HEADER MEMBRANE PROTEIN 09-MAY-17 5NX2
TITLE CRYSTAL STRUCTURE OF THERMOSTABILISED FULL-LENGTH GLP-1R IN COMPLEX
TITLE 2 WITH A TRUNCATED PEPTIDE AGONIST AT 3.7 A RESOLUTION
CAVEAT 5NX2 NAG A 603 HAS WRONG CHIRALITY AT ATOM C3 SOG A 606 HAS WRONG
CAVEAT 2 5NX2 CHIRALITY AT ATOM C3 SOG A 606 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 5NX2 C5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCAGON-LIKE PEPTIDE 1 RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 24-432;
COMPND 5 SYNONYM: GLP-1R;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: TRUNCATED PEPTIDE AGONIST;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GLP1R;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630
KEYWDS 7TM, GPCR, SIGNALLING PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.RAPPAS,A.JAZAYERI,A.J.H.BROWN,J.KEAN,J.C.ERREY,N.ROBERTSON,C.FIEZ-
AUTHOR 2 VANDAL,S.P.ANDREWS,M.CONGREVE,A.BORTOLATO,J.S.MASON,A.H.BAIG,
AUTHOR 3 I.TEOBALD,A.S.DORE,M.WEIR,R.M.COOKE,F.H.MARSHALL
REVDAT 2 29-JUL-20 5NX2 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 14-JUN-17 5NX2 0
JRNL AUTH A.JAZAYERI,M.RAPPAS,A.J.H.BROWN,J.KEAN,J.C.ERREY,
JRNL AUTH 2 N.J.ROBERTSON,C.FIEZ-VANDAL,S.P.ANDREWS,M.CONGREVE,
JRNL AUTH 3 A.BORTOLATO,J.S.MASON,A.H.BAIG,I.TEOBALD,A.S.DORE,M.WEIR,
JRNL AUTH 4 R.M.COOKE,F.H.MARSHALL
JRNL TITL CRYSTAL STRUCTURE OF THE GLP-1 RECEPTOR BOUND TO A PEPTIDE
JRNL TITL 2 AGONIST.
JRNL REF NATURE V. 546 254 2017
JRNL REFN ISSN 0028-0836
JRNL PMID 28562585
JRNL DOI 10.1038/NATURE22800
REMARK 2
REMARK 2 RESOLUTION. 3.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1-2575-000)
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) : 3.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.020
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 9202
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.287
REMARK 3 R VALUE (WORKING SET) : 0.285
REMARK 3 FREE R VALUE : 0.334
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.740
REMARK 3 FREE R VALUE TEST SET COUNT : 763
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 24.6777 - 6.2991 0.92 3043 141 0.2461 0.2890
REMARK 3 2 6.2991 - 5.0135 0.92 3060 180 0.3279 0.3863
REMARK 3 3 5.0135 - 4.3838 0.92 3053 148 0.2770 0.3298
REMARK 3 4 4.3838 - 3.9848 0.93 3116 132 0.3184 0.3818
REMARK 3 5 3.9848 - 3.7002 0.92 3056 162 0.3895 0.4258
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) : 0.810
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 46.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 135.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 3518
REMARK 3 ANGLE : 1.021 4794
REMARK 3 CHIRALITY : 0.052 532
REMARK 3 PLANARITY : 0.005 574
REMARK 3 DIHEDRAL : 16.078 1972
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1542 40.4612 -18.1541
REMARK 3 T TENSOR
REMARK 3 T11: 1.7228 T22: 1.7340
REMARK 3 T33: 1.7214 T12: 0.2591
REMARK 3 T13: 0.2471 T23: 0.1864
REMARK 3 L TENSOR
REMARK 3 L11: 0.2708 L22: 0.9255
REMARK 3 L33: 1.5128 L12: 0.8695
REMARK 3 L13: -0.4122 L23: -0.4356
REMARK 3 S TENSOR
REMARK 3 S11: -0.0147 S12: 1.0621 S13: -0.0494
REMARK 3 S21: 0.2572 S22: 0.0544 S23: 0.8013
REMARK 3 S31: 0.4979 S32: -1.5301 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 139 THROUGH 334 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1628 15.0348 10.2689
REMARK 3 T TENSOR
REMARK 3 T11: 1.1270 T22: 1.0119
REMARK 3 T33: 1.3676 T12: 0.1090
REMARK 3 T13: -0.1726 T23: 0.0772
REMARK 3 L TENSOR
REMARK 3 L11: 1.0371 L22: 1.4869
REMARK 3 L33: 5.7107 L12: 0.4209
REMARK 3 L13: -1.1589 L23: -1.8090
REMARK 3 S TENSOR
REMARK 3 S11: 0.6018 S12: 0.2175 S13: -0.0865
REMARK 3 S21: -0.1350 S22: 0.0088 S23: 0.1016
REMARK 3 S31: 0.3132 S32: -0.4639 S33: -0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 335 THROUGH 417 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3615 20.2115 26.1889
REMARK 3 T TENSOR
REMARK 3 T11: 0.6350 T22: 1.6365
REMARK 3 T33: 1.0128 T12: -0.1807
REMARK 3 T13: -0.2139 T23: 0.2583
REMARK 3 L TENSOR
REMARK 3 L11: 6.0720 L22: 4.4384
REMARK 3 L33: 5.5464 L12: 2.3176
REMARK 3 L13: -2.8845 L23: 3.2096
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 1.0881 S13: 0.3348
REMARK 3 S21: -1.7872 S22: 0.0395 S23: -0.1230
REMARK 3 S31: 2.0604 S32: -1.8198 S33: 0.0618
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 5NX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1200004858.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0 - 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96861
REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : OXFORD DANFYSIK/SESO TWO STAGE
REMARK 200 DEMAGNIFICATION USING TWO K-B
REMARK 200 PAIRS OF BIMORPH TYPE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9266
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.700
REMARK 200 RESOLUTION RANGE LOW (A) : 54.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 2.02400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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: 3IOL, 5EE7
REMARK 200
REMARK 200 REMARK: ROD-LIKE CRYSTALS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.0-9.0, 32-44% (V/V)
REMARK 280 PEG 200, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.63500
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 109.27000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 109.27000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 54.63500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 20
REMARK 465 PRO A 21
REMARK 465 ALA A 22
REMARK 465 SER A 23
REMARK 465 ARG A 24
REMARK 465 PRO A 25
REMARK 465 GLN A 26
REMARK 465 GLY A 27
REMARK 465 ALA A 28
REMARK 465 GLU A 418
REMARK 465 ARG A 419
REMARK 465 TRP A 420
REMARK 465 ARG A 421
REMARK 465 LEU A 422
REMARK 465 GLU A 423
REMARK 465 HIS A 424
REMARK 465 LEU A 425
REMARK 465 HIS A 426
REMARK 465 ILE A 427
REMARK 465 GLN A 428
REMARK 465 ARG A 429
REMARK 465 ASP A 430
REMARK 465 SER A 431
REMARK 465 SER A 432
REMARK 465 ALA A 433
REMARK 465 ALA A 434
REMARK 465 ALA A 435
REMARK 465 LEU A 436
REMARK 465 GLU A 437
REMARK 465 VAL A 438
REMARK 465 LEU A 439
REMARK 465 PHE A 440
REMARK 465 GLN A 441
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASN A 63 NE1 TRP A 110 2.09
REMARK 500 CD LYS A 197 CE MET A 233 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 46 CA - CB - SG ANGL. DEV. = 10.7 DEGREES
REMARK 500 CYS A 126 CA - CB - SG ANGL. DEV. = -10.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 68 0.15 81.41
REMARK 500 ASN A 115 -70.78 -84.26
REMARK 500 SER A 117 -3.49 72.90
REMARK 500 ARG A 215 -32.18 -130.78
REMARK 500 ALA A 298 -77.27 -108.54
REMARK 500 SER A 301 -163.07 -104.18
REMARK 500 ASN A 302 81.69 49.23
REMARK 500 HIS A 374 -165.76 -165.58
REMARK 500 PHE A 390 -71.79 -64.95
REMARK 500 CYS A 403 -70.52 -133.48
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5NX2 A 24 432 UNP P43220 GLP1R_HUMAN 24 432
DBREF 5NX2 B 1 10 PDB 5NX2 5NX2 1 10
SEQADV 5NX2 GLY A 20 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 PRO A 21 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 ALA A 22 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 SER A 23 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 GLU A 207 UNP P43220 THR 207 ENGINEERED MUTATION
SEQADV 5NX2 ALA A 211 UNP P43220 GLN 211 ENGINEERED MUTATION
SEQADV 5NX2 ARG A 215 UNP P43220 ASP 215 ENGINEERED MUTATION
SEQADV 5NX2 PHE A 232 UNP P43220 LEU 232 ENGINEERED MUTATION
SEQADV 5NX2 PHE A 260 UNP P43220 LEU 260 VARIANT
SEQADV 5NX2 ALA A 295 UNP P43220 GLY 295 ENGINEERED MUTATION
SEQADV 5NX2 ALA A 298 UNP P43220 THR 298 ENGINEERED MUTATION
SEQADV 5NX2 ALA A 329 UNP P43220 CYS 329 ENGINEERED MUTATION
SEQADV 5NX2 ALA A 358 UNP P43220 PRO 358 ENGINEERED MUTATION
SEQADV 5NX2 ALA A 361 UNP P43220 GLY 361 ENGINEERED MUTATION
SEQADV 5NX2 VAL A 363 UNP P43220 HIS 363 ENGINEERED MUTATION
SEQADV 5NX2 ALA A 405 UNP P43220 VAL 405 ENGINEERED MUTATION
SEQADV 5NX2 ALA A 433 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 ALA A 434 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 ALA A 435 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 LEU A 436 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 GLU A 437 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 VAL A 438 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 LEU A 439 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 PHE A 440 UNP P43220 EXPRESSION TAG
SEQADV 5NX2 GLN A 441 UNP P43220 EXPRESSION TAG
SEQRES 1 A 422 GLY PRO ALA SER ARG PRO GLN GLY ALA THR VAL SER LEU
SEQRES 2 A 422 TRP GLU THR VAL GLN LYS TRP ARG GLU TYR ARG ARG GLN
SEQRES 3 A 422 CYS GLN ARG SER LEU THR GLU ASP PRO PRO PRO ALA THR
SEQRES 4 A 422 ASP LEU PHE CYS ASN ARG THR PHE ASP GLU TYR ALA CYS
SEQRES 5 A 422 TRP PRO ASP GLY GLU PRO GLY SER PHE VAL ASN VAL SER
SEQRES 6 A 422 CYS PRO TRP TYR LEU PRO TRP ALA SER SER VAL PRO GLN
SEQRES 7 A 422 GLY HIS VAL TYR ARG PHE CYS THR ALA GLU GLY LEU TRP
SEQRES 8 A 422 LEU GLN LYS ASP ASN SER SER LEU PRO TRP ARG ASP LEU
SEQRES 9 A 422 SER GLU CYS GLU GLU SER LYS ARG GLY GLU ARG SER SER
SEQRES 10 A 422 PRO GLU GLU GLN LEU LEU PHE LEU TYR ILE ILE TYR THR
SEQRES 11 A 422 VAL GLY TYR ALA LEU SER PHE SER ALA LEU VAL ILE ALA
SEQRES 12 A 422 SER ALA ILE LEU LEU GLY PHE ARG HIS LEU HIS CYS THR
SEQRES 13 A 422 ARG ASN TYR ILE HIS LEU ASN LEU PHE ALA SER PHE ILE
SEQRES 14 A 422 LEU ARG ALA LEU SER VAL PHE ILE LYS ASP ALA ALA LEU
SEQRES 15 A 422 LYS TRP MET TYR SER GLU ALA ALA GLN ALA HIS GLN TRP
SEQRES 16 A 422 ARG GLY LEU LEU SER TYR GLN ASP SER LEU SER CYS ARG
SEQRES 17 A 422 LEU VAL PHE LEU PHE MET GLN TYR CYS VAL ALA ALA ASN
SEQRES 18 A 422 TYR TYR TRP LEU LEU VAL GLU GLY VAL TYR LEU TYR THR
SEQRES 19 A 422 LEU LEU ALA PHE SER VAL PHE SER GLU GLN TRP ILE PHE
SEQRES 20 A 422 ARG LEU TYR VAL SER ILE GLY TRP GLY VAL PRO LEU LEU
SEQRES 21 A 422 PHE VAL VAL PRO TRP GLY ILE VAL LYS TYR LEU TYR GLU
SEQRES 22 A 422 ASP GLU ALA CYS TRP ALA ARG ASN SER ASN MET ASN TYR
SEQRES 23 A 422 TRP LEU ILE ILE ARG LEU PRO ILE LEU PHE ALA ILE GLY
SEQRES 24 A 422 VAL ASN PHE LEU ILE PHE VAL ARG VAL ILE ALA ILE VAL
SEQRES 25 A 422 VAL SER LYS LEU LYS ALA ASN LEU MET CYS LYS THR ASP
SEQRES 26 A 422 ILE LYS CYS ARG LEU ALA LYS SER THR LEU THR LEU ILE
SEQRES 27 A 422 ALA LEU LEU ALA THR VAL GLU VAL ILE PHE ALA PHE VAL
SEQRES 28 A 422 MET ASP GLU HIS ALA ARG GLY THR LEU ARG PHE ILE LYS
SEQRES 29 A 422 LEU PHE THR GLU LEU SER PHE THR SER PHE GLN GLY LEU
SEQRES 30 A 422 MET VAL ALA ILE LEU TYR CYS PHE ALA ASN ASN GLU VAL
SEQRES 31 A 422 GLN LEU GLU PHE ARG LYS SER TRP GLU ARG TRP ARG LEU
SEQRES 32 A 422 GLU HIS LEU HIS ILE GLN ARG ASP SER SER ALA ALA ALA
SEQRES 33 A 422 LEU GLU VAL LEU PHE GLN
SEQRES 1 B 10 9DK 9DQ GLY THR 9DT THR SER ASP 9DW 9DZ
HET 9DK B 1 15
HET 9DQ B 2 10
HET 9DT B 5 13
HET 9DW B 9 21
HET 9DZ B 10 16
HET NAG C 1 14
HET NAG C 2 14
HET NAG A 603 14
HET SOG A 604 20
HET SOG A 605 20
HET SOG A 606 20
HETNAM 9DK 3-[2-(1~{H}-IMIDAZOL-4-YL)ETHYLAMINO]-2,2-DIMETHYL-3-
HETNAM 2 9DK OXIDANYLIDENE-PROPANOIC ACID
HETNAM 9DQ (2~{S})-2-AZANYL-3-(1~{H}-1,2,3,4-TETRAZOL-5-YL)
HETNAM 2 9DQ PROPANOIC ACID
HETNAM 9DT (2~{S})-2-AZANYL-3-(2-FLUOROPHENYL)-2-METHYL-PROPANOIC
HETNAM 2 9DT ACID
HETNAM 9DW (2~{S})-2-AZANYL-3-[4-(2-ETHYL-4-METHOXY-PHENYL)
HETNAM 2 9DW PHENYL]PROPANOIC ACID
HETNAM 9DZ (2~{S})-2-AZANYL-5-(3,5-DIMETHYLPHENYL)PENTANAMIDE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SOG OCTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE
HETSYN SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE
FORMUL 2 9DK C10 H15 N3 O3
FORMUL 2 9DQ C4 H7 N5 O2
FORMUL 2 9DT C10 H12 F N O2
FORMUL 2 9DW C18 H21 N O3
FORMUL 2 9DZ C13 H20 N2 O
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 5 SOG 3(C14 H28 O5 S)
HELIX 1 AA1 SER A 31 ASP A 53 1 23
HELIX 2 AA2 TRP A 91 VAL A 95 5 5
HELIX 3 AA3 LEU A 123 CYS A 126 5 4
HELIX 4 AA4 GLU A 127 GLY A 132 1 6
HELIX 5 AA5 GLU A 138 PHE A 169 1 32
HELIX 6 AA6 ARG A 170 HIS A 173 5 4
HELIX 7 AA7 CYS A 174 TYR A 205 1 32
HELIX 8 AA8 ARG A 215 SER A 223 1 9
HELIX 9 AA9 SER A 223 PHE A 257 1 35
HELIX 10 AB1 GLU A 262 TYR A 291 1 30
HELIX 11 AB2 GLU A 292 CYS A 296 5 5
HELIX 12 AB3 ASN A 302 LEU A 335 1 34
HELIX 13 AB4 MET A 340 ALA A 358 1 19
HELIX 14 AB5 LEU A 360 ASP A 372 1 13
HELIX 15 AB6 GLY A 377 CYS A 403 1 27
HELIX 16 AB7 ASN A 406 TRP A 417 1 12
HELIX 17 AB8 GLY B 3 THR B 4 5 2
HELIX 18 AB9 THR B 6 ASP B 8 5 3
SHEET 1 AA1 2 THR A 65 PHE A 66 0
SHEET 2 AA1 2 CYS A 71 TRP A 72 -1 O TRP A 72 N THR A 65
SHEET 1 AA2 2 SER A 79 SER A 84 0
SHEET 2 AA2 2 HIS A 99 CYS A 104 -1 O ARG A 102 N VAL A 81
SSBOND 1 CYS A 46 CYS A 71 1555 1555 2.03
SSBOND 2 CYS A 62 CYS A 104 1555 1555 2.04
SSBOND 3 CYS A 85 CYS A 126 1555 1555 2.03
SSBOND 4 CYS A 226 CYS A 296 1555 1555 2.03
LINK ND2 ASN A 63 C1 NAG A 603 1555 1555 1.42
LINK ND2 ASN A 82 C1 NAG C 1 1555 1555 1.44
LINK C67 9DK B 1 N66 9DQ B 2 1555 1555 1.35
LINK C57 9DQ B 2 N GLY B 3 1555 1555 1.34
LINK C THR B 4 N48 9DT B 5 1555 1555 1.35
LINK C36 9DT B 5 N THR B 6 1555 1555 1.35
LINK C ASP B 8 N17 9DW B 9 1555 1555 1.34
LINK C88 9DW B 9 N90 9DZ B 10 1555 1555 1.34
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.43
CRYST1 94.435 94.435 163.905 90.00 90.00 120.00 P 31 2 1 6
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 0.010589 0.006114 0.000000 0.00000
SCALE2 0.000000 0.012227 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006101 0.00000
ATOM 1 N THR A 29 -6.703 41.282 4.277 1.00156.42 N
ANISOU 1 N THR A 29 22875 15071 21487 1375 6376 1977 N
ATOM 2 CA THR A 29 -6.161 40.059 3.697 1.00166.98 C
ANISOU 2 CA THR A 29 24315 16409 22722 1134 6138 1781 C
ATOM 3 C THR A 29 -7.043 39.573 2.546 1.00177.64 C
ANISOU 3 C THR A 29 25162 18317 24016 1054 6017 1684 C
ATOM 4 O THR A 29 -8.197 39.192 2.739 1.00184.94 O
ANISOU 4 O THR A 29 25837 19471 24960 858 6140 1591 O
ATOM 5 CB THR A 29 -6.012 38.960 4.759 1.00176.90 C
ANISOU 5 CB THR A 29 25982 17265 23967 747 6210 1587 C
ATOM 6 OG1 THR A 29 -7.220 38.860 5.522 1.00185.26 O
ANISOU 6 OG1 THR A 29 26909 18395 25087 568 6451 1528 O
ATOM 7 CG2 THR A 29 -4.850 39.279 5.690 1.00173.33 C
ANISOU 7 CG2 THR A 29 26065 16254 23538 807 6246 1677 C
ATOM 8 N VAL A 30 -6.470 39.603 1.348 1.00177.89 N
ANISOU 8 N VAL A 30 25052 18564 23972 1200 5775 1711 N
ATOM 9 CA VAL A 30 -7.132 39.156 0.125 1.00186.32 C
ANISOU 9 CA VAL A 30 25669 20157 24966 1129 5621 1630 C
ATOM 10 C VAL A 30 -7.142 37.633 0.040 1.00166.44 C
ANISOU 10 C VAL A 30 23283 17603 22353 713 5522 1357 C
ATOM 11 O VAL A 30 -6.085 36.996 -0.013 1.00163.35 O
ANISOU 11 O VAL A 30 23246 16917 21904 624 5383 1264 O
ATOM 12 CB VAL A 30 -6.470 39.766 -1.116 1.00207.21 C
ANISOU 12 CB VAL A 30 28145 23027 27559 1430 5401 1758 C
ATOM 13 CG1 VAL A 30 -7.037 39.123 -2.369 1.00213.40 C
ANISOU 13 CG1 VAL A 30 28528 24311 28244 1294 5222 1646 C
ATOM 14 CG2 VAL A 30 -6.664 41.272 -1.141 1.00212.08 C
ANISOU 14 CG2 VAL A 30 28562 23758 28261 1834 5502 2026 C
ATOM 15 N SER A 31 -8.336 37.049 0.034 1.00167.50 N
ANISOU 15 N SER A 31 23136 18035 22472 458 5599 1234 N
ATOM 16 CA SER A 31 -8.506 35.605 0.029 1.00145.86 C
ANISOU 16 CA SER A 31 20511 15273 19635 37 5537 970 C
ATOM 17 C SER A 31 -8.350 35.061 -1.393 1.00204.58 C
ANISOU 17 C SER A 31 27723 23065 26943 -14 5285 887 C
ATOM 18 O SER A 31 -8.459 35.790 -2.382 1.00186.96 O
ANISOU 18 O SER A 31 25137 21198 24699 241 5179 1028 O
ATOM 19 CB SER A 31 -9.872 35.218 0.598 1.00159.47 C
ANISOU 19 CB SER A 31 22021 17188 21383 -229 5727 874 C
ATOM 20 OG SER A 31 -10.916 35.556 -0.299 1.00172.57 O
ANISOU 20 OG SER A 31 23110 19432 23025 -162 5699 937 O
ATOM 21 N LEU A 32 -8.070 33.756 -1.478 1.00177.59 N
ANISOU 21 N LEU A 32 24532 19519 23423 -352 5191 654 N
ATOM 22 CA LEU A 32 -7.949 33.082 -2.771 1.00177.12 C
ANISOU 22 CA LEU A 32 24302 19768 23227 -462 4969 542 C
ATOM 23 C LEU A 32 -9.196 33.277 -3.630 1.00150.38 C
ANISOU 23 C LEU A 32 20336 17005 19796 -491 4949 571 C
ATOM 24 O LEU A 32 -9.097 33.601 -4.820 1.00209.92 O
ANISOU 24 O LEU A 32 27595 24891 27275 -338 4779 643 O
ATOM 25 CB LEU A 32 -7.669 31.594 -2.545 1.00165.80 C
ANISOU 25 CB LEU A 32 23209 18090 21697 -865 4927 273 C
ATOM 26 CG LEU A 32 -6.209 31.133 -2.551 1.00159.05 C
ANISOU 26 CG LEU A 32 22822 16793 20815 -835 4799 217 C
ATOM 27 CD1 LEU A 32 -5.436 31.776 -1.426 1.00159.72 C
ANISOU 27 CD1 LEU A 32 23276 16383 21025 -639 4907 351 C
ATOM 28 CD2 LEU A 32 -6.146 29.625 -2.397 1.00144.96 C
ANISOU 28 CD2 LEU A 32 21314 14832 18931 -1251 4771 -53 C
ATOM 29 N TRP A 33 -10.380 33.086 -3.045 1.00152.88 N
ANISOU 29 N TRP A 33 20465 17483 20142 -693 5119 522 N
ATOM 30 CA TRP A 33 -11.606 33.104 -3.839 1.00156.24 C
ANISOU 30 CA TRP A 33 20339 18511 20512 -778 5094 533 C
ATOM 31 C TRP A 33 -11.838 34.500 -4.403 1.00191.02 C
ANISOU 31 C TRP A 33 24347 23233 24999 -356 5080 806 C
ATOM 32 O TRP A 33 -12.204 34.663 -5.574 1.00185.92 O
ANISOU 32 O TRP A 33 23301 23060 24280 -301 4929 860 O
ATOM 33 CB TRP A 33 -12.811 32.717 -2.989 1.00220.85 C
ANISOU 33 CB TRP A 33 28405 26780 28726 -1053 5301 445 C
ATOM 34 CG TRP A 33 -14.106 32.860 -3.723 1.00227.93 C
ANISOU 34 CG TRP A 33 28710 28307 29585 -1113 5291 491 C
ATOM 35 CD1 TRP A 33 -15.188 33.591 -3.349 1.00212.00 C
ANISOU 35 CD1 TRP A 33 26324 26552 27674 -1005 5467 630 C
ATOM 36 CD2 TRP A 33 -14.520 32.093 -4.862 1.00164.45 C
ANISOU 36 CD2 TRP A 33 20401 20703 21379 -1361 5110 373 C
ATOM 37 NE1 TRP A 33 -16.216 33.416 -4.244 1.00201.22 N
ANISOU 37 NE1 TRP A 33 24446 25780 26227 -1133 5389 631 N
ATOM 38 CE2 TRP A 33 -15.835 32.487 -5.176 1.00193.90 C
ANISOU 38 CE2 TRP A 33 23578 24970 25126 -1367 5169 471 C
ATOM 39 CE3 TRP A 33 -13.892 31.139 -5.670 1.00163.86 C
ANISOU 39 CE3 TRP A 33 20500 20616 21142 -1571 4907 201 C
ATOM 40 CZ2 TRP A 33 -16.532 31.964 -6.263 1.00170.54 C
ANISOU 40 CZ2 TRP A 33 20235 22543 22020 -1589 5019 409 C
ATOM 41 CZ3 TRP A 33 -14.584 30.622 -6.748 1.00166.56 C
ANISOU 41 CZ3 TRP A 33 20477 21472 21335 -1793 4771 130 C
ATOM 42 CH2 TRP A 33 -15.891 31.034 -7.035 1.00169.85 C
ANISOU 42 CH2 TRP A 33 20344 22426 21764 -1807 4822 237 C
ATOM 43 N GLU A 34 -11.613 35.517 -3.566 1.00173.37 N
ANISOU 43 N GLU A 34 22235 20729 22911 -62 5239 982 N
ATOM 44 CA GLU A 34 -11.699 36.911 -3.983 1.00175.65 C
ANISOU 44 CA GLU A 34 22220 21234 23286 370 5245 1252 C
ATOM 45 C GLU A 34 -10.663 37.237 -5.048 1.00184.85 C
ANISOU 45 C GLU A 34 23419 22432 24383 599 5006 1326 C
ATOM 46 O GLU A 34 -10.940 38.027 -5.962 1.00198.94 O
ANISOU 46 O GLU A 34 24813 24609 26166 847 4914 1493 O
ATOM 47 CB GLU A 34 -11.505 37.805 -2.757 1.00179.07 C
ANISOU 47 CB GLU A 34 22893 21274 23873 597 5475 1395 C
ATOM 48 CG GLU A 34 -12.381 39.037 -2.683 1.00200.74 C
ANISOU 48 CG GLU A 34 25239 24295 26738 899 5631 1628 C
ATOM 49 CD GLU A 34 -12.025 39.909 -1.492 1.00209.41 C
ANISOU 49 CD GLU A 34 26644 24950 27971 1121 5856 1763 C
ATOM 50 OE1 GLU A 34 -11.359 39.401 -0.564 1.00212.26 O
ANISOU 50 OE1 GLU A 34 27496 24818 28334 957 5921 1649 O
ATOM 51 OE2 GLU A 34 -12.411 41.096 -1.480 1.00217.35 O
ANISOU 51 OE2 GLU A 34 27411 26095 29079 1454 5971 1986 O
ATOM 52 N THR A 35 -9.489 36.603 -4.982 1.00174.17 N
ANISOU 52 N THR A 35 22516 20691 22971 510 4898 1203 N
ATOM 53 CA THR A 35 -8.494 36.815 -6.025 1.00185.28 C
ANISOU 53 CA THR A 35 23958 22135 24305 699 4670 1253 C
ATOM 54 C THR A 35 -8.992 36.239 -7.341 1.00150.77 C
ANISOU 54 C THR A 35 19223 18268 19796 528 4483 1161 C
ATOM 55 O THR A 35 -8.763 36.817 -8.410 1.00165.31 O
ANISOU 55 O THR A 35 20827 20391 21594 747 4322 1280 O
ATOM 56 CB THR A 35 -7.159 36.178 -5.631 1.00145.53 C
ANISOU 56 CB THR A 35 19481 16574 19242 619 4606 1133 C
ATOM 57 OG1 THR A 35 -6.713 36.720 -4.384 1.00143.59 O
ANISOU 57 OG1 THR A 35 19577 15866 19116 757 4778 1227 O
ATOM 58 CG2 THR A 35 -6.101 36.444 -6.694 1.00143.64 C
ANISOU 58 CG2 THR A 35 19277 16368 18933 830 4381 1190 C
ATOM 59 N VAL A 36 -9.654 35.084 -7.285 1.00152.81 N
ANISOU 59 N VAL A 36 19449 18638 19971 123 4499 948 N
ATOM 60 CA VAL A 36 -10.176 34.476 -8.503 1.00155.11 C
ANISOU 60 CA VAL A 36 19409 19411 20115 -84 4329 852 C
ATOM 61 C VAL A 36 -11.284 35.342 -9.100 1.00157.80 C
ANISOU 61 C VAL A 36 19159 20313 20484 78 4333 1040 C
ATOM 62 O VAL A 36 -11.319 35.580 -10.313 1.00225.53 O
ANISOU 62 O VAL A 36 27436 29276 28978 162 4150 1107 O
ATOM 63 CB VAL A 36 -10.664 33.044 -8.219 1.00156.78 C
ANISOU 63 CB VAL A 36 19745 19598 20225 -573 4364 581 C
ATOM 64 CG1 VAL A 36 -11.531 32.537 -9.361 1.00159.90 C
ANISOU 64 CG1 VAL A 36 19717 20566 20472 -808 4233 509 C
ATOM 65 CG2 VAL A 36 -9.479 32.117 -7.988 1.00177.67 C
ANISOU 65 CG2 VAL A 36 22935 21757 22814 -725 4301 395 C
ATOM 66 N GLN A 37 -12.212 35.816 -8.259 1.00159.33 N
ANISOU 66 N GLN A 37 19177 20563 20798 120 4543 1131 N
ATOM 67 CA GLN A 37 -13.251 36.743 -8.713 1.00161.89 C
ANISOU 67 CA GLN A 37 18943 21389 21178 321 4571 1340 C
ATOM 68 C GLN A 37 -12.682 37.979 -9.404 1.00160.47 C
ANISOU 68 C GLN A 37 18631 21298 21044 772 4464 1582 C
ATOM 69 O GLN A 37 -13.077 38.318 -10.533 1.00162.14 O
ANISOU 69 O GLN A 37 18426 21987 21193 857 4311 1685 O
ATOM 70 CB GLN A 37 -14.116 37.169 -7.524 1.00163.17 C
ANISOU 70 CB GLN A 37 19030 21475 21491 356 4848 1412 C
ATOM 71 CG GLN A 37 -15.054 36.099 -7.004 1.00195.53 C
ANISOU 71 CG GLN A 37 23085 25662 25543 -82 4957 1210 C
ATOM 72 CD GLN A 37 -16.479 36.306 -7.478 1.00199.51 C
ANISOU 72 CD GLN A 37 22981 26775 26047 -136 4984 1298 C
ATOM 73 OE1 GLN A 37 -16.809 37.341 -8.059 1.00202.67 O
ANISOU 73 OE1 GLN A 37 22994 27502 26510 185 4950 1530 O
ATOM 74 NE2 GLN A 37 -17.334 35.320 -7.233 1.00199.08 N
ANISOU 74 NE2 GLN A 37 22838 26881 25921 -547 5043 1118 N
ATOM 75 N LYS A 38 -11.715 38.645 -8.762 1.00157.39 N
ANISOU 75 N LYS A 38 18605 20449 20747 1050 4532 1676 N
ATOM 76 CA LYS A 38 -11.115 39.811 -9.403 1.00176.34 C
ANISOU 76 CA LYS A 38 20913 22910 23176 1469 4430 1900 C
ATOM 77 C LYS A 38 -10.435 39.413 -10.704 1.00198.33 C
ANISOU 77 C LYS A 38 23679 25869 25809 1422 4152 1833 C
ATOM 78 O LYS A 38 -10.513 40.146 -11.692 1.00214.15 O
ANISOU 78 O LYS A 38 25359 28222 27786 1650 4017 1994 O
ATOM 79 CB LYS A 38 -10.177 40.567 -8.458 1.00152.77 C
ANISOU 79 CB LYS A 38 18348 19395 20304 1748 4555 2009 C
ATOM 80 CG LYS A 38 -9.135 39.777 -7.730 1.00167.37 C
ANISOU 80 CG LYS A 38 20768 20694 22129 1570 4566 1832 C
ATOM 81 CD LYS A 38 -8.325 40.700 -6.833 1.00172.06 C
ANISOU 81 CD LYS A 38 21712 20829 22835 1870 4692 1984 C
ATOM 82 CE LYS A 38 -9.217 41.534 -5.926 1.00182.82 C
ANISOU 82 CE LYS A 38 22926 22196 24340 2016 4954 2134 C
ATOM 83 NZ LYS A 38 -8.658 41.651 -4.550 1.00177.69 N
ANISOU 83 NZ LYS A 38 22759 20979 23776 2023 5144 2131 N
ATOM 84 N TRP A 39 -9.716 38.288 -10.710 1.00153.86 N
ANISOU 84 N TRP A 39 18409 19975 20077 1142 4068 1603 N
ATOM 85 CA TRP A 39 -9.042 37.859 -11.932 1.00153.24 C
ANISOU 85 CA TRP A 39 18336 20038 19851 1083 3819 1524 C
ATOM 86 C TRP A 39 -10.028 37.662 -13.081 1.00203.75 C
ANISOU 86 C TRP A 39 24220 27057 26138 935 3688 1525 C
ATOM 87 O TRP A 39 -9.777 38.110 -14.200 1.00216.79 O
ANISOU 87 O TRP A 39 25664 28986 27720 1091 3505 1622 O
ATOM 88 CB TRP A 39 -8.279 36.561 -11.677 1.00151.80 C
ANISOU 88 CB TRP A 39 18609 19485 19584 765 3783 1260 C
ATOM 89 CG TRP A 39 -7.667 36.002 -12.920 1.00151.51 C
ANISOU 89 CG TRP A 39 18580 19597 19390 665 3550 1154 C
ATOM 90 CD1 TRP A 39 -6.506 36.388 -13.517 1.00149.05 C
ANISOU 90 CD1 TRP A 39 18439 19143 19051 894 3406 1212 C
ATOM 91 CD2 TRP A 39 -8.223 34.975 -13.750 1.00153.94 C
ANISOU 91 CD2 TRP A 39 18706 20243 19539 300 3440 974 C
ATOM 92 NE1 TRP A 39 -6.291 35.649 -14.656 1.00149.77 N
ANISOU 92 NE1 TRP A 39 18475 19450 18982 696 3220 1073 N
ATOM 93 CE2 TRP A 39 -7.333 34.776 -14.821 1.00152.77 C
ANISOU 93 CE2 TRP A 39 18645 20125 19276 327 3238 926 C
ATOM 94 CE3 TRP A 39 -9.383 34.198 -13.683 1.00157.04 C
ANISOU 94 CE3 TRP A 39 18880 20917 19870 -59 3498 848 C
ATOM 95 CZ2 TRP A 39 -7.566 33.832 -15.819 1.00177.51 C
ANISOU 95 CZ2 TRP A 39 21667 23548 22233 6 3099 755 C
ATOM 96 CZ3 TRP A 39 -9.614 33.262 -14.673 1.00158.86 C
ANISOU 96 CZ3 TRP A 39 18998 21442 19918 -383 3352 682 C
ATOM 97 CH2 TRP A 39 -8.710 33.087 -15.727 1.00187.77 C
ANISOU 97 CH2 TRP A 39 22762 25115 23466 -349 3158 636 C
ATOM 98 N ARG A 40 -11.120 36.928 -12.843 1.00159.36 N
ANISOU 98 N ARG A 40 18406 21659 20486 606 3769 1407 N
ATOM 99 CA ARG A 40 -12.189 36.790 -13.838 1.00162.85 C
ANISOU 99 CA ARG A 40 18326 22720 20829 452 3661 1431 C
ATOM 100 C ARG A 40 -12.719 38.128 -14.355 1.00170.88 C
ANISOU 100 C ARG A 40 18879 24124 21925 823 3635 1725 C
ATOM 101 O ARG A 40 -12.943 38.288 -15.561 1.00165.53 O
ANISOU 101 O ARG A 40 17864 23885 21146 835 3445 1793 O
ATOM 102 CB ARG A 40 -13.317 35.888 -13.333 1.00166.63 C
ANISOU 102 CB ARG A 40 18676 23358 21278 57 3783 1279 C
ATOM 103 CG ARG A 40 -12.858 34.434 -13.239 1.00165.11 C
ANISOU 103 CG ARG A 40 18873 22910 20950 -360 3744 975 C
ATOM 104 CD ARG A 40 -13.812 33.516 -12.504 1.00167.39 C
ANISOU 104 CD ARG A 40 19150 23232 21217 -753 3892 806 C
ATOM 105 NE ARG A 40 -14.373 34.078 -11.286 1.00167.64 N
ANISOU 105 NE ARG A 40 19158 23113 21424 -625 4132 906 N
ATOM 106 CZ ARG A 40 -15.343 33.490 -10.595 1.00169.88 C
ANISOU 106 CZ ARG A 40 19363 23472 21712 -920 4284 799 C
ATOM 107 NH1 ARG A 40 -15.871 32.355 -11.033 1.00172.09 N
ANISOU 107 NH1 ARG A 40 19568 23993 21826 -1354 4213 600 N
ATOM 108 NH2 ARG A 40 -15.809 34.050 -9.490 1.00172.69 N
ANISOU 108 NH2 ARG A 40 19708 23675 22231 -789 4511 893 N
ATOM 109 N GLU A 41 -12.921 39.105 -13.464 1.00190.73 N
ANISOU 109 N GLU A 41 21376 26476 24615 1125 3825 1904 N
ATOM 110 CA GLU A 41 -13.336 40.434 -13.927 1.00199.53 C
ANISOU 110 CA GLU A 41 22085 27912 25813 1514 3810 2195 C
ATOM 111 C GLU A 41 -12.250 41.101 -14.769 1.00223.09 C
ANISOU 111 C GLU A 41 25172 30838 28752 1808 3622 2305 C
ATOM 112 O GLU A 41 -12.544 41.715 -15.809 1.00253.62 O
ANISOU 112 O GLU A 41 28655 35131 32578 1969 3473 2464 O
ATOM 113 CB GLU A 41 -13.699 41.312 -12.728 1.00204.65 C
ANISOU 113 CB GLU A 41 22758 28340 26659 1773 4077 2351 C
ATOM 114 CG GLU A 41 -14.213 42.717 -13.063 1.00216.07 C
ANISOU 114 CG GLU A 41 23796 30090 28212 2191 4104 2660 C
ATOM 115 CD GLU A 41 -15.336 42.744 -14.093 1.00238.42 C
ANISOU 115 CD GLU A 41 26016 33589 30983 2116 3981 2750 C
ATOM 116 OE1 GLU A 41 -16.032 41.723 -14.275 1.00248.79 O
ANISOU 116 OE1 GLU A 41 27172 35154 32204 1723 3947 2585 O
ATOM 117 OE2 GLU A 41 -15.525 43.805 -14.724 1.00241.88 O
ANISOU 117 OE2 GLU A 41 26133 34307 31466 2451 3916 2995 O
ATOM 118 N TYR A 42 -10.995 40.969 -14.345 1.00219.08 N
ANISOU 118 N TYR A 42 25177 29816 28246 1869 3621 2221 N
ATOM 119 CA TYR A 42 -9.852 41.379 -15.151 1.00156.26 C
ANISOU 119 CA TYR A 42 17374 21774 20224 2082 3432 2276 C
ATOM 120 C TYR A 42 -9.933 40.762 -16.542 1.00160.77 C
ANISOU 120 C TYR A 42 17716 22755 20616 1868 3186 2183 C
ATOM 121 O TYR A 42 -9.698 41.438 -17.544 1.00162.07 O
ANISOU 121 O TYR A 42 17677 23174 20730 2079 3020 2324 O
ATOM 122 CB TYR A 42 -8.557 40.972 -14.440 1.00152.66 C
ANISOU 122 CB TYR A 42 17518 20709 19777 2064 3469 2144 C
ATOM 123 CG TYR A 42 -7.269 41.454 -15.075 1.00149.82 C
ANISOU 123 CG TYR A 42 17371 20184 19368 2307 3305 2207 C
ATOM 124 CD1 TYR A 42 -6.657 40.736 -16.094 1.00149.36 C
ANISOU 124 CD1 TYR A 42 17379 20215 19157 2138 3094 2062 C
ATOM 125 CD2 TYR A 42 -6.641 42.605 -14.621 1.00161.47 C
ANISOU 125 CD2 TYR A 42 19007 21399 20946 2694 3374 2405 C
ATOM 126 CE1 TYR A 42 -5.482 41.180 -16.676 1.00146.83 C
ANISOU 126 CE1 TYR A 42 17247 19750 18792 2358 2950 2119 C
ATOM 127 CE2 TYR A 42 -5.458 43.048 -15.184 1.00145.02 C
ANISOU 127 CE2 TYR A 42 17121 19169 18810 2907 3227 2463 C
ATOM 128 CZ TYR A 42 -4.885 42.334 -16.213 1.00144.65 C
ANISOU 128 CZ TYR A 42 17113 19231 18618 2741 3014 2319 C
ATOM 129 OH TYR A 42 -3.699 42.762 -16.763 1.00142.13 O
ANISOU 129 OH TYR A 42 16991 18765 18249 2949 2874 2372 O
ATOM 130 N ARG A 43 -10.193 39.457 -16.613 1.00172.90 N
ANISOU 130 N ARG A 43 19320 24330 22043 1438 3160 1938 N
ATOM 131 CA ARG A 43 -10.308 38.781 -17.899 1.00175.75 C
ANISOU 131 CA ARG A 43 19488 25070 22218 1188 2942 1831 C
ATOM 132 C ARG A 43 -11.448 39.337 -18.749 1.00209.41 C
ANISOU 132 C ARG A 43 23147 29966 26454 1233 2857 2007 C
ATOM 133 O ARG A 43 -11.299 39.477 -19.966 1.00234.39 O
ANISOU 133 O ARG A 43 26112 33447 29498 1249 2648 2052 O
ATOM 134 CB ARG A 43 -10.547 37.294 -17.643 1.00178.28 C
ANISOU 134 CB ARG A 43 19990 25309 22437 705 2974 1542 C
ATOM 135 CG ARG A 43 -10.789 36.443 -18.867 1.00181.15 C
ANISOU 135 CG ARG A 43 20178 26057 22596 373 2781 1402 C
ATOM 136 CD ARG A 43 -10.809 34.977 -18.473 1.00186.36 C
ANISOU 136 CD ARG A 43 21131 26516 23160 -80 2836 1105 C
ATOM 137 NE ARG A 43 -11.954 34.690 -17.606 1.00188.73 N
ANISOU 137 NE ARG A 43 21274 26913 23521 -271 3013 1078 N
ATOM 138 CZ ARG A 43 -13.224 34.661 -18.003 1.00192.33 C
ANISOU 138 CZ ARG A 43 21252 27897 23928 -438 2998 1132 C
ATOM 139 NH1 ARG A 43 -13.539 34.885 -19.272 1.00193.77 N
ANISOU 139 NH1 ARG A 43 21062 28569 23991 -450 2805 1219 N
ATOM 140 NH2 ARG A 43 -14.183 34.396 -17.126 1.00192.85 N
ANISOU 140 NH2 ARG A 43 21211 28005 24058 -604 3175 1101 N
ATOM 141 N ARG A 44 -12.606 39.619 -18.143 1.00199.02 N
ANISOU 141 N ARG A 44 21528 28850 25243 1236 3015 2105 N
ATOM 142 CA ARG A 44 -13.720 40.184 -18.907 1.00180.67 C
ANISOU 142 CA ARG A 44 18605 27134 22906 1296 2940 2296 C
ATOM 143 C ARG A 44 -13.349 41.528 -19.531 1.00183.80 C
ANISOU 143 C ARG A 44 18829 27651 23356 1750 2840 2565 C
ATOM 144 O ARG A 44 -13.441 41.728 -20.751 1.00184.63 O
ANISOU 144 O ARG A 44 18645 28158 23349 1761 2628 2645 O
ATOM 145 CB ARG A 44 -14.949 40.318 -18.006 1.00182.09 C
ANISOU 145 CB ARG A 44 18522 27446 23216 1262 3158 2364 C
ATOM 146 CG ARG A 44 -15.489 38.987 -17.509 1.00183.16 C
ANISOU 146 CG ARG A 44 18756 27556 23279 781 3241 2107 C
ATOM 147 CD ARG A 44 -16.802 39.159 -16.767 1.00189.94 C
ANISOU 147 CD ARG A 44 19281 28632 24255 741 3440 2189 C
ATOM 148 NE ARG A 44 -17.302 37.891 -16.242 1.00205.65 N
ANISOU 148 NE ARG A 44 21388 30580 26170 274 3526 1938 N
ATOM 149 CZ ARG A 44 -18.348 37.780 -15.430 1.00219.27 C
ANISOU 149 CZ ARG A 44 22924 32406 27981 157 3721 1942 C
ATOM 150 NH1 ARG A 44 -19.014 38.862 -15.052 1.00222.87 N
ANISOU 150 NH1 ARG A 44 23058 33011 28610 481 3859 2188 N
ATOM 151 NH2 ARG A 44 -18.735 36.585 -15.003 1.00221.59 N
ANISOU 151 NH2 ARG A 44 23354 32653 28187 -286 3785 1701 N
ATOM 152 N GLN A 45 -12.913 42.466 -18.689 1.00166.64 N
ANISOU 152 N GLN A 45 16848 25121 21346 2120 2994 2708 N
ATOM 153 CA GLN A 45 -12.510 43.783 -19.172 1.00165.62 C
ANISOU 153 CA GLN A 45 16604 25053 21270 2566 2921 2965 C
ATOM 154 C GLN A 45 -11.367 43.683 -20.170 1.00225.05 C
ANISOU 154 C GLN A 45 24334 32522 28654 2586 2686 2906 C
ATOM 155 O GLN A 45 -11.317 44.413 -21.170 1.00211.59 O
ANISOU 155 O GLN A 45 22371 31122 26901 2789 2519 3074 O
ATOM 156 CB GLN A 45 -12.074 44.651 -17.992 1.00163.30 C
ANISOU 156 CB GLN A 45 16597 24296 21155 2908 3142 3084 C
ATOM 157 CG GLN A 45 -13.144 44.959 -16.968 1.00198.44 C
ANISOU 157 CG GLN A 45 20859 28773 25767 2956 3400 3174 C
ATOM 158 CD GLN A 45 -12.613 45.833 -15.849 1.00197.08 C
ANISOU 158 CD GLN A 45 21012 28117 25752 3287 3615 3288 C
ATOM 159 OE1 GLN A 45 -11.537 46.421 -15.966 1.00160.01 O
ANISOU 159 OE1 GLN A 45 16600 23147 21049 3536 3553 3355 O
ATOM 160 NE2 GLN A 45 -13.355 45.911 -14.751 1.00196.90 N
ANISOU 160 NE2 GLN A 45 20962 27986 25866 3277 3871 3308 N
ATOM 161 N CYS A 46 -10.456 42.752 -19.910 1.00194.43 N
ANISOU 161 N CYS A 46 20916 28253 24707 2367 2674 2665 N
ATOM 162 CA CYS A 46 -9.282 42.534 -20.738 1.00202.66 C
ANISOU 162 CA CYS A 46 22211 29172 25620 2365 2478 2577 C
ATOM 163 C CYS A 46 -9.672 42.071 -22.143 1.00215.00 C
ANISOU 163 C CYS A 46 23444 31243 27002 2131 2247 2530 C
ATOM 164 O CYS A 46 -9.232 42.649 -23.143 1.00222.00 O
ANISOU 164 O CYS A 46 24223 32312 27817 2305 2066 2639 O
ATOM 165 CB CYS A 46 -8.480 41.451 -20.013 1.00209.43 C
ANISOU 165 CB CYS A 46 23589 29528 26456 2119 2552 2313 C
ATOM 166 SG CYS A 46 -6.911 40.824 -20.545 1.00218.12 S
ANISOU 166 SG CYS A 46 25158 30284 27433 2047 2397 2129 S
ATOM 167 N GLN A 47 -10.497 41.018 -22.234 1.00209.38 N
ANISOU 167 N GLN A 47 22583 30765 26205 1721 2250 2365 N
ATOM 168 CA GLN A 47 -11.025 40.563 -23.523 1.00207.66 C
ANISOU 168 CA GLN A 47 22024 31068 25808 1460 2044 2329 C
ATOM 169 C GLN A 47 -11.771 41.677 -24.254 1.00213.09 C
ANISOU 169 C GLN A 47 22183 32259 26521 1714 1946 2619 C
ATOM 170 O GLN A 47 -11.691 41.790 -25.484 1.00229.08 O
ANISOU 170 O GLN A 47 24007 34624 28410 1683 1727 2665 O
ATOM 171 CB GLN A 47 -11.893 39.308 -23.352 1.00207.32 C
ANISOU 171 CB GLN A 47 21903 31191 25678 977 2093 2121 C
ATOM 172 CG GLN A 47 -13.159 39.453 -22.539 1.00220.81 C
ANISOU 172 CG GLN A 47 23310 33080 27507 946 2272 2209 C
ATOM 173 CD GLN A 47 -14.076 38.250 -22.658 1.00234.59 C
ANISOU 173 CD GLN A 47 24905 35104 29125 445 2271 2021 C
ATOM 174 OE1 GLN A 47 -14.064 37.543 -23.665 1.00243.21 O
ANISOU 174 OE1 GLN A 47 25937 36451 30022 147 2095 1900 O
ATOM 175 NE2 GLN A 47 -14.884 38.018 -21.629 1.00231.30 N
ANISOU 175 NE2 GLN A 47 24431 34641 28809 340 2473 1995 N
ATOM 176 N ARG A 48 -12.499 42.516 -23.506 1.00206.28 N
ANISOU 176 N ARG A 48 21097 31446 25835 1969 2109 2820 N
ATOM 177 CA ARG A 48 -13.190 43.650 -24.121 1.00211.02 C
ANISOU 177 CA ARG A 48 21204 32492 26482 2255 2033 3117 C
ATOM 178 C ARG A 48 -12.213 44.642 -24.748 1.00219.86 C
ANISOU 178 C ARG A 48 22426 33518 27593 2626 1900 3270 C
ATOM 179 O ARG A 48 -12.443 45.128 -25.865 1.00226.76 O
ANISOU 179 O ARG A 48 22963 34811 28384 2702 1705 3418 O
ATOM 180 CB ARG A 48 -14.082 44.344 -23.091 1.00187.52 C
ANISOU 180 CB ARG A 48 18019 29518 23711 2475 2268 3294 C
ATOM 181 CG ARG A 48 -15.241 43.486 -22.602 1.00191.89 C
ANISOU 181 CG ARG A 48 18363 30278 24270 2119 2386 3183 C
ATOM 182 CD ARG A 48 -16.205 43.150 -23.729 1.00202.77 C
ANISOU 182 CD ARG A 48 19230 32307 25507 1863 2198 3224 C
ATOM 183 NE ARG A 48 -16.910 41.894 -23.488 1.00206.81 N
ANISOU 183 NE ARG A 48 19704 32944 25931 1379 2245 3005 N
ATOM 184 CZ ARG A 48 -16.562 40.730 -24.027 1.00211.54 C
ANISOU 184 CZ ARG A 48 20499 33544 26333 969 2117 2752 C
ATOM 185 NH1 ARG A 48 -17.270 39.638 -23.771 1.00219.54 N
ANISOU 185 NH1 ARG A 48 21469 34680 27265 534 2173 2566 N
ATOM 186 NH2 ARG A 48 -15.518 40.661 -24.841 1.00214.27 N
ANISOU 186 NH2 ARG A 48 21082 33774 26556 989 1937 2686 N
ATOM 187 N SER A 49 -11.108 44.942 -24.059 1.00165.75 N
ANISOU 187 N SER A 49 16039 26124 20815 2845 1994 3238 N
ATOM 188 CA SER A 49 -10.059 45.750 -24.681 1.00163.31 C
ANISOU 188 CA SER A 49 15880 25700 20470 3150 1856 3347 C
ATOM 189 C SER A 49 -9.487 45.059 -25.917 1.00163.11 C
ANISOU 189 C SER A 49 15904 25836 20235 2901 1609 3194 C
ATOM 190 O SER A 49 -9.262 45.706 -26.947 1.00192.07 O
ANISOU 190 O SER A 49 19395 29758 23826 3061 1423 3331 O
ATOM 191 CB SER A 49 -8.956 46.049 -23.668 1.00159.45 C
ANISOU 191 CB SER A 49 15909 24589 20084 3372 2005 3316 C
ATOM 192 OG SER A 49 -8.188 47.169 -24.072 1.00185.55 O
ANISOU 192 OG SER A 49 19281 27821 23400 3755 1922 3501 O
ATOM 193 N LEU A 50 -9.231 43.751 -25.827 1.00165.75 N
ANISOU 193 N LEU A 50 16493 26013 20472 2509 1609 2909 N
ATOM 194 CA LEU A 50 -8.700 42.998 -26.963 1.00168.82 C
ANISOU 194 CA LEU A 50 16956 26531 20658 2242 1399 2741 C
ATOM 195 C LEU A 50 -9.597 43.153 -28.183 1.00172.96 C
ANISOU 195 C LEU A 50 16964 27692 21060 2127 1208 2855 C
ATOM 196 O LEU A 50 -9.113 43.292 -29.313 1.00173.63 O
ANISOU 196 O LEU A 50 17008 27956 21008 2127 1003 2869 O
ATOM 197 CB LEU A 50 -8.528 41.523 -26.605 1.00167.42 C
ANISOU 197 CB LEU A 50 17086 26124 20402 1814 1459 2425 C
ATOM 198 CG LEU A 50 -7.497 41.216 -25.521 1.00169.95 C
ANISOU 198 CG LEU A 50 17955 25802 20816 1882 1614 2288 C
ATOM 199 CD1 LEU A 50 -7.607 39.769 -25.073 1.00177.95 C
ANISOU 199 CD1 LEU A 50 19205 26639 21768 1450 1695 1999 C
ATOM 200 CD2 LEU A 50 -6.098 41.522 -26.032 1.00162.62 C
ANISOU 200 CD2 LEU A 50 17339 24612 19837 2075 1496 2276 C
ATOM 201 N THR A 51 -10.909 43.131 -27.967 1.00178.07 N
ANISOU 201 N THR A 51 17211 28693 21754 2021 1273 2942 N
ATOM 202 CA THR A 51 -11.863 43.250 -29.062 1.00184.60 C
ANISOU 202 CA THR A 51 17517 30151 22470 1890 1095 3066 C
ATOM 203 C THR A 51 -11.930 44.679 -29.589 1.00191.82 C
ANISOU 203 C THR A 51 18135 31298 23448 2320 999 3384 C
ATOM 204 O THR A 51 -12.042 44.889 -30.803 1.00200.33 O
ANISOU 204 O THR A 51 18950 32774 24391 2277 777 3469 O
ATOM 205 CB THR A 51 -13.249 42.787 -28.605 1.00176.53 C
ANISOU 205 CB THR A 51 16154 29433 21486 1648 1204 3069 C
ATOM 206 OG1 THR A 51 -13.189 41.415 -28.196 1.00176.42 O
ANISOU 206 OG1 THR A 51 16423 29220 21389 1220 1279 2764 O
ATOM 207 CG2 THR A 51 -14.269 42.932 -29.729 1.00180.47 C
ANISOU 207 CG2 THR A 51 16089 30609 21871 1509 1014 3219 C
ATOM 208 N GLU A 52 -11.852 45.679 -28.710 1.00199.02 N
ANISOU 208 N GLU A 52 19097 31965 24558 2732 1163 3563 N
ATOM 209 CA GLU A 52 -12.190 47.035 -29.119 1.00204.77 C
ANISOU 209 CA GLU A 52 19479 32963 25362 3130 1102 3887 C
ATOM 210 C GLU A 52 -11.007 47.925 -29.510 1.00197.69 C
ANISOU 210 C GLU A 52 18831 31830 24452 3478 1008 3983 C
ATOM 211 O GLU A 52 -11.220 48.883 -30.263 1.00202.43 O
ANISOU 211 O GLU A 52 19128 32743 25043 3723 875 4221 O
ATOM 212 CB GLU A 52 -12.975 47.704 -27.975 1.00219.17 C
ANISOU 212 CB GLU A 52 21148 34718 27409 3387 1350 4060 C
ATOM 213 CG GLU A 52 -13.119 49.222 -28.009 1.00244.94 C
ANISOU 213 CG GLU A 52 24194 38069 30803 3890 1371 4391 C
ATOM 214 CD GLU A 52 -11.900 49.956 -27.468 1.00270.60 C
ANISOU 214 CD GLU A 52 27903 40785 34126 4243 1455 4423 C
ATOM 215 OE1 GLU A 52 -11.126 49.344 -26.704 1.00282.12 O
ANISOU 215 OE1 GLU A 52 29831 41767 35597 4132 1569 4210 O
ATOM 216 OE2 GLU A 52 -11.716 51.143 -27.812 1.00271.26 O
ANISOU 216 OE2 GLU A 52 27882 40932 34251 4626 1405 4664 O
ATOM 217 N ASP A 53 -9.772 47.642 -29.089 1.00183.90 N
ANISOU 217 N ASP A 53 17611 29567 22696 3501 1056 3812 N
ATOM 218 CA ASP A 53 -8.686 48.530 -29.505 1.00201.73 C
ANISOU 218 CA ASP A 53 20076 31639 24934 3829 959 3917 C
ATOM 219 C ASP A 53 -8.460 48.451 -31.017 1.00218.62 C
ANISOU 219 C ASP A 53 22048 34144 26874 3702 674 3913 C
ATOM 220 O ASP A 53 -8.514 47.363 -31.601 1.00222.63 O
ANISOU 220 O ASP A 53 22560 34799 27231 3300 569 3705 O
ATOM 221 CB ASP A 53 -7.394 48.195 -28.761 1.00196.63 C
ANISOU 221 CB ASP A 53 20019 30379 24312 3860 1062 3736 C
ATOM 222 CG ASP A 53 -7.457 48.568 -27.292 1.00180.73 C
ANISOU 222 CG ASP A 53 18201 27972 22496 4067 1332 3791 C
ATOM 223 OD1 ASP A 53 -8.241 49.477 -26.944 1.00175.83 O
ANISOU 223 OD1 ASP A 53 17298 27506 22002 4326 1432 4024 O
ATOM 224 OD2 ASP A 53 -6.719 47.961 -26.489 1.00172.13 O
ANISOU 224 OD2 ASP A 53 17552 26416 21436 3971 1448 3606 O
ATOM 225 N PRO A 54 -8.208 49.589 -31.673 1.00214.66 N
ANISOU 225 N PRO A 54 21410 33788 26361 4030 550 4141 N
ATOM 226 CA PRO A 54 -8.002 49.573 -33.122 1.00214.45 C
ANISOU 226 CA PRO A 54 21223 34115 26143 3913 276 4148 C
ATOM 227 C PRO A 54 -6.754 48.812 -33.525 1.00204.56 C
ANISOU 227 C PRO A 54 20403 32574 24748 3717 188 3890 C
ATOM 228 O PRO A 54 -5.781 48.723 -32.755 1.00199.42 O
ANISOU 228 O PRO A 54 20200 31410 24161 3824 313 3780 O
ATOM 229 CB PRO A 54 -7.884 51.067 -33.477 1.00217.99 C
ANISOU 229 CB PRO A 54 21513 34671 26644 4369 206 4455 C
ATOM 230 CG PRO A 54 -7.411 51.709 -32.224 1.00218.72 C
ANISOU 230 CG PRO A 54 21913 34276 26916 4709 438 4520 C
ATOM 231 CD PRO A 54 -8.060 50.941 -31.107 1.00216.42 C
ANISOU 231 CD PRO A 54 21652 33838 26740 4518 659 4395 C
ATOM 232 N PRO A 55 -6.735 48.241 -34.727 1.00187.02 N
ANISOU 232 N PRO A 55 18065 30665 22329 3422 -23 3789 N
ATOM 233 CA PRO A 55 -5.560 47.509 -35.215 1.00182.81 C
ANISOU 233 CA PRO A 55 17925 29882 21653 3230 -108 3542 C
ATOM 234 C PRO A 55 -4.379 48.442 -35.425 1.00176.68 C
ANISOU 234 C PRO A 55 17399 28851 20880 3588 -166 3637 C
ATOM 235 O PRO A 55 -4.557 49.660 -35.574 1.00184.42 O
ANISOU 235 O PRO A 55 18178 29975 21919 3937 -209 3904 O
ATOM 236 CB PRO A 55 -6.044 46.899 -36.541 1.00186.14 C
ANISOU 236 CB PRO A 55 18068 30793 21863 2860 -325 3474 C
ATOM 237 CG PRO A 55 -7.536 46.914 -36.442 1.00174.46 C
ANISOU 237 CG PRO A 55 16108 29750 20430 2755 -305 3611 C
ATOM 238 CD PRO A 55 -7.847 48.168 -35.687 1.00178.83 C
ANISOU 238 CD PRO A 55 16521 30238 21187 3218 -187 3890 C
ATOM 239 N PRO A 56 -3.161 47.910 -35.442 1.00175.34 N
ANISOU 239 N PRO A 56 17669 28305 20647 3514 -168 3429 N
ATOM 240 CA PRO A 56 -1.969 48.758 -35.552 1.00207.27 C
ANISOU 240 CA PRO A 56 21982 32074 24695 3846 -210 3508 C
ATOM 241 C PRO A 56 -1.820 49.375 -36.939 1.00216.00 C
ANISOU 241 C PRO A 56 22878 33546 25647 3902 -455 3625 C
ATOM 242 O PRO A 56 -2.377 48.909 -37.935 1.00226.95 O
ANISOU 242 O PRO A 56 23998 35343 26889 3616 -611 3581 O
ATOM 243 CB PRO A 56 -0.822 47.794 -35.240 1.00149.51 C
ANISOU 243 CB PRO A 56 15158 24302 17346 3676 -147 3228 C
ATOM 244 CG PRO A 56 -1.342 46.502 -35.680 1.00151.74 C
ANISOU 244 CG PRO A 56 15357 24784 17514 3214 -185 3006 C
ATOM 245 CD PRO A 56 -2.787 46.499 -35.267 1.00154.80 C
ANISOU 245 CD PRO A 56 15361 25477 17980 3135 -112 3113 C
ATOM 246 N ALA A 57 -1.041 50.460 -36.965 1.00244.32 N
ANISOU 246 N ALA A 57 26602 36967 29263 4274 -485 3782 N
ATOM 247 CA ALA A 57 -0.751 51.229 -38.176 1.00245.95 C
ANISOU 247 CA ALA A 57 26660 37454 29335 4395 -707 3915 C
ATOM 248 C ALA A 57 -0.287 50.362 -39.345 1.00247.07 C
ANISOU 248 C ALA A 57 26865 37744 29267 4044 -883 3701 C
ATOM 249 O ALA A 57 -0.647 50.631 -40.497 1.00249.47 O
ANISOU 249 O ALA A 57 26880 38472 29434 3965 -1084 3788 O
ATOM 250 CB ALA A 57 0.295 52.301 -37.870 1.00243.48 C
ANISOU 250 CB ALA A 57 26625 36811 29074 4804 -680 4044 C
ATOM 251 N THR A 58 0.503 49.322 -39.087 1.00241.23 N
ANISOU 251 N THR A 58 26497 36662 28496 3825 -810 3425 N
ATOM 252 CA THR A 58 0.962 48.456 -40.167 1.00233.87 C
ANISOU 252 CA THR A 58 25649 35843 27367 3486 -952 3209 C
ATOM 253 C THR A 58 0.857 47.001 -39.734 1.00234.83 C
ANISOU 253 C THR A 58 25949 35794 27481 3107 -832 2926 C
ATOM 254 O THR A 58 0.831 46.681 -38.543 1.00226.89 O
ANISOU 254 O THR A 58 25121 34461 26625 3148 -637 2870 O
ATOM 255 CB THR A 58 2.413 48.760 -40.582 1.00223.62 C
ANISOU 255 CB THR A 58 24697 34268 25999 3639 -1018 3150 C
ATOM 256 OG1 THR A 58 3.285 48.571 -39.460 1.00207.61 O
ANISOU 256 OG1 THR A 58 23080 31698 24103 3781 -834 3057 O
ATOM 257 CG2 THR A 58 2.553 50.189 -41.096 1.00229.33 C
ANISOU 257 CG2 THR A 58 25261 35168 26704 3994 -1149 3422 C
ATOM 258 N ASP A 59 0.800 46.119 -40.738 1.00238.19 N
ANISOU 258 N ASP A 59 26334 36446 27721 2725 -951 2745 N
ATOM 259 CA ASP A 59 0.768 44.678 -40.518 1.00241.06 C
ANISOU 259 CA ASP A 59 26889 36663 28040 2330 -855 2457 C
ATOM 260 C ASP A 59 2.093 44.093 -40.062 1.00241.08 C
ANISOU 260 C ASP A 59 27401 36126 28073 2348 -745 2243 C
ATOM 261 O ASP A 59 2.135 42.906 -39.722 1.00243.10 O
ANISOU 261 O ASP A 59 27860 36192 28316 2056 -638 2007 O
ATOM 262 CB ASP A 59 0.375 43.978 -41.822 1.00247.41 C
ANISOU 262 CB ASP A 59 27516 37873 28616 1919 -1020 2337 C
ATOM 263 CG ASP A 59 -1.042 44.286 -42.254 1.00267.06 C
ANISOU 263 CG ASP A 59 29492 40918 31061 1809 -1125 2518 C
ATOM 264 OD1 ASP A 59 -1.946 44.294 -41.395 1.00276.28 O
ANISOU 264 OD1 ASP A 59 30483 42132 32360 1836 -1009 2600 O
ATOM 265 OD2 ASP A 59 -1.246 44.528 -43.464 1.00272.94 O
ANISOU 265 OD2 ASP A 59 30006 42059 31638 1693 -1326 2583 O
ATOM 266 N LEU A 60 3.168 44.874 -40.042 1.00238.19 N
ANISOU 266 N LEU A 60 27247 35511 27745 2675 -766 2322 N
ATOM 267 CA LEU A 60 4.388 44.471 -39.349 1.00226.77 C
ANISOU 267 CA LEU A 60 26268 33521 26374 2761 -638 2170 C
ATOM 268 C LEU A 60 4.140 44.530 -37.844 1.00224.59 C
ANISOU 268 C LEU A 60 26099 32928 26305 2918 -434 2223 C
ATOM 269 O LEU A 60 4.477 45.506 -37.171 1.00228.05 O
ANISOU 269 O LEU A 60 26606 33173 26869 3283 -380 2404 O
ATOM 270 CB LEU A 60 5.555 45.358 -39.763 1.00211.19 C
ANISOU 270 CB LEU A 60 24462 31406 24375 3065 -726 2261 C
ATOM 271 CG LEU A 60 5.846 45.366 -41.262 1.00199.33 C
ANISOU 271 CG LEU A 60 22864 30208 22664 2919 -927 2213 C
ATOM 272 CD1 LEU A 60 7.051 46.237 -41.570 1.00201.23 C
ANISOU 272 CD1 LEU A 60 23296 30275 22886 3226 -999 2296 C
ATOM 273 CD2 LEU A 60 6.059 43.946 -41.763 1.00199.41 C
ANISOU 273 CD2 LEU A 60 23042 30174 22551 2498 -913 1908 C
ATOM 274 N PHE A 61 3.494 43.490 -37.306 1.00225.59 N
ANISOU 274 N PHE A 61 26239 33015 26462 2628 -318 2067 N
ATOM 275 CA PHE A 61 3.326 43.452 -35.858 1.00209.11 C
ANISOU 275 CA PHE A 61 24292 30594 24565 2748 -118 2092 C
ATOM 276 C PHE A 61 2.947 42.064 -35.358 1.00209.12 C
ANISOU 276 C PHE A 61 24424 30463 24568 2379 6 1850 C
ATOM 277 O PHE A 61 2.178 41.342 -35.999 1.00222.89 O
ANISOU 277 O PHE A 61 25969 32530 26188 2035 -52 1743 O
ATOM 278 CB PHE A 61 2.233 44.433 -35.417 1.00184.06 C
ANISOU 278 CB PHE A 61 20760 27675 21498 2958 -92 2356 C
ATOM 279 CG PHE A 61 0.841 43.950 -35.718 1.00186.57 C
ANISOU 279 CG PHE A 61 20699 28427 21762 2664 -118 2345 C
ATOM 280 CD1 PHE A 61 0.376 43.906 -37.023 1.00202.65 C
ANISOU 280 CD1 PHE A 61 22436 30938 23622 2472 -309 2357 C
ATOM 281 CD2 PHE A 61 0.002 43.528 -34.700 1.00187.48 C
ANISOU 281 CD2 PHE A 61 20760 28481 21993 2563 47 2322 C
ATOM 282 CE1 PHE A 61 -0.900 43.459 -37.305 1.00211.59 C
ANISOU 282 CE1 PHE A 61 23215 32484 24696 2187 -339 2356 C
ATOM 283 CE2 PHE A 61 -1.276 43.080 -34.975 1.00204.61 C
ANISOU 283 CE2 PHE A 61 22574 31062 24107 2284 22 2315 C
ATOM 284 CZ PHE A 61 -1.728 43.046 -36.280 1.00214.02 C
ANISOU 284 CZ PHE A 61 23462 32733 25122 2095 -173 2336 C
ATOM 285 N CYS A 62 3.514 41.710 -34.210 1.00197.27 N
ANISOU 285 N CYS A 62 23270 28480 23202 2448 175 1770 N
ATOM 286 CA CYS A 62 3.076 40.597 -33.378 1.00193.12 C
ANISOU 286 CA CYS A 62 22879 27768 22729 2176 330 1590 C
ATOM 287 C CYS A 62 1.682 40.881 -32.802 1.00172.01 C
ANISOU 287 C CYS A 62 19867 25353 20136 2157 400 1723 C
ATOM 288 O CYS A 62 1.345 42.022 -32.478 1.00161.96 O
ANISOU 288 O CYS A 62 18400 24174 18963 2467 408 1967 O
ATOM 289 CB CYS A 62 4.140 40.270 -32.329 1.00221.80 C
ANISOU 289 CB CYS A 62 26975 30813 26486 2290 474 1498 C
ATOM 290 SG CYS A 62 4.407 41.460 -31.073 1.00217.24 S
ANISOU 290 SG CYS A 62 26493 29936 26114 2729 591 1740 S
ATOM 291 N ASN A 63 0.877 39.827 -32.651 1.00182.40 N
ANISOU 291 N ASN A 63 21122 26771 21410 1790 462 1560 N
ATOM 292 CA ASN A 63 -0.502 39.960 -32.180 1.00194.30 C
ANISOU 292 CA ASN A 63 22288 28559 22978 1720 527 1663 C
ATOM 293 C ASN A 63 -0.685 40.096 -30.675 1.00186.69 C
ANISOU 293 C ASN A 63 21465 27256 22212 1865 735 1711 C
ATOM 294 O ASN A 63 -0.146 39.307 -29.896 1.00165.92 O
ANISOU 294 O ASN A 63 19205 24202 19633 1759 861 1538 O
ATOM 295 CB ASN A 63 -1.320 38.720 -32.534 1.00210.57 C
ANISOU 295 CB ASN A 63 24245 30855 24908 1240 524 1460 C
ATOM 296 CG ASN A 63 -1.717 38.612 -33.971 1.00242.75 C
ANISOU 296 CG ASN A 63 28031 35421 28780 1025 329 1452 C
ATOM 297 OD1 ASN A 63 -1.062 39.078 -34.904 1.00213.00 O
ANISOU 297 OD1 ASN A 63 24261 31743 24924 1142 182 1499 O
ATOM 298 ND2 ASN A 63 -2.860 37.955 -34.136 1.00303.20 N
ANISOU 298 ND2 ASN A 63 35435 43414 36355 678 329 1389 N
ATOM 299 N ARG A 64 -1.476 41.104 -30.283 1.00187.48 N
ANISOU 299 N ARG A 64 21262 27551 22421 2104 772 1953 N
ATOM 300 CA ARG A 64 -2.008 41.265 -28.931 1.00189.19 C
ANISOU 300 CA ARG A 64 21505 27564 22813 2198 974 2017 C
ATOM 301 C ARG A 64 -2.469 39.897 -28.433 1.00196.83 C
ANISOU 301 C ARG A 64 22594 28435 23756 1790 1081 1773 C
ATOM 302 O ARG A 64 -2.986 39.111 -29.233 1.00211.64 O
ANISOU 302 O ARG A 64 24309 30624 25481 1447 991 1642 O
ATOM 303 CB ARG A 64 -3.182 42.254 -28.915 1.00180.73 C
ANISOU 303 CB ARG A 64 19965 26891 21812 2376 978 2275 C
ATOM 304 CG ARG A 64 -4.433 41.733 -29.633 1.00179.94 C
ANISOU 304 CG ARG A 64 19444 27326 21598 2049 895 2245 C
ATOM 305 CD ARG A 64 -5.509 42.784 -29.893 1.00183.83 C
ANISOU 305 CD ARG A 64 19431 28275 22142 2247 853 2524 C
ATOM 306 NE ARG A 64 -5.099 43.828 -30.827 1.00188.20 N
ANISOU 306 NE ARG A 64 19838 29023 22647 2529 682 2715 N
ATOM 307 CZ ARG A 64 -5.907 44.792 -31.259 1.00190.93 C
ANISOU 307 CZ ARG A 64 19746 29783 23017 2720 609 2970 C
ATOM 308 NH1 ARG A 64 -7.175 44.821 -30.868 1.00188.59 N
ANISOU 308 NH1 ARG A 64 19099 29762 22794 2656 693 3064 N
ATOM 309 NH2 ARG A 64 -5.461 45.706 -32.109 1.00195.43 N
ANISOU 309 NH2 ARG A 64 20221 30501 23534 2968 449 3132 N
ATOM 310 N THR A 65 -2.415 39.635 -27.126 1.00188.87 N
ANISOU 310 N THR A 65 21837 27036 22887 1807 1274 1723 N
ATOM 311 CA THR A 65 -2.868 38.339 -26.616 1.00185.88 C
ANISOU 311 CA THR A 65 21587 26557 22483 1417 1381 1491 C
ATOM 312 C THR A 65 -3.073 38.422 -25.115 1.00173.39 C
ANISOU 312 C THR A 65 20170 24629 21081 1508 1597 1520 C
ATOM 313 O THR A 65 -2.324 39.097 -24.409 1.00170.97 O
ANISOU 313 O THR A 65 20100 23961 20899 1816 1670 1624 O
ATOM 314 CB THR A 65 -1.843 37.201 -26.838 1.00202.33 C
ANISOU 314 CB THR A 65 24092 28314 24471 1188 1357 1225 C
ATOM 315 OG1 THR A 65 -0.531 37.642 -26.456 1.00195.15 O
ANISOU 315 OG1 THR A 65 23542 26961 23646 1484 1376 1264 O
ATOM 316 CG2 THR A 65 -1.827 36.633 -28.260 1.00221.55 C
ANISOU 316 CG2 THR A 65 26404 31080 26694 930 1180 1104 C
ATOM 317 N PHE A 66 -3.982 37.609 -24.604 1.00187.74 N
ANISOU 317 N PHE A 66 21883 26550 22898 1210 1699 1415 N
ATOM 318 CA PHE A 66 -4.128 37.528 -23.172 1.00151.07 C
ANISOU 318 CA PHE A 66 17464 21542 18395 1183 1911 1367 C
ATOM 319 C PHE A 66 -3.506 36.182 -22.853 1.00164.78 C
ANISOU 319 C PHE A 66 19605 22936 20069 850 1958 1078 C
ATOM 320 O PHE A 66 -3.961 35.156 -23.343 1.00158.10 O
ANISOU 320 O PHE A 66 18684 22309 19079 479 1906 900 O
ATOM 321 CB PHE A 66 -5.576 37.548 -22.742 1.00154.00 C
ANISOU 321 CB PHE A 66 17456 22237 18820 1090 2011 1450 C
ATOM 322 CG PHE A 66 -5.744 37.486 -21.264 1.00153.33 C
ANISOU 322 CG PHE A 66 17585 21790 18884 1074 2238 1415 C
ATOM 323 CD1 PHE A 66 -5.059 38.365 -20.455 1.00150.55 C
ANISOU 323 CD1 PHE A 66 17489 21027 18687 1406 2349 1538 C
ATOM 324 CD2 PHE A 66 -6.565 36.546 -20.682 1.00163.62 C
ANISOU 324 CD2 PHE A 66 18827 23178 20163 717 2339 1266 C
ATOM 325 CE1 PHE A 66 -5.196 38.314 -19.087 1.00150.01 C
ANISOU 325 CE1 PHE A 66 17623 20626 18749 1378 2558 1509 C
ATOM 326 CE2 PHE A 66 -6.710 36.489 -19.314 1.00155.06 C
ANISOU 326 CE2 PHE A 66 17941 21763 19211 693 2548 1232 C
ATOM 327 CZ PHE A 66 -6.025 37.375 -18.516 1.00152.26 C
ANISOU 327 CZ PHE A 66 17847 20992 19013 1024 2658 1355 C
ATOM 328 N ASP A 67 -2.473 36.185 -22.024 1.00147.54 N
ANISOU 328 N ASP A 67 17855 20214 17991 979 2059 1039 N
ATOM 329 CA ASP A 67 -1.751 34.964 -21.694 1.00146.53 C
ANISOU 329 CA ASP A 67 18159 19690 17827 725 2107 788 C
ATOM 330 C ASP A 67 -2.112 34.394 -20.346 1.00191.97 C
ANISOU 330 C ASP A 67 24104 25149 23686 578 2305 708 C
ATOM 331 O ASP A 67 -1.341 33.605 -19.810 1.00145.11 O
ANISOU 331 O ASP A 67 18591 18773 17772 465 2370 550 O
ATOM 332 CB ASP A 67 -0.260 35.233 -21.696 1.00143.20 C
ANISOU 332 CB ASP A 67 18111 18865 17434 957 2057 793 C
ATOM 333 CG ASP A 67 0.173 35.989 -20.482 1.00140.68 C
ANISOU 333 CG ASP A 67 17934 18231 17287 1326 2153 990 C
ATOM 334 OD1 ASP A 67 -0.681 36.690 -19.910 1.00141.46 O
ANISOU 334 OD1 ASP A 67 17754 18528 17468 1503 2210 1182 O
ATOM 335 OD2 ASP A 67 1.352 35.881 -20.094 1.00138.00 O
ANISOU 335 OD2 ASP A 67 17991 17443 17001 1435 2175 957 O
ATOM 336 N GLU A 68 -3.205 34.915 -19.785 1.00184.12 N
ANISOU 336 N GLU A 68 22813 24376 22769 600 2406 828 N
ATOM 337 CA GLU A 68 -3.826 34.585 -18.481 1.00179.86 C
ANISOU 337 CA GLU A 68 22394 23613 22333 469 2603 776 C
ATOM 338 C GLU A 68 -3.161 35.270 -17.296 1.00172.56 C
ANISOU 338 C GLU A 68 21691 22287 21587 811 2726 938 C
ATOM 339 O GLU A 68 -3.555 35.063 -16.156 1.00165.37 O
ANISOU 339 O GLU A 68 20806 21241 20784 788 2899 965 O
ATOM 340 CB GLU A 68 -4.050 33.085 -18.217 1.00173.15 C
ANISOU 340 CB GLU A 68 21885 22491 21413 74 2658 491 C
ATOM 341 CG GLU A 68 -4.640 32.332 -19.390 1.00177.85 C
ANISOU 341 CG GLU A 68 22311 23449 21814 -302 2553 312 C
ATOM 342 CD GLU A 68 -6.146 32.259 -19.317 1.00200.82 C
ANISOU 342 CD GLU A 68 24706 26917 24681 -422 2548 396 C
ATOM 343 OE1 GLU A 68 -6.686 32.425 -18.207 1.00212.19 O
ANISOU 343 OE1 GLU A 68 26017 28370 26237 -381 2693 483 O
ATOM 344 OE2 GLU A 68 -6.790 32.028 -20.359 1.00211.75 O
ANISOU 344 OE2 GLU A 68 25811 28730 25914 -560 2401 378 O
ATOM 345 N TYR A 69 -2.133 36.063 -17.565 1.00175.60 N
ANISOU 345 N TYR A 69 22244 22478 21998 1117 2645 1046 N
ATOM 346 CA TYR A 69 -1.486 36.817 -16.513 1.00169.25 C
ANISOU 346 CA TYR A 69 21673 21289 21346 1432 2753 1205 C
ATOM 347 C TYR A 69 -1.540 38.301 -16.823 1.00175.35 C
ANISOU 347 C TYR A 69 22143 22311 22173 1813 2721 1481 C
ATOM 348 O TYR A 69 -1.457 39.124 -15.923 1.00175.39 O
ANISOU 348 O TYR A 69 22069 22271 22299 1977 2868 1632 O
ATOM 349 CB TYR A 69 -0.048 36.383 -16.314 1.00168.84 C
ANISOU 349 CB TYR A 69 22083 20778 21289 1495 2701 1128 C
ATOM 350 CG TYR A 69 0.632 37.156 -15.221 1.00170.65 C
ANISOU 350 CG TYR A 69 22581 20604 21653 1805 2792 1295 C
ATOM 351 CD1 TYR A 69 0.780 36.619 -13.960 1.00173.09 C
ANISOU 351 CD1 TYR A 69 23122 20569 22076 1746 2977 1284 C
ATOM 352 CD2 TYR A 69 1.112 38.432 -15.448 1.00167.91 C
ANISOU 352 CD2 TYR A 69 22253 20233 21313 2145 2695 1466 C
ATOM 353 CE1 TYR A 69 1.403 37.327 -12.955 1.00171.64 C
ANISOU 353 CE1 TYR A 69 23196 20015 22003 2007 3063 1439 C
ATOM 354 CE2 TYR A 69 1.735 39.148 -14.451 1.00171.15 C
ANISOU 354 CE2 TYR A 69 22914 20284 21832 2411 2780 1623 C
ATOM 355 CZ TYR A 69 1.877 38.590 -13.206 1.00169.92 C
ANISOU 355 CZ TYR A 69 22997 19782 21784 2337 2964 1609 C
ATOM 356 OH TYR A 69 2.496 39.299 -12.208 1.00170.45 O
ANISOU 356 OH TYR A 69 23329 19488 21948 2583 3050 1768 O
ATOM 357 N ALA A 70 -1.671 38.640 -18.101 1.00172.51 N
ANISOU 357 N ALA A 70 21623 22200 21723 1960 2539 1551 N
ATOM 358 CA ALA A 70 -1.762 40.043 -18.491 1.00155.48 C
ANISOU 358 CA ALA A 70 19202 20267 19605 2331 2492 1814 C
ATOM 359 C ALA A 70 -2.358 40.158 -19.891 1.00172.98 C
ANISOU 359 C ALA A 70 20985 23045 21695 2280 2315 1845 C
ATOM 360 O ALA A 70 -2.281 39.224 -20.693 1.00186.75 O
ANISOU 360 O ALA A 70 22722 24930 23303 2004 2197 1662 O
ATOM 361 CB ALA A 70 -0.388 40.730 -18.456 1.00150.43 C
ANISOU 361 CB ALA A 70 18871 19294 18992 2638 2440 1916 C
ATOM 362 N CYS A 71 -2.947 41.320 -20.190 1.00178.13 N
ANISOU 362 N CYS A 71 21280 24014 22389 2547 2298 2082 N
ATOM 363 CA CYS A 71 -3.404 41.633 -21.546 1.00177.11 C
ANISOU 363 CA CYS A 71 20739 24410 22145 2558 2112 2157 C
ATOM 364 C CYS A 71 -2.280 42.309 -22.315 1.00181.97 C
ANISOU 364 C CYS A 71 21469 24967 22705 2819 1956 2246 C
ATOM 365 O CYS A 71 -1.860 43.418 -21.967 1.00190.26 O
ANISOU 365 O CYS A 71 22582 25866 23841 3176 1996 2444 O
ATOM 366 CB CYS A 71 -4.631 42.544 -21.572 1.00166.80 C
ANISOU 366 CB CYS A 71 18961 23507 20907 2717 2158 2379 C
ATOM 367 SG CYS A 71 -5.719 42.429 -20.198 1.00195.91 S
ANISOU 367 SG CYS A 71 22583 27107 24747 2637 2420 2391 S
ATOM 368 N TRP A 72 -1.796 41.662 -23.320 1.00182.91 N
ANISOU 368 N TRP A 72 21627 25194 22677 2641 1791 2103 N
ATOM 369 CA TRP A 72 -0.716 42.338 -24.002 1.00173.97 C
ANISOU 369 CA TRP A 72 20609 23995 21496 2896 1654 2190 C
ATOM 370 C TRP A 72 -1.304 43.012 -25.226 1.00183.60 C
ANISOU 370 C TRP A 72 21382 25753 22625 2979 1486 2337 C
ATOM 371 O TRP A 72 -1.969 42.340 -26.033 1.00188.59 O
ANISOU 371 O TRP A 72 21765 26752 23138 2690 1388 2233 O
ATOM 372 CB TRP A 72 0.367 41.347 -24.408 1.00158.82 C
ANISOU 372 CB TRP A 72 19036 21830 19476 2702 1571 1962 C
ATOM 373 CG TRP A 72 0.969 40.672 -23.225 1.00156.76 C
ANISOU 373 CG TRP A 72 19214 21041 19307 2623 1725 1828 C
ATOM 374 CD1 TRP A 72 0.632 39.452 -22.714 1.00178.59 C
ANISOU 374 CD1 TRP A 72 22118 23671 22067 2282 1818 1614 C
ATOM 375 CD2 TRP A 72 1.971 41.207 -22.360 1.00168.24 C
ANISOU 375 CD2 TRP A 72 21021 22033 20868 2885 1806 1914 C
ATOM 376 NE1 TRP A 72 1.389 39.180 -21.601 1.00187.47 N
ANISOU 376 NE1 TRP A 72 23665 24272 23294 2320 1945 1560 N
ATOM 377 CE2 TRP A 72 2.219 40.244 -21.362 1.00184.12 C
ANISOU 377 CE2 TRP A 72 23375 23643 22939 2684 1939 1745 C
ATOM 378 CE3 TRP A 72 2.697 42.400 -22.341 1.00180.66 C
ANISOU 378 CE3 TRP A 72 22663 23495 22483 3260 1775 2120 C
ATOM 379 CZ2 TRP A 72 3.159 40.440 -20.358 1.00194.97 C
ANISOU 379 CZ2 TRP A 72 25144 24520 24415 2843 2034 1782 C
ATOM 380 CZ3 TRP A 72 3.628 42.592 -21.346 1.00191.43 C
ANISOU 380 CZ3 TRP A 72 24425 24369 23943 3410 1875 2152 C
ATOM 381 CH2 TRP A 72 3.852 41.618 -20.370 1.00200.47 C
ANISOU 381 CH2 TRP A 72 25893 25130 25147 3201 2000 1988 C
ATOM 382 N PRO A 73 -1.079 44.310 -25.406 1.00177.04 N
ANISOU 382 N PRO A 73 20447 24983 21836 3354 1445 2577 N
ATOM 383 CA PRO A 73 -1.448 44.961 -26.665 1.00186.01 C
ANISOU 383 CA PRO A 73 21200 26604 22872 3446 1259 2717 C
ATOM 384 C PRO A 73 -0.495 44.591 -27.788 1.00199.72 C
ANISOU 384 C PRO A 73 23068 28368 24448 3354 1065 2596 C
ATOM 385 O PRO A 73 0.528 43.933 -27.591 1.00201.63 O
ANISOU 385 O PRO A 73 23702 28239 24667 3266 1079 2423 O
ATOM 386 CB PRO A 73 -1.370 46.452 -26.328 1.00179.43 C
ANISOU 386 CB PRO A 73 20300 25730 22146 3891 1305 3002 C
ATOM 387 CG PRO A 73 -0.370 46.542 -25.213 1.00173.65 C
ANISOU 387 CG PRO A 73 20040 24424 21513 4036 1450 2975 C
ATOM 388 CD PRO A 73 -0.280 45.191 -24.537 1.00172.25 C
ANISOU 388 CD PRO A 73 20131 23969 21349 3697 1551 2716 C
ATOM 389 N ASP A 74 -0.860 45.021 -28.993 1.00187.74 N
ANISOU 389 N ASP A 74 21209 27305 22819 3372 884 2693 N
ATOM 390 CA ASP A 74 0.061 44.910 -30.109 1.00189.58 C
ANISOU 390 CA ASP A 74 21548 27583 22902 3340 698 2618 C
ATOM 391 C ASP A 74 1.339 45.684 -29.800 1.00208.24 C
ANISOU 391 C ASP A 74 24244 29562 25317 3679 709 2705 C
ATOM 392 O ASP A 74 1.354 46.629 -29.006 1.00208.12 O
ANISOU 392 O ASP A 74 24267 29380 25430 3989 816 2892 O
ATOM 393 CB ASP A 74 -0.586 45.420 -31.396 1.00160.78 C
ANISOU 393 CB ASP A 74 17464 24493 19134 3338 503 2749 C
ATOM 394 CG ASP A 74 -1.848 44.659 -31.753 1.00150.68 C
ANISOU 394 CG ASP A 74 15841 23622 17788 2984 478 2674 C
ATOM 395 OD1 ASP A 74 -1.857 43.420 -31.598 1.00150.65 O
ANISOU 395 OD1 ASP A 74 16002 23505 17733 2634 527 2428 O
ATOM 396 OD2 ASP A 74 -2.832 45.297 -32.182 1.00154.00 O
ANISOU 396 OD2 ASP A 74 15828 24478 18205 3054 411 2865 O
ATOM 397 N GLY A 75 2.415 45.274 -30.445 1.00186.59 N
ANISOU 397 N GLY A 75 21746 26682 22467 3610 602 2567 N
ATOM 398 CA GLY A 75 3.715 45.897 -30.261 1.00205.30 C
ANISOU 398 CA GLY A 75 24440 28704 24862 3892 594 2628 C
ATOM 399 C GLY A 75 4.328 46.385 -31.557 1.00210.64 C
ANISOU 399 C GLY A 75 25043 29596 25393 3981 389 2673 C
ATOM 400 O GLY A 75 4.168 45.754 -32.603 1.00216.49 O
ANISOU 400 O GLY A 75 25649 30614 25992 3726 257 2543 O
ATOM 401 N GLU A 76 4.981 47.536 -31.492 1.00206.94 N
ANISOU 401 N GLU A 76 24658 29014 24954 4336 363 2862 N
ATOM 402 CA GLU A 76 5.809 47.943 -32.610 1.00199.76 C
ANISOU 402 CA GLU A 76 23773 28217 23910 4424 181 2881 C
ATOM 403 C GLU A 76 6.976 46.964 -32.713 1.00188.79 C
ANISOU 403 C GLU A 76 22759 26505 22467 4252 176 2639 C
ATOM 404 O GLU A 76 7.538 46.564 -31.688 1.00176.82 O
ANISOU 404 O GLU A 76 21569 24560 21055 4266 318 2565 O
ATOM 405 CB GLU A 76 6.330 49.364 -32.401 1.00201.95 C
ANISOU 405 CB GLU A 76 24108 28393 24230 4838 173 3129 C
ATOM 406 CG GLU A 76 7.350 49.824 -33.428 1.00201.41 C
ANISOU 406 CG GLU A 76 24126 28374 24027 4949 0 3146 C
ATOM 407 CD GLU A 76 8.038 51.112 -33.022 1.00208.14 C
ANISOU 407 CD GLU A 76 25133 29027 24924 5340 20 3363 C
ATOM 408 OE1 GLU A 76 9.173 51.042 -32.503 1.00209.99 O
ANISOU 408 OE1 GLU A 76 25742 28860 25185 5422 76 3311 O
ATOM 409 OE2 GLU A 76 7.441 52.193 -33.209 1.00213.25 O
ANISOU 409 OE2 GLU A 76 25529 29917 25578 5564 -16 3592 O
ATOM 410 N PRO A 77 7.347 46.536 -33.920 1.00189.36 N
ANISOU 410 N PRO A 77 22797 26770 22383 4083 21 2514 N
ATOM 411 CA PRO A 77 8.523 45.669 -34.051 1.00190.70 C
ANISOU 411 CA PRO A 77 23327 26622 22506 3953 24 2296 C
ATOM 412 C PRO A 77 9.766 46.327 -33.476 1.00191.34 C
ANISOU 412 C PRO A 77 23736 26309 22657 4259 64 2386 C
ATOM 413 O PRO A 77 10.021 47.515 -33.682 1.00222.66 O
ANISOU 413 O PRO A 77 27637 30353 26610 4549 -5 2590 O
ATOM 414 CB PRO A 77 8.645 45.462 -35.563 1.00194.27 C
ANISOU 414 CB PRO A 77 23631 27414 22769 3787 -163 2210 C
ATOM 415 CG PRO A 77 7.272 45.636 -36.064 1.00196.34 C
ANISOU 415 CG PRO A 77 23462 28158 22981 3668 -233 2296 C
ATOM 416 CD PRO A 77 6.640 46.695 -35.200 1.00190.87 C
ANISOU 416 CD PRO A 77 22615 27477 22429 3962 -154 2550 C
ATOM 417 N GLY A 78 10.542 45.530 -32.749 1.00196.71 N
ANISOU 417 N GLY A 78 24772 26562 23405 4184 176 2234 N
ATOM 418 CA GLY A 78 11.776 46.009 -32.165 1.00191.14 C
ANISOU 418 CA GLY A 78 24399 25465 22762 4434 216 2303 C
ATOM 419 C GLY A 78 11.576 47.019 -31.060 1.00194.62 C
ANISOU 419 C GLY A 78 24869 25747 23332 4717 322 2531 C
ATOM 420 O GLY A 78 12.403 47.922 -30.901 1.00193.28 O
ANISOU 420 O GLY A 78 24850 25419 23168 4990 302 2677 O
ATOM 421 N SER A 79 10.496 46.897 -30.290 1.00205.90 N
ANISOU 421 N SER A 79 26162 27214 24858 4652 442 2564 N
ATOM 422 CA SER A 79 10.264 47.793 -29.169 1.00215.66 C
ANISOU 422 CA SER A 79 27444 28275 26223 4901 570 2768 C
ATOM 423 C SER A 79 9.758 47.004 -27.970 1.00214.01 C
ANISOU 423 C SER A 79 27354 27819 26143 4736 753 2674 C
ATOM 424 O SER A 79 9.253 45.886 -28.098 1.00217.15 O
ANISOU 424 O SER A 79 27695 28287 26523 4432 771 2480 O
ATOM 425 CB SER A 79 9.262 48.899 -29.529 1.00212.25 C
ANISOU 425 CB SER A 79 26635 28231 25779 5079 525 2989 C
ATOM 426 OG SER A 79 7.955 48.372 -29.678 1.00211.78 O
ANISOU 426 OG SER A 79 26260 28480 25727 4860 545 2933 O
ATOM 427 N PHE A 80 9.897 47.617 -26.799 1.00203.43 N
ANISOU 427 N PHE A 80 26188 26184 24923 4934 891 2816 N
ATOM 428 CA PHE A 80 9.284 47.118 -25.577 1.00204.10 C
ANISOU 428 CA PHE A 80 26357 26055 25138 4818 1077 2774 C
ATOM 429 C PHE A 80 7.833 47.558 -25.433 1.00228.47 C
ANISOU 429 C PHE A 80 29079 29458 28272 4832 1140 2888 C
ATOM 430 O PHE A 80 7.467 48.693 -25.754 1.00239.94 O
ANISOU 430 O PHE A 80 30310 31143 29714 5073 1101 3096 O
ATOM 431 CB PHE A 80 10.102 47.520 -24.351 1.00200.26 C
ANISOU 431 CB PHE A 80 26243 25092 24754 4996 1204 2867 C
ATOM 432 CG PHE A 80 11.352 46.704 -24.179 1.00212.59 C
ANISOU 432 CG PHE A 80 28179 26289 26307 4897 1188 2713 C
ATOM 433 CD1 PHE A 80 11.297 45.477 -23.537 1.00216.53 C
ANISOU 433 CD1 PHE A 80 28855 26549 26867 4634 1283 2520 C
ATOM 434 CD2 PHE A 80 12.568 47.141 -24.673 1.00226.73 C
ANISOU 434 CD2 PHE A 80 30137 27981 28029 5062 1079 2762 C
ATOM 435 CE1 PHE A 80 12.431 44.706 -23.377 1.00219.53 C
ANISOU 435 CE1 PHE A 80 29572 26592 27249 4551 1272 2387 C
ATOM 436 CE2 PHE A 80 13.710 46.373 -24.516 1.00235.97 C
ANISOU 436 CE2 PHE A 80 31635 28822 29201 4977 1068 2627 C
ATOM 437 CZ PHE A 80 13.639 45.154 -23.867 1.00229.82 C
ANISOU 437 CZ PHE A 80 31027 27802 28492 4727 1166 2443 C
ATOM 438 N VAL A 81 7.013 46.635 -24.945 1.00229.87 N
ANISOU 438 N VAL A 81 29197 29640 28502 4571 1241 2751 N
ATOM 439 CA VAL A 81 5.599 46.843 -24.668 1.00221.55 C
ANISOU 439 CA VAL A 81 27813 28858 27509 4537 1327 2829 C
ATOM 440 C VAL A 81 5.434 46.736 -23.161 1.00231.99 C
ANISOU 440 C VAL A 81 29359 29808 28980 4540 1545 2842 C
ATOM 441 O VAL A 81 5.918 45.774 -22.546 1.00223.96 O
ANISOU 441 O VAL A 81 28645 28457 27993 4349 1613 2669 O
ATOM 442 CB VAL A 81 4.721 45.813 -25.397 1.00215.32 C
ANISOU 442 CB VAL A 81 26754 28415 26640 4192 1260 2651 C
ATOM 443 CG1 VAL A 81 3.270 45.936 -24.957 1.00195.49 C
ANISOU 443 CG1 VAL A 81 23921 26153 24206 4137 1369 2725 C
ATOM 444 CG2 VAL A 81 4.852 45.977 -26.899 1.00219.50 C
ANISOU 444 CG2 VAL A 81 27060 29325 27016 4182 1044 2651 C
ATOM 445 N ASN A 82 4.722 47.696 -22.569 1.00241.59 N
ANISOU 445 N ASN A 82 30424 31082 30287 4748 1661 3044 N
ATOM 446 CA ASN A 82 4.481 47.686 -21.137 1.00232.57 C
ANISOU 446 CA ASN A 82 29477 29607 29284 4754 1880 3069 C
ATOM 447 C ASN A 82 3.012 47.643 -20.776 1.00211.97 C
ANISOU 447 C ASN A 82 26545 27246 26749 4664 2001 3099 C
ATOM 448 O ASN A 82 2.171 48.257 -21.441 1.00208.12 O
ANISOU 448 O ASN A 82 25663 27174 26241 4765 1946 3228 O
ATOM 449 CB ASN A 82 4.932 49.014 -20.494 1.00242.26 C
ANISOU 449 CB ASN A 82 30859 30614 30575 5114 1967 3311 C
ATOM 450 CG ASN A 82 6.407 49.148 -20.301 1.00256.45 C
ANISOU 450 CG ASN A 82 33068 32030 32342 5222 1923 3312 C
ATOM 451 OD1 ASN A 82 6.832 49.686 -19.277 1.00257.92 O
ANISOU 451 OD1 ASN A 82 33528 31867 32603 5371 2056 3421 O
ATOM 452 ND2 ASN A 82 7.199 48.703 -21.265 1.00287.94 N
ANISOU 452 ND2 ASN A 82 37104 36081 36218 5151 1743 3201 N
ATOM 453 N VAL A 83 2.721 46.908 -19.709 1.00212.27 N
ANISOU 453 N VAL A 83 26755 27025 26873 4470 2166 2983 N
ATOM 454 CA VAL A 83 1.408 46.917 -19.090 1.00192.20 C
ANISOU 454 CA VAL A 83 23971 24632 24424 4400 2325 3019 C
ATOM 455 C VAL A 83 1.703 46.938 -17.599 1.00183.47 C
ANISOU 455 C VAL A 83 23233 23038 23440 4426 2536 3028 C
ATOM 456 O VAL A 83 2.724 46.403 -17.159 1.00159.06 O
ANISOU 456 O VAL A 83 20539 19553 20342 4347 2536 2919 O
ATOM 457 CB VAL A 83 0.539 45.706 -19.509 1.00184.10 C
ANISOU 457 CB VAL A 83 22719 23885 23346 4024 2286 2813 C
ATOM 458 CG1 VAL A 83 1.346 44.427 -19.453 1.00177.38 C
ANISOU 458 CG1 VAL A 83 22209 22751 22437 3742 2243 2558 C
ATOM 459 CG2 VAL A 83 -0.715 45.597 -18.650 1.00190.35 C
ANISOU 459 CG2 VAL A 83 23330 24750 24244 3923 2478 2828 C
ATOM 460 N SER A 84 0.849 47.583 -16.816 1.00195.31 N
ANISOU 460 N SER A 84 24607 24550 25050 4544 2719 3168 N
ATOM 461 CA SER A 84 1.017 47.478 -15.375 1.00169.83 C
ANISOU 461 CA SER A 84 21724 20871 21932 4513 2931 3154 C
ATOM 462 C SER A 84 0.935 46.010 -14.970 1.00166.29 C
ANISOU 462 C SER A 84 21436 20269 21479 4124 2959 2891 C
ATOM 463 O SER A 84 0.248 45.215 -15.620 1.00172.17 O
ANISOU 463 O SER A 84 21920 21331 22165 3883 2882 2751 O
ATOM 464 CB SER A 84 -0.035 48.306 -14.637 1.00151.76 C
ANISOU 464 CB SER A 84 19243 18655 19762 4666 3139 3324 C
ATOM 465 OG SER A 84 0.199 49.694 -14.806 1.00162.08 O
ANISOU 465 OG SER A 84 20504 19997 21083 5042 3145 3573 O
ATOM 466 N CYS A 85 1.672 45.625 -13.931 1.00153.34 N
ANISOU 466 N CYS A 85 20234 18141 19888 4051 3059 2823 N
ATOM 467 CA CYS A 85 1.417 44.318 -13.341 1.00142.18 C
ANISOU 467 CA CYS A 85 18969 16562 18491 3693 3128 2595 C
ATOM 468 C CYS A 85 -0.082 44.199 -13.086 1.00136.77 C
ANISOU 468 C CYS A 85 17941 16166 17860 3563 3259 2585 C
ATOM 469 O CYS A 85 -0.687 45.126 -12.528 1.00150.50 O
ANISOU 469 O CYS A 85 19558 17935 19691 3757 3410 2760 O
ATOM 470 CB CYS A 85 2.238 44.043 -12.081 1.00154.79 C
ANISOU 470 CB CYS A 85 21062 17595 20155 3644 3250 2559 C
ATOM 471 SG CYS A 85 4.017 44.021 -12.402 1.00183.50 S
ANISOU 471 SG CYS A 85 25090 20905 23725 3759 3086 2556 S
ATOM 472 N PRO A 86 -0.712 43.102 -13.492 1.00148.40 N
ANISOU 472 N PRO A 86 19250 17859 19275 3241 3210 2388 N
ATOM 473 CA PRO A 86 -2.166 42.979 -13.349 1.00155.34 C
ANISOU 473 CA PRO A 86 19765 19063 20193 3106 3318 2382 C
ATOM 474 C PRO A 86 -2.648 43.194 -11.924 1.00157.10 C
ANISOU 474 C PRO A 86 20128 19011 20551 3107 3573 2427 C
ATOM 475 O PRO A 86 -2.139 42.612 -10.965 1.00160.03 O
ANISOU 475 O PRO A 86 20897 18949 20959 2961 3667 2318 O
ATOM 476 CB PRO A 86 -2.441 41.550 -13.829 1.00167.93 C
ANISOU 476 CB PRO A 86 21322 20797 21688 2704 3228 2121 C
ATOM 477 CG PRO A 86 -1.141 40.830 -13.647 1.00163.31 C
ANISOU 477 CG PRO A 86 21205 19781 21063 2609 3164 1976 C
ATOM 478 CD PRO A 86 -0.091 41.849 -13.950 1.00158.81 C
ANISOU 478 CD PRO A 86 20761 19085 20496 2963 3079 2153 C
ATOM 479 N TRP A 87 -3.646 44.074 -11.818 1.00164.70 N
ANISOU 479 N TRP A 87 20752 20239 21589 3281 3685 2601 N
ATOM 480 CA TRP A 87 -4.227 44.602 -10.593 1.00169.70 C
ANISOU 480 CA TRP A 87 21436 20684 22357 3362 3942 2700 C
ATOM 481 C TRP A 87 -4.995 43.568 -9.788 1.00183.06 C
ANISOU 481 C TRP A 87 23166 22304 24084 3006 4087 2513 C
ATOM 482 O TRP A 87 -5.380 43.870 -8.653 1.00198.38 O
ANISOU 482 O TRP A 87 25220 24022 26135 3030 4313 2564 O
ATOM 483 CB TRP A 87 -5.116 45.809 -10.908 1.00140.66 C
ANISOU 483 CB TRP A 87 17332 17370 18743 3657 4005 2938 C
ATOM 484 CG TRP A 87 -6.238 45.550 -11.871 1.00143.98 C
ANISOU 484 CG TRP A 87 17223 18367 19117 3546 3911 2922 C
ATOM 485 CD1 TRP A 87 -6.267 45.886 -13.194 1.00208.60 C
ANISOU 485 CD1 TRP A 87 25085 26961 27214 3662 3700 3002 C
ATOM 486 CD2 TRP A 87 -7.484 44.898 -11.597 1.00146.99 C
ANISOU 486 CD2 TRP A 87 17335 18986 19527 3281 4016 2824 C
ATOM 487 NE1 TRP A 87 -7.457 45.497 -13.757 1.00210.25 N
ANISOU 487 NE1 TRP A 87 24839 27652 27396 3487 3665 2969 N
ATOM 488 CE2 TRP A 87 -8.220 44.883 -12.799 1.00149.58 C
ANISOU 488 CE2 TRP A 87 17174 19878 19782 3251 3857 2860 C
ATOM 489 CE3 TRP A 87 -8.051 44.328 -10.453 1.00169.50 C
ANISOU 489 CE3 TRP A 87 20312 21636 22455 3057 4229 2713 C
ATOM 490 CZ2 TRP A 87 -9.489 44.319 -12.890 1.00152.95 C
ANISOU 490 CZ2 TRP A 87 17231 20675 20207 3005 3902 2792 C
ATOM 491 CZ3 TRP A 87 -9.310 43.768 -10.546 1.00172.02 C
ANISOU 491 CZ3 TRP A 87 20266 22319 22773 2817 4277 2637 C
ATOM 492 CH2 TRP A 87 -10.016 43.768 -11.755 1.00187.56 C
ANISOU 492 CH2 TRP A 87 21745 24854 24667 2793 4114 2680 C
ATOM 493 N TYR A 88 -5.211 42.360 -10.310 1.00198.92 N
ANISOU 493 N TYR A 88 25107 24477 25996 2668 3971 2296 N
ATOM 494 CA TYR A 88 -5.937 41.429 -9.465 1.00174.48 C
ANISOU 494 CA TYR A 88 22073 21291 22933 2333 4122 2125 C
ATOM 495 C TYR A 88 -5.012 40.774 -8.457 1.00162.14 C
ANISOU 495 C TYR A 88 21064 19154 21389 2186 4189 1992 C
ATOM 496 O TYR A 88 -5.488 40.011 -7.611 1.00145.46 O
ANISOU 496 O TYR A 88 19078 16886 19305 1909 4326 1849 O
ATOM 497 CB TYR A 88 -6.605 40.330 -10.304 1.00148.52 C
ANISOU 497 CB TYR A 88 18520 18384 19527 1991 3996 1935 C
ATOM 498 CG TYR A 88 -5.627 39.471 -11.092 1.00151.09 C
ANISOU 498 CG TYR A 88 19062 18628 19719 1839 3784 1768 C
ATOM 499 CD1 TYR A 88 -4.952 38.411 -10.486 1.00153.18 C
ANISOU 499 CD1 TYR A 88 19768 18474 19959 1586 3804 1563 C
ATOM 500 CD2 TYR A 88 -5.372 39.720 -12.432 1.00153.13 C
ANISOU 500 CD2 TYR A 88 19088 19217 19877 1949 3570 1818 C
ATOM 501 CE1 TYR A 88 -4.057 37.627 -11.193 1.00154.97 C
ANISOU 501 CE1 TYR A 88 20195 18614 20074 1460 3627 1414 C
ATOM 502 CE2 TYR A 88 -4.476 38.937 -13.148 1.00142.96 C
ANISOU 502 CE2 TYR A 88 18003 17845 18469 1810 3393 1661 C
ATOM 503 CZ TYR A 88 -3.821 37.895 -12.524 1.00157.76 C
ANISOU 503 CZ TYR A 88 20313 19300 20329 1573 3427 1461 C
ATOM 504 OH TYR A 88 -2.931 37.118 -13.231 1.00165.63 O
ANISOU 504 OH TYR A 88 21513 20205 21216 1448 3266 1309 O
ATOM 505 N LEU A 89 -3.704 40.998 -8.566 1.00167.96 N
ANISOU 505 N LEU A 89 22128 19588 22101 2345 4086 2030 N
ATOM 506 CA LEU A 89 -2.808 40.416 -7.585 1.00158.22 C
ANISOU 506 CA LEU A 89 21415 17810 20893 2217 4145 1926 C
ATOM 507 C LEU A 89 -3.202 41.010 -6.238 1.00171.36 C
ANISOU 507 C LEU A 89 23213 19211 22684 2288 4399 2032 C
ATOM 508 O LEU A 89 -3.476 42.212 -6.159 1.00176.31 O
ANISOU 508 O LEU A 89 23676 19937 23377 2586 4484 2246 O
ATOM 509 CB LEU A 89 -1.343 40.727 -7.889 1.00150.42 C
ANISOU 509 CB LEU A 89 20730 16555 19870 2417 4003 1989 C
ATOM 510 CG LEU A 89 -0.833 40.128 -9.199 1.00132.00 C
ANISOU 510 CG LEU A 89 18309 14435 17410 2349 3761 1878 C
ATOM 511 CD1 LEU A 89 0.558 40.614 -9.584 1.00129.11 C
ANISOU 511 CD1 LEU A 89 18181 13861 17013 2592 3624 1971 C
ATOM 512 CD2 LEU A 89 -0.899 38.625 -9.146 1.00132.80 C
ANISOU 512 CD2 LEU A 89 18556 14451 17451 1953 3733 1609 C
ATOM 513 N PRO A 90 -3.256 40.225 -5.169 1.00167.93 N
ANISOU 513 N PRO A 90 23079 18442 22286 2022 4529 1891 N
ATOM 514 CA PRO A 90 -3.576 40.830 -3.864 1.00188.74 C
ANISOU 514 CA PRO A 90 25871 20803 25038 2087 4778 1995 C
ATOM 515 C PRO A 90 -2.670 41.987 -3.457 1.00207.90 C
ANISOU 515 C PRO A 90 28545 22933 27515 2423 4817 2212 C
ATOM 516 O PRO A 90 -3.133 42.917 -2.785 1.00238.10 O
ANISOU 516 O PRO A 90 32329 26708 31428 2595 5011 2370 O
ATOM 517 CB PRO A 90 -3.449 39.645 -2.905 1.00175.74 C
ANISOU 517 CB PRO A 90 24591 18789 23393 1724 4854 1787 C
ATOM 518 CG PRO A 90 -3.829 38.468 -3.742 1.00168.04 C
ANISOU 518 CG PRO A 90 23433 18098 22316 1435 4711 1572 C
ATOM 519 CD PRO A 90 -3.281 38.751 -5.119 1.00149.60 C
ANISOU 519 CD PRO A 90 20906 16038 19897 1627 4479 1628 C
ATOM 520 N TRP A 91 -1.399 41.962 -3.855 1.00184.63 N
ANISOU 520 N TRP A 91 25851 19791 24509 2519 4645 2226 N
ATOM 521 CA TRP A 91 -0.402 42.961 -3.487 1.00190.11 C
ANISOU 521 CA TRP A 91 26822 20182 25227 2806 4660 2419 C
ATOM 522 C TRP A 91 -0.007 43.896 -4.626 1.00210.19 C
ANISOU 522 C TRP A 91 29139 23002 27721 3136 4503 2582 C
ATOM 523 O TRP A 91 1.043 44.545 -4.545 1.00202.61 O
ANISOU 523 O TRP A 91 28433 21802 26747 3345 4454 2712 O
ATOM 524 CB TRP A 91 0.822 42.215 -2.960 1.00186.84 C
ANISOU 524 CB TRP A 91 26904 19299 24788 2654 4590 2321 C
ATOM 525 CG TRP A 91 1.128 41.150 -3.959 1.00194.00 C
ANISOU 525 CG TRP A 91 27738 20372 25603 2483 4375 2134 C
ATOM 526 CD1 TRP A 91 1.905 41.234 -5.075 1.00193.24 C
ANISOU 526 CD1 TRP A 91 27579 20418 25427 2625 4160 2153 C
ATOM 527 CD2 TRP A 91 0.616 39.810 -3.924 1.00190.61 C
ANISOU 527 CD2 TRP A 91 27298 19982 25145 2118 4369 1892 C
ATOM 528 NE1 TRP A 91 1.888 40.031 -5.746 1.00194.81 N
ANISOU 528 NE1 TRP A 91 27723 20744 25552 2372 4028 1936 N
ATOM 529 CE2 TRP A 91 1.110 39.141 -5.051 1.00192.12 C
ANISOU 529 CE2 TRP A 91 27420 20338 25238 2059 4152 1774 C
ATOM 530 CE3 TRP A 91 -0.215 39.114 -3.040 1.00193.56 C
ANISOU 530 CE3 TRP A 91 27723 20262 25561 1829 4532 1760 C
ATOM 531 CZ2 TRP A 91 0.797 37.807 -5.322 1.00192.68 C
ANISOU 531 CZ2 TRP A 91 27481 20479 25249 1721 4099 1532 C
ATOM 532 CZ3 TRP A 91 -0.517 37.790 -3.309 1.00191.73 C
ANISOU 532 CZ3 TRP A 91 27479 20104 25267 1494 4469 1520 C
ATOM 533 CH2 TRP A 91 -0.009 37.151 -4.438 1.00189.19 C
ANISOU 533 CH2 TRP A 91 27098 19941 24845 1443 4256 1410 C
ATOM 534 N ALA A 92 -0.796 43.943 -5.706 1.00234.10 N
ANISOU 534 N ALA A 92 31703 26533 30712 3171 4411 2574 N
ATOM 535 CA ALA A 92 -0.433 44.783 -6.846 1.00244.63 C
ANISOU 535 CA ALA A 92 32817 28143 31988 3467 4247 2721 C
ATOM 536 C ALA A 92 -0.199 46.228 -6.413 1.00247.32 C
ANISOU 536 C ALA A 92 33231 28354 32386 3820 4363 2978 C
ATOM 537 O ALA A 92 0.663 46.923 -6.960 1.00240.61 O
ANISOU 537 O ALA A 92 32451 27486 31485 4063 4239 3104 O
ATOM 538 CB ALA A 92 -1.512 44.709 -7.926 1.00248.35 C
ANISOU 538 CB ALA A 92 32753 29185 32422 3444 4165 2699 C
ATOM 539 N SER A 93 -0.950 46.674 -5.402 1.00248.35 N
ANISOU 539 N SER A 93 33368 28378 32618 3841 4610 3054 N
ATOM 540 CA SER A 93 -0.880 48.022 -4.842 1.00239.36 C
ANISOU 540 CA SER A 93 32315 27092 31540 4150 4771 3292 C
ATOM 541 C SER A 93 0.428 48.324 -4.127 1.00246.40 C
ANISOU 541 C SER A 93 33724 27484 32414 4219 4781 3358 C
ATOM 542 O SER A 93 0.741 49.499 -3.911 1.00249.17 O
ANISOU 542 O SER A 93 34169 27728 32778 4501 4859 3566 O
ATOM 543 CB SER A 93 -2.042 48.269 -3.880 1.00233.90 C
ANISOU 543 CB SER A 93 31519 26389 30961 4108 5053 3326 C
ATOM 544 OG SER A 93 -3.255 48.469 -4.582 1.00227.22 O
ANISOU 544 OG SER A 93 30147 26044 30144 4169 5063 3359 O
ATOM 545 N SER A 94 1.179 47.311 -3.705 1.00275.03 N
ANISOU 545 N SER A 94 37695 30793 36011 3965 4716 3197 N
ATOM 546 CA SER A 94 2.464 47.635 -3.101 1.00274.79 C
ANISOU 546 CA SER A 94 38133 30316 35958 4041 4704 3282 C
ATOM 547 C SER A 94 3.570 47.913 -4.107 1.00264.22 C
ANISOU 547 C SER A 94 36825 29043 34523 4222 4463 3341 C
ATOM 548 O SER A 94 4.589 48.493 -3.726 1.00261.97 O
ANISOU 548 O SER A 94 36869 28455 34214 4359 4455 3467 O
ATOM 549 CB SER A 94 2.907 46.509 -2.165 1.00279.77 C
ANISOU 549 CB SER A 94 39150 30546 36603 3716 4735 3112 C
ATOM 550 OG SER A 94 3.078 45.291 -2.865 1.00284.10 O
ANISOU 550 OG SER A 94 39630 31217 37099 3497 4550 2903 O
ATOM 551 N VAL A 95 3.412 47.531 -5.368 1.00248.66 N
ANISOU 551 N VAL A 95 34532 27456 32491 4220 4270 3258 N
ATOM 552 CA VAL A 95 4.459 47.799 -6.349 1.00219.86 C
ANISOU 552 CA VAL A 95 30911 23877 28750 4387 4045 3309 C
ATOM 553 C VAL A 95 3.853 48.564 -7.528 1.00218.63 C
ANISOU 553 C VAL A 95 30301 24212 28558 4618 3959 3414 C
ATOM 554 O VAL A 95 4.049 48.160 -8.684 1.00220.94 O
ANISOU 554 O VAL A 95 30398 24779 28771 4595 3752 3332 O
ATOM 555 CB VAL A 95 5.166 46.492 -6.745 1.00189.76 C
ANISOU 555 CB VAL A 95 27241 19979 24881 4142 3868 3094 C
ATOM 556 CG1 VAL A 95 4.203 45.521 -7.437 1.00181.96 C
ANISOU 556 CG1 VAL A 95 25907 19350 23877 3914 3811 2899 C
ATOM 557 CG2 VAL A 95 6.455 46.741 -7.547 1.00174.45 C
ANISOU 557 CG2 VAL A 95 25424 18007 22852 4304 3658 3148 C
ATOM 558 N PRO A 96 3.096 49.662 -7.309 1.00204.59 N
ANISOU 558 N PRO A 96 28337 22565 26835 4840 4113 3597 N
ATOM 559 CA PRO A 96 2.397 50.279 -8.453 1.00194.51 C
ANISOU 559 CA PRO A 96 26590 21785 25531 5034 4026 3690 C
ATOM 560 C PRO A 96 3.367 50.793 -9.491 1.00180.92 C
ANISOU 560 C PRO A 96 24873 20165 23703 5241 3806 3774 C
ATOM 561 O PRO A 96 3.004 50.935 -10.663 1.00185.34 O
ANISOU 561 O PRO A 96 25068 21144 24209 5322 3657 3788 O
ATOM 562 CB PRO A 96 1.607 51.428 -7.818 1.00197.82 C
ANISOU 562 CB PRO A 96 26907 22216 26038 5259 4259 3892 C
ATOM 563 CG PRO A 96 2.389 51.774 -6.633 1.00200.61 C
ANISOU 563 CG PRO A 96 27744 22061 26416 5285 4402 3961 C
ATOM 564 CD PRO A 96 2.887 50.461 -6.090 1.00201.82 C
ANISOU 564 CD PRO A 96 28191 21925 26565 4945 4366 3744 C
ATOM 565 N GLN A 97 4.597 51.106 -9.075 1.00167.38 N
ANISOU 565 N GLN A 97 23566 18078 21952 5326 3783 3839 N
ATOM 566 CA GLN A 97 5.604 51.581 -10.008 1.00174.28 C
ANISOU 566 CA GLN A 97 24477 19023 22720 5512 3578 3914 C
ATOM 567 C GLN A 97 6.127 50.459 -10.888 1.00174.92 C
ANISOU 567 C GLN A 97 24525 19212 22726 5313 3354 3711 C
ATOM 568 O GLN A 97 6.732 50.739 -11.931 1.00183.59 O
ANISOU 568 O GLN A 97 25539 20486 23730 5443 3164 3745 O
ATOM 569 CB GLN A 97 6.763 52.244 -9.242 1.00179.49 C
ANISOU 569 CB GLN A 97 25589 19249 23360 5646 3628 4049 C
ATOM 570 CG GLN A 97 7.977 52.697 -10.082 1.00178.02 C
ANISOU 570 CG GLN A 97 25509 19074 23058 5820 3420 4124 C
ATOM 571 CD GLN A 97 9.060 51.626 -10.222 1.00170.72 C
ANISOU 571 CD GLN A 97 24831 17950 22086 5620 3263 3955 C
ATOM 572 OE1 GLN A 97 9.883 51.444 -9.326 1.00180.63 O
ANISOU 572 OE1 GLN A 97 26483 18795 23355 5548 3315 3961 O
ATOM 573 NE2 GLN A 97 9.070 50.930 -11.355 1.00175.78 N
ANISOU 573 NE2 GLN A 97 25241 18878 22670 5530 3074 3811 N
ATOM 574 N GLY A 98 5.864 49.200 -10.542 1.00165.52 N
ANISOU 574 N GLY A 98 23387 17936 21568 4999 3376 3499 N
ATOM 575 CA GLY A 98 6.326 48.129 -11.384 1.00164.86 C
ANISOU 575 CA GLY A 98 23279 17949 21411 4809 3182 3304 C
ATOM 576 C GLY A 98 5.444 47.938 -12.601 1.00156.81 C
ANISOU 576 C GLY A 98 21791 17449 20341 4773 3065 3243 C
ATOM 577 O GLY A 98 4.262 48.276 -12.617 1.00165.35 O
ANISOU 577 O GLY A 98 22551 18806 21467 4801 3157 3300 O
ATOM 578 N HIS A 99 6.053 47.375 -13.636 1.00166.09 N
ANISOU 578 N HIS A 99 22933 18755 21419 4702 2861 3129 N
ATOM 579 CA HIS A 99 5.383 47.055 -14.881 1.00154.50 C
ANISOU 579 CA HIS A 99 21061 17762 19878 4624 2721 3049 C
ATOM 580 C HIS A 99 5.845 45.696 -15.368 1.00146.38 C
ANISOU 580 C HIS A 99 20136 16698 18784 4338 2598 2801 C
ATOM 581 O HIS A 99 6.955 45.260 -15.051 1.00134.67 O
ANISOU 581 O HIS A 99 19015 14859 17293 4296 2567 2734 O
ATOM 582 CB HIS A 99 5.683 48.095 -15.968 1.00146.79 C
ANISOU 582 CB HIS A 99 19886 17067 18820 4907 2570 3212 C
ATOM 583 CG HIS A 99 5.130 49.454 -15.677 1.00182.12 C
ANISOU 583 CG HIS A 99 24210 21639 23347 5201 2680 3460 C
ATOM 584 ND1 HIS A 99 4.003 49.654 -14.910 1.00185.20 N
ANISOU 584 ND1 HIS A 99 24453 22072 23842 5187 2874 3514 N
ATOM 585 CD2 HIS A 99 5.565 50.685 -16.036 1.00183.89 C
ANISOU 585 CD2 HIS A 99 24421 21913 23534 5519 2631 3668 C
ATOM 586 CE1 HIS A 99 3.762 50.950 -14.816 1.00190.29 C
ANISOU 586 CE1 HIS A 99 24998 22786 24516 5492 2947 3748 C
ATOM 587 NE2 HIS A 99 4.696 51.597 -15.490 1.00194.60 N
ANISOU 587 NE2 HIS A 99 25629 23336 24975 5696 2800 3845 N
ATOM 588 N VAL A 100 5.001 45.015 -16.128 1.00160.68 N
ANISOU 588 N VAL A 100 21634 18872 20545 4134 2532 2667 N
ATOM 589 CA VAL A 100 5.494 43.819 -16.783 1.00168.42 C
ANISOU 589 CA VAL A 100 22703 19849 21441 3886 2403 2441 C
ATOM 590 C VAL A 100 5.581 44.189 -18.258 1.00185.03 C
ANISOU 590 C VAL A 100 24523 22354 23425 3986 2204 2476 C
ATOM 591 O VAL A 100 4.805 45.010 -18.770 1.00196.06 O
ANISOU 591 O VAL A 100 25565 24120 24810 4131 2179 2619 O
ATOM 592 CB VAL A 100 4.588 42.594 -16.522 1.00142.70 C
ANISOU 592 CB VAL A 100 19370 16656 18193 3523 2475 2231 C
ATOM 593 CG1 VAL A 100 3.143 42.911 -16.842 1.00140.98 C
ANISOU 593 CG1 VAL A 100 18697 16891 17978 3496 2510 2289 C
ATOM 594 CG2 VAL A 100 5.057 41.396 -17.314 1.00136.03 C
ANISOU 594 CG2 VAL A 100 18604 15837 17246 3272 2342 2000 C
ATOM 595 N TYR A 101 6.533 43.566 -18.943 1.00191.74 N
ANISOU 595 N TYR A 101 25533 23130 24190 3904 2067 2344 N
ATOM 596 CA TYR A 101 6.889 43.926 -20.306 1.00193.40 C
ANISOU 596 CA TYR A 101 25556 23646 24280 4007 1874 2374 C
ATOM 597 C TYR A 101 7.012 42.703 -21.200 1.00184.37 C
ANISOU 597 C TYR A 101 24393 22629 23032 3714 1761 2132 C
ATOM 598 O TYR A 101 7.408 41.620 -20.760 1.00175.45 O
ANISOU 598 O TYR A 101 23533 21211 21918 3497 1809 1948 O
ATOM 599 CB TYR A 101 8.143 44.820 -20.396 1.00207.23 C
ANISOU 599 CB TYR A 101 27526 25196 26018 4305 1806 2521 C
ATOM 600 CG TYR A 101 9.405 44.360 -19.723 1.00216.43 C
ANISOU 600 CG TYR A 101 29142 25874 27218 4293 1835 2456 C
ATOM 601 CD1 TYR A 101 9.606 44.563 -18.366 1.00197.16 C
ANISOU 601 CD1 TYR A 101 26977 23045 24889 4351 1992 2534 C
ATOM 602 CD2 TYR A 101 10.427 43.783 -20.460 1.00242.25 C
ANISOU 602 CD2 TYR A 101 32562 29076 30408 4235 1703 2332 C
ATOM 603 CE1 TYR A 101 10.779 44.171 -17.756 1.00214.48 C
ANISOU 603 CE1 TYR A 101 29575 24803 27114 4341 2007 2494 C
ATOM 604 CE2 TYR A 101 11.606 43.408 -19.865 1.00247.93 C
ANISOU 604 CE2 TYR A 101 33676 29361 31166 4244 1724 2293 C
ATOM 605 CZ TYR A 101 11.779 43.599 -18.514 1.00236.81 C
ANISOU 605 CZ TYR A 101 32528 27580 29868 4295 1870 2378 C
ATOM 606 OH TYR A 101 12.946 43.186 -17.917 1.00236.18 O
ANISOU 606 OH TYR A 101 32835 27077 29827 4290 1882 2347 O
ATOM 607 N ARG A 102 6.657 42.896 -22.461 1.00197.52 N
ANISOU 607 N ARG A 102 25739 24724 24584 3707 1613 2138 N
ATOM 608 CA ARG A 102 6.992 41.949 -23.513 1.00210.27 C
ANISOU 608 CA ARG A 102 27352 26467 26073 3480 1482 1936 C
ATOM 609 C ARG A 102 7.784 42.681 -24.586 1.00222.62 C
ANISOU 609 C ARG A 102 28865 28180 27542 3690 1313 2028 C
ATOM 610 O ARG A 102 7.852 43.910 -24.619 1.00231.44 O
ANISOU 610 O ARG A 102 29880 29379 28678 3988 1287 2248 O
ATOM 611 CB ARG A 102 5.761 41.263 -24.128 1.00204.22 C
ANISOU 611 CB ARG A 102 26255 26109 25231 3183 1454 1815 C
ATOM 612 CG ARG A 102 5.153 40.142 -23.294 1.00192.75 C
ANISOU 612 CG ARG A 102 24907 24501 23830 2876 1596 1640 C
ATOM 613 CD ARG A 102 4.169 39.328 -24.133 1.00193.25 C
ANISOU 613 CD ARG A 102 24683 24969 23775 2545 1534 1489 C
ATOM 614 NE ARG A 102 3.573 38.218 -23.393 1.00203.96 N
ANISOU 614 NE ARG A 102 26141 26192 25160 2229 1664 1310 N
ATOM 615 CZ ARG A 102 3.172 37.079 -23.950 1.00208.81 C
ANISOU 615 CZ ARG A 102 26714 26962 25661 1870 1631 1094 C
ATOM 616 NH1 ARG A 102 3.301 36.895 -25.257 1.00199.49 N
ANISOU 616 NH1 ARG A 102 25391 26076 24331 1777 1475 1031 N
ATOM 617 NH2 ARG A 102 2.640 36.122 -23.201 1.00218.06 N
ANISOU 617 NH2 ARG A 102 27998 27993 26862 1593 1758 941 N
ATOM 618 N PHE A 103 8.391 41.893 -25.464 1.00211.05 N
ANISOU 618 N PHE A 103 27482 26737 25969 3525 1206 1851 N
ATOM 619 CA PHE A 103 9.065 42.391 -26.652 1.00197.93 C
ANISOU 619 CA PHE A 103 25749 25263 24193 3656 1035 1894 C
ATOM 620 C PHE A 103 8.351 41.820 -27.859 1.00191.91 C
ANISOU 620 C PHE A 103 24694 24934 23290 3399 922 1766 C
ATOM 621 O PHE A 103 8.194 40.600 -27.982 1.00191.96 O
ANISOU 621 O PHE A 103 24777 24907 23254 3084 948 1543 O
ATOM 622 CB PHE A 103 10.538 41.978 -26.650 1.00181.88 C
ANISOU 622 CB PHE A 103 24099 22855 22153 3693 1012 1798 C
ATOM 623 CG PHE A 103 11.338 42.581 -27.761 1.00179.15 C
ANISOU 623 CG PHE A 103 23712 22659 21698 3855 851 1855 C
ATOM 624 CD1 PHE A 103 11.661 43.925 -27.745 1.00177.65 C
ANISOU 624 CD1 PHE A 103 23475 22504 21520 4186 806 2091 C
ATOM 625 CD2 PHE A 103 11.781 41.801 -28.816 1.00201.39 C
ANISOU 625 CD2 PHE A 103 26552 25573 24395 3669 751 1668 C
ATOM 626 CE1 PHE A 103 12.401 44.485 -28.766 1.00201.67 C
ANISOU 626 CE1 PHE A 103 26486 25684 24454 4327 656 2141 C
ATOM 627 CE2 PHE A 103 12.523 42.354 -29.840 1.00205.41 C
ANISOU 627 CE2 PHE A 103 27028 26218 24800 3809 607 1715 C
ATOM 628 CZ PHE A 103 12.834 43.698 -29.813 1.00210.19 C
ANISOU 628 CZ PHE A 103 27581 26865 25418 4137 555 1952 C
ATOM 629 N CYS A 104 7.921 42.712 -28.742 1.00184.53 N
ANISOU 629 N CYS A 104 23432 24401 22278 3528 797 1914 N
ATOM 630 CA CYS A 104 7.307 42.322 -29.997 1.00191.56 C
ANISOU 630 CA CYS A 104 24032 25734 23019 3302 664 1825 C
ATOM 631 C CYS A 104 8.509 42.248 -30.945 1.00179.51 C
ANISOU 631 C CYS A 104 22675 24149 21383 3337 536 1748 C
ATOM 632 O CYS A 104 9.125 43.279 -31.235 1.00176.76 O
ANISOU 632 O CYS A 104 22328 23810 21024 3625 457 1912 O
ATOM 633 CB CYS A 104 6.349 43.424 -30.441 1.00217.75 C
ANISOU 633 CB CYS A 104 26928 29490 26317 3462 587 2051 C
ATOM 634 SG CYS A 104 5.302 43.121 -31.845 1.00230.51 S
ANISOU 634 SG CYS A 104 28108 31714 27763 3191 426 2003 S
ATOM 635 N THR A 105 8.860 41.055 -31.427 1.00181.10 N
ANISOU 635 N THR A 105 23028 24283 21501 3050 522 1503 N
ATOM 636 CA THR A 105 10.059 40.927 -32.260 1.00192.72 C
ANISOU 636 CA THR A 105 24686 25659 22879 3083 424 1418 C
ATOM 637 C THR A 105 9.903 41.551 -33.645 1.00206.25 C
ANISOU 637 C THR A 105 26114 27814 24439 3110 239 1489 C
ATOM 638 O THR A 105 8.808 41.882 -34.109 1.00221.74 O
ANISOU 638 O THR A 105 27717 30191 26345 3041 172 1573 O
ATOM 639 CB THR A 105 10.466 39.467 -32.446 1.00188.77 C
ANISOU 639 CB THR A 105 24429 24966 22328 2767 471 1131 C
ATOM 640 OG1 THR A 105 9.547 38.813 -33.331 1.00191.18 O
ANISOU 640 OG1 THR A 105 24492 25652 22494 2438 411 1003 O
ATOM 641 CG2 THR A 105 10.528 38.759 -31.140 1.00188.18 C
ANISOU 641 CG2 THR A 105 24623 24484 22394 2701 645 1050 C
ATOM 642 N ALA A 106 11.062 41.710 -34.299 1.00195.69 N
ANISOU 642 N ALA A 106 24948 26373 23035 3215 155 1459 N
ATOM 643 CA ALA A 106 11.170 42.390 -35.584 1.00201.48 C
ANISOU 643 CA ALA A 106 25471 27459 23621 3278 -24 1533 C
ATOM 644 C ALA A 106 10.511 41.603 -36.705 1.00219.85 C
ANISOU 644 C ALA A 106 27600 30149 25785 2920 -111 1370 C
ATOM 645 O ALA A 106 10.261 42.161 -37.778 1.00214.10 O
ANISOU 645 O ALA A 106 26622 29798 24927 2924 -266 1447 O
ATOM 646 CB ALA A 106 12.641 42.641 -35.920 1.00182.42 C
ANISOU 646 CB ALA A 106 23328 24802 21181 3456 -72 1517 C
ATOM 647 N GLU A 107 10.251 40.319 -36.489 1.00225.25 N
ANISOU 647 N GLU A 107 28404 30720 26462 2602 -15 1147 N
ATOM 648 CA GLU A 107 9.582 39.471 -37.460 1.00235.86 C
ANISOU 648 CA GLU A 107 29588 32385 27642 2222 -76 979 C
ATOM 649 C GLU A 107 8.071 39.459 -37.229 1.00229.40 C
ANISOU 649 C GLU A 107 28433 31899 26828 2066 -66 1048 C
ATOM 650 O GLU A 107 7.330 38.794 -37.962 1.00232.56 O
ANISOU 650 O GLU A 107 28661 32610 27091 1730 -117 932 O
ATOM 651 CB GLU A 107 10.185 38.056 -37.367 1.00253.27 C
ANISOU 651 CB GLU A 107 32138 34266 29828 1957 32 692 C
ATOM 652 CG GLU A 107 9.456 36.962 -38.112 1.00272.42 C
ANISOU 652 CG GLU A 107 34471 36941 32097 1517 18 485 C
ATOM 653 CD GLU A 107 9.929 35.569 -37.767 1.00286.54 C
ANISOU 653 CD GLU A 107 36615 38364 33894 1274 161 217 C
ATOM 654 OE1 GLU A 107 10.650 35.391 -36.761 1.00290.34 O
ANISOU 654 OE1 GLU A 107 37392 38395 34529 1434 283 200 O
ATOM 655 OE2 GLU A 107 9.548 34.641 -38.506 1.00296.27 O
ANISOU 655 OE2 GLU A 107 37832 39764 34974 910 151 26 O
ATOM 656 N GLY A 108 7.595 40.268 -36.288 1.00233.38 N
ANISOU 656 N GLY A 108 28823 32372 27480 2312 -7 1251 N
ATOM 657 CA GLY A 108 6.180 40.394 -36.007 1.00212.59 C
ANISOU 657 CA GLY A 108 25851 30052 24871 2214 12 1347 C
ATOM 658 C GLY A 108 5.614 39.200 -35.280 1.00192.44 C
ANISOU 658 C GLY A 108 23404 27358 22359 1909 158 1162 C
ATOM 659 O GLY A 108 4.422 38.914 -35.398 1.00199.97 O
ANISOU 659 O GLY A 108 24075 28639 23265 1683 152 1159 O
ATOM 660 N LEU A 109 6.475 38.434 -34.623 1.00208.81 N
ANISOU 660 N LEU A 109 25879 28962 24498 1873 280 996 N
ATOM 661 CA LEU A 109 6.131 37.357 -33.708 1.00185.31 C
ANISOU 661 CA LEU A 109 23080 25741 21587 1638 441 830 C
ATOM 662 C LEU A 109 6.480 37.792 -32.290 1.00169.98 C
ANISOU 662 C LEU A 109 21342 23393 19851 1913 581 940 C
ATOM 663 O LEU A 109 7.484 38.483 -32.091 1.00153.02 O
ANISOU 663 O LEU A 109 19371 21000 17771 2220 568 1044 O
ATOM 664 CB LEU A 109 6.853 36.063 -34.084 1.00180.36 C
ANISOU 664 CB LEU A 109 22775 24882 20870 1363 474 547 C
ATOM 665 CG LEU A 109 6.151 35.308 -35.218 1.00165.85 C
ANISOU 665 CG LEU A 109 20751 23435 18829 967 391 394 C
ATOM 666 CD1 LEU A 109 6.682 33.890 -35.352 1.00167.83 C
ANISOU 666 CD1 LEU A 109 21346 23416 19008 660 474 99 C
ATOM 667 CD2 LEU A 109 4.638 35.309 -35.026 1.00161.62 C
ANISOU 667 CD2 LEU A 109 19861 23271 18277 785 398 461 C
ATOM 668 N TRP A 110 5.666 37.425 -31.299 1.00164.01 N
ANISOU 668 N TRP A 110 20564 22564 19188 1802 714 924 N
ATOM 669 CA TRP A 110 6.122 37.674 -29.935 1.00176.89 C
ANISOU 669 CA TRP A 110 22456 23753 21003 2019 857 994 C
ATOM 670 C TRP A 110 7.371 36.876 -29.612 1.00133.08 C
ANISOU 670 C TRP A 110 17361 17721 15484 1988 918 824 C
ATOM 671 O TRP A 110 7.495 35.694 -29.947 1.00134.12 O
ANISOU 671 O TRP A 110 17643 17784 15533 1689 937 591 O
ATOM 672 CB TRP A 110 5.060 37.330 -28.890 1.00164.83 C
ANISOU 672 CB TRP A 110 20856 22204 19569 1880 1002 986 C
ATOM 673 CG TRP A 110 3.832 38.123 -28.902 1.00169.78 C
ANISOU 673 CG TRP A 110 21063 23233 20214 1945 985 1171 C
ATOM 674 CD1 TRP A 110 2.593 37.736 -29.301 1.00171.96 C
ANISOU 674 CD1 TRP A 110 21015 23915 20408 1675 962 1131 C
ATOM 675 CD2 TRP A 110 3.686 39.423 -28.326 1.00179.70 C
ANISOU 675 CD2 TRP A 110 22194 24490 21596 2307 1016 1433 C
ATOM 676 NE1 TRP A 110 1.695 38.753 -29.082 1.00166.65 N
ANISOU 676 NE1 TRP A 110 19995 23519 19807 1865 966 1363 N
ATOM 677 CE2 TRP A 110 2.343 39.798 -28.477 1.00170.64 C
ANISOU 677 CE2 TRP A 110 20624 23772 20440 2257 1005 1548 C
ATOM 678 CE3 TRP A 110 4.576 40.320 -27.727 1.00134.34 C
ANISOU 678 CE3 TRP A 110 16655 18427 15960 2667 1051 1587 C
ATOM 679 CZ2 TRP A 110 1.863 41.034 -28.054 1.00178.47 C
ANISOU 679 CZ2 TRP A 110 21396 24876 21539 2568 1038 1808 C
ATOM 680 CZ3 TRP A 110 4.101 41.544 -27.307 1.00173.47 C
ANISOU 680 CZ3 TRP A 110 21409 23491 21009 2960 1083 1839 C
ATOM 681 CH2 TRP A 110 2.757 41.891 -27.472 1.00170.31 C
ANISOU 681 CH2 TRP A 110 20591 23511 20607 2916 1081 1946 C
ATOM 682 N LEU A 111 8.304 37.563 -28.961 1.00130.21 N
ANISOU 682 N LEU A 111 17212 17026 15236 2307 950 953 N
ATOM 683 CA LEU A 111 9.540 36.969 -28.490 1.00157.21 C
ANISOU 683 CA LEU A 111 21057 19961 18714 2336 1013 841 C
ATOM 684 C LEU A 111 9.306 35.754 -27.616 1.00171.56 C
ANISOU 684 C LEU A 111 23104 21491 20590 2072 1159 656 C
ATOM 685 O LEU A 111 8.502 35.785 -26.681 1.00191.26 O
ANISOU 685 O LEU A 111 25542 23954 23173 2033 1264 704 O
ATOM 686 CB LEU A 111 10.350 38.009 -27.712 1.00125.06 C
ANISOU 686 CB LEU A 111 17143 15605 14770 2714 1038 1048 C
ATOM 687 CG LEU A 111 11.733 37.548 -27.249 1.00122.64 C
ANISOU 687 CG LEU A 111 17260 14811 14528 2786 1084 973 C
ATOM 688 CD1 LEU A 111 12.652 37.326 -28.440 1.00124.63 C
ANISOU 688 CD1 LEU A 111 17571 15119 14662 2781 966 877 C
ATOM 689 CD2 LEU A 111 12.337 38.550 -26.279 1.00140.08 C
ANISOU 689 CD2 LEU A 111 19617 16741 16864 3118 1129 1190 C
ATOM 690 N GLN A 112 10.013 34.678 -27.931 1.00163.29 N
ANISOU 690 N GLN A 112 22320 20231 19491 1890 1172 442 N
ATOM 691 CA GLN A 112 9.882 33.466 -27.151 1.00162.11 C
ANISOU 691 CA GLN A 112 22422 19785 19389 1636 1307 256 C
ATOM 692 C GLN A 112 11.267 32.846 -27.162 1.00183.10 C
ANISOU 692 C GLN A 112 25464 22033 22071 1677 1325 141 C
ATOM 693 O GLN A 112 12.019 32.999 -28.128 1.00205.94 O
ANISOU 693 O GLN A 112 28366 24998 24885 1758 1226 123 O
ATOM 694 CB GLN A 112 8.788 32.563 -27.743 1.00140.70 C
ANISOU 694 CB GLN A 112 19529 17389 16542 1243 1308 76 C
ATOM 695 CG GLN A 112 8.814 31.103 -27.344 1.00143.75 C
ANISOU 695 CG GLN A 112 20205 17497 16916 924 1423 -174 C
ATOM 696 CD GLN A 112 8.048 30.232 -28.321 1.00153.81 C
ANISOU 696 CD GLN A 112 21331 19103 18005 542 1389 -366 C
ATOM 697 OE1 GLN A 112 6.839 30.397 -28.499 1.00152.66 O
ANISOU 697 OE1 GLN A 112 20864 19344 17797 392 1366 -330 O
ATOM 698 NE2 GLN A 112 8.742 29.295 -28.953 1.00155.85 N
ANISOU 698 NE2 GLN A 112 21826 19216 18174 376 1391 -569 N
ATOM 699 N LYS A 113 11.598 32.137 -26.095 1.00178.40 N
ANISOU 699 N LYS A 113 25186 21013 21586 1618 1451 64 N
ATOM 700 CA LYS A 113 12.848 31.400 -26.048 1.00165.95 C
ANISOU 700 CA LYS A 113 23978 19035 20042 1630 1482 -56 C
ATOM 701 C LYS A 113 12.754 30.060 -26.759 1.00188.09 C
ANISOU 701 C LYS A 113 26881 21859 22726 1288 1506 -328 C
ATOM 702 O LYS A 113 11.750 29.354 -26.631 1.00210.42 O
ANISOU 702 O LYS A 113 29642 24808 25502 991 1566 -454 O
ATOM 703 CB LYS A 113 13.282 31.202 -24.596 1.00141.47 C
ANISOU 703 CB LYS A 113 21185 15457 17110 1711 1601 -11 C
ATOM 704 CG LYS A 113 14.783 31.071 -24.425 1.00140.11 C
ANISOU 704 CG LYS A 113 21341 14883 17013 1898 1599 0 C
ATOM 705 CD LYS A 113 15.153 30.492 -23.074 1.00149.30 C
ANISOU 705 CD LYS A 113 22841 15565 18321 1876 1721 -15 C
ATOM 706 CE LYS A 113 16.659 30.351 -22.937 1.00141.67 C
ANISOU 706 CE LYS A 113 22183 14216 17430 2063 1711 8 C
ATOM 707 NZ LYS A 113 17.086 30.412 -21.513 1.00125.52 N
ANISOU 707 NZ LYS A 113 20398 11750 15543 2167 1792 120 N
ATOM 708 N ASP A 114 13.784 29.731 -27.554 1.00182.19 N
ANISOU 708 N ASP A 114 26286 21010 21926 1325 1463 -419 N
ATOM 709 CA ASP A 114 13.785 28.459 -28.273 1.00186.86 C
ANISOU 709 CA ASP A 114 27003 21595 22398 1009 1499 -683 C
ATOM 710 C ASP A 114 13.479 27.324 -27.308 1.00187.93 C
ANISOU 710 C ASP A 114 27392 21417 22595 774 1646 -832 C
ATOM 711 O ASP A 114 13.027 26.252 -27.718 1.00211.38 O
ANISOU 711 O ASP A 114 30422 24439 25455 443 1697 -1049 O
ATOM 712 CB ASP A 114 15.121 28.241 -28.980 1.00199.65 C
ANISOU 712 CB ASP A 114 28828 23030 24000 1127 1469 -748 C
ATOM 713 CG ASP A 114 15.599 29.483 -29.694 1.00209.17 C
ANISOU 713 CG ASP A 114 29832 24466 25177 1415 1330 -569 C
ATOM 714 OD1 ASP A 114 14.814 30.017 -30.502 1.00215.43 O
ANISOU 714 OD1 ASP A 114 30300 25708 25848 1353 1233 -526 O
ATOM 715 OD2 ASP A 114 16.741 29.927 -29.451 1.00203.57 O
ANISOU 715 OD2 ASP A 114 29285 23500 24563 1695 1315 -465 O
ATOM 716 N ASN A 115 13.753 27.573 -26.027 1.00158.70 N
ANISOU 716 N ASN A 115 23854 17382 19062 942 1713 -713 N
ATOM 717 CA ASN A 115 13.697 26.637 -24.907 1.00157.04 C
ANISOU 717 CA ASN A 115 23935 16787 18945 789 1849 -814 C
ATOM 718 C ASN A 115 12.269 26.549 -24.373 1.00180.22 C
ANISOU 718 C ASN A 115 26687 19929 21858 567 1902 -826 C
ATOM 719 O ASN A 115 11.595 25.526 -24.519 1.00168.80 O
ANISOU 719 O ASN A 115 25278 18538 20320 227 1963 -1025 O
ATOM 720 CB ASN A 115 14.676 27.092 -23.816 1.00137.89 C
ANISOU 720 CB ASN A 115 21749 13938 16705 1086 1879 -650 C
ATOM 721 CG ASN A 115 14.564 26.284 -22.534 1.00148.91 C
ANISOU 721 CG ASN A 115 23429 14940 18209 949 2011 -716 C
ATOM 722 OD1 ASN A 115 13.844 26.660 -21.608 1.00153.18 O
ANISOU 722 OD1 ASN A 115 23902 15483 18817 942 2057 -619 O
ATOM 723 ND2 ASN A 115 15.305 25.185 -22.462 1.00162.79 N
ANISOU 723 ND2 ASN A 115 25517 16348 19989 847 2076 -875 N
ATOM 724 N SER A 116 11.811 27.622 -23.718 1.00187.26 N
ANISOU 724 N SER A 116 27389 20924 22835 759 1887 -612 N
ATOM 725 CA SER A 116 10.563 27.624 -22.953 1.00195.04 C
ANISOU 725 CA SER A 116 28232 22030 23842 600 1960 -595 C
ATOM 726 C SER A 116 9.307 27.355 -23.779 1.00204.74 C
ANISOU 726 C SER A 116 29141 23741 24908 310 1928 -696 C
ATOM 727 O SER A 116 8.264 27.063 -23.186 1.00233.26 O
ANISOU 727 O SER A 116 32669 27437 28522 108 2004 -733 O
ATOM 728 CB SER A 116 10.402 28.959 -22.215 1.00191.10 C
ANISOU 728 CB SER A 116 27580 21564 23464 901 1950 -328 C
ATOM 729 OG SER A 116 9.984 30.004 -23.081 1.00191.69 O
ANISOU 729 OG SER A 116 27279 22088 23468 1045 1836 -188 O
ATOM 730 N SER A 117 9.352 27.500 -25.113 1.00191.09 N
ANISOU 730 N SER A 117 27220 22348 23039 285 1814 -729 N
ATOM 731 CA SER A 117 8.311 26.987 -26.012 1.00207.51 C
ANISOU 731 CA SER A 117 29058 24849 24937 -50 1780 -865 C
ATOM 732 C SER A 117 7.039 27.827 -25.911 1.00191.29 C
ANISOU 732 C SER A 117 26587 23222 22875 -38 1744 -707 C
ATOM 733 O SER A 117 6.056 27.599 -26.628 1.00184.64 O
ANISOU 733 O SER A 117 25470 22798 21886 -287 1696 -768 O
ATOM 734 CB SER A 117 7.990 25.514 -25.723 1.00233.43 C
ANISOU 734 CB SER A 117 32588 27945 28160 -436 1897 -1121 C
ATOM 735 OG SER A 117 9.166 24.724 -25.718 1.00234.58 O
ANISOU 735 OG SER A 117 33131 27665 28333 -425 1945 -1257 O
ATOM 736 N LEU A 118 7.073 28.790 -25.008 1.00188.27 N
ANISOU 736 N LEU A 118 26162 22724 22648 249 1771 -499 N
ATOM 737 CA LEU A 118 6.110 29.729 -24.466 1.00192.02 C
ANISOU 737 CA LEU A 118 26333 23433 23192 364 1785 -307 C
ATOM 738 C LEU A 118 6.779 31.091 -24.539 1.00181.22 C
ANISOU 738 C LEU A 118 24880 22067 21907 789 1705 -63 C
ATOM 739 O LEU A 118 8.005 31.176 -24.411 1.00181.94 O
ANISOU 739 O LEU A 118 25249 21820 22059 985 1695 -45 O
ATOM 740 CB LEU A 118 5.669 29.386 -23.039 1.00204.31 C
ANISOU 740 CB LEU A 118 28050 24705 24874 284 1941 -320 C
ATOM 741 CG LEU A 118 5.070 27.980 -22.948 1.00206.14 C
ANISOU 741 CG LEU A 118 28404 24905 25015 -149 2022 -574 C
ATOM 742 CD1 LEU A 118 5.116 27.450 -21.527 1.00207.66 C
ANISOU 742 CD1 LEU A 118 28906 24660 25337 -213 2175 -623 C
ATOM 743 CD2 LEU A 118 3.640 27.978 -23.492 1.00201.03 C
ANISOU 743 CD2 LEU A 118 27349 24788 24244 -392 1991 -588 C
ATOM 744 N PRO A 119 6.028 32.174 -24.713 1.00172.32 N
ANISOU 744 N PRO A 119 23384 21302 20786 943 1652 133 N
ATOM 745 CA PRO A 119 6.698 33.463 -24.883 1.00159.30 C
ANISOU 745 CA PRO A 119 21668 19663 19195 1339 1571 358 C
ATOM 746 C PRO A 119 7.286 33.941 -23.569 1.00146.17 C
ANISOU 746 C PRO A 119 20262 17567 17708 1586 1676 485 C
ATOM 747 O PRO A 119 6.720 33.778 -22.485 1.00152.17 O
ANISOU 747 O PRO A 119 21079 18175 18562 1516 1805 493 O
ATOM 748 CB PRO A 119 5.577 34.389 -25.370 1.00154.14 C
ANISOU 748 CB PRO A 119 20545 19521 18500 1402 1503 524 C
ATOM 749 CG PRO A 119 4.531 33.480 -25.917 1.00159.50 C
ANISOU 749 CG PRO A 119 21031 20524 19048 1011 1495 356 C
ATOM 750 CD PRO A 119 4.599 32.249 -25.058 1.00165.79 C
ANISOU 750 CD PRO A 119 22160 20951 19881 753 1635 150 C
ATOM 751 N TRP A 120 8.456 34.553 -23.720 1.00132.28 N
ANISOU 751 N TRP A 120 18658 15620 15983 1869 1613 588 N
ATOM 752 CA TRP A 120 9.162 35.275 -22.674 1.00150.03 C
ANISOU 752 CA TRP A 120 21122 17506 18375 2155 1676 756 C
ATOM 753 C TRP A 120 8.356 36.428 -22.096 1.00174.60 C
ANISOU 753 C TRP A 120 23996 20779 21563 2347 1722 980 C
ATOM 754 O TRP A 120 7.694 37.187 -22.810 1.00181.35 O
ANISOU 754 O TRP A 120 24496 22050 22360 2432 1644 1093 O
ATOM 755 CB TRP A 120 10.495 35.776 -23.224 1.00131.64 C
ANISOU 755 CB TRP A 120 18935 15051 16030 2407 1572 828 C
ATOM 756 CG TRP A 120 11.286 36.553 -22.240 1.00144.80 C
ANISOU 756 CG TRP A 120 20825 16369 17825 2695 1621 1010 C
ATOM 757 CD1 TRP A 120 12.037 36.048 -21.219 1.00166.55 C
ANISOU 757 CD1 TRP A 120 23954 18646 20682 2690 1712 974 C
ATOM 758 CD2 TRP A 120 11.401 37.973 -22.159 1.00136.97 C
ANISOU 758 CD2 TRP A 120 19706 15471 16864 3021 1584 1261 C
ATOM 759 NE1 TRP A 120 12.624 37.068 -20.514 1.00148.25 N
ANISOU 759 NE1 TRP A 120 21750 16125 18452 2981 1730 1190 N
ATOM 760 CE2 TRP A 120 12.247 38.261 -21.070 1.00124.92 C
ANISOU 760 CE2 TRP A 120 18500 13511 15454 3189 1658 1365 C
ATOM 761 CE3 TRP A 120 10.874 39.032 -22.904 1.00140.20 C
ANISOU 761 CE3 TRP A 120 19771 16288 17212 3184 1494 1414 C
ATOM 762 CZ2 TRP A 120 12.577 39.561 -20.708 1.00115.12 C
ANISOU 762 CZ2 TRP A 120 17254 12228 14257 3501 1652 1608 C
ATOM 763 CZ3 TRP A 120 11.203 40.321 -22.543 1.00131.07 C
ANISOU 763 CZ3 TRP A 120 18610 15082 16107 3509 1491 1654 C
ATOM 764 CH2 TRP A 120 12.048 40.575 -21.457 1.00127.68 C
ANISOU 764 CH2 TRP A 120 18514 14214 15784 3660 1572 1746 C
ATOM 765 N ARG A 121 8.436 36.535 -20.772 1.00173.02 N
ANISOU 765 N ARG A 121 24012 20231 21498 2411 1856 1045 N
ATOM 766 CA ARG A 121 7.938 37.651 -19.987 1.00154.89 C
ANISOU 766 CA ARG A 121 21600 17953 19299 2630 1934 1267 C
ATOM 767 C ARG A 121 8.920 37.900 -18.853 1.00145.38 C
ANISOU 767 C ARG A 121 20778 16248 18212 2799 2016 1355 C
ATOM 768 O ARG A 121 9.622 36.991 -18.402 1.00150.83 O
ANISOU 768 O ARG A 121 21799 16578 18931 2669 2051 1221 O
ATOM 769 CB ARG A 121 6.570 37.370 -19.358 1.00149.07 C
ANISOU 769 CB ARG A 121 20685 17354 18602 2433 2059 1232 C
ATOM 770 CG ARG A 121 5.497 36.808 -20.259 1.00163.72 C
ANISOU 770 CG ARG A 121 22204 19659 20342 2170 2005 1107 C
ATOM 771 CD ARG A 121 4.307 36.479 -19.381 1.00169.71 C
ANISOU 771 CD ARG A 121 22864 20456 21162 1979 2153 1072 C
ATOM 772 NE ARG A 121 4.622 35.348 -18.511 1.00170.11 N
ANISOU 772 NE ARG A 121 23284 20096 21255 1748 2259 890 N
ATOM 773 CZ ARG A 121 3.835 34.902 -17.538 1.00169.65 C
ANISOU 773 CZ ARG A 121 23261 19939 21259 1562 2406 832 C
ATOM 774 NH1 ARG A 121 2.664 35.478 -17.313 1.00169.24 N
ANISOU 774 NH1 ARG A 121 22886 20177 21240 1580 2472 940 N
ATOM 775 NH2 ARG A 121 4.216 33.870 -16.798 1.00169.79 N
ANISOU 775 NH2 ARG A 121 23637 19568 21308 1358 2488 667 N
ATOM 776 N ASP A 122 8.958 39.147 -18.402 1.00136.60 N
ANISOU 776 N ASP A 122 19620 15119 17164 3086 2046 1588 N
ATOM 777 CA ASP A 122 9.680 39.553 -17.201 1.00157.03 C
ANISOU 777 CA ASP A 122 22538 17266 19862 3241 2143 1708 C
ATOM 778 C ASP A 122 8.666 40.008 -16.161 1.00171.63 C
ANISOU 778 C ASP A 122 24304 19105 21804 3246 2305 1808 C
ATOM 779 O ASP A 122 7.999 41.034 -16.333 1.00170.02 O
ANISOU 779 O ASP A 122 23823 19174 21604 3423 2317 1973 O
ATOM 780 CB ASP A 122 10.682 40.657 -17.526 1.00174.70 C
ANISOU 780 CB ASP A 122 24835 19461 22083 3572 2051 1899 C
ATOM 781 CG ASP A 122 11.564 41.031 -16.341 1.00178.47 C
ANISOU 781 CG ASP A 122 25681 19474 22655 3714 2135 2022 C
ATOM 782 OD1 ASP A 122 11.103 40.970 -15.183 1.00181.31 O
ANISOU 782 OD1 ASP A 122 26159 19625 23107 3644 2285 2048 O
ATOM 783 OD2 ASP A 122 12.736 41.391 -16.575 1.00177.87 O
ANISOU 783 OD2 ASP A 122 25781 19247 22556 3887 2048 2097 O
ATOM 784 N LEU A 123 8.576 39.240 -15.077 1.00196.59 N
ANISOU 784 N LEU A 123 27715 21938 25041 3053 2434 1710 N
ATOM 785 CA LEU A 123 7.665 39.493 -13.971 1.00204.46 C
ANISOU 785 CA LEU A 123 28688 22865 26130 3012 2609 1773 C
ATOM 786 C LEU A 123 8.394 39.984 -12.731 1.00211.52 C
ANISOU 786 C LEU A 123 29940 23306 27124 3154 2711 1909 C
ATOM 787 O LEU A 123 7.800 40.022 -11.648 1.00201.03 O
ANISOU 787 O LEU A 123 28685 21820 25878 3082 2873 1936 O
ATOM 788 CB LEU A 123 6.930 38.198 -13.622 1.00192.35 C
ANISOU 788 CB LEU A 123 27181 21303 24600 2646 2687 1548 C
ATOM 789 CG LEU A 123 5.889 37.673 -14.601 1.00190.22 C
ANISOU 789 CG LEU A 123 26543 21494 24236 2442 2629 1413 C
ATOM 790 CD1 LEU A 123 4.964 36.685 -13.931 1.00186.97 C
ANISOU 790 CD1 LEU A 123 26149 21043 23848 2111 2755 1246 C
ATOM 791 CD2 LEU A 123 5.129 38.815 -15.161 1.00198.11 C
ANISOU 791 CD2 LEU A 123 27137 22915 25221 2648 2602 1592 C
ATOM 792 N SER A 124 9.668 40.357 -12.864 1.00221.15 N
ANISOU 792 N SER A 124 31382 24314 28329 3342 2622 1997 N
ATOM 793 CA SER A 124 10.517 40.508 -11.690 1.00219.72 C
ANISOU 793 CA SER A 124 31600 23658 28228 3403 2701 2086 C
ATOM 794 C SER A 124 10.079 41.641 -10.770 1.00219.62 C
ANISOU 794 C SER A 124 31589 23574 28283 3573 2845 2295 C
ATOM 795 O SER A 124 10.153 41.485 -9.544 1.00254.08 O
ANISOU 795 O SER A 124 36229 27585 32726 3490 2977 2315 O
ATOM 796 CB SER A 124 11.964 40.740 -12.124 1.00220.05 C
ANISOU 796 CB SER A 124 31842 23536 28230 3580 2565 2152 C
ATOM 797 OG SER A 124 12.048 41.830 -13.027 1.00219.68 O
ANISOU 797 OG SER A 124 31559 23794 28117 3840 2468 2298 O
ATOM 798 N GLU A 125 9.530 42.738 -11.307 1.00201.53 N
ANISOU 798 N GLU A 125 28992 21615 25966 3789 2835 2446 N
ATOM 799 CA GLU A 125 9.196 43.811 -10.378 1.00174.53 C
ANISOU 799 CA GLU A 125 25619 18082 22614 3958 2989 2647 C
ATOM 800 C GLU A 125 8.026 43.429 -9.485 1.00170.29 C
ANISOU 800 C GLU A 125 25026 17521 22157 3761 3176 2580 C
ATOM 801 O GLU A 125 7.759 44.095 -8.481 1.00185.06 O
ANISOU 801 O GLU A 125 27007 19210 24097 3839 3340 2712 O
ATOM 802 CB GLU A 125 8.851 45.032 -11.237 1.00163.91 C
ANISOU 802 CB GLU A 125 23946 17112 21220 4239 2933 2818 C
ATOM 803 CG GLU A 125 9.989 45.383 -12.210 1.00161.95 C
ANISOU 803 CG GLU A 125 23738 16916 20880 4418 2740 2871 C
ATOM 804 CD GLU A 125 9.772 46.655 -13.013 1.00167.80 C
ANISOU 804 CD GLU A 125 24201 17989 21566 4708 2678 3056 C
ATOM 805 OE1 GLU A 125 8.851 47.428 -12.701 1.00173.05 O
ANISOU 805 OE1 GLU A 125 24680 18795 22276 4819 2799 3182 O
ATOM 806 OE2 GLU A 125 10.519 46.866 -13.993 1.00166.68 O
ANISOU 806 OE2 GLU A 125 24021 17972 21336 4825 2508 3073 O
ATOM 807 N CYS A 126 7.341 42.364 -9.876 1.00171.06 N
ANISOU 807 N CYS A 126 24956 17804 22235 3500 3153 2373 N
ATOM 808 CA CYS A 126 6.155 41.749 -9.301 1.00181.19 C
ANISOU 808 CA CYS A 126 26128 19146 23568 3256 3295 2257 C
ATOM 809 C CYS A 126 6.445 40.351 -8.758 1.00203.60 C
ANISOU 809 C CYS A 126 29259 21683 26418 2936 3311 2040 C
ATOM 810 O CYS A 126 5.522 39.660 -8.302 1.00203.67 O
ANISOU 810 O CYS A 126 29206 21724 26454 2688 3418 1911 O
ATOM 811 CB CYS A 126 5.007 41.848 -10.302 1.00180.42 C
ANISOU 811 CB CYS A 126 25542 19587 23424 3240 3251 2229 C
ATOM 812 SG CYS A 126 4.862 43.658 -10.597 1.00182.84 S
ANISOU 812 SG CYS A 126 25617 20111 23744 3666 3265 2533 S
ATOM 813 N GLU A 127 7.724 39.949 -8.733 1.00231.15 N
ANISOU 813 N GLU A 127 33076 24860 29890 2943 3216 2009 N
ATOM 814 CA GLU A 127 8.097 38.649 -8.180 1.00241.63 C
ANISOU 814 CA GLU A 127 34710 25862 31235 2663 3231 1821 C
ATOM 815 C GLU A 127 7.819 38.481 -6.695 1.00253.73 C
ANISOU 815 C GLU A 127 36506 27040 32861 2525 3415 1830 C
ATOM 816 O GLU A 127 7.796 37.332 -6.229 1.00258.21 O
ANISOU 816 O GLU A 127 37268 27399 33441 2249 3447 1653 O
ATOM 817 CB GLU A 127 9.581 38.388 -8.451 1.00239.09 C
ANISOU 817 CB GLU A 127 34676 25280 30889 2744 3094 1822 C
ATOM 818 CG GLU A 127 9.975 36.921 -8.368 1.00240.11 C
ANISOU 818 CG GLU A 127 35038 25182 31011 2467 3061 1598 C
ATOM 819 CD GLU A 127 9.207 36.059 -9.353 1.00239.45 C
ANISOU 819 CD GLU A 127 34684 25448 30849 2259 3006 1389 C
ATOM 820 OE1 GLU A 127 8.926 36.540 -10.471 1.00239.73 O
ANISOU 820 OE1 GLU A 127 34393 25882 30812 2378 2910 1418 O
ATOM 821 OE2 GLU A 127 8.878 34.903 -9.009 1.00239.99 O
ANISOU 821 OE2 GLU A 127 34873 25393 30920 1965 3058 1196 O
ATOM 822 N GLU A 128 7.541 39.546 -5.941 1.00263.17 N
ANISOU 822 N GLU A 128 37711 28167 34115 2689 3545 2019 N
ATOM 823 CA GLU A 128 7.244 39.254 -4.544 1.00260.24 C
ANISOU 823 CA GLU A 128 37600 27456 33824 2513 3723 2000 C
ATOM 824 C GLU A 128 5.936 38.480 -4.469 1.00273.24 C
ANISOU 824 C GLU A 128 39035 29308 35476 2239 3817 1823 C
ATOM 825 O GLU A 128 5.639 37.860 -3.439 1.00269.75 O
ANISOU 825 O GLU A 128 38806 28603 35083 2008 3944 1735 O
ATOM 826 CB GLU A 128 7.144 40.531 -3.700 1.00246.79 C
ANISOU 826 CB GLU A 128 35965 25625 32178 2721 3869 2231 C
ATOM 827 CG GLU A 128 7.003 40.256 -2.198 1.00235.85 C
ANISOU 827 CG GLU A 128 34907 23836 30869 2535 4051 2221 C
ATOM 828 CD GLU A 128 7.094 41.500 -1.335 1.00215.55 C
ANISOU 828 CD GLU A 128 32474 21082 28345 2733 4196 2452 C
ATOM 829 OE1 GLU A 128 6.833 42.608 -1.848 1.00199.68 O
ANISOU 829 OE1 GLU A 128 30219 19330 26321 2999 4204 2607 O
ATOM 830 OE2 GLU A 128 7.415 41.366 -0.134 1.00208.33 O
ANISOU 830 OE2 GLU A 128 31920 19760 27476 2614 4306 2478 O
ATOM 831 N SER A 129 5.201 38.460 -5.588 1.00295.58 N
ANISOU 831 N SER A 129 41455 32607 38245 2246 3742 1764 N
ATOM 832 CA SER A 129 4.017 37.627 -5.729 1.00306.48 C
ANISOU 832 CA SER A 129 42607 34235 39606 1967 3795 1582 C
ATOM 833 C SER A 129 4.256 36.193 -5.279 1.00298.56 C
ANISOU 833 C SER A 129 41899 32948 38591 1631 3797 1357 C
ATOM 834 O SER A 129 3.362 35.569 -4.696 1.00301.38 O
ANISOU 834 O SER A 129 42239 33305 38967 1371 3919 1233 O
ATOM 835 CB SER A 129 3.553 37.641 -7.189 1.00309.65 C
ANISOU 835 CB SER A 129 42587 35150 39917 2006 3653 1540 C
ATOM 836 OG SER A 129 2.642 36.585 -7.449 1.00317.29 O
ANISOU 836 OG SER A 129 43391 36329 40836 1686 3664 1330 O
ATOM 837 N LYS A 130 5.442 35.640 -5.554 1.00284.08 N
ANISOU 837 N LYS A 130 40335 30877 36727 1628 3666 1300 N
ATOM 838 CA LYS A 130 5.675 34.251 -5.164 1.00271.11 C
ANISOU 838 CA LYS A 130 38976 28960 35073 1316 3668 1087 C
ATOM 839 C LYS A 130 5.729 34.095 -3.650 1.00259.47 C
ANISOU 839 C LYS A 130 37851 27048 33687 1195 3823 1108 C
ATOM 840 O LYS A 130 5.195 33.122 -3.102 1.00251.72 O
ANISOU 840 O LYS A 130 36979 25954 32708 890 3904 937 O
ATOM 841 CB LYS A 130 6.961 33.713 -5.790 1.00258.28 C
ANISOU 841 CB LYS A 130 37561 27168 33406 1360 3503 1032 C
ATOM 842 CG LYS A 130 7.286 32.282 -5.346 1.00250.67 C
ANISOU 842 CG LYS A 130 36925 25880 32440 1059 3511 825 C
ATOM 843 CD LYS A 130 8.338 31.616 -6.219 1.00246.89 C
ANISOU 843 CD LYS A 130 36568 25333 31906 1077 3353 734 C
ATOM 844 CE LYS A 130 9.616 32.424 -6.295 1.00236.81 C
ANISOU 844 CE LYS A 130 35437 23878 30664 1392 3262 927 C
ATOM 845 NZ LYS A 130 10.583 31.757 -7.208 1.00225.33 N
ANISOU 845 NZ LYS A 130 34072 22387 29157 1408 3117 829 N
ATOM 846 N ARG A 131 6.349 35.045 -2.952 1.00247.12 N
ANISOU 846 N ARG A 131 36472 25235 32188 1415 3868 1315 N
ATOM 847 CA ARG A 131 6.675 34.851 -1.547 1.00236.88 C
ANISOU 847 CA ARG A 131 35573 23466 30964 1299 3986 1343 C
ATOM 848 C ARG A 131 5.952 35.800 -0.603 1.00231.18 C
ANISOU 848 C ARG A 131 34814 22716 30309 1364 4177 1488 C
ATOM 849 O ARG A 131 6.211 35.757 0.605 1.00236.01 O
ANISOU 849 O ARG A 131 35761 22934 30977 1272 4285 1530 O
ATOM 850 CB ARG A 131 8.192 34.973 -1.338 1.00226.44 C
ANISOU 850 CB ARG A 131 34603 21775 29658 1445 3882 1453 C
ATOM 851 CG ARG A 131 8.891 33.650 -1.036 1.00208.83 C
ANISOU 851 CG ARG A 131 32712 19203 27429 1213 3824 1293 C
ATOM 852 CD ARG A 131 8.376 33.038 0.260 1.00209.44 C
ANISOU 852 CD ARG A 131 33035 18983 27558 929 3979 1212 C
ATOM 853 NE ARG A 131 9.118 31.838 0.643 1.00209.17 N
ANISOU 853 NE ARG A 131 33360 18582 27533 725 3924 1085 N
ATOM 854 CZ ARG A 131 8.856 31.113 1.726 1.00200.39 C
ANISOU 854 CZ ARG A 131 32518 17164 26458 454 4030 996 C
ATOM 855 NH1 ARG A 131 7.867 31.462 2.537 1.00187.94 N
ANISOU 855 NH1 ARG A 131 30891 15607 24911 346 4201 1012 N
ATOM 856 NH2 ARG A 131 9.582 30.037 1.999 1.00200.51 N
ANISOU 856 NH2 ARG A 131 32779 16940 26464 289 3932 882 N
ATOM 857 N GLY A 132 5.050 36.641 -1.106 1.00237.30 N
ANISOU 857 N GLY A 132 35196 23888 31078 1514 4227 1567 N
ATOM 858 CA GLY A 132 4.361 37.585 -0.254 1.00243.02 C
ANISOU 858 CA GLY A 132 35876 24590 31870 1599 4422 1711 C
ATOM 859 C GLY A 132 3.293 36.934 0.606 1.00241.81 C
ANISOU 859 C GLY A 132 35735 24387 31755 1296 4598 1573 C
ATOM 860 O GLY A 132 2.861 35.806 0.376 1.00244.58 O
ANISOU 860 O GLY A 132 36038 24824 32067 1022 4566 1360 O
ATOM 861 N GLU A 133 2.868 37.675 1.628 1.00244.28 N
ANISOU 861 N GLU A 133 36126 24552 32138 1340 4796 1695 N
ATOM 862 CA GLU A 133 1.893 37.194 2.596 1.00234.40 C
ANISOU 862 CA GLU A 133 34919 23211 30930 1065 4989 1586 C
ATOM 863 C GLU A 133 0.512 37.813 2.419 1.00237.16 C
ANISOU 863 C GLU A 133 34837 23963 31310 1127 5135 1624 C
ATOM 864 O GLU A 133 -0.380 37.548 3.233 1.00234.75 O
ANISOU 864 O GLU A 133 34534 23614 31047 921 5317 1550 O
ATOM 865 CB GLU A 133 2.405 37.460 4.018 1.00221.58 C
ANISOU 865 CB GLU A 133 33741 21082 29366 1021 5129 1681 C
ATOM 866 CG GLU A 133 1.883 36.504 5.079 1.00232.19 C
ANISOU 866 CG GLU A 133 35307 22178 30735 651 5265 1514 C
ATOM 867 CD GLU A 133 0.949 37.182 6.060 1.00244.96 C
ANISOU 867 CD GLU A 133 36892 23758 32421 631 5526 1590 C
ATOM 868 OE1 GLU A 133 0.704 38.397 5.905 1.00245.82 O
ANISOU 868 OE1 GLU A 133 36804 24032 32562 914 5606 1774 O
ATOM 869 OE2 GLU A 133 0.462 36.502 6.986 1.00250.40 O
ANISOU 869 OE2 GLU A 133 37760 24249 33133 332 5657 1464 O
ATOM 870 N ARG A 134 0.312 38.639 1.389 1.00239.68 N
ANISOU 870 N ARG A 134 34785 24673 31611 1405 5060 1742 N
ATOM 871 CA ARG A 134 -0.943 39.374 1.261 1.00217.83 C
ANISOU 871 CA ARG A 134 31607 22274 28886 1511 5204 1820 C
ATOM 872 C ARG A 134 -2.129 38.453 0.990 1.00203.16 C
ANISOU 872 C ARG A 134 29456 20733 27004 1223 5232 1621 C
ATOM 873 O ARG A 134 -3.267 38.798 1.328 1.00181.94 O
ANISOU 873 O ARG A 134 26518 18241 24371 1203 5409 1648 O
ATOM 874 CB ARG A 134 -0.824 40.427 0.159 1.00206.20 C
ANISOU 874 CB ARG A 134 29810 21144 27391 1873 5095 1996 C
ATOM 875 CG ARG A 134 -1.852 41.549 0.240 1.00201.55 C
ANISOU 875 CG ARG A 134 28885 20824 26871 2084 5269 2159 C
ATOM 876 CD ARG A 134 -1.559 42.488 1.401 1.00200.32 C
ANISOU 876 CD ARG A 134 29029 20291 26791 2233 5469 2332 C
ATOM 877 NE ARG A 134 -2.327 43.729 1.321 1.00202.29 N
ANISOU 877 NE ARG A 134 28972 20785 27101 2514 5617 2524 N
ATOM 878 CZ ARG A 134 -3.406 43.993 2.050 1.00202.98 C
ANISOU 878 CZ ARG A 134 28935 20916 27272 2464 5863 2542 C
ATOM 879 NH1 ARG A 134 -3.851 43.103 2.926 1.00206.80 N
ANISOU 879 NH1 ARG A 134 29577 21216 27781 2131 5985 2375 N
ATOM 880 NH2 ARG A 134 -4.036 45.151 1.908 1.00207.08 N
ANISOU 880 NH2 ARG A 134 29175 21656 27851 2751 5992 2729 N
ATOM 881 N SER A 135 -1.894 37.291 0.378 1.00206.97 N
ANISOU 881 N SER A 135 29961 21275 27402 998 5067 1425 N
ATOM 882 CA SER A 135 -2.974 36.361 0.048 1.00180.96 C
ANISOU 882 CA SER A 135 26402 18293 24062 701 5078 1229 C
ATOM 883 C SER A 135 -3.172 35.388 1.209 1.00197.00 C
ANISOU 883 C SER A 135 28763 19978 26111 345 5209 1060 C
ATOM 884 O SER A 135 -2.709 34.245 1.200 1.00133.46 O
ANISOU 884 O SER A 135 20961 11745 18002 93 5113 878 O
ATOM 885 CB SER A 135 -2.672 35.636 -1.257 1.00181.04 C
ANISOU 885 CB SER A 135 26264 18563 23959 634 4843 1105 C
ATOM 886 OG SER A 135 -3.812 34.934 -1.718 1.00136.72 O
ANISOU 886 OG SER A 135 20325 13334 18288 380 4850 950 O
ATOM 887 N SER A 136 -3.888 35.860 2.227 1.00134.69 N
ANISOU 887 N SER A 136 20877 11994 18303 323 5438 1121 N
ATOM 888 CA SER A 136 -4.129 35.138 3.467 1.00145.42 C
ANISOU 888 CA SER A 136 22555 13007 19691 7 5595 991 C
ATOM 889 C SER A 136 -5.606 35.216 3.830 1.00142.73 C
ANISOU 889 C SER A 136 21901 12940 19388 -127 5796 952 C
ATOM 890 O SER A 136 -6.291 36.160 3.425 1.00149.54 O
ANISOU 890 O SER A 136 22373 14151 20294 106 5861 1097 O
ATOM 891 CB SER A 136 -3.267 35.734 4.594 1.00163.45 C
ANISOU 891 CB SER A 136 25281 14776 22047 123 5694 1131 C
ATOM 892 OG SER A 136 -3.327 34.978 5.789 1.00184.01 O
ANISOU 892 OG SER A 136 28249 16998 24669 -193 5819 1005 O
ATOM 893 N PRO A 137 -6.136 34.232 4.559 1.00155.43 N
ANISOU 893 N PRO A 137 23660 14416 20982 -499 5896 761 N
ATOM 894 CA PRO A 137 -7.519 34.338 5.036 1.00169.35 C
ANISOU 894 CA PRO A 137 25151 16406 22790 -632 6111 730 C
ATOM 895 C PRO A 137 -7.634 35.363 6.152 1.00195.08 C
ANISOU 895 C PRO A 137 28548 19408 26166 -471 6350 899 C
ATOM 896 O PRO A 137 -6.645 35.758 6.774 1.00218.77 O
ANISOU 896 O PRO A 137 31941 21980 29201 -353 6361 1000 O
ATOM 897 CB PRO A 137 -7.829 32.929 5.546 1.00152.46 C
ANISOU 897 CB PRO A 137 23224 14119 20585 -1090 6131 470 C
ATOM 898 CG PRO A 137 -6.528 32.449 6.031 1.00147.64 C
ANISOU 898 CG PRO A 137 23150 12988 19960 -1148 6039 434 C
ATOM 899 CD PRO A 137 -5.501 33.000 5.066 1.00154.89 C
ANISOU 899 CD PRO A 137 24033 13959 20860 -816 5834 571 C
ATOM 900 N GLU A 138 -8.865 35.815 6.385 1.00200.72 N
ANISOU 900 N GLU A 138 28926 20397 26940 -466 6547 935 N
ATOM 901 CA GLU A 138 -9.110 36.716 7.502 1.00190.16 C
ANISOU 901 CA GLU A 138 27718 18818 25714 -351 6811 1073 C
ATOM 902 C GLU A 138 -8.662 36.064 8.805 1.00184.23 C
ANISOU 902 C GLU A 138 27512 17522 24967 -642 6911 961 C
ATOM 903 O GLU A 138 -8.923 34.884 9.053 1.00168.93 O
ANISOU 903 O GLU A 138 25691 15526 22970 -1011 6890 743 O
ATOM 904 CB GLU A 138 -10.591 37.092 7.575 1.00185.19 C
ANISOU 904 CB GLU A 138 26638 18576 25148 -356 7018 1094 C
ATOM 905 CG GLU A 138 -11.024 38.109 6.531 1.00189.63 C
ANISOU 905 CG GLU A 138 26691 19615 25745 13 6976 1282 C
ATOM 906 CD GLU A 138 -12.421 38.643 6.782 1.00177.47 C
ANISOU 906 CD GLU A 138 24740 18395 24295 53 7218 1343 C
ATOM 907 OE1 GLU A 138 -13.365 37.830 6.869 1.00169.86 O
ANISOU 907 OE1 GLU A 138 23590 17645 23303 -255 7272 1176 O
ATOM 908 OE2 GLU A 138 -12.573 39.877 6.902 1.00175.72 O
ANISOU 908 OE2 GLU A 138 24388 18207 24170 393 7359 1560 O
ATOM 909 N GLU A 139 -7.973 36.848 9.637 1.00166.51 N
ANISOU 909 N GLU A 139 24083 18040 21143 -1269 3303 141 N
ATOM 910 CA GLU A 139 -7.322 36.301 10.823 1.00167.32 C
ANISOU 910 CA GLU A 139 24033 18339 21200 -1694 3064 81 C
ATOM 911 C GLU A 139 -8.324 35.753 11.830 1.00159.67 C
ANISOU 911 C GLU A 139 23082 17254 20332 -1547 2988 88 C
ATOM 912 O GLU A 139 -7.975 34.888 12.640 1.00158.04 O
ANISOU 912 O GLU A 139 22596 17275 20177 -1728 2695 62 O
ATOM 913 CB GLU A 139 -6.452 37.370 11.477 1.00175.10 C
ANISOU 913 CB GLU A 139 25435 19221 21874 -2334 3272 19 C
ATOM 914 CG GLU A 139 -5.401 37.968 10.561 1.00182.06 C
ANISOU 914 CG GLU A 139 26312 20238 22624 -2559 3356 21 C
ATOM 915 CD GLU A 139 -5.278 39.468 10.733 1.00195.15 C
ANISOU 915 CD GLU A 139 28654 21520 23975 -2944 3776 -16 C
ATOM 916 OE1 GLU A 139 -6.307 40.164 10.604 1.00202.00 O
ANISOU 916 OE1 GLU A 139 29977 21955 24819 -2650 4107 4 O
ATOM 917 OE2 GLU A 139 -4.158 39.949 11.007 1.00202.39 O
ANISOU 917 OE2 GLU A 139 29665 22580 24655 -3545 3783 -53 O
ATOM 918 N GLN A 140 -9.560 36.255 11.811 1.00126.27 N
ANISOU 918 N GLN A 140 19173 12689 16115 -1218 3259 139 N
ATOM 919 CA GLN A 140 -10.567 35.795 12.760 1.00123.95 C
ANISOU 919 CA GLN A 140 18901 12295 15901 -1071 3217 165 C
ATOM 920 C GLN A 140 -10.880 34.315 12.574 1.00144.30 C
ANISOU 920 C GLN A 140 20906 15174 18746 -769 2806 200 C
ATOM 921 O GLN A 140 -11.074 33.580 13.552 1.00142.27 O
ANISOU 921 O GLN A 140 20512 14997 18548 -863 2605 186 O
ATOM 922 CB GLN A 140 -11.831 36.627 12.585 1.00128.44 C
ANISOU 922 CB GLN A 140 19871 12501 16428 -699 3605 257 C
ATOM 923 CG GLN A 140 -12.176 36.819 11.121 1.00148.11 C
ANISOU 923 CG GLN A 140 22259 15007 19009 -258 3696 346 C
ATOM 924 CD GLN A 140 -13.573 37.327 10.919 1.00184.08 C
ANISOU 924 CD GLN A 140 27050 19320 23572 220 3999 489 C
ATOM 925 OE1 GLN A 140 -14.102 38.055 11.755 1.00211.64 O
ANISOU 925 OE1 GLN A 140 30989 22511 26914 177 4309 512 O
ATOM 926 NE2 GLN A 140 -14.190 36.936 9.812 1.00184.84 N
ANISOU 926 NE2 GLN A 140 26845 19561 23824 688 3918 600 N
ATOM 927 N LEU A 141 -10.930 33.856 11.320 1.00152.05 N
ANISOU 927 N LEU A 141 21580 16315 19876 -417 2682 245 N
ATOM 928 CA LEU A 141 -11.147 32.437 11.071 1.00134.50 C
ANISOU 928 CA LEU A 141 18871 14356 17875 -163 2297 266 C
ATOM 929 C LEU A 141 -9.969 31.612 11.566 1.00134.06 C
ANISOU 929 C LEU A 141 18515 14589 17832 -476 1978 197 C
ATOM 930 O LEU A 141 -10.152 30.475 12.018 1.00133.12 O
ANISOU 930 O LEU A 141 18118 14617 17845 -402 1683 202 O
ATOM 931 CB LEU A 141 -11.393 32.199 9.581 1.00113.27 C
ANISOU 931 CB LEU A 141 15979 11759 15300 246 2255 320 C
ATOM 932 CG LEU A 141 -12.338 33.187 8.886 1.00112.19 C
ANISOU 932 CG LEU A 141 16130 11385 15113 552 2602 414 C
ATOM 933 CD1 LEU A 141 -12.564 32.786 7.439 1.00140.10 C
ANISOU 933 CD1 LEU A 141 19410 15064 18757 936 2500 470 C
ATOM 934 CD2 LEU A 141 -13.666 33.310 9.624 1.00112.77 C
ANISOU 934 CD2 LEU A 141 16367 11281 15199 730 2737 503 C
ATOM 935 N LEU A 142 -8.760 32.173 11.501 1.00142.61 N
ANISOU 935 N LEU A 142 19652 15770 18762 -831 2038 151 N
ATOM 936 CA LEU A 142 -7.612 31.536 12.133 1.00144.68 C
ANISOU 936 CA LEU A 142 19643 16340 18988 -1169 1772 120 C
ATOM 937 C LEU A 142 -7.744 31.531 13.650 1.00161.74 C
ANISOU 937 C LEU A 142 21960 18431 21062 -1503 1747 92 C
ATOM 938 O LEU A 142 -7.193 30.646 14.315 1.00159.70 O
ANISOU 938 O LEU A 142 21415 18427 20836 -1651 1462 95 O
ATOM 939 CB LEU A 142 -6.322 32.236 11.708 1.00159.29 C
ANISOU 939 CB LEU A 142 21508 18352 20665 -1504 1862 105 C
ATOM 940 CG LEU A 142 -5.492 31.492 10.663 1.00173.80 C
ANISOU 940 CG LEU A 142 22904 20536 22598 -1306 1648 139 C
ATOM 941 CD1 LEU A 142 -4.336 32.351 10.179 1.00162.94 C
ANISOU 941 CD1 LEU A 142 21572 19307 21030 -1634 1791 144 C
ATOM 942 CD2 LEU A 142 -4.985 30.184 11.248 1.00194.18 C
ANISOU 942 CD2 LEU A 142 25072 23437 25271 -1305 1285 164 C
ATOM 943 N PHE A 143 -8.456 32.510 14.215 1.00177.33 N
ANISOU 943 N PHE A 143 24404 20061 22911 -1612 2057 74 N
ATOM 944 CA PHE A 143 -8.722 32.489 15.649 1.00181.48 C
ANISOU 944 CA PHE A 143 25112 20491 23352 -1889 2052 47 C
ATOM 945 C PHE A 143 -9.670 31.355 16.012 1.00182.48 C
ANISOU 945 C PHE A 143 24991 20650 23694 -1555 1828 91 C
ATOM 946 O PHE A 143 -9.462 30.661 17.014 1.00208.63 O
ANISOU 946 O PHE A 143 28160 24096 27013 -1750 1608 80 O
ATOM 947 CB PHE A 143 -9.297 33.834 16.096 1.00177.91 C
ANISOU 947 CB PHE A 143 25276 19626 22696 -2035 2480 22 C
ATOM 948 CG PHE A 143 -9.527 33.938 17.578 1.00176.22 C
ANISOU 948 CG PHE A 143 25321 19285 22351 -2352 2519 -15 C
ATOM 949 CD1 PHE A 143 -8.505 34.337 18.423 1.00186.93 C
ANISOU 949 CD1 PHE A 143 26838 20722 23466 -2959 2504 -84 C
ATOM 950 CD2 PHE A 143 -10.766 33.648 18.125 1.00174.97 C
ANISOU 950 CD2 PHE A 143 25241 18949 22291 -2060 2571 29 C
ATOM 951 CE1 PHE A 143 -8.712 34.440 19.785 1.00194.66 C
ANISOU 951 CE1 PHE A 143 28078 21582 24303 -3267 2540 -123 C
ATOM 952 CE2 PHE A 143 -10.978 33.747 19.487 1.00186.09 C
ANISOU 952 CE2 PHE A 143 26898 20237 23569 -2343 2618 -5 C
ATOM 953 CZ PHE A 143 -9.949 34.143 20.318 1.00191.54 C
ANISOU 953 CZ PHE A 143 27775 20984 24017 -2946 2604 -88 C
ATOM 954 N LEU A 144 -10.720 31.151 15.211 1.00162.76 N
ANISOU 954 N LEU A 144 22437 18047 21357 -1071 1876 151 N
ATOM 955 CA LEU A 144 -11.631 30.038 15.468 1.00140.79 C
ANISOU 955 CA LEU A 144 19407 15321 18765 -783 1647 203 C
ATOM 956 C LEU A 144 -10.973 28.688 15.195 1.00128.88 C
ANISOU 956 C LEU A 144 17436 14129 17402 -723 1241 197 C
ATOM 957 O LEU A 144 -11.350 27.675 15.807 1.00127.36 O
ANISOU 957 O LEU A 144 17064 14012 17316 -668 1002 216 O
ATOM 958 CB LEU A 144 -12.897 30.199 14.626 1.00142.81 C
ANISOU 958 CB LEU A 144 19705 15435 19122 -318 1797 292 C
ATOM 959 CG LEU A 144 -13.576 31.569 14.723 1.00151.70 C
ANISOU 959 CG LEU A 144 21297 16242 20098 -272 2245 332 C
ATOM 960 CD1 LEU A 144 -14.890 31.582 13.957 1.00158.13 C
ANISOU 960 CD1 LEU A 144 22069 16999 21015 225 2356 465 C
ATOM 961 CD2 LEU A 144 -13.794 31.966 16.177 1.00157.10 C
ANISOU 961 CD2 LEU A 144 22297 16749 20644 -556 2390 306 C
ATOM 962 N TYR A 145 -9.983 28.660 14.296 1.00144.44 N
ANISOU 962 N TYR A 145 19233 16281 19365 -725 1174 177 N
ATOM 963 CA TYR A 145 -9.390 27.397 13.866 1.00136.27 C
ANISOU 963 CA TYR A 145 17793 15527 18459 -577 834 187 C
ATOM 964 C TYR A 145 -8.725 26.667 15.026 1.00126.54 C
ANISOU 964 C TYR A 145 16399 14482 17199 -848 596 184 C
ATOM 965 O TYR A 145 -8.903 25.454 15.195 1.00167.46 O
ANISOU 965 O TYR A 145 21352 19766 22511 -674 326 210 O
ATOM 966 CB TYR A 145 -8.382 27.655 12.742 1.00145.00 C
ANISOU 966 CB TYR A 145 18770 16799 19525 -544 859 180 C
ATOM 967 CG TYR A 145 -7.388 26.533 12.526 1.00132.14 C
ANISOU 967 CG TYR A 145 16758 15496 17954 -485 558 198 C
ATOM 968 CD1 TYR A 145 -7.717 25.426 11.755 1.00130.64 C
ANISOU 968 CD1 TYR A 145 16358 15357 17922 -86 356 216 C
ATOM 969 CD2 TYR A 145 -6.116 26.586 13.085 1.00144.05 C
ANISOU 969 CD2 TYR A 145 18129 17270 19333 -826 486 213 C
ATOM 970 CE1 TYR A 145 -6.811 24.401 11.552 1.00130.30 C
ANISOU 970 CE1 TYR A 145 16015 15580 17913 15 118 242 C
ATOM 971 CE2 TYR A 145 -5.205 25.565 12.890 1.00150.22 C
ANISOU 971 CE2 TYR A 145 18549 18372 20154 -717 236 263 C
ATOM 972 CZ TYR A 145 -5.558 24.476 12.122 1.00133.52 C
ANISOU 972 CZ TYR A 145 16268 16261 18202 -273 66 276 C
ATOM 973 OH TYR A 145 -4.655 23.457 11.922 1.00132.21 O
ANISOU 973 OH TYR A 145 15792 16383 18059 -119 -147 335 O
ATOM 974 N ILE A 146 -7.959 27.394 15.842 1.00113.73 N
ANISOU 974 N ILE A 146 14914 12909 15389 -1292 694 160 N
ATOM 975 CA ILE A 146 -7.278 26.761 16.967 1.00129.24 C
ANISOU 975 CA ILE A 146 16713 15094 17299 -1575 469 176 C
ATOM 976 C ILE A 146 -8.295 26.208 17.955 1.00127.05 C
ANISOU 976 C ILE A 146 16514 14659 17100 -1523 388 182 C
ATOM 977 O ILE A 146 -8.109 25.124 18.526 1.00118.71 O
ANISOU 977 O ILE A 146 15224 13768 16113 -1501 115 218 O
ATOM 978 CB ILE A 146 -6.324 27.766 17.639 1.00116.39 C
ANISOU 978 CB ILE A 146 15255 13555 15414 -2121 604 153 C
ATOM 979 CG1 ILE A 146 -5.656 28.654 16.586 1.00117.14 C
ANISOU 979 CG1 ILE A 146 15402 13692 15412 -2182 791 142 C
ATOM 980 CG2 ILE A 146 -5.276 27.039 18.466 1.00119.67 C
ANISOU 980 CG2 ILE A 146 15365 14345 15758 -2387 328 208 C
ATOM 981 CD1 ILE A 146 -4.768 29.733 17.167 1.00115.77 C
ANISOU 981 CD1 ILE A 146 15449 13585 14953 -2772 945 118 C
ATOM 982 N ILE A 147 -9.413 26.915 18.125 1.00136.18 N
ANISOU 982 N ILE A 147 17996 15500 18246 -1465 634 163 N
ATOM 983 CA ILE A 147 -10.417 26.501 19.099 1.00141.69 C
ANISOU 983 CA ILE A 147 18781 16058 18996 -1432 595 183 C
ATOM 984 C ILE A 147 -11.084 25.205 18.658 1.00166.54 C
ANISOU 984 C ILE A 147 21649 19264 22363 -1045 339 232 C
ATOM 985 O ILE A 147 -11.069 24.202 19.384 1.00164.37 O
ANISOU 985 O ILE A 147 21214 19093 22147 -1078 90 256 O
ATOM 986 CB ILE A 147 -11.453 27.619 19.317 1.00122.32 C
ANISOU 986 CB ILE A 147 16743 13273 16460 -1414 959 178 C
ATOM 987 CG1 ILE A 147 -10.810 28.818 20.017 1.00118.48 C
ANISOU 987 CG1 ILE A 147 16621 12681 15714 -1872 1207 116 C
ATOM 988 CG2 ILE A 147 -12.637 27.097 20.118 1.00119.84 C
ANISOU 988 CG2 ILE A 147 16459 12847 16227 -1283 920 227 C
ATOM 989 CD1 ILE A 147 -11.782 29.939 20.322 1.00118.81 C
ANISOU 989 CD1 ILE A 147 17146 12358 15640 -1842 1605 115 C
ATOM 990 N TYR A 148 -11.679 25.200 17.459 1.00185.30 N
ANISOU 990 N TYR A 148 23984 21574 24847 -690 394 254 N
ATOM 991 CA TYR A 148 -12.391 23.989 17.057 1.00174.05 C
ANISOU 991 CA TYR A 148 22346 20189 23597 -377 154 298 C
ATOM 992 C TYR A 148 -11.431 22.833 16.800 1.00169.77 C
ANISOU 992 C TYR A 148 21517 19873 23116 -328 -157 290 C
ATOM 993 O TYR A 148 -11.813 21.665 16.960 1.00170.36 O
ANISOU 993 O TYR A 148 21460 19975 23294 -192 -397 317 O
ATOM 994 CB TYR A 148 -13.305 24.262 15.853 1.00183.18 C
ANISOU 994 CB TYR A 148 23530 21247 24823 -37 279 335 C
ATOM 995 CG TYR A 148 -12.677 24.279 14.472 1.00175.67 C
ANISOU 995 CG TYR A 148 22461 20391 23896 146 262 312 C
ATOM 996 CD1 TYR A 148 -12.393 23.097 13.797 1.00177.00 C
ANISOU 996 CD1 TYR A 148 22393 20697 24164 340 -15 308 C
ATOM 997 CD2 TYR A 148 -12.435 25.477 13.814 1.00180.20 C
ANISOU 997 CD2 TYR A 148 23196 20893 24380 143 542 300 C
ATOM 998 CE1 TYR A 148 -11.842 23.110 12.530 1.00195.22 C
ANISOU 998 CE1 TYR A 148 24611 23086 26479 522 -14 288 C
ATOM 999 CE2 TYR A 148 -11.890 25.498 12.542 1.00194.67 C
ANISOU 999 CE2 TYR A 148 24920 22816 26228 314 534 285 C
ATOM 1000 CZ TYR A 148 -11.594 24.312 11.907 1.00207.97 C
ANISOU 1000 CZ TYR A 148 26352 24654 28012 507 255 278 C
ATOM 1001 OH TYR A 148 -11.050 24.326 10.643 1.00225.26 O
ANISOU 1001 OH TYR A 148 28451 26933 30205 688 259 263 O
ATOM 1002 N THR A 149 -10.180 23.128 16.431 1.00169.10 N
ANISOU 1002 N THR A 149 21342 19955 22954 -436 -147 266 N
ATOM 1003 CA THR A 149 -9.196 22.059 16.287 1.00160.36 C
ANISOU 1003 CA THR A 149 19959 19090 21880 -365 -412 288 C
ATOM 1004 C THR A 149 -8.879 21.416 17.633 1.00181.37 C
ANISOU 1004 C THR A 149 22548 21856 24509 -582 -594 320 C
ATOM 1005 O THR A 149 -8.793 20.185 17.732 1.00184.15 O
ANISOU 1005 O THR A 149 22740 22286 24942 -414 -839 359 O
ATOM 1006 CB THR A 149 -7.921 22.595 15.637 1.00122.85 C
ANISOU 1006 CB THR A 149 15099 14546 17032 -443 -339 285 C
ATOM 1007 OG1 THR A 149 -8.240 23.187 14.371 1.00122.80 O
ANISOU 1007 OG1 THR A 149 15172 14433 17054 -233 -167 258 O
ATOM 1008 CG2 THR A 149 -6.918 21.469 15.422 1.00123.27 C
ANISOU 1008 CG2 THR A 149 14850 14873 17112 -294 -587 339 C
ATOM 1009 N VAL A 150 -8.716 22.226 18.684 1.00182.96 N
ANISOU 1009 N VAL A 150 22897 22045 24575 -958 -470 308 N
ATOM 1010 CA VAL A 150 -8.484 21.650 20.007 1.00146.66 C
ANISOU 1010 CA VAL A 150 18243 17548 19932 -1178 -639 345 C
ATOM 1011 C VAL A 150 -9.708 20.871 20.474 1.00129.09 C
ANISOU 1011 C VAL A 150 16081 15135 17833 -1019 -742 359 C
ATOM 1012 O VAL A 150 -9.585 19.794 21.077 1.00121.71 O
ANISOU 1012 O VAL A 150 15013 14291 16942 -990 -979 407 O
ATOM 1013 CB VAL A 150 -8.094 22.751 21.011 1.00114.58 C
ANISOU 1013 CB VAL A 150 14375 13497 15665 -1651 -470 318 C
ATOM 1014 CG1 VAL A 150 -8.151 22.223 22.437 1.00113.11 C
ANISOU 1014 CG1 VAL A 150 14186 13360 15429 -1875 -621 352 C
ATOM 1015 CG2 VAL A 150 -6.703 23.279 20.702 1.00117.62 C
ANISOU 1015 CG2 VAL A 150 14630 14161 15900 -1881 -446 333 C
ATOM 1016 N GLY A 151 -10.907 21.371 20.164 1.00125.28 N
ANISOU 1016 N GLY A 151 15790 14409 17404 -897 -564 336 N
ATOM 1017 CA GLY A 151 -12.107 20.693 20.627 1.00117.99 C
ANISOU 1017 CA GLY A 151 14905 13347 16578 -782 -651 371 C
ATOM 1018 C GLY A 151 -12.318 19.353 19.951 1.00115.47 C
ANISOU 1018 C GLY A 151 14405 13067 16401 -483 -911 400 C
ATOM 1019 O GLY A 151 -12.729 18.381 20.593 1.00117.02 O
ANISOU 1019 O GLY A 151 14565 13248 16650 -476 -1102 438 O
ATOM 1020 N TYR A 152 -12.014 19.270 18.654 1.00114.09 N
ANISOU 1020 N TYR A 152 14146 12932 16272 -247 -918 381 N
ATOM 1021 CA TYR A 152 -12.079 17.984 17.973 1.00119.85 C
ANISOU 1021 CA TYR A 152 14756 13681 17098 20 -1156 397 C
ATOM 1022 C TYR A 152 -10.893 17.088 18.300 1.00150.39 C
ANISOU 1022 C TYR A 152 18472 17724 20944 24 -1361 422 C
ATOM 1023 O TYR A 152 -10.981 15.871 18.099 1.00178.55 O
ANISOU 1023 O TYR A 152 22003 21267 24571 214 -1568 444 O
ATOM 1024 CB TYR A 152 -12.183 18.190 16.461 1.00126.27 C
ANISOU 1024 CB TYR A 152 15556 14472 17947 278 -1085 369 C
ATOM 1025 CG TYR A 152 -13.597 18.446 15.996 1.00155.43 C
ANISOU 1025 CG TYR A 152 19348 18018 21689 388 -997 389 C
ATOM 1026 CD1 TYR A 152 -14.668 17.778 16.577 1.00172.79 C
ANISOU 1026 CD1 TYR A 152 21578 20140 23935 366 -1116 437 C
ATOM 1027 CD2 TYR A 152 -13.865 19.360 14.987 1.00155.60 C
ANISOU 1027 CD2 TYR A 152 19416 18009 21695 511 -793 381 C
ATOM 1028 CE1 TYR A 152 -15.964 18.006 16.161 1.00164.48 C
ANISOU 1028 CE1 TYR A 152 20566 19021 22907 461 -1041 491 C
ATOM 1029 CE2 TYR A 152 -15.160 19.597 14.564 1.00159.38 C
ANISOU 1029 CE2 TYR A 152 19948 18406 22202 631 -712 435 C
ATOM 1030 CZ TYR A 152 -16.205 18.917 15.155 1.00159.84 C
ANISOU 1030 CZ TYR A 152 20003 18428 22301 603 -840 496 C
ATOM 1031 OH TYR A 152 -17.496 19.148 14.740 1.00159.38 O
ANISOU 1031 OH TYR A 152 19952 18354 22252 717 -764 583 O
ATOM 1032 N ALA A 153 -9.791 17.652 18.801 1.00141.55 N
ANISOU 1032 N ALA A 153 17273 16790 19721 -184 -1304 433 N
ATOM 1033 CA ALA A 153 -8.683 16.811 19.237 1.00119.86 C
ANISOU 1033 CA ALA A 153 14343 14266 16934 -174 -1495 499 C
ATOM 1034 C ALA A 153 -9.010 16.118 20.554 1.00117.33 C
ANISOU 1034 C ALA A 153 14051 13917 16613 -315 -1649 548 C
ATOM 1035 O ALA A 153 -8.881 14.892 20.673 1.00 95.83 O
ANISOU 1035 O ALA A 153 11269 11208 13932 -134 -1854 602 O
ATOM 1036 CB ALA A 153 -7.409 17.646 19.367 1.00 96.97 C
ANISOU 1036 CB ALA A 153 11311 11636 13895 -393 -1398 523 C
ATOM 1037 N LEU A 154 -9.453 16.886 21.554 1.00117.38 N
ANISOU 1037 N LEU A 154 14179 13863 16558 -631 -1538 530 N
ATOM 1038 CA LEU A 154 -9.823 16.275 22.827 1.00115.36 C
ANISOU 1038 CA LEU A 154 13961 13576 16294 -776 -1671 576 C
ATOM 1039 C LEU A 154 -11.064 15.405 22.682 1.00126.12 C
ANISOU 1039 C LEU A 154 15421 14713 17785 -583 -1772 577 C
ATOM 1040 O LEU A 154 -11.160 14.339 23.307 1.00146.61 O
ANISOU 1040 O LEU A 154 18002 17299 20406 -553 -1969 633 O
ATOM 1041 CB LEU A 154 -10.040 17.355 23.883 1.00116.39 C
ANISOU 1041 CB LEU A 154 14241 13676 16308 -1156 -1500 549 C
ATOM 1042 CG LEU A 154 -8.851 18.297 24.074 1.00119.14 C
ANISOU 1042 CG LEU A 154 14536 14245 16487 -1441 -1397 543 C
ATOM 1043 CD1 LEU A 154 -9.156 19.331 25.138 1.00120.79 C
ANISOU 1043 CD1 LEU A 154 14979 14365 16552 -1835 -1216 502 C
ATOM 1044 CD2 LEU A 154 -7.594 17.511 24.421 1.00122.61 C
ANISOU 1044 CD2 LEU A 154 14708 15014 16863 -1456 -1620 645 C
ATOM 1045 N SER A 155 -12.017 15.831 21.847 1.00117.09 N
ANISOU 1045 N SER A 155 14377 13405 16709 -459 -1643 531 N
ATOM 1046 CA SER A 155 -13.179 14.991 21.588 1.00115.02 C
ANISOU 1046 CA SER A 155 14178 12980 16546 -303 -1755 549 C
ATOM 1047 C SER A 155 -12.770 13.703 20.890 1.00132.39 C
ANISOU 1047 C SER A 155 16323 15186 18794 -50 -1976 562 C
ATOM 1048 O SER A 155 -13.246 12.620 21.243 1.00151.78 O
ANISOU 1048 O SER A 155 18836 17552 21283 -16 -2158 599 O
ATOM 1049 CB SER A 155 -14.207 15.752 20.751 1.00115.22 C
ANISOU 1049 CB SER A 155 14279 12892 16608 -213 -1571 525 C
ATOM 1050 OG SER A 155 -14.800 16.801 21.495 1.00134.59 O
ANISOU 1050 OG SER A 155 16840 15291 19009 -402 -1353 533 O
ATOM 1051 N PHE A 156 -11.851 13.794 19.927 1.00136.85 N
ANISOU 1051 N PHE A 156 16802 15850 19344 127 -1952 536 N
ATOM 1052 CA PHE A 156 -11.404 12.597 19.224 1.00 93.80 C
ANISOU 1052 CA PHE A 156 11340 10385 13914 405 -2125 550 C
ATOM 1053 C PHE A 156 -10.712 11.630 20.176 1.00116.63 C
ANISOU 1053 C PHE A 156 14190 13355 16771 402 -2300 630 C
ATOM 1054 O PHE A 156 -10.966 10.418 20.140 1.00143.16 O
ANISOU 1054 O PHE A 156 17659 16585 20152 552 -2467 656 O
ATOM 1055 CB PHE A 156 -10.472 12.996 18.078 1.00 94.24 C
ANISOU 1055 CB PHE A 156 11298 10565 13945 598 -2031 521 C
ATOM 1056 CG PHE A 156 -9.852 11.834 17.357 1.00 95.32 C
ANISOU 1056 CG PHE A 156 11441 10699 14076 919 -2168 542 C
ATOM 1057 CD1 PHE A 156 -10.504 11.236 16.292 1.00120.87 C
ANISOU 1057 CD1 PHE A 156 14833 13748 17345 1126 -2218 490 C
ATOM 1058 CD2 PHE A 156 -8.606 11.353 17.729 1.00 97.01 C
ANISOU 1058 CD2 PHE A 156 11518 11111 14230 1020 -2234 627 C
ATOM 1059 CE1 PHE A 156 -9.931 10.172 15.621 1.00110.22 C
ANISOU 1059 CE1 PHE A 156 13557 12357 15964 1430 -2317 502 C
ATOM 1060 CE2 PHE A 156 -8.031 10.288 17.064 1.00100.55 C
ANISOU 1060 CE2 PHE A 156 12005 11542 14656 1367 -2323 662 C
ATOM 1061 CZ PHE A 156 -8.695 9.697 16.008 1.00103.63 C
ANISOU 1061 CZ PHE A 156 12606 11694 15076 1574 -2356 589 C
ATOM 1062 N SER A 157 -9.869 12.153 21.069 1.00 96.43 N
ANISOU 1062 N SER A 157 11494 11007 14138 210 -2262 678 N
ATOM 1063 CA SER A 157 -9.131 11.283 21.977 1.00 97.16 C
ANISOU 1063 CA SER A 157 11510 11227 14178 220 -2425 783 C
ATOM 1064 C SER A 157 -10.062 10.629 22.991 1.00 96.78 C
ANISOU 1064 C SER A 157 11605 11007 14160 86 -2545 807 C
ATOM 1065 O SER A 157 -10.075 9.399 23.136 1.00119.77 O
ANISOU 1065 O SER A 157 14596 13829 17084 252 -2712 864 O
ATOM 1066 CB SER A 157 -8.038 12.082 22.688 1.00 98.29 C
ANISOU 1066 CB SER A 157 11453 11685 14207 -10 -2362 840 C
ATOM 1067 OG SER A 157 -7.282 12.846 21.765 1.00 98.65 O
ANISOU 1067 OG SER A 157 11372 11894 14215 50 -2229 815 O
ATOM 1068 N ALA A 158 -10.866 11.437 23.689 1.00 95.79 N
ANISOU 1068 N ALA A 158 11539 10821 14035 -205 -2445 770 N
ATOM 1069 CA ALA A 158 -11.744 10.878 24.712 1.00 95.57 C
ANISOU 1069 CA ALA A 158 11627 10659 14024 -351 -2544 806 C
ATOM 1070 C ALA A 158 -12.797 9.958 24.113 1.00110.15 C
ANISOU 1070 C ALA A 158 13629 12268 15955 -194 -2647 790 C
ATOM 1071 O ALA A 158 -13.208 8.987 24.755 1.00108.24 O
ANISOU 1071 O ALA A 158 13485 11924 15718 -222 -2802 845 O
ATOM 1072 CB ALA A 158 -12.412 12.000 25.504 1.00 94.85 C
ANISOU 1072 CB ALA A 158 11585 10552 13901 -662 -2376 774 C
ATOM 1073 N LEU A 159 -13.259 10.253 22.895 1.00131.94 N
ANISOU 1073 N LEU A 159 16423 14946 18763 -56 -2568 723 N
ATOM 1074 CA LEU A 159 -14.183 9.345 22.226 1.00134.07 C
ANISOU 1074 CA LEU A 159 16842 15022 19078 61 -2686 713 C
ATOM 1075 C LEU A 159 -13.503 8.048 21.808 1.00112.33 C
ANISOU 1075 C LEU A 159 14183 12196 16301 306 -2856 734 C
ATOM 1076 O LEU A 159 -14.149 6.993 21.787 1.00114.44 O
ANISOU 1076 O LEU A 159 14636 12278 16566 323 -3004 749 O
ATOM 1077 CB LEU A 159 -14.816 10.036 21.020 1.00133.11 C
ANISOU 1077 CB LEU A 159 16721 14867 18989 137 -2559 650 C
ATOM 1078 CG LEU A 159 -15.877 11.073 21.392 1.00143.19 C
ANISOU 1078 CG LEU A 159 17970 16154 20281 -56 -2395 661 C
ATOM 1079 CD1 LEU A 159 -16.106 12.023 20.243 1.00143.87 C
ANISOU 1079 CD1 LEU A 159 18016 16267 20380 55 -2218 616 C
ATOM 1080 CD2 LEU A 159 -17.170 10.400 21.787 1.00159.33 C
ANISOU 1080 CD2 LEU A 159 20099 18098 22341 -173 -2508 719 C
ATOM 1081 N VAL A 160 -12.210 8.096 21.476 1.00114.01 N
ANISOU 1081 N VAL A 160 14286 12554 16478 499 -2827 746 N
ATOM 1082 CA VAL A 160 -11.495 6.855 21.191 1.00107.89 C
ANISOU 1082 CA VAL A 160 13613 11716 15662 782 -2956 794 C
ATOM 1083 C VAL A 160 -11.373 6.013 22.455 1.00120.35 C
ANISOU 1083 C VAL A 160 15246 13274 17206 710 -3096 896 C
ATOM 1084 O VAL A 160 -11.613 4.796 22.436 1.00127.12 O
ANISOU 1084 O VAL A 160 16336 13922 18041 834 -3229 925 O
ATOM 1085 CB VAL A 160 -10.118 7.157 20.571 1.00101.35 C
ANISOU 1085 CB VAL A 160 12609 11106 14791 1026 -2871 817 C
ATOM 1086 CG1 VAL A 160 -9.178 5.974 20.750 1.00103.12 C
ANISOU 1086 CG1 VAL A 160 12881 11351 14949 1318 -2978 927 C
ATOM 1087 CG2 VAL A 160 -10.265 7.492 19.094 1.00101.97 C
ANISOU 1087 CG2 VAL A 160 12732 11120 14890 1196 -2776 719 C
ATOM 1088 N ILE A 161 -11.046 6.651 23.581 1.00119.82 N
ANISOU 1088 N ILE A 161 15001 13407 17120 486 -3063 950 N
ATOM 1089 CA ILE A 161 -10.901 5.912 24.832 1.00110.50 C
ANISOU 1089 CA ILE A 161 13853 12236 15895 407 -3194 1059 C
ATOM 1090 C ILE A 161 -12.241 5.329 25.265 1.00121.82 C
ANISOU 1090 C ILE A 161 15511 13409 17367 234 -3287 1042 C
ATOM 1091 O ILE A 161 -12.345 4.138 25.582 1.00144.08 O
ANISOU 1091 O ILE A 161 18520 16067 20158 320 -3429 1105 O
ATOM 1092 CB ILE A 161 -10.305 6.820 25.925 1.00106.41 C
ANISOU 1092 CB ILE A 161 13104 12005 15322 152 -3136 1112 C
ATOM 1093 CG1 ILE A 161 -9.034 7.510 25.423 1.00108.79 C
ANISOU 1093 CG1 ILE A 161 13163 12603 15569 258 -3040 1133 C
ATOM 1094 CG2 ILE A 161 -10.020 6.019 27.186 1.00117.90 C
ANISOU 1094 CG2 ILE A 161 14572 13509 16714 98 -3280 1243 C
ATOM 1095 CD1 ILE A 161 -7.969 6.559 24.931 1.00135.57 C
ANISOU 1095 CD1 ILE A 161 16508 16090 18914 650 -3114 1240 C
ATOM 1096 N ALA A 162 -13.288 6.157 25.266 1.00115.59 N
ANISOU 1096 N ALA A 162 14710 12582 16628 -4 -3195 971 N
ATOM 1097 CA ALA A 162 -14.597 5.701 25.719 1.00113.00 C
ANISOU 1097 CA ALA A 162 14539 12073 16322 -196 -3272 981 C
ATOM 1098 C ALA A 162 -15.167 4.631 24.798 1.00133.83 C
ANISOU 1098 C ALA A 162 17416 14472 18962 -61 -3391 956 C
ATOM 1099 O ALA A 162 -15.778 3.663 25.268 1.00134.29 O
ANISOU 1099 O ALA A 162 17665 14363 18995 -155 -3530 1003 O
ATOM 1100 CB ALA A 162 -15.554 6.889 25.815 1.00111.75 C
ANISOU 1100 CB ALA A 162 14291 11966 16202 -421 -3113 938 C
ATOM 1101 N SER A 163 -14.975 4.782 23.484 1.00163.09 N
ANISOU 1101 N SER A 163 21137 18152 22677 137 -3339 882 N
ATOM 1102 CA SER A 163 -15.438 3.754 22.560 1.00130.75 C
ANISOU 1102 CA SER A 163 17312 13820 18547 249 -3452 848 C
ATOM 1103 C SER A 163 -14.681 2.450 22.770 1.00134.57 C
ANISOU 1103 C SER A 163 18020 14151 18960 459 -3575 903 C
ATOM 1104 O SER A 163 -15.259 1.362 22.649 1.00147.28 O
ANISOU 1104 O SER A 163 19940 15507 20512 427 -3704 907 O
ATOM 1105 CB SER A 163 -15.291 4.237 21.117 1.00110.98 C
ANISOU 1105 CB SER A 163 14780 11336 16051 428 -3358 757 C
ATOM 1106 OG SER A 163 -15.851 3.305 20.208 1.00126.42 O
ANISOU 1106 OG SER A 163 17024 13064 17948 480 -3466 714 O
ATOM 1107 N ALA A 164 -13.390 2.538 23.107 1.00130.13 N
ANISOU 1107 N ALA A 164 17314 13749 18381 669 -3531 962 N
ATOM 1108 CA ALA A 164 -12.647 1.330 23.444 1.00136.81 C
ANISOU 1108 CA ALA A 164 18351 14481 19148 909 -3625 1056 C
ATOM 1109 C ALA A 164 -13.154 0.702 24.736 1.00135.01 C
ANISOU 1109 C ALA A 164 18234 14161 18902 692 -3747 1143 C
ATOM 1110 O ALA A 164 -13.130 -0.526 24.879 1.00126.03 O
ANISOU 1110 O ALA A 164 17408 12786 17691 813 -3850 1199 O
ATOM 1111 CB ALA A 164 -11.155 1.639 23.551 1.00139.74 C
ANISOU 1111 CB ALA A 164 18471 15130 19492 1179 -3547 1140 C
ATOM 1112 N ILE A 165 -13.631 1.522 25.676 1.00143.43 N
ANISOU 1112 N ILE A 165 19086 15393 20019 374 -3722 1156 N
ATOM 1113 CA ILE A 165 -14.095 0.989 26.954 1.00128.78 C
ANISOU 1113 CA ILE A 165 17316 13475 18140 159 -3827 1244 C
ATOM 1114 C ILE A 165 -15.434 0.281 26.784 1.00141.74 C
ANISOU 1114 C ILE A 165 19243 14839 19773 -41 -3927 1213 C
ATOM 1115 O ILE A 165 -15.616 -0.852 27.244 1.00144.37 O
ANISOU 1115 O ILE A 165 19851 14962 20042 -54 -4052 1279 O
ATOM 1116 CB ILE A 165 -14.181 2.110 28.005 1.00111.60 C
ANISOU 1116 CB ILE A 165 14849 11556 15997 -117 -3750 1265 C
ATOM 1117 CG1 ILE A 165 -12.790 2.673 28.302 1.00102.56 C
ANISOU 1117 CG1 ILE A 165 13446 10706 14818 19 -3685 1320 C
ATOM 1118 CG2 ILE A 165 -14.830 1.595 29.281 1.00102.94 C
ANISOU 1118 CG2 ILE A 165 13852 10385 14874 -364 -3850 1348 C
ATOM 1119 CD1 ILE A 165 -12.807 3.925 29.153 1.00101.30 C
ANISOU 1119 CD1 ILE A 165 13044 10787 14659 -279 -3582 1310 C
ATOM 1120 N LEU A 166 -16.392 0.937 26.122 1.00153.15 N
ANISOU 1120 N LEU A 166 20627 16296 21266 -212 -3873 1127 N
ATOM 1121 CA LEU A 166 -17.691 0.303 25.917 1.00133.12 C
ANISOU 1121 CA LEU A 166 18316 13564 18698 -443 -3978 1119 C
ATOM 1122 C LEU A 166 -17.581 -0.900 24.989 1.00139.42 C
ANISOU 1122 C LEU A 166 19499 14069 19405 -276 -4081 1083 C
ATOM 1123 O LEU A 166 -18.258 -1.913 25.194 1.00152.00 O
ANISOU 1123 O LEU A 166 21400 15434 20919 -444 -4215 1115 O
ATOM 1124 CB LEU A 166 -18.695 1.313 25.361 1.00133.87 C
ANISOU 1124 CB LEU A 166 18219 13797 18847 -626 -3887 1068 C
ATOM 1125 CG LEU A 166 -19.533 2.109 26.365 1.00138.68 C
ANISOU 1125 CG LEU A 166 18610 14581 19501 -909 -3817 1128 C
ATOM 1126 CD1 LEU A 166 -18.661 3.029 27.196 1.00144.85 C
ANISOU 1126 CD1 LEU A 166 19162 15553 20322 -858 -3685 1139 C
ATOM 1127 CD2 LEU A 166 -20.619 2.897 25.650 1.00147.06 C
ANISOU 1127 CD2 LEU A 166 19530 15756 20588 -1031 -3730 1110 C
ATOM 1128 N LEU A 167 -16.737 -0.804 23.960 1.00139.90 N
ANISOU 1128 N LEU A 167 19577 14121 19456 43 -4011 1017 N
ATOM 1129 CA LEU A 167 -16.543 -1.935 23.058 1.00134.02 C
ANISOU 1129 CA LEU A 167 19249 13073 18600 239 -4079 978 C
ATOM 1130 C LEU A 167 -15.820 -3.093 23.737 1.00136.77 C
ANISOU 1130 C LEU A 167 19879 13223 18864 438 -4142 1073 C
ATOM 1131 O LEU A 167 -16.065 -4.257 23.398 1.00127.83 O
ANISOU 1131 O LEU A 167 19210 11752 17609 463 -4227 1063 O
ATOM 1132 CB LEU A 167 -15.784 -1.479 21.813 1.00114.77 C
ANISOU 1132 CB LEU A 167 16742 10698 16168 557 -3963 893 C
ATOM 1133 CG LEU A 167 -15.488 -2.506 20.718 1.00114.75 C
ANISOU 1133 CG LEU A 167 17178 10386 16034 810 -3988 835 C
ATOM 1134 CD1 LEU A 167 -15.751 -1.903 19.348 1.00113.54 C
ANISOU 1134 CD1 LEU A 167 16975 10282 15882 836 -3923 715 C
ATOM 1135 CD2 LEU A 167 -14.052 -2.999 20.813 1.00125.51 C
ANISOU 1135 CD2 LEU A 167 18609 11726 17352 1273 -3916 906 C
ATOM 1136 N GLY A 168 -14.943 -2.803 24.701 1.00143.11 N
ANISOU 1136 N GLY A 168 20433 14232 19710 569 -4100 1174 N
ATOM 1137 CA GLY A 168 -14.057 -3.832 25.219 1.00143.49 C
ANISOU 1137 CA GLY A 168 20703 14146 19669 859 -4133 1292 C
ATOM 1138 C GLY A 168 -14.664 -4.762 26.249 1.00142.49 C
ANISOU 1138 C GLY A 168 20849 13808 19483 643 -4262 1379 C
ATOM 1139 O GLY A 168 -14.249 -5.920 26.353 1.00149.16 O
ANISOU 1139 O GLY A 168 22074 14387 20214 872 -4299 1455 O
ATOM 1140 N PHE A 169 -15.639 -4.289 27.022 1.00136.91 N
ANISOU 1140 N PHE A 169 19975 13206 18838 223 -4316 1381 N
ATOM 1141 CA PHE A 169 -16.186 -5.066 28.130 1.00141.41 C
ANISOU 1141 CA PHE A 169 20746 13627 19356 -5 -4431 1479 C
ATOM 1142 C PHE A 169 -17.396 -5.868 27.665 1.00160.41 C
ANISOU 1142 C PHE A 169 23558 15712 21679 -293 -4539 1423 C
ATOM 1143 O PHE A 169 -18.387 -5.295 27.200 1.00172.32 O
ANISOU 1143 O PHE A 169 24940 17306 23228 -587 -4546 1345 O
ATOM 1144 CB PHE A 169 -16.555 -4.153 29.298 1.00168.76 C
ANISOU 1144 CB PHE A 169 23822 17391 22909 -302 -4419 1528 C
ATOM 1145 CG PHE A 169 -15.387 -3.787 30.170 1.00197.78 C
ANISOU 1145 CG PHE A 169 27227 21324 26597 -106 -4371 1632 C
ATOM 1146 CD1 PHE A 169 -14.584 -2.702 29.859 1.00182.69 C
ANISOU 1146 CD1 PHE A 169 24947 19721 24747 40 -4253 1597 C
ATOM 1147 CD2 PHE A 169 -15.088 -4.533 31.298 1.00198.87 C
ANISOU 1147 CD2 PHE A 169 27482 21414 26668 -90 -4450 1777 C
ATOM 1148 CE1 PHE A 169 -13.507 -2.366 30.660 1.00163.62 C
ANISOU 1148 CE1 PHE A 169 22270 17585 22312 166 -4225 1706 C
ATOM 1149 CE2 PHE A 169 -14.012 -4.203 32.102 1.00187.06 C
ANISOU 1149 CE2 PHE A 169 25714 20203 25159 68 -4422 1893 C
ATOM 1150 CZ PHE A 169 -13.221 -3.117 31.783 1.00165.33 C
ANISOU 1150 CZ PHE A 169 22581 17781 22455 179 -4316 1859 C
ATOM 1151 N ARG A 170 -17.314 -7.196 27.803 1.00167.10 N
ANISOU 1151 N ARG A 170 24899 16201 22390 -216 -4618 1479 N
ATOM 1152 CA ARG A 170 -18.438 -8.055 27.443 1.00161.82 C
ANISOU 1152 CA ARG A 170 24671 15212 21603 -550 -4735 1436 C
ATOM 1153 C ARG A 170 -19.632 -7.847 28.365 1.00155.02 C
ANISOU 1153 C ARG A 170 23653 14474 20774 -1054 -4826 1492 C
ATOM 1154 O ARG A 170 -20.776 -8.074 27.955 1.00149.45 O
ANISOU 1154 O ARG A 170 23097 13684 20003 -1431 -4914 1453 O
ATOM 1155 CB ARG A 170 -18.004 -9.521 27.459 1.00174.39 C
ANISOU 1155 CB ARG A 170 26884 16357 23019 -344 -4774 1490 C
ATOM 1156 CG ARG A 170 -17.542 -10.035 26.109 1.00179.34 C
ANISOU 1156 CG ARG A 170 27906 16704 23531 -38 -4715 1389 C
ATOM 1157 CD ARG A 170 -18.697 -10.050 25.124 1.00173.86 C
ANISOU 1157 CD ARG A 170 27396 15898 22765 -437 -4794 1254 C
ATOM 1158 NE ARG A 170 -18.255 -10.294 23.755 1.00170.28 N
ANISOU 1158 NE ARG A 170 27243 15242 22212 -160 -4723 1136 N
ATOM 1159 CZ ARG A 170 -19.073 -10.356 22.709 1.00175.22 C
ANISOU 1159 CZ ARG A 170 28073 15763 22740 -443 -4783 1013 C
ATOM 1160 NH1 ARG A 170 -18.587 -10.581 21.496 1.00176.73 N
ANISOU 1160 NH1 ARG A 170 28556 15765 22829 -164 -4706 906 N
ATOM 1161 NH2 ARG A 170 -20.379 -10.196 22.877 1.00179.23 N
ANISOU 1161 NH2 ARG A 170 28484 16379 23237 -1006 -4919 1011 N
ATOM 1162 N HIS A 171 -19.392 -7.418 29.603 1.00175.88 N
ANISOU 1162 N HIS A 171 25990 17340 23498 -1076 -4805 1593 N
ATOM 1163 CA HIS A 171 -20.473 -7.178 30.549 1.00185.04 C
ANISOU 1163 CA HIS A 171 26986 18636 24685 -1518 -4865 1658 C
ATOM 1164 C HIS A 171 -21.212 -5.872 30.284 1.00184.26 C
ANISOU 1164 C HIS A 171 26432 18879 24700 -1726 -4791 1603 C
ATOM 1165 O HIS A 171 -22.281 -5.655 30.865 1.00180.48 O
ANISOU 1165 O HIS A 171 25822 18524 24228 -2093 -4824 1661 O
ATOM 1166 CB HIS A 171 -19.923 -7.181 31.979 1.00201.88 C
ANISOU 1166 CB HIS A 171 28983 20878 26842 -1459 -4859 1787 C
ATOM 1167 CG HIS A 171 -18.937 -8.276 32.243 1.00214.30 C
ANISOU 1167 CG HIS A 171 30919 22188 28315 -1128 -4891 1870 C
ATOM 1168 ND1 HIS A 171 -19.315 -9.585 32.453 1.00216.74 N
ANISOU 1168 ND1 HIS A 171 31751 22119 28482 -1236 -4994 1930 N
ATOM 1169 CD2 HIS A 171 -17.585 -8.258 32.326 1.00211.45 C
ANISOU 1169 CD2 HIS A 171 30478 21903 27960 -679 -4821 1923 C
ATOM 1170 CE1 HIS A 171 -18.240 -10.325 32.655 1.00210.13 C
ANISOU 1170 CE1 HIS A 171 31160 21111 27570 -830 -4972 2018 C
ATOM 1171 NE2 HIS A 171 -17.177 -9.544 32.584 1.00210.00 N
ANISOU 1171 NE2 HIS A 171 30759 21390 27643 -480 -4871 2025 N
ATOM 1172 N LEU A 172 -20.670 -5.001 29.433 1.00183.72 N
ANISOU 1172 N LEU A 172 26126 18968 24712 -1485 -4678 1509 N
ATOM 1173 CA LEU A 172 -21.268 -3.708 29.128 1.00165.22 C
ANISOU 1173 CA LEU A 172 23375 16932 22469 -1617 -4575 1464 C
ATOM 1174 C LEU A 172 -21.983 -3.679 27.781 1.00169.94 C
ANISOU 1174 C LEU A 172 24050 17490 23030 -1707 -4598 1381 C
ATOM 1175 O LEU A 172 -22.358 -2.598 27.319 1.00169.00 O
ANISOU 1175 O LEU A 172 23607 17618 22986 -1734 -4495 1347 O
ATOM 1176 CB LEU A 172 -20.199 -2.613 29.160 1.00143.04 C
ANISOU 1176 CB LEU A 172 20227 14358 19764 -1327 -4419 1425 C
ATOM 1177 CG LEU A 172 -19.584 -2.249 30.511 1.00157.97 C
ANISOU 1177 CG LEU A 172 21923 16411 21688 -1310 -4376 1508 C
ATOM 1178 CD1 LEU A 172 -18.502 -1.193 30.337 1.00139.07 C
ANISOU 1178 CD1 LEU A 172 19229 14251 19361 -1066 -4233 1460 C
ATOM 1179 CD2 LEU A 172 -20.657 -1.765 31.471 1.00181.45 C
ANISOU 1179 CD2 LEU A 172 24730 19529 24682 -1667 -4355 1570 C
ATOM 1180 N HIS A 173 -22.188 -4.833 27.142 1.00162.77 N
ANISOU 1180 N HIS A 173 23583 16274 21987 -1762 -4725 1354 N
ATOM 1181 CA HIS A 173 -22.702 -4.868 25.771 1.00150.81 C
ANISOU 1181 CA HIS A 173 22184 14712 20405 -1831 -4757 1266 C
ATOM 1182 C HIS A 173 -24.216 -4.646 25.773 1.00155.22 C
ANISOU 1182 C HIS A 173 22590 15459 20926 -2291 -4828 1332 C
ATOM 1183 O HIS A 173 -25.024 -5.543 25.521 1.00167.40 O
ANISOU 1183 O HIS A 173 24442 16844 22316 -2614 -4980 1356 O
ATOM 1184 CB HIS A 173 -22.319 -6.176 25.093 1.00148.31 C
ANISOU 1184 CB HIS A 173 22448 13979 19924 -1729 -4851 1208 C
ATOM 1185 CG HIS A 173 -20.913 -6.192 24.579 1.00149.93 C
ANISOU 1185 CG HIS A 173 22741 14072 20152 -1214 -4744 1139 C
ATOM 1186 ND1 HIS A 173 -20.362 -7.282 23.941 1.00163.57 N
ANISOU 1186 ND1 HIS A 173 25000 15417 21731 -1001 -4771 1090 N
ATOM 1187 CD2 HIS A 173 -19.947 -5.243 24.604 1.00147.33 C
ANISOU 1187 CD2 HIS A 173 22039 13979 19962 -874 -4598 1123 C
ATOM 1188 CE1 HIS A 173 -19.117 -7.006 23.598 1.00167.84 C
ANISOU 1188 CE1 HIS A 173 25457 15990 22326 -519 -4642 1061 C
ATOM 1189 NE2 HIS A 173 -18.840 -5.775 23.990 1.00151.21 N
ANISOU 1189 NE2 HIS A 173 22792 14269 20393 -456 -4547 1082 N
ATOM 1190 N CYS A 174 -24.589 -3.408 26.081 1.00143.54 N
ANISOU 1190 N CYS A 174 20629 14337 19573 -2319 -4705 1375 N
ATOM 1191 CA CYS A 174 -25.971 -2.964 26.001 1.00142.88 C
ANISOU 1191 CA CYS A 174 20301 14522 19466 -2665 -4723 1466 C
ATOM 1192 C CYS A 174 -26.341 -2.595 24.568 1.00176.78 C
ANISOU 1192 C CYS A 174 24534 18917 23717 -2653 -4719 1406 C
ATOM 1193 O CYS A 174 -25.482 -2.256 23.749 1.00190.32 O
ANISOU 1193 O CYS A 174 26267 20569 25476 -2330 -4639 1287 O
ATOM 1194 CB CYS A 174 -26.190 -1.764 26.921 1.00143.29 C
ANISOU 1194 CB CYS A 174 19903 14892 19650 -2645 -4553 1547 C
ATOM 1195 SG CYS A 174 -25.483 -1.967 28.567 1.00160.40 S
ANISOU 1195 SG CYS A 174 22102 16972 21871 -2590 -4526 1595 S
ATOM 1196 N THR A 175 -27.638 -2.677 24.264 1.00186.16 N
ANISOU 1196 N THR A 175 25636 20290 24804 -3019 -4810 1504 N
ATOM 1197 CA THR A 175 -28.129 -2.162 22.989 1.00179.92 C
ANISOU 1197 CA THR A 175 24699 19693 23971 -3031 -4799 1486 C
ATOM 1198 C THR A 175 -27.950 -0.649 22.913 1.00161.72 C
ANISOU 1198 C THR A 175 21933 17685 21830 -2744 -4564 1496 C
ATOM 1199 O THR A 175 -27.440 -0.115 21.915 1.00163.07 O
ANISOU 1199 O THR A 175 22058 17867 22034 -2488 -4482 1397 O
ATOM 1200 CB THR A 175 -29.602 -2.537 22.804 1.00193.39 C
ANISOU 1200 CB THR A 175 26348 21614 25516 -3512 -4951 1636 C
ATOM 1201 OG1 THR A 175 -29.742 -3.963 22.811 1.00215.32 O
ANISOU 1201 OG1 THR A 175 29623 24076 28112 -3818 -5168 1613 O
ATOM 1202 CG2 THR A 175 -30.138 -1.983 21.491 1.00183.35 C
ANISOU 1202 CG2 THR A 175 24890 20593 24181 -3529 -4948 1645 C
ATOM 1203 N ARG A 176 -28.343 0.057 23.977 1.00135.60 N
ANISOU 1203 N ARG A 176 18314 14598 18611 -2779 -4440 1614 N
ATOM 1204 CA ARG A 176 -28.140 1.499 24.021 1.00133.51 C
ANISOU 1204 CA ARG A 176 17685 14563 18480 -2511 -4189 1620 C
ATOM 1205 C ARG A 176 -26.660 1.847 23.990 1.00136.86 C
ANISOU 1205 C ARG A 176 18191 14797 19011 -2147 -4079 1459 C
ATOM 1206 O ARG A 176 -26.279 2.891 23.451 1.00135.15 O
ANISOU 1206 O ARG A 176 17786 14696 18870 -1904 -3904 1408 O
ATOM 1207 CB ARG A 176 -28.798 2.087 25.271 1.00132.73 C
ANISOU 1207 CB ARG A 176 17323 14682 18427 -2620 -4063 1772 C
ATOM 1208 CG ARG A 176 -28.265 1.525 26.578 1.00148.03 C
ANISOU 1208 CG ARG A 176 19426 16427 20391 -2674 -4105 1760 C
ATOM 1209 CD ARG A 176 -28.691 2.371 27.766 1.00157.96 C
ANISOU 1209 CD ARG A 176 20424 17892 21703 -2701 -3920 1876 C
ATOM 1210 NE ARG A 176 -28.047 1.932 29.000 1.00170.14 N
ANISOU 1210 NE ARG A 176 22117 19260 23268 -2728 -3950 1855 N
ATOM 1211 CZ ARG A 176 -26.845 2.336 29.399 1.00176.74 C
ANISOU 1211 CZ ARG A 176 22990 19984 24179 -2497 -3855 1745 C
ATOM 1212 NH1 ARG A 176 -26.151 3.192 28.660 1.00197.92 N
ANISOU 1212 NH1 ARG A 176 25581 22695 26926 -2232 -3718 1639 N
ATOM 1213 NH2 ARG A 176 -26.335 1.884 30.537 1.00134.20 N
ANISOU 1213 NH2 ARG A 176 17723 14479 18789 -2547 -3903 1753 N
ATOM 1214 N ASN A 177 -25.811 0.996 24.575 1.00154.72 N
ANISOU 1214 N ASN A 177 20726 16791 21271 -2104 -4173 1396 N
ATOM 1215 CA ASN A 177 -24.373 1.217 24.472 1.00158.69 C
ANISOU 1215 CA ASN A 177 21288 17159 21847 -1761 -4089 1271 C
ATOM 1216 C ASN A 177 -23.872 1.042 23.045 1.00178.23 C
ANISOU 1216 C ASN A 177 23910 19524 24286 -1561 -4114 1154 C
ATOM 1217 O ASN A 177 -22.897 1.692 22.656 1.00183.52 O
ANISOU 1217 O ASN A 177 24486 20215 25028 -1265 -3984 1070 O
ATOM 1218 CB ASN A 177 -23.619 0.288 25.420 1.00155.87 C
ANISOU 1218 CB ASN A 177 21172 16577 21473 -1737 -4186 1270 C
ATOM 1219 CG ASN A 177 -23.546 0.836 26.831 1.00155.02 C
ANISOU 1219 CG ASN A 177 20867 16601 21432 -1797 -4091 1345 C
ATOM 1220 OD1 ASN A 177 -23.403 0.088 27.794 1.00161.14 O
ANISOU 1220 OD1 ASN A 177 21794 17256 22175 -1892 -4185 1398 O
ATOM 1221 ND2 ASN A 177 -23.647 2.154 26.957 1.00151.13 N
ANISOU 1221 ND2 ASN A 177 20064 16342 21017 -1743 -3893 1351 N
ATOM 1222 N TYR A 178 -24.492 0.154 22.262 1.00186.10 N
ANISOU 1222 N TYR A 178 25155 20400 25153 -1735 -4280 1147 N
ATOM 1223 CA TYR A 178 -24.142 0.089 20.848 1.00185.49 C
ANISOU 1223 CA TYR A 178 25214 20242 25023 -1565 -4288 1037 C
ATOM 1224 C TYR A 178 -24.610 1.332 20.103 1.00177.05 C
ANISOU 1224 C TYR A 178 23793 19472 24007 -1509 -4149 1054 C
ATOM 1225 O TYR A 178 -23.936 1.784 19.169 1.00176.49 O
ANISOU 1225 O TYR A 178 23704 19393 23961 -1244 -4060 957 O
ATOM 1226 CB TYR A 178 -24.725 -1.171 20.206 1.00199.35 C
ANISOU 1226 CB TYR A 178 27373 21782 26589 -1813 -4500 1022 C
ATOM 1227 CG TYR A 178 -23.896 -1.691 19.049 1.00216.57 C
ANISOU 1227 CG TYR A 178 29891 23708 28688 -1566 -4518 878 C
ATOM 1228 CD1 TYR A 178 -24.010 -1.135 17.781 1.00223.53 C
ANISOU 1228 CD1 TYR A 178 30681 24709 29541 -1479 -4471 818 C
ATOM 1229 CD2 TYR A 178 -22.994 -2.732 19.229 1.00227.25 C
ANISOU 1229 CD2 TYR A 178 31662 24703 29978 -1393 -4565 816 C
ATOM 1230 CE1 TYR A 178 -23.251 -1.604 16.723 1.00232.11 C
ANISOU 1230 CE1 TYR A 178 32089 25562 30540 -1244 -4473 687 C
ATOM 1231 CE2 TYR A 178 -22.232 -3.209 18.177 1.00235.25 C
ANISOU 1231 CE2 TYR A 178 33004 25479 30901 -1128 -4551 697 C
ATOM 1232 CZ TYR A 178 -22.365 -2.641 16.927 1.00236.19 C
ANISOU 1232 CZ TYR A 178 33029 25718 30993 -1063 -4505 626 C
ATOM 1233 OH TYR A 178 -21.609 -3.111 15.877 1.00236.89 O
ANISOU 1233 OH TYR A 178 33458 25570 30980 -792 -4478 507 O
ATOM 1234 N ILE A 179 -25.744 1.910 20.512 1.00165.81 N
ANISOU 1234 N ILE A 179 22085 18321 22593 -1731 -4113 1192 N
ATOM 1235 CA ILE A 179 -26.195 3.155 19.894 1.00156.88 C
ANISOU 1235 CA ILE A 179 20617 17482 21508 -1632 -3946 1238 C
ATOM 1236 C ILE A 179 -25.220 4.286 20.202 1.00166.38 C
ANISOU 1236 C ILE A 179 21642 18720 22857 -1317 -3707 1175 C
ATOM 1237 O ILE A 179 -24.793 5.028 19.306 1.00169.81 O
ANISOU 1237 O ILE A 179 21987 19210 23323 -1091 -3583 1109 O
ATOM 1238 CB ILE A 179 -27.623 3.497 20.358 1.00116.62 C
ANISOU 1238 CB ILE A 179 15251 12687 16373 -1899 -3936 1436 C
ATOM 1239 CG1 ILE A 179 -28.633 2.527 19.741 1.00120.87 C
ANISOU 1239 CG1 ILE A 179 15920 13271 16733 -2244 -4175 1509 C
ATOM 1240 CG2 ILE A 179 -27.972 4.938 20.010 1.00116.27 C
ANISOU 1240 CG2 ILE A 179 14849 12934 16393 -1713 -3695 1511 C
ATOM 1241 CD1 ILE A 179 -30.073 2.841 20.089 1.00124.14 C
ANISOU 1241 CD1 ILE A 179 16020 14060 17087 -2510 -4173 1741 C
ATOM 1242 N HIS A 180 -24.834 4.419 21.474 1.00167.59 N
ANISOU 1242 N HIS A 180 21757 18839 23080 -1323 -3643 1195 N
ATOM 1243 CA HIS A 180 -23.846 5.423 21.845 1.00143.10 C
ANISOU 1243 CA HIS A 180 18525 15765 20081 -1090 -3436 1133 C
ATOM 1244 C HIS A 180 -22.506 5.150 21.180 1.00157.82 C
ANISOU 1244 C HIS A 180 20540 17465 21958 -836 -3456 992 C
ATOM 1245 O HIS A 180 -21.759 6.086 20.885 1.00179.07 O
ANISOU 1245 O HIS A 180 23104 20226 24708 -633 -3285 932 O
ATOM 1246 CB HIS A 180 -23.679 5.464 23.365 1.00137.08 C
ANISOU 1246 CB HIS A 180 17733 14996 19356 -1193 -3399 1182 C
ATOM 1247 CG HIS A 180 -24.953 5.715 24.110 1.00149.61 C
ANISOU 1247 CG HIS A 180 19175 16747 20922 -1420 -3358 1332 C
ATOM 1248 ND1 HIS A 180 -25.146 5.303 25.411 1.00160.77 N
ANISOU 1248 ND1 HIS A 180 20626 18133 22327 -1599 -3406 1401 N
ATOM 1249 CD2 HIS A 180 -26.095 6.340 23.739 1.00163.48 C
ANISOU 1249 CD2 HIS A 180 20735 18725 22655 -1477 -3262 1446 C
ATOM 1250 CE1 HIS A 180 -26.355 5.659 25.808 1.00163.98 C
ANISOU 1250 CE1 HIS A 180 20868 18730 22707 -1759 -3336 1546 C
ATOM 1251 NE2 HIS A 180 -26.951 6.291 24.813 1.00161.85 N
ANISOU 1251 NE2 HIS A 180 20444 18625 22425 -1679 -3246 1585 N
ATOM 1252 N LEU A 181 -22.186 3.876 20.939 1.00148.17 N
ANISOU 1252 N LEU A 181 19606 16024 20667 -838 -3649 948 N
ATOM 1253 CA LEU A 181 -20.964 3.540 20.219 1.00150.43 C
ANISOU 1253 CA LEU A 181 20049 16163 20944 -554 -3654 837 C
ATOM 1254 C LEU A 181 -21.030 4.031 18.779 1.00176.56 C
ANISOU 1254 C LEU A 181 23319 19533 24234 -418 -3590 771 C
ATOM 1255 O LEU A 181 -20.031 4.517 18.232 1.00186.85 O
ANISOU 1255 O LEU A 181 24568 20852 25574 -152 -3476 696 O
ATOM 1256 CB LEU A 181 -20.739 2.027 20.277 1.00147.39 C
ANISOU 1256 CB LEU A 181 20042 15499 20462 -572 -3850 821 C
ATOM 1257 CG LEU A 181 -19.378 1.421 19.928 1.00168.59 C
ANISOU 1257 CG LEU A 181 22935 18003 23121 -242 -3852 749 C
ATOM 1258 CD1 LEU A 181 -19.194 0.113 20.680 1.00171.40 C
ANISOU 1258 CD1 LEU A 181 23611 18112 23401 -281 -3997 792 C
ATOM 1259 CD2 LEU A 181 -19.244 1.186 18.432 1.00199.17 C
ANISOU 1259 CD2 LEU A 181 26989 21771 26914 -82 -3859 654 C
ATOM 1260 N ASN A 182 -22.208 3.936 18.157 1.00185.42 N
ANISOU 1260 N ASN A 182 24445 20720 25286 -610 -3663 814 N
ATOM 1261 CA ASN A 182 -22.369 4.491 16.818 1.00168.03 C
ANISOU 1261 CA ASN A 182 22174 18614 23055 -497 -3600 772 C
ATOM 1262 C ASN A 182 -22.253 6.010 16.833 1.00143.00 C
ANISOU 1262 C ASN A 182 18673 15670 19991 -358 -3355 796 C
ATOM 1263 O ASN A 182 -21.682 6.604 15.909 1.00140.14 O
ANISOU 1263 O ASN A 182 18263 15340 19644 -138 -3243 726 O
ATOM 1264 CB ASN A 182 -23.711 4.060 16.231 1.00180.52 C
ANISOU 1264 CB ASN A 182 23801 20274 24513 -773 -3747 845 C
ATOM 1265 CG ASN A 182 -23.800 2.563 16.017 1.00206.10 C
ANISOU 1265 CG ASN A 182 27450 23250 27607 -937 -3981 800 C
ATOM 1266 OD1 ASN A 182 -22.858 1.936 15.533 1.00227.68 O
ANISOU 1266 OD1 ASN A 182 30472 25736 30298 -738 -4009 682 O
ATOM 1267 ND2 ASN A 182 -24.935 1.979 16.384 1.00200.96 N
ANISOU 1267 ND2 ASN A 182 26844 22649 26861 -1302 -4137 904 N
ATOM 1268 N LEU A 183 -22.776 6.657 17.880 1.00118.77 N
ANISOU 1268 N LEU A 183 15404 12740 16981 -481 -3255 896 N
ATOM 1269 CA LEU A 183 -22.614 8.104 17.990 1.00119.42 C
ANISOU 1269 CA LEU A 183 15249 12983 17141 -351 -2994 913 C
ATOM 1270 C LEU A 183 -21.148 8.481 18.171 1.00131.02 C
ANISOU 1270 C LEU A 183 16734 14376 18670 -154 -2887 805 C
ATOM 1271 O LEU A 183 -20.686 9.498 17.633 1.00138.70 O
ANISOU 1271 O LEU A 183 17601 15425 19674 6 -2701 766 O
ATOM 1272 CB LEU A 183 -23.457 8.637 19.149 1.00124.52 C
ANISOU 1272 CB LEU A 183 15740 13759 17812 -516 -2893 1042 C
ATOM 1273 CG LEU A 183 -23.439 10.149 19.383 1.00136.99 C
ANISOU 1273 CG LEU A 183 17142 15468 19441 -402 -2592 1074 C
ATOM 1274 CD1 LEU A 183 -23.901 10.888 18.138 1.00128.46 C
ANISOU 1274 CD1 LEU A 183 15952 14518 18337 -253 -2475 1106 C
ATOM 1275 CD2 LEU A 183 -24.305 10.515 20.578 1.00142.81 C
ANISOU 1275 CD2 LEU A 183 17782 16304 20177 -555 -2493 1206 C
ATOM 1276 N PHE A 184 -20.394 7.655 18.901 1.00137.56 N
ANISOU 1276 N PHE A 184 17694 15072 19502 -168 -3005 772 N
ATOM 1277 CA PHE A 184 -18.968 7.908 19.066 1.00132.60 C
ANISOU 1277 CA PHE A 184 17048 14430 18906 10 -2929 702 C
ATOM 1278 C PHE A 184 -18.238 7.769 17.739 1.00153.76 C
ANISOU 1278 C PHE A 184 19794 17066 21560 257 -2927 615 C
ATOM 1279 O PHE A 184 -17.376 8.592 17.407 1.00148.87 O
ANISOU 1279 O PHE A 184 19057 16538 20968 409 -2774 571 O
ATOM 1280 CB PHE A 184 -18.365 6.946 20.093 1.00130.98 C
ANISOU 1280 CB PHE A 184 16957 14121 18687 -30 -3068 720 C
ATOM 1281 CG PHE A 184 -18.981 7.032 21.464 1.00130.50 C
ANISOU 1281 CG PHE A 184 16844 14099 18641 -273 -3073 804 C
ATOM 1282 CD1 PHE A 184 -19.690 8.152 21.867 1.00128.93 C
ANISOU 1282 CD1 PHE A 184 16482 14035 18469 -396 -2899 849 C
ATOM 1283 CD2 PHE A 184 -18.842 5.981 22.355 1.00118.62 C
ANISOU 1283 CD2 PHE A 184 15477 12484 17110 -357 -3235 846 C
ATOM 1284 CE1 PHE A 184 -20.246 8.217 23.131 1.00119.22 C
ANISOU 1284 CE1 PHE A 184 15223 12836 17238 -602 -2886 927 C
ATOM 1285 CE2 PHE A 184 -19.397 6.042 23.618 1.00120.44 C
ANISOU 1285 CE2 PHE A 184 15664 12752 17345 -582 -3238 924 C
ATOM 1286 CZ PHE A 184 -20.099 7.162 24.007 1.00118.89 C
ANISOU 1286 CZ PHE A 184 15300 12698 17174 -706 -3063 962 C
ATOM 1287 N ALA A 185 -18.587 6.744 16.958 1.00155.12 N
ANISOU 1287 N ALA A 185 20176 17100 21664 282 -3090 589 N
ATOM 1288 CA ALA A 185 -17.974 6.588 15.644 1.00143.32 C
ANISOU 1288 CA ALA A 185 18778 15550 20125 521 -3079 505 C
ATOM 1289 C ALA A 185 -18.330 7.749 14.727 1.00140.61 C
ANISOU 1289 C ALA A 185 18261 15362 19801 572 -2920 493 C
ATOM 1290 O ALA A 185 -17.510 8.158 13.894 1.00125.93 O
ANISOU 1290 O ALA A 185 16373 13533 17942 792 -2818 429 O
ATOM 1291 CB ALA A 185 -18.398 5.262 15.017 1.00123.68 C
ANISOU 1291 CB ALA A 185 16614 12854 17525 491 -3278 475 C
ATOM 1292 N SER A 186 -19.534 8.306 14.877 1.00138.51 N
ANISOU 1292 N SER A 186 17871 15212 19545 388 -2883 571 N
ATOM 1293 CA SER A 186 -19.919 9.442 14.049 1.00132.00 C
ANISOU 1293 CA SER A 186 16884 14541 18729 465 -2713 589 C
ATOM 1294 C SER A 186 -19.126 10.690 14.419 1.00146.20 C
ANISOU 1294 C SER A 186 18523 16426 20602 569 -2470 572 C
ATOM 1295 O SER A 186 -18.641 11.409 13.534 1.00134.99 O
ANISOU 1295 O SER A 186 17051 15057 19181 738 -2332 527 O
ATOM 1296 CB SER A 186 -21.420 9.696 14.178 1.00118.43 C
ANISOU 1296 CB SER A 186 15055 12957 16984 275 -2722 717 C
ATOM 1297 OG SER A 186 -21.866 10.593 13.180 1.00132.98 O
ANISOU 1297 OG SER A 186 16773 14948 18807 382 -2586 754 O
ATOM 1298 N PHE A 187 -18.969 10.959 15.719 1.00142.53 N
ANISOU 1298 N PHE A 187 18000 15975 20181 446 -2415 606 N
ATOM 1299 CA PHE A 187 -18.170 12.111 16.130 1.00133.69 C
ANISOU 1299 CA PHE A 187 16776 14925 19095 482 -2193 583 C
ATOM 1300 C PHE A 187 -16.706 11.944 15.734 1.00142.31 C
ANISOU 1300 C PHE A 187 17881 16009 20182 644 -2201 498 C
ATOM 1301 O PHE A 187 -16.036 12.920 15.369 1.00145.85 O
ANISOU 1301 O PHE A 187 18250 16537 20631 720 -2019 466 O
ATOM 1302 CB PHE A 187 -18.285 12.319 17.638 1.00114.47 C
ANISOU 1302 CB PHE A 187 14315 12500 16678 284 -2155 633 C
ATOM 1303 CG PHE A 187 -19.343 13.303 18.045 1.00117.75 C
ANISOU 1303 CG PHE A 187 14668 12980 17094 191 -1965 717 C
ATOM 1304 CD1 PHE A 187 -19.140 14.664 17.883 1.00163.53 C
ANISOU 1304 CD1 PHE A 187 20431 18822 22882 246 -1691 708 C
ATOM 1305 CD2 PHE A 187 -20.527 12.871 18.617 1.00120.30 C
ANISOU 1305 CD2 PHE A 187 14982 13317 17409 54 -2044 818 C
ATOM 1306 CE1 PHE A 187 -20.106 15.573 18.268 1.00183.37 C
ANISOU 1306 CE1 PHE A 187 22926 21371 25376 209 -1480 801 C
ATOM 1307 CE2 PHE A 187 -21.497 13.774 19.003 1.00181.37 C
ANISOU 1307 CE2 PHE A 187 22648 21133 25131 15 -1844 923 C
ATOM 1308 CZ PHE A 187 -21.287 15.128 18.828 1.00192.14 C
ANISOU 1308 CZ PHE A 187 24003 22519 26483 114 -1552 915 C
ATOM 1309 N ILE A 188 -16.198 10.710 15.777 1.00133.99 N
ANISOU 1309 N ILE A 188 16935 14866 19108 709 -2397 477 N
ATOM 1310 CA ILE A 188 -14.795 10.474 15.450 1.00125.18 C
ANISOU 1310 CA ILE A 188 15809 13780 17974 905 -2396 432 C
ATOM 1311 C ILE A 188 -14.559 10.644 13.954 1.00137.17 C
ANISOU 1311 C ILE A 188 17352 15300 19464 1124 -2337 372 C
ATOM 1312 O ILE A 188 -13.594 11.298 13.532 1.00120.08 O
ANISOU 1312 O ILE A 188 15080 13249 17295 1248 -2203 347 O
ATOM 1313 CB ILE A 188 -14.365 9.081 15.945 1.00108.71 C
ANISOU 1313 CB ILE A 188 13862 11584 15859 961 -2595 451 C
ATOM 1314 CG1 ILE A 188 -14.261 9.069 17.472 1.00114.25 C
ANISOU 1314 CG1 ILE A 188 14498 12333 16580 766 -2626 516 C
ATOM 1315 CG2 ILE A 188 -13.049 8.663 15.309 1.00105.73 C
ANISOU 1315 CG2 ILE A 188 13497 11237 15440 1250 -2592 429 C
ATOM 1316 CD1 ILE A 188 -14.070 7.689 18.061 1.00110.15 C
ANISOU 1316 CD1 ILE A 188 14139 11686 16028 802 -2821 557 C
ATOM 1317 N LEU A 189 -15.447 10.081 13.127 1.00136.23 N
ANISOU 1317 N LEU A 189 17375 15076 19311 1147 -2438 355 N
ATOM 1318 CA LEU A 189 -15.333 10.292 11.689 1.00 98.67 C
ANISOU 1318 CA LEU A 189 12652 10327 14512 1334 -2382 300 C
ATOM 1319 C LEU A 189 -15.505 11.760 11.332 1.00109.56 C
ANISOU 1319 C LEU A 189 13855 11849 15925 1324 -2159 313 C
ATOM 1320 O LEU A 189 -14.875 12.249 10.385 1.00122.43 O
ANISOU 1320 O LEU A 189 15449 13533 17534 1498 -2045 270 O
ATOM 1321 CB LEU A 189 -16.367 9.443 10.946 1.00 98.57 C
ANISOU 1321 CB LEU A 189 12833 10194 14425 1290 -2546 289 C
ATOM 1322 CG LEU A 189 -16.137 7.931 10.909 1.00108.95 C
ANISOU 1322 CG LEU A 189 14430 11304 15662 1342 -2745 253 C
ATOM 1323 CD1 LEU A 189 -17.306 7.232 10.234 1.00104.58 C
ANISOU 1323 CD1 LEU A 189 14081 10649 15005 1196 -2905 246 C
ATOM 1324 CD2 LEU A 189 -14.834 7.608 10.196 1.00136.60 C
ANISOU 1324 CD2 LEU A 189 18020 14762 19121 1660 -2693 189 C
ATOM 1325 N ARG A 190 -16.332 12.485 12.090 1.00122.24 N
ANISOU 1325 N ARG A 190 15370 13507 17569 1137 -2074 379 N
ATOM 1326 CA ARG A 190 -16.475 13.916 11.849 1.00122.47 C
ANISOU 1326 CA ARG A 190 15284 13635 17613 1145 -1827 402 C
ATOM 1327 C ARG A 190 -15.175 14.653 12.143 1.00118.53 C
ANISOU 1327 C ARG A 190 14713 13200 17123 1168 -1671 361 C
ATOM 1328 O ARG A 190 -14.726 15.480 11.339 1.00113.19 O
ANISOU 1328 O ARG A 190 13997 12581 16428 1276 -1507 335 O
ATOM 1329 CB ARG A 190 -17.615 14.484 12.691 1.00123.63 C
ANISOU 1329 CB ARG A 190 15384 13810 17781 972 -1745 496 C
ATOM 1330 CG ARG A 190 -17.794 15.979 12.516 1.00116.86 C
ANISOU 1330 CG ARG A 190 14468 13015 16919 1007 -1453 532 C
ATOM 1331 CD ARG A 190 -18.984 16.497 13.293 1.00115.12 C
ANISOU 1331 CD ARG A 190 14220 12820 16700 895 -1346 647 C
ATOM 1332 NE ARG A 190 -19.488 17.737 12.713 1.00135.95 N
ANISOU 1332 NE ARG A 190 16836 15508 19309 1015 -1081 715 N
ATOM 1333 CZ ARG A 190 -20.522 18.420 13.191 1.00151.28 C
ANISOU 1333 CZ ARG A 190 18758 17490 21232 1002 -910 841 C
ATOM 1334 NH1 ARG A 190 -21.163 17.988 14.268 1.00151.39 N
ANISOU 1334 NH1 ARG A 190 18756 17508 21257 853 -985 908 N
ATOM 1335 NH2 ARG A 190 -20.911 19.538 12.595 1.00171.83 N
ANISOU 1335 NH2 ARG A 190 21364 20127 23796 1160 -650 915 N
ATOM 1336 N ALA A 191 -14.541 14.350 13.281 1.00127.66 N
ANISOU 1336 N ALA A 191 15847 14368 18291 1049 -1728 366 N
ATOM 1337 CA ALA A 191 -13.279 15.009 13.600 1.00117.96 C
ANISOU 1337 CA ALA A 191 14527 13253 17041 1019 -1605 347 C
ATOM 1338 C ALA A 191 -12.198 14.673 12.581 1.00119.04 C
ANISOU 1338 C ALA A 191 14623 13458 17147 1250 -1627 308 C
ATOM 1339 O ALA A 191 -11.382 15.536 12.232 1.00121.43 O
ANISOU 1339 O ALA A 191 14838 13881 17418 1262 -1467 295 O
ATOM 1340 CB ALA A 191 -12.821 14.618 15.005 1.00124.30 C
ANISOU 1340 CB ALA A 191 15298 14092 17840 843 -1696 379 C
ATOM 1341 N LEU A 192 -12.202 13.442 12.058 1.00105.88 N
ANISOU 1341 N LEU A 192 13046 11711 15473 1431 -1809 293 N
ATOM 1342 CA LEU A 192 -11.224 13.086 11.036 1.00104.96 C
ANISOU 1342 CA LEU A 192 12920 11647 15313 1695 -1807 263 C
ATOM 1343 C LEU A 192 -11.472 13.856 9.746 1.00116.32 C
ANISOU 1343 C LEU A 192 14364 13097 16735 1802 -1665 222 C
ATOM 1344 O LEU A 192 -10.531 14.391 9.147 1.00115.43 O
ANISOU 1344 O LEU A 192 14157 13111 16592 1915 -1538 211 O
ATOM 1345 CB LEU A 192 -11.258 11.579 10.781 1.00107.72 C
ANISOU 1345 CB LEU A 192 13446 11852 15632 1872 -2009 252 C
ATOM 1346 CG LEU A 192 -10.739 10.696 11.919 1.00109.75 C
ANISOU 1346 CG LEU A 192 13708 12107 15886 1851 -2141 309 C
ATOM 1347 CD1 LEU A 192 -11.151 9.246 11.719 1.00117.16 C
ANISOU 1347 CD1 LEU A 192 14914 12820 16783 1973 -2328 294 C
ATOM 1348 CD2 LEU A 192 -9.226 10.813 12.031 1.00111.04 C
ANISOU 1348 CD2 LEU A 192 13691 12489 16011 2001 -2071 362 C
ATOM 1349 N SER A 193 -12.734 13.944 9.316 1.00119.38 N
ANISOU 1349 N SER A 193 14845 13383 17133 1760 -1683 216 N
ATOM 1350 CA SER A 193 -13.032 14.659 8.079 1.00109.29 C
ANISOU 1350 CA SER A 193 13568 12129 15827 1873 -1554 196 C
ATOM 1351 C SER A 193 -12.710 16.142 8.206 1.00113.19 C
ANISOU 1351 C SER A 193 13948 12726 16332 1791 -1300 215 C
ATOM 1352 O SER A 193 -12.215 16.761 7.255 1.00107.10 O
ANISOU 1352 O SER A 193 13147 12018 15527 1917 -1163 194 O
ATOM 1353 CB SER A 193 -14.498 14.461 7.704 1.00118.58 C
ANISOU 1353 CB SER A 193 14830 13232 16993 1820 -1634 223 C
ATOM 1354 OG SER A 193 -15.350 14.945 8.726 1.00107.02 O
ANISOU 1354 OG SER A 193 13313 11774 15574 1615 -1592 293 O
ATOM 1355 N VAL A 194 -12.967 16.726 9.379 1.00112.98 N
ANISOU 1355 N VAL A 194 13888 12703 16336 1570 -1226 254 N
ATOM 1356 CA VAL A 194 -12.600 18.122 9.590 1.00106.63 C
ANISOU 1356 CA VAL A 194 13047 11958 15511 1457 -972 264 C
ATOM 1357 C VAL A 194 -11.085 18.277 9.590 1.00114.51 C
ANISOU 1357 C VAL A 194 13946 13096 16468 1450 -929 238 C
ATOM 1358 O VAL A 194 -10.558 19.298 9.127 1.00107.25 O
ANISOU 1358 O VAL A 194 13005 12243 15501 1429 -731 231 O
ATOM 1359 CB VAL A 194 -13.233 18.649 10.892 1.00 90.94 C
ANISOU 1359 CB VAL A 194 11099 9917 13538 1217 -895 306 C
ATOM 1360 CG1 VAL A 194 -12.814 20.083 11.152 1.00 91.21 C
ANISOU 1360 CG1 VAL A 194 11172 9967 13515 1073 -616 306 C
ATOM 1361 CG2 VAL A 194 -14.747 18.551 10.820 1.00 90.50 C
ANISOU 1361 CG2 VAL A 194 11097 9780 13510 1249 -915 366 C
ATOM 1362 N PHE A 195 -10.355 17.265 10.074 1.00116.07 N
ANISOU 1362 N PHE A 195 14075 13359 16666 1475 -1109 243 N
ATOM 1363 CA PHE A 195 -8.898 17.335 10.022 1.00114.87 C
ANISOU 1363 CA PHE A 195 13777 13408 16458 1500 -1079 257 C
ATOM 1364 C PHE A 195 -8.392 17.306 8.585 1.00110.12 C
ANISOU 1364 C PHE A 195 13151 12863 15825 1770 -1024 233 C
ATOM 1365 O PHE A 195 -7.492 18.074 8.223 1.00137.66 O
ANISOU 1365 O PHE A 195 16533 16515 19256 1743 -875 246 O
ATOM 1366 CB PHE A 195 -8.286 16.190 10.827 1.00150.97 C
ANISOU 1366 CB PHE A 195 18276 18055 21029 1528 -1277 301 C
ATOM 1367 CG PHE A 195 -8.432 16.346 12.313 1.00162.67 C
ANISOU 1367 CG PHE A 195 19742 19551 22514 1232 -1313 336 C
ATOM 1368 CD1 PHE A 195 -8.682 17.589 12.872 1.00165.03 C
ANISOU 1368 CD1 PHE A 195 20071 19847 22786 943 -1137 326 C
ATOM 1369 CD2 PHE A 195 -8.316 15.250 13.151 1.00148.35 C
ANISOU 1369 CD2 PHE A 195 17915 17738 20714 1246 -1509 381 C
ATOM 1370 CE1 PHE A 195 -8.815 17.734 14.241 1.00156.74 C
ANISOU 1370 CE1 PHE A 195 19038 18800 21718 664 -1160 352 C
ATOM 1371 CE2 PHE A 195 -8.448 15.388 14.520 1.00132.54 C
ANISOU 1371 CE2 PHE A 195 15899 15756 18703 969 -1544 415 C
ATOM 1372 CZ PHE A 195 -8.698 16.632 15.065 1.00156.17 C
ANISOU 1372 CZ PHE A 195 18921 18753 21665 672 -1371 396 C
ATOM 1373 N ILE A 196 -8.959 16.432 7.748 1.00 97.22 N
ANISOU 1373 N ILE A 196 11631 11099 14209 2008 -1140 200 N
ATOM 1374 CA ILE A 196 -8.538 16.398 6.351 1.00101.44 C
ANISOU 1374 CA ILE A 196 12175 11671 14697 2268 -1081 171 C
ATOM 1375 C ILE A 196 -8.922 17.692 5.642 1.00111.74 C
ANISOU 1375 C ILE A 196 13493 12973 15990 2215 -871 157 C
ATOM 1376 O ILE A 196 -8.185 18.174 4.769 1.00125.80 O
ANISOU 1376 O ILE A 196 15213 14865 17719 2329 -742 153 O
ATOM 1377 CB ILE A 196 -9.125 15.165 5.642 1.00102.52 C
ANISOU 1377 CB ILE A 196 12490 11642 14823 2491 -1254 130 C
ATOM 1378 CG1 ILE A 196 -8.957 13.918 6.508 1.00 99.08 C
ANISOU 1378 CG1 ILE A 196 12106 11145 14395 2513 -1449 151 C
ATOM 1379 CG2 ILE A 196 -8.426 14.936 4.318 1.00130.39 C
ANISOU 1379 CG2 ILE A 196 16042 15221 18279 2786 -1201 101 C
ATOM 1380 CD1 ILE A 196 -9.654 12.697 5.948 1.00101.45 C
ANISOU 1380 CD1 ILE A 196 12655 11230 14659 2659 -1620 103 C
ATOM 1381 N LYS A 197 -10.050 18.297 6.025 1.00105.55 N
ANISOU 1381 N LYS A 197 12787 12073 15243 2056 -816 167 N
ATOM 1382 CA LYS A 197 -10.408 19.594 5.463 1.00106.26 C
ANISOU 1382 CA LYS A 197 12912 12152 15310 2024 -584 178 C
ATOM 1383 C LYS A 197 -9.383 20.654 5.840 1.00123.63 C
ANISOU 1383 C LYS A 197 15043 14470 17462 1846 -387 188 C
ATOM 1384 O LYS A 197 -8.955 21.449 4.995 1.00136.75 O
ANISOU 1384 O LYS A 197 16703 16185 19070 1899 -213 186 O
ATOM 1385 CB LYS A 197 -11.798 20.011 5.941 1.00104.59 C
ANISOU 1385 CB LYS A 197 12792 11813 15133 1917 -543 218 C
ATOM 1386 CG LYS A 197 -12.098 21.491 5.723 1.00114.07 C
ANISOU 1386 CG LYS A 197 14058 12984 16298 1864 -253 255 C
ATOM 1387 CD LYS A 197 -13.334 21.942 6.489 1.00106.19 C
ANISOU 1387 CD LYS A 197 13143 11883 15322 1764 -176 323 C
ATOM 1388 CE LYS A 197 -13.009 22.229 7.940 1.00102.34 C
ANISOU 1388 CE LYS A 197 12684 11366 14834 1495 -129 317 C
ATOM 1389 NZ LYS A 197 -11.862 23.177 8.024 1.00102.80 N
ANISOU 1389 NZ LYS A 197 12773 11469 14819 1345 64 282 N
ATOM 1390 N ASP A 198 -8.973 20.678 7.112 1.00151.55 N
ANISOU 1390 N ASP A 198 18531 18056 20997 1605 -416 204 N
ATOM 1391 CA ASP A 198 -7.986 21.663 7.544 1.00168.44 C
ANISOU 1391 CA ASP A 198 20617 20327 23054 1362 -248 218 C
ATOM 1392 C ASP A 198 -6.639 21.437 6.874 1.00152.52 C
ANISOU 1392 C ASP A 198 18422 18549 20980 1469 -262 234 C
ATOM 1393 O ASP A 198 -5.907 22.399 6.614 1.00154.58 O
ANISOU 1393 O ASP A 198 18650 18929 21155 1329 -83 247 O
ATOM 1394 CB ASP A 198 -7.837 21.629 9.066 1.00202.16 C
ANISOU 1394 CB ASP A 198 24873 24625 27312 1062 -307 237 C
ATOM 1395 CG ASP A 198 -9.115 22.010 9.779 1.00210.96 C
ANISOU 1395 CG ASP A 198 26171 25520 28464 946 -244 234 C
ATOM 1396 OD1 ASP A 198 -10.072 22.407 9.088 1.00211.69 O
ANISOU 1396 OD1 ASP A 198 26380 25468 28583 1094 -136 235 O
ATOM 1397 OD2 ASP A 198 -9.167 21.910 11.025 1.00210.89 O
ANISOU 1397 OD2 ASP A 198 26179 25502 28446 720 -297 245 O
ATOM 1398 N ALA A 199 -6.288 20.180 6.597 1.00140.47 N
ANISOU 1398 N ALA A 199 16795 17096 19483 1719 -457 243 N
ATOM 1399 CA ALA A 199 -5.057 19.912 5.862 1.00130.21 C
ANISOU 1399 CA ALA A 199 15323 16031 18119 1897 -448 279 C
ATOM 1400 C ALA A 199 -5.150 20.414 4.425 1.00127.23 C
ANISOU 1400 C ALA A 199 15009 15617 17717 2090 -303 246 C
ATOM 1401 O ALA A 199 -4.187 20.987 3.897 1.00112.42 O
ANISOU 1401 O ALA A 199 13011 13941 15762 2079 -170 279 O
ATOM 1402 CB ALA A 199 -4.746 18.416 5.892 1.00129.07 C
ANISOU 1402 CB ALA A 199 15119 15925 17996 2172 -660 304 C
ATOM 1403 N ALA A 200 -6.311 20.240 3.786 1.00131.53 N
ANISOU 1403 N ALA A 200 15731 15931 18313 2245 -327 192 N
ATOM 1404 CA ALA A 200 -6.450 20.687 2.404 1.00118.53 C
ANISOU 1404 CA ALA A 200 14148 14257 16631 2434 -201 169 C
ATOM 1405 C ALA A 200 -6.432 22.208 2.311 1.00123.49 C
ANISOU 1405 C ALA A 200 14817 14889 17215 2228 55 185 C
ATOM 1406 O ALA A 200 -5.681 22.781 1.513 1.00127.02 O
ANISOU 1406 O ALA A 200 15210 15462 17591 2271 201 199 O
ATOM 1407 CB ALA A 200 -7.735 20.125 1.794 1.00 99.38 C
ANISOU 1407 CB ALA A 200 11890 11624 14245 2611 -308 129 C
ATOM 1408 N LEU A 201 -7.245 22.880 3.132 1.00120.62 N
ANISOU 1408 N LEU A 201 14574 14377 16878 2005 129 189 N
ATOM 1409 CA LEU A 201 -7.270 24.339 3.115 1.00119.03 C
ANISOU 1409 CA LEU A 201 14489 14125 16613 1811 401 206 C
ATOM 1410 C LEU A 201 -5.945 24.934 3.574 1.00116.04 C
ANISOU 1410 C LEU A 201 14009 13942 16138 1533 501 225 C
ATOM 1411 O LEU A 201 -5.542 25.995 3.081 1.00118.11 O
ANISOU 1411 O LEU A 201 14341 14225 16311 1427 722 236 O
ATOM 1412 CB LEU A 201 -8.409 24.854 3.994 1.00119.24 C
ANISOU 1412 CB LEU A 201 14692 13942 16671 1661 475 218 C
ATOM 1413 CG LEU A 201 -9.833 24.502 3.560 1.00117.15 C
ANISOU 1413 CG LEU A 201 14510 13528 16473 1889 413 238 C
ATOM 1414 CD1 LEU A 201 -10.814 24.869 4.656 1.00125.14 C
ANISOU 1414 CD1 LEU A 201 15646 14392 17511 1737 472 273 C
ATOM 1415 CD2 LEU A 201 -10.194 25.206 2.262 1.00110.80 C
ANISOU 1415 CD2 LEU A 201 13788 12686 15625 2090 586 266 C
ATOM 1416 N LYS A 202 -5.258 24.276 4.511 1.00128.80 N
ANISOU 1416 N LYS A 202 15462 15721 17753 1396 340 243 N
ATOM 1417 CA LYS A 202 -3.936 24.744 4.911 1.00137.62 C
ANISOU 1417 CA LYS A 202 16427 17107 18754 1118 402 289 C
ATOM 1418 C LYS A 202 -2.944 24.616 3.765 1.00109.05 C
ANISOU 1418 C LYS A 202 12625 13728 15080 1317 434 326 C
ATOM 1419 O LYS A 202 -2.095 25.495 3.568 1.00109.39 O
ANISOU 1419 O LYS A 202 12616 13944 15004 1097 594 364 O
ATOM 1420 CB LYS A 202 -3.445 23.965 6.132 1.00154.79 C
ANISOU 1420 CB LYS A 202 18433 19448 20932 969 202 328 C
ATOM 1421 CG LYS A 202 -1.959 24.135 6.410 1.00164.86 C
ANISOU 1421 CG LYS A 202 19450 21113 22076 749 204 415 C
ATOM 1422 CD LYS A 202 -1.537 23.447 7.697 1.00167.41 C
ANISOU 1422 CD LYS A 202 19608 21615 22385 584 12 475 C
ATOM 1423 CE LYS A 202 -1.815 21.957 7.660 1.00164.54 C
ANISOU 1423 CE LYS A 202 19159 21218 22141 981 -215 487 C
ATOM 1424 NZ LYS A 202 -1.387 21.299 8.926 1.00160.87 N
ANISOU 1424 NZ LYS A 202 18538 20931 21654 836 -393 562 N
ATOM 1425 N TRP A 203 -3.044 23.534 2.990 1.00106.31 N
ANISOU 1425 N TRP A 203 12203 13389 14801 1720 295 318 N
ATOM 1426 CA TRP A 203 -2.197 23.405 1.812 1.00123.83 C
ANISOU 1426 CA TRP A 203 14282 15807 16960 1960 350 352 C
ATOM 1427 C TRP A 203 -2.544 24.441 0.752 1.00144.11 C
ANISOU 1427 C TRP A 203 17012 18251 19491 1984 569 321 C
ATOM 1428 O TRP A 203 -1.662 24.876 0.006 1.00150.32 O
ANISOU 1428 O TRP A 203 17690 19238 20186 2000 695 364 O
ATOM 1429 CB TRP A 203 -2.307 21.991 1.240 1.00124.99 C
ANISOU 1429 CB TRP A 203 14394 15932 17164 2392 169 338 C
ATOM 1430 CG TRP A 203 -1.497 21.778 0.001 1.00133.02 C
ANISOU 1430 CG TRP A 203 15302 17129 18110 2688 238 370 C
ATOM 1431 CD1 TRP A 203 -0.186 21.406 -0.070 1.00140.02 C
ANISOU 1431 CD1 TRP A 203 15922 18365 18915 2788 238 474 C
ATOM 1432 CD2 TRP A 203 -1.947 21.921 -1.350 1.00148.30 C
ANISOU 1432 CD2 TRP A 203 17385 18928 20035 2938 325 315 C
ATOM 1433 NE1 TRP A 203 0.208 21.309 -1.382 1.00137.93 N
ANISOU 1433 NE1 TRP A 203 15642 18173 18592 3095 333 480 N
ATOM 1434 CE2 TRP A 203 -0.856 21.619 -2.188 1.00149.11 C
ANISOU 1434 CE2 TRP A 203 17320 19284 20049 3181 382 374 C
ATOM 1435 CE3 TRP A 203 -3.168 22.274 -1.932 1.00151.05 C
ANISOU 1435 CE3 TRP A 203 17974 18993 20425 2987 362 240 C
ATOM 1436 CZ2 TRP A 203 -0.949 21.659 -3.576 1.00158.77 C
ANISOU 1436 CZ2 TRP A 203 18642 20457 21228 3455 473 340 C
ATOM 1437 CZ3 TRP A 203 -3.257 22.317 -3.308 1.00152.26 C
ANISOU 1437 CZ3 TRP A 203 18205 19118 20530 3247 439 215 C
ATOM 1438 CH2 TRP A 203 -2.154 22.011 -4.116 1.00153.28 C
ANISOU 1438 CH2 TRP A 203 18195 19474 20573 3471 494 255 C
ATOM 1439 N MET A 204 -3.812 24.862 0.681 1.00172.12 N
ANISOU 1439 N MET A 204 20808 21493 23097 1991 626 266 N
ATOM 1440 CA MET A 204 -4.212 25.827 -0.341 1.00157.00 C
ANISOU 1440 CA MET A 204 19057 19456 21141 2057 840 258 C
ATOM 1441 C MET A 204 -3.529 27.176 -0.147 1.00153.06 C
ANISOU 1441 C MET A 204 18609 19023 20522 1710 1084 292 C
ATOM 1442 O MET A 204 -3.282 27.889 -1.127 1.00149.14 O
ANISOU 1442 O MET A 204 18169 18542 19954 1762 1265 307 O
ATOM 1443 CB MET A 204 -5.730 25.998 -0.343 1.00141.59 C
ANISOU 1443 CB MET A 204 17329 17207 19261 2145 854 233 C
ATOM 1444 CG MET A 204 -6.495 24.759 -0.783 1.00139.36 C
ANISOU 1444 CG MET A 204 17033 16858 19061 2457 626 203 C
ATOM 1445 SD MET A 204 -8.283 24.990 -0.780 1.00140.66 S
ANISOU 1445 SD MET A 204 17396 16768 19283 2529 635 218 S
ATOM 1446 CE MET A 204 -8.839 23.313 -1.079 1.00138.69 C
ANISOU 1446 CE MET A 204 17099 16506 19091 2770 308 177 C
ATOM 1447 N TYR A 205 -3.230 27.549 1.095 1.00168.56 N
ANISOU 1447 N TYR A 205 20582 21018 22446 1333 1096 302 N
ATOM 1448 CA TYR A 205 -2.504 28.777 1.392 1.00169.89 C
ANISOU 1448 CA TYR A 205 20832 21256 22463 923 1312 329 C
ATOM 1449 C TYR A 205 -1.006 28.562 1.561 1.00180.25 C
ANISOU 1449 C TYR A 205 21830 22985 23672 731 1244 399 C
ATOM 1450 O TYR A 205 -0.279 29.531 1.799 1.00187.48 O
ANISOU 1450 O TYR A 205 22784 24017 24432 331 1401 433 O
ATOM 1451 CB TYR A 205 -3.079 29.437 2.648 1.00169.02 C
ANISOU 1451 CB TYR A 205 20973 20925 22324 575 1393 302 C
ATOM 1452 CG TYR A 205 -4.401 30.128 2.410 1.00148.19 C
ANISOU 1452 CG TYR A 205 18678 17906 19721 706 1578 276 C
ATOM 1453 CD1 TYR A 205 -5.595 29.422 2.454 1.00128.89 C
ANISOU 1453 CD1 TYR A 205 16257 15295 17420 1007 1450 262 C
ATOM 1454 CD2 TYR A 205 -4.454 31.487 2.133 1.00152.77 C
ANISOU 1454 CD2 TYR A 205 19562 18311 20175 532 1889 285 C
ATOM 1455 CE1 TYR A 205 -6.806 30.052 2.234 1.00127.12 C
ANISOU 1455 CE1 TYR A 205 16300 14787 17213 1150 1623 277 C
ATOM 1456 CE2 TYR A 205 -5.658 32.124 1.911 1.00146.78 C
ANISOU 1456 CE2 TYR A 205 19111 17223 19435 705 2082 293 C
ATOM 1457 CZ TYR A 205 -6.830 31.404 1.965 1.00128.98 C
ANISOU 1457 CZ TYR A 205 16824 14856 17325 1024 1946 300 C
ATOM 1458 OH TYR A 205 -8.029 32.041 1.745 1.00127.78 O
ANISOU 1458 OH TYR A 205 16935 14439 17178 1217 2142 346 O
ATOM 1459 N SER A 206 -0.529 27.325 1.447 1.00195.82 N
ANISOU 1459 N SER A 206 23505 25192 25706 1000 1026 435 N
ATOM 1460 CA SER A 206 0.888 27.042 1.618 1.00185.49 C
ANISOU 1460 CA SER A 206 21849 24336 24292 878 962 542 C
ATOM 1461 C SER A 206 1.699 27.616 0.461 1.00182.57 C
ANISOU 1461 C SER A 206 21384 24172 23813 918 1132 598 C
ATOM 1462 O SER A 206 1.193 27.807 -0.648 1.00189.02 O
ANISOU 1462 O SER A 206 22353 24799 24668 1193 1239 549 O
ATOM 1463 CB SER A 206 1.126 25.537 1.729 1.00180.39 C
ANISOU 1463 CB SER A 206 20952 23853 23733 1242 717 583 C
ATOM 1464 OG SER A 206 0.705 24.864 0.555 1.00178.42 O
ANISOU 1464 OG SER A 206 20751 23475 23566 1734 693 541 O
ATOM 1465 N GLU A 207 2.975 27.897 0.738 1.00176.78 N
ANISOU 1465 N GLU A 207 20381 23862 22927 620 1153 714 N
ATOM 1466 CA GLU A 207 3.845 28.500 -0.267 1.00173.70 C
ANISOU 1466 CA GLU A 207 19870 23721 22407 590 1322 789 C
ATOM 1467 C GLU A 207 3.999 27.608 -1.494 1.00169.14 C
ANISOU 1467 C GLU A 207 19134 23236 21896 1173 1284 812 C
ATOM 1468 O GLU A 207 4.180 28.114 -2.608 1.00178.95 O
ANISOU 1468 O GLU A 207 20420 24488 23084 1281 1450 818 O
ATOM 1469 CB GLU A 207 5.213 28.800 0.355 1.00183.64 C
ANISOU 1469 CB GLU A 207 20801 25499 23475 153 1310 942 C
ATOM 1470 CG GLU A 207 6.301 29.216 -0.626 1.00190.44 C
ANISOU 1470 CG GLU A 207 21427 26743 24187 134 1450 1063 C
ATOM 1471 CD GLU A 207 6.101 30.614 -1.178 1.00193.60 C
ANISOU 1471 CD GLU A 207 22158 26916 24484 -181 1711 1004 C
ATOM 1472 OE1 GLU A 207 5.313 31.385 -0.591 1.00191.16 O
ANISOU 1472 OE1 GLU A 207 22244 26215 24175 -486 1798 894 O
ATOM 1473 OE2 GLU A 207 6.739 30.942 -2.202 1.00194.42 O
ANISOU 1473 OE2 GLU A 207 22143 27229 24497 -109 1845 1076 O
ATOM 1474 N ALA A 208 3.915 26.288 -1.320 1.00160.27 N
ANISOU 1474 N ALA A 208 17864 22155 20876 1552 1082 822 N
ATOM 1475 CA ALA A 208 4.091 25.385 -2.453 1.00159.46 C
ANISOU 1475 CA ALA A 208 17666 22115 20807 2106 1058 839 C
ATOM 1476 C ALA A 208 2.900 25.451 -3.402 1.00157.87 C
ANISOU 1476 C ALA A 208 17811 21472 20701 2379 1112 694 C
ATOM 1477 O ALA A 208 3.071 25.620 -4.616 1.00141.62 O
ANISOU 1477 O ALA A 208 15774 19438 18597 2609 1235 696 O
ATOM 1478 CB ALA A 208 4.311 23.957 -1.958 1.00152.48 C
ANISOU 1478 CB ALA A 208 16601 21355 19981 2426 845 892 C
ATOM 1479 N ALA A 209 1.682 25.309 -2.870 1.00164.78 N
ANISOU 1479 N ALA A 209 18943 21968 21697 2356 1019 583 N
ATOM 1480 CA ALA A 209 0.497 25.429 -3.714 1.00156.64 C
ANISOU 1480 CA ALA A 209 18211 20569 20738 2577 1062 476 C
ATOM 1481 C ALA A 209 0.332 26.850 -4.232 1.00165.70 C
ANISOU 1481 C ALA A 209 19530 21615 21814 2357 1309 469 C
ATOM 1482 O ALA A 209 -0.081 27.057 -5.379 1.00130.61 O
ANISOU 1482 O ALA A 209 15219 17045 17361 2594 1404 439 O
ATOM 1483 CB ALA A 209 -0.747 24.996 -2.943 1.00125.87 C
ANISOU 1483 CB ALA A 209 14507 16351 16968 2569 911 393 C
ATOM 1484 N GLN A 210 0.673 27.840 -3.411 1.00198.88 N
ANISOU 1484 N GLN A 210 23753 25867 25944 1896 1422 502 N
ATOM 1485 CA GLN A 210 0.699 29.232 -3.853 1.00201.79 C
ANISOU 1485 CA GLN A 210 24315 26147 26209 1650 1685 510 C
ATOM 1486 C GLN A 210 2.052 29.514 -4.507 1.00203.76 C
ANISOU 1486 C GLN A 210 24320 26784 26315 1579 1790 609 C
ATOM 1487 O GLN A 210 2.880 30.288 -4.024 1.00229.54 O
ANISOU 1487 O GLN A 210 27515 30255 29445 1140 1892 676 O
ATOM 1488 CB GLN A 210 0.428 30.171 -2.685 1.00207.03 C
ANISOU 1488 CB GLN A 210 25187 26648 26827 1169 1779 493 C
ATOM 1489 CG GLN A 210 0.242 31.624 -3.081 1.00214.57 C
ANISOU 1489 CG GLN A 210 26458 27401 27668 936 2077 491 C
ATOM 1490 CD GLN A 210 -0.041 32.510 -1.891 1.00218.24 C
ANISOU 1490 CD GLN A 210 27197 27661 28062 473 2189 466 C
ATOM 1491 OE1 GLN A 210 0.394 33.660 -1.842 1.00223.97 O
ANISOU 1491 OE1 GLN A 210 28120 28354 28623 92 2414 488 O
ATOM 1492 NE2 GLN A 210 -0.774 31.979 -0.920 1.00213.74 N
ANISOU 1492 NE2 GLN A 210 26672 26939 27600 490 2041 420 N
ATOM 1493 N ALA A 211 2.266 28.845 -5.635 1.00192.70 N
ANISOU 1493 N ALA A 211 22795 25492 24929 2010 1763 623 N
ATOM 1494 CA ALA A 211 3.475 29.024 -6.423 1.00178.82 C
ANISOU 1494 CA ALA A 211 20796 24109 23039 2034 1874 727 C
ATOM 1495 C ALA A 211 3.463 30.383 -7.120 1.00205.65 C
ANISOU 1495 C ALA A 211 24407 27402 26330 1817 2140 732 C
ATOM 1496 O ALA A 211 2.423 31.035 -7.239 1.00192.82 O
ANISOU 1496 O ALA A 211 23130 25388 24746 1793 2240 655 O
ATOM 1497 CB ALA A 211 3.606 27.906 -7.456 1.00147.20 C
ANISOU 1497 CB ALA A 211 16664 20195 19069 2596 1791 729 C
ATOM 1498 N HIS A 212 4.647 30.835 -7.538 1.00235.96 N
ANISOU 1498 N HIS A 212 28031 31607 30014 1648 2265 844 N
ATOM 1499 CA HIS A 212 4.713 31.988 -8.432 1.00245.69 C
ANISOU 1499 CA HIS A 212 29461 32758 31135 1518 2522 859 C
ATOM 1500 C HIS A 212 3.819 31.731 -9.629 1.00234.47 C
ANISOU 1500 C HIS A 212 28237 31055 29797 2015 2554 784 C
ATOM 1501 O HIS A 212 4.010 30.748 -10.352 1.00264.76 O
ANISOU 1501 O HIS A 212 31896 35032 33667 2450 2454 790 O
ATOM 1502 CB HIS A 212 6.150 32.235 -8.904 1.00250.00 C
ANISOU 1502 CB HIS A 212 29680 33803 31506 1366 2622 1006 C
ATOM 1503 CG HIS A 212 6.733 31.095 -9.684 1.00246.63 C
ANISOU 1503 CG HIS A 212 28920 33688 31099 1874 2528 1071 C
ATOM 1504 ND1 HIS A 212 7.028 29.877 -9.110 1.00249.08 N
ANISOU 1504 ND1 HIS A 212 28952 34208 31479 2104 2313 1106 N
ATOM 1505 CD2 HIS A 212 7.056 30.980 -10.995 1.00248.93 C
ANISOU 1505 CD2 HIS A 212 29150 34095 31336 2220 2637 1108 C
ATOM 1506 CE1 HIS A 212 7.516 29.064 -10.030 1.00247.74 C
ANISOU 1506 CE1 HIS A 212 28584 34255 31290 2580 2308 1164 C
ATOM 1507 NE2 HIS A 212 7.544 29.709 -11.182 1.00250.18 N
ANISOU 1507 NE2 HIS A 212 29015 34518 31524 2654 2500 1161 N
ATOM 1508 N GLN A 213 2.841 32.611 -9.836 1.00209.10 N
ANISOU 1508 N GLN A 213 25405 27450 26596 1955 2701 725 N
ATOM 1509 CA GLN A 213 1.841 32.425 -10.883 1.00162.36 C
ANISOU 1509 CA GLN A 213 19681 21265 20743 2391 2716 669 C
ATOM 1510 C GLN A 213 1.253 31.021 -10.772 1.00148.03 C
ANISOU 1510 C GLN A 213 17767 19405 19071 2772 2444 600 C
ATOM 1511 O GLN A 213 1.352 30.196 -11.681 1.00183.06 O
ANISOU 1511 O GLN A 213 22107 23937 23513 3162 2366 589 O
ATOM 1512 CB GLN A 213 2.439 32.675 -12.270 1.00158.53 C
ANISOU 1512 CB GLN A 213 19138 20950 20147 2582 2867 724 C
ATOM 1513 CG GLN A 213 3.048 34.057 -12.454 1.00167.97 C
ANISOU 1513 CG GLN A 213 20452 22189 21181 2189 3144 799 C
ATOM 1514 CD GLN A 213 4.372 34.220 -11.730 1.00178.57 C
ANISOU 1514 CD GLN A 213 21515 23922 22413 1759 3148 885 C
ATOM 1515 OE1 GLN A 213 5.365 33.581 -12.077 1.00177.08 O
ANISOU 1515 OE1 GLN A 213 20962 24143 22176 1885 3084 962 O
ATOM 1516 NE2 GLN A 213 4.388 35.071 -10.710 1.00193.55 N
ANISOU 1516 NE2 GLN A 213 23583 25708 24247 1248 3229 885 N
ATOM 1517 N TRP A 214 0.658 30.763 -9.606 1.00142.67 N
ANISOU 1517 N TRP A 214 17142 18571 18493 2630 2309 554 N
ATOM 1518 CA TRP A 214 0.440 29.398 -9.140 1.00162.37 C
ANISOU 1518 CA TRP A 214 19493 21099 21102 2856 2038 509 C
ATOM 1519 C TRP A 214 -0.364 28.578 -10.141 1.00168.15 C
ANISOU 1519 C TRP A 214 20321 21683 21884 3316 1932 448 C
ATOM 1520 O TRP A 214 -1.372 29.034 -10.686 1.00158.62 O
ANISOU 1520 O TRP A 214 19347 20233 20689 3412 1998 423 O
ATOM 1521 CB TRP A 214 -0.269 29.415 -7.782 1.00173.91 C
ANISOU 1521 CB TRP A 214 21057 22363 22657 2615 1939 469 C
ATOM 1522 CG TRP A 214 -1.434 30.360 -7.709 1.00173.18 C
ANISOU 1522 CG TRP A 214 21297 21919 22585 2523 2079 443 C
ATOM 1523 CD1 TRP A 214 -2.754 30.044 -7.846 1.00165.52 C
ANISOU 1523 CD1 TRP A 214 20492 20691 21708 2756 1997 402 C
ATOM 1524 CD2 TRP A 214 -1.383 31.775 -7.479 1.00185.46 C
ANISOU 1524 CD2 TRP A 214 23071 23353 24044 2183 2341 477 C
ATOM 1525 NE1 TRP A 214 -3.527 31.173 -7.718 1.00167.98 N
ANISOU 1525 NE1 TRP A 214 21080 20752 21994 2629 2201 427 N
ATOM 1526 CE2 TRP A 214 -2.710 32.249 -7.493 1.00167.82 C
ANISOU 1526 CE2 TRP A 214 21131 20777 21857 2286 2425 464 C
ATOM 1527 CE3 TRP A 214 -0.344 32.687 -7.266 1.00205.26 C
ANISOU 1527 CE3 TRP A 214 25568 26012 26409 1789 2520 528 C
ATOM 1528 CZ2 TRP A 214 -3.025 33.593 -7.302 1.00140.62 C
ANISOU 1528 CZ2 TRP A 214 18003 17102 18325 2058 2703 497 C
ATOM 1529 CZ3 TRP A 214 -0.660 34.020 -7.077 1.00181.97 C
ANISOU 1529 CZ3 TRP A 214 22961 22814 23366 1508 2783 542 C
ATOM 1530 CH2 TRP A 214 -1.988 34.460 -7.096 1.00141.99 C
ANISOU 1530 CH2 TRP A 214 18220 17373 18354 1667 2884 525 C
ATOM 1531 N ARG A 215 0.102 27.352 -10.377 1.00191.91 N
ANISOU 1531 N ARG A 215 23161 24854 24903 3600 1770 437 N
ATOM 1532 CA ARG A 215 -0.505 26.452 -11.349 1.00204.87 C
ANISOU 1532 CA ARG A 215 24916 26374 26550 4011 1660 372 C
ATOM 1533 C ARG A 215 -0.731 25.086 -10.717 1.00202.12 C
ANISOU 1533 C ARG A 215 24537 25980 26281 4163 1407 320 C
ATOM 1534 O ARG A 215 -1.690 24.387 -11.057 1.00196.25 O
ANISOU 1534 O ARG A 215 23974 25024 25567 4360 1264 245 O
ATOM 1535 CB ARG A 215 0.378 26.325 -12.593 1.00226.54 C
ANISOU 1535 CB ARG A 215 27573 29332 29171 4272 1775 410 C
ATOM 1536 CG ARG A 215 -0.141 25.335 -13.625 1.00240.84 C
ANISOU 1536 CG ARG A 215 29537 31022 30948 4684 1666 334 C
ATOM 1537 CD ARG A 215 0.989 24.779 -14.475 1.00247.52 C
ANISOU 1537 CD ARG A 215 30249 32122 31676 4982 1738 375 C
ATOM 1538 NE ARG A 215 0.611 23.528 -15.127 1.00230.43 N
ANISOU 1538 NE ARG A 215 28259 29824 29470 5361 1598 290 N
ATOM 1539 CZ ARG A 215 0.295 23.417 -16.413 1.00206.76 C
ANISOU 1539 CZ ARG A 215 25451 26745 26366 5606 1644 243 C
ATOM 1540 NH1 ARG A 215 -0.039 22.236 -16.914 1.00198.69 N
ANISOU 1540 NH1 ARG A 215 24632 25581 25280 5903 1508 156 N
ATOM 1541 NH2 ARG A 215 0.322 24.484 -17.200 1.00200.89 N
ANISOU 1541 NH2 ARG A 215 24720 26051 25559 5542 1829 284 N
ATOM 1542 N GLY A 216 0.151 24.700 -9.791 1.00196.07 N
ANISOU 1542 N GLY A 216 23546 25422 25529 4055 1348 373 N
ATOM 1543 CA GLY A 216 -0.029 23.435 -9.105 1.00193.96 C
ANISOU 1543 CA GLY A 216 23266 25100 25330 4191 1123 338 C
ATOM 1544 C GLY A 216 -1.288 23.406 -8.265 1.00190.11 C
ANISOU 1544 C GLY A 216 22952 24322 24960 4015 985 269 C
ATOM 1545 O GLY A 216 -1.921 22.356 -8.121 1.00199.32 O
ANISOU 1545 O GLY A 216 24233 25326 26173 4179 794 207 O
ATOM 1546 N LEU A 217 -1.671 24.555 -7.704 1.00198.35 N
ANISOU 1546 N LEU A 217 24037 25290 26035 3679 1094 285 N
ATOM 1547 CA LEU A 217 -2.946 24.649 -7.003 1.00185.41 C
ANISOU 1547 CA LEU A 217 22570 23383 24494 3542 1005 239 C
ATOM 1548 C LEU A 217 -4.118 24.451 -7.958 1.00199.90 C
ANISOU 1548 C LEU A 217 24613 25011 26329 3770 960 190 C
ATOM 1549 O LEU A 217 -5.122 23.824 -7.596 1.00211.44 O
ANISOU 1549 O LEU A 217 26176 26305 27856 3799 787 151 O
ATOM 1550 CB LEU A 217 -3.039 26.000 -6.296 1.00128.90 C
ANISOU 1550 CB LEU A 217 15461 16180 17337 3169 1184 277 C
ATOM 1551 CG LEU A 217 -4.355 26.453 -5.666 1.00140.58 C
ANISOU 1551 CG LEU A 217 17139 17386 18888 3036 1186 259 C
ATOM 1552 CD1 LEU A 217 -4.882 25.416 -4.689 1.00172.05 C
ANISOU 1552 CD1 LEU A 217 21099 21299 22975 3031 942 223 C
ATOM 1553 CD2 LEU A 217 -4.140 27.787 -4.971 1.00133.26 C
ANISOU 1553 CD2 LEU A 217 16293 16422 17916 2672 1407 298 C
ATOM 1554 N LEU A 218 -4.006 24.964 -9.187 1.00268.02 N
ANISOU 1554 N LEU A 218 33295 33671 34869 3918 1108 204 N
ATOM 1555 CA LEU A 218 -5.060 24.733 -10.171 1.00268.93 C
ANISOU 1555 CA LEU A 218 33587 33641 34953 4132 1051 173 C
ATOM 1556 C LEU A 218 -5.100 23.272 -10.599 1.00268.25 C
ANISOU 1556 C LEU A 218 33549 33537 34838 4388 834 102 C
ATOM 1557 O LEU A 218 -6.180 22.721 -10.841 1.00274.08 O
ANISOU 1557 O LEU A 218 34436 34129 35573 4457 678 63 O
ATOM 1558 CB LEU A 218 -4.866 25.647 -11.382 1.00275.31 C
ANISOU 1558 CB LEU A 218 34447 34500 35659 4227 1268 213 C
ATOM 1559 CG LEU A 218 -5.917 25.544 -12.493 1.00288.11 C
ANISOU 1559 CG LEU A 218 36234 36017 37217 4435 1225 206 C
ATOM 1560 CD1 LEU A 218 -6.308 26.926 -12.995 1.00298.79 C
ANISOU 1560 CD1 LEU A 218 37671 37331 38526 4387 1464 290 C
ATOM 1561 CD2 LEU A 218 -5.419 24.683 -13.648 1.00286.45 C
ANISOU 1561 CD2 LEU A 218 36052 35889 36896 4721 1164 151 C
ATOM 1562 N SER A 219 -3.933 22.630 -10.709 1.00254.79 N
ANISOU 1562 N SER A 219 31732 31988 33090 4531 831 95 N
ATOM 1563 CA SER A 219 -3.916 21.203 -11.006 1.00227.83 C
ANISOU 1563 CA SER A 219 28422 28513 29630 4788 650 29 C
ATOM 1564 C SER A 219 -4.536 20.398 -9.873 1.00197.08 C
ANISOU 1564 C SER A 219 24574 24475 25832 4673 432 -5 C
ATOM 1565 O SER A 219 -5.166 19.363 -10.121 1.00195.88 O
ANISOU 1565 O SER A 219 24619 24164 25643 4796 254 -74 O
ATOM 1566 CB SER A 219 -2.486 20.735 -11.274 1.00222.95 C
ANISOU 1566 CB SER A 219 27663 28111 28938 5006 731 63 C
ATOM 1567 OG SER A 219 -1.666 20.922 -10.135 1.00218.45 O
ANISOU 1567 OG SER A 219 26845 27722 28435 4830 755 139 O
ATOM 1568 N TYR A 220 -4.362 20.848 -8.629 1.00177.65 N
ANISOU 1568 N TYR A 220 21957 22067 23476 4415 443 42 N
ATOM 1569 CA TYR A 220 -5.073 20.231 -7.516 1.00162.91 C
ANISOU 1569 CA TYR A 220 20136 20058 21703 4274 250 18 C
ATOM 1570 C TYR A 220 -6.572 20.479 -7.603 1.00155.74 C
ANISOU 1570 C TYR A 220 19385 18963 20826 4167 176 -2 C
ATOM 1571 O TYR A 220 -7.365 19.626 -7.188 1.00134.67 O
ANISOU 1571 O TYR A 220 16827 16156 18186 4140 -25 -39 O
ATOM 1572 CB TYR A 220 -4.523 20.761 -6.194 1.00139.39 C
ANISOU 1572 CB TYR A 220 16960 17194 18807 4004 296 78 C
ATOM 1573 CG TYR A 220 -5.057 20.066 -4.959 1.00165.31 C
ANISOU 1573 CG TYR A 220 20266 20363 22182 3869 103 63 C
ATOM 1574 CD1 TYR A 220 -4.451 18.916 -4.468 1.00201.04 C
ANISOU 1574 CD1 TYR A 220 24749 24931 26706 3995 -34 66 C
ATOM 1575 CD2 TYR A 220 -6.154 20.571 -4.273 1.00161.16 C
ANISOU 1575 CD2 TYR A 220 19808 19693 21735 3634 77 63 C
ATOM 1576 CE1 TYR A 220 -4.931 18.282 -3.336 1.00207.57 C
ANISOU 1576 CE1 TYR A 220 25607 25649 27610 3867 -207 58 C
ATOM 1577 CE2 TYR A 220 -6.640 19.943 -3.140 1.00165.42 C
ANISOU 1577 CE2 TYR A 220 20364 20138 22351 3504 -93 55 C
ATOM 1578 CZ TYR A 220 -6.025 18.799 -2.677 1.00180.11 C
ANISOU 1578 CZ TYR A 220 22188 22034 24213 3608 -241 48 C
ATOM 1579 OH TYR A 220 -6.505 18.171 -1.551 1.00173.93 O
ANISOU 1579 OH TYR A 220 21433 21152 23501 3475 -408 45 O
ATOM 1580 N GLN A 221 -6.981 21.636 -8.134 1.00153.39 N
ANISOU 1580 N GLN A 221 19097 18674 20510 4108 343 39 N
ATOM 1581 CA GLN A 221 -8.406 21.915 -8.281 1.00169.41 C
ANISOU 1581 CA GLN A 221 21239 20580 22548 4051 293 61 C
ATOM 1582 C GLN A 221 -9.063 20.956 -9.265 1.00192.23 C
ANISOU 1582 C GLN A 221 24289 23409 25340 4228 117 10 C
ATOM 1583 O GLN A 221 -10.219 20.560 -9.078 1.00195.58 O
ANISOU 1583 O GLN A 221 24791 23752 25770 4150 -46 20 O
ATOM 1584 CB GLN A 221 -8.612 23.361 -8.729 1.00155.30 C
ANISOU 1584 CB GLN A 221 19447 18821 20738 4008 541 138 C
ATOM 1585 CG GLN A 221 -10.055 23.708 -9.041 1.00155.40 C
ANISOU 1585 CG GLN A 221 19548 18761 20734 4017 520 203 C
ATOM 1586 CD GLN A 221 -10.182 24.688 -10.189 1.00178.28 C
ANISOU 1586 CD GLN A 221 22495 21704 23539 4143 722 269 C
ATOM 1587 OE1 GLN A 221 -9.187 25.097 -10.788 1.00195.65 O
ANISOU 1587 OE1 GLN A 221 24677 23974 25688 4211 876 253 O
ATOM 1588 NE2 GLN A 221 -11.413 25.066 -10.506 1.00178.55 N
ANISOU 1588 NE2 GLN A 221 22578 21722 23542 4182 725 363 N
ATOM 1589 N ASP A 222 -8.337 20.562 -10.315 1.00211.38 N
ANISOU 1589 N ASP A 222 26775 25884 27656 4449 148 -38 N
ATOM 1590 CA ASP A 222 -8.882 19.616 -11.281 1.00215.37 C
ANISOU 1590 CA ASP A 222 27488 26312 28030 4595 -13 -102 C
ATOM 1591 C ASP A 222 -8.948 18.201 -10.725 1.00216.63 C
ANISOU 1591 C ASP A 222 27782 26343 28186 4597 -242 -178 C
ATOM 1592 O ASP A 222 -9.667 17.361 -11.278 1.00245.09 O
ANISOU 1592 O ASP A 222 31606 29841 31675 4618 -416 -233 O
ATOM 1593 CB ASP A 222 -8.049 19.634 -12.564 1.00218.39 C
ANISOU 1593 CB ASP A 222 27931 26769 28278 4845 115 -133 C
ATOM 1594 CG ASP A 222 -7.997 21.007 -13.206 1.00222.92 C
ANISOU 1594 CG ASP A 222 28407 27456 28837 4846 344 -54 C
ATOM 1595 OD1 ASP A 222 -8.974 21.773 -13.064 1.00224.62 O
ANISOU 1595 OD1 ASP A 222 28600 27657 29089 4712 367 19 O
ATOM 1596 OD2 ASP A 222 -6.977 21.321 -13.855 1.00225.46 O
ANISOU 1596 OD2 ASP A 222 28680 27885 29099 4995 514 -52 O
ATOM 1597 N SER A 223 -8.217 17.922 -9.650 1.00210.19 N
ANISOU 1597 N SER A 223 26855 25537 27473 4558 -246 -176 N
ATOM 1598 CA SER A 223 -8.176 16.583 -9.084 1.00176.26 C
ANISOU 1598 CA SER A 223 22699 21106 23166 4589 -438 -234 C
ATOM 1599 C SER A 223 -9.497 16.227 -8.413 1.00150.18 C
ANISOU 1599 C SER A 223 19476 17676 19907 4348 -643 -234 C
ATOM 1600 O SER A 223 -10.202 17.085 -7.874 1.00152.38 O
ANISOU 1600 O SER A 223 19612 18004 20282 4147 -612 -163 O
ATOM 1601 CB SER A 223 -7.036 16.468 -8.073 1.00169.28 C
ANISOU 1601 CB SER A 223 21631 20313 22373 4613 -380 -198 C
ATOM 1602 OG SER A 223 -7.227 17.361 -6.989 1.00134.81 O
ANISOU 1602 OG SER A 223 17054 16018 18149 4347 -333 -132 O
ATOM 1603 N LEU A 224 -9.830 14.935 -8.457 1.00154.97 N
ANISOU 1603 N LEU A 224 20339 18115 20428 4372 -842 -306 N
ATOM 1604 CA LEU A 224 -10.960 14.433 -7.685 1.00168.96 C
ANISOU 1604 CA LEU A 224 22182 19781 22236 4122 -1053 -298 C
ATOM 1605 C LEU A 224 -10.706 14.558 -6.188 1.00182.95 C
ANISOU 1605 C LEU A 224 23766 21569 24179 3986 -1055 -250 C
ATOM 1606 O LEU A 224 -11.654 14.682 -5.404 1.00201.60 O
ANISOU 1606 O LEU A 224 26070 23913 26615 3748 -1154 -204 O
ATOM 1607 CB LEU A 224 -11.240 12.977 -8.065 1.00160.66 C
ANISOU 1607 CB LEU A 224 21498 18522 21025 4157 -1253 -393 C
ATOM 1608 CG LEU A 224 -12.162 12.132 -7.181 1.00166.07 C
ANISOU 1608 CG LEU A 224 22311 19066 21722 3904 -1488 -397 C
ATOM 1609 CD1 LEU A 224 -13.569 12.707 -7.142 1.00166.00 C
ANISOU 1609 CD1 LEU A 224 22184 19164 21725 3623 -1581 -317 C
ATOM 1610 CD2 LEU A 224 -12.181 10.689 -7.662 1.00172.41 C
ANISOU 1610 CD2 LEU A 224 23552 19626 22331 3964 -1641 -505 C
ATOM 1611 N SER A 225 -9.435 14.542 -5.776 1.00168.30 N
ANISOU 1611 N SER A 225 21797 19776 22373 4131 -943 -244 N
ATOM 1612 CA SER A 225 -9.108 14.635 -4.357 1.00156.74 C
ANISOU 1612 CA SER A 225 20155 18352 21047 3991 -953 -194 C
ATOM 1613 C SER A 225 -9.533 15.969 -3.757 1.00158.35 C
ANISOU 1613 C SER A 225 20133 18666 21365 3757 -838 -122 C
ATOM 1614 O SER A 225 -9.826 16.041 -2.558 1.00164.17 O
ANISOU 1614 O SER A 225 20787 19388 22201 3556 -891 -86 O
ATOM 1615 CB SER A 225 -7.609 14.419 -4.151 1.00178.97 C
ANISOU 1615 CB SER A 225 22855 21284 23861 4198 -849 -171 C
ATOM 1616 OG SER A 225 -7.233 14.687 -2.811 1.00192.61 O
ANISOU 1616 OG SER A 225 24372 23107 25705 4030 -845 -106 O
ATOM 1617 N CYS A 226 -9.563 17.035 -4.562 1.00163.05 N
ANISOU 1617 N CYS A 226 20658 19357 21935 3788 -665 -97 N
ATOM 1618 CA CYS A 226 -9.967 18.336 -4.038 1.00145.62 C
ANISOU 1618 CA CYS A 226 18305 17214 19811 3594 -518 -25 C
ATOM 1619 C CYS A 226 -11.413 18.309 -3.561 1.00163.21 C
ANISOU 1619 C CYS A 226 20580 19358 22076 3422 -634 15 C
ATOM 1620 O CYS A 226 -11.735 18.845 -2.494 1.00161.90 O
ANISOU 1620 O CYS A 226 20326 19189 21999 3236 -588 67 O
ATOM 1621 CB CYS A 226 -9.784 19.415 -5.111 1.00131.88 C
ANISOU 1621 CB CYS A 226 16533 15563 18013 3690 -304 2 C
ATOM 1622 SG CYS A 226 -9.662 21.127 -4.500 1.00135.24 S
ANISOU 1622 SG CYS A 226 16826 16053 18505 3495 -29 85 S
ATOM 1623 N ARG A 227 -12.293 17.661 -4.322 1.00181.89 N
ANISOU 1623 N ARG A 227 23085 21671 24353 3468 -787 -1 N
ATOM 1624 CA ARG A 227 -13.720 17.691 -4.034 1.00187.18 C
ANISOU 1624 CA ARG A 227 23759 22333 25029 3307 -893 72 C
ATOM 1625 C ARG A 227 -14.180 16.520 -3.176 1.00168.41 C
ANISOU 1625 C ARG A 227 21465 19852 22671 3159 -1135 46 C
ATOM 1626 O ARG A 227 -15.101 16.679 -2.363 1.00172.42 O
ANISOU 1626 O ARG A 227 21902 20374 23236 2979 -1185 123 O
ATOM 1627 CB ARG A 227 -14.503 17.714 -5.354 1.00213.35 C
ANISOU 1627 CB ARG A 227 27152 25705 28206 3385 -935 98 C
ATOM 1628 CG ARG A 227 -13.966 18.739 -6.351 1.00218.02 C
ANISOU 1628 CG ARG A 227 27698 26383 28757 3562 -703 116 C
ATOM 1629 CD ARG A 227 -14.817 18.831 -7.611 1.00229.34 C
ANISOU 1629 CD ARG A 227 29192 27902 30046 3630 -745 166 C
ATOM 1630 NE ARG A 227 -14.485 17.814 -8.606 1.00228.04 N
ANISOU 1630 NE ARG A 227 29226 27683 29735 3734 -887 55 N
ATOM 1631 CZ ARG A 227 -13.720 18.034 -9.671 1.00231.69 C
ANISOU 1631 CZ ARG A 227 29750 28169 30113 3934 -765 6 C
ATOM 1632 NH1 ARG A 227 -13.473 17.052 -10.528 1.00241.75 N
ANISOU 1632 NH1 ARG A 227 31248 29370 31234 4031 -887 -98 N
ATOM 1633 NH2 ARG A 227 -13.203 19.237 -9.883 1.00238.86 N
ANISOU 1633 NH2 ARG A 227 30522 29162 31072 4031 -511 60 N
ATOM 1634 N LEU A 228 -13.550 15.351 -3.333 1.00157.23 N
ANISOU 1634 N LEU A 228 20215 18327 21199 3246 -1270 -52 N
ATOM 1635 CA LEU A 228 -13.977 14.173 -2.588 1.00160.91 C
ANISOU 1635 CA LEU A 228 20816 18662 21661 3109 -1498 -78 C
ATOM 1636 C LEU A 228 -13.774 14.342 -1.090 1.00143.07 C
ANISOU 1636 C LEU A 228 18411 16401 19547 2972 -1480 -38 C
ATOM 1637 O LEU A 228 -14.575 13.835 -0.298 1.00141.12 O
ANISOU 1637 O LEU A 228 18196 16097 19326 2780 -1632 -7 O
ATOM 1638 CB LEU A 228 -13.218 12.939 -3.082 1.00171.81 C
ANISOU 1638 CB LEU A 228 22454 19892 22933 3283 -1595 -185 C
ATOM 1639 CG LEU A 228 -13.488 11.645 -2.312 1.00173.02 C
ANISOU 1639 CG LEU A 228 22810 19864 23066 3168 -1810 -218 C
ATOM 1640 CD1 LEU A 228 -14.945 11.231 -2.458 1.00174.93 C
ANISOU 1640 CD1 LEU A 228 23173 20072 23220 2908 -2008 -194 C
ATOM 1641 CD2 LEU A 228 -12.558 10.537 -2.772 1.00176.65 C
ANISOU 1641 CD2 LEU A 228 23551 20155 23411 3412 -1838 -310 C
ATOM 1642 N VAL A 229 -12.722 15.052 -0.680 1.00143.80 N
ANISOU 1642 N VAL A 229 18346 16570 19720 3039 -1300 -31 N
ATOM 1643 CA VAL A 229 -12.495 15.264 0.745 1.00151.74 C
ANISOU 1643 CA VAL A 229 19224 17592 20840 2879 -1282 8 C
ATOM 1644 C VAL A 229 -13.604 16.121 1.337 1.00141.51 C
ANISOU 1644 C VAL A 229 17834 16330 19603 2677 -1224 92 C
ATOM 1645 O VAL A 229 -14.097 15.857 2.441 1.00124.26 O
ANISOU 1645 O VAL A 229 15631 14105 17478 2501 -1312 126 O
ATOM 1646 CB VAL A 229 -11.113 15.900 0.975 1.00144.46 C
ANISOU 1646 CB VAL A 229 18149 16788 19951 2952 -1104 10 C
ATOM 1647 CG1 VAL A 229 -11.016 16.464 2.384 1.00140.16 C
ANISOU 1647 CG1 VAL A 229 17469 16287 19499 2725 -1049 60 C
ATOM 1648 CG2 VAL A 229 -10.008 14.885 0.720 1.00147.47 C
ANISOU 1648 CG2 VAL A 229 18591 17164 20278 3170 -1171 -33 C
ATOM 1649 N PHE A 230 -14.028 17.149 0.603 1.00152.21 N
ANISOU 1649 N PHE A 230 19138 17760 20933 2721 -1063 139 N
ATOM 1650 CA PHE A 230 -15.047 18.050 1.124 1.00155.85 C
ANISOU 1650 CA PHE A 230 19521 18260 21435 2592 -958 244 C
ATOM 1651 C PHE A 230 -16.418 17.387 1.117 1.00125.97 C
ANISOU 1651 C PHE A 230 15769 14481 17613 2501 -1152 307 C
ATOM 1652 O PHE A 230 -17.222 17.602 2.033 1.00122.04 O
ANISOU 1652 O PHE A 230 15206 14001 17164 2356 -1149 394 O
ATOM 1653 CB PHE A 230 -15.039 19.354 0.326 1.00130.50 C
ANISOU 1653 CB PHE A 230 16270 15121 18193 2704 -703 295 C
ATOM 1654 CG PHE A 230 -13.833 20.219 0.598 1.00120.68 C
ANISOU 1654 CG PHE A 230 14987 13885 16979 2698 -486 260 C
ATOM 1655 CD1 PHE A 230 -12.554 19.757 0.324 1.00122.58 C
ANISOU 1655 CD1 PHE A 230 15216 14153 17205 2776 -518 174 C
ATOM 1656 CD2 PHE A 230 -13.978 21.486 1.134 1.00124.02 C
ANISOU 1656 CD2 PHE A 230 15400 14299 17425 2607 -240 325 C
ATOM 1657 CE1 PHE A 230 -11.444 20.541 0.577 1.00122.57 C
ANISOU 1657 CE1 PHE A 230 15148 14214 17210 2726 -334 164 C
ATOM 1658 CE2 PHE A 230 -12.870 22.278 1.389 1.00142.06 C
ANISOU 1658 CE2 PHE A 230 17677 16595 19705 2535 -50 292 C
ATOM 1659 CZ PHE A 230 -11.602 21.804 1.110 1.00120.58 C
ANISOU 1659 CZ PHE A 230 14899 13946 16968 2576 -109 216 C
ATOM 1660 N LEU A 231 -16.694 16.549 0.112 1.00130.44 N
ANISOU 1660 N LEU A 231 16444 15042 18075 2562 -1324 270 N
ATOM 1661 CA LEU A 231 -17.923 15.762 0.148 1.00152.16 C
ANISOU 1661 CA LEU A 231 19238 17816 20761 2408 -1547 328 C
ATOM 1662 C LEU A 231 -17.905 14.771 1.304 1.00140.17 C
ANISOU 1662 C LEU A 231 17787 16178 19293 2239 -1724 291 C
ATOM 1663 O LEU A 231 -18.929 14.550 1.966 1.00145.75 O
ANISOU 1663 O LEU A 231 18444 16930 20006 2050 -1827 382 O
ATOM 1664 CB LEU A 231 -18.119 15.030 -1.181 1.00139.15 C
ANISOU 1664 CB LEU A 231 17749 16169 18954 2465 -1700 276 C
ATOM 1665 CG LEU A 231 -19.238 13.985 -1.222 1.00108.89 C
ANISOU 1665 CG LEU A 231 14019 12347 15007 2244 -1976 312 C
ATOM 1666 CD1 LEU A 231 -20.591 14.609 -0.912 1.00107.29 C
ANISOU 1666 CD1 LEU A 231 13598 12363 14803 2106 -1964 505 C
ATOM 1667 CD2 LEU A 231 -19.270 13.283 -2.569 1.00112.05 C
ANISOU 1667 CD2 LEU A 231 14636 12720 15218 2281 -2112 236 C
ATOM 1668 N PHE A 232 -16.738 14.185 1.581 1.00131.19 N
ANISOU 1668 N PHE A 232 16749 14911 18186 2316 -1749 179 N
ATOM 1669 CA PHE A 232 -16.619 13.267 2.707 1.00115.20 C
ANISOU 1669 CA PHE A 232 14795 12769 16207 2186 -1899 156 C
ATOM 1670 C PHE A 232 -16.850 13.992 4.027 1.00111.87 C
ANISOU 1670 C PHE A 232 14197 12403 15905 2041 -1797 235 C
ATOM 1671 O PHE A 232 -17.484 13.447 4.941 1.00126.22 O
ANISOU 1671 O PHE A 232 16028 14183 17746 1857 -1929 277 O
ATOM 1672 CB PHE A 232 -15.242 12.602 2.669 1.00118.17 C
ANISOU 1672 CB PHE A 232 15286 13036 16578 2362 -1908 53 C
ATOM 1673 CG PHE A 232 -14.874 11.876 3.926 1.00130.14 C
ANISOU 1673 CG PHE A 232 16835 14459 18153 2277 -2008 50 C
ATOM 1674 CD1 PHE A 232 -15.521 10.706 4.283 1.00155.38 C
ANISOU 1674 CD1 PHE A 232 20225 17514 21299 2141 -2228 44 C
ATOM 1675 CD2 PHE A 232 -13.856 12.349 4.736 1.00119.60 C
ANISOU 1675 CD2 PHE A 232 15346 13189 16906 2317 -1885 62 C
ATOM 1676 CE1 PHE A 232 -15.170 10.031 5.436 1.00143.30 C
ANISOU 1676 CE1 PHE A 232 18736 15893 19817 2078 -2314 52 C
ATOM 1677 CE2 PHE A 232 -13.501 11.679 5.887 1.00124.65 C
ANISOU 1677 CE2 PHE A 232 16003 13771 17588 2246 -1981 75 C
ATOM 1678 CZ PHE A 232 -14.158 10.519 6.239 1.00136.42 C
ANISOU 1678 CZ PHE A 232 17690 15104 19040 2145 -2191 71 C
ATOM 1679 N MET A 233 -16.427 15.246 4.077 1.00100.27 N
ANISOU 1679 N MET A 233 12589 11015 14495 2104 -1553 260 N
ATOM 1680 CA MET A 233 -16.679 16.053 5.249 1.00 98.83 C
ANISOU 1680 CA MET A 233 12293 10864 14394 1960 -1423 332 C
ATOM 1681 C MET A 233 -18.167 16.276 5.395 1.00 99.19 C
ANISOU 1681 C MET A 233 12280 10986 14423 1865 -1423 461 C
ATOM 1682 O MET A 233 -18.721 16.132 6.473 1.00 96.68 O
ANISOU 1682 O MET A 233 11921 10666 14149 1709 -1442 525 O
ATOM 1683 CB MET A 233 -16.016 17.415 5.122 1.00117.93 C
ANISOU 1683 CB MET A 233 14641 13328 16839 2025 -1148 325 C
ATOM 1684 CG MET A 233 -16.531 18.405 6.147 1.00117.72 C
ANISOU 1684 CG MET A 233 14564 13303 16860 1875 -968 393 C
ATOM 1685 SD MET A 233 -16.161 20.124 5.780 1.00 96.63 S
ANISOU 1685 SD MET A 233 11890 10670 14154 1972 -619 457 S
ATOM 1686 CE MET A 233 -14.398 20.196 6.047 1.00165.66 C
ANISOU 1686 CE MET A 233 20642 19454 22849 2168 -610 369 C
ATOM 1687 N GLN A 234 -18.822 16.601 4.290 1.00133.09 N
ANISOU 1687 N GLN A 234 16553 15374 18640 1964 -1406 517 N
ATOM 1688 CA GLN A 234 -20.256 16.862 4.335 1.00148.84 C
ANISOU 1688 CA GLN A 234 18447 17509 20598 1895 -1410 680 C
ATOM 1689 C GLN A 234 -21.024 15.634 4.807 1.00162.58 C
ANISOU 1689 C GLN A 234 20218 19251 22305 1687 -1693 707 C
ATOM 1690 O GLN A 234 -21.978 15.751 5.591 1.00201.50 O
ANISOU 1690 O GLN A 234 25042 24272 27247 1560 -1693 838 O
ATOM 1691 CB GLN A 234 -20.756 17.316 2.962 1.00149.60 C
ANISOU 1691 CB GLN A 234 18501 17745 20594 2044 -1358 751 C
ATOM 1692 CG GLN A 234 -20.155 18.627 2.464 1.00148.82 C
ANISOU 1692 CG GLN A 234 18382 17648 20513 2245 -1055 753 C
ATOM 1693 CD GLN A 234 -20.565 19.829 3.299 1.00148.23 C
ANISOU 1693 CD GLN A 234 18239 17594 20489 2261 -780 876 C
ATOM 1694 OE1 GLN A 234 -21.413 19.729 4.185 1.00167.48 O
ANISOU 1694 OE1 GLN A 234 20609 20080 22945 2151 -806 982 O
ATOM 1695 NE2 GLN A 234 -19.962 20.978 3.014 1.00141.12 N
ANISOU 1695 NE2 GLN A 234 17380 16645 19593 2396 -499 866 N
ATOM 1696 N TYR A 235 -20.600 14.440 4.376 1.00136.59 N
ANISOU 1696 N TYR A 235 17094 15846 18956 1649 -1921 587 N
ATOM 1697 CA TYR A 235 -21.253 13.231 4.867 1.00148.93 C
ANISOU 1697 CA TYR A 235 18747 17368 20472 1420 -2185 601 C
ATOM 1698 C TYR A 235 -20.987 13.022 6.353 1.00150.34 C
ANISOU 1698 C TYR A 235 18917 17447 20760 1304 -2188 593 C
ATOM 1699 O TYR A 235 -21.906 12.681 7.103 1.00156.98 O
ANISOU 1699 O TYR A 235 19706 18343 21594 1104 -2289 692 O
ATOM 1700 CB TYR A 235 -20.811 12.002 4.069 1.00162.68 C
ANISOU 1700 CB TYR A 235 20752 18957 22104 1420 -2397 468 C
ATOM 1701 CG TYR A 235 -21.453 10.715 4.557 1.00147.56 C
ANISOU 1701 CG TYR A 235 18996 16956 20113 1155 -2665 474 C
ATOM 1702 CD1 TYR A 235 -22.752 10.711 5.056 1.00146.18 C
ANISOU 1702 CD1 TYR A 235 18679 16954 19910 913 -2751 630 C
ATOM 1703 CD2 TYR A 235 -20.758 9.513 4.538 1.00136.76 C
ANISOU 1703 CD2 TYR A 235 17932 15339 18691 1156 -2816 338 C
ATOM 1704 CE1 TYR A 235 -23.339 9.551 5.517 1.00146.03 C
ANISOU 1704 CE1 TYR A 235 18811 16863 19809 633 -2995 642 C
ATOM 1705 CE2 TYR A 235 -21.342 8.342 4.994 1.00140.59 C
ANISOU 1705 CE2 TYR A 235 18614 15713 19092 898 -3048 343 C
ATOM 1706 CZ TYR A 235 -22.634 8.370 5.482 1.00143.09 C
ANISOU 1706 CZ TYR A 235 18780 16207 19381 614 -3144 491 C
ATOM 1707 OH TYR A 235 -23.225 7.214 5.939 1.00146.77 O
ANISOU 1707 OH TYR A 235 19445 16572 19750 319 -3376 504 O
ATOM 1708 N CYS A 236 -19.752 13.239 6.813 1.00141.74 N
ANISOU 1708 N CYS A 236 17858 16241 19756 1413 -2079 493 N
ATOM 1709 CA CYS A 236 -19.496 13.044 8.238 1.00122.10 C
ANISOU 1709 CA CYS A 236 15358 13683 17352 1287 -2091 496 C
ATOM 1710 C CYS A 236 -20.293 14.027 9.090 1.00129.52 C
ANISOU 1710 C CYS A 236 16132 14737 18343 1193 -1925 624 C
ATOM 1711 O CYS A 236 -20.778 13.662 10.169 1.00100.86 O
ANISOU 1711 O CYS A 236 12488 11095 14740 1019 -2000 679 O
ATOM 1712 CB CYS A 236 -18.004 13.162 8.531 1.00101.16 C
ANISOU 1712 CB CYS A 236 12732 10948 14756 1408 -2005 392 C
ATOM 1713 SG CYS A 236 -16.999 11.900 7.724 1.00103.49 S
ANISOU 1713 SG CYS A 236 13238 11102 14982 1576 -2172 268 S
ATOM 1714 N VAL A 237 -20.483 15.254 8.604 1.00154.40 N
ANISOU 1714 N VAL A 237 19181 17991 21494 1318 -1689 684 N
ATOM 1715 CA VAL A 237 -21.219 16.251 9.377 1.00149.52 C
ANISOU 1715 CA VAL A 237 18453 17455 20902 1281 -1482 815 C
ATOM 1716 C VAL A 237 -22.706 15.910 9.417 1.00131.70 C
ANISOU 1716 C VAL A 237 16093 15357 18591 1182 -1589 981 C
ATOM 1717 O VAL A 237 -23.322 15.860 10.492 1.00122.06 O
ANISOU 1717 O VAL A 237 14819 14165 17391 1048 -1584 1071 O
ATOM 1718 CB VAL A 237 -20.973 17.660 8.804 1.00138.93 C
ANISOU 1718 CB VAL A 237 17083 16149 19555 1468 -1174 840 C
ATOM 1719 CG1 VAL A 237 -21.913 18.674 9.438 1.00134.37 C
ANISOU 1719 CG1 VAL A 237 16438 15647 18971 1483 -933 1002 C
ATOM 1720 CG2 VAL A 237 -19.527 18.077 9.016 1.00132.99 C
ANISOU 1720 CG2 VAL A 237 16412 15275 18843 1491 -1057 699 C
ATOM 1721 N ALA A 238 -23.305 15.659 8.247 1.00130.72 N
ANISOU 1721 N ALA A 238 15928 15362 18378 1231 -1693 1037 N
ATOM 1722 CA ALA A 238 -24.733 15.353 8.220 1.00138.88 C
ANISOU 1722 CA ALA A 238 16822 16616 19330 1109 -1807 1225 C
ATOM 1723 C ALA A 238 -25.040 14.052 8.951 1.00154.44 C
ANISOU 1723 C ALA A 238 18861 18533 21287 833 -2088 1206 C
ATOM 1724 O ALA A 238 -26.078 13.937 9.616 1.00186.35 O
ANISOU 1724 O ALA A 238 22772 22729 25303 685 -2125 1368 O
ATOM 1725 CB ALA A 238 -25.225 15.286 6.775 1.00144.71 C
ANISOU 1725 CB ALA A 238 17511 17525 19947 1177 -1890 1284 C
ATOM 1726 N ALA A 239 -24.135 13.076 8.862 1.00128.71 N
ANISOU 1726 N ALA A 239 15815 15054 18035 778 -2270 1023 N
ATOM 1727 CA ALA A 239 -24.284 11.843 9.625 1.00114.98 C
ANISOU 1727 CA ALA A 239 14199 13206 16282 535 -2512 993 C
ATOM 1728 C ALA A 239 -24.150 12.090 11.121 1.00123.68 C
ANISOU 1728 C ALA A 239 15252 14251 17490 469 -2414 1019 C
ATOM 1729 O ALA A 239 -24.798 11.402 11.920 1.00 97.96 O
ANISOU 1729 O ALA A 239 11997 11010 14214 247 -2558 1090 O
ATOM 1730 CB ALA A 239 -23.258 10.809 9.164 1.00106.61 C
ANISOU 1730 CB ALA A 239 13414 11900 15193 563 -2680 803 C
ATOM 1731 N ASN A 240 -23.329 13.064 11.523 1.00139.00 N
ANISOU 1731 N ASN A 240 17161 16129 19522 629 -2173 966 N
ATOM 1732 CA ASN A 240 -23.229 13.368 12.947 1.00142.39 C
ANISOU 1732 CA ASN A 240 17564 16514 20025 542 -2070 991 C
ATOM 1733 C ASN A 240 -24.515 13.997 13.467 1.00146.89 C
ANISOU 1733 C ASN A 240 17963 17273 20573 489 -1939 1190 C
ATOM 1734 O ASN A 240 -25.018 13.606 14.529 1.00165.30 O
ANISOU 1734 O ASN A 240 20274 19618 22914 315 -2000 1260 O
ATOM 1735 CB ASN A 240 -22.036 14.282 13.217 1.00132.65 C
ANISOU 1735 CB ASN A 240 16362 15182 18857 675 -1847 888 C
ATOM 1736 CG ASN A 240 -21.851 14.574 14.696 1.00131.16 C
ANISOU 1736 CG ASN A 240 16180 14941 18714 550 -1751 900 C
ATOM 1737 OD1 ASN A 240 -22.269 15.620 15.192 1.00131.21 O
ANISOU 1737 OD1 ASN A 240 16136 14998 18720 567 -1508 981 O
ATOM 1738 ND2 ASN A 240 -21.228 13.642 15.410 1.00146.40 N
ANISOU 1738 ND2 ASN A 240 18197 16762 20668 433 -1933 826 N
ATOM 1739 N TYR A 241 -25.074 14.957 12.725 1.00123.70 N
ANISOU 1739 N TYR A 241 14902 14497 17600 656 -1750 1301 N
ATOM 1740 CA TYR A 241 -26.311 15.581 13.184 1.00124.02 C
ANISOU 1740 CA TYR A 241 14770 14748 17605 666 -1594 1525 C
ATOM 1741 C TYR A 241 -27.470 14.591 13.175 1.00138.57 C
ANISOU 1741 C TYR A 241 16491 16791 19368 454 -1850 1671 C
ATOM 1742 O TYR A 241 -28.283 14.566 14.112 1.00165.70 O
ANISOU 1742 O TYR A 241 19820 20344 22793 345 -1821 1820 O
ATOM 1743 CB TYR A 241 -26.632 16.802 12.326 1.00119.80 C
ANISOU 1743 CB TYR A 241 14139 14348 17032 933 -1325 1635 C
ATOM 1744 CG TYR A 241 -25.758 17.994 12.636 1.00114.16 C
ANISOU 1744 CG TYR A 241 13552 13454 16370 1098 -1002 1545 C
ATOM 1745 CD1 TYR A 241 -25.840 18.632 13.864 1.00128.33 C
ANISOU 1745 CD1 TYR A 241 15402 15174 18184 1076 -780 1586 C
ATOM 1746 CD2 TYR A 241 -24.852 18.480 11.705 1.00110.44 C
ANISOU 1746 CD2 TYR A 241 13168 12885 15907 1249 -916 1421 C
ATOM 1747 CE1 TYR A 241 -25.046 19.723 14.159 1.00140.11 C
ANISOU 1747 CE1 TYR A 241 17058 16488 19688 1171 -487 1499 C
ATOM 1748 CE2 TYR A 241 -24.057 19.573 11.989 1.00109.26 C
ANISOU 1748 CE2 TYR A 241 13153 12579 15780 1345 -626 1345 C
ATOM 1749 CZ TYR A 241 -24.156 20.189 13.217 1.00132.20 C
ANISOU 1749 CZ TYR A 241 16138 15402 18691 1291 -416 1381 C
ATOM 1750 OH TYR A 241 -23.360 21.276 13.499 1.00127.56 O
ANISOU 1750 OH TYR A 241 15730 14644 18093 1334 -129 1298 O
ATOM 1751 N TYR A 242 -27.551 13.749 12.143 1.00136.23 N
ANISOU 1751 N TYR A 242 16228 16535 18998 369 -2104 1630 N
ATOM 1752 CA TYR A 242 -28.607 12.745 12.125 1.00136.44 C
ANISOU 1752 CA TYR A 242 16178 16745 18918 95 -2372 1759 C
ATOM 1753 C TYR A 242 -28.417 11.707 13.223 1.00145.00 C
ANISOU 1753 C TYR A 242 17409 17651 20035 -160 -2558 1683 C
ATOM 1754 O TYR A 242 -29.403 11.160 13.728 1.00156.82 O
ANISOU 1754 O TYR A 242 18805 19315 21465 -399 -2690 1835 O
ATOM 1755 CB TYR A 242 -28.684 12.078 10.753 1.00134.06 C
ANISOU 1755 CB TYR A 242 15945 16496 18495 27 -2598 1713 C
ATOM 1756 CG TYR A 242 -29.753 12.691 9.881 1.00140.37 C
ANISOU 1756 CG TYR A 242 16479 17675 19180 99 -2537 1943 C
ATOM 1757 CD1 TYR A 242 -29.500 13.839 9.145 1.00142.99 C
ANISOU 1757 CD1 TYR A 242 16731 18065 19533 422 -2286 1967 C
ATOM 1758 CD2 TYR A 242 -31.024 12.136 9.814 1.00142.31 C
ANISOU 1758 CD2 TYR A 242 16544 18248 19280 -164 -2726 2158 C
ATOM 1759 CE1 TYR A 242 -30.478 14.411 8.358 1.00158.68 C
ANISOU 1759 CE1 TYR A 242 18466 20420 21405 520 -2221 2203 C
ATOM 1760 CE2 TYR A 242 -32.008 12.701 9.028 1.00139.21 C
ANISOU 1760 CE2 TYR A 242 15866 18264 18764 -90 -2675 2404 C
ATOM 1761 CZ TYR A 242 -31.729 13.837 8.300 1.00166.11 C
ANISOU 1761 CZ TYR A 242 19199 21717 22200 271 -2419 2429 C
ATOM 1762 OH TYR A 242 -32.704 14.405 7.513 1.00191.52 O
ANISOU 1762 OH TYR A 242 22125 25358 25285 376 -2361 2698 O
ATOM 1763 N TRP A 243 -27.170 11.415 13.606 1.00140.00 N
ANISOU 1763 N TRP A 243 16998 16704 19491 -117 -2573 1469 N
ATOM 1764 CA TRP A 243 -26.962 10.507 14.729 1.00139.83 C
ANISOU 1764 CA TRP A 243 17111 16516 19500 -324 -2723 1418 C
ATOM 1765 C TRP A 243 -27.348 11.145 16.057 1.00137.38 C
ANISOU 1765 C TRP A 243 16668 16279 19251 -347 -2538 1532 C
ATOM 1766 O TRP A 243 -27.843 10.448 16.953 1.00152.98 O
ANISOU 1766 O TRP A 243 18654 18262 21208 -575 -2667 1598 O
ATOM 1767 CB TRP A 243 -25.517 10.013 14.756 1.00141.25 C
ANISOU 1767 CB TRP A 243 17539 16388 19741 -238 -2784 1194 C
ATOM 1768 CG TRP A 243 -25.384 8.683 14.092 1.00145.24 C
ANISOU 1768 CG TRP A 243 18282 16751 20154 -361 -3065 1105 C
ATOM 1769 CD1 TRP A 243 -24.717 8.404 12.936 1.00155.93 C
ANISOU 1769 CD1 TRP A 243 19795 17991 21461 -222 -3120 975 C
ATOM 1770 CD2 TRP A 243 -25.971 7.450 14.526 1.00152.01 C
ANISOU 1770 CD2 TRP A 243 19284 17547 20926 -659 -3315 1143 C
ATOM 1771 NE1 TRP A 243 -24.838 7.069 12.633 1.00163.04 N
ANISOU 1771 NE1 TRP A 243 20964 18739 22246 -403 -3378 922 N
ATOM 1772 CE2 TRP A 243 -25.603 6.462 13.593 1.00169.75 C
ANISOU 1772 CE2 TRP A 243 21818 19612 23069 -686 -3506 1022 C
ATOM 1773 CE3 TRP A 243 -26.764 7.085 15.618 1.00171.01 C
ANISOU 1773 CE3 TRP A 243 21628 20025 23323 -910 -3387 1268 C
ATOM 1774 CZ2 TRP A 243 -26.001 5.132 13.718 1.00192.91 C
ANISOU 1774 CZ2 TRP A 243 25012 22406 25878 -970 -3760 1018 C
ATOM 1775 CZ3 TRP A 243 -27.158 5.765 15.741 1.00190.30 C
ANISOU 1775 CZ3 TRP A 243 24292 22358 25655 -1200 -3651 1271 C
ATOM 1776 CH2 TRP A 243 -26.778 4.805 14.796 1.00197.45 C
ANISOU 1776 CH2 TRP A 243 25516 23056 26448 -1236 -3834 1144 C
ATOM 1777 N LEU A 244 -27.155 12.460 16.206 1.00117.88 N
ANISOU 1777 N LEU A 244 14105 13849 16836 -124 -2227 1558 N
ATOM 1778 CA LEU A 244 -27.712 13.130 17.376 1.00119.59 C
ANISOU 1778 CA LEU A 244 14218 14149 17071 -136 -2020 1691 C
ATOM 1779 C LEU A 244 -29.233 13.043 17.371 1.00131.40 C
ANISOU 1779 C LEU A 244 15484 15963 18478 -226 -2045 1950 C
ATOM 1780 O LEU A 244 -29.862 12.853 18.423 1.00164.60 O
ANISOU 1780 O LEU A 244 19623 20245 22670 -368 -2038 2068 O
ATOM 1781 CB LEU A 244 -27.262 14.591 17.420 1.00118.47 C
ANISOU 1781 CB LEU A 244 14081 13964 16967 119 -1658 1672 C
ATOM 1782 CG LEU A 244 -26.037 14.964 18.258 1.00111.39 C
ANISOU 1782 CG LEU A 244 13364 12822 16138 119 -1541 1499 C
ATOM 1783 CD1 LEU A 244 -24.757 14.427 17.640 1.00106.37 C
ANISOU 1783 CD1 LEU A 244 12858 12016 15541 135 -1705 1293 C
ATOM 1784 CD2 LEU A 244 -25.956 16.473 18.442 1.00109.78 C
ANISOU 1784 CD2 LEU A 244 13188 12600 15922 307 -1152 1532 C
ATOM 1785 N LEU A 245 -29.838 13.136 16.183 1.00125.59 N
ANISOU 1785 N LEU A 245 14609 15445 17664 -159 -2088 2054 N
ATOM 1786 CA LEU A 245 -31.285 12.982 16.087 1.00147.95 C
ANISOU 1786 CA LEU A 245 17178 18653 20384 -270 -2144 2330 C
ATOM 1787 C LEU A 245 -31.718 11.578 16.492 1.00170.52 C
ANISOU 1787 C LEU A 245 20079 21530 23181 -658 -2485 2345 C
ATOM 1788 O LEU A 245 -32.730 11.406 17.184 1.00195.49 O
ANISOU 1788 O LEU A 245 23060 24931 26286 -814 -2499 2555 O
ATOM 1789 CB LEU A 245 -31.749 13.303 14.666 1.00150.87 C
ANISOU 1789 CB LEU A 245 17395 19268 20661 -145 -2154 2434 C
ATOM 1790 CG LEU A 245 -33.242 13.161 14.371 1.00145.70 C
ANISOU 1790 CG LEU A 245 16417 19087 19857 -262 -2232 2754 C
ATOM 1791 CD1 LEU A 245 -34.054 14.044 15.302 1.00144.17 C
ANISOU 1791 CD1 LEU A 245 15996 19115 19664 -96 -1930 3007 C
ATOM 1792 CD2 LEU A 245 -33.528 13.502 12.917 1.00144.48 C
ANISOU 1792 CD2 LEU A 245 16131 19162 19602 -128 -2248 2837 C
ATOM 1793 N VAL A 246 -30.940 10.563 16.104 1.00145.57 N
ANISOU 1793 N VAL A 246 17179 18107 20022 -808 -2745 2129 N
ATOM 1794 CA VAL A 246 -31.245 9.197 16.518 1.00151.04 C
ANISOU 1794 CA VAL A 246 18000 18742 20645 -1179 -3054 2122 C
ATOM 1795 C VAL A 246 -31.105 9.061 18.025 1.00146.96 C
ANISOU 1795 C VAL A 246 17532 18097 20209 -1262 -2999 2120 C
ATOM 1796 O VAL A 246 -31.861 8.317 18.665 1.00142.18 O
ANISOU 1796 O VAL A 246 16892 17594 19535 -1555 -3153 2241 O
ATOM 1797 CB VAL A 246 -30.338 8.197 15.771 1.00162.99 C
ANISOU 1797 CB VAL A 246 19850 19946 22132 -1254 -3292 1884 C
ATOM 1798 CG1 VAL A 246 -30.541 6.786 16.301 1.00169.72 C
ANISOU 1798 CG1 VAL A 246 20922 20659 22906 -1620 -3579 1860 C
ATOM 1799 CG2 VAL A 246 -30.609 8.244 14.276 1.00166.23 C
ANISOU 1799 CG2 VAL A 246 20225 20506 22427 -1223 -3369 1899 C
ATOM 1800 N GLU A 247 -30.168 9.801 18.622 1.00151.78 N
ANISOU 1800 N GLU A 247 18220 18503 20947 -1032 -2776 1995 N
ATOM 1801 CA GLU A 247 -30.022 9.766 20.072 1.00153.48 C
ANISOU 1801 CA GLU A 247 18482 18614 21221 -1110 -2708 1997 C
ATOM 1802 C GLU A 247 -31.258 10.333 20.757 1.00151.01 C
ANISOU 1802 C GLU A 247 17906 18607 20863 -1138 -2540 2258 C
ATOM 1803 O GLU A 247 -31.787 9.740 21.709 1.00181.11 O
ANISOU 1803 O GLU A 247 21700 22467 24646 -1367 -2632 2351 O
ATOM 1804 CB GLU A 247 -28.770 10.539 20.486 1.00169.24 C
ANISOU 1804 CB GLU A 247 20606 20370 23327 -886 -2499 1822 C
ATOM 1805 CG GLU A 247 -28.518 10.558 21.982 1.00182.94 C
ANISOU 1805 CG GLU A 247 22408 21995 25104 -976 -2427 1811 C
ATOM 1806 CD GLU A 247 -28.204 9.183 22.535 1.00196.21 C
ANISOU 1806 CD GLU A 247 24267 23505 26779 -1219 -2720 1740 C
ATOM 1807 OE1 GLU A 247 -27.647 8.352 21.786 1.00206.14 O
ANISOU 1807 OE1 GLU A 247 25684 24614 28025 -1239 -2930 1620 O
ATOM 1808 OE2 GLU A 247 -28.519 8.931 23.717 1.00216.64 O
ANISOU 1808 OE2 GLU A 247 26858 26095 29361 -1376 -2726 1811 O
ATOM 1809 N GLY A 248 -31.763 11.465 20.258 1.00118.52 N
ANISOU 1809 N GLY A 248 13588 14716 16729 -890 -2284 2396 N
ATOM 1810 CA GLY A 248 -32.939 12.055 20.877 1.00127.59 C
ANISOU 1810 CA GLY A 248 14482 16176 17820 -848 -2083 2672 C
ATOM 1811 C GLY A 248 -34.186 11.208 20.699 1.00153.67 C
ANISOU 1811 C GLY A 248 17562 19828 20997 -1128 -2317 2903 C
ATOM 1812 O GLY A 248 -34.965 11.027 21.644 1.00164.36 O
ANISOU 1812 O GLY A 248 18785 21354 22308 -1269 -2293 3081 O
ATOM 1813 N VAL A 249 -34.375 10.644 19.502 1.00154.74 N
ANISOU 1813 N VAL A 249 17664 20076 21054 -1247 -2554 2902 N
ATOM 1814 CA VAL A 249 -35.539 9.791 19.276 1.00157.67 C
ANISOU 1814 CA VAL A 249 17841 20797 21271 -1588 -2807 3119 C
ATOM 1815 C VAL A 249 -35.454 8.543 20.142 1.00157.44 C
ANISOU 1815 C VAL A 249 18013 20578 21229 -1974 -3067 3039 C
ATOM 1816 O VAL A 249 -36.468 8.052 20.656 1.00171.22 O
ANISOU 1816 O VAL A 249 19583 22603 22872 -2253 -3170 3257 O
ATOM 1817 CB VAL A 249 -35.666 9.429 17.784 1.00150.54 C
ANISOU 1817 CB VAL A 249 16921 20020 20257 -1672 -3018 3106 C
ATOM 1818 CG1 VAL A 249 -36.884 8.543 17.551 1.00147.12 C
ANISOU 1818 CG1 VAL A 249 16295 19976 19626 -2095 -3297 3339 C
ATOM 1819 CG2 VAL A 249 -35.752 10.679 16.930 1.00152.41 C
ANISOU 1819 CG2 VAL A 249 16959 20448 20501 -1274 -2754 3200 C
ATOM 1820 N TYR A 250 -34.241 8.019 20.335 1.00140.55 N
ANISOU 1820 N TYR A 250 16239 17978 19186 -1986 -3167 2745 N
ATOM 1821 CA TYR A 250 -34.084 6.837 21.173 1.00139.66 C
ANISOU 1821 CA TYR A 250 16356 17649 19059 -2312 -3395 2670 C
ATOM 1822 C TYR A 250 -34.394 7.147 22.632 1.00136.96 C
ANISOU 1822 C TYR A 250 15912 17358 18767 -2318 -3227 2784 C
ATOM 1823 O TYR A 250 -35.009 6.330 23.332 1.00137.92 O
ANISOU 1823 O TYR A 250 16032 17554 18816 -2641 -3386 2894 O
ATOM 1824 CB TYR A 250 -32.671 6.278 21.023 1.00143.00 C
ANISOU 1824 CB TYR A 250 17173 17594 19565 -2248 -3504 2359 C
ATOM 1825 CG TYR A 250 -32.436 5.021 21.818 1.00154.48 C
ANISOU 1825 CG TYR A 250 18908 18793 20994 -2542 -3733 2285 C
ATOM 1826 CD1 TYR A 250 -33.224 3.897 21.619 1.00170.60 C
ANISOU 1826 CD1 TYR A 250 21032 20912 22877 -2948 -4010 2376 C
ATOM 1827 CD2 TYR A 250 -31.423 4.956 22.763 1.00173.47 C
ANISOU 1827 CD2 TYR A 250 21507 20888 23514 -2428 -3671 2136 C
ATOM 1828 CE1 TYR A 250 -33.014 2.744 22.342 1.00189.12 C
ANISOU 1828 CE1 TYR A 250 23677 22994 25187 -3211 -4204 2314 C
ATOM 1829 CE2 TYR A 250 -31.205 3.808 23.489 1.00183.05 C
ANISOU 1829 CE2 TYR A 250 22984 21871 24698 -2666 -3869 2088 C
ATOM 1830 CZ TYR A 250 -32.002 2.705 23.274 1.00193.27 C
ANISOU 1830 CZ TYR A 250 24386 23207 25840 -3046 -4127 2174 C
ATOM 1831 OH TYR A 250 -31.787 1.560 23.998 1.00206.16 O
ANISOU 1831 OH TYR A 250 26323 24579 27431 -3278 -4309 2130 O
ATOM 1832 N LEU A 251 -34.001 8.335 23.104 1.00128.21 N
ANISOU 1832 N LEU A 251 14739 16210 17764 -1979 -2898 2764 N
ATOM 1833 CA LEU A 251 -34.349 8.719 24.468 1.00133.83 C
ANISOU 1833 CA LEU A 251 15374 16979 18498 -1971 -2707 2880 C
ATOM 1834 C LEU A 251 -35.858 8.856 24.624 1.00159.05 C
ANISOU 1834 C LEU A 251 18212 20650 21572 -2068 -2649 3222 C
ATOM 1835 O LEU A 251 -36.435 8.395 25.620 1.00170.86 O
ANISOU 1835 O LEU A 251 19652 22242 23023 -2286 -2691 3352 O
ATOM 1836 CB LEU A 251 -33.641 10.025 24.837 1.00134.44 C
ANISOU 1836 CB LEU A 251 15503 16907 18672 -1606 -2348 2786 C
ATOM 1837 CG LEU A 251 -33.236 10.271 26.295 1.00144.38 C
ANISOU 1837 CG LEU A 251 16897 17983 19977 -1609 -2193 2732 C
ATOM 1838 CD1 LEU A 251 -32.274 11.448 26.383 1.00169.83 C
ANISOU 1838 CD1 LEU A 251 20261 20994 23271 -1311 -1899 2573 C
ATOM 1839 CD2 LEU A 251 -34.446 10.511 27.184 1.00123.07 C
ANISOU 1839 CD2 LEU A 251 13982 15579 17200 -1657 -2036 3006 C
ATOM 1840 N TYR A 252 -36.523 9.454 23.629 1.00164.45 N
ANISOU 1840 N TYR A 252 18632 21664 22189 -1911 -2561 3392 N
ATOM 1841 CA TYR A 252 -37.974 9.580 23.710 1.00174.63 C
ANISOU 1841 CA TYR A 252 19529 23480 23344 -1985 -2509 3761 C
ATOM 1842 C TYR A 252 -38.668 8.228 23.647 1.00173.83 C
ANISOU 1842 C TYR A 252 19377 23560 23111 -2493 -2891 3863 C
ATOM 1843 O TYR A 252 -39.737 8.057 24.241 1.00176.46 O
ANISOU 1843 O TYR A 252 19442 24263 23340 -2668 -2885 4145 O
ATOM 1844 CB TYR A 252 -38.496 10.481 22.596 1.00189.45 C
ANISOU 1844 CB TYR A 252 21126 25696 25160 -1695 -2346 3939 C
ATOM 1845 CG TYR A 252 -39.990 10.698 22.651 1.00200.54 C
ANISOU 1845 CG TYR A 252 22072 27714 26412 -1715 -2265 4366 C
ATOM 1846 CD1 TYR A 252 -40.543 11.626 23.522 1.00207.10 C
ANISOU 1846 CD1 TYR A 252 22721 28729 27238 -1417 -1887 4588 C
ATOM 1847 CD2 TYR A 252 -40.848 9.973 21.834 1.00206.57 C
ANISOU 1847 CD2 TYR A 252 22588 28888 27011 -2037 -2559 4559 C
ATOM 1848 CE1 TYR A 252 -41.906 11.827 23.578 1.00211.76 C
ANISOU 1848 CE1 TYR A 252 22862 29920 27676 -1394 -1793 5011 C
ATOM 1849 CE2 TYR A 252 -42.215 10.167 21.882 1.00220.21 C
ANISOU 1849 CE2 TYR A 252 23845 31245 28579 -2066 -2493 4984 C
ATOM 1850 CZ TYR A 252 -42.738 11.097 22.755 1.00221.70 C
ANISOU 1850 CZ TYR A 252 23825 31631 28778 -1721 -2103 5219 C
ATOM 1851 OH TYR A 252 -44.098 11.295 22.808 1.00229.42 O
ANISOU 1851 OH TYR A 252 24305 33276 29587 -1708 -2017 5674 O
ATOM 1852 N THR A 253 -38.100 7.265 22.924 1.00146.79 N
ANISOU 1852 N THR A 253 16219 19888 19668 -2741 -3212 3651 N
ATOM 1853 CA THR A 253 -38.698 5.935 22.906 1.00155.84 C
ANISOU 1853 CA THR A 253 17413 21135 20665 -3267 -3572 3723 C
ATOM 1854 C THR A 253 -38.517 5.235 24.245 1.00174.55 C
ANISOU 1854 C THR A 253 19983 23265 23072 -3488 -3636 3668 C
ATOM 1855 O THR A 253 -39.422 4.539 24.719 1.00182.74 O
ANISOU 1855 O THR A 253 20901 24549 23981 -3866 -3788 3867 O
ATOM 1856 CB THR A 253 -38.096 5.104 21.774 1.00157.98 C
ANISOU 1856 CB THR A 253 17997 21145 20883 -3449 -3865 3497 C
ATOM 1857 OG1 THR A 253 -38.405 5.718 20.518 1.00156.77 O
ANISOU 1857 OG1 THR A 253 17626 21276 20665 -3286 -3823 3583 O
ATOM 1858 CG2 THR A 253 -38.649 3.683 21.787 1.00169.52 C
ANISOU 1858 CG2 THR A 253 19612 22634 22164 -4029 -4230 3544 C
ATOM 1859 N LEU A 254 -37.352 5.405 24.873 1.00180.56 N
ANISOU 1859 N LEU A 254 21038 23570 23996 -3273 -3528 3412 N
ATOM 1860 CA LEU A 254 -37.129 4.755 26.161 1.00169.32 C
ANISOU 1860 CA LEU A 254 19810 21921 22603 -3464 -3588 3364 C
ATOM 1861 C LEU A 254 -37.947 5.398 27.276 1.00159.29 C
ANISOU 1861 C LEU A 254 18249 20952 21324 -3401 -3340 3611 C
ATOM 1862 O LEU A 254 -38.254 4.741 28.277 1.00160.14 O
ANISOU 1862 O LEU A 254 18409 21045 21393 -3668 -3427 3680 O
ATOM 1863 CB LEU A 254 -35.643 4.762 26.510 1.00161.60 C
ANISOU 1863 CB LEU A 254 19196 20427 21778 -3256 -3549 3049 C
ATOM 1864 CG LEU A 254 -34.751 3.867 25.640 1.00154.81 C
ANISOU 1864 CG LEU A 254 18692 19214 20914 -3334 -3807 2805 C
ATOM 1865 CD1 LEU A 254 -33.414 3.594 26.322 1.00148.47 C
ANISOU 1865 CD1 LEU A 254 18223 17959 20228 -3204 -3806 2565 C
ATOM 1866 CD2 LEU A 254 -35.446 2.560 25.278 1.00168.61 C
ANISOU 1866 CD2 LEU A 254 20562 21011 22490 -3801 -4138 2881 C
ATOM 1867 N LEU A 255 -38.313 6.669 27.130 1.00169.81 N
ANISOU 1867 N LEU A 255 19297 22545 22679 -3039 -3016 3752 N
ATOM 1868 CA LEU A 255 -38.999 7.347 28.217 1.00173.64 C
ANISOU 1868 CA LEU A 255 19562 23267 23147 -2912 -2729 3974 C
ATOM 1869 C LEU A 255 -40.509 7.446 28.007 1.00184.15 C
ANISOU 1869 C LEU A 255 20435 25214 24319 -3009 -2697 4373 C
ATOM 1870 O LEU A 255 -41.282 7.107 28.908 1.00191.68 O
ANISOU 1870 O LEU A 255 21240 26396 25195 -3213 -2695 4581 O
ATOM 1871 CB LEU A 255 -38.390 8.739 28.425 1.00170.17 C
ANISOU 1871 CB LEU A 255 19171 22671 22814 -2423 -2330 3882 C
ATOM 1872 CG LEU A 255 -39.021 9.578 29.538 1.00172.48 C
ANISOU 1872 CG LEU A 255 19310 23149 23073 -2227 -1968 4091 C
ATOM 1873 CD1 LEU A 255 -39.036 8.808 30.849 1.00201.10 C
ANISOU 1873 CD1 LEU A 255 23067 26654 26687 -2521 -2075 4079 C
ATOM 1874 CD2 LEU A 255 -38.321 10.927 29.703 1.00167.91 C
ANISOU 1874 CD2 LEU A 255 18885 22340 22572 -1783 -1576 3963 C
ATOM 1875 N ALA A 256 -40.952 7.899 26.835 1.00182.97 N
ANISOU 1875 N ALA A 256 20039 25373 24109 -2869 -2674 4503 N
ATOM 1876 CA ALA A 256 -42.385 8.062 26.611 1.00185.65 C
ANISOU 1876 CA ALA A 256 19889 26372 24280 -2930 -2631 4923 C
ATOM 1877 C ALA A 256 -43.088 6.718 26.457 1.00168.37 C
ANISOU 1877 C ALA A 256 17621 24422 21930 -3535 -3042 5047 C
ATOM 1878 O ALA A 256 -44.218 6.544 26.929 1.00181.37 O
ANISOU 1878 O ALA A 256 18921 26555 23439 -3728 -3037 5386 O
ATOM 1879 CB ALA A 256 -42.628 8.939 25.386 1.00198.10 C
ANISOU 1879 CB ALA A 256 21222 28225 25822 -2597 -2492 5041 C
ATOM 1880 N PHE A 257 -42.446 5.762 25.790 1.00163.79 N
ANISOU 1880 N PHE A 257 17371 23514 21346 -3845 -3387 4786 N
ATOM 1881 CA PHE A 257 -43.006 4.423 25.665 1.00176.82 C
ANISOU 1881 CA PHE A 257 19067 25292 22824 -4463 -3779 4859 C
ATOM 1882 C PHE A 257 -42.687 3.540 26.863 1.00205.43 C
ANISOU 1882 C PHE A 257 23003 28567 26483 -4750 -3895 4737 C
ATOM 1883 O PHE A 257 -43.469 2.637 27.179 1.00220.10 O
ANISOU 1883 O PHE A 257 24796 30652 28181 -5243 -4117 4913 O
ATOM 1884 CB PHE A 257 -42.494 3.757 24.384 1.00150.40 C
ANISOU 1884 CB PHE A 257 16001 21724 19422 -4670 -4082 4638 C
ATOM 1885 CG PHE A 257 -43.058 4.346 23.121 1.00167.25 C
ANISOU 1885 CG PHE A 257 17796 24304 21449 -4550 -4064 4816 C
ATOM 1886 CD1 PHE A 257 -42.572 5.542 22.614 1.00162.72 C
ANISOU 1886 CD1 PHE A 257 17138 23682 21007 -3988 -3776 4752 C
ATOM 1887 CD2 PHE A 257 -44.064 3.693 22.430 1.00191.32 C
ANISOU 1887 CD2 PHE A 257 20622 27826 24244 -5026 -4343 5053 C
ATOM 1888 CE1 PHE A 257 -43.088 6.078 21.447 1.00157.91 C
ANISOU 1888 CE1 PHE A 257 16221 23487 20291 -3864 -3757 4929 C
ATOM 1889 CE2 PHE A 257 -44.583 4.222 21.264 1.00199.90 C
ANISOU 1889 CE2 PHE A 257 21381 29358 25213 -4926 -4340 5233 C
ATOM 1890 CZ PHE A 257 -44.095 5.416 20.771 1.00179.72 C
ANISOU 1890 CZ PHE A 257 18737 26745 22802 -4325 -4043 5174 C
ATOM 1891 N SER A 258 -41.566 3.796 27.543 1.00230.03 N
ANISOU 1891 N SER A 258 26448 31162 29790 -4467 -3749 4458 N
ATOM 1892 CA SER A 258 -41.118 2.983 28.677 1.00237.36 C
ANISOU 1892 CA SER A 258 27703 31724 30760 -4693 -3853 4325 C
ATOM 1893 C SER A 258 -41.044 1.504 28.302 1.00249.02 C
ANISOU 1893 C SER A 258 29514 32987 32115 -5218 -4263 4220 C
ATOM 1894 O SER A 258 -41.408 0.622 29.081 1.00255.05 O
ANISOU 1894 O SER A 258 30386 33727 32792 -5605 -4417 4294 O
ATOM 1895 CB SER A 258 -42.020 3.194 29.897 1.00238.85 C
ANISOU 1895 CB SER A 258 27608 32246 30899 -4754 -3685 4608 C
ATOM 1896 OG SER A 258 -43.333 2.720 29.653 1.00245.39 O
ANISOU 1896 OG SER A 258 28094 33622 31521 -5146 -3840 4942 O
ATOM 1897 N VAL A 259 -40.570 1.233 27.088 1.00249.64 N
ANISOU 1897 N VAL A 259 29790 32892 32169 -5233 -4428 4045 N
ATOM 1898 CA VAL A 259 -40.519 -0.119 26.551 1.00242.43 C
ANISOU 1898 CA VAL A 259 29249 31760 31104 -5715 -4795 3940 C
ATOM 1899 C VAL A 259 -39.071 -0.567 26.405 1.00223.07 C
ANISOU 1899 C VAL A 259 27342 28642 28774 -5536 -4858 3565 C
ATOM 1900 O VAL A 259 -38.140 0.239 26.307 1.00205.88 O
ANISOU 1900 O VAL A 259 25191 26256 26779 -5058 -4655 3390 O
ATOM 1901 CB VAL A 259 -41.248 -0.228 25.197 1.00234.60 C
ANISOU 1901 CB VAL A 259 28080 31136 29920 -5951 -4965 4065 C
ATOM 1902 CG1 VAL A 259 -42.720 0.110 25.353 1.00219.67 C
ANISOU 1902 CG1 VAL A 259 25616 29972 27876 -6160 -4927 4483 C
ATOM 1903 CG2 VAL A 259 -40.589 0.682 24.174 1.00231.16 C
ANISOU 1903 CG2 VAL A 259 27599 30632 29598 -5479 -4816 3917 C
ATOM 1904 N PHE A 260 -38.891 -1.890 26.400 1.00220.18 N
ANISOU 1904 N PHE A 260 27424 27946 28286 -5933 -5136 3458 N
ATOM 1905 CA PHE A 260 -37.614 -2.512 26.055 1.00219.54 C
ANISOU 1905 CA PHE A 260 27892 27261 28263 -5797 -5230 3137 C
ATOM 1906 C PHE A 260 -37.616 -2.747 24.545 1.00226.54 C
ANISOU 1906 C PHE A 260 28914 28141 29018 -5887 -5381 3051 C
ATOM 1907 O PHE A 260 -37.835 -3.852 24.045 1.00212.91 O
ANISOU 1907 O PHE A 260 27554 26257 27087 -6314 -5640 3013 O
ATOM 1908 CB PHE A 260 -37.409 -3.803 26.842 1.00221.13 C
ANISOU 1908 CB PHE A 260 28556 27080 28384 -6129 -5416 3079 C
ATOM 1909 CG PHE A 260 -37.765 -3.696 28.312 1.00219.55 C
ANISOU 1909 CG PHE A 260 28175 27000 28244 -6185 -5312 3233 C
ATOM 1910 CD1 PHE A 260 -37.531 -2.529 29.026 1.00230.64 C
ANISOU 1910 CD1 PHE A 260 29239 28553 29841 -5766 -5023 3267 C
ATOM 1911 CD2 PHE A 260 -38.335 -4.772 28.977 1.00209.61 C
ANISOU 1911 CD2 PHE A 260 27123 25690 26829 -6676 -5500 3342 C
ATOM 1912 CE1 PHE A 260 -37.861 -2.438 30.370 1.00225.01 C
ANISOU 1912 CE1 PHE A 260 28391 27942 29163 -5822 -4921 3403 C
ATOM 1913 CE2 PHE A 260 -38.666 -4.687 30.322 1.00212.08 C
ANISOU 1913 CE2 PHE A 260 27275 26118 27189 -6730 -5403 3487 C
ATOM 1914 CZ PHE A 260 -38.429 -3.519 31.018 1.00222.61 C
ANISOU 1914 CZ PHE A 260 28264 27604 28713 -6295 -5112 3516 C
ATOM 1915 N SER A 261 -37.357 -1.666 23.813 1.00241.38 N
ANISOU 1915 N SER A 261 30524 30182 31007 -5482 -5204 3017 N
ATOM 1916 CA SER A 261 -37.429 -1.681 22.355 1.00262.08 C
ANISOU 1916 CA SER A 261 33191 32878 33509 -5525 -5313 2963 C
ATOM 1917 C SER A 261 -36.371 -2.605 21.763 1.00254.64 C
ANISOU 1917 C SER A 261 32871 31353 32529 -5517 -5461 2664 C
ATOM 1918 O SER A 261 -35.329 -2.861 22.373 1.00250.86 O
ANISOU 1918 O SER A 261 32698 30431 32184 -5275 -5400 2482 O
ATOM 1919 CB SER A 261 -37.256 -0.268 21.805 1.00252.25 C
ANISOU 1919 CB SER A 261 31550 31884 32410 -5032 -5055 2983 C
ATOM 1920 OG SER A 261 -36.025 0.279 22.235 1.00233.73 O
ANISOU 1920 OG SER A 261 29332 29178 30296 -4551 -4847 2772 O
ATOM 1921 N GLU A 262 -36.854 -3.214 20.669 1.00254.84 N
ANISOU 1921 N GLU A 262 33092 31392 32344 -5789 -5656 2629 N
ATOM 1922 CA GLU A 262 -36.286 -4.294 19.843 1.00250.13 C
ANISOU 1922 CA GLU A 262 33161 30239 31640 -5868 -5814 2376 C
ATOM 1923 C GLU A 262 -35.301 -4.017 18.711 1.00233.07 C
ANISOU 1923 C GLU A 262 31097 28039 29422 -5688 -5821 2236 C
ATOM 1924 O GLU A 262 -34.731 -2.930 18.615 1.00231.87 O
ANISOU 1924 O GLU A 262 30524 28190 29384 -5357 -5658 2280 O
ATOM 1925 CB GLU A 262 -37.422 -5.173 19.302 1.00255.51 C
ANISOU 1925 CB GLU A 262 34232 30811 32040 -6524 -6093 2437 C
ATOM 1926 CG GLU A 262 -38.248 -5.853 20.381 1.00257.71 C
ANISOU 1926 CG GLU A 262 34998 30564 32357 -6539 -6119 2322 C
ATOM 1927 CD GLU A 262 -37.418 -6.768 21.260 1.00263.47 C
ANISOU 1927 CD GLU A 262 36007 30806 33296 -5939 -5955 2071 C
ATOM 1928 OE1 GLU A 262 -36.197 -6.875 21.021 1.00254.67 O
ANISOU 1928 OE1 GLU A 262 35102 29496 32167 -5690 -5933 1896 O
ATOM 1929 OE2 GLU A 262 -37.986 -7.379 22.189 1.00268.41 O
ANISOU 1929 OE2 GLU A 262 36627 31268 34088 -5724 -5847 2064 O
ATOM 1930 N GLN A 263 -35.110 -5.027 17.855 1.00239.07 N
ANISOU 1930 N GLN A 263 32461 28391 29982 -5903 -6002 2062 N
ATOM 1931 CA GLN A 263 -34.076 -4.922 16.828 1.00232.09 C
ANISOU 1931 CA GLN A 263 31863 27191 29129 -5520 -5935 1824 C
ATOM 1932 C GLN A 263 -34.599 -4.324 15.528 1.00239.44 C
ANISOU 1932 C GLN A 263 32534 28498 29945 -5568 -5967 1877 C
ATOM 1933 O GLN A 263 -33.809 -3.810 14.728 1.00241.72 O
ANISOU 1933 O GLN A 263 32854 28667 30321 -5153 -5845 1724 O
ATOM 1934 CB GLN A 263 -33.426 -6.296 16.597 1.00216.27 C
ANISOU 1934 CB GLN A 263 30659 24565 26949 -5660 -6073 1616 C
ATOM 1935 CG GLN A 263 -32.488 -6.432 15.384 1.00209.70 C
ANISOU 1935 CG GLN A 263 30224 23392 26062 -5353 -6036 1380 C
ATOM 1936 CD GLN A 263 -31.628 -7.687 15.484 1.00216.48 C
ANISOU 1936 CD GLN A 263 31864 23580 26808 -5314 -6081 1188 C
ATOM 1937 OE1 GLN A 263 -30.732 -7.930 14.671 1.00229.66 O
ANISOU 1937 OE1 GLN A 263 33928 24898 28433 -5007 -6021 995 O
ATOM 1938 NE2 GLN A 263 -31.899 -8.488 16.503 1.00211.88 N
ANISOU 1938 NE2 GLN A 263 31513 22820 26170 -5603 -6169 1255 N
ATOM 1939 N TRP A 264 -35.909 -4.357 15.289 1.00266.65 N
ANISOU 1939 N TRP A 264 35700 32429 33188 -6061 -6126 2107 N
ATOM 1940 CA TRP A 264 -36.403 -3.730 14.066 1.00264.73 C
ANISOU 1940 CA TRP A 264 35164 32591 32829 -6079 -6151 2186 C
ATOM 1941 C TRP A 264 -36.167 -2.226 14.104 1.00253.57 C
ANISOU 1941 C TRP A 264 33166 31483 31695 -5498 -5864 2258 C
ATOM 1942 O TRP A 264 -35.710 -1.629 13.120 1.00252.88 O
ANISOU 1942 O TRP A 264 33035 31405 31643 -5181 -5773 2162 O
ATOM 1943 CB TRP A 264 -37.886 -4.040 13.854 1.00274.31 C
ANISOU 1943 CB TRP A 264 36129 34345 33752 -6734 -6382 2464 C
ATOM 1944 CG TRP A 264 -38.553 -3.031 12.960 1.00293.58 C
ANISOU 1944 CG TRP A 264 38005 37395 36145 -6647 -6340 2658 C
ATOM 1945 CD1 TRP A 264 -38.418 -2.913 11.604 1.00305.99 C
ANISOU 1945 CD1 TRP A 264 39686 39004 37571 -6623 -6403 2570 C
ATOM 1946 CD2 TRP A 264 -39.435 -1.980 13.367 1.00298.04 C
ANISOU 1946 CD2 TRP A 264 37819 38618 36804 -6530 -6204 2985 C
ATOM 1947 NE1 TRP A 264 -39.172 -1.858 11.145 1.00316.03 N
ANISOU 1947 NE1 TRP A 264 40307 40928 38842 -6507 -6326 2830 N
ATOM 1948 CE2 TRP A 264 -39.806 -1.269 12.207 1.00306.86 C
ANISOU 1948 CE2 TRP A 264 38615 40154 37825 -6432 -6194 3093 C
ATOM 1949 CE3 TRP A 264 -39.955 -1.574 14.600 1.00290.74 C
ANISOU 1949 CE3 TRP A 264 36480 37968 36022 -6482 -6076 3205 C
ATOM 1950 CZ2 TRP A 264 -40.671 -0.177 12.245 1.00304.58 C
ANISOU 1950 CZ2 TRP A 264 37607 40544 37576 -6261 -6052 3428 C
ATOM 1951 CZ3 TRP A 264 -40.812 -0.491 14.635 1.00294.39 C
ANISOU 1951 CZ3 TRP A 264 36244 39090 36519 -6313 -5925 3528 C
ATOM 1952 CH2 TRP A 264 -41.161 0.196 13.466 1.00299.36 C
ANISOU 1952 CH2 TRP A 264 36567 40124 37051 -6191 -5910 3643 C
ATOM 1953 N ILE A 265 -36.422 -1.610 15.258 1.00233.20 N
ANISOU 1953 N ILE A 265 30182 29113 29309 -5346 -5702 2416 N
ATOM 1954 CA ILE A 265 -36.135 -0.194 15.444 1.00213.71 C
ANISOU 1954 CA ILE A 265 27246 26856 27098 -4793 -5398 2471 C
ATOM 1955 C ILE A 265 -34.638 0.079 15.366 1.00194.21 C
ANISOU 1955 C ILE A 265 25057 23893 24841 -4277 -5225 2180 C
ATOM 1956 O ILE A 265 -34.220 1.115 14.841 1.00181.96 O
ANISOU 1956 O ILE A 265 23281 22437 23418 -3859 -5027 2147 O
ATOM 1957 CB ILE A 265 -36.754 0.270 16.777 1.00203.25 C
ANISOU 1957 CB ILE A 265 25520 25813 25892 -4792 -5265 2696 C
ATOM 1958 CG1 ILE A 265 -38.212 0.694 16.577 1.00193.03 C
ANISOU 1958 CG1 ILE A 265 23690 25212 24442 -5048 -5301 3052 C
ATOM 1959 CG2 ILE A 265 -35.957 1.391 17.410 1.00191.39 C
ANISOU 1959 CG2 ILE A 265 23831 24205 24684 -4213 -4937 2627 C
ATOM 1960 CD1 ILE A 265 -38.930 1.004 17.865 1.00190.11 C
ANISOU 1960 CD1 ILE A 265 22956 25138 24141 -5094 -5183 3298 C
ATOM 1961 N PHE A 266 -33.805 -0.847 15.849 1.00192.41 N
ANISOU 1961 N PHE A 266 25322 23149 24636 -4296 -5296 1982 N
ATOM 1962 CA PHE A 266 -32.359 -0.652 15.783 1.00189.49 C
ANISOU 1962 CA PHE A 266 25194 22358 24445 -3812 -5142 1735 C
ATOM 1963 C PHE A 266 -31.858 -0.718 14.343 1.00197.53 C
ANISOU 1963 C PHE A 266 26449 23240 25365 -3678 -5177 1574 C
ATOM 1964 O PHE A 266 -31.016 0.089 13.928 1.00206.35 O
ANISOU 1964 O PHE A 266 27466 24303 26635 -3225 -4986 1467 O
ATOM 1965 CB PHE A 266 -31.669 -1.700 16.655 1.00200.57 C
ANISOU 1965 CB PHE A 266 27054 23287 25864 -3864 -5215 1608 C
ATOM 1966 CG PHE A 266 -30.176 -1.631 16.620 1.00202.87 C
ANISOU 1966 CG PHE A 266 27590 23182 26309 -3385 -5076 1388 C
ATOM 1967 CD1 PHE A 266 -29.510 -0.549 17.167 1.00188.44 C
ANISOU 1967 CD1 PHE A 266 25437 21436 24725 -2969 -4835 1378 C
ATOM 1968 CD2 PHE A 266 -29.436 -2.652 16.049 1.00216.22 C
ANISOU 1968 CD2 PHE A 266 29848 24429 27877 -3357 -5178 1205 C
ATOM 1969 CE1 PHE A 266 -28.135 -0.481 17.135 1.00191.73 C
ANISOU 1969 CE1 PHE A 266 26037 21550 25262 -2561 -4718 1202 C
ATOM 1970 CE2 PHE A 266 -28.062 -2.590 16.016 1.00207.89 C
ANISOU 1970 CE2 PHE A 266 28975 23064 26950 -2891 -5040 1038 C
ATOM 1971 CZ PHE A 266 -27.410 -1.503 16.559 1.00201.97 C
ANISOU 1971 CZ PHE A 266 27844 22451 26444 -2506 -4820 1043 C
ATOM 1972 N ARG A 267 -32.390 -1.660 13.565 1.00197.47 N
ANISOU 1972 N ARG A 267 26764 23185 25082 -4093 -5417 1561 N
ATOM 1973 CA ARG A 267 -32.093 -1.738 12.141 1.00190.71 C
ANISOU 1973 CA ARG A 267 26133 22245 24084 -4029 -5464 1429 C
ATOM 1974 C ARG A 267 -32.545 -0.466 11.435 1.00173.75 C
ANISOU 1974 C ARG A 267 23444 20585 21988 -3842 -5341 1563 C
ATOM 1975 O ARG A 267 -31.854 0.045 10.541 1.00159.49 O
ANISOU 1975 O ARG A 267 21666 18704 20230 -3494 -5227 1436 O
ATOM 1976 CB ARG A 267 -32.795 -2.974 11.571 1.00210.49 C
ANISOU 1976 CB ARG A 267 29075 24663 26239 -4619 -5759 1426 C
ATOM 1977 CG ARG A 267 -32.353 -3.469 10.209 1.00226.00 C
ANISOU 1977 CG ARG A 267 31510 26364 27995 -4623 -5840 1235 C
ATOM 1978 CD ARG A 267 -32.837 -4.906 9.995 1.00239.65 C
ANISOU 1978 CD ARG A 267 33849 27831 29376 -5221 -6112 1189 C
ATOM 1979 NE ARG A 267 -34.034 -5.212 10.779 1.00239.89 N
ANISOU 1979 NE ARG A 267 33660 28183 29303 -5767 -6277 1420 N
ATOM 1980 CZ ARG A 267 -35.279 -5.084 10.330 1.00234.69 C
ANISOU 1980 CZ ARG A 267 32687 28054 28430 -6248 -6449 1634 C
ATOM 1981 NH1 ARG A 267 -36.305 -5.385 11.115 1.00234.19 N
ANISOU 1981 NH1 ARG A 267 32414 28292 28277 -6727 -6585 1857 N
ATOM 1982 NH2 ARG A 267 -35.499 -4.653 9.096 1.00225.18 N
ANISOU 1982 NH2 ARG A 267 31361 27107 27090 -6252 -6484 1641 N
ATOM 1983 N LEU A 268 -33.673 0.097 11.880 1.00184.73 N
ANISOU 1983 N LEU A 268 24328 22484 23378 -4029 -5335 1835 N
ATOM 1984 CA LEU A 268 -34.127 1.377 11.351 1.00186.83 C
ANISOU 1984 CA LEU A 268 24059 23223 23704 -3789 -5175 2001 C
ATOM 1985 C LEU A 268 -33.155 2.503 11.689 1.00167.34 C
ANISOU 1985 C LEU A 268 21412 20635 21536 -3188 -4855 1911 C
ATOM 1986 O LEU A 268 -32.856 3.340 10.832 1.00164.54 O
ANISOU 1986 O LEU A 268 20911 20383 21225 -2874 -4716 1884 O
ATOM 1987 CB LEU A 268 -35.518 1.697 11.893 1.00195.79 C
ANISOU 1987 CB LEU A 268 24696 24925 24769 -4072 -5207 2340 C
ATOM 1988 CG LEU A 268 -36.022 3.121 11.672 1.00173.27 C
ANISOU 1988 CG LEU A 268 21253 22571 22010 -3741 -4974 2565 C
ATOM 1989 CD1 LEU A 268 -36.241 3.382 10.191 1.00171.07 C
ANISOU 1989 CD1 LEU A 268 20913 22523 21563 -3736 -5042 2590 C
ATOM 1990 CD2 LEU A 268 -37.296 3.359 12.464 1.00168.64 C
ANISOU 1990 CD2 LEU A 268 20200 22504 21373 -3962 -4967 2911 C
ATOM 1991 N TYR A 269 -32.647 2.542 12.927 1.00148.33 N
ANISOU 1991 N TYR A 269 19028 18014 19319 -3044 -4737 1866 N
ATOM 1992 CA TYR A 269 -31.715 3.602 13.305 1.00144.94 C
ANISOU 1992 CA TYR A 269 18451 17478 19144 -2538 -4443 1781 C
ATOM 1993 C TYR A 269 -30.423 3.496 12.511 1.00152.10 C
ANISOU 1993 C TYR A 269 19685 18014 20093 -2242 -4404 1519 C
ATOM 1994 O TYR A 269 -29.852 4.515 12.094 1.00136.01 O
ANISOU 1994 O TYR A 269 17482 16018 18178 -1865 -4190 1473 O
ATOM 1995 CB TYR A 269 -31.409 3.542 14.804 1.00153.13 C
ANISOU 1995 CB TYR A 269 19489 18356 20337 -2505 -4358 1780 C
ATOM 1996 CG TYR A 269 -32.554 3.924 15.715 1.00162.67 C
ANISOU 1996 CG TYR A 269 20321 19941 21546 -2681 -4307 2044 C
ATOM 1997 CD1 TYR A 269 -33.628 4.666 15.245 1.00152.79 C
ANISOU 1997 CD1 TYR A 269 18657 19177 20217 -2703 -4244 2285 C
ATOM 1998 CD2 TYR A 269 -32.554 3.544 17.052 1.00179.46 C
ANISOU 1998 CD2 TYR A 269 22497 21950 23740 -2800 -4311 2070 C
ATOM 1999 CE1 TYR A 269 -34.675 5.013 16.080 1.00157.29 C
ANISOU 1999 CE1 TYR A 269 18871 20115 20776 -2822 -4173 2551 C
ATOM 2000 CE2 TYR A 269 -33.593 3.888 17.893 1.00176.23 C
ANISOU 2000 CE2 TYR A 269 21749 21887 23322 -2944 -4247 2317 C
ATOM 2001 CZ TYR A 269 -34.652 4.622 17.403 1.00155.63 C
ANISOU 2001 CZ TYR A 269 18730 19768 20635 -2945 -4172 2561 C
ATOM 2002 OH TYR A 269 -35.691 4.965 18.238 1.00158.38 O
ANISOU 2002 OH TYR A 269 18728 20486 20961 -3050 -4085 2832 O
ATOM 2003 N VAL A 270 -29.961 2.267 12.270 1.00174.70 N
ANISOU 2003 N VAL A 270 23030 20512 22837 -2404 -4596 1357 N
ATOM 2004 CA VAL A 270 -28.763 2.085 11.460 1.00175.17 C
ANISOU 2004 CA VAL A 270 23415 20236 22907 -2107 -4553 1128 C
ATOM 2005 C VAL A 270 -29.014 2.551 10.033 1.00181.05 C
ANISOU 2005 C VAL A 270 24075 21179 23537 -2051 -4551 1130 C
ATOM 2006 O VAL A 270 -28.134 3.143 9.397 1.00173.03 O
ANISOU 2006 O VAL A 270 23061 20076 22608 -1677 -4394 1011 O
ATOM 2007 CB VAL A 270 -28.300 0.616 11.511 1.00183.63 C
ANISOU 2007 CB VAL A 270 25067 20862 23841 -2277 -4739 978 C
ATOM 2008 CG1 VAL A 270 -27.172 0.374 10.520 1.00188.81 C
ANISOU 2008 CG1 VAL A 270 26073 21204 24462 -1963 -4690 767 C
ATOM 2009 CG2 VAL A 270 -27.853 0.251 12.920 1.00181.35 C
ANISOU 2009 CG2 VAL A 270 24852 20365 23687 -2241 -4708 973 C
ATOM 2010 N SER A 271 -30.223 2.317 9.511 1.00183.71 N
ANISOU 2010 N SER A 271 24317 21820 23667 -2434 -4727 1281 N
ATOM 2011 CA SER A 271 -30.533 2.841 8.184 1.00167.51 C
ANISOU 2011 CA SER A 271 22133 20018 21496 -2384 -4725 1316 C
ATOM 2012 C SER A 271 -30.642 4.363 8.178 1.00148.18 C
ANISOU 2012 C SER A 271 19165 17912 19225 -2029 -4461 1453 C
ATOM 2013 O SER A 271 -30.342 4.999 7.160 1.00166.51 O
ANISOU 2013 O SER A 271 21422 20308 21537 -1785 -4362 1414 O
ATOM 2014 CB SER A 271 -31.820 2.214 7.651 1.00166.82 C
ANISOU 2014 CB SER A 271 22044 20226 21113 -2918 -4993 1471 C
ATOM 2015 OG SER A 271 -31.633 0.837 7.375 1.00166.69 O
ANISOU 2015 OG SER A 271 22613 19838 20885 -3241 -5221 1310 O
ATOM 2016 N ILE A 272 -31.044 4.962 9.297 1.00121.28 N
ANISOU 2016 N ILE A 272 15423 14691 15967 -1985 -4329 1611 N
ATOM 2017 CA ILE A 272 -31.316 6.397 9.324 1.00122.01 C
ANISOU 2017 CA ILE A 272 15063 15110 16186 -1675 -4063 1772 C
ATOM 2018 C ILE A 272 -30.022 7.189 9.427 1.00139.63 C
ANISOU 2018 C ILE A 272 17348 17072 18633 -1217 -3801 1595 C
ATOM 2019 O ILE A 272 -29.712 8.021 8.564 1.00157.78 O
ANISOU 2019 O ILE A 272 19548 19447 20954 -938 -3649 1576 O
ATOM 2020 CB ILE A 272 -32.270 6.746 10.482 1.00121.48 C
ANISOU 2020 CB ILE A 272 14651 15340 16168 -1793 -3994 2019 C
ATOM 2021 CG1 ILE A 272 -33.692 6.270 10.182 1.00150.19 C
ANISOU 2021 CG1 ILE A 272 18090 19406 19570 -2215 -4215 2269 C
ATOM 2022 CG2 ILE A 272 -32.260 8.247 10.753 1.00109.29 C
ANISOU 2022 CG2 ILE A 272 12756 13984 14784 -1386 -3648 2137 C
ATOM 2023 CD1 ILE A 272 -34.681 6.573 11.292 1.00156.75 C
ANISOU 2023 CD1 ILE A 272 18559 20572 20428 -2325 -4143 2540 C
ATOM 2024 N GLY A 273 -29.233 6.916 10.472 1.00137.29 N
ANISOU 2024 N GLY A 273 17215 16470 18480 -1155 -3754 1470 N
ATOM 2025 CA GLY A 273 -28.148 7.816 10.823 1.00134.21 C
ANISOU 2025 CA GLY A 273 16786 15920 18287 -776 -3490 1360 C
ATOM 2026 C GLY A 273 -27.023 7.836 9.812 1.00156.24 C
ANISOU 2026 C GLY A 273 19789 18491 21084 -527 -3453 1159 C
ATOM 2027 O GLY A 273 -26.292 8.826 9.707 1.00145.25 O
ANISOU 2027 O GLY A 273 18295 17081 19814 -218 -3219 1108 O
ATOM 2028 N TRP A 274 -26.854 6.749 9.065 1.00166.91 N
ANISOU 2028 N TRP A 274 21462 19667 22289 -663 -3671 1044 N
ATOM 2029 CA TRP A 274 -25.939 6.745 7.937 1.00171.20 C
ANISOU 2029 CA TRP A 274 22204 20046 22799 -426 -3635 878 C
ATOM 2030 C TRP A 274 -26.646 6.864 6.595 1.00167.90 C
ANISOU 2030 C TRP A 274 21743 19847 22203 -505 -3713 938 C
ATOM 2031 O TRP A 274 -26.019 7.293 5.619 1.00181.31 O
ANISOU 2031 O TRP A 274 23486 21509 23895 -255 -3613 846 O
ATOM 2032 CB TRP A 274 -25.088 5.471 7.946 1.00186.90 C
ANISOU 2032 CB TRP A 274 24647 21641 24727 -447 -3780 692 C
ATOM 2033 CG TRP A 274 -24.407 5.205 9.256 1.00197.01 C
ANISOU 2033 CG TRP A 274 25980 22723 26151 -388 -3737 653 C
ATOM 2034 CD1 TRP A 274 -24.762 4.274 10.188 1.00200.77 C
ANISOU 2034 CD1 TRP A 274 26614 23075 26593 -648 -3894 684 C
ATOM 2035 CD2 TRP A 274 -23.252 5.876 9.780 1.00191.34 C
ANISOU 2035 CD2 TRP A 274 25156 21930 25614 -70 -3530 587 C
ATOM 2036 NE1 TRP A 274 -23.899 4.319 11.256 1.00191.69 N
ANISOU 2036 NE1 TRP A 274 25458 21779 25596 -489 -3798 644 N
ATOM 2037 CE2 TRP A 274 -22.962 5.293 11.030 1.00176.57 C
ANISOU 2037 CE2 TRP A 274 23376 19906 23808 -148 -3581 586 C
ATOM 2038 CE3 TRP A 274 -22.434 6.910 9.313 1.00191.37 C
ANISOU 2038 CE3 TRP A 274 25001 21996 25715 246 -3312 536 C
ATOM 2039 CZ2 TRP A 274 -21.893 5.712 11.820 1.00174.28 C
ANISOU 2039 CZ2 TRP A 274 23002 19551 23665 70 -3433 544 C
ATOM 2040 CZ3 TRP A 274 -21.372 7.322 10.098 1.00184.50 C
ANISOU 2040 CZ3 TRP A 274 24059 21055 24988 439 -3163 490 C
ATOM 2041 CH2 TRP A 274 -21.111 6.724 11.337 1.00172.21 C
ANISOU 2041 CH2 TRP A 274 22576 19373 23483 346 -3230 497 C
ATOM 2042 N GLY A 275 -27.928 6.512 6.528 1.00152.03 N
ANISOU 2042 N GLY A 275 19633 18094 20038 -856 -3890 1104 N
ATOM 2043 CA GLY A 275 -28.642 6.478 5.267 1.00146.03 C
ANISOU 2043 CA GLY A 275 18846 17572 19066 -997 -4010 1175 C
ATOM 2044 C GLY A 275 -29.169 7.819 4.799 1.00137.20 C
ANISOU 2044 C GLY A 275 17294 16850 17985 -790 -3821 1362 C
ATOM 2045 O GLY A 275 -28.878 8.241 3.676 1.00137.57 O
ANISOU 2045 O GLY A 275 17356 16940 17974 -606 -3761 1315 O
ATOM 2046 N VAL A 276 -29.969 8.486 5.639 1.00145.48 N
ANISOU 2046 N VAL A 276 17972 18191 19115 -805 -3714 1586 N
ATOM 2047 CA VAL A 276 -30.551 9.772 5.241 1.00149.86 C
ANISOU 2047 CA VAL A 276 18129 19126 19686 -575 -3505 1800 C
ATOM 2048 C VAL A 276 -29.489 10.809 4.893 1.00149.71 C
ANISOU 2048 C VAL A 276 18124 18935 19825 -127 -3216 1674 C
ATOM 2049 O VAL A 276 -29.630 11.483 3.854 1.00167.38 O
ANISOU 2049 O VAL A 276 20241 21361 21994 48 -3129 1742 O
ATOM 2050 CB VAL A 276 -31.536 10.261 6.324 1.00149.71 C
ANISOU 2050 CB VAL A 276 17752 19408 19720 -629 -3404 2064 C
ATOM 2051 CG1 VAL A 276 -32.365 11.419 5.794 1.00150.67 C
ANISOU 2051 CG1 VAL A 276 17478 19978 19793 -416 -3218 2340 C
ATOM 2052 CG2 VAL A 276 -32.426 9.117 6.784 1.00153.89 C
ANISOU 2052 CG2 VAL A 276 18307 20064 20102 -1109 -3701 2161 C
ATOM 2053 N PRO A 277 -28.430 11.007 5.690 1.00139.27 N
ANISOU 2053 N PRO A 277 16931 17288 18695 56 -3062 1508 N
ATOM 2054 CA PRO A 277 -27.398 11.972 5.284 1.00157.83 C
ANISOU 2054 CA PRO A 277 19303 19500 21165 427 -2803 1393 C
ATOM 2055 C PRO A 277 -26.778 11.646 3.943 1.00138.84 C
ANISOU 2055 C PRO A 277 17107 16985 18659 509 -2885 1239 C
ATOM 2056 O PRO A 277 -26.411 12.565 3.202 1.00152.73 O
ANISOU 2056 O PRO A 277 18791 18797 20441 779 -2693 1237 O
ATOM 2057 CB PRO A 277 -26.367 11.881 6.417 1.00161.94 C
ANISOU 2057 CB PRO A 277 19964 19707 21861 491 -2715 1236 C
ATOM 2058 CG PRO A 277 -27.143 11.409 7.582 1.00161.00 C
ANISOU 2058 CG PRO A 277 19768 19655 21751 238 -2815 1351 C
ATOM 2059 CD PRO A 277 -28.149 10.457 7.031 1.00143.54 C
ANISOU 2059 CD PRO A 277 17577 17616 19345 -75 -3103 1443 C
ATOM 2060 N LEU A 278 -26.654 10.364 3.601 1.00104.24 N
ANISOU 2060 N LEU A 278 13019 12438 14151 287 -3152 1112 N
ATOM 2061 CA LEU A 278 -26.303 10.011 2.233 1.00119.69 C
ANISOU 2061 CA LEU A 278 15189 14331 15957 332 -3241 996 C
ATOM 2062 C LEU A 278 -27.400 10.442 1.268 1.00130.21 C
ANISOU 2062 C LEU A 278 16300 16056 17119 251 -3289 1191 C
ATOM 2063 O LEU A 278 -27.115 10.946 0.171 1.00107.31 O
ANISOU 2063 O LEU A 278 13400 13212 14161 447 -3205 1164 O
ATOM 2064 CB LEU A 278 -26.065 8.502 2.141 1.00115.67 C
ANISOU 2064 CB LEU A 278 15097 13541 15312 85 -3506 834 C
ATOM 2065 CG LEU A 278 -25.522 7.884 0.854 1.00117.34 C
ANISOU 2065 CG LEU A 278 15662 13573 15347 127 -3600 664 C
ATOM 2066 CD1 LEU A 278 -24.046 8.205 0.695 1.00114.87 C
ANISOU 2066 CD1 LEU A 278 15472 12999 15176 527 -3394 485 C
ATOM 2067 CD2 LEU A 278 -25.750 6.379 0.857 1.00110.85 C
ANISOU 2067 CD2 LEU A 278 15262 12527 14330 -217 -3878 571 C
ATOM 2068 N LEU A 279 -28.663 10.314 1.698 1.00130.01 N
ANISOU 2068 N LEU A 279 16048 16341 17011 -22 -3409 1414 N
ATOM 2069 CA LEU A 279 -29.794 10.539 0.805 1.00127.53 C
ANISOU 2069 CA LEU A 279 15504 16461 16489 -157 -3506 1636 C
ATOM 2070 C LEU A 279 -29.874 11.986 0.342 1.00134.12 C
ANISOU 2070 C LEU A 279 16027 17539 17395 222 -3219 1788 C
ATOM 2071 O LEU A 279 -30.239 12.252 -0.808 1.00147.76 O
ANISOU 2071 O LEU A 279 17673 19507 18961 255 -3253 1877 O
ATOM 2072 CB LEU A 279 -31.099 10.133 1.497 1.00131.18 C
ANISOU 2072 CB LEU A 279 15739 17249 16854 -521 -3676 1876 C
ATOM 2073 CG LEU A 279 -32.406 10.594 0.843 1.00141.75 C
ANISOU 2073 CG LEU A 279 16691 19167 17999 -623 -3730 2200 C
ATOM 2074 CD1 LEU A 279 -32.632 9.890 -0.488 1.00180.24 C
ANISOU 2074 CD1 LEU A 279 21756 24140 22588 -890 -3995 2154 C
ATOM 2075 CD2 LEU A 279 -33.589 10.385 1.777 1.00134.26 C
ANISOU 2075 CD2 LEU A 279 15445 18563 17005 -905 -3823 2468 C
ATOM 2076 N PHE A 280 -29.528 12.942 1.207 1.00139.62 N
ANISOU 2076 N PHE A 280 16573 18163 18311 506 -2927 1821 N
ATOM 2077 CA PHE A 280 -29.507 14.321 0.733 1.00141.91 C
ANISOU 2077 CA PHE A 280 16652 18614 18654 880 -2626 1946 C
ATOM 2078 C PHE A 280 -28.103 14.858 0.489 1.00134.78 C
ANISOU 2078 C PHE A 280 15957 17358 17896 1184 -2412 1711 C
ATOM 2079 O PHE A 280 -27.967 15.965 -0.045 1.00131.69 O
ANISOU 2079 O PHE A 280 15456 17051 17528 1482 -2165 1785 O
ATOM 2080 CB PHE A 280 -30.258 15.249 1.702 1.00157.68 C
ANISOU 2080 CB PHE A 280 18335 20835 20743 1014 -2391 2203 C
ATOM 2081 CG PHE A 280 -29.582 15.440 3.027 1.00151.23 C
ANISOU 2081 CG PHE A 280 17619 19705 20136 1078 -2228 2078 C
ATOM 2082 CD1 PHE A 280 -28.648 16.449 3.210 1.00152.71 C
ANISOU 2082 CD1 PHE A 280 17888 19661 20475 1390 -1915 1974 C
ATOM 2083 CD2 PHE A 280 -29.906 14.634 4.102 1.00143.46 C
ANISOU 2083 CD2 PHE A 280 16651 18678 19180 802 -2386 2079 C
ATOM 2084 CE1 PHE A 280 -28.035 16.630 4.431 1.00153.44 C
ANISOU 2084 CE1 PHE A 280 18076 19496 20730 1406 -1778 1867 C
ATOM 2085 CE2 PHE A 280 -29.300 14.815 5.323 1.00141.03 C
ANISOU 2085 CE2 PHE A 280 16432 18106 19047 851 -2243 1975 C
ATOM 2086 CZ PHE A 280 -28.364 15.812 5.489 1.00148.58 C
ANISOU 2086 CZ PHE A 280 17465 18847 20141 1145 -1944 1869 C
ATOM 2087 N VAL A 281 -27.062 14.112 0.855 1.00148.03 N
ANISOU 2087 N VAL A 281 17925 18664 19657 1122 -2495 1449 N
ATOM 2088 CA VAL A 281 -25.702 14.586 0.622 1.00138.06 C
ANISOU 2088 CA VAL A 281 16821 17123 18513 1392 -2302 1249 C
ATOM 2089 C VAL A 281 -25.235 14.241 -0.790 1.00141.83 C
ANISOU 2089 C VAL A 281 17482 17553 18855 1455 -2395 1125 C
ATOM 2090 O VAL A 281 -24.522 15.026 -1.425 1.00146.35 O
ANISOU 2090 O VAL A 281 18063 18077 19467 1723 -2192 1071 O
ATOM 2091 CB VAL A 281 -24.757 14.033 1.707 1.00123.90 C
ANISOU 2091 CB VAL A 281 15206 15004 16865 1342 -2319 1064 C
ATOM 2092 CG1 VAL A 281 -23.402 13.675 1.127 1.00120.34 C
ANISOU 2092 CG1 VAL A 281 15010 14284 16429 1487 -2316 828 C
ATOM 2093 CG2 VAL A 281 -24.591 15.058 2.824 1.00117.60 C
ANISOU 2093 CG2 VAL A 281 14256 14187 16238 1465 -2049 1130 C
ATOM 2094 N VAL A 282 -25.631 13.072 -1.312 1.00148.62 N
ANISOU 2094 N VAL A 282 18516 18419 19535 1195 -2692 1079 N
ATOM 2095 CA VAL A 282 -25.265 12.714 -2.689 1.00148.47 C
ANISOU 2095 CA VAL A 282 18709 18355 19349 1239 -2779 964 C
ATOM 2096 C VAL A 282 -25.759 13.738 -3.710 1.00148.16 C
ANISOU 2096 C VAL A 282 18445 18623 19224 1408 -2651 1129 C
ATOM 2097 O VAL A 282 -24.957 14.159 -4.567 1.00147.93 O
ANISOU 2097 O VAL A 282 18515 18499 19192 1651 -2518 1024 O
ATOM 2098 CB VAL A 282 -25.744 11.285 -3.009 1.00145.93 C
ANISOU 2098 CB VAL A 282 18658 17981 18807 874 -3120 900 C
ATOM 2099 CG1 VAL A 282 -25.531 10.969 -4.478 1.00143.98 C
ANISOU 2099 CG1 VAL A 282 18641 17718 18345 894 -3205 803 C
ATOM 2100 CG2 VAL A 282 -25.008 10.279 -2.138 1.00152.20 C
ANISOU 2100 CG2 VAL A 282 19750 18398 19682 792 -3204 712 C
ATOM 2101 N PRO A 283 -27.028 14.196 -3.680 1.00139.14 N
ANISOU 2101 N PRO A 283 16992 17869 18005 1318 -2669 1404 N
ATOM 2102 CA PRO A 283 -27.439 15.214 -4.656 1.00134.52 C
ANISOU 2102 CA PRO A 283 16196 17580 17336 1533 -2522 1582 C
ATOM 2103 C PRO A 283 -26.617 16.482 -4.579 1.00138.08 C
ANISOU 2103 C PRO A 283 16594 17900 17971 1930 -2155 1556 C
ATOM 2104 O PRO A 283 -26.406 17.140 -5.612 1.00138.57 O
ANISOU 2104 O PRO A 283 16643 18040 17968 2145 -2029 1582 O
ATOM 2105 CB PRO A 283 -28.905 15.476 -4.278 1.00139.66 C
ANISOU 2105 CB PRO A 283 16487 18672 17906 1398 -2572 1913 C
ATOM 2106 CG PRO A 283 -29.349 14.232 -3.611 1.00137.00 C
ANISOU 2106 CG PRO A 283 16246 18302 17506 987 -2869 1874 C
ATOM 2107 CD PRO A 283 -28.154 13.754 -2.846 1.00137.74 C
ANISOU 2107 CD PRO A 283 16641 17907 17786 1021 -2832 1583 C
ATOM 2108 N TRP A 284 -26.145 16.860 -3.389 1.00151.38 N
ANISOU 2108 N TRP A 284 18265 19387 19866 2011 -1978 1509 N
ATOM 2109 CA TRP A 284 -25.294 18.044 -3.273 1.00151.12 C
ANISOU 2109 CA TRP A 284 18232 19201 19983 2326 -1632 1467 C
ATOM 2110 C TRP A 284 -23.994 17.872 -4.042 1.00153.04 C
ANISOU 2110 C TRP A 284 18715 19197 20234 2443 -1609 1223 C
ATOM 2111 O TRP A 284 -23.478 18.845 -4.604 1.00151.68 O
ANISOU 2111 O TRP A 284 18535 19009 20086 2691 -1367 1226 O
ATOM 2112 CB TRP A 284 -25.010 18.330 -1.801 1.00150.23 C
ANISOU 2112 CB TRP A 284 18102 18917 20060 2314 -1487 1442 C
ATOM 2113 CG TRP A 284 -24.187 19.559 -1.557 1.00146.86 C
ANISOU 2113 CG TRP A 284 17706 18334 19761 2565 -1133 1406 C
ATOM 2114 CD1 TRP A 284 -24.645 20.836 -1.417 1.00146.46 C
ANISOU 2114 CD1 TRP A 284 17533 18389 19726 2770 -829 1597 C
ATOM 2115 CD2 TRP A 284 -22.764 19.625 -1.398 1.00156.28 C
ANISOU 2115 CD2 TRP A 284 19080 19240 21060 2621 -1038 1177 C
ATOM 2116 NE1 TRP A 284 -23.598 21.694 -1.191 1.00149.99 N
ANISOU 2116 NE1 TRP A 284 18112 18603 20274 2911 -556 1482 N
ATOM 2117 CE2 TRP A 284 -22.432 20.976 -1.174 1.00157.31 C
ANISOU 2117 CE2 TRP A 284 19196 19316 21258 2809 -689 1231 C
ATOM 2118 CE3 TRP A 284 -21.739 18.675 -1.429 1.00166.91 C
ANISOU 2118 CE3 TRP A 284 20602 20383 22432 2538 -1204 948 C
ATOM 2119 CZ2 TRP A 284 -21.119 21.400 -0.980 1.00177.30 C
ANISOU 2119 CZ2 TRP A 284 21860 21629 23876 2860 -526 1064 C
ATOM 2120 CZ3 TRP A 284 -20.436 19.098 -1.238 1.00178.71 C
ANISOU 2120 CZ3 TRP A 284 22187 21691 24022 2639 -1033 804 C
ATOM 2121 CH2 TRP A 284 -20.138 20.448 -1.017 1.00178.16 C
ANISOU 2121 CH2 TRP A 284 22078 21603 24013 2772 -710 861 C
ATOM 2122 N GLY A 285 -23.452 16.652 -4.082 1.00150.92 N
ANISOU 2122 N GLY A 285 18675 18736 19933 2282 -1841 1022 N
ATOM 2123 CA GLY A 285 -22.271 16.420 -4.890 1.00151.12 C
ANISOU 2123 CA GLY A 285 18922 18562 19935 2424 -1816 816 C
ATOM 2124 C GLY A 285 -22.573 16.366 -6.372 1.00157.67 C
ANISOU 2124 C GLY A 285 19805 19541 20560 2469 -1891 842 C
ATOM 2125 O GLY A 285 -21.771 16.835 -7.192 1.00157.59 O
ANISOU 2125 O GLY A 285 19868 19469 20539 2690 -1740 761 O
ATOM 2126 N ILE A 286 -23.745 15.838 -6.738 1.00165.36 N
ANISOU 2126 N ILE A 286 20729 20743 21355 2245 -2121 969 N
ATOM 2127 CA ILE A 286 -24.129 15.811 -8.149 1.00157.49 C
ANISOU 2127 CA ILE A 286 19770 19936 20133 2251 -2209 1016 C
ATOM 2128 C ILE A 286 -24.262 17.232 -8.686 1.00148.42 C
ANISOU 2128 C ILE A 286 18390 18992 19010 2541 -1935 1188 C
ATOM 2129 O ILE A 286 -23.678 17.587 -9.719 1.00150.05 O
ANISOU 2129 O ILE A 286 18692 19169 19151 2730 -1835 1122 O
ATOM 2130 CB ILE A 286 -25.435 15.017 -8.333 1.00156.73 C
ANISOU 2130 CB ILE A 286 19628 20103 19818 1896 -2520 1153 C
ATOM 2131 CG1 ILE A 286 -25.286 13.602 -7.771 1.00158.45 C
ANISOU 2131 CG1 ILE A 286 20136 20071 19999 1594 -2775 978 C
ATOM 2132 CG2 ILE A 286 -25.834 14.977 -9.802 1.00160.96 C
ANISOU 2132 CG2 ILE A 286 20208 20862 20090 1865 -2629 1208 C
ATOM 2133 CD1 ILE A 286 -26.582 12.818 -7.743 1.00153.93 C
ANISOU 2133 CD1 ILE A 286 19519 19751 19215 1175 -3082 1120 C
ATOM 2134 N VAL A 287 -25.013 18.075 -7.972 1.00129.11 N
ANISOU 2134 N VAL A 287 15662 16740 16655 2599 -1789 1417 N
ATOM 2135 CA VAL A 287 -25.120 19.481 -8.347 1.00120.05 C
ANISOU 2135 CA VAL A 287 14339 15737 15536 2908 -1482 1592 C
ATOM 2136 C VAL A 287 -23.762 20.157 -8.247 1.00137.96 C
ANISOU 2136 C VAL A 287 16755 17695 17969 3141 -1205 1414 C
ATOM 2137 O VAL A 287 -23.452 21.070 -9.023 1.00151.41 O
ANISOU 2137 O VAL A 287 18452 19430 19646 3381 -990 1460 O
ATOM 2138 CB VAL A 287 -26.171 20.185 -7.467 1.00107.16 C
ANISOU 2138 CB VAL A 287 12422 14334 13961 2947 -1352 1873 C
ATOM 2139 CG1 VAL A 287 -26.282 21.660 -7.826 1.00107.36 C
ANISOU 2139 CG1 VAL A 287 12324 14466 14001 3302 -997 2065 C
ATOM 2140 CG2 VAL A 287 -27.523 19.499 -7.597 1.00109.60 C
ANISOU 2140 CG2 VAL A 287 12537 15019 14085 2693 -1638 2080 C
ATOM 2141 N LYS A 288 -22.922 19.709 -7.310 1.00147.77 N
ANISOU 2141 N LYS A 288 18127 18653 19366 3058 -1213 1220 N
ATOM 2142 CA LYS A 288 -21.610 20.322 -7.147 1.00171.97 C
ANISOU 2142 CA LYS A 288 21300 21473 22569 3230 -968 1069 C
ATOM 2143 C LYS A 288 -20.706 20.071 -8.348 1.00188.23 C
ANISOU 2143 C LYS A 288 23530 23452 24538 3343 -985 911 C
ATOM 2144 O LYS A 288 -19.828 20.893 -8.631 1.00191.08 O
ANISOU 2144 O LYS A 288 23922 23726 24955 3529 -740 865 O
ATOM 2145 CB LYS A 288 -20.957 19.831 -5.855 1.00160.11 C
ANISOU 2145 CB LYS A 288 19864 19742 21227 3099 -1001 925 C
ATOM 2146 CG LYS A 288 -21.065 20.818 -4.697 1.00141.82 C
ANISOU 2146 CG LYS A 288 17439 17390 19055 3129 -755 1025 C
ATOM 2147 CD LYS A 288 -20.443 22.162 -5.048 1.00138.71 C
ANISOU 2147 CD LYS A 288 17064 16946 18693 3348 -412 1049 C
ATOM 2148 CE LYS A 288 -20.561 23.147 -3.896 1.00135.82 C
ANISOU 2148 CE LYS A 288 16666 16505 18435 3356 -150 1138 C
ATOM 2149 NZ LYS A 288 -19.769 24.386 -4.127 1.00135.03 N
ANISOU 2149 NZ LYS A 288 16660 16291 18353 3506 185 1124 N
ATOM 2150 N TYR A 289 -20.884 18.954 -9.066 1.00174.14 N
ANISOU 2150 N TYR A 289 21880 21688 22595 3223 -1257 828 N
ATOM 2151 CA TYR A 289 -20.212 18.886 -10.362 1.00155.22 C
ANISOU 2151 CA TYR A 289 19639 19261 20075 3368 -1235 722 C
ATOM 2152 C TYR A 289 -20.971 19.658 -11.432 1.00166.93 C
ANISOU 2152 C TYR A 289 21003 21011 21411 3478 -1167 908 C
ATOM 2153 O TYR A 289 -20.357 20.365 -12.239 1.00172.11 O
ANISOU 2153 O TYR A 289 21691 21657 22044 3694 -973 892 O
ATOM 2154 CB TYR A 289 -20.017 17.448 -10.843 1.00147.57 C
ANISOU 2154 CB TYR A 289 18938 18175 18957 3226 -1513 549 C
ATOM 2155 CG TYR A 289 -19.584 17.431 -12.300 1.00160.22 C
ANISOU 2155 CG TYR A 289 20699 19794 20383 3374 -1491 477 C
ATOM 2156 CD1 TYR A 289 -18.300 17.819 -12.664 1.00162.14 C
ANISOU 2156 CD1 TYR A 289 21019 19896 20690 3619 -1277 357 C
ATOM 2157 CD2 TYR A 289 -20.469 17.076 -13.313 1.00185.58 C
ANISOU 2157 CD2 TYR A 289 23967 23195 23349 3256 -1677 547 C
ATOM 2158 CE1 TYR A 289 -17.900 17.832 -13.987 1.00177.15 C
ANISOU 2158 CE1 TYR A 289 23063 21819 22427 3768 -1239 299 C
ATOM 2159 CE2 TYR A 289 -20.076 17.086 -14.643 1.00194.41 C
ANISOU 2159 CE2 TYR A 289 25245 24329 24292 3389 -1648 482 C
ATOM 2160 CZ TYR A 289 -18.790 17.464 -14.973 1.00191.05 C
ANISOU 2160 CZ TYR A 289 24906 23739 23947 3658 -1422 354 C
ATOM 2161 OH TYR A 289 -18.392 17.475 -16.290 1.00197.95 O
ANISOU 2161 OH TYR A 289 25940 24631 24641 3800 -1381 293 O
ATOM 2162 N LEU A 290 -22.302 19.526 -11.468 1.00163.70 N
ANISOU 2162 N LEU A 290 20443 20868 20887 3332 -1326 1103 N
ATOM 2163 CA LEU A 290 -23.059 20.146 -12.552 1.00169.01 C
ANISOU 2163 CA LEU A 290 20987 21845 21384 3436 -1294 1304 C
ATOM 2164 C LEU A 290 -22.924 21.661 -12.533 1.00190.53 C
ANISOU 2164 C LEU A 290 23568 24610 24215 3739 -926 1457 C
ATOM 2165 O LEU A 290 -22.989 22.305 -13.587 1.00182.36 O
ANISOU 2165 O LEU A 290 22510 23715 23062 3921 -814 1554 O
ATOM 2166 CB LEU A 290 -24.530 19.741 -12.473 1.00149.26 C
ANISOU 2166 CB LEU A 290 18296 19683 18735 3209 -1531 1526 C
ATOM 2167 CG LEU A 290 -24.833 18.248 -12.617 1.00144.15 C
ANISOU 2167 CG LEU A 290 17828 19022 17921 2848 -1912 1401 C
ATOM 2168 CD1 LEU A 290 -26.334 18.008 -12.653 1.00149.16 C
ANISOU 2168 CD1 LEU A 290 18225 20076 18375 2601 -2134 1667 C
ATOM 2169 CD2 LEU A 290 -24.160 17.672 -13.854 1.00146.33 C
ANISOU 2169 CD2 LEU A 290 18408 19174 18019 2854 -2007 1203 C
ATOM 2170 N TYR A 291 -22.719 22.241 -11.355 1.00222.11 N
ANISOU 2170 N TYR A 291 27505 28469 28417 3787 -728 1476 N
ATOM 2171 CA TYR A 291 -22.481 23.668 -11.218 1.00230.10 C
ANISOU 2171 CA TYR A 291 28468 29438 29520 4045 -352 1590 C
ATOM 2172 C TYR A 291 -21.528 23.879 -10.052 1.00229.76 C
ANISOU 2172 C TYR A 291 28521 29090 29687 4009 -194 1430 C
ATOM 2173 O TYR A 291 -21.519 23.102 -9.094 1.00228.00 O
ANISOU 2173 O TYR A 291 28303 28776 29552 3810 -357 1338 O
ATOM 2174 CB TYR A 291 -23.788 24.445 -11.006 1.00237.86 C
ANISOU 2174 CB TYR A 291 29224 30699 30455 4159 -235 1921 C
ATOM 2175 CG TYR A 291 -24.737 24.374 -12.183 1.00257.54 C
ANISOU 2175 CG TYR A 291 31575 33562 32717 4207 -373 2127 C
ATOM 2176 CD1 TYR A 291 -24.661 25.298 -13.217 1.00268.72 C
ANISOU 2176 CD1 TYR A 291 32995 35071 34036 4476 -165 2246 C
ATOM 2177 CD2 TYR A 291 -25.703 23.379 -12.263 1.00265.90 C
ANISOU 2177 CD2 TYR A 291 32500 34892 33637 3957 -717 2212 C
ATOM 2178 CE1 TYR A 291 -25.523 25.235 -14.297 1.00278.28 C
ANISOU 2178 CE1 TYR A 291 34062 36652 35019 4514 -300 2451 C
ATOM 2179 CE2 TYR A 291 -26.568 23.307 -13.339 1.00273.17 C
ANISOU 2179 CE2 TYR A 291 33278 36194 34318 3957 -862 2413 C
ATOM 2180 CZ TYR A 291 -26.474 24.238 -14.352 1.00281.24 C
ANISOU 2180 CZ TYR A 291 34288 37320 35249 4245 -655 2535 C
ATOM 2181 OH TYR A 291 -27.335 24.170 -15.424 1.00290.18 O
ANISOU 2181 OH TYR A 291 35265 38865 36127 4241 -808 2752 O
ATOM 2182 N GLU A 292 -20.722 24.936 -10.150 1.00208.72 N
ANISOU 2182 N GLU A 292 25940 26280 27085 4182 121 1405 N
ATOM 2183 CA GLU A 292 -19.672 25.232 -9.175 1.00195.37 C
ANISOU 2183 CA GLU A 292 24350 24325 25557 4120 282 1252 C
ATOM 2184 C GLU A 292 -18.672 24.085 -9.045 1.00177.27 C
ANISOU 2184 C GLU A 292 22147 21897 23311 3969 64 1000 C
ATOM 2185 O GLU A 292 -18.091 23.875 -7.977 1.00182.51 O
ANISOU 2185 O GLU A 292 22835 22409 24101 3841 67 894 O
ATOM 2186 CB GLU A 292 -20.260 25.578 -7.803 1.00189.73 C
ANISOU 2186 CB GLU A 292 23574 23567 24947 4041 375 1354 C
ATOM 2187 CG GLU A 292 -21.222 26.744 -7.819 1.00191.79 C
ANISOU 2187 CG GLU A 292 23773 23941 25157 4241 641 1623 C
ATOM 2188 CD GLU A 292 -21.938 26.917 -6.498 1.00209.17 C
ANISOU 2188 CD GLU A 292 25913 26126 27435 4176 707 1736 C
ATOM 2189 OE1 GLU A 292 -21.389 26.493 -5.458 1.00217.75 O
ANISOU 2189 OE1 GLU A 292 27058 27038 28640 3977 645 1577 O
ATOM 2190 OE2 GLU A 292 -23.056 27.468 -6.503 1.00214.95 O
ANISOU 2190 OE2 GLU A 292 26533 27041 28099 4339 827 1998 O
ATOM 2191 N ASP A 293 -18.465 23.327 -10.125 1.00156.71 N
ANISOU 2191 N ASP A 293 19606 19348 20587 3997 -118 912 N
ATOM 2192 CA ASP A 293 -17.374 22.357 -10.146 1.00163.34 C
ANISOU 2192 CA ASP A 293 20570 20042 21449 3940 -254 687 C
ATOM 2193 C ASP A 293 -16.014 23.038 -10.097 1.00179.34 C
ANISOU 2193 C ASP A 293 22638 21949 23554 4032 -7 593 C
ATOM 2194 O ASP A 293 -15.044 22.429 -9.634 1.00174.95 O
ANISOU 2194 O ASP A 293 22125 21284 23063 3979 -64 446 O
ATOM 2195 CB ASP A 293 -17.475 21.467 -11.388 1.00163.30 C
ANISOU 2195 CB ASP A 293 20679 20104 21265 3972 -464 620 C
ATOM 2196 CG ASP A 293 -16.262 20.568 -11.565 1.00156.90 C
ANISOU 2196 CG ASP A 293 20034 19131 20451 3999 -539 404 C
ATOM 2197 OD1 ASP A 293 -15.267 21.016 -12.172 1.00153.54 O
ANISOU 2197 OD1 ASP A 293 19646 18678 20014 4163 -360 345 O
ATOM 2198 OD2 ASP A 293 -16.291 19.423 -11.067 1.00149.28 O
ANISOU 2198 OD2 ASP A 293 19163 18070 19486 3867 -760 308 O
ATOM 2199 N GLU A 294 -15.931 24.293 -10.543 1.00191.56 N
ANISOU 2199 N GLU A 294 24170 23530 25083 4162 269 693 N
ATOM 2200 CA GLU A 294 -14.698 25.061 -10.464 1.00207.30 C
ANISOU 2200 CA GLU A 294 26202 25431 27131 4195 519 627 C
ATOM 2201 C GLU A 294 -14.395 25.529 -9.048 1.00217.71 C
ANISOU 2201 C GLU A 294 27498 26635 28585 4031 641 622 C
ATOM 2202 O GLU A 294 -13.313 26.074 -8.817 1.00221.21 O
ANISOU 2202 O GLU A 294 27967 27019 29062 3983 818 562 O
ATOM 2203 CB GLU A 294 -14.777 26.268 -11.402 1.00214.23 C
ANISOU 2203 CB GLU A 294 27115 26359 27922 4363 782 744 C
ATOM 2204 CG GLU A 294 -14.895 25.906 -12.875 1.00212.52 C
ANISOU 2204 CG GLU A 294 26932 26263 27552 4524 688 743 C
ATOM 2205 CD GLU A 294 -13.547 25.698 -13.535 1.00203.66 C
ANISOU 2205 CD GLU A 294 25873 25112 26397 4589 737 597 C
ATOM 2206 OE1 GLU A 294 -12.672 26.577 -13.386 1.00201.41 O
ANISOU 2206 OE1 GLU A 294 25598 24776 26154 4585 987 592 O
ATOM 2207 OE2 GLU A 294 -13.359 24.656 -14.198 1.00197.58 O
ANISOU 2207 OE2 GLU A 294 25156 24373 25541 4637 536 494 O
ATOM 2208 N ALA A 295 -15.331 25.363 -8.115 1.00231.23 N
ANISOU 2208 N ALA A 295 29164 28336 30357 3927 558 694 N
ATOM 2209 CA ALA A 295 -15.166 25.779 -6.728 1.00222.23 C
ANISOU 2209 CA ALA A 295 28027 27084 29328 3762 667 692 C
ATOM 2210 C ALA A 295 -14.533 24.717 -5.832 1.00208.36 C
ANISOU 2210 C ALA A 295 26236 25276 27657 3592 454 551 C
ATOM 2211 O ALA A 295 -14.295 24.998 -4.653 1.00207.64 O
ANISOU 2211 O ALA A 295 26145 25104 27647 3430 526 539 O
ATOM 2212 CB ALA A 295 -16.521 26.191 -6.144 1.00218.91 C
ANISOU 2212 CB ALA A 295 27575 26685 28916 3765 717 863 C
ATOM 2213 N CYS A 296 -14.263 23.512 -6.344 1.00175.34 N
ANISOU 2213 N CYS A 296 22049 21128 23442 3630 206 451 N
ATOM 2214 CA CYS A 296 -13.749 22.391 -5.547 1.00149.60 C
ANISOU 2214 CA CYS A 296 18780 17814 20247 3515 -3 339 C
ATOM 2215 C CYS A 296 -14.671 22.071 -4.367 1.00136.44 C
ANISOU 2215 C CYS A 296 17078 16109 18654 3347 -122 391 C
ATOM 2216 O CYS A 296 -14.259 21.452 -3.382 1.00115.84 O
ANISOU 2216 O CYS A 296 14456 13439 16118 3219 -232 326 O
ATOM 2217 CB CYS A 296 -12.299 22.662 -5.090 1.00133.39 C
ANISOU 2217 CB CYS A 296 16695 15746 18243 3467 124 262 C
ATOM 2218 SG CYS A 296 -11.523 21.588 -3.826 1.00144.46 S
ANISOU 2218 SG CYS A 296 18046 17113 19730 3327 -62 173 S
ATOM 2219 N TRP A 297 -15.944 22.454 -4.475 1.00148.58 N
ANISOU 2219 N TRP A 297 18587 17707 20161 3360 -105 527 N
ATOM 2220 CA TRP A 297 -16.957 22.154 -3.464 1.00162.52 C
ANISOU 2220 CA TRP A 297 20298 19477 21976 3218 -214 607 C
ATOM 2221 C TRP A 297 -16.534 22.658 -2.083 1.00183.20 C
ANISOU 2221 C TRP A 297 22915 21990 24703 3076 -74 592 C
ATOM 2222 O TRP A 297 -16.847 22.047 -1.058 1.00216.82 O
ANISOU 2222 O TRP A 297 27147 26213 29021 2925 -215 585 O
ATOM 2223 CB TRP A 297 -17.274 20.651 -3.431 1.00147.83 C
ANISOU 2223 CB TRP A 297 18462 17618 20089 3120 -555 539 C
ATOM 2224 CG TRP A 297 -17.542 20.042 -4.799 1.00135.28 C
ANISOU 2224 CG TRP A 297 16936 16107 18358 3213 -710 520 C
ATOM 2225 CD1 TRP A 297 -17.570 20.693 -6.002 1.00137.15 C
ANISOU 2225 CD1 TRP A 297 17174 16436 18500 3382 -585 568 C
ATOM 2226 CD2 TRP A 297 -17.814 18.663 -5.091 1.00140.91 C
ANISOU 2226 CD2 TRP A 297 17757 16797 18985 3123 -1011 445 C
ATOM 2227 NE1 TRP A 297 -17.840 19.811 -7.017 1.00138.60 N
ANISOU 2227 NE1 TRP A 297 17450 16671 18542 3396 -796 525 N
ATOM 2228 CE2 TRP A 297 -17.993 18.558 -6.486 1.00136.98 C
ANISOU 2228 CE2 TRP A 297 17331 16384 18332 3229 -1056 445 C
ATOM 2229 CE3 TRP A 297 -17.924 17.509 -4.310 1.00178.26 C
ANISOU 2229 CE3 TRP A 297 22564 21428 23738 2952 -1240 379 C
ATOM 2230 CZ2 TRP A 297 -18.279 17.348 -7.115 1.00143.11 C
ANISOU 2230 CZ2 TRP A 297 18276 17138 18962 3149 -1319 371 C
ATOM 2231 CZ3 TRP A 297 -18.206 16.307 -4.938 1.00194.75 C
ANISOU 2231 CZ3 TRP A 297 24830 23480 25687 2882 -1493 310 C
ATOM 2232 CH2 TRP A 297 -18.380 16.237 -6.325 1.00180.66 C
ANISOU 2232 CH2 TRP A 297 23137 21770 23735 2970 -1530 301 C
ATOM 2233 N ALA A 298 -15.807 23.779 -2.064 1.00166.43 N
ANISOU 2233 N ALA A 298 20838 19814 22585 3102 204 588 N
ATOM 2234 CA ALA A 298 -15.341 24.416 -0.838 1.00151.87 C
ANISOU 2234 CA ALA A 298 19034 17868 20803 2933 368 572 C
ATOM 2235 C ALA A 298 -16.111 25.703 -0.599 1.00191.68 C
ANISOU 2235 C ALA A 298 24156 22859 25815 2977 662 713 C
ATOM 2236 O ALA A 298 -16.988 25.768 0.269 1.00185.47 O
ANISOU 2236 O ALA A 298 23365 22050 25055 2923 677 801 O
ATOM 2237 CB ALA A 298 -13.844 24.716 -0.919 1.00117.19 C
ANISOU 2237 CB ALA A 298 14666 13456 16404 2872 469 462 C
ATOM 2238 N ARG A 299 -15.748 26.745 -1.336 1.00217.52 N
ANISOU 2238 N ARG A 299 27523 26104 29022 3085 919 743 N
ATOM 2239 CA ARG A 299 -16.608 27.911 -1.438 1.00204.39 C
ANISOU 2239 CA ARG A 299 25965 24395 27300 3223 1209 907 C
ATOM 2240 C ARG A 299 -17.832 27.548 -2.266 1.00201.94 C
ANISOU 2240 C ARG A 299 25528 24254 26946 3440 1089 1054 C
ATOM 2241 O ARG A 299 -17.747 26.775 -3.225 1.00175.87 O
ANISOU 2241 O ARG A 299 22131 21075 23618 3506 870 1009 O
ATOM 2242 CB ARG A 299 -15.852 29.082 -2.064 1.00198.66 C
ANISOU 2242 CB ARG A 299 25404 23580 26499 3274 1513 901 C
ATOM 2243 CG ARG A 299 -16.729 30.267 -2.436 1.00164.82 C
ANISOU 2243 CG ARG A 299 21257 19239 22126 3492 1830 1088 C
ATOM 2244 CD ARG A 299 -17.355 30.925 -1.212 1.00161.22 C
ANISOU 2244 CD ARG A 299 20953 18634 21669 3436 2044 1177 C
ATOM 2245 NE ARG A 299 -16.446 31.871 -0.571 1.00165.14 N
ANISOU 2245 NE ARG A 299 21721 18904 22121 3227 2316 1091 N
ATOM 2246 CZ ARG A 299 -16.559 33.193 -0.657 1.00175.95 C
ANISOU 2246 CZ ARG A 299 23384 20088 23381 3313 2708 1183 C
ATOM 2247 NH1 ARG A 299 -17.545 33.734 -1.359 1.00183.27 N
ANISOU 2247 NH1 ARG A 299 24344 21045 24244 3654 2883 1382 N
ATOM 2248 NH2 ARG A 299 -15.678 33.975 -0.048 1.00175.18 N
ANISOU 2248 NH2 ARG A 299 23562 19781 23219 3049 2928 1087 N
ATOM 2249 N ASN A 300 -18.984 28.092 -1.887 1.00225.61 N
ANISOU 2249 N ASN A 300 28527 27277 29917 3546 1234 1242 N
ATOM 2250 CA ASN A 300 -20.216 27.781 -2.595 1.00231.77 C
ANISOU 2250 CA ASN A 300 29143 28286 30635 3729 1117 1424 C
ATOM 2251 C ASN A 300 -21.070 29.028 -2.740 1.00237.36 C
ANISOU 2251 C ASN A 300 29914 29012 31259 3984 1463 1666 C
ATOM 2252 O ASN A 300 -21.283 29.761 -1.769 1.00253.47 O
ANISOU 2252 O ASN A 300 32089 30907 33311 3984 1715 1731 O
ATOM 2253 CB ASN A 300 -21.003 26.681 -1.871 1.00229.97 C
ANISOU 2253 CB ASN A 300 28748 28178 30453 3586 823 1452 C
ATOM 2254 CG ASN A 300 -21.082 26.908 -0.374 1.00224.29 C
ANISOU 2254 CG ASN A 300 28096 27315 29807 3446 934 1448 C
ATOM 2255 OD1 ASN A 300 -20.352 26.285 0.397 1.00227.24 O
ANISOU 2255 OD1 ASN A 300 28501 27577 30263 3219 789 1275 O
ATOM 2256 ND2 ASN A 300 -21.972 27.800 0.046 1.00215.81 N
ANISOU 2256 ND2 ASN A 300 27054 26254 28691 3598 1202 1653 N
ATOM 2257 N SER A 301 -21.558 29.254 -3.954 1.00229.17 N
ANISOU 2257 N SER A 301 28798 28152 30122 4213 1481 1807 N
ATOM 2258 CA SER A 301 -22.570 30.249 -4.257 1.00214.31 C
ANISOU 2258 CA SER A 301 26916 26373 28139 4518 1762 2093 C
ATOM 2259 C SER A 301 -23.902 29.527 -4.473 1.00202.19 C
ANISOU 2259 C SER A 301 25078 25198 26548 4583 1518 2304 C
ATOM 2260 O SER A 301 -24.049 28.358 -4.096 1.00202.28 O
ANISOU 2260 O SER A 301 24942 25305 26611 4349 1176 2213 O
ATOM 2261 CB SER A 301 -22.134 31.076 -5.472 1.00213.55 C
ANISOU 2261 CB SER A 301 26943 26247 27951 4725 1968 2126 C
ATOM 2262 OG SER A 301 -20.891 31.713 -5.237 1.00213.16 O
ANISOU 2262 OG SER A 301 27162 25890 27937 4609 2179 1938 O
ATOM 2263 N ASN A 302 -24.870 30.208 -5.094 1.00211.08 N
ANISOU 2263 N ASN A 302 26109 26541 27551 4891 1691 2601 N
ATOM 2264 CA ASN A 302 -26.202 29.651 -5.317 1.00206.87 C
ANISOU 2264 CA ASN A 302 25251 26420 26929 4952 1484 2857 C
ATOM 2265 C ASN A 302 -26.749 29.062 -4.024 1.00178.46 C
ANISOU 2265 C ASN A 302 21543 22855 23408 4768 1365 2877 C
ATOM 2266 O ASN A 302 -26.687 27.845 -3.817 1.00173.89 O
ANISOU 2266 O ASN A 302 20852 22343 22876 4468 990 2731 O
ATOM 2267 CB ASN A 302 -26.174 28.585 -6.417 1.00224.90 C
ANISOU 2267 CB ASN A 302 27371 28937 29145 4802 1081 2776 C
ATOM 2268 CG ASN A 302 -25.873 29.164 -7.785 1.00241.83 C
ANISOU 2268 CG ASN A 302 29576 31130 31179 5017 1192 2817 C
ATOM 2269 OD1 ASN A 302 -26.170 30.326 -8.059 1.00248.62 O
ANISOU 2269 OD1 ASN A 302 30494 31998 31971 5336 1539 3029 O
ATOM 2270 ND2 ASN A 302 -25.285 28.350 -8.654 1.00246.66 N
ANISOU 2270 ND2 ASN A 302 30198 31763 31760 4856 911 2621 N
ATOM 2271 N MET A 303 -27.302 29.915 -3.159 1.00184.34 N
ANISOU 2271 N MET A 303 22346 23543 24151 4958 1695 3065 N
ATOM 2272 CA MET A 303 -27.556 29.518 -1.779 1.00198.64 C
ANISOU 2272 CA MET A 303 24139 25283 26051 4776 1652 3033 C
ATOM 2273 C MET A 303 -28.515 28.342 -1.668 1.00211.89 C
ANISOU 2273 C MET A 303 25467 27340 27703 4597 1268 3150 C
ATOM 2274 O MET A 303 -28.461 27.614 -0.673 1.00229.76 O
ANISOU 2274 O MET A 303 27715 29526 30057 4331 1096 3028 O
ATOM 2275 CB MET A 303 -28.086 30.710 -0.981 1.00197.43 C
ANISOU 2275 CB MET A 303 24133 25020 25861 5064 2115 3250 C
ATOM 2276 CG MET A 303 -27.056 31.809 -0.766 1.00188.68 C
ANISOU 2276 CG MET A 303 23459 23456 24774 5126 2495 3088 C
ATOM 2277 SD MET A 303 -25.555 31.199 0.028 1.00138.45 S
ANISOU 2277 SD MET A 303 17312 16723 18569 4655 2307 2644 S
ATOM 2278 CE MET A 303 -24.635 32.721 0.239 1.00137.80 C
ANISOU 2278 CE MET A 303 17726 16191 18440 4744 2814 2556 C
ATOM 2279 N ASN A 304 -29.383 28.131 -2.662 1.00194.37 N
ANISOU 2279 N ASN A 304 22972 25535 25345 4710 1122 3386 N
ATOM 2280 CA ASN A 304 -30.294 26.991 -2.608 1.00211.61 C
ANISOU 2280 CA ASN A 304 24832 28101 27469 4474 737 3501 C
ATOM 2281 C ASN A 304 -29.532 25.670 -2.614 1.00233.04 C
ANISOU 2281 C ASN A 304 27628 30660 30258 4052 324 3157 C
ATOM 2282 O ASN A 304 -29.922 24.714 -1.929 1.00244.17 O
ANISOU 2282 O ASN A 304 28925 32158 31690 3769 62 3134 O
ATOM 2283 CB ASN A 304 -31.266 27.048 -3.786 1.00206.63 C
ANISOU 2283 CB ASN A 304 23904 27965 26641 4636 647 3815 C
ATOM 2284 CG ASN A 304 -31.856 28.429 -3.990 1.00192.61 C
ANISOU 2284 CG ASN A 304 22090 26317 24778 5131 1090 4156 C
ATOM 2285 OD1 ASN A 304 -31.512 29.375 -3.282 1.00182.63 O
ANISOU 2285 OD1 ASN A 304 21076 24724 23592 5347 1484 4139 O
ATOM 2286 ND2 ASN A 304 -32.743 28.555 -4.971 1.00187.46 N
ANISOU 2286 ND2 ASN A 304 21147 26139 23940 5309 1036 4476 N
ATOM 2287 N TYR A 305 -28.422 25.604 -3.360 1.00232.86 N
ANISOU 2287 N TYR A 305 27817 30395 30265 4019 282 2896 N
ATOM 2288 CA TYR A 305 -27.624 24.382 -3.379 1.00238.43 C
ANISOU 2288 CA TYR A 305 28636 30926 31030 3682 -64 2579 C
ATOM 2289 C TYR A 305 -27.019 24.095 -2.015 1.00237.83 C
ANISOU 2289 C TYR A 305 28703 30541 31120 3501 -51 2384 C
ATOM 2290 O TYR A 305 -26.864 22.931 -1.633 1.00229.48 O
ANISOU 2290 O TYR A 305 27657 29436 30098 3209 -360 2230 O
ATOM 2291 CB TYR A 305 -26.506 24.483 -4.420 1.00243.55 C
ANISOU 2291 CB TYR A 305 29482 31384 31673 3742 -53 2361 C
ATOM 2292 CG TYR A 305 -26.960 24.660 -5.853 1.00250.78 C
ANISOU 2292 CG TYR A 305 30290 32581 32412 3891 -100 2513 C
ATOM 2293 CD1 TYR A 305 -28.264 24.374 -6.238 1.00257.54 C
ANISOU 2293 CD1 TYR A 305 30868 33877 33108 3869 -265 2794 C
ATOM 2294 CD2 TYR A 305 -26.074 25.108 -6.825 1.00251.23 C
ANISOU 2294 CD2 TYR A 305 30512 32495 32449 4037 16 2387 C
ATOM 2295 CE1 TYR A 305 -28.673 24.536 -7.550 1.00262.75 C
ANISOU 2295 CE1 TYR A 305 31422 34825 33586 3987 -320 2945 C
ATOM 2296 CE2 TYR A 305 -26.474 25.273 -8.138 1.00257.34 C
ANISOU 2296 CE2 TYR A 305 31198 33526 33051 4172 -26 2525 C
ATOM 2297 CZ TYR A 305 -27.774 24.985 -8.495 1.00260.79 C
ANISOU 2297 CZ TYR A 305 31363 34400 33326 4145 -198 2803 C
ATOM 2298 OH TYR A 305 -28.175 25.148 -9.802 1.00259.88 O
ANISOU 2298 OH TYR A 305 31150 34573 33020 4261 -253 2954 O
ATOM 2299 N TRP A 306 -26.655 25.141 -1.276 1.00244.19 N
ANISOU 2299 N TRP A 306 29648 31123 32011 3660 308 2387 N
ATOM 2300 CA TRP A 306 -26.162 24.959 0.081 1.00237.45 C
ANISOU 2300 CA TRP A 306 28920 30010 31290 3481 336 2233 C
ATOM 2301 C TRP A 306 -27.294 24.634 1.050 1.00233.08 C
ANISOU 2301 C TRP A 306 28182 29647 30729 3402 277 2427 C
ATOM 2302 O TRP A 306 -27.075 23.949 2.062 1.00252.88 O
ANISOU 2302 O TRP A 306 30728 32028 33325 3159 133 2298 O
ATOM 2303 CB TRP A 306 -25.401 26.211 0.506 1.00244.48 C
ANISOU 2303 CB TRP A 306 30057 30599 32233 3632 741 2171 C
ATOM 2304 CG TRP A 306 -24.513 25.997 1.662 1.00251.65 C
ANISOU 2304 CG TRP A 306 31135 31219 33260 3403 737 1947 C
ATOM 2305 CD1 TRP A 306 -23.462 25.132 1.741 1.00257.29 C
ANISOU 2305 CD1 TRP A 306 31915 31792 34051 3171 494 1684 C
ATOM 2306 CD2 TRP A 306 -24.578 26.670 2.916 1.00252.18 C
ANISOU 2306 CD2 TRP A 306 31338 31117 33364 3392 999 1979 C
ATOM 2307 NE1 TRP A 306 -22.873 25.220 2.978 1.00254.19 N
ANISOU 2307 NE1 TRP A 306 31655 31184 33742 3004 570 1562 N
ATOM 2308 CE2 TRP A 306 -23.541 26.160 3.717 1.00250.26 C
ANISOU 2308 CE2 TRP A 306 31215 30654 33217 3115 874 1728 C
ATOM 2309 CE3 TRP A 306 -25.416 27.655 3.442 1.00247.82 C
ANISOU 2309 CE3 TRP A 306 30829 30577 32752 3604 1339 2207 C
ATOM 2310 CZ2 TRP A 306 -23.323 26.599 5.015 1.00243.04 C
ANISOU 2310 CZ2 TRP A 306 30463 29544 32339 3003 1057 1686 C
ATOM 2311 CZ3 TRP A 306 -25.195 28.090 4.728 1.00243.88 C
ANISOU 2311 CZ3 TRP A 306 30527 29847 32288 3508 1541 2153 C
ATOM 2312 CH2 TRP A 306 -24.159 27.565 5.501 1.00239.93 C
ANISOU 2312 CH2 TRP A 306 30144 29139 31880 3190 1390 1889 C
ATOM 2313 N LEU A 307 -28.509 25.103 0.750 1.00185.00 N
ANISOU 2313 N LEU A 307 21876 23890 24526 3612 388 2756 N
ATOM 2314 CA LEU A 307 -29.684 24.670 1.493 1.00148.03 C
ANISOU 2314 CA LEU A 307 16951 19488 19808 3528 289 2979 C
ATOM 2315 C LEU A 307 -29.996 23.203 1.243 1.00157.01 C
ANISOU 2315 C LEU A 307 17931 20823 20902 3174 -189 2921 C
ATOM 2316 O LEU A 307 -30.692 22.583 2.052 1.00168.43 O
ANISOU 2316 O LEU A 307 19232 22418 22348 2983 -336 3015 O
ATOM 2317 CB LEU A 307 -30.912 25.515 1.134 1.00138.26 C
ANISOU 2317 CB LEU A 307 15475 18624 18431 3869 524 3387 C
ATOM 2318 CG LEU A 307 -30.935 27.048 1.211 1.00152.07 C
ANISOU 2318 CG LEU A 307 17376 20244 20158 4299 1041 3546 C
ATOM 2319 CD1 LEU A 307 -32.335 27.538 1.563 1.00178.28 C
ANISOU 2319 CD1 LEU A 307 20431 23941 23366 4574 1243 3973 C
ATOM 2320 CD2 LEU A 307 -29.917 27.609 2.182 1.00119.18 C
ANISOU 2320 CD2 LEU A 307 13588 15576 16120 4266 1298 3297 C
ATOM 2321 N ILE A 308 -29.509 22.641 0.131 1.00144.88 N
ANISOU 2321 N ILE A 308 16449 19285 19314 3077 -421 2770 N
ATOM 2322 CA ILE A 308 -29.727 21.222 -0.142 1.00151.14 C
ANISOU 2322 CA ILE A 308 17188 20201 20038 2719 -863 2685 C
ATOM 2323 C ILE A 308 -29.103 20.355 0.944 1.00155.61 C
ANISOU 2323 C ILE A 308 17925 20464 20737 2442 -1019 2440 C
ATOM 2324 O ILE A 308 -29.661 19.312 1.311 1.00159.76 O
ANISOU 2324 O ILE A 308 18374 21112 21216 2144 -1309 2463 O
ATOM 2325 CB ILE A 308 -29.190 20.863 -1.541 1.00178.43 C
ANISOU 2325 CB ILE A 308 20750 23643 23400 2701 -1031 2542 C
ATOM 2326 CG1 ILE A 308 -30.075 21.479 -2.627 1.00203.09 C
ANISOU 2326 CG1 ILE A 308 23646 27173 26348 2905 -965 2836 C
ATOM 2327 CG2 ILE A 308 -29.079 19.357 -1.717 1.00177.16 C
ANISOU 2327 CG2 ILE A 308 20689 23446 23178 2319 -1452 2362 C
ATOM 2328 CD1 ILE A 308 -29.615 21.164 -4.030 1.00216.89 C
ANISOU 2328 CD1 ILE A 308 25501 28929 27979 2886 -1124 2711 C
ATOM 2329 N ILE A 309 -27.968 20.768 1.499 1.00161.11 N
ANISOU 2329 N ILE A 309 18848 20782 21583 2518 -833 2221 N
ATOM 2330 CA ILE A 309 -27.380 20.028 2.612 1.00141.30 C
ANISOU 2330 CA ILE A 309 16479 18017 19194 2284 -957 2023 C
ATOM 2331 C ILE A 309 -27.825 20.594 3.950 1.00145.58 C
ANISOU 2331 C ILE A 309 16962 18544 19809 2315 -741 2148 C
ATOM 2332 O ILE A 309 -28.229 19.844 4.841 1.00171.96 O
ANISOU 2332 O ILE A 309 20252 21912 23171 2089 -910 2164 O
ATOM 2333 CB ILE A 309 -25.838 19.990 2.511 1.00111.77 C
ANISOU 2333 CB ILE A 309 12996 13917 15554 2300 -925 1719 C
ATOM 2334 CG1 ILE A 309 -25.267 21.349 2.099 1.00109.65 C
ANISOU 2334 CG1 ILE A 309 12801 13554 15308 2585 -566 1723 C
ATOM 2335 CG2 ILE A 309 -25.383 18.872 1.595 1.00112.49 C
ANISOU 2335 CG2 ILE A 309 13192 13969 15580 2168 -1235 1551 C
ATOM 2336 CD1 ILE A 309 -24.619 22.109 3.241 1.00106.52 C
ANISOU 2336 CD1 ILE A 309 12538 12911 15023 2605 -298 1649 C
ATOM 2337 N ARG A 310 -27.740 21.916 4.136 1.00123.81 N
ANISOU 2337 N ARG A 310 14249 15719 17075 2588 -354 2235 N
ATOM 2338 CA ARG A 310 -27.999 22.441 5.473 1.00134.48 C
ANISOU 2338 CA ARG A 310 15629 16982 18484 2608 -126 2311 C
ATOM 2339 C ARG A 310 -29.469 22.325 5.871 1.00143.19 C
ANISOU 2339 C ARG A 310 16461 18439 19507 2622 -142 2623 C
ATOM 2340 O ARG A 310 -29.762 22.105 7.050 1.00188.17 O
ANISOU 2340 O ARG A 310 22146 24102 25247 2497 -133 2651 O
ATOM 2341 CB ARG A 310 -27.515 23.887 5.585 1.00148.15 C
ANISOU 2341 CB ARG A 310 17551 18507 20230 2876 313 2314 C
ATOM 2342 CG ARG A 310 -28.403 24.930 4.948 1.00179.24 C
ANISOU 2342 CG ARG A 310 21384 22662 24058 3229 601 2608 C
ATOM 2343 CD ARG A 310 -28.313 26.231 5.724 1.00207.07 C
ANISOU 2343 CD ARG A 310 25131 25964 27582 3442 1065 2668 C
ATOM 2344 NE ARG A 310 -28.303 27.388 4.841 1.00228.83 N
ANISOU 2344 NE ARG A 310 27986 28703 30257 3781 1387 2785 N
ATOM 2345 CZ ARG A 310 -28.310 28.650 5.256 1.00249.93 C
ANISOU 2345 CZ ARG A 310 30902 31176 32882 4024 1838 2873 C
ATOM 2346 NH1 ARG A 310 -28.326 28.924 6.553 1.00267.30 N
ANISOU 2346 NH1 ARG A 310 33274 33183 35105 3956 2021 2849 N
ATOM 2347 NH2 ARG A 310 -28.294 29.637 4.373 1.00246.02 N
ANISOU 2347 NH2 ARG A 310 30515 30658 32304 4331 2117 2982 N
ATOM 2348 N LEU A 311 -30.398 22.455 4.919 1.00117.11 N
ANISOU 2348 N LEU A 311 12920 15503 16074 2763 -171 2872 N
ATOM 2349 CA LEU A 311 -31.818 22.415 5.268 1.00129.22 C
ANISOU 2349 CA LEU A 311 14144 17445 17509 2795 -167 3217 C
ATOM 2350 C LEU A 311 -32.227 21.101 5.926 1.00133.91 C
ANISOU 2350 C LEU A 311 14626 18148 18107 2397 -532 3189 C
ATOM 2351 O LEU A 311 -32.889 21.149 6.980 1.00124.54 O
ANISOU 2351 O LEU A 311 13330 17062 16927 2376 -440 3346 O
ATOM 2352 CB LEU A 311 -32.668 22.717 4.026 1.00140.23 C
ANISOU 2352 CB LEU A 311 15275 19265 18741 2990 -174 3498 C
ATOM 2353 CG LEU A 311 -34.184 22.557 4.176 1.00150.72 C
ANISOU 2353 CG LEU A 311 16202 21137 19928 2998 -228 3900 C
ATOM 2354 CD1 LEU A 311 -34.724 23.466 5.270 1.00177.98 C
ANISOU 2354 CD1 LEU A 311 19620 24602 23403 3281 169 4120 C
ATOM 2355 CD2 LEU A 311 -34.888 22.829 2.856 1.00128.86 C
ANISOU 2355 CD2 LEU A 311 13171 18808 16981 3172 -263 4168 C
ATOM 2356 N PRO A 312 -31.895 19.918 5.385 1.00136.31 N
ANISOU 2356 N PRO A 312 14976 18426 18389 2080 -928 3006 N
ATOM 2357 CA PRO A 312 -32.148 18.694 6.164 1.00149.91 C
ANISOU 2357 CA PRO A 312 16682 20155 20122 1693 -1238 2949 C
ATOM 2358 C PRO A 312 -31.418 18.678 7.494 1.00164.06 C
ANISOU 2358 C PRO A 312 18686 21574 22073 1630 -1135 2757 C
ATOM 2359 O PRO A 312 -31.955 18.130 8.476 1.00166.67 O
ANISOU 2359 O PRO A 312 18939 21978 22411 1426 -1234 2831 O
ATOM 2360 CB PRO A 312 -31.641 17.580 5.226 1.00148.44 C
ANISOU 2360 CB PRO A 312 16638 19884 19878 1431 -1610 2733 C
ATOM 2361 CG PRO A 312 -31.715 18.172 3.867 1.00142.15 C
ANISOU 2361 CG PRO A 312 15768 19261 18979 1652 -1539 2816 C
ATOM 2362 CD PRO A 312 -31.360 19.614 4.050 1.00136.14 C
ANISOU 2362 CD PRO A 312 15042 18375 18310 2061 -1100 2864 C
ATOM 2363 N ILE A 313 -30.226 19.256 7.563 1.00168.40 N
ANISOU 2363 N ILE A 313 19492 21756 22735 1778 -946 2527 N
ATOM 2364 CA ILE A 313 -29.504 19.329 8.829 1.00147.64 C
ANISOU 2364 CA ILE A 313 17057 18807 20234 1706 -840 2360 C
ATOM 2365 C ILE A 313 -30.230 20.243 9.808 1.00160.47 C
ANISOU 2365 C ILE A 313 18603 20516 21853 1870 -512 2576 C
ATOM 2366 O ILE A 313 -30.291 19.964 11.012 1.00169.53 O
ANISOU 2366 O ILE A 313 19791 21574 23050 1719 -516 2555 O
ATOM 2367 CB ILE A 313 -28.052 19.785 8.582 1.00103.80 C
ANISOU 2367 CB ILE A 313 11770 12902 14769 1802 -716 2089 C
ATOM 2368 CG1 ILE A 313 -27.291 18.715 7.793 1.00 99.74 C
ANISOU 2368 CG1 ILE A 313 11354 12285 14259 1642 -1044 1872 C
ATOM 2369 CG2 ILE A 313 -27.353 20.092 9.893 1.00 99.23 C
ANISOU 2369 CG2 ILE A 313 11371 12044 14288 1738 -559 1958 C
ATOM 2370 CD1 ILE A 313 -25.875 19.110 7.437 1.00 96.54 C
ANISOU 2370 CD1 ILE A 313 11156 11603 13922 1746 -936 1637 C
ATOM 2371 N LEU A 314 -30.817 21.335 9.305 1.00148.07 N
ANISOU 2371 N LEU A 314 16930 19121 20207 2199 -212 2800 N
ATOM 2372 CA LEU A 314 -31.651 22.175 10.159 1.00160.94 C
ANISOU 2372 CA LEU A 314 18488 20863 21798 2405 122 3050 C
ATOM 2373 C LEU A 314 -32.884 21.419 10.628 1.00187.46 C
ANISOU 2373 C LEU A 314 21539 24599 25090 2245 -67 3296 C
ATOM 2374 O LEU A 314 -33.353 21.624 11.755 1.00216.59 O
ANISOU 2374 O LEU A 314 25210 28301 28782 2263 98 3411 O
ATOM 2375 CB LEU A 314 -32.070 23.442 9.407 1.00157.71 C
ANISOU 2375 CB LEU A 314 18039 20583 21300 2831 483 3272 C
ATOM 2376 CG LEU A 314 -30.996 24.337 8.781 1.00155.18 C
ANISOU 2376 CG LEU A 314 18009 19940 21013 3016 710 3084 C
ATOM 2377 CD1 LEU A 314 -31.603 25.222 7.704 1.00157.48 C
ANISOU 2377 CD1 LEU A 314 18181 20467 21189 3396 935 3342 C
ATOM 2378 CD2 LEU A 314 -30.303 25.186 9.825 1.00160.14 C
ANISOU 2378 CD2 LEU A 314 18981 20172 21691 3065 1050 2946 C
ATOM 2379 N PHE A 315 -33.407 20.528 9.782 1.00171.67 N
ANISOU 2379 N PHE A 315 19309 22909 23010 2062 -414 3377 N
ATOM 2380 CA PHE A 315 -34.547 19.706 10.169 1.00159.39 C
ANISOU 2380 CA PHE A 315 17457 21738 21368 1829 -640 3606 C
ATOM 2381 C PHE A 315 -34.176 18.755 11.301 1.00159.41 C
ANISOU 2381 C PHE A 315 17604 21503 21461 1474 -846 3410 C
ATOM 2382 O PHE A 315 -34.913 18.630 12.288 1.00153.04 O
ANISOU 2382 O PHE A 315 16661 20854 20634 1402 -801 3584 O
ATOM 2383 CB PHE A 315 -35.059 18.943 8.944 1.00147.15 C
ANISOU 2383 CB PHE A 315 15692 20535 19683 1643 -987 3699 C
ATOM 2384 CG PHE A 315 -35.989 17.807 9.265 1.00147.23 C
ANISOU 2384 CG PHE A 315 15471 20877 19592 1249 -1324 3849 C
ATOM 2385 CD1 PHE A 315 -37.328 18.040 9.528 1.00156.20 C
ANISOU 2385 CD1 PHE A 315 16218 22531 20601 1312 -1242 4256 C
ATOM 2386 CD2 PHE A 315 -35.528 16.500 9.273 1.00147.09 C
ANISOU 2386 CD2 PHE A 315 15634 20666 19588 817 -1716 3600 C
ATOM 2387 CE1 PHE A 315 -38.186 16.993 9.813 1.00153.31 C
ANISOU 2387 CE1 PHE A 315 15628 22499 20123 905 -1560 4407 C
ATOM 2388 CE2 PHE A 315 -36.379 15.450 9.557 1.00150.09 C
ANISOU 2388 CE2 PHE A 315 15846 21328 19853 416 -2024 3735 C
ATOM 2389 CZ PHE A 315 -37.710 15.696 9.827 1.00151.29 C
ANISOU 2389 CZ PHE A 315 15590 22014 19879 435 -1956 4137 C
ATOM 2390 N ALA A 316 -33.020 18.093 11.188 1.00163.66 N
ANISOU 2390 N ALA A 316 18419 21670 22093 1274 -1057 3064 N
ATOM 2391 CA ALA A 316 -32.580 17.203 12.258 1.00169.26 C
ANISOU 2391 CA ALA A 316 19287 22137 22885 971 -1240 2882 C
ATOM 2392 C ALA A 316 -32.286 17.973 13.541 1.00179.09 C
ANISOU 2392 C ALA A 316 20663 23165 24217 1102 -921 2856 C
ATOM 2393 O ALA A 316 -32.557 17.479 14.643 1.00203.73 O
ANISOU 2393 O ALA A 316 23779 26273 27358 909 -986 2879 O
ATOM 2394 CB ALA A 316 -31.347 16.418 11.808 1.00161.81 C
ANISOU 2394 CB ALA A 316 18617 20855 22010 806 -1488 2543 C
ATOM 2395 N ILE A 317 -31.762 19.195 13.417 1.00156.49 N
ANISOU 2395 N ILE A 317 17941 20130 21386 1413 -568 2814 N
ATOM 2396 CA ILE A 317 -31.460 19.992 14.603 1.00155.40 C
ANISOU 2396 CA ILE A 317 17989 19762 21296 1514 -245 2778 C
ATOM 2397 C ILE A 317 -32.743 20.385 15.321 1.00162.30 C
ANISOU 2397 C ILE A 317 18664 20916 22087 1639 -35 3101 C
ATOM 2398 O ILE A 317 -32.875 20.204 16.538 1.00169.05 O
ANISOU 2398 O ILE A 317 19575 21697 22961 1512 5 3102 O
ATOM 2399 CB ILE A 317 -30.633 21.233 14.224 1.00184.24 C
ANISOU 2399 CB ILE A 317 21879 23160 24966 1785 92 2667 C
ATOM 2400 CG1 ILE A 317 -29.186 20.850 13.908 1.00192.37 C
ANISOU 2400 CG1 ILE A 317 23127 23880 26085 1626 -84 2331 C
ATOM 2401 CG2 ILE A 317 -30.678 22.253 15.353 1.00189.65 C
ANISOU 2401 CG2 ILE A 317 22755 23674 25631 1926 496 2715 C
ATOM 2402 CD1 ILE A 317 -28.321 20.692 15.137 1.00181.55 C
ANISOU 2402 CD1 ILE A 317 21979 22218 24785 1421 -82 2128 C
ATOM 2403 N GLY A 318 -33.716 20.909 14.575 1.00133.74 N
ANISOU 2403 N GLY A 318 14798 17653 18365 1901 103 3397 N
ATOM 2404 CA GLY A 318 -34.942 21.363 15.207 1.00128.90 C
ANISOU 2404 CA GLY A 318 13970 17348 17657 2088 346 3745 C
ATOM 2405 C GLY A 318 -35.778 20.221 15.752 1.00134.34 C
ANISOU 2405 C GLY A 318 14389 18342 18311 1764 36 3884 C
ATOM 2406 O GLY A 318 -36.390 20.344 16.818 1.00142.93 O
ANISOU 2406 O GLY A 318 15417 19520 19370 1787 196 4044 O
ATOM 2407 N VAL A 319 -35.810 19.091 15.040 1.00118.57 N
ANISOU 2407 N VAL A 319 12258 16492 16302 1445 -402 3823 N
ATOM 2408 CA VAL A 319 -36.578 17.950 15.527 1.00135.01 C
ANISOU 2408 CA VAL A 319 14124 18843 18331 1078 -715 3944 C
ATOM 2409 C VAL A 319 -35.921 17.350 16.764 1.00155.47 C
ANISOU 2409 C VAL A 319 16971 21071 21030 814 -808 3704 C
ATOM 2410 O VAL A 319 -36.603 17.009 17.740 1.00176.29 O
ANISOU 2410 O VAL A 319 19487 23862 23635 675 -817 3856 O
ATOM 2411 CB VAL A 319 -36.758 16.910 14.407 1.00120.50 C
ANISOU 2411 CB VAL A 319 12152 17216 16417 776 -1148 3928 C
ATOM 2412 CG1 VAL A 319 -37.349 15.626 14.966 1.00123.83 C
ANISOU 2412 CG1 VAL A 319 12458 17810 16781 314 -1497 3986 C
ATOM 2413 CG2 VAL A 319 -37.656 17.463 13.312 1.00124.31 C
ANISOU 2413 CG2 VAL A 319 12300 18178 16753 1005 -1069 4246 C
ATOM 2414 N ASN A 320 -34.589 17.229 16.759 1.00145.08 N
ANISOU 2414 N ASN A 320 15997 19295 19834 750 -871 3346 N
ATOM 2415 CA ASN A 320 -33.902 16.737 17.950 1.00136.41 C
ANISOU 2415 CA ASN A 320 15134 17868 18827 531 -940 3134 C
ATOM 2416 C ASN A 320 -34.096 17.680 19.129 1.00142.15 C
ANISOU 2416 C ASN A 320 15932 18522 19555 723 -552 3226 C
ATOM 2417 O ASN A 320 -34.220 17.226 20.275 1.00150.00 O
ANISOU 2417 O ASN A 320 16968 19463 20563 530 -598 3222 O
ATOM 2418 CB ASN A 320 -32.415 16.546 17.664 1.00135.62 C
ANISOU 2418 CB ASN A 320 15347 17348 18834 476 -1048 2773 C
ATOM 2419 CG ASN A 320 -31.628 16.156 18.902 1.00164.09 C
ANISOU 2419 CG ASN A 320 19186 20640 22522 287 -1092 2575 C
ATOM 2420 OD1 ASN A 320 -31.539 14.979 19.249 1.00148.42 O
ANISOU 2420 OD1 ASN A 320 17234 18608 20552 -10 -1405 2501 O
ATOM 2421 ND2 ASN A 320 -31.057 17.147 19.579 1.00190.57 N
ANISOU 2421 ND2 ASN A 320 22723 23776 25909 447 -774 2496 N
ATOM 2422 N PHE A 321 -34.152 18.988 18.869 1.00154.60 N
ANISOU 2422 N PHE A 321 17553 20088 21101 1104 -156 3317 N
ATOM 2423 CA PHE A 321 -34.425 19.936 19.943 1.00157.55 C
ANISOU 2423 CA PHE A 321 18043 20381 21437 1311 255 3422 C
ATOM 2424 C PHE A 321 -35.839 19.771 20.483 1.00160.14 C
ANISOU 2424 C PHE A 321 18055 21126 21666 1344 314 3780 C
ATOM 2425 O PHE A 321 -36.051 19.830 21.698 1.00190.10 O
ANISOU 2425 O PHE A 321 21929 24855 25445 1300 456 3818 O
ATOM 2426 CB PHE A 321 -34.209 21.369 19.455 1.00167.39 C
ANISOU 2426 CB PHE A 321 19454 21503 22644 1723 684 3454 C
ATOM 2427 CG PHE A 321 -34.792 22.414 20.369 1.00177.81 C
ANISOU 2427 CG PHE A 321 20882 22805 23871 2011 1159 3645 C
ATOM 2428 CD1 PHE A 321 -34.066 22.900 21.443 1.00172.87 C
ANISOU 2428 CD1 PHE A 321 20645 21783 23256 1954 1375 3448 C
ATOM 2429 CD2 PHE A 321 -36.072 22.908 20.156 1.00185.39 C
ANISOU 2429 CD2 PHE A 321 21566 24161 24714 2343 1397 4036 C
ATOM 2430 CE1 PHE A 321 -34.606 23.857 22.286 1.00169.69 C
ANISOU 2430 CE1 PHE A 321 20403 21330 22741 2219 1833 3614 C
ATOM 2431 CE2 PHE A 321 -36.614 23.860 20.997 1.00183.94 C
ANISOU 2431 CE2 PHE A 321 21514 23948 24429 2653 1866 4225 C
ATOM 2432 CZ PHE A 321 -35.878 24.339 22.060 1.00180.94 C
ANISOU 2432 CZ PHE A 321 21575 23121 24055 2591 2091 4002 C
ATOM 2433 N LEU A 322 -36.824 19.580 19.599 1.00141.99 N
ANISOU 2433 N LEU A 322 15383 19285 19281 1418 213 4060 N
ATOM 2434 CA LEU A 322 -38.200 19.452 20.070 1.00140.87 C
ANISOU 2434 CA LEU A 322 14886 19616 19024 1455 276 4444 C
ATOM 2435 C LEU A 322 -38.398 18.170 20.868 1.00144.42 C
ANISOU 2435 C LEU A 322 15259 20122 19492 990 -79 4403 C
ATOM 2436 O LEU A 322 -39.129 18.159 21.866 1.00145.74 O
ANISOU 2436 O LEU A 322 15307 20464 19602 984 51 4603 O
ATOM 2437 CB LEU A 322 -39.174 19.507 18.894 1.00137.11 C
ANISOU 2437 CB LEU A 322 13995 19672 18429 1600 216 4770 C
ATOM 2438 CG LEU A 322 -39.307 20.863 18.201 1.00118.49 C
ANISOU 2438 CG LEU A 322 11644 17364 16012 2138 634 4931 C
ATOM 2439 CD1 LEU A 322 -40.508 20.877 17.268 1.00121.79 C
ANISOU 2439 CD1 LEU A 322 11568 18429 16277 2286 587 5349 C
ATOM 2440 CD2 LEU A 322 -39.403 21.985 19.224 1.00119.37 C
ANISOU 2440 CD2 LEU A 322 11977 17280 16097 2511 1162 5018 C
ATOM 2441 N ILE A 323 -37.749 17.081 20.449 1.00160.62 N
ANISOU 2441 N ILE A 323 17402 22016 21612 610 -510 4150 N
ATOM 2442 CA ILE A 323 -37.797 15.861 21.245 1.00173.59 C
ANISOU 2442 CA ILE A 323 19060 23624 23271 170 -832 4078 C
ATOM 2443 C ILE A 323 -37.066 16.060 22.567 1.00170.40 C
ANISOU 2443 C ILE A 323 18977 22813 22955 153 -671 3877 C
ATOM 2444 O ILE A 323 -37.461 15.500 23.599 1.00169.53 O
ANISOU 2444 O ILE A 323 18831 22758 22826 -64 -741 3945 O
ATOM 2445 CB ILE A 323 -37.225 14.690 20.428 1.00183.69 C
ANISOU 2445 CB ILE A 323 20431 24782 24582 -185 -1293 3853 C
ATOM 2446 CG1 ILE A 323 -38.108 14.436 19.205 1.00195.95 C
ANISOU 2446 CG1 ILE A 323 21655 26794 26002 -235 -1469 4085 C
ATOM 2447 CG2 ILE A 323 -37.116 13.441 21.275 1.00182.20 C
ANISOU 2447 CG2 ILE A 323 20352 24464 24412 -619 -1603 3745 C
ATOM 2448 CD1 ILE A 323 -37.625 13.323 18.319 1.00203.75 C
ANISOU 2448 CD1 ILE A 323 22775 27661 26980 -576 -1896 3876 C
ATOM 2449 N PHE A 324 -36.024 16.893 22.569 1.00176.83 N
ANISOU 2449 N PHE A 324 20102 23238 23846 368 -444 3643 N
ATOM 2450 CA PHE A 324 -35.328 17.219 23.809 1.00180.57 C
ANISOU 2450 CA PHE A 324 20887 23354 24369 346 -264 3466 C
ATOM 2451 C PHE A 324 -36.262 17.933 24.782 1.00183.61 C
ANISOU 2451 C PHE A 324 21196 23909 24658 547 106 3730 C
ATOM 2452 O PHE A 324 -36.376 17.548 25.955 1.00192.17 O
ANISOU 2452 O PHE A 324 22343 24938 25734 364 89 3729 O
ATOM 2453 CB PHE A 324 -34.103 18.077 23.478 1.00191.40 C
ANISOU 2453 CB PHE A 324 22581 24340 25803 523 -78 3202 C
ATOM 2454 CG PHE A 324 -33.198 18.353 24.645 1.00204.26 C
ANISOU 2454 CG PHE A 324 24550 25595 27463 427 51 2983 C
ATOM 2455 CD1 PHE A 324 -32.218 17.446 25.010 1.00218.76 C
ANISOU 2455 CD1 PHE A 324 26536 27199 29382 113 -264 2728 C
ATOM 2456 CD2 PHE A 324 -33.299 19.542 25.347 1.00198.16 C
ANISOU 2456 CD2 PHE A 324 23973 24702 26616 659 498 3038 C
ATOM 2457 CE1 PHE A 324 -31.373 17.708 26.072 1.00211.93 C
ANISOU 2457 CE1 PHE A 324 25958 26039 28526 7 -160 2547 C
ATOM 2458 CE2 PHE A 324 -32.456 19.810 26.409 1.00201.39 C
ANISOU 2458 CE2 PHE A 324 24716 24779 27023 525 606 2834 C
ATOM 2459 CZ PHE A 324 -31.493 18.891 26.773 1.00208.90 C
ANISOU 2459 CZ PHE A 324 25764 25551 28057 188 265 2594 C
ATOM 2460 N VAL A 325 -36.973 18.953 24.295 1.00172.85 N
ANISOU 2460 N VAL A 325 19696 22770 23209 944 449 3980 N
ATOM 2461 CA VAL A 325 -37.893 19.700 25.146 1.00158.18 C
ANISOU 2461 CA VAL A 325 17779 21083 21239 1214 854 4262 C
ATOM 2462 C VAL A 325 -39.039 18.814 25.613 1.00169.54 C
ANISOU 2462 C VAL A 325 18839 22966 22613 1011 664 4544 C
ATOM 2463 O VAL A 325 -39.486 18.909 26.764 1.00161.37 O
ANISOU 2463 O VAL A 325 17829 21962 21521 1020 849 4661 O
ATOM 2464 CB VAL A 325 -38.408 20.942 24.396 1.00126.08 C
ANISOU 2464 CB VAL A 325 13644 17178 17083 1727 1263 4497 C
ATOM 2465 CG1 VAL A 325 -39.535 21.613 25.168 1.00130.01 C
ANISOU 2465 CG1 VAL A 325 14022 17938 17439 2056 1681 4859 C
ATOM 2466 CG2 VAL A 325 -37.271 21.915 24.156 1.00134.07 C
ANISOU 2466 CG2 VAL A 325 15101 17704 18135 1905 1510 4217 C
ATOM 2467 N ARG A 326 -39.521 17.924 24.742 1.00182.64 N
ANISOU 2467 N ARG A 326 20159 24974 24260 793 288 4657 N
ATOM 2468 CA ARG A 326 -40.599 17.035 25.157 1.00194.10 C
ANISOU 2468 CA ARG A 326 21254 26867 25630 530 80 4928 C
ATOM 2469 C ARG A 326 -40.131 16.082 26.248 1.00185.30 C
ANISOU 2469 C ARG A 326 20342 25482 24580 113 -161 4715 C
ATOM 2470 O ARG A 326 -40.873 15.809 27.198 1.00190.38 O
ANISOU 2470 O ARG A 326 20844 26336 25155 13 -113 4913 O
ATOM 2471 CB ARG A 326 -41.143 16.263 23.954 1.00202.49 C
ANISOU 2471 CB ARG A 326 21965 28335 26638 315 -294 5068 C
ATOM 2472 CG ARG A 326 -42.285 15.321 24.298 1.00214.12 C
ANISOU 2472 CG ARG A 326 23056 30306 27994 -22 -534 5366 C
ATOM 2473 CD ARG A 326 -43.155 15.030 23.086 1.00221.50 C
ANISOU 2473 CD ARG A 326 23561 31801 28798 -98 -742 5647 C
ATOM 2474 NE ARG A 326 -44.187 14.041 23.385 1.00217.12 N
ANISOU 2474 NE ARG A 326 22657 31728 28111 -515 -1018 5916 N
ATOM 2475 CZ ARG A 326 -45.355 14.326 23.952 1.00217.69 C
ANISOU 2475 CZ ARG A 326 22341 32321 28052 -386 -810 6338 C
ATOM 2476 NH1 ARG A 326 -46.233 13.361 24.189 1.00224.00 N
ANISOU 2476 NH1 ARG A 326 22825 33562 28722 -830 -1095 6570 N
ATOM 2477 NH2 ARG A 326 -45.643 15.575 24.290 1.00206.78 N
ANISOU 2477 NH2 ARG A 326 20902 31014 26650 187 -302 6536 N
ATOM 2478 N VAL A 327 -38.884 15.609 26.158 1.00181.47 N
ANISOU 2478 N VAL A 327 20192 24538 24220 -104 -396 4326 N
ATOM 2479 CA VAL A 327 -38.342 14.772 27.225 1.00168.97 C
ANISOU 2479 CA VAL A 327 18831 22676 22695 -452 -597 4126 C
ATOM 2480 C VAL A 327 -38.225 15.572 28.515 1.00159.80 C
ANISOU 2480 C VAL A 327 17880 21322 21516 -274 -217 4119 C
ATOM 2481 O VAL A 327 -38.465 15.051 29.615 1.00158.47 O
ANISOU 2481 O VAL A 327 17733 21156 21323 -489 -270 4156 O
ATOM 2482 CB VAL A 327 -36.989 14.172 26.798 1.00159.96 C
ANISOU 2482 CB VAL A 327 17990 21111 21676 -652 -895 3742 C
ATOM 2483 CG1 VAL A 327 -36.252 13.592 27.995 1.00146.13 C
ANISOU 2483 CG1 VAL A 327 16515 19026 19981 -904 -1007 3532 C
ATOM 2484 CG2 VAL A 327 -37.198 13.104 25.737 1.00170.53 C
ANISOU 2484 CG2 VAL A 327 19173 22620 23001 -917 -1311 3750 C
ATOM 2485 N ILE A 328 -37.904 16.865 28.402 1.00165.87 N
ANISOU 2485 N ILE A 328 18828 21923 22272 113 186 4084 N
ATOM 2486 CA ILE A 328 -37.880 17.711 29.592 1.00167.90 C
ANISOU 2486 CA ILE A 328 19330 21997 22468 290 590 4093 C
ATOM 2487 C ILE A 328 -39.271 17.803 30.204 1.00171.35 C
ANISOU 2487 C ILE A 328 19474 22853 22777 417 795 4482 C
ATOM 2488 O ILE A 328 -39.425 17.809 31.431 1.00178.41 O
ANISOU 2488 O ILE A 328 20494 23673 23620 355 938 4507 O
ATOM 2489 CB ILE A 328 -37.327 19.106 29.251 1.00167.81 C
ANISOU 2489 CB ILE A 328 19608 21717 22436 672 1001 3995 C
ATOM 2490 CG1 ILE A 328 -35.918 18.998 28.678 1.00175.19 C
ANISOU 2490 CG1 ILE A 328 20804 22272 23487 521 793 3623 C
ATOM 2491 CG2 ILE A 328 -37.320 19.998 30.483 1.00171.08 C
ANISOU 2491 CG2 ILE A 328 20343 21910 22748 833 1438 3999 C
ATOM 2492 CD1 ILE A 328 -35.445 20.274 28.048 1.00181.89 C
ANISOU 2492 CD1 ILE A 328 21880 22920 24311 860 1140 3552 C
ATOM 2493 N ALA A 329 -40.307 17.855 29.362 1.00161.46 N
ANISOU 2493 N ALA A 329 17810 22081 21458 591 808 4809 N
ATOM 2494 CA ALA A 329 -41.668 17.882 29.888 1.00150.72 C
ANISOU 2494 CA ALA A 329 16099 21205 19962 710 985 5224 C
ATOM 2495 C ALA A 329 -42.025 16.567 30.570 1.00158.32 C
ANISOU 2495 C ALA A 329 16892 22335 20926 224 609 5262 C
ATOM 2496 O ALA A 329 -42.715 16.561 31.600 1.00162.65 O
ANISOU 2496 O ALA A 329 17355 23058 21387 234 780 5465 O
ATOM 2497 CB ALA A 329 -42.659 18.194 28.767 1.00134.80 C
ANISOU 2497 CB ALA A 329 13637 19724 17858 983 1049 5587 C
ATOM 2498 N ILE A 330 -41.543 15.443 30.029 1.00151.53 N
ANISOU 2498 N ILE A 330 16020 21400 20155 -202 111 5066 N
ATOM 2499 CA ILE A 330 -41.834 14.157 30.653 1.00154.97 C
ANISOU 2499 CA ILE A 330 16357 21943 20580 -685 -250 5088 C
ATOM 2500 C ILE A 330 -41.176 14.070 32.022 1.00177.98 C
ANISOU 2500 C ILE A 330 19634 24452 23538 -803 -175 4875 C
ATOM 2501 O ILE A 330 -41.793 13.618 32.994 1.00206.28 O
ANISOU 2501 O ILE A 330 23119 28205 27055 -978 -181 5035 O
ATOM 2502 CB ILE A 330 -41.386 12.992 29.751 1.00158.71 C
ANISOU 2502 CB ILE A 330 16833 22350 21118 -1091 -769 4903 C
ATOM 2503 CG1 ILE A 330 -41.852 13.198 28.313 1.00173.90 C
ANISOU 2503 CG1 ILE A 330 18465 24615 22994 -962 -832 5062 C
ATOM 2504 CG2 ILE A 330 -41.934 11.680 30.281 1.00161.54 C
ANISOU 2504 CG2 ILE A 330 17060 22896 21421 -1587 -1118 5003 C
ATOM 2505 CD1 ILE A 330 -41.513 12.052 27.386 1.00178.29 C
ANISOU 2505 CD1 ILE A 330 19046 25122 23573 -1368 -1325 4900 C
ATOM 2506 N VAL A 331 -39.916 14.504 32.124 1.00171.56 N
ANISOU 2506 N VAL A 331 19236 23127 22823 -727 -106 4523 N
ATOM 2507 CA VAL A 331 -39.248 14.479 33.421 1.00160.09 C
ANISOU 2507 CA VAL A 331 18127 21313 21387 -849 -34 4327 C
ATOM 2508 C VAL A 331 -39.894 15.469 34.383 1.00160.96 C
ANISOU 2508 C VAL A 331 18275 21510 21374 -547 456 4528 C
ATOM 2509 O VAL A 331 -39.957 15.217 35.594 1.00171.20 O
ANISOU 2509 O VAL A 331 19693 22730 22625 -700 499 4527 O
ATOM 2510 CB VAL A 331 -37.742 14.756 33.247 1.00158.74 C
ANISOU 2510 CB VAL A 331 18357 20636 21323 -853 -77 3931 C
ATOM 2511 CG1 VAL A 331 -37.028 14.704 34.589 1.00159.56 C
ANISOU 2511 CG1 VAL A 331 18797 20408 21419 -1017 -30 3741 C
ATOM 2512 CG2 VAL A 331 -37.132 13.751 32.281 1.00161.82 C
ANISOU 2512 CG2 VAL A 331 18715 20949 21819 -1106 -535 3754 C
ATOM 2513 N VAL A 332 -40.401 16.593 33.871 1.00149.71 N
ANISOU 2513 N VAL A 332 16765 20241 19878 -99 846 4715 N
ATOM 2514 CA VAL A 332 -41.105 17.545 34.727 1.00154.03 C
ANISOU 2514 CA VAL A 332 17364 20881 20282 246 1354 4942 C
ATOM 2515 C VAL A 332 -42.384 16.927 35.274 1.00163.77 C
ANISOU 2515 C VAL A 332 18194 22614 21419 149 1315 5309 C
ATOM 2516 O VAL A 332 -42.784 17.205 36.412 1.00162.23 O
ANISOU 2516 O VAL A 332 18094 22425 21119 232 1595 5424 O
ATOM 2517 CB VAL A 332 -41.381 18.852 33.953 1.00151.02 C
ANISOU 2517 CB VAL A 332 16989 20559 19835 785 1786 5086 C
ATOM 2518 CG1 VAL A 332 -42.485 19.664 34.616 1.00149.32 C
ANISOU 2518 CG1 VAL A 332 16685 20608 19441 1199 2298 5453 C
ATOM 2519 CG2 VAL A 332 -40.110 19.683 33.857 1.00148.02 C
ANISOU 2519 CG2 VAL A 332 17126 19615 19499 883 1955 4723 C
ATOM 2520 N SER A 333 -43.030 16.053 34.496 1.00176.46 N
ANISOU 2520 N SER A 333 19360 24647 23041 -64 961 5497 N
ATOM 2521 CA SER A 333 -44.273 15.448 34.962 1.00190.04 C
ANISOU 2521 CA SER A 333 20661 26897 24650 -203 905 5872 C
ATOM 2522 C SER A 333 -44.028 14.269 35.900 1.00202.55 C
ANISOU 2522 C SER A 333 22349 28342 26268 -723 562 5732 C
ATOM 2523 O SER A 333 -44.754 14.101 36.886 1.00213.04 O
ANISOU 2523 O SER A 333 23557 29894 27497 -774 686 5952 O
ATOM 2524 CB SER A 333 -45.118 15.005 33.768 1.00185.40 C
ANISOU 2524 CB SER A 333 19557 26864 24021 -270 664 6156 C
ATOM 2525 OG SER A 333 -46.404 14.582 34.189 1.00190.21 O
ANISOU 2525 OG SER A 333 19717 28066 24490 -370 666 6575 O
ATOM 2526 N LYS A 334 -43.014 13.447 35.621 1.00194.49 N
ANISOU 2526 N LYS A 334 21560 26957 25380 -1090 148 5383 N
ATOM 2527 CA LYS A 334 -42.888 12.156 36.291 1.00195.79 C
ANISOU 2527 CA LYS A 334 21775 27050 25568 -1601 -237 5296 C
ATOM 2528 C LYS A 334 -42.144 12.209 37.621 1.00214.92 C
ANISOU 2528 C LYS A 334 24604 29047 28010 -1672 -132 5071 C
ATOM 2529 O LYS A 334 -42.441 11.405 38.511 1.00228.47 O
ANISOU 2529 O LYS A 334 26299 30824 29685 -1983 -284 5137 O
ATOM 2530 CB LYS A 334 -42.201 11.151 35.361 1.00192.03 C
ANISOU 2530 CB LYS A 334 21367 26397 25197 -1947 -730 5060 C
ATOM 2531 CG LYS A 334 -43.055 10.746 34.174 1.00204.65 C
ANISOU 2531 CG LYS A 334 22558 28464 26737 -2049 -940 5299 C
ATOM 2532 CD LYS A 334 -42.444 9.583 33.413 1.00215.46 C
ANISOU 2532 CD LYS A 334 24059 29632 28174 -2456 -1436 5069 C
ATOM 2533 CE LYS A 334 -43.406 9.069 32.355 1.00220.59 C
ANISOU 2533 CE LYS A 334 24316 30781 28716 -2657 -1671 5328 C
ATOM 2534 NZ LYS A 334 -42.843 7.925 31.588 1.00222.41 N
ANISOU 2534 NZ LYS A 334 24738 30788 28981 -3060 -2135 5100 N
ATOM 2535 N LEU A 335 -41.184 13.119 37.788 1.00225.05 N
ANISOU 2535 N LEU A 335 24838 35432 25237 -8315 -1761 -1410 N
ATOM 2536 CA LEU A 335 -40.411 13.213 39.021 1.00224.00 C
ANISOU 2536 CA LEU A 335 24870 34989 25252 -8177 -1652 -1224 C
ATOM 2537 C LEU A 335 -40.946 14.280 39.969 1.00247.82 C
ANISOU 2537 C LEU A 335 27426 38264 28471 -7982 -1573 -1310 C
ATOM 2538 O LEU A 335 -40.205 14.756 40.836 1.00254.07 O
ANISOU 2538 O LEU A 335 28197 38849 29489 -7687 -1535 -1130 O
ATOM 2539 CB LEU A 335 -38.937 13.480 38.712 1.00200.90 C
ANISOU 2539 CB LEU A 335 22030 31634 22668 -7643 -1802 -871 C
ATOM 2540 CG LEU A 335 -38.171 12.360 38.006 1.00195.62 C
ANISOU 2540 CG LEU A 335 21900 30694 21734 -7926 -1844 -776 C
ATOM 2541 CD1 LEU A 335 -36.686 12.694 37.916 1.00205.05 C
ANISOU 2541 CD1 LEU A 335 23123 31620 23165 -7510 -1952 -430 C
ATOM 2542 CD2 LEU A 335 -38.391 11.033 38.717 1.00187.12 C
ANISOU 2542 CD2 LEU A 335 21437 29534 20125 -8709 -1634 -884 C
ATOM 2543 N LYS A 336 -42.220 14.656 39.824 1.00263.28 N
ANISOU 2543 N LYS A 336 29007 40673 30354 -8155 -1548 -1613 N
ATOM 2544 CA LYS A 336 -42.735 15.865 40.464 1.00270.55 C
ANISOU 2544 CA LYS A 336 29409 41814 31574 -7877 -1525 -1720 C
ATOM 2545 C LYS A 336 -42.652 15.804 41.985 1.00276.71 C
ANISOU 2545 C LYS A 336 30341 42540 32255 -8065 -1290 -1780 C
ATOM 2546 O LYS A 336 -42.492 16.843 42.636 1.00280.84 O
ANISOU 2546 O LYS A 336 30549 43054 33105 -7704 -1272 -1753 O
ATOM 2547 CB LYS A 336 -44.181 16.099 40.029 1.00266.91 C
ANISOU 2547 CB LYS A 336 28537 41853 31023 -8108 -1552 -2086 C
ATOM 2548 CG LYS A 336 -44.667 17.522 40.229 1.00258.51 C
ANISOU 2548 CG LYS A 336 26850 40960 30411 -7688 -1639 -2163 C
ATOM 2549 CD LYS A 336 -43.856 18.494 39.390 1.00242.42 C
ANISOU 2549 CD LYS A 336 24577 38681 28851 -7011 -1895 -1816 C
ATOM 2550 CE LYS A 336 -44.294 19.928 39.629 1.00241.97 C
ANISOU 2550 CE LYS A 336 23940 38701 29298 -6608 -1969 -1871 C
ATOM 2551 NZ LYS A 336 -43.488 20.884 38.824 1.00237.95 N
ANISOU 2551 NZ LYS A 336 23238 37921 29251 -5979 -2178 -1524 N
ATOM 2552 N ALA A 337 -42.758 14.613 42.570 1.00276.19 N
ANISOU 2552 N ALA A 337 30775 42432 31731 -8647 -1101 -1866 N
ATOM 2553 CA ALA A 337 -42.782 14.499 44.022 1.00274.30 C
ANISOU 2553 CA ALA A 337 30701 42208 31312 -8903 -878 -1936 C
ATOM 2554 C ALA A 337 -41.402 14.316 44.635 1.00268.16 C
ANISOU 2554 C ALA A 337 30261 41004 30623 -8681 -920 -1562 C
ATOM 2555 O ALA A 337 -41.152 14.821 45.736 1.00266.51 O
ANISOU 2555 O ALA A 337 29968 40818 30476 -8582 -829 -1540 O
ATOM 2556 CB ALA A 337 -43.679 13.332 44.447 1.00275.47 C
ANISOU 2556 CB ALA A 337 31234 42546 30887 -9701 -624 -2232 C
ATOM 2557 N ASN A 338 -40.502 13.609 43.958 1.00260.62 N
ANISOU 2557 N ASN A 338 29670 39677 29678 -8612 -1058 -1295 N
ATOM 2558 CA ASN A 338 -39.228 13.236 44.554 1.00249.50 C
ANISOU 2558 CA ASN A 338 28615 37860 28324 -8483 -1108 -970 C
ATOM 2559 C ASN A 338 -38.201 14.346 44.375 1.00239.04 C
ANISOU 2559 C ASN A 338 26919 36381 27524 -7736 -1261 -728 C
ATOM 2560 O ASN A 338 -38.051 14.898 43.280 1.00222.30 O
ANISOU 2560 O ASN A 338 24529 34238 25695 -7339 -1399 -679 O
ATOM 2561 CB ASN A 338 -38.707 11.933 43.943 1.00246.88 C
ANISOU 2561 CB ASN A 338 28868 37137 27799 -8768 -1177 -838 C
ATOM 2562 CG ASN A 338 -37.615 11.293 44.783 1.00242.81 C
ANISOU 2562 CG ASN A 338 28804 36201 27249 -8820 -1212 -557 C
ATOM 2563 OD1 ASN A 338 -37.013 11.943 45.637 1.00241.21 O
ANISOU 2563 OD1 ASN A 338 28400 36011 27239 -8510 -1235 -404 O
ATOM 2564 ND2 ASN A 338 -37.355 10.011 44.545 1.00242.81 N
ANISOU 2564 ND2 ASN A 338 29481 36018 26756 -9459 -1189 -469 N
ATOM 2565 N LEU A 339 -37.493 14.658 45.459 1.00246.77 N
ANISOU 2565 N LEU A 339 27902 37270 28591 -7576 -1222 -586 N
ATOM 2566 CA LEU A 339 -36.311 15.513 45.420 1.00236.46 C
ANISOU 2566 CA LEU A 339 26350 35756 27738 -6928 -1325 -351 C
ATOM 2567 C LEU A 339 -35.305 14.974 46.423 1.00234.50 C
ANISOU 2567 C LEU A 339 26410 35287 27404 -6994 -1338 -128 C
ATOM 2568 O LEU A 339 -35.566 14.971 47.630 1.00220.74 O
ANISOU 2568 O LEU A 339 24720 33723 25427 -7265 -1216 -195 O
ATOM 2569 CB LEU A 339 -36.645 16.977 45.732 1.00234.38 C
ANISOU 2569 CB LEU A 339 25554 35718 27782 -6548 -1248 -494 C
ATOM 2570 CG LEU A 339 -37.032 17.869 44.548 1.00222.65 C
ANISOU 2570 CG LEU A 339 23675 34285 26637 -6171 -1336 -557 C
ATOM 2571 CD1 LEU A 339 -37.492 19.250 45.010 1.00216.97 C
ANISOU 2571 CD1 LEU A 339 22485 33731 26224 -5898 -1251 -732 C
ATOM 2572 CD2 LEU A 339 -35.873 17.991 43.570 1.00207.79 C
ANISOU 2572 CD2 LEU A 339 21816 32075 25061 -5698 -1484 -285 C
ATOM 2573 N MET A 340 -34.171 14.512 45.918 1.00236.76 N
ANISOU 2573 N MET A 340 26885 35202 27870 -6764 -1494 123 N
ATOM 2574 CA MET A 340 -33.042 14.085 46.725 1.00227.40 C
ANISOU 2574 CA MET A 340 25913 33776 26712 -6718 -1569 366 C
ATOM 2575 C MET A 340 -31.841 14.938 46.342 1.00203.98 C
ANISOU 2575 C MET A 340 22602 30661 24241 -6014 -1648 517 C
ATOM 2576 O MET A 340 -31.884 15.707 45.378 1.00203.99 O
ANISOU 2576 O MET A 340 22307 30679 24522 -5627 -1645 456 O
ATOM 2577 CB MET A 340 -32.755 12.593 46.519 1.00236.96 C
ANISOU 2577 CB MET A 340 27765 34897 27370 -7438 -1689 595 C
ATOM 2578 CG MET A 340 -32.141 12.260 45.170 1.00235.70 C
ANISOU 2578 CG MET A 340 27719 34585 27249 -7392 -1851 751 C
ATOM 2579 SD MET A 340 -32.268 10.517 44.726 1.00247.04 S
ANISOU 2579 SD MET A 340 30093 35795 27975 -8423 -1929 876 S
ATOM 2580 CE MET A 340 -34.001 10.405 44.285 1.00253.81 C
ANISOU 2580 CE MET A 340 30921 36881 28633 -8701 -1680 397 C
ATOM 2581 N CYS A 341 -30.766 14.832 47.127 1.00192.73 N
ANISOU 2581 N CYS A 341 21210 29142 22875 -5888 -1713 722 N
ATOM 2582 CA CYS A 341 -29.580 15.627 46.824 1.00179.41 C
ANISOU 2582 CA CYS A 341 19195 27300 21671 -5203 -1745 809 C
ATOM 2583 C CYS A 341 -29.002 15.240 45.467 1.00156.47 C
ANISOU 2583 C CYS A 341 16352 24326 18773 -5154 -1898 999 C
ATOM 2584 O CYS A 341 -28.523 16.102 44.712 1.00136.57 O
ANISOU 2584 O CYS A 341 13533 21646 16713 -4536 -1847 919 O
ATOM 2585 CB CYS A 341 -28.545 15.464 47.937 1.00171.31 C
ANISOU 2585 CB CYS A 341 18171 26384 20534 -5226 -1824 1053 C
ATOM 2586 SG CYS A 341 -27.210 16.673 47.900 1.00163.60 S
ANISOU 2586 SG CYS A 341 16744 25233 20182 -4335 -1754 1005 S
ATOM 2587 N LYS A 342 -29.078 13.953 45.118 1.00162.57 N
ANISOU 2587 N LYS A 342 17590 25148 19032 -5857 -2079 1230 N
ATOM 2588 CA LYS A 342 -28.675 13.536 43.780 1.00165.97 C
ANISOU 2588 CA LYS A 342 18145 25473 19444 -5908 -2233 1371 C
ATOM 2589 C LYS A 342 -29.560 14.161 42.711 1.00168.80 C
ANISOU 2589 C LYS A 342 18285 25868 19984 -5647 -2101 1061 C
ATOM 2590 O LYS A 342 -29.073 14.501 41.629 1.00182.47 O
ANISOU 2590 O LYS A 342 19849 27554 21929 -5308 -2156 1113 O
ATOM 2591 CB LYS A 342 -28.703 12.010 43.663 1.00191.02 C
ANISOU 2591 CB LYS A 342 22059 28483 22036 -6832 -2438 1599 C
ATOM 2592 CG LYS A 342 -28.676 11.529 42.221 1.00200.46 C
ANISOU 2592 CG LYS A 342 23517 29513 23137 -7036 -2534 1586 C
ATOM 2593 CD LYS A 342 -28.374 10.051 42.093 1.00204.26 C
ANISOU 2593 CD LYS A 342 24943 29501 23165 -7916 -2723 1798 C
ATOM 2594 CE LYS A 342 -28.366 9.636 40.629 1.00202.31 C
ANISOU 2594 CE LYS A 342 25071 28964 22836 -7917 -2670 1674 C
ATOM 2595 NZ LYS A 342 -27.874 8.246 40.433 1.00204.02 N
ANISOU 2595 NZ LYS A 342 26527 28230 22762 -7906 -2481 1836 N
ATOM 2596 N THR A 343 -30.852 14.340 42.995 1.00162.40 N
ANISOU 2596 N THR A 343 17451 25155 19097 -5800 -1954 765 N
ATOM 2597 CA THR A 343 -31.701 15.069 42.060 1.00163.86 C
ANISOU 2597 CA THR A 343 17359 25377 19523 -5503 -1897 520 C
ATOM 2598 C THR A 343 -31.274 16.527 41.956 1.00168.14 C
ANISOU 2598 C THR A 343 17431 25866 20587 -4780 -1827 503 C
ATOM 2599 O THR A 343 -31.377 17.129 40.880 1.00182.15 O
ANISOU 2599 O THR A 343 19007 27674 22528 -4510 -1856 488 O
ATOM 2600 CB THR A 343 -33.166 14.959 42.479 1.00137.35 C
ANISOU 2600 CB THR A 343 14030 22218 15938 -5885 -1793 260 C
ATOM 2601 OG1 THR A 343 -33.528 13.577 42.597 1.00125.88 O
ANISOU 2601 OG1 THR A 343 13103 20811 13914 -6653 -1801 266 O
ATOM 2602 CG2 THR A 343 -34.076 15.615 41.446 1.00117.49 C
ANISOU 2602 CG2 THR A 343 11217 19961 13465 -5792 -1806 112 C
ATOM 2603 N ASP A 344 -30.778 17.104 43.054 1.00171.71 N
ANISOU 2603 N ASP A 344 17733 26333 21177 -4578 -1731 544 N
ATOM 2604 CA ASP A 344 -30.229 18.453 42.988 1.00181.66 C
ANISOU 2604 CA ASP A 344 18627 27570 22826 -4018 -1635 550 C
ATOM 2605 C ASP A 344 -28.979 18.508 42.122 1.00169.59 C
ANISOU 2605 C ASP A 344 17084 25770 21583 -3580 -1684 683 C
ATOM 2606 O ASP A 344 -28.690 19.549 41.522 1.00164.43 O
ANISOU 2606 O ASP A 344 16191 25067 21219 -3165 -1609 673 O
ATOM 2607 CB ASP A 344 -29.914 18.973 44.390 1.00199.55 C
ANISOU 2607 CB ASP A 344 20776 29910 25132 -3956 -1516 523 C
ATOM 2608 CG ASP A 344 -31.152 19.426 45.139 1.00214.57 C
ANISOU 2608 CG ASP A 344 22555 32111 26861 -4250 -1413 323 C
ATOM 2609 OD1 ASP A 344 -32.270 19.051 44.729 1.00218.86 O
ANISOU 2609 OD1 ASP A 344 23156 32816 27183 -4590 -1444 213 O
ATOM 2610 OD2 ASP A 344 -31.006 20.167 46.135 1.00234.65 O
ANISOU 2610 OD2 ASP A 344 24929 34743 29486 -4151 -1295 242 O
ATOM 2611 N ILE A 345 -28.228 17.409 42.044 1.00178.24 N
ANISOU 2611 N ILE A 345 18439 26671 22613 -3678 -1806 790 N
ATOM 2612 CA ILE A 345 -27.007 17.390 41.243 1.00185.35 C
ANISOU 2612 CA ILE A 345 19269 27516 23639 -3375 -1870 993 C
ATOM 2613 C ILE A 345 -27.359 17.158 39.778 1.00177.85 C
ANISOU 2613 C ILE A 345 18368 26679 22529 -3518 -1973 1060 C
ATOM 2614 O ILE A 345 -27.150 18.034 38.930 1.00179.88 O
ANISOU 2614 O ILE A 345 18429 26832 23086 -3065 -1892 990 O
ATOM 2615 CB ILE A 345 -26.027 16.315 41.749 1.00189.53 C
ANISOU 2615 CB ILE A 345 19950 28156 23905 -3663 -2070 1358 C
ATOM 2616 CG1 ILE A 345 -25.797 16.473 43.250 1.00207.48 C
ANISOU 2616 CG1 ILE A 345 22178 30435 26223 -3614 -2003 1319 C
ATOM 2617 CG2 ILE A 345 -24.691 16.415 41.022 1.00163.33 C
ANISOU 2617 CG2 ILE A 345 16456 24761 20840 -3214 -2133 1575 C
ATOM 2618 CD1 ILE A 345 -25.190 15.256 43.894 1.00223.89 C
ANISOU 2618 CD1 ILE A 345 24482 32662 27926 -4104 -2301 1750 C
ATOM 2619 N LYS A 346 -27.896 15.974 39.478 1.00174.22 N
ANISOU 2619 N LYS A 346 18232 26407 21559 -4214 -2149 1171 N
ATOM 2620 CA LYS A 346 -28.157 15.593 38.095 1.00192.17 C
ANISOU 2620 CA LYS A 346 20623 28807 23585 -4466 -2274 1214 C
ATOM 2621 C LYS A 346 -29.214 16.476 37.444 1.00193.13 C
ANISOU 2621 C LYS A 346 20519 29027 23836 -4237 -2186 974 C
ATOM 2622 O LYS A 346 -29.159 16.705 36.231 1.00205.76 O
ANISOU 2622 O LYS A 346 22037 30741 25401 -4136 -2256 1032 O
ATOM 2623 CB LYS A 346 -28.583 14.124 38.035 1.00208.72 C
ANISOU 2623 CB LYS A 346 23280 30941 25086 -5369 -2433 1253 C
ATOM 2624 CG LYS A 346 -27.896 13.327 36.941 1.00219.34 C
ANISOU 2624 CG LYS A 346 24956 32196 26186 -5723 -2645 1420 C
ATOM 2625 CD LYS A 346 -26.390 13.290 37.157 1.00213.81 C
ANISOU 2625 CD LYS A 346 24227 31213 25797 -5297 -2732 1739 C
ATOM 2626 CE LYS A 346 -25.694 12.442 36.105 1.00196.81 C
ANISOU 2626 CE LYS A 346 22925 28379 23475 -5007 -2554 1770 C
ATOM 2627 NZ LYS A 346 -24.213 12.453 36.275 1.00170.11 N
ANISOU 2627 NZ LYS A 346 19682 24471 20479 -4145 -2418 1986 N
ATOM 2628 N CYS A 347 -30.182 16.974 38.219 1.00182.88 N
ANISOU 2628 N CYS A 347 19112 27688 22687 -4178 -2071 733 N
ATOM 2629 CA CYS A 347 -31.166 17.888 37.647 1.00176.56 C
ANISOU 2629 CA CYS A 347 18055 26956 22072 -3964 -2052 561 C
ATOM 2630 C CYS A 347 -30.510 19.197 37.223 1.00160.03 C
ANISOU 2630 C CYS A 347 15647 24792 20364 -3376 -1975 663 C
ATOM 2631 O CYS A 347 -30.820 19.745 36.156 1.00152.66 O
ANISOU 2631 O CYS A 347 14560 23973 19471 -3226 -2040 691 O
ATOM 2632 CB CYS A 347 -32.284 18.142 38.657 1.00195.61 C
ANISOU 2632 CB CYS A 347 20354 29613 24357 -4237 -1969 425 C
ATOM 2633 SG CYS A 347 -33.740 18.967 37.983 1.00214.01 S
ANISOU 2633 SG CYS A 347 22336 32317 26661 -4283 -2022 286 S
ATOM 2634 N ARG A 348 -29.580 19.697 38.038 1.00149.59 N
ANISOU 2634 N ARG A 348 14249 23281 19306 -3059 -1832 712 N
ATOM 2635 CA ARG A 348 -28.814 20.874 37.652 1.00146.21 C
ANISOU 2635 CA ARG A 348 13601 22721 19232 -2540 -1711 774 C
ATOM 2636 C ARG A 348 -27.925 20.584 36.450 1.00147.24 C
ANISOU 2636 C ARG A 348 13821 22712 19411 -2321 -1763 874 C
ATOM 2637 O ARG A 348 -27.700 21.471 35.615 1.00143.27 O
ANISOU 2637 O ARG A 348 13165 22194 19077 -2005 -1708 933 O
ATOM 2638 CB ARG A 348 -27.992 21.363 38.845 1.00150.37 C
ANISOU 2638 CB ARG A 348 14064 23091 19979 -2317 -1541 748 C
ATOM 2639 CG ARG A 348 -27.340 22.712 38.648 1.00180.95 C
ANISOU 2639 CG ARG A 348 17727 26815 24209 -1862 -1369 736 C
ATOM 2640 CD ARG A 348 -28.305 23.714 38.039 1.00204.42 C
ANISOU 2640 CD ARG A 348 20476 29911 27285 -1818 -1376 708 C
ATOM 2641 NE ARG A 348 -29.470 23.971 38.881 1.00215.35 N
ANISOU 2641 NE ARG A 348 21718 31473 28632 -2076 -1392 581 N
ATOM 2642 CZ ARG A 348 -29.568 24.990 39.729 1.00221.40 C
ANISOU 2642 CZ ARG A 348 22278 32177 29667 -1969 -1255 458 C
ATOM 2643 NH1 ARG A 348 -28.567 25.850 39.856 1.00228.45 N
ANISOU 2643 NH1 ARG A 348 23102 32827 30871 -1633 -1088 434 N
ATOM 2644 NH2 ARG A 348 -30.670 25.149 40.450 1.00233.32 N
ANISOU 2644 NH2 ARG A 348 23646 33867 31138 -2225 -1275 329 N
ATOM 2645 N LEU A 349 -27.426 19.351 36.333 1.00155.83 N
ANISOU 2645 N LEU A 349 15120 23845 20242 -2585 -1886 992 N
ATOM 2646 CA LEU A 349 -26.688 18.974 35.131 1.00163.73 C
ANISOU 2646 CA LEU A 349 16123 25021 21065 -2588 -1990 1264 C
ATOM 2647 C LEU A 349 -27.593 18.992 33.903 1.00138.84 C
ANISOU 2647 C LEU A 349 12962 22178 17615 -2825 -2140 1298 C
ATOM 2648 O LEU A 349 -27.159 19.366 32.805 1.00138.17 O
ANISOU 2648 O LEU A 349 12771 22200 17529 -2615 -2160 1463 O
ATOM 2649 CB LEU A 349 -26.057 17.595 35.324 1.00186.44 C
ANISOU 2649 CB LEU A 349 19210 28006 23623 -3026 -2170 1494 C
ATOM 2650 CG LEU A 349 -25.248 16.998 34.174 1.00198.77 C
ANISOU 2650 CG LEU A 349 20812 29699 25013 -3140 -2340 1770 C
ATOM 2651 CD1 LEU A 349 -24.172 17.965 33.711 1.00204.09 C
ANISOU 2651 CD1 LEU A 349 21176 30222 26146 -2382 -2125 1858 C
ATOM 2652 CD2 LEU A 349 -24.630 15.679 34.607 1.00220.33 C
ANISOU 2652 CD2 LEU A 349 23992 32192 27532 -3493 -2481 1913 C
ATOM 2653 N ALA A 350 -28.863 18.613 34.075 1.00121.79 N
ANISOU 2653 N ALA A 350 10898 20191 15184 -3254 -2236 1137 N
ATOM 2654 CA ALA A 350 -29.824 18.751 32.986 1.00119.25 C
ANISOU 2654 CA ALA A 350 10517 20191 14602 -3430 -2380 1114 C
ATOM 2655 C ALA A 350 -30.056 20.215 32.646 1.00126.79 C
ANISOU 2655 C ALA A 350 11156 21026 15992 -2870 -2302 1083 C
ATOM 2656 O ALA A 350 -30.262 20.556 31.473 1.00139.32 O
ANISOU 2656 O ALA A 350 12631 22882 17424 -2821 -2425 1223 O
ATOM 2657 CB ALA A 350 -31.141 18.071 33.347 1.00118.37 C
ANISOU 2657 CB ALA A 350 10545 20260 14169 -3968 -2454 889 C
ATOM 2658 N LYS A 351 -30.017 21.098 33.649 1.00125.53 N
ANISOU 2658 N LYS A 351 10864 20531 16300 -2527 -2113 934 N
ATOM 2659 CA LYS A 351 -30.057 22.525 33.348 1.00128.78 C
ANISOU 2659 CA LYS A 351 10977 20959 16996 -2142 -2025 1019 C
ATOM 2660 C LYS A 351 -28.830 22.953 32.556 1.00133.27 C
ANISOU 2660 C LYS A 351 11567 21329 17739 -1738 -1924 1163 C
ATOM 2661 O LYS A 351 -28.918 23.847 31.705 1.00145.79 O
ANISOU 2661 O LYS A 351 12987 22991 19414 -1497 -1931 1287 O
ATOM 2662 CB LYS A 351 -30.168 23.344 34.634 1.00131.69 C
ANISOU 2662 CB LYS A 351 11175 21220 17640 -2036 -1842 923 C
ATOM 2663 CG LYS A 351 -30.344 24.838 34.391 1.00146.68 C
ANISOU 2663 CG LYS A 351 12767 23099 19864 -1705 -1757 958 C
ATOM 2664 CD LYS A 351 -29.362 25.668 35.204 1.00186.54 C
ANISOU 2664 CD LYS A 351 17779 27844 25255 -1407 -1495 902 C
ATOM 2665 CE LYS A 351 -30.044 26.337 36.387 1.00210.13 C
ANISOU 2665 CE LYS A 351 20556 30829 28453 -1490 -1419 717 C
ATOM 2666 NZ LYS A 351 -29.086 27.153 37.186 1.00216.89 N
ANISOU 2666 NZ LYS A 351 21376 31407 29626 -1247 -1175 614 N
ATOM 2667 N SER A 352 -27.683 22.313 32.804 1.00128.44 N
ANISOU 2667 N SER A 352 11146 20475 17179 -1658 -1833 1148 N
ATOM 2668 CA SER A 352 -26.480 22.644 32.048 1.00146.20 C
ANISOU 2668 CA SER A 352 13361 22669 19519 -1327 -1714 1350 C
ATOM 2669 C SER A 352 -26.621 22.242 30.585 1.00116.16 C
ANISOU 2669 C SER A 352 9507 19349 15279 -1511 -1924 1707 C
ATOM 2670 O SER A 352 -26.370 23.049 29.680 1.00106.65 O
ANISOU 2670 O SER A 352 8177 18197 14149 -1222 -1869 1885 O
ATOM 2671 CB SER A 352 -25.263 21.966 32.677 1.00162.08 C
ANISOU 2671 CB SER A 352 15474 24508 21600 -1256 -1603 1370 C
ATOM 2672 OG SER A 352 -24.112 22.139 31.868 1.00 70.55 O
ANISOU 2672 OG SER A 352 3822 12890 10092 -944 -1479 1571 O
ATOM 2673 N THR A 353 -27.042 20.999 30.331 1.00116.84 N
ANISOU 2673 N THR A 353 9728 19804 14861 -2055 -2176 1787 N
ATOM 2674 CA THR A 353 -27.202 20.565 28.947 1.00136.84 C
ANISOU 2674 CA THR A 353 12284 22826 16881 -2342 -2417 2023 C
ATOM 2675 C THR A 353 -28.301 21.343 28.229 1.00141.49 C
ANISOU 2675 C THR A 353 12718 23681 17361 -2299 -2546 2044 C
ATOM 2676 O THR A 353 -28.176 21.614 27.028 1.00145.92 O
ANISOU 2676 O THR A 353 13207 24572 17664 -2236 -2666 2309 O
ATOM 2677 CB THR A 353 -27.490 19.066 28.888 1.00141.54 C
ANISOU 2677 CB THR A 353 13199 23676 16903 -3078 -2659 1940 C
ATOM 2678 OG1 THR A 353 -28.665 18.775 29.653 1.00151.68 O
ANISOU 2678 OG1 THR A 353 14578 24945 18109 -3401 -2688 1665 O
ATOM 2679 CG2 THR A 353 -26.313 18.279 29.447 1.00133.27 C
ANISOU 2679 CG2 THR A 353 12285 22391 15962 -3137 -2611 2000 C
ATOM 2680 N LEU A 354 -29.369 21.727 28.940 1.00141.70 N
ANISOU 2680 N LEU A 354 12669 23587 17583 -2314 -2542 1786 N
ATOM 2681 CA LEU A 354 -30.403 22.549 28.315 1.00145.61 C
ANISOU 2681 CA LEU A 354 12944 24307 18074 -2210 -2688 1808 C
ATOM 2682 C LEU A 354 -29.851 23.915 27.937 1.00147.20 C
ANISOU 2682 C LEU A 354 12947 24297 18685 -1634 -2534 1998 C
ATOM 2683 O LEU A 354 -30.004 24.364 26.795 1.00159.98 O
ANISOU 2683 O LEU A 354 14435 26261 20089 -1531 -2685 2298 O
ATOM 2684 CB LEU A 354 -31.607 22.704 29.252 1.00169.62 C
ANISOU 2684 CB LEU A 354 15900 27205 21342 -2314 -2704 1457 C
ATOM 2685 CG LEU A 354 -32.907 23.379 28.770 1.00190.83 C
ANISOU 2685 CG LEU A 354 18312 30141 24055 -2278 -2914 1402 C
ATOM 2686 CD1 LEU A 354 -34.041 23.052 29.726 1.00202.08 C
ANISOU 2686 CD1 LEU A 354 19666 31608 25509 -2592 -2936 1099 C
ATOM 2687 CD2 LEU A 354 -32.807 24.899 28.617 1.00201.81 C
ANISOU 2687 CD2 LEU A 354 19411 31359 25908 -1759 -2830 1531 C
ATOM 2688 N THR A 355 -29.205 24.595 28.889 1.00146.84 N
ANISOU 2688 N THR A 355 12910 23691 19194 -1285 -2229 1805 N
ATOM 2689 CA THR A 355 -28.714 25.940 28.620 1.00171.79 C
ANISOU 2689 CA THR A 355 15940 26589 22744 -811 -2033 1880 C
ATOM 2690 C THR A 355 -27.626 25.938 27.560 1.00173.48 C
ANISOU 2690 C THR A 355 16171 26967 22777 -630 -1958 2304 C
ATOM 2691 O THR A 355 -27.414 26.959 26.898 1.00171.43 O
ANISOU 2691 O THR A 355 15785 26690 22660 -309 -1868 2533 O
ATOM 2692 CB THR A 355 -28.195 26.593 29.903 1.00179.13 C
ANISOU 2692 CB THR A 355 16841 27140 24080 -644 -1717 1693 C
ATOM 2693 OG1 THR A 355 -27.291 25.704 30.572 1.00174.86 O
ANISOU 2693 OG1 THR A 355 16530 26379 23531 -718 -1597 1550 O
ATOM 2694 CG2 THR A 355 -29.353 26.940 30.828 1.00171.54 C
ANISOU 2694 CG2 THR A 355 15673 26289 23216 -821 -1779 1543 C
ATOM 2695 N LEU A 356 -26.923 24.817 27.400 1.00181.83 N
ANISOU 2695 N LEU A 356 17367 28180 23541 -830 -1984 2419 N
ATOM 2696 CA LEU A 356 -25.915 24.723 26.354 1.00146.56 C
ANISOU 2696 CA LEU A 356 12876 23909 18900 -669 -1920 2806 C
ATOM 2697 C LEU A 356 -26.525 24.427 24.986 1.00130.63 C
ANISOU 2697 C LEU A 356 10806 22578 16249 -916 -2288 3168 C
ATOM 2698 O LEU A 356 -26.183 25.084 23.999 1.00146.46 O
ANISOU 2698 O LEU A 356 12706 24766 18177 -633 -2260 3548 O
ATOM 2699 CB LEU A 356 -24.881 23.657 26.710 1.00145.81 C
ANISOU 2699 CB LEU A 356 12906 23716 18779 -765 -1822 2753 C
ATOM 2700 CG LEU A 356 -23.619 23.726 25.848 1.00188.91 C
ANISOU 2700 CG LEU A 356 18284 29215 24276 -440 -1608 3058 C
ATOM 2701 CD1 LEU A 356 -22.642 24.756 26.403 1.00194.00 C
ANISOU 2701 CD1 LEU A 356 18949 29204 25556 94 -1116 2863 C
ATOM 2702 CD2 LEU A 356 -22.952 22.366 25.680 1.00195.25 C
ANISOU 2702 CD2 LEU A 356 19477 29945 24766 -670 -1601 2972 C
ATOM 2703 N ILE A 357 -27.433 23.462 24.894 1.00135.03 N
ANISOU 2703 N ILE A 357 11488 23518 16298 -1462 -2631 3029 N
ATOM 2704 CA ILE A 357 -27.950 23.023 23.597 1.00149.69 C
ANISOU 2704 CA ILE A 357 13446 26027 17401 -1804 -3011 3233 C
ATOM 2705 C ILE A 357 -29.333 23.594 23.312 1.00153.34 C
ANISOU 2705 C ILE A 357 13755 26738 17772 -1834 -3234 3206 C
ATOM 2706 O ILE A 357 -29.573 24.149 22.240 1.00159.60 O
ANISOU 2706 O ILE A 357 14475 27891 18275 -1685 -3416 3532 O
ATOM 2707 CB ILE A 357 -27.938 21.480 23.508 1.00169.69 C
ANISOU 2707 CB ILE A 357 16360 28805 19309 -2489 -3226 3000 C
ATOM 2708 CG1 ILE A 357 -26.543 21.007 23.109 1.00158.10 C
ANISOU 2708 CG1 ILE A 357 15440 26849 17782 -2311 -2867 3006 C
ATOM 2709 CG2 ILE A 357 -28.993 20.982 22.523 1.00174.73 C
ANISOU 2709 CG2 ILE A 357 17233 29998 19158 -2998 -3581 2916 C
ATOM 2710 CD1 ILE A 357 -26.229 21.180 21.634 1.00167.58 C
ANISOU 2710 CD1 ILE A 357 17101 28097 18474 -2196 -2772 3183 C
ATOM 2711 N ALA A 358 -30.253 23.488 24.271 1.00176.01 N
ANISOU 2711 N ALA A 358 16565 29421 20891 -1989 -3230 2833 N
ATOM 2712 CA ALA A 358 -31.624 23.917 24.024 1.00215.35 C
ANISOU 2712 CA ALA A 358 21350 34669 25805 -2032 -3473 2753 C
ATOM 2713 C ALA A 358 -31.733 25.437 23.961 1.00229.20 C
ANISOU 2713 C ALA A 358 22794 36212 28079 -1449 -3393 2956 C
ATOM 2714 O ALA A 358 -32.317 25.990 23.021 1.00200.42 O
ANISOU 2714 O ALA A 358 18985 32948 24219 -1323 -3649 3219 O
ATOM 2715 CB ALA A 358 -32.544 23.355 25.104 1.00225.09 C
ANISOU 2715 CB ALA A 358 22602 35746 27174 -2354 -3467 2283 C
ATOM 2716 N LEU A 359 -31.175 26.134 24.955 1.00249.27 N
ANISOU 2716 N LEU A 359 25290 38139 31283 -1111 -3044 2809 N
ATOM 2717 CA LEU A 359 -31.305 27.587 24.996 1.00250.08 C
ANISOU 2717 CA LEU A 359 25152 37972 31894 -637 -2932 2893 C
ATOM 2718 C LEU A 359 -30.530 28.275 23.879 1.00248.46 C
ANISOU 2718 C LEU A 359 24906 37916 31583 -291 -2877 3453 C
ATOM 2719 O LEU A 359 -30.951 29.337 23.405 1.00272.08 O
ANISOU 2719 O LEU A 359 27681 40963 34735 19 -2952 3694 O
ATOM 2720 CB LEU A 359 -30.845 28.119 26.353 1.00251.72 C
ANISOU 2720 CB LEU A 359 25412 37476 32756 -449 -2555 2473 C
ATOM 2721 CG LEU A 359 -30.943 29.634 26.552 1.00251.63 C
ANISOU 2721 CG LEU A 359 25153 37225 33229 -66 -2389 2515 C
ATOM 2722 CD1 LEU A 359 -32.357 30.131 26.276 1.00259.02 C
ANISOU 2722 CD1 LEU A 359 25739 38508 34170 -70 -2712 2563 C
ATOM 2723 CD2 LEU A 359 -30.500 30.012 27.955 1.00251.10 C
ANISOU 2723 CD2 LEU A 359 25073 36790 33544 -59 -2035 2266 C
ATOM 2724 N LEU A 360 -29.413 27.700 23.436 1.00201.10 N
ANISOU 2724 N LEU A 360 19096 31987 25325 -320 -2750 3686 N
ATOM 2725 CA LEU A 360 -28.512 28.408 22.535 1.00160.88 C
ANISOU 2725 CA LEU A 360 13976 26920 20233 68 -2585 4201 C
ATOM 2726 C LEU A 360 -28.403 27.775 21.158 1.00159.41 C
ANISOU 2726 C LEU A 360 13919 27394 19257 -91 -2904 4640 C
ATOM 2727 O LEU A 360 -28.567 28.474 20.152 1.00158.41 O
ANISOU 2727 O LEU A 360 13746 27539 18904 162 -3043 5111 O
ATOM 2728 CB LEU A 360 -27.111 28.525 23.156 1.00102.54 C
ANISOU 2728 CB LEU A 360 6697 18969 13294 296 -2084 4080 C
ATOM 2729 CG LEU A 360 -26.077 29.348 22.369 1.00131.16 C
ANISOU 2729 CG LEU A 360 10289 22490 17058 745 -1767 4551 C
ATOM 2730 CD1 LEU A 360 -26.676 30.610 21.755 1.00141.78 C
ANISOU 2730 CD1 LEU A 360 11454 23909 18505 1051 -1831 4936 C
ATOM 2731 CD2 LEU A 360 -24.901 29.726 23.255 1.00139.78 C
ANISOU 2731 CD2 LEU A 360 11494 22873 18744 966 -1221 4200 C
ATOM 2732 N ALA A 361 -28.118 26.473 21.079 1.00144.97 N
ANISOU 2732 N ALA A 361 12333 25812 16939 -524 -3038 4478 N
ATOM 2733 CA ALA A 361 -27.783 25.878 19.789 1.00144.14 C
ANISOU 2733 CA ALA A 361 12541 26248 15977 -711 -3301 4803 C
ATOM 2734 C ALA A 361 -28.931 26.028 18.798 1.00165.10 C
ANISOU 2734 C ALA A 361 15268 29435 18026 -873 -3730 4954 C
ATOM 2735 O ALA A 361 -28.729 26.483 17.666 1.00191.83 O
ANISOU 2735 O ALA A 361 18847 33083 20956 -668 -3830 5420 O
ATOM 2736 CB ALA A 361 -27.399 24.407 19.966 1.00140.04 C
ANISOU 2736 CB ALA A 361 12440 25757 15012 -1254 -3333 4424 C
ATOM 2737 N THR A 362 -30.155 25.705 19.222 1.00158.04 N
ANISOU 2737 N THR A 362 14236 28674 17139 -1197 -3957 4568 N
ATOM 2738 CA THR A 362 -31.285 25.798 18.302 1.00174.07 C
ANISOU 2738 CA THR A 362 16265 31233 18639 -1332 -4372 4651 C
ATOM 2739 C THR A 362 -31.601 27.243 17.931 1.00186.85 C
ANISOU 2739 C THR A 362 17574 32809 20613 -733 -4419 5098 C
ATOM 2740 O THR A 362 -32.182 27.491 16.869 1.00196.77 O
ANISOU 2740 O THR A 362 18894 34516 21354 -694 -4760 5372 O
ATOM 2741 CB THR A 362 -32.522 25.121 18.896 1.00186.48 C
ANISOU 2741 CB THR A 362 17716 32942 20198 -1777 -4562 4113 C
ATOM 2742 OG1 THR A 362 -33.511 24.963 17.871 1.00179.45 O
ANISOU 2742 OG1 THR A 362 16865 32650 18669 -1986 -4974 4138 O
ATOM 2743 CG2 THR A 362 -33.114 25.965 20.010 1.00208.66 C
ANISOU 2743 CG2 THR A 362 20098 35325 23858 -1450 -4428 3939 C
ATOM 2744 N VAL A 363 -31.249 28.206 18.785 1.00193.99 N
ANISOU 2744 N VAL A 363 18184 33151 22372 -286 -4072 5142 N
ATOM 2745 CA VAL A 363 -31.493 29.606 18.447 1.00214.32 C
ANISOU 2745 CA VAL A 363 20510 35614 25307 263 -4070 5557 C
ATOM 2746 C VAL A 363 -30.618 30.020 17.271 1.00210.43 C
ANISOU 2746 C VAL A 363 20279 35258 24415 567 -4013 6214 C
ATOM 2747 O VAL A 363 -31.107 30.535 16.256 1.00224.03 O
ANISOU 2747 O VAL A 363 22061 37316 25745 755 -4314 6632 O
ATOM 2748 CB VAL A 363 -31.259 30.500 19.680 1.00198.95 C
ANISOU 2748 CB VAL A 363 18300 32964 24329 577 -3640 5328 C
ATOM 2749 CG1 VAL A 363 -31.013 31.946 19.268 1.00205.48 C
ANISOU 2749 CG1 VAL A 363 18975 33559 25536 1152 -3471 5829 C
ATOM 2750 CG2 VAL A 363 -32.442 30.408 20.635 1.00199.53 C
ANISOU 2750 CG2 VAL A 363 18150 32943 24720 375 -3794 4757 C
ATOM 2751 N GLU A 364 -29.312 29.765 17.381 1.00192.74 N
ANISOU 2751 N GLU A 364 18247 32752 22232 627 -3629 6305 N
ATOM 2752 CA GLU A 364 -28.390 30.082 16.299 1.00171.12 C
ANISOU 2752 CA GLU A 364 15876 30079 19063 909 -3497 6905 C
ATOM 2753 C GLU A 364 -28.670 29.259 15.047 1.00203.34 C
ANISOU 2753 C GLU A 364 20516 34766 21979 504 -3901 7013 C
ATOM 2754 O GLU A 364 -28.497 29.761 13.931 1.00215.57 O
ANISOU 2754 O GLU A 364 22434 36447 23024 712 -3933 7521 O
ATOM 2755 CB GLU A 364 -26.951 29.863 16.765 1.00157.55 C
ANISOU 2755 CB GLU A 364 14253 27946 17664 1056 -2983 6891 C
ATOM 2756 CG GLU A 364 -26.620 30.496 18.113 1.00159.49 C
ANISOU 2756 CG GLU A 364 14031 27533 19036 1311 -2503 6553 C
ATOM 2757 CD GLU A 364 -26.420 32.006 18.054 1.00159.48 C
ANISOU 2757 CD GLU A 364 13840 27107 19648 1865 -2135 6914 C
ATOM 2758 OE1 GLU A 364 -27.065 32.694 17.231 1.00174.64 O
ANISOU 2758 OE1 GLU A 364 15787 29258 21309 2061 -2392 7370 O
ATOM 2759 OE2 GLU A 364 -25.604 32.508 18.853 1.00146.10 O
ANISOU 2759 OE2 GLU A 364 12020 24803 18687 2073 -1565 6685 O
ATOM 2760 N VAL A 365 -29.105 28.009 15.200 1.00225.65 N
ANISOU 2760 N VAL A 365 23486 37907 24345 -116 -4151 6494 N
ATOM 2761 CA VAL A 365 -29.299 27.169 14.021 1.00243.51 C
ANISOU 2761 CA VAL A 365 26359 40677 25489 -599 -4421 6452 C
ATOM 2762 C VAL A 365 -30.600 27.519 13.307 1.00244.39 C
ANISOU 2762 C VAL A 365 26321 41252 25285 -614 -4897 6541 C
ATOM 2763 O VAL A 365 -30.637 27.609 12.076 1.00246.84 O
ANISOU 2763 O VAL A 365 27069 41876 24842 -648 -5054 6835 O
ATOM 2764 CB VAL A 365 -29.241 25.683 14.413 1.00257.76 C
ANISOU 2764 CB VAL A 365 28430 42588 26921 -1292 -4437 5824 C
ATOM 2765 CG1 VAL A 365 -29.600 24.810 13.226 1.00263.23 C
ANISOU 2765 CG1 VAL A 365 29734 43765 26518 -1874 -4653 5630 C
ATOM 2766 CG2 VAL A 365 -27.852 25.327 14.916 1.00258.41 C
ANISOU 2766 CG2 VAL A 365 28860 41980 27346 -1219 -3834 5644 C
ATOM 2767 N ILE A 366 -31.685 27.725 14.056 1.00239.34 N
ANISOU 2767 N ILE A 366 25102 40648 25189 -587 -5113 6270 N
ATOM 2768 CA ILE A 366 -32.954 28.077 13.428 1.00252.95 C
ANISOU 2768 CA ILE A 366 26632 42827 26649 -543 -5588 6346 C
ATOM 2769 C ILE A 366 -32.892 29.479 12.836 1.00259.10 C
ANISOU 2769 C ILE A 366 27327 43496 27622 132 -5626 7032 C
ATOM 2770 O ILE A 366 -33.399 29.723 11.735 1.00249.88 O
ANISOU 2770 O ILE A 366 26348 42748 25847 199 -5987 7337 O
ATOM 2771 CB ILE A 366 -34.110 27.928 14.435 1.00246.04 C
ANISOU 2771 CB ILE A 366 25217 41959 26308 -683 -5748 5838 C
ATOM 2772 CG1 ILE A 366 -34.449 26.450 14.627 1.00236.31 C
ANISOU 2772 CG1 ILE A 366 24185 40993 24610 -1430 -5811 5209 C
ATOM 2773 CG2 ILE A 366 -35.341 28.689 13.966 1.00251.14 C
ANISOU 2773 CG2 ILE A 366 25519 42945 26957 -396 -6199 6013 C
ATOM 2774 CD1 ILE A 366 -34.809 25.739 13.337 1.00240.68 C
ANISOU 2774 CD1 ILE A 366 25145 42173 24129 -1855 -6126 5170 C
ATOM 2775 N PHE A 367 -32.255 30.421 13.537 1.00269.16 N
ANISOU 2775 N PHE A 367 28349 44186 29732 633 -5231 7279 N
ATOM 2776 CA PHE A 367 -32.063 31.727 12.921 1.00280.99 C
ANISOU 2776 CA PHE A 367 29868 45505 31392 1252 -5178 7960 C
ATOM 2777 C PHE A 367 -31.046 31.676 11.789 1.00279.46 C
ANISOU 2777 C PHE A 367 30379 45338 30466 1282 -5000 8435 C
ATOM 2778 O PHE A 367 -31.085 32.537 10.905 1.00288.83 O
ANISOU 2778 O PHE A 367 31781 46534 31425 1661 -5082 9013 O
ATOM 2779 CB PHE A 367 -31.660 32.769 13.966 1.00282.64 C
ANISOU 2779 CB PHE A 367 29644 45038 32709 1730 -4720 8031 C
ATOM 2780 CG PHE A 367 -32.826 33.538 14.524 1.00295.24 C
ANISOU 2780 CG PHE A 367 30691 46572 34914 1965 -4948 7888 C
ATOM 2781 CD1 PHE A 367 -33.613 34.320 13.693 1.00305.67 C
ANISOU 2781 CD1 PHE A 367 31955 48148 36038 2314 -5354 8328 C
ATOM 2782 CD2 PHE A 367 -33.138 33.476 15.871 1.00285.10 C
ANISOU 2782 CD2 PHE A 367 29009 44952 34363 1836 -4763 7292 C
ATOM 2783 CE1 PHE A 367 -34.691 35.027 14.196 1.00308.48 C
ANISOU 2783 CE1 PHE A 367 31804 48447 36959 2557 -5586 8178 C
ATOM 2784 CE2 PHE A 367 -34.214 34.183 16.381 1.00284.17 C
ANISOU 2784 CE2 PHE A 367 28452 44750 34768 2033 -4959 7100 C
ATOM 2785 CZ PHE A 367 -34.991 34.958 15.541 1.00297.06 C
ANISOU 2785 CZ PHE A 367 29968 46661 36242 2405 -5378 7544 C
ATOM 2786 N ALA A 368 -30.182 30.656 11.768 1.00280.23 N
ANISOU 2786 N ALA A 368 30911 45431 30131 860 -4755 8176 N
ATOM 2787 CA ALA A 368 -29.143 30.551 10.749 1.00255.69 C
ANISOU 2787 CA ALA A 368 28585 42262 26303 821 -4465 8521 C
ATOM 2788 C ALA A 368 -29.716 30.423 9.346 1.00260.47 C
ANISOU 2788 C ALA A 368 29682 43389 25895 609 -4865 8707 C
ATOM 2789 O ALA A 368 -29.020 30.737 8.374 1.00263.06 O
ANISOU 2789 O ALA A 368 30663 43604 25683 697 -4621 9115 O
ATOM 2790 CB ALA A 368 -28.230 29.361 11.044 1.00220.75 C
ANISOU 2790 CB ALA A 368 24551 37750 21573 338 -4140 8084 C
ATOM 2791 N PHE A 369 -30.961 29.958 9.218 1.00284.03 N
ANISOU 2791 N PHE A 369 32389 46926 28604 312 -5431 8387 N
ATOM 2792 CA PHE A 369 -31.612 29.939 7.913 1.00314.28 C
ANISOU 2792 CA PHE A 369 36577 51298 31537 178 -5861 8577 C
ATOM 2793 C PHE A 369 -31.717 31.343 7.332 1.00354.35 C
ANISOU 2793 C PHE A 369 41662 56217 36759 856 -5950 9337 C
ATOM 2794 O PHE A 369 -31.727 31.513 6.108 1.00361.50 O
ANISOU 2794 O PHE A 369 43118 57375 36862 842 -6110 9687 O
ATOM 2795 CB PHE A 369 -32.994 29.293 8.037 1.00309.53 C
ANISOU 2795 CB PHE A 369 35536 51291 30782 -180 -6420 8086 C
ATOM 2796 CG PHE A 369 -33.727 29.154 6.733 1.00319.83 C
ANISOU 2796 CG PHE A 369 37135 53240 31147 -360 -6896 8201 C
ATOM 2797 CD1 PHE A 369 -33.440 28.110 5.868 1.00323.43 C
ANISOU 2797 CD1 PHE A 369 38223 54034 30631 -1002 -6843 7887 C
ATOM 2798 CD2 PHE A 369 -34.720 30.054 6.382 1.00330.95 C
ANISOU 2798 CD2 PHE A 369 38181 54914 32649 104 -7391 8586 C
ATOM 2799 CE1 PHE A 369 -34.119 27.975 4.672 1.00331.13 C
ANISOU 2799 CE1 PHE A 369 39444 55635 30736 -1189 -7270 7960 C
ATOM 2800 CE2 PHE A 369 -35.403 29.924 5.187 1.00339.93 C
ANISOU 2800 CE2 PHE A 369 39566 56690 32902 -40 -7869 8702 C
ATOM 2801 CZ PHE A 369 -35.102 28.883 4.331 1.00336.45 C
ANISOU 2801 CZ PHE A 369 39735 56616 31484 -696 -7807 8387 C
ATOM 2802 N VAL A 370 -31.803 32.357 8.194 1.00377.61 N
ANISOU 2802 N VAL A 370 44035 58722 40719 1431 -5825 9577 N
ATOM 2803 CA VAL A 370 -31.745 33.748 7.760 1.00395.21 C
ANISOU 2803 CA VAL A 370 46306 60640 43216 2100 -5779 10306 C
ATOM 2804 C VAL A 370 -30.363 34.371 7.958 1.00407.62 C
ANISOU 2804 C VAL A 370 48186 61480 45210 2419 -5032 10665 C
ATOM 2805 O VAL A 370 -30.047 35.369 7.292 1.00415.94 O
ANISOU 2805 O VAL A 370 49583 62239 46217 2850 -4866 11299 O
ATOM 2806 CB VAL A 370 -32.815 34.585 8.493 1.00389.19 C
ANISOU 2806 CB VAL A 370 44733 59825 43316 2543 -6084 10327 C
ATOM 2807 CG1 VAL A 370 -33.088 35.886 7.753 1.00396.95 C
ANISOU 2807 CG1 VAL A 370 45825 60673 44323 3168 -6248 11075 C
ATOM 2808 CG2 VAL A 370 -34.091 33.778 8.662 1.00391.08 C
ANISOU 2808 CG2 VAL A 370 44568 60700 43324 2147 -6674 9763 C
ATOM 2809 N MET A 371 -29.529 33.808 8.835 1.00415.61 N
ANISOU 2809 N MET A 371 49111 62181 46621 2219 -4560 10278 N
ATOM 2810 CA MET A 371 -28.279 34.445 9.237 1.00413.11 C
ANISOU 2810 CA MET A 371 48916 61146 46901 2578 -3810 10545 C
ATOM 2811 C MET A 371 -27.167 34.344 8.200 1.00411.56 C
ANISOU 2811 C MET A 371 49675 60757 45944 2455 -3344 10841 C
ATOM 2812 O MET A 371 -26.169 35.059 8.328 1.00411.25 O
ANISOU 2812 O MET A 371 49821 60079 46355 2807 -2662 11147 O
ATOM 2813 CB MET A 371 -27.779 33.856 10.557 1.00415.81 C
ANISOU 2813 CB MET A 371 48813 61244 47931 2432 -3487 10011 C
ATOM 2814 CG MET A 371 -28.664 34.148 11.755 1.00428.95 C
ANISOU 2814 CG MET A 371 49580 62872 50528 2562 -3705 9665 C
ATOM 2815 SD MET A 371 -29.079 35.892 11.912 1.00438.99 S
ANISOU 2815 SD MET A 371 50424 63700 52673 3280 -3583 10161 S
ATOM 2816 CE MET A 371 -27.446 36.585 12.119 1.00440.99 C
ANISOU 2816 CE MET A 371 50920 63153 53484 3667 -2629 10487 C
ATOM 2817 N ASP A 372 -27.278 33.463 7.205 1.00366.34 N
ANISOU 2817 N ASP A 372 44573 55516 39105 1919 -3599 10679 N
ATOM 2818 CA ASP A 372 -26.282 33.448 6.141 1.00291.20 C
ANISOU 2818 CA ASP A 372 36021 45788 28834 1748 -3105 10905 C
ATOM 2819 C ASP A 372 -26.752 34.148 4.874 1.00254.27 C
ANISOU 2819 C ASP A 372 31814 41299 23498 1896 -3416 11455 C
ATOM 2820 O ASP A 372 -25.913 34.616 4.097 1.00253.96 O
ANISOU 2820 O ASP A 372 32512 40882 23099 1946 -2909 11807 O
ATOM 2821 CB ASP A 372 -25.864 32.013 5.802 1.00254.96 C
ANISOU 2821 CB ASP A 372 31956 41503 23415 991 -3000 10301 C
ATOM 2822 CG ASP A 372 -24.465 31.943 5.206 1.00242.68 C
ANISOU 2822 CG ASP A 372 31261 39482 21464 813 -2154 10327 C
ATOM 2823 OD1 ASP A 372 -23.825 33.007 5.062 1.00240.73 O
ANISOU 2823 OD1 ASP A 372 31207 38673 21587 1270 -1642 10818 O
ATOM 2824 OD2 ASP A 372 -23.999 30.831 4.887 1.00242.01 O
ANISOU 2824 OD2 ASP A 372 31662 39551 20739 192 -1935 9801 O
ATOM 2825 N GLU A 373 -28.065 34.227 4.646 1.00268.28 N
ANISOU 2825 N GLU A 373 33199 43635 25099 1958 -4210 11519 N
ATOM 2826 CA GLU A 373 -28.563 35.010 3.522 1.00268.71 C
ANISOU 2826 CA GLU A 373 33635 43854 24610 2214 -4555 12119 C
ATOM 2827 C GLU A 373 -28.300 36.497 3.726 1.00277.48 C
ANISOU 2827 C GLU A 373 34633 44294 26502 2946 -4237 12786 C
ATOM 2828 O GLU A 373 -28.168 37.241 2.747 1.00293.73 O
ANISOU 2828 O GLU A 373 37298 46198 28107 3156 -4198 13370 O
ATOM 2829 CB GLU A 373 -30.055 34.749 3.319 1.00257.78 C
ANISOU 2829 CB GLU A 373 31775 43231 22941 2155 -5462 11994 C
ATOM 2830 CG GLU A 373 -30.444 33.283 3.440 1.00248.61 C
ANISOU 2830 CG GLU A 373 30498 42673 21291 1443 -5732 11217 C
ATOM 2831 CD GLU A 373 -29.529 32.366 2.651 1.00248.90 C
ANISOU 2831 CD GLU A 373 31415 42762 20394 813 -5330 10935 C
ATOM 2832 OE1 GLU A 373 -29.336 32.607 1.441 1.00265.43 O
ANISOU 2832 OE1 GLU A 373 34231 44961 21658 747 -5324 11282 O
ATOM 2833 OE2 GLU A 373 -28.992 31.411 3.248 1.00239.34 O
ANISOU 2833 OE2 GLU A 373 30195 41461 19282 375 -4996 10349 O
ATOM 2834 N HIS A 374 -28.216 36.940 4.974 1.00269.99 N
ANISOU 2834 N HIS A 374 32946 42924 26714 3310 -3977 12687 N
ATOM 2835 CA HIS A 374 -27.899 38.324 5.314 1.00286.86 C
ANISOU 2835 CA HIS A 374 34908 44350 29736 3970 -3545 13207 C
ATOM 2836 C HIS A 374 -27.540 38.367 6.796 1.00302.58 C
ANISOU 2836 C HIS A 374 36136 45931 32900 4125 -3110 12817 C
ATOM 2837 O HIS A 374 -27.303 37.327 7.420 1.00292.52 O
ANISOU 2837 O HIS A 374 34665 44849 31632 3719 -3062 12234 O
ATOM 2838 CB HIS A 374 -29.060 39.263 4.971 1.00291.73 C
ANISOU 2838 CB HIS A 374 35236 45139 30469 4445 -4161 13688 C
ATOM 2839 CG HIS A 374 -28.620 40.623 4.531 1.00290.06 C
ANISOU 2839 CG HIS A 374 35407 44262 30541 4986 -3744 14411 C
ATOM 2840 ND1 HIS A 374 -28.756 41.743 5.323 1.00289.70 N
ANISOU 2840 ND1 HIS A 374 34774 43664 31634 5563 -3484 14621 N
ATOM 2841 CD2 HIS A 374 -28.036 41.043 3.384 1.00298.00 C
ANISOU 2841 CD2 HIS A 374 37363 45029 30834 4989 -3493 14936 C
ATOM 2842 CE1 HIS A 374 -28.279 42.794 4.681 1.00294.50 C
ANISOU 2842 CE1 HIS A 374 35945 43712 32239 5922 -3092 15265 C
ATOM 2843 NE2 HIS A 374 -27.836 42.396 3.502 1.00303.05 N
ANISOU 2843 NE2 HIS A 374 37980 44966 32198 5579 -3097 15477 N
ATOM 2844 N ALA A 375 -27.506 39.577 7.362 1.00321.79 N
ANISOU 2844 N ALA A 375 38154 47789 36323 4697 -2781 13120 N
ATOM 2845 CA ALA A 375 -27.176 39.797 8.772 1.00309.44 C
ANISOU 2845 CA ALA A 375 35845 45788 35939 4870 -2316 12751 C
ATOM 2846 C ALA A 375 -25.784 39.264 9.116 1.00303.23 C
ANISOU 2846 C ALA A 375 35359 44610 35243 4662 -1543 12485 C
ATOM 2847 O ALA A 375 -25.589 38.548 10.100 1.00297.94 O
ANISOU 2847 O ALA A 375 34232 43996 34975 4453 -1461 11937 O
ATOM 2848 CB ALA A 375 -28.241 39.190 9.690 1.00300.72 C
ANISOU 2848 CB ALA A 375 33925 45171 35164 4661 -2905 12168 C
ATOM 2849 N ARG A 376 -24.809 39.619 8.283 1.00309.54 N
ANISOU 2849 N ARG A 376 36973 44986 35651 4707 -950 12853 N
ATOM 2850 CA ARG A 376 -23.411 39.293 8.518 1.00295.37 C
ANISOU 2850 CA ARG A 376 35543 42697 33988 4564 -64 12619 C
ATOM 2851 C ARG A 376 -22.738 40.378 9.360 1.00275.47 C
ANISOU 2851 C ARG A 376 32618 39352 32697 5050 757 12681 C
ATOM 2852 O ARG A 376 -23.284 41.460 9.584 1.00286.71 O
ANISOU 2852 O ARG A 376 33624 40547 34766 5474 698 12970 O
ATOM 2853 CB ARG A 376 -22.665 39.112 7.195 1.00313.98 C
ANISOU 2853 CB ARG A 376 39025 44965 35309 4255 291 12825 C
ATOM 2854 CG ARG A 376 -23.199 37.998 6.307 1.00326.10 C
ANISOU 2854 CG ARG A 376 41024 47289 35589 3686 -401 12668 C
ATOM 2855 CD ARG A 376 -24.226 38.518 5.315 1.00336.34 C
ANISOU 2855 CD ARG A 376 42544 48973 36277 3799 -1120 13178 C
ATOM 2856 NE ARG A 376 -24.723 37.464 4.435 1.00337.49 N
ANISOU 2856 NE ARG A 376 43132 49873 35226 3227 -1728 12970 N
ATOM 2857 CZ ARG A 376 -24.217 37.191 3.236 1.00339.74 C
ANISOU 2857 CZ ARG A 376 44389 50218 34480 2830 -1529 13055 C
ATOM 2858 NH1 ARG A 376 -23.196 37.896 2.768 1.00342.19 N
ANISOU 2858 NH1 ARG A 376 45355 49865 34798 2928 -735 13350 N
ATOM 2859 NH2 ARG A 376 -24.733 36.213 2.504 1.00344.89 N
ANISOU 2859 NH2 ARG A 376 45357 51580 34105 2293 -2076 12787 N
ATOM 2860 N GLY A 377 -21.534 40.068 9.837 1.00253.89 N
ANISOU 2860 N GLY A 377 30009 36157 30301 4957 1577 12347 N
ATOM 2861 CA GLY A 377 -20.754 41.015 10.612 1.00250.55 C
ANISOU 2861 CA GLY A 377 29240 34916 31041 5307 2473 12205 C
ATOM 2862 C GLY A 377 -20.133 40.388 11.842 1.00245.20 C
ANISOU 2862 C GLY A 377 27993 34055 31118 5078 2815 11196 C
ATOM 2863 O GLY A 377 -19.824 39.193 11.842 1.00239.33 O
ANISOU 2863 O GLY A 377 27470 33570 29895 4602 2682 10583 O
ATOM 2864 N THR A 378 -19.954 41.178 12.906 1.00235.93 N
ANISOU 2864 N THR A 378 26081 32439 31122 5413 3257 11017 N
ATOM 2865 CA THR A 378 -19.513 40.602 14.171 1.00218.88 C
ANISOU 2865 CA THR A 378 23280 30223 29660 5223 3450 10114 C
ATOM 2866 C THR A 378 -20.529 39.593 14.685 1.00203.10 C
ANISOU 2866 C THR A 378 20819 28957 27392 4986 2487 9899 C
ATOM 2867 O THR A 378 -20.172 38.659 15.414 1.00191.14 O
ANISOU 2867 O THR A 378 19098 27535 25993 4664 2480 9165 O
ATOM 2868 CB THR A 378 -19.297 41.706 15.210 1.00205.30 C
ANISOU 2868 CB THR A 378 20789 28003 29213 5605 4035 10002 C
ATOM 2869 OG1 THR A 378 -20.565 42.202 15.653 1.00209.04 O
ANISOU 2869 OG1 THR A 378 20750 28771 29905 5626 3404 10154 O
ATOM 2870 CG2 THR A 378 -18.503 42.855 14.609 1.00201.61 C
ANISOU 2870 CG2 THR A 378 20791 26810 29000 5864 4962 10349 C
ATOM 2871 N LEU A 379 -21.798 39.770 14.313 1.00220.13 N
ANISOU 2871 N LEU A 379 22811 31639 29187 5145 1674 10533 N
ATOM 2872 CA LEU A 379 -22.825 38.788 14.632 1.00219.93 C
ANISOU 2872 CA LEU A 379 22448 32353 28764 4816 766 10280 C
ATOM 2873 C LEU A 379 -22.532 37.449 13.963 1.00229.08 C
ANISOU 2873 C LEU A 379 24311 33844 28886 4286 547 9977 C
ATOM 2874 O LEU A 379 -22.745 36.384 14.558 1.00236.62 O
ANISOU 2874 O LEU A 379 25048 35119 29738 3903 207 9403 O
ATOM 2875 CB LEU A 379 -24.183 39.343 14.199 1.00228.14 C
ANISOU 2875 CB LEU A 379 23378 33749 29555 4848 106 10588 C
ATOM 2876 CG LEU A 379 -25.492 38.587 14.398 1.00235.26 C
ANISOU 2876 CG LEU A 379 23990 35336 30060 4467 -787 10250 C
ATOM 2877 CD1 LEU A 379 -25.637 38.119 15.830 1.00241.23 C
ANISOU 2877 CD1 LEU A 379 24201 36013 31443 4136 -745 9402 C
ATOM 2878 CD2 LEU A 379 -26.646 39.501 14.013 1.00240.90 C
ANISOU 2878 CD2 LEU A 379 24555 36172 30806 4697 -1210 10593 C
ATOM 2879 N ARG A 380 -22.007 37.486 12.734 1.00221.88 N
ANISOU 2879 N ARG A 380 24293 32804 27207 4201 811 10281 N
ATOM 2880 CA ARG A 380 -21.564 36.264 12.071 1.00210.60 C
ANISOU 2880 CA ARG A 380 23588 31571 24858 3639 785 9860 C
ATOM 2881 C ARG A 380 -20.389 35.631 12.805 1.00189.62 C
ANISOU 2881 C ARG A 380 20933 28420 22696 3420 1444 8988 C
ATOM 2882 O ARG A 380 -20.302 34.399 12.895 1.00186.86 O
ANISOU 2882 O ARG A 380 20769 28285 21945 2976 1241 8439 O
ATOM 2883 CB ARG A 380 -21.197 36.581 10.620 1.00210.63 C
ANISOU 2883 CB ARG A 380 24531 31508 23991 3594 1024 10371 C
ATOM 2884 CG ARG A 380 -20.855 35.390 9.738 1.00205.84 C
ANISOU 2884 CG ARG A 380 24718 31174 22317 2981 975 10002 C
ATOM 2885 CD ARG A 380 -20.487 35.872 8.338 1.00199.06 C
ANISOU 2885 CD ARG A 380 24764 30239 20630 2943 1271 10550 C
ATOM 2886 NE ARG A 380 -20.248 34.782 7.397 1.00205.84 N
ANISOU 2886 NE ARG A 380 26388 31427 20395 2315 1212 10218 N
ATOM 2887 CZ ARG A 380 -21.169 34.290 6.575 1.00216.94 C
ANISOU 2887 CZ ARG A 380 28065 33629 20734 2016 453 10530 C
ATOM 2888 NH1 ARG A 380 -20.862 33.300 5.748 1.00226.58 N
ANISOU 2888 NH1 ARG A 380 29979 35099 21011 1395 514 10136 N
ATOM 2889 NH2 ARG A 380 -22.399 34.785 6.580 1.00226.07 N
ANISOU 2889 NH2 ARG A 380 28764 35354 21779 2329 -356 11195 N
ATOM 2890 N PHE A 381 -19.507 36.458 13.374 1.00167.29 N
ANISOU 2890 N PHE A 381 17857 24938 20768 3739 2224 8839 N
ATOM 2891 CA PHE A 381 -18.355 35.936 14.102 1.00153.01 C
ANISOU 2891 CA PHE A 381 15970 22696 19471 3597 2839 8014 C
ATOM 2892 C PHE A 381 -18.782 35.256 15.394 1.00152.24 C
ANISOU 2892 C PHE A 381 15143 22848 19852 3500 2415 7531 C
ATOM 2893 O PHE A 381 -18.278 34.178 15.729 1.00161.88 O
ANISOU 2893 O PHE A 381 16499 24042 20967 3198 2453 6907 O
ATOM 2894 CB PHE A 381 -17.371 37.071 14.387 1.00165.24 C
ANISOU 2894 CB PHE A 381 17366 23562 21855 3947 3772 7962 C
ATOM 2895 CG PHE A 381 -16.110 36.628 15.069 1.00161.13 C
ANISOU 2895 CG PHE A 381 16735 22632 21854 3843 4432 7109 C
ATOM 2896 CD1 PHE A 381 -15.226 35.773 14.433 1.00157.38 C
ANISOU 2896 CD1 PHE A 381 16937 22014 20847 3519 4749 6660 C
ATOM 2897 CD2 PHE A 381 -15.798 37.083 16.340 1.00162.56 C
ANISOU 2897 CD2 PHE A 381 16109 22596 23063 4073 4742 6736 C
ATOM 2898 CE1 PHE A 381 -14.064 35.368 15.056 1.00143.18 C
ANISOU 2898 CE1 PHE A 381 14987 19857 19556 3483 5320 5873 C
ATOM 2899 CE2 PHE A 381 -14.635 36.682 16.967 1.00146.06 C
ANISOU 2899 CE2 PHE A 381 13914 20180 21401 3988 5263 5939 C
ATOM 2900 CZ PHE A 381 -13.767 35.824 16.324 1.00138.30 C
ANISOU 2900 CZ PHE A 381 13550 19071 19927 3743 5570 5538 C
ATOM 2901 N ILE A 382 -19.707 35.872 16.136 1.00160.09 N
ANISOU 2901 N ILE A 382 15374 24067 21385 3752 2026 7809 N
ATOM 2902 CA ILE A 382 -20.224 35.231 17.340 1.00174.10 C
ANISOU 2902 CA ILE A 382 16482 26137 23532 3597 1592 7382 C
ATOM 2903 C ILE A 382 -20.991 33.962 16.987 1.00167.77 C
ANISOU 2903 C ILE A 382 15989 25906 21851 3137 846 7289 C
ATOM 2904 O ILE A 382 -20.943 32.970 17.728 1.00180.39 O
ANISOU 2904 O ILE A 382 17455 27594 23493 2839 683 6748 O
ATOM 2905 CB ILE A 382 -21.096 36.224 18.132 1.00185.32 C
ANISOU 2905 CB ILE A 382 17238 27575 25602 3778 1383 7524 C
ATOM 2906 CG1 ILE A 382 -20.267 37.443 18.540 1.00187.40 C
ANISOU 2906 CG1 ILE A 382 17616 27046 26542 3904 2143 7269 C
ATOM 2907 CG2 ILE A 382 -21.703 35.556 19.357 1.00196.84 C
ANISOU 2907 CG2 ILE A 382 18613 29064 27113 3247 945 6721 C
ATOM 2908 CD1 ILE A 382 -21.041 38.471 19.334 1.00182.91 C
ANISOU 2908 CD1 ILE A 382 16920 26210 26369 3767 1969 7035 C
ATOM 2909 N LYS A 383 -21.679 33.956 15.842 1.00119.66 N
ANISOU 2909 N LYS A 383 10340 20205 14920 3051 407 7801 N
ATOM 2910 CA LYS A 383 -22.422 32.768 15.432 1.00123.46 C
ANISOU 2910 CA LYS A 383 11117 21273 14519 2559 -264 7670 C
ATOM 2911 C LYS A 383 -21.481 31.599 15.161 1.00158.21 C
ANISOU 2911 C LYS A 383 16196 25421 18496 2150 78 7080 C
ATOM 2912 O LYS A 383 -21.661 30.498 15.702 1.00176.62 O
ANISOU 2912 O LYS A 383 18488 27902 20719 1784 -177 6592 O
ATOM 2913 CB LYS A 383 -23.254 33.088 14.191 1.00139.71 C
ANISOU 2913 CB LYS A 383 13512 23839 15733 2569 -762 8341 C
ATOM 2914 CG LYS A 383 -23.977 31.901 13.590 1.00134.44 C
ANISOU 2914 CG LYS A 383 13206 23828 14045 2007 -1397 8183 C
ATOM 2915 CD LYS A 383 -24.263 32.146 12.119 1.00146.24 C
ANISOU 2915 CD LYS A 383 15319 25692 14553 1966 -1627 8756 C
ATOM 2916 CE LYS A 383 -25.270 31.154 11.581 1.00154.52 C
ANISOU 2916 CE LYS A 383 16515 27572 14622 1437 -2386 8657 C
ATOM 2917 NZ LYS A 383 -24.911 29.750 11.916 1.00156.98 N
ANISOU 2917 NZ LYS A 383 17105 27803 14737 850 -2256 7853 N
ATOM 2918 N LEU A 384 -20.450 31.831 14.341 1.00170.42 N
ANISOU 2918 N LEU A 384 18375 26541 19836 2206 701 7099 N
ATOM 2919 CA LEU A 384 -19.477 30.778 14.071 1.00152.80 C
ANISOU 2919 CA LEU A 384 16751 24010 17297 1859 1100 6494 C
ATOM 2920 C LEU A 384 -18.723 30.383 15.332 1.00144.21 C
ANISOU 2920 C LEU A 384 15257 22497 17040 1947 1441 5867 C
ATOM 2921 O LEU A 384 -18.319 29.224 15.478 1.00144.59 O
ANISOU 2921 O LEU A 384 15599 22434 16906 1640 1478 5330 O
ATOM 2922 CB LEU A 384 -18.495 31.232 12.993 1.00140.52 C
ANISOU 2922 CB LEU A 384 15881 22067 15442 1911 1770 6605 C
ATOM 2923 CG LEU A 384 -19.112 31.743 11.693 1.00158.77 C
ANISOU 2923 CG LEU A 384 18669 24765 16892 1862 1499 7301 C
ATOM 2924 CD1 LEU A 384 -18.030 32.206 10.732 1.00169.15 C
ANISOU 2924 CD1 LEU A 384 20684 25622 17964 1875 2272 7356 C
ATOM 2925 CD2 LEU A 384 -19.980 30.674 11.062 1.00157.29 C
ANISOU 2925 CD2 LEU A 384 18823 25242 15699 1340 814 7263 C
ATOM 2926 N PHE A 385 -18.529 31.331 16.249 1.00145.52 N
ANISOU 2926 N PHE A 385 14748 22427 18118 2365 1695 5928 N
ATOM 2927 CA PHE A 385 -17.836 31.034 17.497 1.00141.47 C
ANISOU 2927 CA PHE A 385 13784 21596 18373 2462 1981 5359 C
ATOM 2928 C PHE A 385 -18.636 30.057 18.349 1.00143.56 C
ANISOU 2928 C PHE A 385 13750 22220 18576 2178 1348 5127 C
ATOM 2929 O PHE A 385 -18.119 29.011 18.768 1.00144.93 O
ANISOU 2929 O PHE A 385 14113 22214 18741 1986 1412 4619 O
ATOM 2930 CB PHE A 385 -17.577 32.341 18.250 1.00167.07 C
ANISOU 2930 CB PHE A 385 16331 24599 22549 2915 2378 5485 C
ATOM 2931 CG PHE A 385 -17.008 32.157 19.626 1.00174.73 C
ANISOU 2931 CG PHE A 385 16710 25380 24301 3015 2590 4943 C
ATOM 2932 CD1 PHE A 385 -15.669 31.851 19.802 1.00180.32 C
ANISOU 2932 CD1 PHE A 385 17697 25588 25229 3027 3134 4344 C
ATOM 2933 CD2 PHE A 385 -17.807 32.317 20.746 1.00177.95 C
ANISOU 2933 CD2 PHE A 385 16954 25768 24890 2776 2020 4663 C
ATOM 2934 CE1 PHE A 385 -15.141 31.691 21.069 1.00181.09 C
ANISOU 2934 CE1 PHE A 385 17948 25245 25614 2779 2903 3511 C
ATOM 2935 CE2 PHE A 385 -17.285 32.158 22.015 1.00179.57 C
ANISOU 2935 CE2 PHE A 385 17372 25502 25354 2520 1950 3809 C
ATOM 2936 CZ PHE A 385 -15.951 31.845 22.177 1.00174.92 C
ANISOU 2936 CZ PHE A 385 17041 24517 24902 2536 2331 3278 C
ATOM 2937 N THR A 386 -19.916 30.362 18.583 1.00156.70 N
ANISOU 2937 N THR A 386 14971 24384 20185 2140 740 5493 N
ATOM 2938 CA THR A 386 -20.727 29.499 19.435 1.00169.89 C
ANISOU 2938 CA THR A 386 16332 26404 21814 1822 181 5253 C
ATOM 2939 C THR A 386 -20.994 28.152 18.774 1.00160.89 C
ANISOU 2939 C THR A 386 15875 25463 19793 1308 -137 5045 C
ATOM 2940 O THR A 386 -20.909 27.109 19.433 1.00168.54 O
ANISOU 2940 O THR A 386 16916 26354 20767 1035 -232 4612 O
ATOM 2941 CB THR A 386 -22.044 30.188 19.789 1.00157.45 C
ANISOU 2941 CB THR A 386 14079 25339 20408 1887 -359 5640 C
ATOM 2942 OG1 THR A 386 -22.751 30.518 18.588 1.00166.34 O
ANISOU 2942 OG1 THR A 386 15494 26833 20874 1873 -694 6154 O
ATOM 2943 CG2 THR A 386 -21.782 31.456 20.586 1.00147.86 C
ANISOU 2943 CG2 THR A 386 12508 23636 20035 2211 49 5542 C
ATOM 2944 N GLU A 387 -21.306 28.145 17.474 1.00129.09 N
ANISOU 2944 N GLU A 387 12377 21683 14989 1153 -282 5344 N
ATOM 2945 CA GLU A 387 -21.602 26.872 16.823 1.00122.12 C
ANISOU 2945 CA GLU A 387 12121 21029 13251 602 -552 5093 C
ATOM 2946 C GLU A 387 -20.355 26.002 16.705 1.00138.95 C
ANISOU 2946 C GLU A 387 14845 22576 15373 491 2 4568 C
ATOM 2947 O GLU A 387 -20.404 24.797 16.988 1.00170.17 O
ANISOU 2947 O GLU A 387 19058 26477 19119 119 -118 4148 O
ATOM 2948 CB GLU A 387 -22.225 27.110 15.448 1.00132.77 C
ANISOU 2948 CB GLU A 387 13865 22858 13723 441 -845 5526 C
ATOM 2949 CG GLU A 387 -23.582 27.790 15.496 1.00140.47 C
ANISOU 2949 CG GLU A 387 14257 24496 14620 530 -1511 6019 C
ATOM 2950 CD GLU A 387 -24.439 27.458 14.291 1.00171.64 C
ANISOU 2950 CD GLU A 387 18597 29118 17500 161 -2023 6262 C
ATOM 2951 OE1 GLU A 387 -24.256 26.366 13.713 1.00185.60 O
ANISOU 2951 OE1 GLU A 387 20997 30937 18587 -349 -1980 5885 O
ATOM 2952 OE2 GLU A 387 -25.296 28.288 13.923 1.00183.86 O
ANISOU 2952 OE2 GLU A 387 19805 31156 18896 385 -2466 6818 O
ATOM 2953 N LEU A 388 -19.223 26.598 16.322 1.00126.91 N
ANISOU 2953 N LEU A 388 13524 20579 14117 817 640 4563 N
ATOM 2954 CA LEU A 388 -17.991 25.829 16.172 1.00129.52 C
ANISOU 2954 CA LEU A 388 14360 20355 14497 757 1195 4027 C
ATOM 2955 C LEU A 388 -17.522 25.281 17.511 1.00162.80 C
ANISOU 2955 C LEU A 388 18210 24236 19411 891 1273 3591 C
ATOM 2956 O LEU A 388 -17.206 24.090 17.631 1.00195.53 O
ANISOU 2956 O LEU A 388 22732 28153 23407 646 1301 3158 O
ATOM 2957 CB LEU A 388 -16.901 26.697 15.545 1.00114.39 C
ANISOU 2957 CB LEU A 388 12645 18037 12781 1075 1891 4081 C
ATOM 2958 CG LEU A 388 -16.739 26.663 14.026 1.00115.75 C
ANISOU 2958 CG LEU A 388 13583 18279 12117 807 2091 4211 C
ATOM 2959 CD1 LEU A 388 -15.755 27.726 13.561 1.00116.73 C
ANISOU 2959 CD1 LEU A 388 13811 18008 12531 1140 2797 4325 C
ATOM 2960 CD2 LEU A 388 -16.291 25.283 13.567 1.00139.94 C
ANISOU 2960 CD2 LEU A 388 17290 21162 14718 369 2236 3641 C
ATOM 2961 N SER A 389 -17.479 26.136 18.537 1.00139.10 N
ANISOU 2961 N SER A 389 14478 21201 17174 1278 1312 3706 N
ATOM 2962 CA SER A 389 -17.056 25.663 19.850 1.00133.50 C
ANISOU 2962 CA SER A 389 13394 20252 17077 1402 1347 3329 C
ATOM 2963 C SER A 389 -18.015 24.609 20.375 1.00126.92 C
ANISOU 2963 C SER A 389 12599 19700 15923 985 757 3244 C
ATOM 2964 O SER A 389 -17.593 23.613 20.984 1.00137.56 O
ANISOU 2964 O SER A 389 14120 20760 17386 902 786 2869 O
ATOM 2965 CB SER A 389 -16.967 26.835 20.823 1.00146.50 C
ANISOU 2965 CB SER A 389 14213 21919 19532 1812 1479 3465 C
ATOM 2966 OG SER A 389 -16.246 27.907 20.247 1.00136.61 O
ANISOU 2966 OG SER A 389 12943 20433 18528 2140 2034 3592 O
ATOM 2967 N PHE A 390 -19.303 24.773 20.081 1.00133.44 N
ANISOU 2967 N PHE A 390 13309 21080 16312 708 231 3581 N
ATOM 2968 CA PHE A 390 -20.282 23.813 20.552 1.00151.46 C
ANISOU 2968 CA PHE A 390 15610 23667 18270 246 -295 3462 C
ATOM 2969 C PHE A 390 -20.019 22.470 19.898 1.00134.39 C
ANISOU 2969 C PHE A 390 14268 21285 15508 -159 -224 3119 C
ATOM 2970 O PHE A 390 -19.470 21.578 20.548 1.00141.80 O
ANISOU 2970 O PHE A 390 15402 21812 16665 -192 -82 2760 O
ATOM 2971 CB PHE A 390 -21.700 24.309 20.291 1.00164.34 C
ANISOU 2971 CB PHE A 390 16895 25988 19559 40 -858 3841 C
ATOM 2972 CG PHE A 390 -22.223 25.194 21.377 1.00161.16 C
ANISOU 2972 CG PHE A 390 15614 25803 19816 278 -1042 4014 C
ATOM 2973 CD1 PHE A 390 -21.387 25.618 22.400 1.00166.80 C
ANISOU 2973 CD1 PHE A 390 15917 26135 21324 650 -670 3862 C
ATOM 2974 CD2 PHE A 390 -23.548 25.583 21.393 1.00173.42 C
ANISOU 2974 CD2 PHE A 390 16715 27972 21205 110 -1578 4276 C
ATOM 2975 CE1 PHE A 390 -21.860 26.424 23.406 1.00172.60 C
ANISOU 2975 CE1 PHE A 390 15926 27013 22642 799 -777 3920 C
ATOM 2976 CE2 PHE A 390 -24.025 26.388 22.397 1.00168.04 C
ANISOU 2976 CE2 PHE A 390 15271 27410 21167 299 -1677 4342 C
ATOM 2977 CZ PHE A 390 -23.182 26.805 23.408 1.00166.76 C
ANISOU 2977 CZ PHE A 390 15148 26520 21691 574 -1172 3977 C
ATOM 2978 N THR A 391 -20.305 22.339 18.599 1.00121.34 N
ANISOU 2978 N THR A 391 13116 19863 13125 -437 -269 3219 N
ATOM 2979 CA THR A 391 -20.215 21.021 17.975 1.00132.04 C
ANISOU 2979 CA THR A 391 15223 21069 13876 -923 -211 2845 C
ATOM 2980 C THR A 391 -18.812 20.436 18.086 1.00143.70 C
ANISOU 2980 C THR A 391 17094 21788 15718 -704 376 2427 C
ATOM 2981 O THR A 391 -18.652 19.211 18.061 1.00142.74 O
ANISOU 2981 O THR A 391 17480 21371 15385 -1023 448 2043 O
ATOM 2982 CB THR A 391 -20.646 21.082 16.509 1.00131.55 C
ANISOU 2982 CB THR A 391 15612 21421 12949 -1255 -301 3002 C
ATOM 2983 OG1 THR A 391 -20.619 19.761 15.952 1.00128.02 O
ANISOU 2983 OG1 THR A 391 15863 20851 11926 -1801 -219 2566 O
ATOM 2984 CG2 THR A 391 -19.716 21.978 15.706 1.00142.93 C
ANISOU 2984 CG2 THR A 391 17213 22631 14462 -875 183 3183 C
ATOM 2985 N SER A 392 -17.788 21.285 18.222 1.00155.58 N
ANISOU 2985 N SER A 392 18353 22960 17802 -161 817 2466 N
ATOM 2986 CA SER A 392 -16.437 20.769 18.408 1.00160.82 C
ANISOU 2986 CA SER A 392 19272 22944 18886 99 1353 2027 C
ATOM 2987 C SER A 392 -16.289 20.086 19.762 1.00148.84 C
ANISOU 2987 C SER A 392 17517 21155 17879 223 1214 1814 C
ATOM 2988 O SER A 392 -15.760 18.972 19.849 1.00144.94 O
ANISOU 2988 O SER A 392 17474 20206 17393 143 1374 1440 O
ATOM 2989 CB SER A 392 -15.418 21.899 18.263 1.00179.14 C
ANISOU 2989 CB SER A 392 21317 25039 21707 616 1869 2076 C
ATOM 2990 OG SER A 392 -15.544 22.826 19.324 1.00190.18 O
ANISOU 2990 OG SER A 392 21939 26576 23747 990 1754 2301 O
ATOM 2991 N PHE A 393 -16.757 20.732 20.832 1.00156.92 N
ANISOU 2991 N PHE A 393 17848 22445 19330 413 924 2054 N
ATOM 2992 CA PHE A 393 -16.634 20.138 22.159 1.00158.55 C
ANISOU 2992 CA PHE A 393 17830 22448 19965 509 775 1894 C
ATOM 2993 C PHE A 393 -17.759 19.167 22.505 1.00134.99 C
ANISOU 2993 C PHE A 393 15071 19676 16541 -41 291 1901 C
ATOM 2994 O PHE A 393 -17.688 18.517 23.555 1.00121.91 O
ANISOU 2994 O PHE A 393 13375 17806 15139 -33 171 1781 O
ATOM 2995 CB PHE A 393 -16.548 21.235 23.224 1.00178.63 C
ANISOU 2995 CB PHE A 393 19521 25176 23176 910 748 2069 C
ATOM 2996 CG PHE A 393 -15.188 21.858 23.334 1.00173.23 C
ANISOU 2996 CG PHE A 393 18595 24135 23089 1468 1288 1883 C
ATOM 2997 CD1 PHE A 393 -14.812 22.887 22.488 1.00158.83 C
ANISOU 2997 CD1 PHE A 393 16694 22338 21315 1664 1659 1993 C
ATOM 2998 CD2 PHE A 393 -14.279 21.405 24.276 1.00171.61 C
ANISOU 2998 CD2 PHE A 393 18249 23579 23377 1787 1430 1589 C
ATOM 2999 CE1 PHE A 393 -13.558 23.457 22.583 1.00137.12 C
ANISOU 2999 CE1 PHE A 393 13716 19268 19116 2122 2210 1754 C
ATOM 3000 CE2 PHE A 393 -13.024 21.971 24.376 1.00149.65 C
ANISOU 3000 CE2 PHE A 393 15184 20532 21143 2283 1926 1349 C
ATOM 3001 CZ PHE A 393 -12.663 22.999 23.529 1.00133.86 C
ANISOU 3001 CZ PHE A 393 13095 18559 19207 2427 2342 1399 C
ATOM 3002 N GLN A 394 -18.797 19.059 21.665 1.00139.05 N
ANISOU 3002 N GLN A 394 15818 20628 16385 -531 12 2031 N
ATOM 3003 CA GLN A 394 -19.905 18.159 21.973 1.00146.01 C
ANISOU 3003 CA GLN A 394 16882 21754 16839 -1116 -410 1972 C
ATOM 3004 C GLN A 394 -19.479 16.703 21.940 1.00144.57 C
ANISOU 3004 C GLN A 394 17444 21009 16479 -1367 -222 1593 C
ATOM 3005 O GLN A 394 -20.119 15.866 22.583 1.00140.55 O
ANISOU 3005 O GLN A 394 17086 20488 15828 -1754 -465 1498 O
ATOM 3006 CB GLN A 394 -21.079 18.350 21.007 1.00163.86 C
ANISOU 3006 CB GLN A 394 19197 24671 18390 -1591 -748 2137 C
ATOM 3007 CG GLN A 394 -21.795 19.704 21.034 1.00167.85 C
ANISOU 3007 CG GLN A 394 18970 25790 19017 -1399 -1044 2558 C
ATOM 3008 CD GLN A 394 -22.267 20.141 22.418 1.00166.79 C
ANISOU 3008 CD GLN A 394 18105 25830 19436 -1280 -1298 2659 C
ATOM 3009 OE1 GLN A 394 -23.446 20.023 22.762 1.00164.53 O
ANISOU 3009 OE1 GLN A 394 17545 26036 18934 -1678 -1735 2694 O
ATOM 3010 NE2 GLN A 394 -21.347 20.675 23.206 1.00116.24 N
ANISOU 3010 NE2 GLN A 394 11354 19069 13744 -758 -1004 2665 N
ATOM 3011 N GLY A 395 -18.448 16.366 21.163 1.00159.52 N
ANISOU 3011 N GLY A 395 19829 22419 18364 -1191 233 1356 N
ATOM 3012 CA GLY A 395 -17.971 14.996 21.174 1.00159.56 C
ANISOU 3012 CA GLY A 395 20513 21798 18314 -1358 457 981 C
ATOM 3013 C GLY A 395 -17.293 14.638 22.480 1.00133.82 C
ANISOU 3013 C GLY A 395 17098 18041 15706 -930 495 934 C
ATOM 3014 O GLY A 395 -17.433 13.517 22.977 1.00113.06 O
ANISOU 3014 O GLY A 395 14893 15042 13023 -1160 438 787 O
ATOM 3015 N LEU A 396 -16.561 15.589 23.063 1.00128.15 N
ANISOU 3015 N LEU A 396 15778 17321 15592 -317 596 1063 N
ATOM 3016 CA LEU A 396 -16.006 15.377 24.394 1.00122.88 C
ANISOU 3016 CA LEU A 396 14846 16345 15499 87 547 1061 C
ATOM 3017 C LEU A 396 -17.104 15.356 25.450 1.00125.27 C
ANISOU 3017 C LEU A 396 14839 17042 15718 -237 68 1295 C
ATOM 3018 O LEU A 396 -17.039 14.574 26.407 1.00 92.31 O
ANISOU 3018 O LEU A 396 10830 12566 11679 -239 -53 1271 O
ATOM 3019 CB LEU A 396 -14.973 16.461 24.703 1.00142.13 C
ANISOU 3019 CB LEU A 396 16659 18777 18568 762 803 1074 C
ATOM 3020 CG LEU A 396 -14.330 16.514 26.089 1.00114.26 C
ANISOU 3020 CG LEU A 396 12676 15094 15644 1239 740 1077 C
ATOM 3021 CD1 LEU A 396 -13.746 15.169 26.483 1.00 90.71 C
ANISOU 3021 CD1 LEU A 396 10252 11471 12744 1358 779 880 C
ATOM 3022 CD2 LEU A 396 -13.255 17.586 26.102 1.00101.32 C
ANISOU 3022 CD2 LEU A 396 10464 13469 14564 1833 1099 976 C
ATOM 3023 N MET A 397 -18.126 16.203 25.288 1.00116.85 N
ANISOU 3023 N MET A 397 13329 16642 14425 -514 -204 1522 N
ATOM 3024 CA MET A 397 -19.253 16.194 26.217 1.00112.43 C
ANISOU 3024 CA MET A 397 12447 16503 13769 -897 -635 1676 C
ATOM 3025 C MET A 397 -20.028 14.884 26.149 1.00115.56 C
ANISOU 3025 C MET A 397 13511 16771 13625 -1554 -795 1528 C
ATOM 3026 O MET A 397 -20.541 14.412 27.170 1.00112.78 O
ANISOU 3026 O MET A 397 13138 16432 13282 -1814 -1020 1555 O
ATOM 3027 CB MET A 397 -20.178 17.375 25.920 1.00126.61 C
ANISOU 3027 CB MET A 397 13616 19023 15465 -1023 -872 1914 C
ATOM 3028 CG MET A 397 -21.279 17.583 26.945 1.00144.55 C
ANISOU 3028 CG MET A 397 15377 21777 17769 -1355 -1276 2029 C
ATOM 3029 SD MET A 397 -22.438 18.882 26.473 1.00173.46 S
ANISOU 3029 SD MET A 397 18319 26261 21326 -1485 -1574 2285 S
ATOM 3030 CE MET A 397 -23.373 18.053 25.191 1.00166.79 C
ANISOU 3030 CE MET A 397 18114 25673 19586 -2144 -1775 2180 C
ATOM 3031 N VAL A 398 -20.122 14.290 24.961 1.00120.51 N
ANISOU 3031 N VAL A 398 14746 17279 13764 -1873 -647 1346 N
ATOM 3032 CA VAL A 398 -20.803 13.010 24.806 1.00138.42 C
ANISOU 3032 CA VAL A 398 17690 19383 15521 -2540 -707 1130 C
ATOM 3033 C VAL A 398 -19.931 11.875 25.324 1.00167.33 C
ANISOU 3033 C VAL A 398 21954 22183 19442 -2349 -443 962 C
ATOM 3034 O VAL A 398 -20.432 10.902 25.899 1.00169.23 O
ANISOU 3034 O VAL A 398 22606 22189 19504 -2770 -533 891 O
ATOM 3035 CB VAL A 398 -21.204 12.812 23.332 1.00131.15 C
ANISOU 3035 CB VAL A 398 17167 18697 13967 -2979 -620 955 C
ATOM 3036 CG1 VAL A 398 -21.574 11.371 23.054 1.00131.58 C
ANISOU 3036 CG1 VAL A 398 18029 18398 13567 -3616 -503 615 C
ATOM 3037 CG2 VAL A 398 -22.369 13.724 22.979 1.00136.01 C
ANISOU 3037 CG2 VAL A 398 17223 20225 14231 -3273 -1016 1156 C
ATOM 3038 N ALA A 399 -18.612 11.990 25.150 1.00166.73 N
ANISOU 3038 N ALA A 399 21930 21611 19808 -1700 -107 895 N
ATOM 3039 CA ALA A 399 -17.707 10.974 25.674 1.00151.02 C
ANISOU 3039 CA ALA A 399 20436 18796 18148 -1390 113 762 C
ATOM 3040 C ALA A 399 -17.747 10.941 27.196 1.00144.77 C
ANISOU 3040 C ALA A 399 19349 17968 17687 -1190 -162 1003 C
ATOM 3041 O ALA A 399 -17.877 9.870 27.801 1.00135.99 O
ANISOU 3041 O ALA A 399 18767 16394 16508 -1386 -197 996 O
ATOM 3042 CB ALA A 399 -16.284 11.232 25.179 1.00130.54 C
ANISOU 3042 CB ALA A 399 17819 15777 16004 -703 514 600 C
ATOM 3043 N ILE A 400 -17.629 12.108 27.836 1.00154.35 N
ANISOU 3043 N ILE A 400 19740 19656 19250 -820 -331 1217 N
ATOM 3044 CA ILE A 400 -17.717 12.146 29.292 1.00111.33 C
ANISOU 3044 CA ILE A 400 13963 14282 14056 -699 -596 1426 C
ATOM 3045 C ILE A 400 -19.127 11.813 29.766 1.00110.22 C
ANISOU 3045 C ILE A 400 13908 14507 13464 -1468 -916 1513 C
ATOM 3046 O ILE A 400 -19.299 11.200 30.825 1.00128.72 O
ANISOU 3046 O ILE A 400 16443 16656 15809 -1601 -1066 1620 O
ATOM 3047 CB ILE A 400 -17.249 13.513 29.828 1.00108.79 C
ANISOU 3047 CB ILE A 400 12701 14409 14227 -173 -638 1558 C
ATOM 3048 CG1 ILE A 400 -18.185 14.635 29.372 1.00119.57 C
ANISOU 3048 CG1 ILE A 400 13490 16516 15424 -476 -774 1650 C
ATOM 3049 CG2 ILE A 400 -15.820 13.794 29.388 1.00124.71 C
ANISOU 3049 CG2 ILE A 400 14634 16055 16695 550 -276 1401 C
ATOM 3050 CD1 ILE A 400 -17.794 16.008 29.881 1.00125.29 C
ANISOU 3050 CD1 ILE A 400 13300 17641 16662 -11 -751 1758 C
ATOM 3051 N LEU A 401 -20.153 12.182 28.996 1.00129.86 N
ANISOU 3051 N LEU A 401 16268 17536 15537 -1996 -1025 1460 N
ATOM 3052 CA LEU A 401 -21.521 12.053 29.489 1.00141.43 C
ANISOU 3052 CA LEU A 401 17626 19479 16633 -2711 -1338 1491 C
ATOM 3053 C LEU A 401 -22.018 10.614 29.415 1.00128.14 C
ANISOU 3053 C LEU A 401 16834 17360 14494 -3338 -1275 1310 C
ATOM 3054 O LEU A 401 -22.619 10.107 30.369 1.00114.26 O
ANISOU 3054 O LEU A 401 15212 15588 12615 -3744 -1426 1354 O
ATOM 3055 CB LEU A 401 -22.450 12.983 28.705 1.00143.69 C
ANISOU 3055 CB LEU A 401 17389 20544 16662 -3003 -1516 1493 C
ATOM 3056 CG LEU A 401 -23.942 12.915 29.047 1.00134.41 C
ANISOU 3056 CG LEU A 401 16008 19963 15098 -3765 -1845 1444 C
ATOM 3057 CD1 LEU A 401 -24.169 13.128 30.536 1.00148.48 C
ANISOU 3057 CD1 LEU A 401 17359 21878 17178 -3790 -2022 1568 C
ATOM 3058 CD2 LEU A 401 -24.730 13.932 28.232 1.00104.90 C
ANISOU 3058 CD2 LEU A 401 11674 16998 11185 -3883 -2052 1487 C
ATOM 3059 N TYR A 402 -21.783 9.943 28.290 1.00137.98 N
ANISOU 3059 N TYR A 402 18710 18241 15475 -3468 -1008 1080 N
ATOM 3060 CA TYR A 402 -22.311 8.602 28.082 1.00160.70 C
ANISOU 3060 CA TYR A 402 22437 20713 17908 -4136 -876 842 C
ATOM 3061 C TYR A 402 -21.378 7.494 28.550 1.00177.06 C
ANISOU 3061 C TYR A 402 25248 21779 20246 -3823 -604 840 C
ATOM 3062 O TYR A 402 -21.774 6.323 28.520 1.00202.06 O
ANISOU 3062 O TYR A 402 29179 24485 23110 -4360 -444 666 O
ATOM 3063 CB TYR A 402 -22.648 8.399 26.602 1.00154.69 C
ANISOU 3063 CB TYR A 402 21982 20125 16667 -4549 -711 537 C
ATOM 3064 CG TYR A 402 -23.821 9.232 26.141 1.00156.87 C
ANISOU 3064 CG TYR A 402 21659 21401 16541 -5005 -1040 533 C
ATOM 3065 CD1 TYR A 402 -23.642 10.536 25.703 1.00165.12 C
ANISOU 3065 CD1 TYR A 402 21995 22990 17755 -4553 -1178 731 C
ATOM 3066 CD2 TYR A 402 -25.108 8.716 26.152 1.00169.00 C
ANISOU 3066 CD2 TYR A 402 23332 23331 17550 -5876 -1203 324 C
ATOM 3067 CE1 TYR A 402 -24.711 11.301 25.281 1.00175.40 C
ANISOU 3067 CE1 TYR A 402 22744 25180 18722 -4895 -1509 773 C
ATOM 3068 CE2 TYR A 402 -26.185 9.473 25.733 1.00189.23 C
ANISOU 3068 CE2 TYR A 402 25286 26844 19769 -6243 -1544 307 C
ATOM 3069 CZ TYR A 402 -25.980 10.765 25.299 1.00190.29 C
ANISOU 3069 CZ TYR A 402 24722 27485 20094 -5719 -1716 558 C
ATOM 3070 OH TYR A 402 -27.048 11.526 24.880 1.00202.28 O
ANISOU 3070 OH TYR A 402 25630 29925 21302 -6012 -2085 586 O
ATOM 3071 N CYS A 403 -20.163 7.819 28.989 1.00166.66 N
ANISOU 3071 N CYS A 403 23719 20108 19497 -2971 -538 1018 N
ATOM 3072 CA CYS A 403 -19.222 6.778 29.380 1.00155.69 C
ANISOU 3072 CA CYS A 403 22996 17761 18398 -2572 -311 1032 C
ATOM 3073 C CYS A 403 -18.543 7.075 30.711 1.00162.12 C
ANISOU 3073 C CYS A 403 23441 18475 19681 -1930 -518 1369 C
ATOM 3074 O CYS A 403 -18.808 6.402 31.711 1.00195.21 O
ANISOU 3074 O CYS A 403 27984 22385 23801 -2108 -648 1561 O
ATOM 3075 CB CYS A 403 -18.161 6.580 28.297 1.00149.54 C
ANISOU 3075 CB CYS A 403 22494 16481 17845 -2115 83 776 C
ATOM 3076 SG CYS A 403 -16.791 5.513 28.807 1.00160.05 S
ANISOU 3076 SG CYS A 403 24433 16654 19726 -1371 336 804 S
ATOM 3077 N PHE A 404 -17.655 8.074 30.725 1.00156.38 N
ANISOU 3077 N PHE A 404 22022 17986 19408 -1208 -529 1429 N
ATOM 3078 CA PHE A 404 -16.811 8.297 31.896 1.00107.85 C
ANISOU 3078 CA PHE A 404 15527 11724 13726 -528 -683 1678 C
ATOM 3079 C PHE A 404 -17.634 8.683 33.120 1.00152.18 C
ANISOU 3079 C PHE A 404 20735 17892 19194 -873 -1054 1942 C
ATOM 3080 O PHE A 404 -17.297 8.301 34.248 1.00151.55 O
ANISOU 3080 O PHE A 404 20758 17580 19244 -631 -1214 2182 O
ATOM 3081 CB PHE A 404 -15.772 9.376 31.590 1.00103.88 C
ANISOU 3081 CB PHE A 404 14296 11459 13713 212 -569 1598 C
ATOM 3082 CG PHE A 404 -14.904 9.069 30.400 1.00106.63 C
ANISOU 3082 CG PHE A 404 14991 11297 14225 541 -165 1291 C
ATOM 3083 CD1 PHE A 404 -14.527 7.767 30.114 1.00112.78 C
ANISOU 3083 CD1 PHE A 404 16631 11224 14995 570 56 1161 C
ATOM 3084 CD2 PHE A 404 -14.468 10.086 29.566 1.00103.52 C
ANISOU 3084 CD2 PHE A 404 14081 11250 14003 797 33 1118 C
ATOM 3085 CE1 PHE A 404 -13.730 7.486 29.018 1.00115.65 C
ANISOU 3085 CE1 PHE A 404 17286 11123 15531 833 468 817 C
ATOM 3086 CE2 PHE A 404 -13.671 9.810 28.469 1.00106.38 C
ANISOU 3086 CE2 PHE A 404 14770 11164 14487 1038 441 798 C
ATOM 3087 CZ PHE A 404 -13.302 8.509 28.195 1.00112.38 C
ANISOU 3087 CZ PHE A 404 16342 11109 15249 1048 659 623 C
ATOM 3088 N ALA A 405 -18.720 9.432 32.924 1.00124.80 N
ANISOU 3088 N ALA A 405 16798 15169 15450 -1439 -1198 1899 N
ATOM 3089 CA ALA A 405 -19.561 9.853 34.038 1.00129.59 C
ANISOU 3089 CA ALA A 405 16956 16342 15939 -1829 -1508 2073 C
ATOM 3090 C ALA A 405 -20.657 8.854 34.385 1.00126.17 C
ANISOU 3090 C ALA A 405 17177 15771 14989 -2674 -1583 2068 C
ATOM 3091 O ALA A 405 -21.323 9.029 35.411 1.00126.56 O
ANISOU 3091 O ALA A 405 16967 16202 14917 -3049 -1806 2192 O
ATOM 3092 CB ALA A 405 -20.198 11.216 33.749 1.00130.83 C
ANISOU 3092 CB ALA A 405 16197 17376 16138 -1981 -1625 2015 C
ATOM 3093 N ASN A 406 -20.867 7.825 33.567 1.00108.50 N
ANISOU 3093 N ASN A 406 15770 13009 12444 -3032 -1362 1885 N
ATOM 3094 CA ASN A 406 -21.910 6.851 33.860 1.00166.47 C
ANISOU 3094 CA ASN A 406 23766 20192 19294 -3894 -1361 1822 C
ATOM 3095 C ASN A 406 -21.563 6.075 35.125 1.00179.14 C
ANISOU 3095 C ASN A 406 25868 21242 20956 -3770 -1416 2122 C
ATOM 3096 O ASN A 406 -20.410 5.691 35.340 1.00167.67 O
ANISOU 3096 O ASN A 406 24704 19154 19848 -3036 -1338 2301 O
ATOM 3097 CB ASN A 406 -22.098 5.896 32.682 1.00151.97 C
ANISOU 3097 CB ASN A 406 22726 17866 17150 -4285 -1042 1512 C
ATOM 3098 CG ASN A 406 -23.416 5.148 32.745 1.00152.23 C
ANISOU 3098 CG ASN A 406 23236 17989 16614 -5341 -1015 1313 C
ATOM 3099 OD1 ASN A 406 -24.459 5.673 32.356 1.00164.63 O
ANISOU 3099 OD1 ASN A 406 24352 20333 17869 -5928 -1156 1105 O
ATOM 3100 ND2 ASN A 406 -23.374 3.914 33.233 1.00152.65 N
ANISOU 3100 ND2 ASN A 406 24207 17246 16545 -5582 -822 1367 N
ATOM 3101 N ASN A 407 -22.573 5.846 35.967 1.00206.59 N
ANISOU 3101 N ASN A 407 29439 24976 24080 -4495 -1556 2175 N
ATOM 3102 CA ASN A 407 -22.323 5.225 37.265 1.00216.56 C
ANISOU 3102 CA ASN A 407 31138 25820 25326 -4428 -1647 2519 C
ATOM 3103 C ASN A 407 -21.912 3.764 37.120 1.00212.36 C
ANISOU 3103 C ASN A 407 31802 24181 24705 -4397 -1371 2597 C
ATOM 3104 O ASN A 407 -20.980 3.306 37.794 1.00213.65 O
ANISOU 3104 O ASN A 407 32320 23748 25110 -3758 -1413 2945 O
ATOM 3105 CB ASN A 407 -23.564 5.350 38.147 1.00225.53 C
ANISOU 3105 CB ASN A 407 32101 27523 26069 -5313 -1808 2503 C
ATOM 3106 CG ASN A 407 -24.094 6.769 38.207 1.00221.96 C
ANISOU 3106 CG ASN A 407 30460 28135 25738 -5405 -2038 2366 C
ATOM 3107 OD1 ASN A 407 -23.801 7.590 37.337 1.00223.27 O
ANISOU 3107 OD1 ASN A 407 30036 28628 26167 -4998 -2038 2233 O
ATOM 3108 ND2 ASN A 407 -24.878 7.066 39.236 1.00223.91 N
ANISOU 3108 ND2 ASN A 407 30369 28902 25803 -5953 -2206 2394 N
ATOM 3109 N GLU A 408 -22.591 3.018 36.243 1.00225.46 N
ANISOU 3109 N GLU A 408 34081 25553 26030 -5069 -1082 2266 N
ATOM 3110 CA GLU A 408 -22.249 1.611 36.062 1.00229.85 C
ANISOU 3110 CA GLU A 408 35800 24996 26537 -5094 -743 2290 C
ATOM 3111 C GLU A 408 -20.855 1.445 35.474 1.00220.42 C
ANISOU 3111 C GLU A 408 34741 23149 25858 -4090 -593 2339 C
ATOM 3112 O GLU A 408 -20.156 0.479 35.801 1.00223.62 O
ANISOU 3112 O GLU A 408 35919 22597 26451 -3684 -445 2566 O
ATOM 3113 CB GLU A 408 -23.283 0.925 35.165 1.00239.00 C
ANISOU 3113 CB GLU A 408 37503 26073 27232 -6085 -416 1823 C
ATOM 3114 CG GLU A 408 -24.697 0.907 35.730 1.00237.90 C
ANISOU 3114 CG GLU A 408 37322 26496 26572 -7158 -501 1691 C
ATOM 3115 CD GLU A 408 -25.469 2.174 35.417 1.00224.19 C
ANISOU 3115 CD GLU A 408 34472 25983 24728 -7447 -790 1453 C
ATOM 3116 OE1 GLU A 408 -25.225 2.771 34.348 1.00215.67 O
ANISOU 3116 OE1 GLU A 408 32928 25238 23779 -7143 -793 1249 O
ATOM 3117 OE2 GLU A 408 -26.318 2.574 36.241 1.00219.04 O
ANISOU 3117 OE2 GLU A 408 33417 25942 23865 -7974 -1002 1473 O
ATOM 3118 N VAL A 409 -20.432 2.371 34.609 1.00227.90 N
ANISOU 3118 N VAL A 409 34957 24581 27053 -3675 -614 2126 N
ATOM 3119 CA VAL A 409 -19.071 2.327 34.087 1.00234.39 C
ANISOU 3119 CA VAL A 409 35797 24867 28396 -2723 -458 2118 C
ATOM 3120 C VAL A 409 -18.062 2.648 35.182 1.00243.09 C
ANISOU 3120 C VAL A 409 36545 25889 29929 -1818 -740 2541 C
ATOM 3121 O VAL A 409 -16.929 2.152 35.157 1.00246.20 O
ANISOU 3121 O VAL A 409 37240 25562 30743 -1034 -629 2633 O
ATOM 3122 CB VAL A 409 -18.935 3.282 32.885 1.00210.50 C
ANISOU 3122 CB VAL A 409 32097 22423 25461 -2600 -378 1775 C
ATOM 3123 CG1 VAL A 409 -17.515 3.268 32.336 1.00211.00 C
ANISOU 3123 CG1 VAL A 409 32144 21957 26069 -1664 -168 1697 C
ATOM 3124 CG2 VAL A 409 -19.928 2.904 31.796 1.00213.93 C
ANISOU 3124 CG2 VAL A 409 32899 22985 25401 -3501 -135 1360 C
ATOM 3125 N GLN A 410 -18.451 3.458 36.168 1.00227.45 N
ANISOU 3125 N GLN A 410 33903 24661 27857 -1918 -1105 2774 N
ATOM 3126 CA GLN A 410 -17.530 3.787 37.252 1.00230.63 C
ANISOU 3126 CA GLN A 410 33924 25101 28603 -1124 -1390 3147 C
ATOM 3127 C GLN A 410 -17.370 2.620 38.220 1.00265.28 C
ANISOU 3127 C GLN A 410 39203 28718 32875 -1059 -1453 3554 C
ATOM 3128 O GLN A 410 -16.245 2.250 38.575 1.00269.57 O
ANISOU 3128 O GLN A 410 39914 28720 33791 -190 -1517 3798 O
ATOM 3129 CB GLN A 410 -18.009 5.039 37.987 1.00191.06 C
ANISOU 3129 CB GLN A 410 27909 21158 23527 -1309 -1712 3217 C
ATOM 3130 CG GLN A 410 -17.808 6.328 37.204 1.00158.13 C
ANISOU 3130 CG GLN A 410 22770 17676 19636 -1054 -1678 2930 C
ATOM 3131 CD GLN A 410 -18.250 7.558 37.972 1.00156.10 C
ANISOU 3131 CD GLN A 410 21521 18396 19394 -1207 -1948 2988 C
ATOM 3132 OE1 GLN A 410 -19.109 7.481 38.850 1.00159.84 O
ANISOU 3132 OE1 GLN A 410 22020 19175 19536 -1810 -2127 3122 O
ATOM 3133 NE2 GLN A 410 -17.659 8.702 37.646 1.00150.96 N
ANISOU 3133 NE2 GLN A 410 19997 18218 19142 -687 -1933 2855 N
ATOM 3134 N LEU A 411 -18.485 2.026 38.658 1.00281.49 N
ANISOU 3134 N LEU A 411 41838 30706 34411 -1967 -1430 3633 N
ATOM 3135 CA LEU A 411 -18.388 0.864 39.539 1.00291.57 C
ANISOU 3135 CA LEU A 411 44088 31168 35528 -1968 -1438 4053 C
ATOM 3136 C LEU A 411 -17.745 -0.317 38.825 1.00301.55 C
ANISOU 3136 C LEU A 411 46300 31242 37034 -1597 -1075 4009 C
ATOM 3137 O LEU A 411 -16.983 -1.080 39.431 1.00310.56 O
ANISOU 3137 O LEU A 411 48022 31605 38371 -976 -1133 4417 O
ATOM 3138 CB LEU A 411 -19.770 0.482 40.064 1.00289.72 C
ANISOU 3138 CB LEU A 411 44305 31104 34671 -3127 -1400 4065 C
ATOM 3139 CG LEU A 411 -20.372 1.392 41.136 1.00282.54 C
ANISOU 3139 CG LEU A 411 42651 31188 33511 -3501 -1759 4209 C
ATOM 3140 CD1 LEU A 411 -21.801 0.980 41.454 1.00281.90 C
ANISOU 3140 CD1 LEU A 411 43013 31264 32830 -4740 -1633 4078 C
ATOM 3141 CD2 LEU A 411 -19.515 1.367 42.391 1.00285.33 C
ANISOU 3141 CD2 LEU A 411 42989 31440 33983 -2797 -2095 4765 C
ATOM 3142 N GLU A 412 -18.040 -0.487 37.533 1.00299.62 N
ANISOU 3142 N GLU A 412 46217 30845 36780 -1964 -696 3511 N
ATOM 3143 CA GLU A 412 -17.405 -1.554 36.769 1.00284.25 C
ANISOU 3143 CA GLU A 412 45101 27786 35114 -1635 -285 3372 C
ATOM 3144 C GLU A 412 -15.918 -1.292 36.569 1.00302.40 C
ANISOU 3144 C GLU A 412 46997 29820 38080 -404 -349 3422 C
ATOM 3145 O GLU A 412 -15.122 -2.237 36.529 1.00298.83 O
ANISOU 3145 O GLU A 412 47219 28342 37980 180 -164 3544 O
ATOM 3146 CB GLU A 412 -18.112 -1.722 35.424 1.00250.48 C
ANISOU 3146 CB GLU A 412 41016 23551 30605 -2405 137 2769 C
ATOM 3147 CG GLU A 412 -18.364 -3.169 35.022 1.00239.07 C
ANISOU 3147 CG GLU A 412 40797 20995 29043 -2865 639 2619 C
ATOM 3148 CD GLU A 412 -17.157 -3.816 34.376 1.00240.33 C
ANISOU 3148 CD GLU A 412 41363 20165 29786 -2034 961 2511 C
ATOM 3149 OE1 GLU A 412 -16.238 -3.078 33.966 1.00236.70 O
ANISOU 3149 OE1 GLU A 412 40177 20001 29756 -1251 850 2407 O
ATOM 3150 OE2 GLU A 412 -17.127 -5.062 34.276 1.00244.68 O
ANISOU 3150 OE2 GLU A 412 42956 19622 30390 -2181 1360 2500 O
ATOM 3151 N PHE A 413 -15.524 -0.022 36.435 1.00323.27 N
ANISOU 3151 N PHE A 413 48540 33352 40935 2 -581 3302 N
ATOM 3152 CA PHE A 413 -14.103 0.299 36.344 1.00332.26 C
ANISOU 3152 CA PHE A 413 49207 34331 42705 1146 -644 3308 C
ATOM 3153 C PHE A 413 -13.398 0.044 37.667 1.00348.75 C
ANISOU 3153 C PHE A 413 51342 36189 44980 1879 -1029 3869 C
ATOM 3154 O PHE A 413 -12.234 -0.372 37.693 1.00359.57 O
ANISOU 3154 O PHE A 413 52820 36942 46858 2824 -1021 3955 O
ATOM 3155 CB PHE A 413 -13.918 1.752 35.907 1.00315.12 C
ANISOU 3155 CB PHE A 413 45870 33178 40682 1311 -747 3028 C
ATOM 3156 CG PHE A 413 -12.505 2.249 36.028 1.00305.18 C
ANISOU 3156 CG PHE A 413 43974 31941 40041 2427 -848 3023 C
ATOM 3157 CD1 PHE A 413 -11.570 1.968 35.047 1.00303.12 C
ANISOU 3157 CD1 PHE A 413 43821 31113 40239 2976 -495 2664 C
ATOM 3158 CD2 PHE A 413 -12.116 3.009 37.120 1.00299.64 C
ANISOU 3158 CD2 PHE A 413 42530 31866 39453 2884 -1269 3317 C
ATOM 3159 CE1 PHE A 413 -10.271 2.428 35.156 1.00297.79 C
ANISOU 3159 CE1 PHE A 413 42512 30489 40144 3976 -564 2590 C
ATOM 3160 CE2 PHE A 413 -10.819 3.471 37.234 1.00295.39 C
ANISOU 3160 CE2 PHE A 413 41355 31407 39472 3878 -1349 3247 C
ATOM 3161 CZ PHE A 413 -9.896 3.181 36.251 1.00293.94 C
ANISOU 3161 CZ PHE A 413 41271 30651 39761 4431 -998 2877 C
ATOM 3162 N ARG A 414 -14.090 0.286 38.778 1.00342.79 N
ANISOU 3162 N ARG A 414 50488 35950 43805 1452 -1374 4241 N
ATOM 3163 CA ARG A 414 -13.512 0.025 40.087 1.00329.93 C
ANISOU 3163 CA ARG A 414 48953 34178 42227 2054 -1772 4815 C
ATOM 3164 C ARG A 414 -13.570 -1.450 40.465 1.00327.48 C
ANISOU 3164 C ARG A 414 49929 32709 41789 2026 -1658 5209 C
ATOM 3165 O ARG A 414 -12.904 -1.854 41.426 1.00345.67 O
ANISOU 3165 O ARG A 414 52459 34685 44196 2703 -1972 5734 O
ATOM 3166 CB ARG A 414 -14.227 0.876 41.140 1.00310.27 C
ANISOU 3166 CB ARG A 414 45859 32719 39311 1553 -2152 5032 C
ATOM 3167 CG ARG A 414 -13.397 1.186 42.370 1.00301.80 C
ANISOU 3167 CG ARG A 414 44337 31969 38363 2320 -2629 5478 C
ATOM 3168 CD ARG A 414 -13.824 2.509 42.986 1.00290.25 C
ANISOU 3168 CD ARG A 414 41799 31769 36715 1978 -2897 5397 C
ATOM 3169 NE ARG A 414 -15.269 2.573 43.182 1.00288.20 N
ANISOU 3169 NE ARG A 414 41744 31876 35881 793 -2829 5351 N
ATOM 3170 CZ ARG A 414 -15.944 3.690 43.436 1.00281.00 C
ANISOU 3170 CZ ARG A 414 39960 31999 34810 264 -2933 5146 C
ATOM 3171 NH1 ARG A 414 -15.308 4.851 43.522 1.00274.39 N
ANISOU 3171 NH1 ARG A 414 38015 31906 34333 791 -3081 4982 N
ATOM 3172 NH2 ARG A 414 -17.259 3.647 43.598 1.00280.58 N
ANISOU 3172 NH2 ARG A 414 40123 32220 34263 -804 -2858 5070 N
ATOM 3173 N LYS A 415 -14.341 -2.256 39.730 1.00317.73 N
ANISOU 3173 N LYS A 415 49542 30853 40329 1262 -1207 4969 N
ATOM 3174 CA LYS A 415 -14.391 -3.691 39.993 1.00292.16 C
ANISOU 3174 CA LYS A 415 47593 26395 37021 1207 -990 5296 C
ATOM 3175 C LYS A 415 -13.055 -4.366 39.708 1.00308.21 C
ANISOU 3175 C LYS A 415 49932 27441 39732 2364 -894 5386 C
ATOM 3176 O LYS A 415 -12.710 -5.356 40.362 1.00304.08 O
ANISOU 3176 O LYS A 415 50252 26001 39282 2773 -945 5897 O
ATOM 3177 CB LYS A 415 -15.496 -4.332 39.151 1.00252.91 C
ANISOU 3177 CB LYS A 415 43362 21041 31693 84 -455 4882 C
ATOM 3178 CG LYS A 415 -15.981 -5.676 39.662 1.00235.67 C
ANISOU 3178 CG LYS A 415 42514 17806 29224 -370 -214 5232 C
ATOM 3179 CD LYS A 415 -16.858 -5.510 40.891 1.00234.68 C
ANISOU 3179 CD LYS A 415 42481 18211 28476 -1040 -527 5655 C
ATOM 3180 CE LYS A 415 -17.556 -6.811 41.249 1.00252.32 C
ANISOU 3180 CE LYS A 415 46094 19444 30334 -1755 -167 5891 C
ATOM 3181 NZ LYS A 415 -18.506 -6.633 42.381 1.00255.04 N
ANISOU 3181 NZ LYS A 415 46536 20351 30015 -2565 -401 6214 N
ATOM 3182 N SER A 416 -12.292 -3.845 38.746 1.00319.29 N
ANISOU 3182 N SER A 416 50669 29005 41642 2908 -745 4899 N
ATOM 3183 CA SER A 416 -10.986 -4.396 38.399 1.00325.95 C
ANISOU 3183 CA SER A 416 51659 28989 43199 4016 -626 4865 C
ATOM 3184 C SER A 416 -9.877 -3.376 38.610 1.00320.55 C
ANISOU 3184 C SER A 416 49801 29028 42965 5012 -1003 4818 C
ATOM 3185 O SER A 416 -8.944 -3.643 39.374 1.00334.77 O
ANISOU 3185 O SER A 416 51562 30534 45100 5989 -1342 5230 O
ATOM 3186 CB SER A 416 -10.995 -4.905 36.952 1.00326.58 C
ANISOU 3186 CB SER A 416 52146 28413 43526 3732 33 4219 C
ATOM 3187 OG SER A 416 -11.864 -6.016 36.811 1.00334.42 O
ANISOU 3187 OG SER A 416 54304 28574 44185 2917 428 4253 O
ATOM 3188 N TRP A 417 -9.946 -2.222 37.946 1.00283.68 N
ANISOU 3188 N TRP A 417 44182 25292 38312 4795 -943 4322 N
ATOM 3189 CA TRP A 417 -9.063 -1.085 38.214 1.00256.08 C
ANISOU 3189 CA TRP A 417 39496 22647 35154 5545 -1268 4235 C
ATOM 3190 C TRP A 417 -7.582 -1.391 37.965 1.00248.31 C
ANISOU 3190 C TRP A 417 38329 21082 34934 6759 -1218 4094 C
ATOM 3191 O TRP A 417 -6.912 -2.049 38.762 1.00233.05 O
ANISOU 3191 O TRP A 417 36692 18623 33235 7535 -1506 4542 O
ATOM 3192 CB TRP A 417 -9.291 -0.594 39.651 1.00240.61 C
ANISOU 3192 CB TRP A 417 37151 21428 32843 5560 -1853 4785 C
ATOM 3193 CG TRP A 417 -8.131 0.103 40.282 1.00222.07 C
ANISOU 3193 CG TRP A 417 33855 19623 30899 6579 -2249 4866 C
ATOM 3194 CD1 TRP A 417 -7.641 1.336 39.969 1.00211.45 C
ANISOU 3194 CD1 TRP A 417 31361 19155 29825 6836 -2256 4440 C
ATOM 3195 CD2 TRP A 417 -7.325 -0.389 41.359 1.00227.07 C
ANISOU 3195 CD2 TRP A 417 34600 19989 31686 7458 -2696 5400 C
ATOM 3196 NE1 TRP A 417 -6.571 1.639 40.778 1.00207.21 N
ANISOU 3196 NE1 TRP A 417 30180 18938 29615 7790 -2653 4611 N
ATOM 3197 CE2 TRP A 417 -6.358 0.595 41.640 1.00221.90 C
ANISOU 3197 CE2 TRP A 417 32775 20142 31395 8207 -2963 5211 C
ATOM 3198 CE3 TRP A 417 -7.325 -1.569 42.108 1.00217.21 C
ANISOU 3198 CE3 TRP A 417 34337 17900 30292 7683 -2889 6030 C
ATOM 3199 CZ2 TRP A 417 -5.400 0.436 42.639 1.00221.44 C
ANISOU 3199 CZ2 TRP A 417 32190 20368 31579 8838 -3350 5502 C
ATOM 3200 CZ3 TRP A 417 -6.374 -1.726 43.099 1.00216.61 C
ANISOU 3200 CZ3 TRP A 417 33700 18137 30466 8361 -3290 6360 C
ATOM 3201 CH2 TRP A 417 -5.425 -0.729 43.356 1.00212.36 C
ANISOU 3201 CH2 TRP A 417 31839 18561 30286 8916 -3530 6092 C
TER 3202 TRP A 417
HETATM 3203 C67 9DK B 1 -19.464 23.922 10.142 1.00217.72 C
HETATM 3204 C69 9DK B 1 -20.257 24.871 11.093 1.00193.70 C
HETATM 3205 C70 9DK B 1 -19.300 25.990 11.624 1.00147.74 C
HETATM 3206 C71 9DK B 1 -20.792 24.096 12.330 1.00206.78 C
HETATM 3207 C72 9DK B 1 -21.472 25.487 10.338 1.00175.75 C
HETATM 3208 C75 9DK B 1 -23.462 27.074 10.613 1.00195.39 C
HETATM 3209 C76 9DK B 1 -24.295 26.540 9.442 1.00191.13 C
HETATM 3210 C77 9DK B 1 -24.961 25.242 9.785 1.00175.48 C
HETATM 3211 C78 9DK B 1 -24.589 23.948 9.459 1.00171.26 C
HETATM 3212 C80 9DK B 1 -26.427 24.015 10.634 1.00167.82 C
HETATM 3213 N74 9DK B 1 -22.267 26.326 11.031 1.00190.04 N
HETATM 3214 N79 9DK B 1 -25.554 23.160 10.021 1.00172.01 N
HETATM 3215 N81 9DK B 1 -26.076 25.267 10.494 1.00170.45 N
HETATM 3216 O68 9DK B 1 -19.947 22.860 9.743 1.00233.48 O
HETATM 3217 O73 9DK B 1 -21.667 25.205 9.149 1.00151.13 O
HETATM 3218 C57 9DQ B 2 -17.481 24.101 7.447 1.00202.74 C
HETATM 3219 C59 9DQ B 2 -17.221 23.713 8.912 1.00191.30 C
HETATM 3220 C60 9DQ B 2 -16.959 22.180 9.004 1.00177.46 C
HETATM 3221 C61 9DQ B 2 -17.117 21.588 10.382 1.00147.42 C
HETATM 3222 N62 9DQ B 2 -16.864 22.276 11.533 1.00147.44 N
HETATM 3223 N63 9DQ B 2 -17.086 21.502 12.593 1.00147.26 N
HETATM 3224 N64 9DQ B 2 -17.488 20.296 12.052 1.00147.48 N
HETATM 3225 N65 9DQ B 2 -17.500 20.371 10.666 1.00147.69 N
HETATM 3226 N66 9DQ B 2 -18.231 24.336 9.784 1.00199.24 N
HETATM 3227 O58 9DQ B 2 -16.653 24.802 6.875 1.00194.74 O
ATOM 3228 N GLY B 3 -18.602 23.658 6.861 1.00206.65 N
ATOM 3229 CA GLY B 3 -19.005 23.934 5.485 1.00188.51 C
ATOM 3230 C GLY B 3 -19.193 25.441 5.271 1.00185.02 C
ATOM 3231 O GLY B 3 -18.769 25.954 4.240 1.00193.04 O
ATOM 3232 N THR B 4 -19.812 26.155 6.224 1.00168.47 N
ATOM 3233 CA THR B 4 -20.039 27.604 6.114 1.00149.26 C
ATOM 3234 C THR B 4 -18.730 28.413 6.277 1.00156.52 C
ATOM 3235 O THR B 4 -18.499 29.342 5.505 1.00199.42 O
ATOM 3236 CB THR B 4 -21.155 28.112 7.084 1.00163.71 C
ATOM 3237 OG1 THR B 4 -21.758 29.328 6.690 1.00159.15 O
ATOM 3238 CG2 THR B 4 -20.745 28.297 8.555 1.00184.02 C
HETATM 3239 C36 9DT B 5 -15.574 28.484 6.498 1.00158.90 C
HETATM 3240 C38 9DT B 5 -16.599 28.623 7.681 1.00131.28 C
HETATM 3241 C39 9DT B 5 -16.829 30.110 8.061 1.00131.46 C
HETATM 3242 C40 9DT B 5 -16.079 27.882 8.954 1.00132.24 C
HETATM 3243 C41 9DT B 5 -14.574 27.590 8.948 1.00155.29 C
HETATM 3244 C42 9DT B 5 -14.102 26.340 8.529 1.00167.56 C
HETATM 3245 C43 9DT B 5 -12.732 26.081 8.518 1.00168.12 C
HETATM 3246 C44 9DT B 5 -11.825 27.059 8.921 1.00164.42 C
HETATM 3247 C45 9DT B 5 -12.287 28.305 9.335 1.00150.63 C
HETATM 3248 C46 9DT B 5 -13.653 28.569 9.347 1.00150.30 C
HETATM 3249 F47 9DT B 5 -14.077 29.786 9.753 1.00150.48 F
HETATM 3250 N48 9DT B 5 -17.902 28.036 7.278 1.00137.12 N
HETATM 3251 O37 9DT B 5 -14.763 29.379 6.279 1.00175.67 O
ATOM 3252 N THR B 6 -15.605 27.368 5.745 1.00157.95 N
ATOM 3253 CA THR B 6 -14.724 27.085 4.610 1.00160.97 C
ATOM 3254 C THR B 6 -14.806 28.163 3.522 1.00163.21 C
ATOM 3255 O THR B 6 -13.777 28.513 2.946 1.00182.07 O
ATOM 3256 CB THR B 6 -15.109 25.776 3.874 1.00164.63 C
ATOM 3257 OG1 THR B 6 -16.491 25.543 4.001 1.00188.54 O
ATOM 3258 CG2 THR B 6 -14.408 24.513 4.371 1.00128.81 C
ATOM 3259 N SER B 7 -16.033 28.640 3.275 1.00154.40 N
ATOM 3260 CA SER B 7 -16.352 29.655 2.288 1.00151.93 C
ATOM 3261 C SER B 7 -15.491 30.922 2.483 1.00155.86 C
ATOM 3262 O SER B 7 -14.648 31.199 1.630 1.00172.52 O
ATOM 3263 CB SER B 7 -17.890 29.857 2.244 1.00161.17 C
ATOM 3264 OG SER B 7 -18.511 29.130 1.200 1.00165.77 O
ATOM 3265 N ASP B 8 -15.700 31.666 3.583 1.00145.14 N
ATOM 3266 CA ASP B 8 -14.944 32.893 3.889 1.00160.85 C
ATOM 3267 C ASP B 8 -13.425 32.634 3.965 1.00188.69 C
ATOM 3268 O ASP B 8 -12.635 33.543 3.711 1.00221.50 O
ATOM 3269 CB ASP B 8 -15.386 33.650 5.170 1.00168.25 C
ATOM 3270 CG ASP B 8 -16.840 33.490 5.629 1.00173.39 C
ATOM 3271 OD1 ASP B 8 -17.148 34.035 6.712 1.00193.63 O
ATOM 3272 OD2 ASP B 8 -17.642 32.842 4.927 1.00160.78 O1-
HETATM 3273 C01 9DW B 9 -7.941 25.823 8.237 1.00187.69 C
HETATM 3274 C02 9DW B 9 -6.726 25.826 7.293 1.00177.49 C
HETATM 3275 C05 9DW B 9 -3.609 27.957 7.855 1.00156.29 C
HETATM 3276 C07 9DW B 9 -5.327 29.424 7.025 1.00155.18 C
HETATM 3277 C08 9DW B 9 -6.235 28.365 6.943 1.00144.84 C
HETATM 3278 C09 9DW B 9 -7.601 28.664 6.461 1.00132.61 C
HETATM 3279 C11 9DW B 9 -9.316 28.532 4.775 1.00128.81 C
HETATM 3280 C12 9DW B 9 -10.182 29.237 5.614 1.00128.81 C
HETATM 3281 C13 9DW B 9 -9.757 29.661 6.872 1.00128.81 C
HETATM 3282 C14 9DW B 9 -8.469 29.371 7.296 1.00130.57 C
HETATM 3283 C15 9DW B 9 -11.596 29.572 5.165 1.00128.81 C
HETATM 3284 C03 9DW B 9 -5.824 27.071 7.334 1.00158.18 C
HETATM 3285 C04 9DW B 9 -4.511 26.889 7.783 1.00149.88 C
HETATM 3286 C06 9DW B 9 -4.028 29.224 7.474 1.00173.00 C
HETATM 3287 C10 9DW B 9 -8.026 28.244 5.201 1.00132.68 C
HETATM 3288 C16 9DW B 9 -11.672 30.936 4.438 1.00159.80 C
HETATM 3289 C88 9DW B 9 -10.984 30.848 3.070 1.00162.39 C
HETATM 3290 CA7 9DW B 9 -2.016 26.669 9.063 1.00146.32 C
HETATM 3291 N17 9DW B 9 -13.052 31.397 4.313 1.00177.85 N
HETATM 3292 O89 9DW B 9 -9.894 31.399 2.923 1.00163.30 O
HETATM 3293 OA6 9DW B 9 -2.312 27.825 8.291 1.00148.27 O
HETATM 3294 C91 9DZ B 10 -11.177 29.936 0.752 1.00145.95 C
HETATM 3295 C92 9DZ B 10 -12.248 29.206 -0.096 1.00128.81 C
HETATM 3296 C93 9DZ B 10 -11.869 28.890 -1.567 1.00137.51 C
HETATM 3297 C94 9DZ B 10 -11.051 27.599 -1.745 1.00147.37 C
HETATM 3298 C95 9DZ B 10 -10.534 27.429 -3.164 1.00169.71 C
HETATM 3299 C96 9DZ B 10 -11.247 26.663 -4.089 1.00180.48 C
HETATM 3300 C97 9DZ B 10 -10.753 26.526 -5.386 1.00184.25 C
HETATM 3301 C98 9DZ B 10 -9.574 27.137 -5.769 1.00211.30 C
HETATM 3302 C99 9DZ B 10 -8.862 27.898 -4.865 1.00194.55 C
HETATM 3303 CA0 9DZ B 10 -9.339 28.049 -3.556 1.00180.68 C
HETATM 3304 CA1 9DZ B 10 -7.588 28.530 -5.371 1.00202.50 C
HETATM 3305 CA2 9DZ B 10 -11.457 25.723 -6.427 1.00184.27 C
HETATM 3306 CA3 9DZ B 10 -10.757 31.288 0.160 1.00154.60 C
HETATM 3307 N90 9DZ B 10 -11.630 30.154 2.120 1.00156.76 N
HETATM 3308 NA5 9DZ B 10 -9.467 31.535 0.083 1.00173.61 N
HETATM 3309 OA4 9DZ B 10 -11.577 32.113 -0.209 1.00128.81 O
TER 3310 9DZ B 10
HETATM 3311 C1 NAG C 1 8.623 48.837 -21.113 1.00196.20 C
HETATM 3312 C2 NAG C 1 9.078 50.232 -21.511 1.00190.31 C
HETATM 3313 C3 NAG C 1 10.590 50.227 -21.556 1.00194.77 C
HETATM 3314 C4 NAG C 1 11.212 49.719 -20.259 1.00212.18 C
HETATM 3315 C5 NAG C 1 10.370 48.807 -19.364 1.00219.58 C
HETATM 3316 C6 NAG C 1 10.361 49.356 -17.938 1.00225.41 C
HETATM 3317 C7 NAG C 1 7.843 51.708 -23.014 1.00175.28 C
HETATM 3318 C8 NAG C 1 7.401 51.953 -24.427 1.00168.05 C
HETATM 3319 N2 NAG C 1 8.553 50.598 -22.814 1.00182.57 N
HETATM 3320 O3 NAG C 1 11.059 51.555 -21.819 1.00203.27 O
HETATM 3321 O4 NAG C 1 12.314 48.906 -20.647 1.00218.76 O
HETATM 3322 O5 NAG C 1 9.015 48.583 -19.762 1.00223.62 O
HETATM 3323 O6 NAG C 1 9.721 48.420 -17.064 1.00226.99 O
HETATM 3324 O7 NAG C 1 7.571 52.480 -22.110 1.00169.91 O
HETATM 3325 C1 NAG C 2 13.530 49.506 -20.184 1.00214.09 C
HETATM 3326 C2 NAG C 2 14.330 48.346 -19.569 1.00213.26 C
HETATM 3327 C3 NAG C 2 15.829 48.350 -19.846 1.00226.53 C
HETATM 3328 C4 NAG C 2 16.117 48.871 -21.242 1.00227.64 C
HETATM 3329 C5 NAG C 2 15.541 50.270 -21.335 1.00213.19 C
HETATM 3330 C6 NAG C 2 15.951 50.958 -22.630 1.00196.24 C
HETATM 3331 C7 NAG C 2 14.091 47.189 -17.435 1.00191.97 C
HETATM 3332 C8 NAG C 2 13.964 47.347 -15.949 1.00191.43 C
HETATM 3333 N2 NAG C 2 14.095 48.321 -18.134 1.00199.78 N
HETATM 3334 O3 NAG C 2 16.325 47.013 -19.729 1.00237.70 O
HETATM 3335 O4 NAG C 2 17.528 48.908 -21.474 1.00235.70 O
HETATM 3336 O5 NAG C 2 14.124 50.178 -21.304 1.00211.75 O
HETATM 3337 O6 NAG C 2 15.415 52.287 -22.649 1.00187.38 O
HETATM 3338 O7 NAG C 2 14.183 46.094 -17.964 1.00187.27 O
HETATM 3339 C1 NAG A 603 -3.760 37.404 -35.085 1.00228.51 C
HETATM 3340 C2 NAG A 603 -5.105 38.124 -35.025 1.00255.41 C
HETATM 3341 C3 NAG A 603 -6.083 37.621 -36.014 1.00274.00 C
HETATM 3342 C4 NAG A 603 -5.443 37.544 -37.396 1.00272.84 C
HETATM 3343 C5 NAG A 603 -4.110 36.803 -37.327 1.00263.12 C
HETATM 3344 C6 NAG A 603 -3.445 36.827 -38.701 1.00279.01 C
HETATM 3345 C7 NAG A 603 -6.877 38.713 -33.340 1.00283.56 C
HETATM 3346 C8 NAG A 603 -7.446 38.606 -31.928 1.00295.76 C
HETATM 3347 N2 NAG A 603 -5.646 38.022 -33.681 1.00268.39 N
HETATM 3348 O3 NAG A 603 -6.437 36.306 -35.688 1.00283.64 O
HETATM 3349 O4 NAG A 603 -6.304 36.870 -38.270 1.00280.57 O
HETATM 3350 O5 NAG A 603 -3.272 37.425 -36.395 1.00241.08 O
HETATM 3351 O6 NAG A 603 -3.158 35.517 -39.104 1.00289.77 O
HETATM 3352 O7 NAG A 603 -7.439 39.359 -34.159 1.00289.11 O
HETATM 3353 C1 SOG A 604 -15.960 40.794 10.806 1.00213.12 C
HETATM 3354 C2 SOG A 604 -17.080 39.810 10.802 1.00199.98 C
HETATM 3355 C3 SOG A 604 -16.982 38.861 9.683 1.00175.18 C
HETATM 3356 C4 SOG A 604 -16.781 39.510 8.369 1.00185.25 C
HETATM 3357 C5 SOG A 604 -15.656 40.508 8.394 1.00196.30 C
HETATM 3358 C6 SOG A 604 -15.623 41.251 7.106 1.00188.11 C
HETATM 3359 C1' SOG A 604 -14.708 42.502 12.732 1.00200.14 C
HETATM 3360 C2' SOG A 604 -14.716 42.983 14.177 1.00180.30 C
HETATM 3361 C3' SOG A 604 -13.602 43.906 14.618 1.00159.30 C
HETATM 3362 C4' SOG A 604 -13.619 45.332 14.092 1.00149.25 C
HETATM 3363 C5' SOG A 604 -14.493 46.308 14.784 1.00167.13 C
HETATM 3364 C6' SOG A 604 -15.913 45.909 15.044 1.00173.56 C
HETATM 3365 C7' SOG A 604 -16.152 44.781 16.003 1.00169.11 C
HETATM 3366 C8' SOG A 604 -17.589 44.439 16.345 1.00161.63 C
HETATM 3367 S1 SOG A 604 -16.247 41.995 12.029 1.00216.37 S
HETATM 3368 O2 SOG A 604 -17.109 39.140 12.057 1.00194.27 O
HETATM 3369 O3 SOG A 604 -18.155 38.033 9.643 1.00168.85 O
HETATM 3370 O4 SOG A 604 -16.529 38.556 7.362 1.00192.97 O
HETATM 3371 O5 SOG A 604 -15.774 41.448 9.486 1.00213.47 O
HETATM 3372 O6 SOG A 604 -15.119 42.545 7.118 1.00181.57 O
HETATM 3373 C1 SOG A 605 -9.047 42.489 11.519 1.00198.38 C
HETATM 3374 C2 SOG A 605 -10.454 42.821 11.885 1.00194.38 C
HETATM 3375 C3 SOG A 605 -11.428 42.187 10.985 1.00211.91 C
HETATM 3376 C4 SOG A 605 -11.141 42.402 9.550 1.00206.33 C
HETATM 3377 C5 SOG A 605 -9.716 42.072 9.200 1.00203.29 C
HETATM 3378 C6 SOG A 605 -9.443 42.479 7.795 1.00196.59 C
HETATM 3379 C1' SOG A 605 -6.362 43.458 11.737 1.00191.20 C
HETATM 3380 C2' SOG A 605 -5.151 43.584 12.651 1.00192.83 C
HETATM 3381 C3' SOG A 605 -3.893 44.195 12.072 1.00179.16 C
HETATM 3382 C4' SOG A 605 -2.621 44.104 12.899 1.00142.65 C
HETATM 3383 C5' SOG A 605 -1.551 45.089 12.622 1.00126.47 C
HETATM 3384 C6' SOG A 605 -0.231 44.893 13.303 1.00135.52 C
HETATM 3385 C7' SOG A 605 0.802 45.969 13.138 1.00152.15 C
HETATM 3386 C8' SOG A 605 2.095 45.829 13.916 1.00157.42 C
HETATM 3387 S1 SOG A 605 -7.958 43.429 12.494 1.00192.51 S
HETATM 3388 O2 SOG A 605 -10.676 42.452 13.241 1.00160.30 O
HETATM 3389 O3 SOG A 605 -12.752 42.655 11.292 1.00229.35 O
HETATM 3390 O4 SOG A 605 -12.003 41.640 8.736 1.00205.38 O
HETATM 3391 O5 SOG A 605 -8.766 42.719 10.079 1.00204.55 O
HETATM 3392 O6 SOG A 605 -9.623 41.528 6.800 1.00190.11 O
HETATM 3393 C1 SOG A 606 -21.584 10.931 42.084 1.00221.03 C
HETATM 3394 C2 SOG A 606 -20.704 11.116 40.895 1.00216.15 C
HETATM 3395 C3 SOG A 606 -21.076 10.228 39.784 1.00208.32 C
HETATM 3396 C4 SOG A 606 -22.515 10.268 39.446 1.00214.08 C
HETATM 3397 C5 SOG A 606 -23.389 10.094 40.658 1.00209.81 C
HETATM 3398 C6 SOG A 606 -24.810 10.327 40.282 1.00202.98 C
HETATM 3399 C1' SOG A 606 -19.957 9.651 44.061 1.00190.39 C
HETATM 3400 C2' SOG A 606 -18.712 8.780 43.966 1.00164.51 C
HETATM 3401 C3' SOG A 606 -18.109 8.270 45.257 1.00164.62 C
HETATM 3402 C4' SOG A 606 -16.665 8.640 45.555 1.00161.73 C
HETATM 3403 C5' SOG A 606 -16.143 8.330 46.906 1.00170.42 C
HETATM 3404 C6' SOG A 606 -14.886 9.019 47.341 1.00156.80 C
HETATM 3405 C7' SOG A 606 -14.540 8.975 48.800 1.00155.36 C
HETATM 3406 C8' SOG A 606 -13.124 9.343 49.200 1.00149.50 C
HETATM 3407 S1 SOG A 606 -21.217 9.413 42.846 1.00222.01 S
HETATM 3408 O2 SOG A 606 -20.736 12.484 40.506 1.00213.09 O
HETATM 3409 O3 SOG A 606 -20.294 10.548 38.621 1.00182.44 O
HETATM 3410 O4 SOG A 606 -22.856 11.475 38.802 1.00220.82 O
HETATM 3411 O5 SOG A 606 -23.027 10.987 41.735 1.00216.50 O
HETATM 3412 O6 SOG A 606 -25.232 9.877 39.038 1.00199.94 O
CONECT 166 367
CONECT 290 634
CONECT 298 3339
CONECT 367 166
CONECT 452 3311
CONECT 471 812
CONECT 634 290
CONECT 812 471
CONECT 1622 2218
CONECT 2218 1622
CONECT 3203 3204 3216 3226
CONECT 3204 3203 3205 3206 3207
CONECT 3205 3204
CONECT 3206 3204
CONECT 3207 3204 3213 3217
CONECT 3208 3209 3213
CONECT 3209 3208 3210
CONECT 3210 3209 3211 3215
CONECT 3211 3210 3214
CONECT 3212 3214 3215
CONECT 3213 3207 3208
CONECT 3214 3211 3212
CONECT 3215 3210 3212
CONECT 3216 3203
CONECT 3217 3207
CONECT 3218 3219 3227 3228
CONECT 3219 3218 3220 3226
CONECT 3220 3219 3221
CONECT 3221 3220 3222 3225
CONECT 3222 3221 3223
CONECT 3223 3222 3224
CONECT 3224 3223 3225
CONECT 3225 3221 3224
CONECT 3226 3203 3219
CONECT 3227 3218
CONECT 3228 3218
CONECT 3234 3250
CONECT 3239 3240 3251 3252
CONECT 3240 3239 3241 3242 3250
CONECT 3241 3240
CONECT 3242 3240 3243
CONECT 3243 3242 3244 3248
CONECT 3244 3243 3245
CONECT 3245 3244 3246
CONECT 3246 3245 3247
CONECT 3247 3246 3248
CONECT 3248 3243 3247 3249
CONECT 3249 3248
CONECT 3250 3234 3240
CONECT 3251 3239
CONECT 3252 3239
CONECT 3267 3291
CONECT 3273 3274
CONECT 3274 3273 3284
CONECT 3275 3285 3286 3293
CONECT 3276 3277 3286
CONECT 3277 3276 3278 3284
CONECT 3278 3277 3282 3287
CONECT 3279 3280 3287
CONECT 3280 3279 3281 3283
CONECT 3281 3280 3282
CONECT 3282 3278 3281
CONECT 3283 3280 3288
CONECT 3284 3274 3277 3285
CONECT 3285 3275 3284
CONECT 3286 3275 3276
CONECT 3287 3278 3279
CONECT 3288 3283 3289 3291
CONECT 3289 3288 3292 3307
CONECT 3290 3293
CONECT 3291 3267 3288
CONECT 3292 3289
CONECT 3293 3275 3290
CONECT 3294 3295 3306 3307
CONECT 3295 3294 3296
CONECT 3296 3295 3297
CONECT 3297 3296 3298
CONECT 3298 3297 3299 3303
CONECT 3299 3298 3300
CONECT 3300 3299 3301 3305
CONECT 3301 3300 3302
CONECT 3302 3301 3303 3304
CONECT 3303 3298 3302
CONECT 3304 3302
CONECT 3305 3300
CONECT 3306 3294 3308 3309
CONECT 3307 3289 3294
CONECT 3308 3306
CONECT 3309 3306
CONECT 3311 452 3312 3322
CONECT 3312 3311 3313 3319
CONECT 3313 3312 3314 3320
CONECT 3314 3313 3315 3321
CONECT 3315 3314 3316 3322
CONECT 3316 3315 3323
CONECT 3317 3318 3319 3324
CONECT 3318 3317
CONECT 3319 3312 3317
CONECT 3320 3313
CONECT 3321 3314 3325
CONECT 3322 3311 3315
CONECT 3323 3316
CONECT 3324 3317
CONECT 3325 3321 3326 3336
CONECT 3326 3325 3327 3333
CONECT 3327 3326 3328 3334
CONECT 3328 3327 3329 3335
CONECT 3329 3328 3330 3336
CONECT 3330 3329 3337
CONECT 3331 3332 3333 3338
CONECT 3332 3331
CONECT 3333 3326 3331
CONECT 3334 3327
CONECT 3335 3328
CONECT 3336 3325 3329
CONECT 3337 3330
CONECT 3338 3331
CONECT 3339 298 3340 3350
CONECT 3340 3339 3341 3347
CONECT 3341 3340 3342 3348
CONECT 3342 3341 3343 3349
CONECT 3343 3342 3344 3350
CONECT 3344 3343 3351
CONECT 3345 3346 3347 3352
CONECT 3346 3345
CONECT 3347 3340 3345
CONECT 3348 3341
CONECT 3349 3342
CONECT 3350 3339 3343
CONECT 3351 3344
CONECT 3352 3345
CONECT 3353 3354 3367 3371
CONECT 3354 3353 3355 3368
CONECT 3355 3354 3356 3369
CONECT 3356 3355 3357 3370
CONECT 3357 3356 3358 3371
CONECT 3358 3357 3372
CONECT 3359 3360 3367
CONECT 3360 3359 3361
CONECT 3361 3360 3362
CONECT 3362 3361 3363
CONECT 3363 3362 3364
CONECT 3364 3363 3365
CONECT 3365 3364 3366
CONECT 3366 3365
CONECT 3367 3353 3359
CONECT 3368 3354
CONECT 3369 3355
CONECT 3370 3356
CONECT 3371 3353 3357
CONECT 3372 3358
CONECT 3373 3374 3387 3391
CONECT 3374 3373 3375 3388
CONECT 3375 3374 3376 3389
CONECT 3376 3375 3377 3390
CONECT 3377 3376 3378 3391
CONECT 3378 3377 3392
CONECT 3379 3380 3387
CONECT 3380 3379 3381
CONECT 3381 3380 3382
CONECT 3382 3381 3383
CONECT 3383 3382 3384
CONECT 3384 3383 3385
CONECT 3385 3384 3386
CONECT 3386 3385
CONECT 3387 3373 3379
CONECT 3388 3374
CONECT 3389 3375
CONECT 3390 3376
CONECT 3391 3373 3377
CONECT 3392 3378
CONECT 3393 3394 3407 3411
CONECT 3394 3393 3395 3408
CONECT 3395 3394 3396 3409
CONECT 3396 3395 3397 3410
CONECT 3397 3396 3398 3411
CONECT 3398 3397 3412
CONECT 3399 3400 3407
CONECT 3400 3399 3401
CONECT 3401 3400 3402
CONECT 3402 3401 3403
CONECT 3403 3402 3404
CONECT 3404 3403 3405
CONECT 3405 3404 3406
CONECT 3406 3405
CONECT 3407 3393 3399
CONECT 3408 3394
CONECT 3409 3395
CONECT 3410 3396
CONECT 3411 3393 3397
CONECT 3412 3398
MASTER 350 0 11 18 4 0 0 6 3410 2 191 34
END