA LYS A 261 14184 9359 11402 670 -1268 -1746 C
ATOM 3017 C LYS A 261 -11.892 -19.140 20.135 1.00 95.87 C
ANISOU 3017 C LYS A 261 14432 10024 11968 723 -1410 -1778 C
ATOM 3018 O LYS A 261 -11.171 -18.952 19.149 1.00 89.46 O
ANISOU 3018 O LYS A 261 13562 9304 11126 900 -1500 -1685 O
ATOM 3019 CB LYS A 261 -12.591 -21.524 20.477 1.00 77.59 C
ANISOU 3019 CB LYS A 261 12470 7415 9597 594 -1166 -1937 C
ATOM 3020 CG LYS A 261 -12.105 -22.920 20.853 1.00 87.07 C
ANISOU 3020 CG LYS A 261 13926 8457 10700 621 -1042 -1871 C
ATOM 3021 CD LYS A 261 -13.173 -23.971 20.571 1.00 90.64 C
ANISOU 3021 CD LYS A 261 14479 8774 11184 498 -923 -2087 C
ATOM 3022 CE LYS A 261 -13.430 -24.133 19.087 1.00 94.01 C
ANISOU 3022 CE LYS A 261 14823 9259 11639 587 -981 -2187 C
ATOM 3023 NZ LYS A 261 -12.334 -24.900 18.438 1.00 96.32 N
ANISOU 3023 NZ LYS A 261 15234 9533 11829 782 -990 -2036 N
ATOM 3024 N ARG A 262 -12.844 -18.278 20.500 1.00108.09 N
ANISOU 3024 N ARG A 262 15838 11617 13613 575 -1429 -1908 N
ATOM 3025 CA ARG A 262 -13.042 -17.003 19.822 1.00118.74 C
ANISOU 3025 CA ARG A 262 16955 13129 15033 616 -1561 -1935 C
ATOM 3026 C ARG A 262 -12.218 -15.876 20.434 1.00114.53 C
ANISOU 3026 C ARG A 262 16324 12705 14489 670 -1645 -1753 C
ATOM 3027 O ARG A 262 -11.849 -14.934 19.722 1.00106.92 O
ANISOU 3027 O ARG A 262 15200 11882 13545 782 -1764 -1694 O
ATOM 3028 CB ARG A 262 -14.528 -16.622 19.836 1.00102.95 C
ANISOU 3028 CB ARG A 262 14843 11130 13145 433 -1543 -2178 C
ATOM 3029 CG ARG A 262 -15.408 -17.471 18.923 1.00 92.88 C
ANISOU 3029 CG ARG A 262 13599 9792 11898 400 -1495 -2379 C
ATOM 3030 CD ARG A 262 -15.173 -17.124 17.460 1.00 94.66 C
ANISOU 3030 CD ARG A 262 13701 10137 12128 567 -1608 -2378 C
ATOM 3031 NE ARG A 262 -15.950 -17.954 16.541 1.00119.04 N
ANISOU 3031 NE ARG A 262 16820 13172 15239 549 -1566 -2565 N
ATOM 3032 CZ ARG A 262 -15.515 -19.096 16.015 1.00121.82 C
ANISOU 3032 CZ ARG A 262 17322 13443 15522 638 -1514 -2535 C
ATOM 3033 NH1 ARG A 262 -14.308 -19.554 16.324 1.00116.39 N
ANISOU 3033 NH1 ARG A 262 16770 12718 14737 754 -1498 -2325 N
ATOM 3034 NH2 ARG A 262 -16.285 -19.783 15.181 1.00 87.90 N
ANISOU 3034 NH2 ARG A 262 13040 9106 11254 613 -1478 -2718 N
ATOM 3035 N LEU A 263 -11.917 -15.948 21.734 1.00102.28 N
ANISOU 3035 N LEU A 263 14867 11090 12905 594 -1583 -1665 N
ATOM 3036 CA LEU A 263 -11.088 -14.921 22.362 1.00 86.98 C
ANISOU 3036 CA LEU A 263 12843 9252 10952 645 -1658 -1490 C
ATOM 3037 C LEU A 263 -9.646 -15.009 21.876 1.00106.17 C
ANISOU 3037 C LEU A 263 15307 11742 13289 865 -1721 -1274 C
ATOM 3038 O LEU A 263 -9.040 -13.994 21.513 1.00 90.10 O
ANISOU 3038 O LEU A 263 13125 9845 11263 971 -1832 -1169 O
ATOM 3039 CB LEU A 263 -11.150 -15.045 23.887 1.00 89.31 C
ANISOU 3039 CB LEU A 263 13241 9461 11233 508 -1571 -1458 C
ATOM 3040 CG LEU A 263 -12.276 -14.313 24.624 1.00107.94 C
ANISOU 3040 CG LEU A 263 15497 11825 13692 305 -1554 -1604 C
ATOM 3041 CD1 LEU A 263 -12.335 -14.748 26.080 1.00 84.62 C
ANISOU 3041 CD1 LEU A 263 12689 8753 10708 176 -1446 -1578 C
ATOM 3042 CD2 LEU A 263 -12.088 -12.806 24.527 1.00 94.97 C
ANISOU 3042 CD2 LEU A 263 13635 10348 12103 339 -1681 -1547 C
ATOM 3043 N SER A 264 -9.079 -16.219 21.863 1.00123.65 N
ANISOU 3043 N SER A 264 17717 13852 15414 937 -1648 -1207 N
ATOM 3044 CA SER A 264 -7.698 -16.387 21.422 1.00105.68 C
ANISOU 3044 CA SER A 264 15484 11625 13044 1147 -1702 -1004 C
ATOM 3045 C SER A 264 -7.540 -16.078 19.940 1.00100.22 C
ANISOU 3045 C SER A 264 14671 11037 12370 1289 -1800 -1015 C
ATOM 3046 O SER A 264 -6.449 -15.695 19.501 1.00 99.59 O
ANISOU 3046 O SER A 264 14546 11053 12242 1460 -1882 -850 O
ATOM 3047 CB SER A 264 -7.219 -17.804 21.727 1.00 96.12 C
ANISOU 3047 CB SER A 264 14517 10272 11734 1186 -1595 -945 C
ATOM 3048 OG SER A 264 -7.236 -18.047 23.122 1.00106.53 O
ANISOU 3048 OG SER A 264 15951 11499 13025 1073 -1509 -911 O
ATOM 3049 N LEU A 265 -8.605 -16.244 19.156 1.00 95.97 N
ANISOU 3049 N LEU A 265 14081 10484 11899 1225 -1792 -1210 N
ATOM 3050 CA LEU A 265 -8.577 -15.785 17.775 1.00 93.64 C
ANISOU 3050 CA LEU A 265 13648 10301 11632 1348 -1893 -1236 C
ATOM 3051 C LEU A 265 -8.749 -14.275 17.689 1.00 90.12 C
ANISOU 3051 C LEU A 265 12978 10003 11261 1338 -2001 -1236 C
ATOM 3052 O LEU A 265 -8.245 -13.652 16.748 1.00 94.24 O
ANISOU 3052 O LEU A 265 13382 10642 11782 1483 -2103 -1169 O
ATOM 3053 CB LEU A 265 -9.659 -16.497 16.961 1.00 97.75 C
ANISOU 3053 CB LEU A 265 14189 10757 12196 1287 -1848 -1450 C
ATOM 3054 CG LEU A 265 -9.192 -17.693 16.126 1.00115.04 C
ANISOU 3054 CG LEU A 265 16520 12879 14311 1414 -1814 -1423 C
ATOM 3055 CD1 LEU A 265 -8.241 -17.233 15.029 1.00110.52 C
ANISOU 3055 CD1 LEU A 265 15856 12431 13703 1628 -1930 -1291 C
ATOM 3056 CD2 LEU A 265 -8.533 -18.757 16.999 1.00 96.11 C
ANISOU 3056 CD2 LEU A 265 14346 10350 11820 1415 -1710 -1312 C
ATOM 3057 N ALA A 266 -9.437 -13.674 18.664 1.00 94.12 N
ANISOU 3057 N ALA A 266 13427 10504 11830 1171 -1979 -1307 N
ATOM 3058 CA ALA A 266 -9.639 -12.228 18.656 1.00 99.24 C
ANISOU 3058 CA ALA A 266 13867 11288 12551 1151 -2075 -1310 C
ATOM 3059 C ALA A 266 -8.337 -11.483 18.923 1.00 83.33 C
ANISOU 3059 C ALA A 266 11804 9371 10487 1281 -2148 -1082 C
ATOM 3060 O ALA A 266 -8.088 -10.425 18.329 1.00 66.38 O
ANISOU 3060 O ALA A 266 9491 7358 8373 1364 -2252 -1038 O
ATOM 3061 CB ALA A 266 -10.702 -11.838 19.686 1.00 90.79 C
ANISOU 3061 CB ALA A 266 12759 10180 11557 934 -2025 -1443 C
ATOM 3062 N ARG A 267 -7.498 -12.017 19.817 1.00 81.27 N
ANISOU 3062 N ARG A 267 11686 9046 10148 1301 -2094 -938 N
ATOM 3063 CA ARG A 267 -6.199 -11.402 20.072 1.00 76.68 C
ANISOU 3063 CA ARG A 267 11068 8555 9513 1431 -2160 -721 C
ATOM 3064 C ARG A 267 -5.349 -11.358 18.809 1.00 78.79 C
ANISOU 3064 C ARG A 267 11292 8905 9738 1640 -2240 -623 C
ATOM 3065 O ARG A 267 -4.637 -10.378 18.572 1.00 79.79 O
ANISOU 3065 O ARG A 267 11292 9157 9868 1740 -2331 -506 O
ATOM 3066 CB ARG A 267 -5.460 -12.158 21.181 1.00 82.96 C
ANISOU 3066 CB ARG A 267 12043 9256 10220 1428 -2081 -594 C
ATOM 3067 CG ARG A 267 -4.003 -11.734 21.349 1.00 83.32 C
ANISOU 3067 CG ARG A 267 12074 9389 10195 1586 -2143 -365 C
ATOM 3068 CD ARG A 267 -3.287 -12.625 22.345 1.00100.55 C
ANISOU 3068 CD ARG A 267 14450 11473 12281 1597 -2063 -249 C
ATOM 3069 NE ARG A 267 -3.763 -12.442 23.713 1.00 95.16 N
ANISOU 3069 NE ARG A 267 13798 10736 11623 1429 -2002 -282 N
ATOM 3070 CZ ARG A 267 -3.378 -11.451 24.511 1.00 94.08 C
ANISOU 3070 CZ ARG A 267 13564 10681 11502 1404 -2046 -193 C
ATOM 3071 NH1 ARG A 267 -2.524 -10.537 24.072 1.00 83.92 N
ANISOU 3071 NH1 ARG A 267 12141 9534 10212 1534 -2148 -69 N
ATOM 3072 NH2 ARG A 267 -3.851 -11.368 25.747 1.00 89.90 N
ANISOU 3072 NH2 ARG A 267 13073 10093 10991 1249 -1985 -231 N
ATOM 3073 N ASN A 268 -5.426 -12.396 17.972 1.00 82.16 N
ANISOU 3073 N ASN A 268 11823 9266 10130 1706 -2208 -674 N
ATOM 3074 CA ASN A 268 -4.579 -12.429 16.784 1.00 88.48 C
ANISOU 3074 CA ASN A 268 12595 10139 10884 1909 -2280 -576 C
ATOM 3075 C ASN A 268 -5.030 -11.407 15.748 1.00 68.99 C
ANISOU 3075 C ASN A 268 9928 7794 8492 1946 -2378 -652 C
ATOM 3076 O ASN A 268 -4.228 -10.971 14.911 1.00 71.36 O
ANISOU 3076 O ASN A 268 10154 8192 8767 2112 -2460 -543 O
ATOM 3077 CB ASN A 268 -4.557 -13.834 16.177 1.00 90.19 C
ANISOU 3077 CB ASN A 268 12979 10248 11041 1967 -2216 -613 C
ATOM 3078 CG ASN A 268 -3.639 -14.770 16.923 1.00 88.84 C
ANISOU 3078 CG ASN A 268 13001 9986 10768 2014 -2146 -471 C
ATOM 3079 OD1 ASN A 268 -2.441 -14.842 16.637 1.00106.48 O
ANISOU 3079 OD1 ASN A 268 15263 12266 12927 2181 -2187 -299 O
ATOM 3080 ND2 ASN A 268 -4.191 -15.490 17.893 1.00 82.85 N
ANISOU 3080 ND2 ASN A 268 12377 9098 10002 1868 -2038 -541 N
ATOM 3081 N VAL A 269 -6.306 -11.021 15.777 1.00 45.15 N
ANISOU 3081 N VAL A 269 6820 4771 5563 1799 -2371 -840 N
ATOM 3082 CA VAL A 269 -6.782 -9.984 14.871 1.00 59.93 C
ANISOU 3082 CA VAL A 269 8500 6763 7508 1829 -2464 -916 C
ATOM 3083 C VAL A 269 -6.442 -8.603 15.412 1.00 66.98 C
ANISOU 3083 C VAL A 269 9245 7768 8437 1819 -2532 -823 C
ATOM 3084 O VAL A 269 -6.003 -7.720 14.666 1.00 70.72 O
ANISOU 3084 O VAL A 269 9586 8362 8923 1937 -2624 -757 O
ATOM 3085 CB VAL A 269 -8.293 -10.137 14.637 1.00 73.51 C
ANISOU 3085 CB VAL A 269 10183 8440 9308 1682 -2431 -1161 C
ATOM 3086 CG1 VAL A 269 -8.730 -9.238 13.498 1.00 61.43 C
ANISOU 3086 CG1 VAL A 269 8473 7030 7838 1747 -2529 -1240 C
ATOM 3087 CG2 VAL A 269 -8.643 -11.585 14.358 1.00 75.02 C
ANISOU 3087 CG2 VAL A 269 10541 8500 9462 1664 -2343 -1255 C
ATOM 3088 N LEU A 270 -6.635 -8.400 16.716 1.00 61.68 N
ANISOU 3088 N LEU A 270 8596 7058 7783 1677 -2484 -817 N
ATOM 3089 CA LEU A 270 -6.362 -7.103 17.321 1.00 52.78 C
ANISOU 3089 CA LEU A 270 7331 6031 6693 1651 -2541 -736 C
ATOM 3090 C LEU A 270 -4.880 -6.762 17.282 1.00 61.87 C
ANISOU 3090 C LEU A 270 8475 7258 7776 1817 -2594 -510 C
ATOM 3091 O LEU A 270 -4.519 -5.580 17.255 1.00 61.16 O
ANISOU 3091 O LEU A 270 8238 7283 7716 1856 -2668 -437 O
ATOM 3092 CB LEU A 270 -6.881 -7.092 18.754 1.00 50.81 C
ANISOU 3092 CB LEU A 270 7124 5711 6470 1462 -2470 -780 C
ATOM 3093 CG LEU A 270 -8.404 -7.169 18.813 1.00 58.99 C
ANISOU 3093 CG LEU A 270 8130 6694 7589 1286 -2429 -1012 C
ATOM 3094 CD1 LEU A 270 -8.887 -7.727 20.138 1.00 53.70 C
ANISOU 3094 CD1 LEU A 270 7578 5905 6921 1110 -2325 -1063 C
ATOM 3095 CD2 LEU A 270 -8.968 -5.785 18.570 1.00 51.98 C
ANISOU 3095 CD2 LEU A 270 7034 5927 6791 1248 -2511 -1077 C
ATOM 3096 N ILE A 271 -4.012 -7.775 17.274 1.00 63.37 N
ANISOU 3096 N ILE A 271 8820 7384 7873 1917 -2555 -400 N
ATOM 3097 CA ILE A 271 -2.577 -7.525 17.178 1.00 57.30 C
ANISOU 3097 CA ILE A 271 8049 6689 7036 2081 -2602 -189 C
ATOM 3098 C ILE A 271 -2.239 -6.876 15.843 1.00 64.60 C
ANISOU 3098 C ILE A 271 8816 7744 7983 2087 -2521 -173 C
ATOM 3099 O ILE A 271 -1.443 -5.931 15.778 1.00 62.83 O
ANISOU 3099 O ILE A 271 8462 7640 7769 2032 -2421 -57 O
ATOM 3100 CB ILE A 271 -1.797 -8.834 17.394 1.00 60.21 C
ANISOU 3100 CB ILE A 271 8619 6958 7299 2159 -2540 -92 C
ATOM 3101 CG1 ILE A 271 -1.759 -9.183 18.884 1.00 64.70 C
ANISOU 3101 CG1 ILE A 271 9298 7443 7841 2037 -2461 -59 C
ATOM 3102 CG2 ILE A 271 -0.396 -8.723 16.815 1.00 69.90 C
ANISOU 3102 CG2 ILE A 271 9782 8299 8479 2192 -2412 67 C
ATOM 3103 CD1 ILE A 271 -1.240 -10.571 19.185 1.00 50.45 C
ANISOU 3103 CD1 ILE A 271 7711 5520 5939 2082 -2381 2 C
ATOM 3104 N ALA A 272 -2.842 -7.367 14.757 1.00 73.13 N
ANISOU 3104 N ALA A 272 9915 8798 9074 2153 -2564 -288 N
ATOM 3105 CA ALA A 272 -2.640 -6.742 13.454 1.00 59.33 C
ANISOU 3105 CA ALA A 272 8032 7162 7347 2153 -2495 -281 C
ATOM 3106 C ALA A 272 -3.221 -5.335 13.426 1.00 59.68 C
ANISOU 3106 C ALA A 272 7899 7300 7475 2052 -2494 -333 C
ATOM 3107 O ALA A 272 -2.628 -4.420 12.842 1.00 67.20 O
ANISOU 3107 O ALA A 272 8734 8361 8437 2014 -2395 -241 O
ATOM 3108 CB ALA A 272 -3.262 -7.604 12.356 1.00 58.50 C
ANISOU 3108 CB ALA A 272 7989 7003 7235 2246 -2550 -408 C
ATOM 3109 N LEU A 273 -4.382 -5.143 14.057 1.00 50.65 N
ANISOU 3109 N LEU A 273 6737 6111 6396 2001 -2603 -479 N
ATOM 3110 CA LEU A 273 -4.962 -3.809 14.155 1.00 55.02 C
ANISOU 3110 CA LEU A 273 7129 6748 7029 1893 -2593 -529 C
ATOM 3111 C LEU A 273 -4.089 -2.872 14.980 1.00 55.89 C
ANISOU 3111 C LEU A 273 7175 6930 7130 1817 -2501 -365 C
ATOM 3112 O LEU A 273 -4.087 -1.660 14.741 1.00 53.89 O
ANISOU 3112 O LEU A 273 6790 6771 6916 1746 -2435 -335 O
ATOM 3113 CB LEU A 273 -6.363 -3.895 14.753 1.00 54.76 C
ANISOU 3113 CB LEU A 273 7082 6653 7071 1833 -2730 -729 C
ATOM 3114 CG LEU A 273 -7.409 -4.553 13.857 1.00 70.93 C
ANISOU 3114 CG LEU A 273 9141 8660 9150 1872 -2809 -926 C
ATOM 3115 CD1 LEU A 273 -8.633 -4.940 14.665 1.00 65.36 C
ANISOU 3115 CD1 LEU A 273 8476 7862 8497 1663 -2733 -1103 C
ATOM 3116 CD2 LEU A 273 -7.789 -3.617 12.719 1.00 40.36 C
ANISOU 3116 CD2 LEU A 273 5127 4887 5322 1859 -2757 -976 C
ATOM 3117 N ALA A 274 -3.346 -3.408 15.950 1.00 56.57 N
ANISOU 3117 N ALA A 274 7359 6971 7165 1831 -2493 -259 N
ATOM 3118 CA ALA A 274 -2.456 -2.564 16.740 1.00 60.21 C
ANISOU 3118 CA ALA A 274 7753 7506 7616 1763 -2405 -106 C
ATOM 3119 C ALA A 274 -1.362 -1.957 15.870 1.00 72.86 C
ANISOU 3119 C ALA A 274 9267 9219 9198 1768 -2271 37 C
ATOM 3120 O ALA A 274 -1.012 -0.781 16.029 1.00 78.40 O
ANISOU 3120 O ALA A 274 9849 10012 9927 1692 -2198 115 O
ATOM 3121 CB ALA A 274 -1.849 -3.367 17.890 1.00 62.74 C
ANISOU 3121 CB ALA A 274 8207 7753 7877 1786 -2419 -22 C
ATOM 3122 N PHE A 275 -0.809 -2.745 14.943 1.00 68.43 N
ANISOU 3122 N PHE A 275 8764 8645 8590 1850 -2239 74 N
ATOM 3123 CA PHE A 275 0.148 -2.197 13.987 1.00 65.23 C
ANISOU 3123 CA PHE A 275 8271 8333 8181 1844 -2128 194 C
ATOM 3124 C PHE A 275 -0.497 -1.144 13.100 1.00 71.66 C
ANISOU 3124 C PHE A 275 8969 9210 9050 1800 -2114 132 C
ATOM 3125 O PHE A 275 0.192 -0.252 12.590 1.00 66.50 O
ANISOU 3125 O PHE A 275 8220 8638 8412 1756 -2024 239 O
ATOM 3126 CB PHE A 275 0.741 -3.318 13.133 1.00 56.09 C
ANISOU 3126 CB PHE A 275 7201 7139 6970 1936 -2110 224 C
ATOM 3127 CG PHE A 275 1.771 -4.141 13.847 1.00 67.35 C
ANISOU 3127 CG PHE A 275 8718 8532 8340 1966 -2078 338 C
ATOM 3128 CD1 PHE A 275 1.397 -5.231 14.613 1.00 68.91 C
ANISOU 3128 CD1 PHE A 275 9070 8622 8491 2021 -2149 283 C
ATOM 3129 CD2 PHE A 275 3.117 -3.822 13.751 1.00 59.33 C
ANISOU 3129 CD2 PHE A 275 7638 7584 7322 1935 -1981 497 C
ATOM 3130 CE1 PHE A 275 2.345 -5.990 15.274 1.00 63.47 C
ANISOU 3130 CE1 PHE A 275 8472 7900 7742 2050 -2110 391 C
ATOM 3131 CE2 PHE A 275 4.069 -4.577 14.406 1.00 66.71 C
ANISOU 3131 CE2 PHE A 275 8647 8490 8209 1958 -1952 595 C
ATOM 3132 CZ PHE A 275 3.683 -5.662 15.170 1.00 57.93 C
ANISOU 3132 CZ PHE A 275 7693 7279 7041 2018 -2011 544 C
ATOM 3133 N LEU A 276 -1.813 -1.233 12.908 1.00 65.60 N
ANISOU 3133 N LEU A 276 8211 8399 8316 1808 -2204 -41 N
ATOM 3134 CA LEU A 276 -2.529 -0.247 12.109 1.00 63.55 C
ANISOU 3134 CA LEU A 276 7847 8193 8106 1766 -2191 -112 C
ATOM 3135 C LEU A 276 -2.699 1.067 12.861 1.00 58.35 C
ANISOU 3135 C LEU A 276 7086 7593 7490 1660 -2157 -80 C
ATOM 3136 O LEU A 276 -2.640 2.140 12.252 1.00 61.74 O
ANISOU 3136 O LEU A 276 7423 8093 7941 1615 -2089 -38 O
ATOM 3137 CB LEU A 276 -3.887 -0.808 11.699 1.00 69.41 C
ANISOU 3137 CB LEU A 276 8623 8871 8878 1804 -2300 -319 C
ATOM 3138 CG LEU A 276 -4.561 -0.178 10.488 1.00 53.55 C
ANISOU 3138 CG LEU A 276 6539 6906 6901 1800 -2285 -402 C
ATOM 3139 CD1 LEU A 276 -3.783 -0.502 9.221 1.00 54.70 C
ANISOU 3139 CD1 LEU A 276 6705 7079 7001 1868 -2221 -322 C
ATOM 3140 CD2 LEU A 276 -5.996 -0.652 10.383 1.00 50.80 C
ANISOU 3140 CD2 LEU A 276 6204 6497 6599 1816 -2400 -624 C
ATOM 3141 N SER A 277 -2.899 1.003 14.183 1.00 57.32 N
ANISOU 3141 N SER A 277 6963 9417 5400 1662 -1265 -1113 N
ATOM 3142 CA SER A 277 -3.029 2.221 14.978 1.00 64.64 C
ANISOU 3142 CA SER A 277 7951 10257 6351 1607 -1270 -1050 C
ATOM 3143 C SER A 277 -1.779 3.078 14.887 1.00 60.58 C
ANISOU 3143 C SER A 277 7412 9760 5847 1518 -1204 -1020 C
ATOM 3144 O SER A 277 -1.853 4.307 14.996 1.00 85.28 O
ANISOU 3144 O SER A 277 10604 12837 8960 1466 -1181 -951 O
ATOM 3145 CB SER A 277 -3.311 1.877 16.440 1.00 70.68 C
ANISOU 3145 CB SER A 277 8704 10949 7202 1619 -1345 -1079 C
ATOM 3146 OG SER A 277 -2.143 1.420 17.099 1.00 56.30 O
ANISOU 3146 OG SER A 277 6791 9147 5454 1584 -1342 -1127 O
ATOM 3147 N SER A 278 -0.624 2.448 14.694 1.00 51.68 N
ANISOU 3147 N SER A 278 6191 8702 4744 1500 -1174 -1070 N
ATOM 3148 CA SER A 278 0.623 3.175 14.535 1.00 70.40 C
ANISOU 3148 CA SER A 278 8530 11097 7121 1417 -1108 -1045 C
ATOM 3149 C SER A 278 0.695 3.953 13.228 1.00 67.36 C
ANISOU 3149 C SER A 278 8188 10756 6648 1394 -1036 -991 C
ATOM 3150 O SER A 278 1.671 4.678 13.012 1.00 78.59 O
ANISOU 3150 O SER A 278 9594 12197 8069 1323 -978 -961 O
ATOM 3151 CB SER A 278 1.792 2.197 14.623 1.00 69.23 C
ANISOU 3151 CB SER A 278 8268 11016 7020 1411 -1096 -1116 C
ATOM 3152 OG SER A 278 2.985 2.796 14.159 1.00 81.22 O
ANISOU 3152 OG SER A 278 9753 12579 8528 1340 -1024 -1095 O
ATOM 3153 N SER A 279 -0.301 3.829 12.355 1.00 52.62 N
ANISOU 3153 N SER A 279 6378 8907 4710 1450 -1038 -975 N
ATOM 3154 CA SER A 279 -0.289 4.525 11.077 1.00 65.55 C
ANISOU 3154 CA SER A 279 8057 10589 6261 1432 -971 -925 C
ATOM 3155 C SER A 279 -1.458 5.489 10.920 1.00 84.23 C
ANISOU 3155 C SER A 279 10536 12891 8576 1440 -980 -852 C
ATOM 3156 O SER A 279 -1.615 6.090 9.850 1.00 90.51 O
ANISOU 3156 O SER A 279 11377 13718 9295 1432 -929 -806 O
ATOM 3157 CB SER A 279 -0.282 3.509 9.936 1.00 70.53 C
ANISOU 3157 CB SER A 279 8646 11314 6839 1489 -952 -971 C
ATOM 3158 OG SER A 279 -1.391 2.634 10.033 1.00 86.82 O
ANISOU 3158 OG SER A 279 10727 13365 8896 1572 -1014 -1006 O
ATOM 3159 N VAL A 280 -2.279 5.661 11.959 1.00 65.14 N
ANISOU 3159 N VAL A 280 8165 10386 6199 1456 -1044 -841 N
ATOM 3160 CA VAL A 280 -3.426 6.560 11.870 1.00 59.21 C
ANISOU 3160 CA VAL A 280 7522 9572 5403 1466 -1056 -773 C
ATOM 3161 C VAL A 280 -3.105 7.975 12.335 1.00 67.60 C
ANISOU 3161 C VAL A 280 8634 10571 6479 1386 -1028 -703 C
ATOM 3162 O VAL A 280 -3.782 8.920 11.912 1.00 70.25 O
ANISOU 3162 O VAL A 280 9057 10875 6760 1378 -1010 -635 O
ATOM 3163 CB VAL A 280 -4.623 6.005 12.665 1.00 68.61 C
ANISOU 3163 CB VAL A 280 8745 10702 6622 1532 -1140 -794 C
ATOM 3164 CG1 VAL A 280 -4.418 6.181 14.167 1.00 91.18 C
ANISOU 3164 CG1 VAL A 280 11591 13481 9572 1501 -1187 -801 C
ATOM 3165 CG2 VAL A 280 -5.929 6.644 12.212 1.00 61.95 C
ANISOU 3165 CG2 VAL A 280 8007 9818 5712 1564 -1150 -734 C
ATOM 3166 N ASN A 281 -2.080 8.154 13.167 1.00 76.17 N
ANISOU 3166 N ASN A 281 9667 11639 7634 1326 -1022 -716 N
ATOM 3167 CA ASN A 281 -1.716 9.504 13.594 1.00 64.32 C
ANISOU 3167 CA ASN A 281 8211 10081 6147 1247 -993 -650 C
ATOM 3168 C ASN A 281 -1.226 10.376 12.444 1.00 61.93 C
ANISOU 3168 C ASN A 281 7933 9824 5775 1200 -910 -596 C
ATOM 3169 O ASN A 281 -1.657 11.540 12.361 1.00 76.00 O
ANISOU 3169 O ASN A 281 9797 11555 7525 1169 -892 -524 O
ATOM 3170 CB ASN A 281 -0.678 9.439 14.720 1.00 73.42 C
ANISOU 3170 CB ASN A 281 9296 11210 7391 1194 -1004 -680 C
ATOM 3171 CG ASN A 281 -1.251 8.892 16.017 1.00 77.91 C
ANISOU 3171 CG ASN A 281 9860 11711 8030 1229 -1087 -715 C
ATOM 3172 OD1 ASN A 281 -2.440 9.052 16.304 1.00 70.62 O
ANISOU 3172 OD1 ASN A 281 9009 10729 7095 1270 -1133 -692 O
ATOM 3173 ND2 ASN A 281 -0.402 8.249 16.812 1.00 73.54 N
ANISOU 3173 ND2 ASN A 281 9222 11166 7553 1213 -1107 -771 N
ATOM 3174 N PRO A 282 -0.338 9.918 11.546 1.00 72.36 N
ANISOU 3174 N PRO A 282 9186 11237 7069 1192 -857 -625 N
ATOM 3175 CA PRO A 282 0.088 10.814 10.457 1.00 52.64 C
ANISOU 3175 CA PRO A 282 6717 8780 4504 1146 -778 -569 C
ATOM 3176 C PRO A 282 -1.029 11.166 9.491 1.00 63.57 C
ANISOU 3176 C PRO A 282 8186 10166 5799 1189 -768 -524 C
ATOM 3177 O PRO A 282 -1.078 12.302 9.003 1.00 65.05 O
ANISOU 3177 O PRO A 282 8436 10338 5940 1147 -722 -453 O
ATOM 3178 CB PRO A 282 1.214 10.026 9.771 1.00 51.60 C
ANISOU 3178 CB PRO A 282 6488 8750 4369 1141 -734 -622 C
ATOM 3179 CG PRO A 282 0.937 8.609 10.104 1.00 84.08 C
ANISOU 3179 CG PRO A 282 10544 12886 8516 1211 -791 -702 C
ATOM 3180 CD PRO A 282 0.397 8.639 11.502 1.00 90.63 C
ANISOU 3180 CD PRO A 282 11396 13622 9416 1218 -863 -707 C
ATOM 3181 N VAL A 283 -1.935 10.230 9.194 1.00 62.45 N
ANISOU 3181 N VAL A 283 8050 10044 5633 1272 -810 -561 N
ATOM 3182 CA VAL A 283 -3.046 10.592 8.322 1.00 63.47 C
ANISOU 3182 CA VAL A 283 8264 10172 5679 1313 -803 -515 C
ATOM 3183 C VAL A 283 -3.987 11.556 9.036 1.00 60.61 C
ANISOU 3183 C VAL A 283 7997 9708 5324 1304 -838 -454 C
ATOM 3184 O VAL A 283 -4.534 12.468 8.409 1.00 69.68 O
ANISOU 3184 O VAL A 283 9225 10841 6409 1294 -808 -387 O
ATOM 3185 CB VAL A 283 -3.778 9.338 7.799 1.00 65.96 C
ANISOU 3185 CB VAL A 283 8560 10537 5965 1404 -839 -570 C
ATOM 3186 CG1 VAL A 283 -2.783 8.378 7.171 1.00 71.97 C
ANISOU 3186 CG1 VAL A 283 9224 11397 6726 1411 -806 -633 C
ATOM 3187 CG2 VAL A 283 -4.583 8.646 8.890 1.00 52.86 C
ANISOU 3187 CG2 VAL A 283 6903 8817 4362 1456 -926 -609 C
ATOM 3188 N LEU A 284 -4.157 11.406 10.354 1.00 66.19 N
ANISOU 3188 N LEU A 284 8698 10344 6108 1303 -898 -474 N
ATOM 3189 CA LEU A 284 -4.980 12.349 11.108 1.00 50.15 C
ANISOU 3189 CA LEU A 284 6754 8212 4088 1290 -930 -416 C
ATOM 3190 C LEU A 284 -4.380 13.749 11.081 1.00 60.51 C
ANISOU 3190 C LEU A 284 8104 9494 5392 1204 -874 -346 C
ATOM 3191 O LEU A 284 -5.112 14.742 10.990 1.00 65.47 O
ANISOU 3191 O LEU A 284 8823 10068 5983 1194 -868 -277 O
ATOM 3192 CB LEU A 284 -5.149 11.872 12.549 1.00 48.05 C
ANISOU 3192 CB LEU A 284 6465 7881 3910 1303 -1004 -455 C
ATOM 3193 CG LEU A 284 -6.183 10.776 12.814 1.00 56.15 C
ANISOU 3193 CG LEU A 284 7490 8899 4944 1392 -1076 -504 C
ATOM 3194 CD1 LEU A 284 -6.104 10.320 14.261 1.00 66.33 C
ANISOU 3194 CD1 LEU A 284 8744 10131 6328 1393 -1141 -545 C
ATOM 3195 CD2 LEU A 284 -7.583 11.263 12.481 1.00 46.86 C
ANISOU 3195 CD2 LEU A 284 6417 7680 3709 1435 -1096 -451 C
ATOM 3196 N TYR A 285 -3.051 13.850 11.169 1.00 68.82 N
ANISOU 3196 N TYR A 285 9089 10581 6480 1141 -832 -361 N
ATOM 3197 CA TYR A 285 -2.396 15.147 11.033 1.00 51.62 C
ANISOU 3197 CA TYR A 285 6941 8384 4289 1057 -772 -296 C
ATOM 3198 C TYR A 285 -2.774 15.805 9.713 1.00 61.79 C
ANISOU 3198 C TYR A 285 8290 9706 5481 1060 -715 -238 C
ATOM 3199 O TYR A 285 -3.167 16.977 9.676 1.00 75.38 O
ANISOU 3199 O TYR A 285 10092 11374 7174 1026 -696 -166 O
ATOM 3200 CB TYR A 285 -0.876 14.993 11.122 1.00 51.46 C
ANISOU 3200 CB TYR A 285 6828 8413 4312 997 -730 -328 C
ATOM 3201 CG TYR A 285 -0.353 14.388 12.406 1.00 58.32 C
ANISOU 3201 CG TYR A 285 7630 9253 5277 987 -779 -383 C
ATOM 3202 CD1 TYR A 285 -1.065 14.483 13.596 1.00 58.88 C
ANISOU 3202 CD1 TYR A 285 7738 9233 5400 1001 -847 -381 C
ATOM 3203 CD2 TYR A 285 0.864 13.726 12.423 1.00 51.26 C
ANISOU 3203 CD2 TYR A 285 6634 8421 4421 963 -757 -438 C
ATOM 3204 CE1 TYR A 285 -0.570 13.926 14.766 1.00 68.73 C
ANISOU 3204 CE1 TYR A 285 8923 10455 6736 991 -891 -432 C
ATOM 3205 CE2 TYR A 285 1.362 13.170 13.579 1.00 71.78 C
ANISOU 3205 CE2 TYR A 285 9171 10996 7108 953 -801 -489 C
ATOM 3206 CZ TYR A 285 0.646 13.269 14.747 1.00 66.85 C
ANISOU 3206 CZ TYR A 285 8584 10282 6534 967 -867 -486 C
ATOM 3207 OH TYR A 285 1.163 12.703 15.891 1.00 88.33 O
ANISOU 3207 OH TYR A 285 11240 12980 9342 957 -910 -537 O
ATOM 3208 N ALA A 286 -2.668 15.055 8.614 1.00 64.86 N
ANISOU 3208 N ALA A 286 8640 10185 5817 1100 -688 -270 N
ATOM 3209 CA ALA A 286 -2.986 15.611 7.305 1.00 80.44 C
ANISOU 3209 CA ALA A 286 10667 12199 7698 1104 -633 -219 C
ATOM 3210 C ALA A 286 -4.491 15.712 7.086 1.00 71.87 C
ANISOU 3210 C ALA A 286 9670 11075 6563 1167 -671 -189 C
ATOM 3211 O ALA A 286 -4.958 16.658 6.441 1.00 68.64 O
ANISOU 3211 O ALA A 286 9338 10651 6090 1154 -636 -121 O
ATOM 3212 CB ALA A 286 -2.338 14.773 6.203 1.00 86.31 C
ANISOU 3212 CB ALA A 286 11338 13053 8402 1125 -590 -264 C
ATOM 3213 N PHE A 287 -5.261 14.758 7.619 1.00 88.94 N
ANISOU 3213 N PHE A 287 11823 13217 8751 1236 -741 -238 N
ATOM 3214 CA PHE A 287 -6.712 14.783 7.447 1.00 94.56 C
ANISOU 3214 CA PHE A 287 12616 13893 9418 1299 -781 -212 C
ATOM 3215 C PHE A 287 -7.312 16.052 8.038 1.00 99.13 C
ANISOU 3215 C PHE A 287 13289 14375 10000 1265 -791 -137 C
ATOM 3216 O PHE A 287 -8.008 16.805 7.350 1.00115.32 O
ANISOU 3216 O PHE A 287 15419 16414 11983 1271 -767 -75 O
ATOM 3217 CB PHE A 287 -7.342 13.536 8.081 1.00104.60 C
ANISOU 3217 CB PHE A 287 13856 15156 10732 1373 -859 -280 C
ATOM 3218 CG PHE A 287 -8.811 13.677 8.404 1.00113.48 C
ANISOU 3218 CG PHE A 287 15065 16212 11839 1427 -916 -253 C
ATOM 3219 CD1 PHE A 287 -9.764 13.630 7.398 1.00110.36 C
ANISOU 3219 CD1 PHE A 287 14724 15844 11361 1480 -909 -230 C
ATOM 3220 CD2 PHE A 287 -9.237 13.827 9.718 1.00110.60 C
ANISOU 3220 CD2 PHE A 287 14724 15758 11541 1425 -977 -251 C
ATOM 3221 CE1 PHE A 287 -11.106 13.751 7.696 1.00119.24 C
ANISOU 3221 CE1 PHE A 287 15926 16909 12472 1530 -962 -204 C
ATOM 3222 CE2 PHE A 287 -10.577 13.947 10.016 1.00 90.32 C
ANISOU 3222 CE2 PHE A 287 12232 13129 8957 1475 -1029 -226 C
ATOM 3223 CZ PHE A 287 -11.510 13.908 9.005 1.00 95.90 C
ANISOU 3223 CZ PHE A 287 12992 13863 9581 1527 -1021 -202 C
ATOM 3224 N ALA A 288 -7.042 16.312 9.317 1.00 92.94 N
ANISOU 3224 N ALA A 288 12496 13520 9295 1229 -825 -140 N
ATOM 3225 CA ALA A 288 -7.599 17.499 9.956 1.00 88.83 C
ANISOU 3225 CA ALA A 288 12064 12906 8783 1196 -837 -72 C
ATOM 3226 C ALA A 288 -7.030 18.775 9.346 1.00 83.78 C
ANISOU 3226 C ALA A 288 11462 12269 8103 1123 -761 -1 C
ATOM 3227 O ALA A 288 -7.748 19.769 9.175 1.00106.13 O
ANISOU 3227 O ALA A 288 14383 15049 10891 1114 -751 69 O
ATOM 3228 CB ALA A 288 -7.336 17.451 11.459 1.00 70.54 C
ANISOU 3228 CB ALA A 288 9723 10517 6562 1170 -888 -95 C
ATOM 3229 N GLY A 289 -5.740 18.770 9.019 1.00 75.81 N
ANISOU 3229 N GLY A 289 10384 11318 7104 1070 -707 -18 N
ATOM 3230 CA GLY A 289 -5.086 19.936 8.461 1.00 81.27 C
ANISOU 3230 CA GLY A 289 11101 12016 7762 997 -633 45 C
ATOM 3231 C GLY A 289 -5.657 20.401 7.139 1.00 88.84 C
ANISOU 3231 C GLY A 289 12122 13012 8622 1017 -587 96 C
ATOM 3232 O GLY A 289 -6.273 21.469 7.064 1.00 92.00 O
ANISOU 3232 O GLY A 289 12610 13356 8988 999 -576 167 O
ATOM 3233 N GLY A 290 -5.457 19.610 6.084 1.00 74.08 N
ANISOU 3233 N GLY A 290 10206 11236 6706 1053 -560 60 N
ATOM 3234 CA GLY A 290 -5.977 19.990 4.782 1.00 70.47 C
ANISOU 3234 CA GLY A 290 9803 10820 6153 1075 -516 105 C
ATOM 3235 C GLY A 290 -7.487 20.092 4.748 1.00 89.36 C
ANISOU 3235 C GLY A 290 12282 13164 8505 1137 -561 135 C
ATOM 3236 O GLY A 290 -8.043 20.900 4.000 1.00106.65 O
ANISOU 3236 O GLY A 290 14547 15349 10627 1136 -528 199 O
ATOM 3237 N GLY A 291 -8.173 19.293 5.565 1.00113.91 N
ANISOU 3237 N GLY A 291 15385 16238 11659 1192 -636 90 N
ATOM 3238 CA GLY A 291 -9.623 19.255 5.496 1.00113.00 C
ANISOU 3238 CA GLY A 291 15345 16083 11505 1258 -681 112 C
ATOM 3239 C GLY A 291 -10.279 20.545 5.940 1.00120.62 C
ANISOU 3239 C GLY A 291 16410 16956 12462 1228 -685 191 C
ATOM 3240 O GLY A 291 -11.336 20.918 5.425 1.00139.20 O
ANISOU 3240 O GLY A 291 18842 19293 14755 1265 -689 236 O
ATOM 3241 N LEU A 292 -9.665 21.247 6.884 1.00120.77 N
ANISOU 3241 N LEU A 292 16427 16915 12543 1161 -683 210 N
ATOM 3242 CA LEU A 292 -10.260 22.450 7.445 1.00141.99 C
ANISOU 3242 CA LEU A 292 19207 19510 15234 1131 -692 282 C
ATOM 3243 C LEU A 292 -9.466 23.713 7.150 1.00134.98 C
ANISOU 3243 C LEU A 292 18343 18614 14329 1046 -621 345 C
ATOM 3244 O LEU A 292 -10.062 24.736 6.808 1.00133.33 O
ANISOU 3244 O LEU A 292 18221 18367 14072 1033 -598 418 O
ATOM 3245 CB LEU A 292 -10.433 22.287 8.964 1.00142.41 C
ANISOU 3245 CB LEU A 292 19254 19480 15374 1130 -761 258 C
ATOM 3246 CG LEU A 292 -11.552 23.132 9.573 1.00139.26 C
ANISOU 3246 CG LEU A 292 18957 18983 14973 1138 -797 317 C
ATOM 3247 CD1 LEU A 292 -12.910 22.698 9.038 1.00122.89 C
ANISOU 3247 CD1 LEU A 292 16936 16915 12841 1223 -831 322 C
ATOM 3248 CD2 LEU A 292 -11.518 23.063 11.091 1.00145.93 C
ANISOU 3248 CD2 LEU A 292 19790 19748 15909 1124 -857 294 C
ATOM 3249 N LEU A 293 -8.135 23.675 7.266 1.00109.07 N
ANISOU 3249 N LEU A 293 14986 15367 11087 986 -584 320 N
ATOM 3250 CA LEU A 293 -7.341 24.877 7.021 1.00 97.04 C
ANISOU 3250 CA LEU A 293 13483 13836 9553 902 -517 379 C
ATOM 3251 C LEU A 293 -7.394 25.287 5.555 1.00100.54 C
ANISOU 3251 C LEU A 293 13957 14343 9903 904 -450 422 C
ATOM 3252 O LEU A 293 -7.565 26.470 5.238 1.00118.05 O
ANISOU 3252 O LEU A 293 16246 16527 12081 865 -411 497 O
ATOM 3253 CB LEU A 293 -5.894 24.664 7.461 1.00 82.18 C
ANISOU 3253 CB LEU A 293 11509 11982 7734 841 -494 339 C
ATOM 3254 CG LEU A 293 -5.661 24.543 8.964 1.00 79.55 C
ANISOU 3254 CG LEU A 293 11151 11579 7497 819 -549 310 C
ATOM 3255 CD1 LEU A 293 -4.194 24.775 9.290 1.00 88.86 C
ANISOU 3255 CD1 LEU A 293 12259 12776 8727 739 -510 296 C
ATOM 3256 CD2 LEU A 293 -6.550 25.513 9.723 1.00 91.24 C
ANISOU 3256 CD2 LEU A 293 12727 12952 8987 809 -581 369 C
ATOM 3257 N ARG A 294 -7.231 24.325 4.644 1.00 85.79 N
ANISOU 3257 N ARG A 294 12033 12567 7996 947 -435 376 N
ATOM 3258 CA ARG A 294 -7.385 24.638 3.228 1.00 92.85 C
ANISOU 3258 CA ARG A 294 12957 13523 8798 957 -376 414 C
ATOM 3259 C ARG A 294 -8.814 25.050 2.908 1.00 94.27 C
ANISOU 3259 C ARG A 294 13237 13662 8919 1007 -397 464 C
ATOM 3260 O ARG A 294 -9.038 25.853 1.995 1.00 88.63 O
ANISOU 3260 O ARG A 294 12581 12962 8134 994 -347 525 O
ATOM 3261 CB ARG A 294 -6.966 23.444 2.371 1.00 87.17 C
ANISOU 3261 CB ARG A 294 12157 12909 8053 999 -361 349 C
ATOM 3262 CG ARG A 294 -5.514 23.039 2.548 1.00 55.83 C
ANISOU 3262 CG ARG A 294 8088 8990 4135 950 -332 301 C
ATOM 3263 CD ARG A 294 -4.578 24.167 2.150 1.00 56.76 C
ANISOU 3263 CD ARG A 294 8214 9117 4237 865 -256 357 C
ATOM 3264 N SER A 295 -9.786 24.524 3.652 1.00 85.09 N
ANISOU 3264 N SER A 295 12098 12449 7784 1064 -472 440 N
ATOM 3265 CA SER A 295 -11.181 24.916 3.501 1.00 84.74 C
ANISOU 3265 CA SER A 295 12149 12357 7691 1112 -500 487 C
ATOM 3266 C SER A 295 -11.530 26.169 4.293 1.00 93.54 C
ANISOU 3266 C SER A 295 13344 13368 8827 1067 -507 556 C
ATOM 3267 O SER A 295 -12.707 26.543 4.343 1.00110.92 O
ANISOU 3267 O SER A 295 15627 15518 10998 1104 -536 596 O
ATOM 3268 CB SER A 295 -12.101 23.769 3.927 1.00 80.46 C
ANISOU 3268 CB SER A 295 11595 11807 7168 1196 -577 431 C
ATOM 3269 OG SER A 295 -11.917 22.627 3.110 1.00 88.43 O
ANISOU 3269 OG SER A 295 12540 12910 8148 1244 -571 371 O
ATOM 3270 N ALA A 296 -10.550 26.815 4.920 1.00 93.02 N
ANISOU 3270 N ALA A 296 13257 13272 8815 989 -483 569 N
ATOM 3271 CA ALA A 296 -10.744 28.067 5.640 1.00 79.84 C
ANISOU 3271 CA ALA A 296 11661 11509 7167 937 -483 635 C
ATOM 3272 C ALA A 296 -9.702 29.088 5.216 1.00 76.63 C
ANISOU 3272 C ALA A 296 11252 11116 6747 852 -406 682 C
ATOM 3273 O ALA A 296 -9.223 29.889 6.023 1.00 84.47 O
ANISOU 3273 O ALA A 296 12258 12047 7789 787 -400 710 O
ATOM 3274 CB ALA A 296 -10.700 27.851 7.149 1.00 63.85 C
ANISOU 3274 CB ALA A 296 9616 9409 5234 928 -547 602 C
ATOM 3275 N GLY A 297 -9.332 29.067 3.936 1.00 85.65 N
ANISOU 3275 N GLY A 297 12378 12343 7823 850 -344 691 N
ATOM 3276 CA GLY A 297 -8.388 30.028 3.394 1.00 94.68 C
ANISOU 3276 CA GLY A 297 13523 13507 8946 773 -267 739 C
ATOM 3277 C GLY A 297 -7.069 29.408 2.985 1.00 95.37 C
ANISOU 3277 C GLY A 297 13507 13681 9049 743 -226 688 C
ATOM 3278 O GLY A 297 -6.192 29.190 3.825 1.00100.63 O
ANISOU 3278 O GLY A 297 14110 14335 9789 703 -238 650 O
ATOM 3279 N VAL A 298 -6.919 29.118 1.691 1.00 81.36 N
ANISOU 3279 N VAL A 298 11714 11996 7205 764 -178 685 N
ATOM 3280 CA VAL A 298 -5.677 28.527 1.203 1.00 83.90 C
ANISOU 3280 CA VAL A 298 11939 12406 7535 739 -136 638 C
ATOM 3281 C VAL A 298 -4.521 29.511 1.336 1.00 91.60 C
ANISOU 3281 C VAL A 298 12900 13369 8533 643 -77 676 C
ATOM 3282 O VAL A 298 -3.383 29.110 1.616 1.00 92.64 O
ANISOU 3282 O VAL A 298 12947 13536 8715 605 -64 632 O
ATOM 3283 CB VAL A 298 -5.852 28.042 -0.248 1.00 88.28 C
ANISOU 3283 CB VAL A 298 12482 13055 8004 785 -97 632 C
ATOM 3284 CG1 VAL A 298 -4.548 27.485 -0.791 1.00 63.79 C
ANISOU 3284 CG1 VAL A 298 9283 10045 4909 756 -49 587 C
ATOM 3285 CG2 VAL A 298 -6.954 26.990 -0.323 1.00 85.01 C
ANISOU 3285 CG2 VAL A 298 12075 12653 7572 880 -158 588 C
ATOM 3286 N GLY A 299 -4.782 30.808 1.156 1.00 88.81 N
ANISOU 3286 N GLY A 299 12629 12968 8147 601 -43 758 N
ATOM 3287 CA GLY A 299 -3.735 31.795 1.365 1.00 89.54 C
ANISOU 3287 CA GLY A 299 12714 13040 8265 508 8 796 C
ATOM 3288 C GLY A 299 -3.315 31.921 2.816 1.00 97.67 C
ANISOU 3288 C GLY A 299 13722 13997 9390 466 -33 777 C
ATOM 3289 O GLY A 299 -2.137 32.155 3.106 1.00 76.30 O
ANISOU 3289 O GLY A 299 10962 11301 6726 398 -2 769 O
ATOM 3290 N PHE A 300 -4.262 31.760 3.745 1.00103.43 N
ANISOU 3290 N PHE A 300 14493 14652 10154 505 -104 769 N
ATOM 3291 CA PHE A 300 -3.936 31.843 5.165 1.00 79.02 C
ANISOU 3291 CA PHE A 300 11384 11487 7153 470 -148 750 C
ATOM 3292 C PHE A 300 -2.976 30.739 5.583 1.00 75.79 C
ANISOU 3292 C PHE A 300 10863 11129 6806 468 -165 666 C
ATOM 3293 O PHE A 300 -2.170 30.934 6.500 1.00 77.57 O
ANISOU 3293 O PHE A 300 11051 11321 7103 412 -171 653 O
ATOM 3294 CB PHE A 300 -5.223 31.783 5.992 1.00 68.26 C
ANISOU 3294 CB PHE A 300 10086 10041 5808 522 -223 755 C
ATOM 3295 CG PHE A 300 -4.998 31.737 7.475 1.00 81.87 C
ANISOU 3295 CG PHE A 300 11791 11692 7625 497 -276 728 C
ATOM 3296 CD1 PHE A 300 -4.561 32.858 8.160 1.00 90.83 C
ANISOU 3296 CD1 PHE A 300 12958 12756 8796 420 -260 776 C
ATOM 3297 CD2 PHE A 300 -5.244 30.574 8.188 1.00 87.64 C
ANISOU 3297 CD2 PHE A 300 12471 12422 8407 550 -344 656 C
ATOM 3298 CE1 PHE A 300 -4.360 32.816 9.528 1.00101.77 C
ANISOU 3298 CE1 PHE A 300 14326 14074 10267 397 -309 751 C
ATOM 3299 CE2 PHE A 300 -5.044 30.528 9.556 1.00 80.66 C
ANISOU 3299 CE2 PHE A 300 11569 11470 7608 527 -393 632 C
ATOM 3300 CZ PHE A 300 -4.602 31.650 10.226 1.00 82.89 C
ANISOU 3300 CZ PHE A 300 11884 11685 7926 451 -376 679 C
ATOM 3301 N VAL A 301 -3.036 29.583 4.916 1.00 82.56 N
ANISOU 3301 N VAL A 301 11665 12068 7637 529 -171 610 N
ATOM 3302 CA VAL A 301 -2.156 28.468 5.258 1.00 74.77 C
ANISOU 3302 CA VAL A 301 10570 11133 6706 533 -187 528 C
ATOM 3303 C VAL A 301 -0.712 28.786 4.889 1.00 83.98 C
ANISOU 3303 C VAL A 301 11674 12353 7881 458 -119 530 C
ATOM 3304 O VAL A 301 0.214 28.530 5.670 1.00 86.79 O
ANISOU 3304 O VAL A 301 11962 12705 8309 417 -128 492 O
ATOM 3305 CB VAL A 301 -2.643 27.179 4.570 1.00 57.69 C
ANISOU 3305 CB VAL A 301 8370 9044 4507 619 -210 471 C
ATOM 3306 CG1 VAL A 301 -1.695 26.028 4.858 1.00 57.31 C
ANISOU 3306 CG1 VAL A 301 8208 9054 4513 623 -222 387 C
ATOM 3307 CG2 VAL A 301 -4.061 26.839 5.015 1.00 64.56 C
ANISOU 3307 CG2 VAL A 301 9298 9857 5373 693 -281 466 C
ATOM 3308 N ALA A 302 -0.497 29.348 3.696 1.00 85.08 N
ANISOU 3308 N ALA A 302 11835 12543 7948 438 -49 575 N
ATOM 3309 CA ALA A 302 0.861 29.596 3.219 1.00102.72 C
ANISOU 3309 CA ALA A 302 14008 14838 10184 371 19 577 C
ATOM 3310 C ALA A 302 1.607 30.563 4.131 1.00 93.82 C
ANISOU 3310 C ALA A 302 12886 13645 9117 283 32 609 C
ATOM 3311 O ALA A 302 2.787 30.352 4.437 1.00 84.95 O
ANISOU 3311 O ALA A 302 11684 12551 8043 234 51 576 O
ATOM 3312 CB ALA A 302 0.822 30.127 1.785 1.00114.80 C
ANISOU 3312 CB ALA A 302 15572 16425 11622 367 90 627 C
ATOM 3313 N LYS A 303 0.928 31.623 4.588 1.00 77.12 N
ANISOU 3313 N LYS A 303 10862 11440 6999 262 20 673 N
ATOM 3314 CA LYS A 303 1.553 32.589 5.488 1.00 93.64 C
ANISOU 3314 CA LYS A 303 12968 13464 9149 179 29 707 C
ATOM 3315 C LYS A 303 2.094 31.919 6.744 1.00108.91 C
ANISOU 3315 C LYS A 303 14831 15372 11177 168 -23 643 C
ATOM 3316 O LYS A 303 3.120 32.346 7.283 1.00114.70 O
ANISOU 3316 O LYS A 303 15527 16091 11961 95 -1 645 O
ATOM 3317 CB LYS A 303 0.552 33.683 5.865 1.00 89.46 C
ANISOU 3317 CB LYS A 303 12550 12837 8604 173 12 778 C
ATOM 3318 CG LYS A 303 -0.144 34.356 4.679 1.00 85.26 C
ANISOU 3318 CG LYS A 303 12097 12322 7977 190 57 844 C
ATOM 3319 CD LYS A 303 0.829 35.194 3.859 1.00101.22 C
ANISOU 3319 CD LYS A 303 14109 14385 9963 118 142 890 C
ATOM 3320 CE LYS A 303 0.191 35.731 2.572 1.00 93.78 C
ANISOU 3320 CE LYS A 303 13235 13473 8923 141 189 949 C
ATOM 3321 NZ LYS A 303 -0.961 36.658 2.789 1.00 79.42 N
ANISOU 3321 NZ LYS A 303 11529 11568 7079 151 170 1016 N
ATOM 3322 N LEU A 304 1.427 30.863 7.214 1.00100.71 N
ANISOU 3322 N LEU A 304 13773 14328 10162 240 -90 586 N
ATOM 3323 CA LEU A 304 1.946 30.106 8.347 1.00 92.21 C
ANISOU 3323 CA LEU A 304 12623 13236 9174 236 -140 520 C
ATOM 3324 C LEU A 304 3.158 29.278 7.947 1.00 95.23 C
ANISOU 3324 C LEU A 304 12895 13713 9573 221 -108 462 C
ATOM 3325 O LEU A 304 4.163 29.247 8.667 1.00 89.40 O
ANISOU 3325 O LEU A 304 12096 12970 8901 168 -106 436 O
ATOM 3326 CB LEU A 304 0.856 29.204 8.919 1.00 74.41 C
ANISOU 3326 CB LEU A 304 10381 10952 6939 319 -220 477 C
ATOM 3327 CG LEU A 304 -0.455 29.876 9.324 1.00 79.36 C
ANISOU 3327 CG LEU A 304 11115 11488 7549 345 -259 528 C
ATOM 3328 CD1 LEU A 304 -1.462 28.831 9.780 1.00 64.08 C
ANISOU 3328 CD1 LEU A 304 9180 9537 5629 432 -336 478 C
ATOM 3329 CD2 LEU A 304 -0.213 30.911 10.414 1.00 83.95 C
ANISOU 3329 CD2 LEU A 304 11734 11976 8187 276 -268 568 C
ATOM 3330 N LEU A 305 3.083 28.604 6.799 1.00103.21 N
ANISOU 3330 N LEU A 305 13880 14812 10523 269 -81 440 N
ATOM 3331 CA LEU A 305 4.171 27.741 6.363 1.00108.63 C
ANISOU 3331 CA LEU A 305 14462 15592 11221 263 -52 382 C
ATOM 3332 C LEU A 305 5.400 28.522 5.922 1.00126.97 C
ANISOU 3332 C LEU A 305 16757 17949 13538 177 24 416 C
ATOM 3333 O LEU A 305 6.499 27.958 5.912 1.00121.25 O
ANISOU 3333 O LEU A 305 15940 17283 12845 153 45 369 O
ATOM 3334 CB LEU A 305 3.694 26.840 5.225 1.00 98.26 C
ANISOU 3334 CB LEU A 305 13133 14360 9840 339 -45 352 C
ATOM 3335 CG LEU A 305 2.697 25.751 5.615 1.00 75.03 C
ANISOU 3335 CG LEU A 305 10189 11407 6910 428 -120 299 C
ATOM 3336 CD1 LEU A 305 2.003 25.220 4.381 1.00 62.08 C
ANISOU 3336 CD1 LEU A 305 8567 9833 5188 498 -107 294 C
ATOM 3337 CD2 LEU A 305 3.400 24.625 6.356 1.00 66.52 C
ANISOU 3337 CD2 LEU A 305 9011 10355 5907 437 -157 215 C
ATOM 3338 N GLU A 306 5.244 29.800 5.557 1.00146.23 N
ANISOU 3338 N GLU A 306 19273 20352 15936 132 68 496 N
ATOM 3339 CA GLU A 306 6.397 30.588 5.126 1.00138.38 C
ANISOU 3339 CA GLU A 306 18256 19389 14935 49 142 531 C
ATOM 3340 C GLU A 306 7.430 30.738 6.236 1.00131.16 C
ANISOU 3340 C GLU A 306 17285 18440 14108 -20 133 510 C
ATOM 3341 O GLU A 306 8.623 30.896 5.952 1.00147.64 O
ANISOU 3341 O GLU A 306 19313 20576 16205 -78 185 508 O
ATOM 3342 CB GLU A 306 5.953 31.967 4.634 1.00134.12 C
ANISOU 3342 CB GLU A 306 17815 18805 14339 14 184 623 C
ATOM 3343 CG GLU A 306 5.476 32.001 3.190 1.00136.79 C
ANISOU 3343 CG GLU A 306 18187 19207 14580 53 228 652 C
ATOM 3344 CD GLU A 306 5.236 33.415 2.695 1.00141.45 C
ANISOU 3344 CD GLU A 306 18866 19760 15119 7 278 743 C
ATOM 3345 OE1 GLU A 306 6.103 34.284 2.934 1.00139.99 O
ANISOU 3345 OE1 GLU A 306 18677 19555 14960 -75 319 778 O
ATOM 3346 OE2 GLU A 306 4.178 33.660 2.077 1.00134.16 O
ANISOU 3346 OE2 GLU A 306 18017 18826 14130 53 277 780 O
ATOM 3347 N GLY A 307 7.004 30.692 7.496 1.00 93.53 N
ANISOU 3347 N GLY A 307 12537 13593 9407 -14 67 496 N
ATOM 3348 CA GLY A 307 7.944 30.758 8.599 1.00102.04 C
ANISOU 3348 CA GLY A 307 13560 14639 10570 -75 53 471 C
ATOM 3349 C GLY A 307 8.734 29.478 8.773 1.00120.53 C
ANISOU 3349 C GLY A 307 15789 17049 12956 -55 38 387 C
ATOM 3350 O GLY A 307 8.812 28.662 7.849 1.00113.33 O
ANISOU 3350 O GLY A 307 14834 16224 12003 -10 57 352 O
ATOM 3351 N THR A 308 9.332 29.289 9.953 1.00135.23 N
ANISOU 3351 N THR A 308 17602 18875 14904 -89 3 352 N
ATOM 3352 CA THR A 308 10.057 28.052 10.230 1.00130.52 C
ANISOU 3352 CA THR A 308 16899 18338 14356 -69 -17 269 C
ATOM 3353 C THR A 308 9.152 26.831 10.179 1.00142.20 C
ANISOU 3353 C THR A 308 18367 19838 15826 29 -74 213 C
ATOM 3354 O THR A 308 9.642 25.722 9.938 1.00149.03 O
ANISOU 3354 O THR A 308 19146 20776 16702 60 -77 148 O
ATOM 3355 CB THR A 308 10.736 28.129 11.601 1.00118.34 C
ANISOU 3355 CB THR A 308 15315 16742 12908 -121 -50 246 C
ATOM 3356 OG1 THR A 308 9.744 28.328 12.619 1.00122.03 O
ANISOU 3356 OG1 THR A 308 15846 17113 13408 -97 -117 256 O
ATOM 3357 CG2 THR A 308 11.729 29.284 11.647 1.00114.18 C
ANISOU 3357 CG2 THR A 308 14790 16200 12392 -221 8 297 C
ATOM 3358 N GLY A 309 7.851 27.010 10.391 1.00122.28 N
ANISOU 3358 N GLY A 309 15926 17252 13282 78 -119 237 N
ATOM 3359 CA GLY A 309 6.904 25.916 10.388 1.00123.86 C
ANISOU 3359 CA GLY A 309 16124 17464 13474 171 -176 188 C
ATOM 3360 C GLY A 309 6.273 25.630 11.728 1.00 98.34 C
ANISOU 3360 C GLY A 309 12907 14150 10308 196 -257 163 C
ATOM 3361 O GLY A 309 5.406 24.753 11.806 1.00 89.07 O
ANISOU 3361 O GLY A 309 11736 12977 9129 275 -309 124 O
ATOM 3362 N ALA A 310 6.670 26.342 12.784 1.00 97.65 N
ANISOU 3362 N ALA A 310 12830 13991 10283 133 -269 183 N
ATOM 3363 CA ALA A 310 6.115 26.076 14.105 1.00116.30 C
ANISOU 3363 CA ALA A 310 15203 16274 12710 155 -346 158 C
ATOM 3364 C ALA A 310 4.667 26.540 14.202 1.00108.12 C
ANISOU 3364 C ALA A 310 14274 15166 11640 200 -383 202 C
ATOM 3365 O ALA A 310 3.834 25.867 14.821 1.00113.53 O
ANISOU 3365 O ALA A 310 14969 15817 12350 261 -451 168 O
ATOM 3366 CB ALA A 310 6.973 26.750 15.175 1.00118.22 C
ANISOU 3366 CB ALA A 310 15428 16462 13027 72 -346 170 C
ATOM 3367 N GLU A 311 4.343 27.682 13.591 1.00 91.05 N
ANISOU 3367 N GLU A 311 12194 12981 9421 171 -340 279 N
ATOM 3368 CA GLU A 311 2.978 28.189 13.666 1.00 97.32 C
ANISOU 3368 CA GLU A 311 13091 13705 10180 210 -372 325 C
ATOM 3369 C GLU A 311 1.990 27.309 12.912 1.00 81.80 C
ANISOU 3369 C GLU A 311 11139 11784 8159 304 -395 300 C
ATOM 3370 O GLU A 311 0.793 27.348 13.215 1.00 69.98 O
ANISOU 3370 O GLU A 311 9710 10230 6651 354 -443 316 O
ATOM 3371 CB GLU A 311 2.909 29.626 13.142 1.00 87.30 C
ANISOU 3371 CB GLU A 311 11904 12405 8860 155 -315 413 C
ATOM 3372 CG GLU A 311 3.555 29.847 11.781 1.00107.08 C
ANISOU 3372 CG GLU A 311 14390 14996 11300 131 -235 435 C
ATOM 3373 CD GLU A 311 4.980 30.367 11.880 1.00114.41 C
ANISOU 3373 CD GLU A 311 15264 15945 12261 40 -182 443 C
ATOM 3374 OE1 GLU A 311 5.816 29.714 12.541 1.00107.89 O
ANISOU 3374 OE1 GLU A 311 14354 15137 11502 23 -200 386 O
ATOM 3375 OE2 GLU A 311 5.261 31.438 11.300 1.00111.07 O
ANISOU 3375 OE2 GLU A 311 14884 15519 11798 -14 -122 507 O
ATOM 3376 N PHE A 312 2.454 26.512 11.948 1.00 64.90 N
ANISOU 3376 N PHE A 312 8934 9741 5984 329 -362 262 N
ATOM 3377 CA PHE A 312 1.543 25.615 11.246 1.00 63.43 C
ANISOU 3377 CA PHE A 312 8755 9599 5747 419 -386 234 C
ATOM 3378 C PHE A 312 1.084 24.483 12.156 1.00 84.35 C
ANISOU 3378 C PHE A 312 11368 12229 8454 480 -466 165 C
ATOM 3379 O PHE A 312 -0.110 24.170 12.218 1.00 92.77 O
ANISOU 3379 O PHE A 312 12484 13266 9500 547 -514 164 O
ATOM 3380 CB PHE A 312 2.210 25.060 9.988 1.00 72.88 C
ANISOU 3380 CB PHE A 312 9891 10907 6893 428 -329 209 C
ATOM 3381 CG PHE A 312 1.325 24.147 9.186 1.00 71.60 C
ANISOU 3381 CG PHE A 312 9734 10795 6674 518 -348 180 C
ATOM 3382 CD1 PHE A 312 0.300 24.661 8.410 1.00 64.71 C
ANISOU 3382 CD1 PHE A 312 8949 9912 5726 551 -336 234 C
ATOM 3383 CD2 PHE A 312 1.522 22.776 9.204 1.00 66.89 C
ANISOU 3383 CD2 PHE A 312 9056 10257 6102 569 -378 100 C
ATOM 3384 CE1 PHE A 312 -0.516 23.825 7.671 1.00 66.32 C
ANISOU 3384 CE1 PHE A 312 9158 10162 5877 633 -354 208 C
ATOM 3385 CE2 PHE A 312 0.710 21.934 8.465 1.00 81.47 C
ANISOU 3385 CE2 PHE A 312 10909 12150 7898 652 -396 73 C
ATOM 3386 CZ PHE A 312 -0.310 22.460 7.698 1.00 69.55 C
ANISOU 3386 CZ PHE A 312 9486 10628 6311 683 -385 127 C
ATOM 3387 N LEU A 313 2.020 23.863 12.879 1.00 85.87 N
ANISOU 3387 N LEU A 313 11471 12436 8718 456 -481 108 N
ATOM 3388 CA LEU A 313 1.656 22.760 13.764 1.00 83.71 C
ANISOU 3388 CA LEU A 313 11156 12146 8502 512 -556 40 C
ATOM 3389 C LEU A 313 0.751 23.227 14.898 1.00 79.91 C
ANISOU 3389 C LEU A 313 10746 11557 8059 519 -618 65 C
ATOM 3390 O LEU A 313 -0.224 22.549 15.242 1.00 88.96 O
ANISOU 3390 O LEU A 313 11910 12680 9212 590 -679 37 O
ATOM 3391 CB LEU A 313 2.913 22.097 14.325 1.00 68.03 C
ANISOU 3391 CB LEU A 313 9063 10198 6588 478 -556 -22 C
ATOM 3392 CG LEU A 313 3.746 21.276 13.346 1.00 76.60 C
ANISOU 3392 CG LEU A 313 10063 11394 7646 488 -511 -67 C
ATOM 3393 CD1 LEU A 313 4.917 20.664 14.085 1.00 82.71 C
ANISOU 3393 CD1 LEU A 313 10736 12192 8500 455 -519 -126 C
ATOM 3394 CD2 LEU A 313 2.894 20.200 12.687 1.00 58.91 C
ANISOU 3394 CD2 LEU A 313 7819 9202 5363 582 -539 -107 C
ATOM 3395 N GLU A 314 1.059 24.383 15.494 1.00 81.49 N
ANISOU 3395 N GLU A 314 10986 11691 8285 447 -602 117 N
ATOM 3396 CA GLU A 314 0.245 24.883 16.598 1.00 91.84 C
ANISOU 3396 CA GLU A 314 12364 12897 9634 451 -659 142 C
ATOM 3397 C GLU A 314 -1.177 25.201 16.155 1.00 80.34 C
ANISOU 3397 C GLU A 314 11006 11406 8114 507 -677 187 C
ATOM 3398 O GLU A 314 -2.114 25.065 16.948 1.00100.48 O
ANISOU 3398 O GLU A 314 13599 13889 10690 548 -741 183 O
ATOM 3399 CB GLU A 314 0.897 26.117 17.223 1.00101.82 C
ANISOU 3399 CB GLU A 314 13654 14100 10932 359 -632 193 C
ATOM 3400 CG GLU A 314 1.897 25.812 18.338 1.00 95.69 C
ANISOU 3400 CG GLU A 314 12801 13310 10248 314 -653 147 C
ATOM 3401 CD GLU A 314 3.337 25.839 17.866 1.00108.19 C
ANISOU 3401 CD GLU A 314 14306 14964 11837 251 -590 134 C
ATOM 3402 OE1 GLU A 314 3.891 26.947 17.704 1.00120.53 O
ANISOU 3402 OE1 GLU A 314 15897 16510 13390 177 -538 189 O
ATOM 3403 OE2 GLU A 314 3.910 24.752 17.650 1.00 98.71 O
ANISOU 3403 OE2 GLU A 314 13016 13837 10653 276 -591 69 O
ATOM 3404 N VAL A 315 -1.362 25.604 14.897 1.00 52.68 N
ANISOU 3404 N VAL A 315 7540 7948 4529 511 -622 228 N
ATOM 3405 CA VAL A 315 -2.708 25.895 14.412 1.00 73.89 C
ANISOU 3405 CA VAL A 315 10319 10606 7151 566 -637 271 C
ATOM 3406 C VAL A 315 -3.485 24.604 14.162 1.00 82.97 C
ANISOU 3406 C VAL A 315 11445 11795 8285 661 -685 214 C
ATOM 3407 O VAL A 315 -4.709 24.564 14.350 1.00103.36 O
ANISOU 3407 O VAL A 315 14091 14330 10849 716 -732 229 O
ATOM 3408 CB VAL A 315 -2.637 26.789 13.156 1.00 56.55 C
ANISOU 3408 CB VAL A 315 8171 8444 4871 537 -561 336 C
ATOM 3409 CG1 VAL A 315 -3.976 26.840 12.438 1.00 55.43 C
ANISOU 3409 CG1 VAL A 315 8109 8297 4655 605 -573 369 C
ATOM 3410 CG2 VAL A 315 -2.208 28.199 13.537 1.00 53.74 C
ANISOU 3410 CG2 VAL A 315 7865 8026 4529 452 -526 404 C
ATOM 3411 N LEU A 316 -2.801 23.528 13.757 1.00 74.47 N
ANISOU 3411 N LEU A 316 10276 10803 7216 681 -676 149 N
ATOM 3412 CA LEU A 316 -3.471 22.240 13.579 1.00 61.56 C
ANISOU 3412 CA LEU A 316 8611 9206 5572 769 -723 89 C
ATOM 3413 C LEU A 316 -4.044 21.734 14.896 1.00 79.60 C
ANISOU 3413 C LEU A 316 10895 11422 7928 803 -806 54 C
ATOM 3414 O LEU A 316 -5.188 21.267 14.955 1.00 78.22 O
ANISOU 3414 O LEU A 316 10759 11226 7736 874 -857 45 O
ATOM 3415 CB LEU A 316 -2.496 21.209 13.006 1.00 62.00 C
ANISOU 3415 CB LEU A 316 8563 9364 5633 776 -697 24 C
ATOM 3416 CG LEU A 316 -1.800 21.507 11.680 1.00 78.49 C
ANISOU 3416 CG LEU A 316 10634 11534 7656 746 -615 46 C
ATOM 3417 CD1 LEU A 316 -0.774 20.429 11.366 1.00 75.39 C
ANISOU 3417 CD1 LEU A 316 10130 11232 7283 751 -597 -26 C
ATOM 3418 CD2 LEU A 316 -2.813 21.614 10.566 1.00 78.06 C
ANISOU 3418 CD2 LEU A 316 10646 11503 7510 800 -600 81 C
ATOM 3419 N PHE A 317 -3.254 21.809 15.962 1.00 82.40 N
ANISOU 3419 N PHE A 317 11205 11742 8361 753 -822 33 N
ATOM 3420 CA PHE A 317 -3.685 21.410 17.294 1.00 82.30 C
ANISOU 3420 CA PHE A 317 11188 11659 8421 776 -898 1 C
ATOM 3421 C PHE A 317 -4.536 22.467 17.984 1.00106.73 C
ANISOU 3421 C PHE A 317 14383 14650 11520 761 -924 64 C
ATOM 3422 O PHE A 317 -4.706 22.393 19.207 1.00102.23 O
ANISOU 3422 O PHE A 317 13812 14012 11017 760 -980 48 O
ATOM 3423 CB PHE A 317 -2.461 21.079 18.152 1.00 79.64 C
ANISOU 3423 CB PHE A 317 10763 11330 8167 725 -902 -47 C
ATOM 3424 CG PHE A 317 -1.817 19.773 17.798 1.00 74.80 C
ANISOU 3424 CG PHE A 317 10047 10805 7567 757 -902 -124 C
ATOM 3425 CD1 PHE A 317 -1.077 19.639 16.634 1.00 70.54 C
ANISOU 3425 CD1 PHE A 317 9466 10357 6980 742 -836 -129 C
ATOM 3426 CD2 PHE A 317 -1.966 18.675 18.622 1.00 71.10 C
ANISOU 3426 CD2 PHE A 317 9525 10331 7159 804 -967 -192 C
ATOM 3427 CE1 PHE A 317 -0.496 18.433 16.306 1.00 64.38 C
ANISOU 3427 CE1 PHE A 317 8592 9659 6212 773 -835 -200 C
ATOM 3428 CE2 PHE A 317 -1.390 17.470 18.300 1.00 68.38 C
ANISOU 3428 CE2 PHE A 317 9087 10067 6826 834 -966 -263 C
ATOM 3429 CZ PHE A 317 -0.654 17.347 17.141 1.00 82.61 C
ANISOU 3429 CZ PHE A 317 10849 11959 8581 819 -901 -268 C
ATOM 3430 N GLN A 318 -5.062 23.433 17.229 1.00152.79 N
ANISOU 3430 N GLN A 318 20299 20469 17284 751 -886 135 N
ATOM 3431 CA GLN A 318 -5.897 24.527 17.742 1.00140.95 C
ANISOU 3431 CA GLN A 318 18902 18874 15779 737 -903 203 C
ATOM 3432 C GLN A 318 -5.155 25.475 18.691 1.00149.77 C
ANISOU 3432 C GLN A 318 20025 19927 16955 652 -893 232 C
ATOM 3433 O GLN A 318 -5.016 26.670 18.406 1.00160.38 O
ANISOU 3433 O GLN A 318 21425 21242 18268 597 -846 299 O
ATOM 3434 CB GLN A 318 -7.143 23.969 18.436 1.00132.34 C
ANISOU 3434 CB GLN A 318 17847 17730 14706 812 -984 184 C
ATOM 3435 CG GLN A 318 -8.418 24.049 17.606 1.00146.26 C
ANISOU 3435 CG GLN A 318 19688 19494 16390 875 -989 219 C
ATOM 3436 CD GLN A 318 -8.344 23.238 16.327 1.00152.50 C
ANISOU 3436 CD GLN A 318 20436 20386 17120 919 -958 188 C
ATOM 3437 OE1 GLN A 318 -8.163 23.788 15.241 1.00161.18 O
ANISOU 3437 OE1 GLN A 318 21560 21529 18153 898 -895 229 O
ATOM 3438 NE2 GLN A 318 -8.492 21.924 16.449 1.00134.89 N
ANISOU 3438 NE2 GLN A 318 18144 18196 14912 981 -1002 116 N
ATOM 3439 OXT GLN A 318 -4.688 25.078 19.761 1.00169.93 O
ANISOU 3439 OXT GLN A 318 22526 22453 19586 637 -931 189 O
TER 3440 GLN A 318
HETATM 3441 O5 VRJ A2101 1.772 -13.530 20.916 1.00 94.83 O
HETATM 3442 O4 VRJ A2101 2.541 -15.635 19.784 1.00 80.14 O
HETATM 3443 C4 VRJ A2101 3.689 -8.905 17.217 1.00 49.59 C
HETATM 3444 C3 VRJ A2101 3.857 -7.937 18.205 1.00 62.50 C
HETATM 3445 O3 VRJ A2101 3.873 -13.189 18.443 1.00 55.38 O
HETATM 3446 C2 VRJ A2101 3.200 -8.046 19.434 1.00 71.35 C
HETATM 3447 O2 VRJ A2101 4.508 -7.407 21.288 1.00 76.20 O
HETATM 3448 C1 VRJ A2101 2.370 -9.152 19.647 1.00 76.15 C
HETATM 3449 O1 VRJ A2101 1.658 -9.365 20.837 1.00 86.02 O
HETATM 3450 C10 VRJ A2101 2.013 -3.917 20.731 1.00 61.51 C
HETATM 3451 C11 VRJ A2101 2.432 -2.784 20.037 1.00 71.71 C
HETATM 3452 C12 VRJ A2101 2.278 -2.728 18.657 1.00 54.93 C
HETATM 3453 C13 VRJ A2101 1.713 -3.826 18.019 1.00 63.19 C
HETATM 3454 C14 VRJ A2101 2.206 -10.113 18.651 1.00 66.00 C
HETATM 3455 C15 VRJ A2101 2.861 -10.023 17.412 1.00 50.87 C
HETATM 3456 C16 VRJ A2101 2.707 -11.030 16.347 1.00 58.09 C
HETATM 3457 C17 VRJ A2101 2.593 -10.558 15.029 1.00 68.36 C
HETATM 3458 C18 VRJ A2101 2.455 -11.417 13.947 1.00 82.73 C
HETATM 3459 C19 VRJ A2101 2.679 -12.452 16.520 1.00 72.05 C
HETATM 3460 C20 VRJ A2101 2.543 -13.304 15.409 1.00 69.28 C
HETATM 3461 C21 VRJ A2101 2.429 -12.790 14.124 1.00 82.01 C
HETATM 3462 C22 VRJ A2101 2.804 -13.131 17.848 1.00 62.36 C
HETATM 3463 C23 VRJ A2101 -0.077 -15.200 20.005 1.00 89.37 C
HETATM 3464 C24 VRJ A2101 -1.067 -14.155 19.475 1.00 82.28 C
HETATM 3465 C25 VRJ A2101 -0.411 -15.496 21.476 1.00 77.13 C
HETATM 3466 C26 VRJ A2101 -0.229 -16.477 19.166 1.00 92.93 C
HETATM 3467 C5 VRJ A2101 3.379 -7.016 20.509 1.00 65.58 C
HETATM 3468 C6 VRJ A2101 2.154 -6.954 21.430 1.00 67.99 C
HETATM 3469 C7 VRJ A2101 1.811 -8.383 21.885 1.00 75.24 C
HETATM 3470 C8 VRJ A2101 0.986 -6.226 20.732 1.00 68.53 C
HETATM 3471 C9 VRJ A2101 1.451 -4.982 20.014 1.00 69.46 C
HETATM 3472 F1 VRJ A2101 2.345 -10.903 12.711 1.00105.68 F
HETATM 3473 N1 VRJ A2101 1.301 -4.943 18.662 1.00 63.25 N
HETATM 3474 N2 VRJ A2101 1.605 -13.709 18.372 1.00 66.00 N
HETATM 3475 S1 VRJ A2101 1.610 -14.527 19.877 1.00 85.85 S
HETATM 3476 NA NA A2102 1.595 3.713 18.706 1.00 67.22 NA
HETATM 3477 N1 FMN A2103 -54.622 51.409 21.765 1.00 43.35 N
HETATM 3478 C2 FMN A2103 -53.752 52.280 22.394 1.00 43.33 C
HETATM 3479 O2 FMN A2103 -52.596 52.376 21.981 1.00 39.90 O
HETATM 3480 N3 FMN A2103 -54.182 53.036 23.474 1.00 34.35 N
HETATM 3481 C4 FMN A2103 -55.487 52.915 23.924 1.00 65.59 C
HETATM 3482 O4 FMN A2103 -55.895 53.571 24.883 1.00 51.11 O
HETATM 3483 C4A FMN A2103 -56.360 52.040 23.293 1.00 57.81 C
HETATM 3484 N5 FMN A2103 -57.655 51.921 23.749 1.00 42.21 N
HETATM 3485 C5A FMN A2103 -58.529 51.058 23.123 1.00 39.90 C
HETATM 3486 C6 FMN A2103 -59.842 50.941 23.578 1.00 49.10 C
HETATM 3487 C7 FMN A2103 -60.721 50.066 22.947 1.00 49.07 C
HETATM 3488 C7M FMN A2103 -62.136 49.923 23.425 1.00 60.80 C
HETATM 3489 C8 FMN A2103 -60.288 49.313 21.864 1.00 48.15 C
HETATM 3490 C8M FMN A2103 -61.233 48.372 21.180 1.00 58.44 C
HETATM 3491 C9 FMN A2103 -58.982 49.434 21.411 1.00 62.76 C
HETATM 3492 C9A FMN A2103 -58.095 50.305 22.038 1.00 43.49 C
HETATM 3493 N10 FMN A2103 -56.790 50.417 21.589 1.00 47.68 N
HETATM 3494 C10 FMN A2103 -55.923 51.288 22.210 1.00 48.43 C
HETATM 3495 C1' FMN A2103 -56.314 49.616 20.409 1.00 59.76 C
HETATM 3496 C2' FMN A2103 -55.892 48.196 20.773 1.00 53.24 C
HETATM 3497 O2' FMN A2103 -54.777 48.220 21.636 1.00 51.67 O
HETATM 3498 C3' FMN A2103 -55.547 47.446 19.492 1.00 52.11 C
HETATM 3499 O3' FMN A2103 -56.730 47.056 18.833 1.00 49.26 O
HETATM 3500 C4' FMN A2103 -54.716 46.203 19.764 1.00 61.88 C
HETATM 3501 O4' FMN A2103 -54.422 45.577 18.535 1.00 58.78 O
HETATM 3502 C5' FMN A2103 -55.446 45.218 20.668 1.00 34.26 C
HETATM 3503 O5' FMN A2103 -54.678 44.037 20.685 1.00 52.40 O
HETATM 3504 P FMN A2103 -55.192 42.680 21.382 1.00 34.14 P
HETATM 3505 O1P FMN A2103 -56.652 42.840 21.722 1.00 65.34 O
HETATM 3506 O2P FMN A2103 -55.022 41.549 20.400 1.00 52.86 O
HETATM 3507 O3P FMN A2103 -54.400 42.354 22.624 1.00 58.40 O
HETATM 3508 C1 OLA A2104 9.483 17.876 36.311 1.00102.19 C
HETATM 3509 O1 OLA A2104 10.075 18.924 36.659 1.00 88.32 O
HETATM 3510 O2 OLA A2104 8.472 17.508 36.954 1.00103.54 O
HETATM 3511 C2 OLA A2104 9.990 17.061 35.117 1.00 79.95 C
HETATM 3512 C3 OLA A2104 9.008 15.960 34.716 1.00 59.75 C
HETATM 3513 C4 OLA A2104 9.320 14.641 35.418 1.00 57.00 C
HETATM 3514 C5 OLA A2104 9.126 13.462 34.469 1.00 57.06 C
HETATM 3515 C6 OLA A2104 7.651 13.154 34.227 1.00 42.69 C
HETATM 3516 C7 OLA A2104 7.515 11.683 33.847 1.00 40.08 C
HETATM 3517 C8 OLA A2104 6.121 11.346 33.361 1.00 40.88 C
HETATM 3518 C9 OLA A2104 6.066 9.899 32.946 1.00 50.85 C
HETATM 3519 C10 OLA A2104 4.902 9.347 32.620 1.00 49.31 C
HETATM 3520 C24 OLC A2105 -14.272 15.179 36.345 1.00 92.64 C
HETATM 3521 C6 OLC A2105 -5.765 14.072 36.373 1.00 32.09 C
HETATM 3522 C5 OLC A2105 -6.932 14.654 35.594 1.00 40.21 C
HETATM 3523 C4 OLC A2105 -7.097 16.134 35.917 1.00 29.26 C
HETATM 3524 C3 OLC A2105 -8.566 16.502 35.759 1.00 50.28 C
HETATM 3525 C2 OLC A2105 -9.451 15.738 36.751 1.00 72.79 C
HETATM 3526 C21 OLC A2105 -12.045 15.162 37.541 1.00 99.77 C
HETATM 3527 C1 OLC A2105 -10.296 16.746 37.455 1.00 85.90 C
HETATM 3528 C22 OLC A2105 -13.586 15.187 37.752 1.00104.55 C
HETATM 3529 O19 OLC A2105 -9.898 17.726 38.069 1.00 80.67 O
HETATM 3530 O25 OLC A2105 -15.378 16.040 36.449 1.00 56.58 O
HETATM 3531 O23 OLC A2105 -13.981 14.106 38.526 1.00 61.91 O
HETATM 3532 O20 OLC A2105 -11.649 16.521 37.386 1.00 91.89 O
HETATM 3533 C18 OLC A2106 1.945 2.591 36.606 1.00 67.10 C
HETATM 3534 C10 OLC A2106 1.720 11.069 35.647 1.00 82.26 C
HETATM 3535 C9 OLC A2106 1.430 12.271 36.144 1.00 92.25 C
HETATM 3536 C17 OLC A2106 3.206 3.209 36.022 1.00 86.80 C
HETATM 3537 C11 OLC A2106 2.977 10.354 36.020 1.00 85.30 C
HETATM 3538 C8 OLC A2106 2.347 12.965 37.097 1.00 71.31 C
HETATM 3539 C24 OLC A2106 2.972 24.560 39.827 1.00 73.00 C
HETATM 3540 C16 OLC A2106 2.870 4.531 35.345 1.00 65.36 C
HETATM 3541 C12 OLC A2106 2.940 8.914 35.524 1.00 66.77 C
HETATM 3542 C7 OLC A2106 2.146 14.469 37.019 1.00 53.22 C
HETATM 3543 C15 OLC A2106 2.917 5.700 36.321 1.00 74.48 C
HETATM 3544 C13 OLC A2106 2.132 8.075 36.499 1.00 69.11 C
HETATM 3545 C6 OLC A2106 0.845 14.835 37.718 1.00 62.30 C
HETATM 3546 C14 OLC A2106 1.858 6.710 35.900 1.00 68.06 C
HETATM 3547 C5 OLC A2106 0.879 16.298 38.129 1.00 77.81 C
HETATM 3548 C4 OLC A2106 1.002 17.192 36.899 1.00 80.45 C
HETATM 3549 C3 OLC A2106 0.472 18.574 37.251 1.00 77.52 C
HETATM 3550 C2 OLC A2106 1.473 19.362 38.094 1.00 36.58 C
HETATM 3551 C21 OLC A2106 1.472 22.544 39.647 1.00 73.86 C
HETATM 3552 C1 OLC A2106 0.882 20.717 38.284 1.00 46.30 C
HETATM 3553 C22 OLC A2106 2.845 23.045 40.174 1.00101.85 C
HETATM 3554 O19 OLC A2106 -0.302 21.019 38.216 1.00 63.38 O
HETATM 3555 O25 OLC A2106 4.348 24.822 39.864 1.00 56.61 O
HETATM 3556 O23 OLC A2106 2.972 22.813 41.536 1.00 96.20 O
HETATM 3557 O20 OLC A2106 1.796 21.695 38.552 1.00 75.95 O
HETATM 3558 OH2 1PE A2107 -27.180 43.676 32.091 1.00 76.77 O
HETATM 3559 C12 1PE A2107 -28.220 42.784 31.666 1.00 80.69 C
HETATM 3560 C22 1PE A2107 -27.847 42.234 30.295 1.00 73.77 C
HETATM 3561 OH3 1PE A2107 -27.708 40.811 30.326 1.00 57.81 O
HETATM 3562 C13 1PE A2107 -25.816 39.414 29.617 1.00 77.67 C
HETATM 3563 C23 1PE A2107 -26.352 40.452 30.596 1.00 88.37 C
HETATM 3564 OH4 1PE A2107 -25.632 40.051 28.354 1.00 86.40 O
HETATM 3565 C14 1PE A2107 -24.427 40.215 26.280 1.00 63.34 C
HETATM 3566 C24 1PE A2107 -24.519 39.527 27.636 1.00 70.77 C
HETATM 3567 OH5 1PE A2107 -25.107 41.460 26.385 1.00 71.82 O
HETATM 3568 C15 1PE A2107 -24.887 43.802 26.318 1.00 63.89 C
HETATM 3569 C25 1PE A2107 -24.458 42.499 25.664 1.00 58.43 C
HETATM 3570 OH6 1PE A2107 -24.846 43.609 27.731 1.00 62.84 O
HETATM 3571 C16 1PE A2107 -24.510 44.681 29.861 1.00 88.30 C
HETATM 3572 C26 1PE A2107 -25.023 44.835 28.434 1.00 97.23 C
HETATM 3573 OH7 1PE A2107 -24.293 45.978 30.428 1.00 92.96 O
HETATM 3574 O1 2PE A2108 2.646 11.575 32.249 1.00 49.77 O
HETATM 3575 C2 2PE A2108 2.093 12.729 31.677 1.00 58.33 C
HETATM 3576 C3 2PE A2108 2.978 13.946 31.958 1.00 51.89 C
HETATM 3577 O4 2PE A2108 2.929 14.270 33.320 1.00 67.14 O
HETATM 3578 C5 2PE A2108 3.321 15.580 33.624 1.00 58.06 C
HETATM 3579 C6 2PE A2108 2.147 16.534 33.414 1.00 66.65 C
HETATM 3580 O7 2PE A2108 2.503 17.528 32.496 1.00 76.97 O
HETATM 3581 C8 2PE A2108 1.650 18.639 32.496 1.00 56.84 C
HETATM 3582 C9 2PE A2108 1.943 19.523 31.282 1.00 77.11 C
HETATM 3583 O10 2PE A2108 3.040 20.359 31.533 1.00 74.97 O
HETATM 3584 C11 2PE A2108 3.603 20.924 30.378 1.00 78.53 C
HETATM 3585 C12 2PE A2108 4.646 19.972 29.787 1.00 77.58 C
HETATM 3586 O13 2PE A2108 4.793 20.192 28.410 1.00 68.04 O
HETATM 3587 C14 2PE A2108 4.797 19.022 27.635 1.00 60.04 C
HETATM 3588 C15 2PE A2108 3.384 18.443 27.557 1.00 58.20 C
HETATM 3589 O16 2PE A2108 3.100 18.030 26.249 1.00 66.14 O
HETATM 3590 C17 2PE A2108 2.690 19.060 25.394 1.00 61.07 C
HETATM 3591 C18 2PE A2108 1.943 18.480 24.194 1.00 55.85 C
HETATM 3592 O19 2PE A2108 0.942 19.380 23.812 1.00 74.33 O
HETATM 3593 C20 2PE A2108 0.165 18.956 22.731 1.00 74.26 C
HETATM 3594 C21 2PE A2108 -1.308 19.001 23.130 1.00 70.46 C
HETATM 3595 O22 2PE A2108 -1.935 20.073 22.489 1.00 79.27 O
HETATM 3596 C23 2PE A2108 -1.739 21.296 23.139 1.00 97.18 C
HETATM 3597 C24 2PE A2108 -2.241 22.440 22.262 1.00 87.94 C
HETATM 3598 O25 2PE A2108 -2.091 23.643 22.961 1.00 91.97 O
HETATM 3599 C26 2PE A2108 -3.066 23.862 23.942 1.00 78.84 C
HETATM 3600 C27 2PE A2108 -2.397 24.296 25.246 1.00 72.49 C
HETATM 3601 O28 2PE A2108 -1.433 25.283 24.996 1.00 73.50 O
HETATM 3602 O1 P6G A2109 -26.769 28.362 32.913 1.00 50.39 O
HETATM 3603 C2 P6G A2109 -26.883 29.785 33.027 1.00 71.27 C
HETATM 3604 C3 P6G A2109 -28.192 30.238 32.395 1.00 66.74 C
HETATM 3605 O4 P6G A2109 -28.028 31.543 31.843 1.00 76.66 O
HETATM 3606 C5 P6G A2109 -28.935 31.741 30.761 1.00 57.17 C
HETATM 3607 C6 P6G A2109 -28.750 33.116 30.129 1.00 59.79 C
HETATM 3608 O7 P6G A2109 -28.196 32.954 28.825 1.00 50.87 O
HETATM 3609 C8 P6G A2109 -29.224 32.682 27.878 1.00 40.90 C
HETATM 3610 C9 P6G A2109 -28.742 32.918 26.454 1.00 47.51 C
HETATM 3611 O10 P6G A2109 -27.614 32.096 26.170 1.00 49.75 O
HETATM 3612 C11 P6G A2109 -27.525 31.832 24.771 1.00 78.11 C
HETATM 3613 C12 P6G A2109 -26.071 31.630 24.362 1.00 68.61 C
HETATM 3614 O13 P6G A2109 -25.489 30.534 25.061 1.00 72.81 O
HETATM 3615 C14 P6G A2109 -24.119 30.402 24.694 1.00 60.42 C
HETATM 3616 C15 P6G A2109 -23.449 29.318 25.524 1.00 71.34 C
HETATM 3617 O16 P6G A2109 -23.829 28.027 25.060 1.00 64.17 O
HETATM 3618 C17 P6G A2109 -22.688 27.386 24.502 1.00 64.13 C
HETATM 3619 C18 P6G A2109 -22.277 26.193 25.350 1.00 70.54 C
HETATM 3620 O19 P6G A2109 -20.952 25.812 24.961 1.00 67.72 O
HETATM 3621 O HOH A2201 4.061 -5.326 29.966 1.00 60.55 O
HETATM 3622 O HOH A2202 2.511 9.348 14.737 1.00 62.59 O
HETATM 3623 O HOH A2203 -1.324 -12.709 15.222 1.00 54.49 O
HETATM 3624 O HOH A2204 -51.539 46.925 42.555 1.00 35.03 O
HETATM 3625 O HOH A2205 1.732 1.261 18.606 1.00 66.49 O
CONECT 370 3476
CONECT 568 1184
CONECT 676 3476
CONECT 1184 568
CONECT 3441 3475
CONECT 3442 3475
CONECT 3443 3444 3455
CONECT 3444 3443 3446
CONECT 3445 3462
CONECT 3446 3444 3448 3467
CONECT 3447 3467
CONECT 3448 3446 3449 3454
CONECT 3449 3448 3469
CONECT 3450 3451 3471
CONECT 3451 3450 3452
CONECT 3452 3451 3453
CONECT 3453 3452 3473
CONECT 3454 3448 3455
CONECT 3455 3443 3454 3456
CONECT 3456 3455 3457 3459
CONECT 3457 3456 3458
CONECT 3458 3457 3461 3472
CONECT 3459 3456 3460 3462
CONECT 3460 3459 3461
CONECT 3461 3458 3460
CONECT 3462 3445 3459 3474
CONECT 3463 3464 3465 3466 3475
CONECT 3464 3463
CONECT 3465 3463
CONECT 3466 3463
CONECT 3467 3446 3447 3468
CONECT 3468 3467 3469 3470
CONECT 3469 3449 3468
CONECT 3470 3468 3471
CONECT 3471 3450 3470 3473
CONECT 3472 3458
CONECT 3473 3453 3471
CONECT 3474 3462 3475
CONECT 3475 3441 3442 3463 3474
CONECT 3476 370 676 3625
CONECT 3477 3478 3494
CONECT 3478 3477 3479 3480
CONECT 3479 3478
CONECT 3480 3478 3481
CONECT 3481 3480 3482 3483
CONECT 3482 3481
CONECT 3483 3481 3484 3494
CONECT 3484 3483 3485
CONECT 3485 3484 3486 3492
CONECT 3486 3485 3487
CONECT 3487 3486 3488 3489
CONECT 3488 3487
CONECT 3489 3487 3490 3491
CONECT 3490 3489
CONECT 3491 3489 3492
CONECT 3492 3485 3491 3493
CONECT 3493 3492 3494 3495
CONECT 3494 3477 3483 3493
CONECT 3495 3493 3496
CONECT 3496 3495 3497 3498
CONECT 3497 3496
CONECT 3498 3496 3499 3500
CONECT 3499 3498
CONECT 3500 3498 3501 3502
CONECT 3501 3500
CONECT 3502 3500 3503
CONECT 3503 3502 3504
CONECT 3504 3503 3505 3506 3507
CONECT 3505 3504
CONECT 3506 3504
CONECT 3507 3504
CONECT 3508 3509 3510 3511
CONECT 3509 3508
CONECT 3510 3508
CONECT 3511 3508 3512
CONECT 3512 3511 3513
CONECT 3513 3512 3514
CONECT 3514 3513 3515
CONECT 3515 3514 3516
CONECT 3516 3515 3517
CONECT 3517 3516 3518
CONECT 3518 3517 3519
CONECT 3519 3518
CONECT 3520 3528 3530
CONECT 3521 3522
CONECT 3522 3521 3523
CONECT 3523 3522 3524
CONECT 3524 3523 3525
CONECT 3525 3524 3527
CONECT 3526 3528 3532
CONECT 3527 3525 3529 3532
CONECT 3528 3520 3526 3531
CONECT 3529 3527
CONECT 3530 3520
CONECT 3531 3528
CONECT 3532 3526 3527
CONECT 3533 3536
CONECT 3534 3535 3537
CONECT 3535 3534 3538
CONECT 3536 3533 3540
CONECT 3537 3534 3541
CONECT 3538 3535 3542
CONECT 3539 3553 3555
CONECT 3540 3536 3543
CONECT 3541 3537 3544
CONECT 3542 3538 3545
CONECT 3543 3540 3546
CONECT 3544 3541 3546
CONECT 3545 3542 3547
CONECT 3546 3543 3544
CONECT 3547 3545 3548
CONECT 3548 3547 3549
CONECT 3549 3548 3550
CONECT 3550 3549 3552
CONECT 3551 3553 3557
CONECT 3552 3550 3554 3557
CONECT 3553 3539 3551 3556
CONECT 3554 3552
CONECT 3555 3539
CONECT 3556 3553
CONECT 3557 3551 3552
CONECT 3558 3559
CONECT 3559 3558 3560
CONECT 3560 3559 3561
CONECT 3561 3560 3563
CONECT 3562 3563 3564
CONECT 3563 3561 3562
CONECT 3564 3562 3566
CONECT 3565 3566 3567
CONECT 3566 3564 3565
CONECT 3567 3565 3569
CONECT 3568 3569 3570
CONECT 3569 3567 3568
CONECT 3570 3568 3572
CONECT 3571 3572 3573
CONECT 3572 3570 3571
CONECT 3573 3571
CONECT 3574 3575
CONECT 3575 3574 3576
CONECT 3576 3575 3577
CONECT 3577 3576 3578
CONECT 3578 3577 3579
CONECT 3579 3578 3580
CONECT 3580 3579 3581
CONECT 3581 3580 3582
CONECT 3582 3581 3583
CONECT 3583 3582 3584
CONECT 3584 3583 3585
CONECT 3585 3584 3586
CONECT 3586 3585 3587
CONECT 3587 3586 3588
CONECT 3588 3587 3589
CONECT 3589 3588 3590
CONECT 3590 3589 3591
CONECT 3591 3590 3592
CONECT 3592 3591 3593
CONECT 3593 3592 3594
CONECT 3594 3593 3595
CONECT 3595 3594 3596
CONECT 3596 3595 3597
CONECT 3597 3596 3598
CONECT 3598 3597 3599
CONECT 3599 3598 3600
CONECT 3600 3599 3601
CONECT 3601 3600
CONECT 3602 3603
CONECT 3603 3602 3604
CONECT 3604 3603 3605
CONECT 3605 3604 3606
CONECT 3606 3605 3607
CONECT 3607 3606 3608
CONECT 3608 3607 3609
CONECT 3609 3608 3610
CONECT 3610 3609 3611
CONECT 3611 3610 3612
CONECT 3612 3611 3613
CONECT 3613 3612 3614
CONECT 3614 3613 3615
CONECT 3615 3614 3616
CONECT 3616 3615 3617
CONECT 3617 3616 3618
CONECT 3618 3617 3619
CONECT 3619 3618 3620
CONECT 3620 3619
CONECT 3625 3476
MASTER 402 0 9 22 12 0 0 6 3616 1 185 38
END