HEADER HYDROLASE 03-DEC-15 5FPY
TITLE STRUCTURE OF HEPATITIS C VIRUS (HCV) FULL-LENGTH NS3 COMPLEX WITH
TITLE 2 SMALL-MOLECULE LIGAND 5-BROMO-1-METHYL-1H-INDOLE-2-CARBOXYLIC ACID
TITLE 3 (AT21457) IN AN ALTERNATE BINDING SITE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE NS3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HEPACIVIRIN, NS3P, P70;
COMPND 5 EC: 3.4.21.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS (ISOLATE BK);
SOURCE 3 ORGANISM_TAXID: 11105;
SOURCE 4 STRAIN: GENOTYPE 1B;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET17
KEYWDS HEPATITIS C VIRUS, HCV, NS3 COMPLEX, PROTEASE-HELICASE, HYDROLASE,
KEYWDS 2 PROTEIN-LIGAND COMPLEX, FRAGMENT SCREENING, ALTERNATE BINDING SITE,
KEYWDS 3 AT21457.
EXPDTA X-RAY DIFFRACTION
AUTHOR T.G.DAVIES,H.JHOTI,R.F.LUDLOW,H.K.SAINI,I.J.TICKLE,M.VERDONK
REVDAT 3 10-JAN-24 5FPY 1 REMARK SHEET
REVDAT 2 13-JAN-16 5FPY 1 JRNL
REVDAT 1 23-DEC-15 5FPY 0
JRNL AUTH R.F.LUDLOW,M.L.VERDONK,H.K.SAINI,I.J.TICKLE,H.JHOTI
JRNL TITL DETECTION OF SECONDARY BINDING SITES IN PROTEINS USING
JRNL TITL 2 FRAGMENT SCREENING.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 112 15910 2015
JRNL REFN ISSN 0027-8424
JRNL PMID 26655740
JRNL DOI 10.1073/PNAS.1518946112
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.YAO,P.REICHERT,S.S.TAREMI,W.W.PROSISE,P.C.WEBER
REMARK 1 TITL MOLECULAR VIEWS OF VIRAL POLYPROTEIN PROCESSING REVEALED BY
REMARK 1 TITL 2 THE CRYSTAL STRUCTURE OF THE HEPATITIS C VIRUS BIFUNCTIONAL
REMARK 1 TITL 3 PROTEASE-HELICASE.
REMARK 1 REF STRUCTURE V. 7 1353 1999
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 10574797
REMARK 1 DOI 10.1016/S0969-2126(00)80025-8
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.M.SAALAU-BETHELL,A.J.WOODHEAD,G.CHESSARI,M.G.CARR,J.COYLE,
REMARK 1 AUTH 2 B.GRAHAM,S.D.HISCOCK,C.W.MURRAY,P.PATHURI,S.J.RICH,
REMARK 1 AUTH 3 C.J.RICHARDSON,P.A.WILLIAMS,H.JHOTI
REMARK 1 TITL DISCOVERY OF AN ALLOSTERIC MECHANISM FOR THE REGULATION OF
REMARK 1 TITL 2 HCV NS3 PROTEIN FUNCTION.
REMARK 1 REF NAT.CHEM.BIOL. V. 8 920 2012
REMARK 1 REFN ISSN 1552-4450
REMARK 1 PMID 23023261
REMARK 1 DOI 10.1038/NCHEMBIO.1081
REMARK 2
REMARK 2 RESOLUTION. 2.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 46396
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2354
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.52
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.58
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.63
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3440
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2200
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3262
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.17
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 178
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9416
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 728
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 14.27620
REMARK 3 B22 (A**2) : -5.38510
REMARK 3 B33 (A**2) : -8.89110
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.260
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.820
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.293
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.558
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.288
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9674 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 13249 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3067 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 158 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1545 ; 16.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9674 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1345 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 11518 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.12
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.60
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.47
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|705 - A|631 }
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3196 15.1134 -31.6625
REMARK 3 T TENSOR
REMARK 3 T11: -0.1547 T22: -0.1549
REMARK 3 T33: -0.0246 T12: 0.0066
REMARK 3 T13: 0.0514 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 1.2222 L22: 0.8246
REMARK 3 L33: 0.7811 L12: -0.1861
REMARK 3 L13: -0.4847 L23: -0.2044
REMARK 3 S TENSOR
REMARK 3 S11: 0.1353 S12: -0.0406 S13: 0.1828
REMARK 3 S21: -0.0095 S22: 0.0310 S23: -0.0191
REMARK 3 S31: -0.1075 S32: -0.0605 S33: -0.1662
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|705 - B|631 }
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3391 7.0493 -49.5155
REMARK 3 T TENSOR
REMARK 3 T11: -0.1759 T22: -0.1009
REMARK 3 T33: -0.0110 T12: -0.0386
REMARK 3 T13: 0.0523 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.9711 L22: 0.4312
REMARK 3 L33: 1.1171 L12: 0.0191
REMARK 3 L13: -0.2496 L23: 0.0854
REMARK 3 S TENSOR
REMARK 3 S11: -0.0271 S12: -0.0554 S13: -0.0066
REMARK 3 S21: 0.0224 S22: 0.0327 S23: -0.0711
REMARK 3 S31: -0.0633 S32: 0.2050 S33: -0.0055
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY DISORDERED REGIONS
REMARK 3 WERE DELETED. THERE'S ALSO A HINT OF THE LIGAND PARALLEL-
REMARK 3 STACKING WITH TRP A501 BUT DENSITY IS NOT SUFFICIENTLY GOOD TO
REMARK 3 BE CERTAIN.
REMARK 4
REMARK 4 5FPY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1290065686.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0723
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52097
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.520
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.53000
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: CSEARCH
REMARK 200 STARTING MODEL: PDB ENTRY 5FPS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MES/NAOH, 14% W/V PEG 6000, 10%
REMARK 280 V/V MPD. PROTEIN CONC. = 6 MG/ML., PH 6.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 45.45100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.00200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.88650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.00200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.45100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.88650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 684
REMARK 465 GLY A 685
REMARK 465 SER A 686
REMARK 465 SER A 687
REMARK 465 HIS A 688
REMARK 465 HIS A 689
REMARK 465 HIS A 690
REMARK 465 HIS A 691
REMARK 465 HIS A 692
REMARK 465 HIS A 693
REMARK 465 SER A 694
REMARK 465 SER A 695
REMARK 465 GLY A 696
REMARK 465 LEU A 697
REMARK 465 VAL A 698
REMARK 465 PRO A 699
REMARK 465 ARG A 700
REMARK 465 GLY A 701
REMARK 465 SER A 702
REMARK 465 HIS A 703
REMARK 465 MET A 704
REMARK 465 MET B 684
REMARK 465 GLY B 685
REMARK 465 SER B 686
REMARK 465 SER B 687
REMARK 465 HIS B 688
REMARK 465 HIS B 689
REMARK 465 HIS B 690
REMARK 465 HIS B 691
REMARK 465 HIS B 692
REMARK 465 HIS B 693
REMARK 465 SER B 694
REMARK 465 SER B 695
REMARK 465 GLY B 696
REMARK 465 LEU B 697
REMARK 465 VAL B 698
REMARK 465 PRO B 699
REMARK 465 ARG B 700
REMARK 465 GLY B 701
REMARK 465 SER B 702
REMARK 465 HIS B 703
REMARK 465 MET B 704
REMARK 465 GLY B 717
REMARK 465 SER B 718
REMARK 465 GLY B 719
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 18 CD1
REMARK 470 ARG A 24 CD NE CZ NH1 NH2
REMARK 470 LYS A 26 CD CE NZ
REMARK 470 LYS A 68 CD CE NZ
REMARK 470 ARG A 92 CD NE CZ NH1 NH2
REMARK 470 ARG A 117 NE CZ NH1 NH2
REMARK 470 LYS A 165 CD CE NZ
REMARK 470 GLU A 176 CG CD OE1 OE2
REMARK 470 ARG A 180 NH1 NH2
REMARK 470 LYS A 224 CD CE NZ
REMARK 470 ARG A 316 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 337 CG CD OE2
REMARK 470 GLU A 338 CG CD OE1 OE2
REMARK 470 SER A 342 OG
REMARK 470 LYS A 352 NZ
REMARK 470 ILE A 356 CG1 CG2 CD1
REMARK 470 GLU A 357 CG CD OE1 OE2
REMARK 470 ILE A 359 CD1
REMARK 470 ARG A 360 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 373 CG CD CE NZ
REMARK 470 GLU A 376 OE1 OE2
REMARK 470 LYS A 380 NZ
REMARK 470 SER A 382 OG
REMARK 470 LEU A 384 CD1 CD2
REMARK 470 LEU A 395 CD1 CD2
REMARK 470 VAL A 399 CG1 CG2
REMARK 470 ILE A 400 CG1 CG2 CD1
REMARK 470 ILE A 403 CG1 CG2 CD1
REMARK 470 GLY A 404 C O
REMARK 470 ASP A 421 CG OD1 OD2
REMARK 470 ARG A 464 NE CZ NH1 NH2
REMARK 470 ARG A 467 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 470 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 580 CD OE1 NE2
REMARK 470 GLU A 608 OE1 OE2
REMARK 470 SER B 720 OG
REMARK 470 ARG B 24 NE CZ NH1 NH2
REMARK 470 LYS B 26 NZ
REMARK 470 GLU B 30 OE1 OE2
REMARK 470 LYS B 68 CG CD CE NZ
REMARK 470 GLN B 80 OE1 NE2
REMARK 470 GLN B 86 CG CD OE1 NE2
REMARK 470 ARG B 92 NE CZ NH1 NH2
REMARK 470 ILE B 114 CD1
REMARK 470 LYS B 165 CD CE NZ
REMARK 470 VAL B 183 CG1 CG2
REMARK 470 PHE B 184 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER B 189 OG
REMARK 470 GLN B 195 CG CD OE1 NE2
REMARK 470 LYS B 213 NZ
REMARK 470 LYS B 224 CE NZ
REMARK 470 LYS B 244 CG CD CE NZ
REMARK 470 ARG B 316 CD NE CZ NH1 NH2
REMARK 470 ILE B 356 CG2 CD1
REMARK 470 GLU B 357 OE1 OE2
REMARK 470 ARG B 393 NE CZ NH1 NH2
REMARK 470 ARG B 469 CD NE CZ NH1 NH2
REMARK 470 GLU B 530 OE1 OE2
REMARK 470 ILE B 542 CG2
REMARK 470 GLN B 552 CD OE1 NE2
REMARK 470 LYS B 583 NZ
REMARK 470 ARG B 587 NE CZ NH1 NH2
REMARK 470 GLU B 608 OE1 OE2
REMARK 470 THR B 631 CG2
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 THR A 40 -53.81 -121.56
REMARK 500 ASN A 49 37.02 70.52
REMARK 500 LYS A 68 40.41 -98.82
REMARK 500 ARG A 119 41.46 -141.80
REMARK 500 PRO A 146 2.18 -62.64
REMARK 500 ASP A 186 -95.52 -70.48
REMARK 500 THR A 212 -65.28 -121.29
REMARK 500 ALA A 245 -89.54 -78.11
REMARK 500 HIS A 246 4.26 -61.63
REMARK 500 LYS A 352 -162.39 -120.71
REMARK 500 THR A 443 -95.91 -135.89
REMARK 500 CYS B 99 85.63 -62.34
REMARK 500 ARG B 119 -78.03 -123.73
REMARK 500 THR B 212 -68.53 -125.46
REMARK 500 SER B 342 -168.93 -110.13
REMARK 500 LEU B 384 3.52 -66.62
REMARK 500 THR B 443 -96.43 -130.48
REMARK 500 TRP B 578 48.27 -102.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2179 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH B2022 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH B2039 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH B2059 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH B2075 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH B2325 DISTANCE = 6.19 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 5-BROMO-1-METHYL-1H-INDOLE-2-CARBOXYLIC ACID (R2N): ASTEX
REMARK 600 COMPOUND REGISTRY AT21457.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R2N B 1721
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R2N A 1721
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FP5 RELATED DB: PDB
REMARK 900 STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 WITH SMALL- MOLECULE LIGAND
REMARK 900 4-FLUOROBENZOIC ACID (AT222) IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FP6 RELATED DB: PDB
REMARK 900 STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 WITH SMALL- MOLECULE LIGAND
REMARK 900 3-(4,7-DICHLORO-1H-INDOL-3-YL)PROP -2-YN-1-OL (AT17833) IN AN
REMARK 900 ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPD RELATED DB: PDB
REMARK 900 STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH SMALL-MOLECULE
REMARK 900 LIGAND PYRAZINE-2-CARBOXAMIDE (AT513) IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPE RELATED DB: PDB
REMARK 900 STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH SMALL-MOLECULE
REMARK 900 LIGAND 1H-1,2,4-TRIAZOL-3-AMINE ( AT485) IN AN ALTERNATE BINDING
REMARK 900 SITE.
REMARK 900 RELATED ID: 5FPM RELATED DB: PDB
REMARK 900 STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH SMALL-MOLECULE
REMARK 900 LIGAND 5-PHENYL-1,3,4-OXADIAZOLE-2- THIOL (AT809) IN AN ALTERNATE
REMARK 900 BINDING SITE.
REMARK 900 RELATED ID: 5FPN RELATED DB: PDB
REMARK 900 STRUCTURE OF HEAT SHOCK-RELATED 70KDA PROTEIN 2 WITH SMALL-MOLECULE
REMARK 900 LIGAND 3,5-DIMETHYL-1H-PYRAZOLE-4- CARBOXYLIC ACID (AT9084) IN AN
REMARK 900 ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPO RELATED DB: PDB
REMARK 900 STRUCTURE OF BACTERIAL DNA LIGASE WITH SMALL-MOLECULE LIGAND 1H-
REMARK 900 INDAZOL-7-AMINE (AT4213) IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPR RELATED DB: PDB
REMARK 900 STRUCTURE OF BACTERIAL DNA LIGASE WITH SMALL-MOLECULE LIGAND
REMARK 900 PYRIMIDIN-2-AMINE (AT371) IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPS RELATED DB: PDB
REMARK 900 STRUCTURE OF HEPATITIS C VIRUS (HCV) FULL-LENGTH NS3 COMPLEX WITH
REMARK 900 SMALL-MOLECULE LIGAND 3-AMINOBENZENE-1,2 -DICARBOXYLIC ACID (AT1246)
REMARK 900 IN AN ALTERNATE BINDING SITE.
REMARK 900 RELATED ID: 5FPT RELATED DB: PDB
REMARK 900 STRUCTURE OF HEPATITIS C VIRUS (HCV) FULL-LENGTH NS3 COMPLEX WITH
REMARK 900 SMALL-MOLECULE LIGAND 2-(1-METHYL-1H- INDOL-3-YL)ACETIC ACID
REMARK 900 (AT3437) IN AN ALTERNATE BINDING SITE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERM HIS TAG (37). DELETION 1-2. DELETION 632-686.
DBREF 5FPY A 3 631 UNP P26663 POLG_HCVBK 1029 1657
DBREF 5FPY B 3 631 UNP P26663 POLG_HCVBK 1029 1657
SEQADV 5FPY MET A 684 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY A 685 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER A 686 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER A 687 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS A 688 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS A 689 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS A 690 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS A 691 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS A 692 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS A 693 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER A 694 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER A 695 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY A 696 UNP P26663 EXPRESSION TAG
SEQADV 5FPY LEU A 697 UNP P26663 EXPRESSION TAG
SEQADV 5FPY VAL A 698 UNP P26663 EXPRESSION TAG
SEQADV 5FPY PRO A 699 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ARG A 700 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY A 701 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER A 702 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS A 703 UNP P26663 EXPRESSION TAG
SEQADV 5FPY MET A 704 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY A 705 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER A 706 UNP P26663 EXPRESSION TAG
SEQADV 5FPY VAL A 707 UNP P26663 EXPRESSION TAG
SEQADV 5FPY VAL A 708 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ILE A 709 UNP P26663 EXPRESSION TAG
SEQADV 5FPY VAL A 710 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY A 711 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ARG A 712 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ILE A 713 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ILE A 714 UNP P26663 EXPRESSION TAG
SEQADV 5FPY LEU A 715 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER A 716 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY A 717 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER A 718 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY A 719 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER A 720 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY A 66 UNP P26663 ALA 1092 CONFLICT
SEQADV 5FPY GLN A 86 UNP P26663 PRO 1112 CONFLICT
SEQADV 5FPY ALA A 87 UNP P26663 LYS 1113 CONFLICT
SEQADV 5FPY SER A 147 UNP P26663 PHE 1173 CONFLICT
SEQADV 5FPY MET B 684 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY B 685 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER B 686 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER B 687 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS B 688 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS B 689 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS B 690 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS B 691 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS B 692 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS B 693 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER B 694 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER B 695 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY B 696 UNP P26663 EXPRESSION TAG
SEQADV 5FPY LEU B 697 UNP P26663 EXPRESSION TAG
SEQADV 5FPY VAL B 698 UNP P26663 EXPRESSION TAG
SEQADV 5FPY PRO B 699 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ARG B 700 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY B 701 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER B 702 UNP P26663 EXPRESSION TAG
SEQADV 5FPY HIS B 703 UNP P26663 EXPRESSION TAG
SEQADV 5FPY MET B 704 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY B 705 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER B 706 UNP P26663 EXPRESSION TAG
SEQADV 5FPY VAL B 707 UNP P26663 EXPRESSION TAG
SEQADV 5FPY VAL B 708 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ILE B 709 UNP P26663 EXPRESSION TAG
SEQADV 5FPY VAL B 710 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY B 711 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ARG B 712 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ILE B 713 UNP P26663 EXPRESSION TAG
SEQADV 5FPY ILE B 714 UNP P26663 EXPRESSION TAG
SEQADV 5FPY LEU B 715 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER B 716 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY B 717 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER B 718 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY B 719 UNP P26663 EXPRESSION TAG
SEQADV 5FPY SER B 720 UNP P26663 EXPRESSION TAG
SEQADV 5FPY GLY B 66 UNP P26663 ALA 1092 CONFLICT
SEQADV 5FPY GLN B 86 UNP P26663 PRO 1112 CONFLICT
SEQADV 5FPY ALA B 87 UNP P26663 LYS 1113 CONFLICT
SEQADV 5FPY SER B 147 UNP P26663 PHE 1173 CONFLICT
SEQRES 1 A 666 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 666 LEU VAL PRO ARG GLY SER HIS MET GLY SER VAL VAL ILE
SEQRES 3 A 666 VAL GLY ARG ILE ILE LEU SER GLY SER GLY SER ILE THR
SEQRES 4 A 666 ALA TYR SER GLN GLN THR ARG GLY LEU LEU GLY CYS ILE
SEQRES 5 A 666 ILE THR SER LEU THR GLY ARG ASP LYS ASN GLN VAL GLU
SEQRES 6 A 666 GLY GLU VAL GLN VAL VAL SER THR ALA THR GLN SER PHE
SEQRES 7 A 666 LEU ALA THR CYS VAL ASN GLY VAL CYS TRP THR VAL TYR
SEQRES 8 A 666 HIS GLY ALA GLY SER LYS THR LEU ALA GLY PRO LYS GLY
SEQRES 9 A 666 PRO ILE THR GLN MET TYR THR ASN VAL ASP GLN ASP LEU
SEQRES 10 A 666 VAL GLY TRP GLN ALA PRO PRO GLY ALA ARG SER LEU THR
SEQRES 11 A 666 PRO CYS THR CYS GLY SER SER ASP LEU TYR LEU VAL THR
SEQRES 12 A 666 ARG HIS ALA ASP VAL ILE PRO VAL ARG ARG ARG GLY ASP
SEQRES 13 A 666 SER ARG GLY SER LEU LEU SER PRO ARG PRO VAL SER TYR
SEQRES 14 A 666 LEU LYS GLY SER SER GLY GLY PRO LEU LEU CYS PRO SER
SEQRES 15 A 666 GLY HIS ALA VAL GLY ILE PHE ARG ALA ALA VAL CYS THR
SEQRES 16 A 666 ARG GLY VAL ALA LYS ALA VAL ASP PHE VAL PRO VAL GLU
SEQRES 17 A 666 SER MET GLU THR THR MET ARG SER PRO VAL PHE THR ASP
SEQRES 18 A 666 ASN SER SER PRO PRO ALA VAL PRO GLN SER PHE GLN VAL
SEQRES 19 A 666 ALA HIS LEU HIS ALA PRO THR GLY SER GLY LYS SER THR
SEQRES 20 A 666 LYS VAL PRO ALA ALA TYR ALA ALA GLN GLY TYR LYS VAL
SEQRES 21 A 666 LEU VAL LEU ASN PRO SER VAL ALA ALA THR LEU GLY PHE
SEQRES 22 A 666 GLY ALA TYR MET SER LYS ALA HIS GLY ILE ASP PRO ASN
SEQRES 23 A 666 ILE ARG THR GLY VAL ARG THR ILE THR THR GLY ALA PRO
SEQRES 24 A 666 VAL THR TYR SER THR TYR GLY LYS PHE LEU ALA ASP GLY
SEQRES 25 A 666 GLY CYS SER GLY GLY ALA TYR ASP ILE ILE ILE CYS ASP
SEQRES 26 A 666 GLU CYS HIS SER THR ASP SER THR THR ILE LEU GLY ILE
SEQRES 27 A 666 GLY THR VAL LEU ASP GLN ALA GLU THR ALA GLY ALA ARG
SEQRES 28 A 666 LEU VAL VAL LEU ALA THR ALA THR PRO PRO GLY SER VAL
SEQRES 29 A 666 THR VAL PRO HIS PRO ASN ILE GLU GLU VAL ALA LEU SER
SEQRES 30 A 666 ASN THR GLY GLU ILE PRO PHE TYR GLY LYS ALA ILE PRO
SEQRES 31 A 666 ILE GLU ALA ILE ARG GLY GLY ARG HIS LEU ILE PHE CYS
SEQRES 32 A 666 HIS SER LYS LYS LYS CYS ASP GLU LEU ALA ALA LYS LEU
SEQRES 33 A 666 SER GLY LEU GLY ILE ASN ALA VAL ALA TYR TYR ARG GLY
SEQRES 34 A 666 LEU ASP VAL SER VAL ILE PRO THR ILE GLY ASP VAL VAL
SEQRES 35 A 666 VAL VAL ALA THR ASP ALA LEU MET THR GLY TYR THR GLY
SEQRES 36 A 666 ASP PHE ASP SER VAL ILE ASP CYS ASN THR CYS VAL THR
SEQRES 37 A 666 GLN THR VAL ASP PHE SER LEU ASP PRO THR PHE THR ILE
SEQRES 38 A 666 GLU THR THR THR VAL PRO GLN ASP ALA VAL SER ARG SER
SEQRES 39 A 666 GLN ARG ARG GLY ARG THR GLY ARG GLY ARG ARG GLY ILE
SEQRES 40 A 666 TYR ARG PHE VAL THR PRO GLY GLU ARG PRO SER GLY MET
SEQRES 41 A 666 PHE ASP SER SER VAL LEU CYS GLU CYS TYR ASP ALA GLY
SEQRES 42 A 666 CYS ALA TRP TYR GLU LEU THR PRO ALA GLU THR SER VAL
SEQRES 43 A 666 ARG LEU ARG ALA TYR LEU ASN THR PRO GLY LEU PRO VAL
SEQRES 44 A 666 CYS GLN ASP HIS LEU GLU PHE TRP GLU SER VAL PHE THR
SEQRES 45 A 666 GLY LEU THR HIS ILE ASP ALA HIS PHE LEU SER GLN THR
SEQRES 46 A 666 LYS GLN ALA GLY ASP ASN PHE PRO TYR LEU VAL ALA TYR
SEQRES 47 A 666 GLN ALA THR VAL CYS ALA ARG ALA GLN ALA PRO PRO PRO
SEQRES 48 A 666 SER TRP ASP GLN MET TRP LYS CYS LEU ILE ARG LEU LYS
SEQRES 49 A 666 PRO THR LEU HIS GLY PRO THR PRO LEU LEU TYR ARG LEU
SEQRES 50 A 666 GLY ALA VAL GLN ASN GLU VAL THR LEU THR HIS PRO ILE
SEQRES 51 A 666 THR LYS TYR ILE MET ALA CYS MET SER ALA ASP LEU GLU
SEQRES 52 A 666 VAL VAL THR
SEQRES 1 B 666 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 666 LEU VAL PRO ARG GLY SER HIS MET GLY SER VAL VAL ILE
SEQRES 3 B 666 VAL GLY ARG ILE ILE LEU SER GLY SER GLY SER ILE THR
SEQRES 4 B 666 ALA TYR SER GLN GLN THR ARG GLY LEU LEU GLY CYS ILE
SEQRES 5 B 666 ILE THR SER LEU THR GLY ARG ASP LYS ASN GLN VAL GLU
SEQRES 6 B 666 GLY GLU VAL GLN VAL VAL SER THR ALA THR GLN SER PHE
SEQRES 7 B 666 LEU ALA THR CYS VAL ASN GLY VAL CYS TRP THR VAL TYR
SEQRES 8 B 666 HIS GLY ALA GLY SER LYS THR LEU ALA GLY PRO LYS GLY
SEQRES 9 B 666 PRO ILE THR GLN MET TYR THR ASN VAL ASP GLN ASP LEU
SEQRES 10 B 666 VAL GLY TRP GLN ALA PRO PRO GLY ALA ARG SER LEU THR
SEQRES 11 B 666 PRO CYS THR CYS GLY SER SER ASP LEU TYR LEU VAL THR
SEQRES 12 B 666 ARG HIS ALA ASP VAL ILE PRO VAL ARG ARG ARG GLY ASP
SEQRES 13 B 666 SER ARG GLY SER LEU LEU SER PRO ARG PRO VAL SER TYR
SEQRES 14 B 666 LEU LYS GLY SER SER GLY GLY PRO LEU LEU CYS PRO SER
SEQRES 15 B 666 GLY HIS ALA VAL GLY ILE PHE ARG ALA ALA VAL CYS THR
SEQRES 16 B 666 ARG GLY VAL ALA LYS ALA VAL ASP PHE VAL PRO VAL GLU
SEQRES 17 B 666 SER MET GLU THR THR MET ARG SER PRO VAL PHE THR ASP
SEQRES 18 B 666 ASN SER SER PRO PRO ALA VAL PRO GLN SER PHE GLN VAL
SEQRES 19 B 666 ALA HIS LEU HIS ALA PRO THR GLY SER GLY LYS SER THR
SEQRES 20 B 666 LYS VAL PRO ALA ALA TYR ALA ALA GLN GLY TYR LYS VAL
SEQRES 21 B 666 LEU VAL LEU ASN PRO SER VAL ALA ALA THR LEU GLY PHE
SEQRES 22 B 666 GLY ALA TYR MET SER LYS ALA HIS GLY ILE ASP PRO ASN
SEQRES 23 B 666 ILE ARG THR GLY VAL ARG THR ILE THR THR GLY ALA PRO
SEQRES 24 B 666 VAL THR TYR SER THR TYR GLY LYS PHE LEU ALA ASP GLY
SEQRES 25 B 666 GLY CYS SER GLY GLY ALA TYR ASP ILE ILE ILE CYS ASP
SEQRES 26 B 666 GLU CYS HIS SER THR ASP SER THR THR ILE LEU GLY ILE
SEQRES 27 B 666 GLY THR VAL LEU ASP GLN ALA GLU THR ALA GLY ALA ARG
SEQRES 28 B 666 LEU VAL VAL LEU ALA THR ALA THR PRO PRO GLY SER VAL
SEQRES 29 B 666 THR VAL PRO HIS PRO ASN ILE GLU GLU VAL ALA LEU SER
SEQRES 30 B 666 ASN THR GLY GLU ILE PRO PHE TYR GLY LYS ALA ILE PRO
SEQRES 31 B 666 ILE GLU ALA ILE ARG GLY GLY ARG HIS LEU ILE PHE CYS
SEQRES 32 B 666 HIS SER LYS LYS LYS CYS ASP GLU LEU ALA ALA LYS LEU
SEQRES 33 B 666 SER GLY LEU GLY ILE ASN ALA VAL ALA TYR TYR ARG GLY
SEQRES 34 B 666 LEU ASP VAL SER VAL ILE PRO THR ILE GLY ASP VAL VAL
SEQRES 35 B 666 VAL VAL ALA THR ASP ALA LEU MET THR GLY TYR THR GLY
SEQRES 36 B 666 ASP PHE ASP SER VAL ILE ASP CYS ASN THR CYS VAL THR
SEQRES 37 B 666 GLN THR VAL ASP PHE SER LEU ASP PRO THR PHE THR ILE
SEQRES 38 B 666 GLU THR THR THR VAL PRO GLN ASP ALA VAL SER ARG SER
SEQRES 39 B 666 GLN ARG ARG GLY ARG THR GLY ARG GLY ARG ARG GLY ILE
SEQRES 40 B 666 TYR ARG PHE VAL THR PRO GLY GLU ARG PRO SER GLY MET
SEQRES 41 B 666 PHE ASP SER SER VAL LEU CYS GLU CYS TYR ASP ALA GLY
SEQRES 42 B 666 CYS ALA TRP TYR GLU LEU THR PRO ALA GLU THR SER VAL
SEQRES 43 B 666 ARG LEU ARG ALA TYR LEU ASN THR PRO GLY LEU PRO VAL
SEQRES 44 B 666 CYS GLN ASP HIS LEU GLU PHE TRP GLU SER VAL PHE THR
SEQRES 45 B 666 GLY LEU THR HIS ILE ASP ALA HIS PHE LEU SER GLN THR
SEQRES 46 B 666 LYS GLN ALA GLY ASP ASN PHE PRO TYR LEU VAL ALA TYR
SEQRES 47 B 666 GLN ALA THR VAL CYS ALA ARG ALA GLN ALA PRO PRO PRO
SEQRES 48 B 666 SER TRP ASP GLN MET TRP LYS CYS LEU ILE ARG LEU LYS
SEQRES 49 B 666 PRO THR LEU HIS GLY PRO THR PRO LEU LEU TYR ARG LEU
SEQRES 50 B 666 GLY ALA VAL GLN ASN GLU VAL THR LEU THR HIS PRO ILE
SEQRES 51 B 666 THR LYS TYR ILE MET ALA CYS MET SER ALA ASP LEU GLU
SEQRES 52 B 666 VAL VAL THR
HET R2N A1721 21
HET R2N B1721 21
HETNAM R2N 5-BROMO-1-METHYL-1H-INDOLE-2-CARBOXYLIC ACID
FORMUL 3 R2N 2(C10 H8 BR N O2)
FORMUL 5 HOH *728(H2 O)
HELIX 1 1 GLY A 12 GLY A 23 1 12
HELIX 2 2 VAL A 55 GLY A 60 1 6
HELIX 3 3 SER A 133 LYS A 136 5 4
HELIX 4 4 VAL A 172 SER A 181 1 10
HELIX 5 5 THR A 212 GLN A 221 1 10
HELIX 6 6 SER A 231 ALA A 245 1 15
HELIX 7 7 TYR A 270 ASP A 276 1 7
HELIX 8 8 ASP A 296 ALA A 310 1 15
HELIX 9 9 PRO A 355 GLY A 361 1 7
HELIX 10 10 SER A 370 LEU A 384 1 15
HELIX 11 11 ASP A 396 ILE A 400 5 5
HELIX 12 12 ALA A 413 TYR A 418 1 6
HELIX 13 13 ASP A 454 GLY A 463 1 10
HELIX 14 14 ASP A 487 TYR A 502 1 16
HELIX 15 15 THR A 505 THR A 519 1 15
HELIX 16 16 HIS A 528 GLY A 538 1 11
HELIX 17 17 ASP A 543 GLY A 554 1 12
HELIX 18 18 PHE A 557 ALA A 571 1 15
HELIX 19 19 ASP A 579 LEU A 592 5 14
HELIX 20 20 HIS A 613 MET A 623 1 11
HELIX 21 21 GLY B 12 GLY B 23 1 12
HELIX 22 22 VAL B 55 GLY B 60 1 6
HELIX 23 23 SER B 133 LYS B 136 5 4
HELIX 24 24 VAL B 172 SER B 181 1 10
HELIX 25 25 THR B 212 GLN B 221 1 10
HELIX 26 26 SER B 231 HIS B 246 1 16
HELIX 27 27 TYR B 270 ASP B 276 1 7
HELIX 28 28 ASP B 296 ALA B 310 1 15
HELIX 29 29 PRO B 355 ARG B 360 1 6
HELIX 30 30 SER B 370 LEU B 384 1 15
HELIX 31 31 ASP B 396 ILE B 400 5 5
HELIX 32 32 ALA B 413 TYR B 418 1 6
HELIX 33 33 ASP B 454 GLY B 463 1 10
HELIX 34 34 ASP B 487 TRP B 501 1 15
HELIX 35 35 THR B 505 ASN B 518 1 14
HELIX 36 36 HIS B 528 GLY B 538 1 11
HELIX 37 37 ASP B 543 ALA B 553 1 11
HELIX 38 38 PHE B 557 ALA B 571 1 15
HELIX 39 39 ASP B 579 LYS B 589 5 11
HELIX 40 40 HIS B 613 MET B 623 1 11
SHEET 1 AA 7 ALA A 5 GLN A 9 0
SHEET 2 AA 7 VAL A 708 LEU A 715 -1 O ARG A 712 N GLN A 8
SHEET 3 AA 7 VAL A 33 SER A 37 -1 O VAL A 33 N ILE A 713
SHEET 4 AA 7 SER A 42 VAL A 48 -1 O PHE A 43 N VAL A 36
SHEET 5 AA 7 VAL A 51 THR A 54 -1 O VAL A 51 N VAL A 48
SHEET 6 AA 7 LEU A 82 GLN A 86 -1 O VAL A 83 N THR A 54
SHEET 7 AA 7 TYR A 75 ASN A 77 -1 O TYR A 75 N GLY A 84
SHEET 1 AB 2 LEU A 64 GLY A 66 0
SHEET 2 AB 2 GLY A 69 ILE A 71 -1 O GLY A 69 N GLY A 66
SHEET 1 AC 7 ASP A 103 VAL A 107 0
SHEET 2 AC 7 VAL A 113 ARG A 118 -1 O ILE A 114 N LEU A 106
SHEET 3 AC 7 ARG A 123 PRO A 131 -1 O SER A 125 N ARG A 117
SHEET 4 AC 7 VAL A 163 PRO A 171 -1 O ALA A 164 N ARG A 130
SHEET 5 AC 7 ALA A 150 THR A 160 1 O ILE A 153 N VAL A 170
SHEET 6 AC 7 PRO A 142 LEU A 144 -1 O LEU A 143 N VAL A 151
SHEET 7 AC 7 ASP A 103 VAL A 107 0
SHEET 1 AD 7 GLN A 198 HIS A 203 0
SHEET 2 AD 7 LEU A 317 THR A 322 1 O VAL A 318 N ALA A 200
SHEET 3 AD 7 ILE A 286 ASP A 290 1 O ILE A 287 N VAL A 319
SHEET 4 AD 7 VAL A 225 ASN A 229 1 O LEU A 226 N ILE A 288
SHEET 5 AD 7 VAL A 265 THR A 269 1 O THR A 266 N VAL A 227
SHEET 6 AD 7 ASN A 251 ARG A 253 1 O ASN A 251 N TYR A 267
SHEET 7 AD 7 THR A 258 ILE A 259 -1 O ILE A 259 N ILE A 252
SHEET 1 AE 6 ILE A 336 ALA A 340 0
SHEET 2 AE 6 GLY A 471 PHE A 475 1 O GLY A 471 N GLU A 337
SHEET 3 AE 6 SER A 424 ASP A 427 1 O VAL A 425 N ARG A 474
SHEET 4 AE 6 ARG A 363 PHE A 367 1 O LEU A 365 N ILE A 426
SHEET 5 AE 6 VAL A 406 ALA A 410 1 O VAL A 406 N HIS A 364
SHEET 6 AE 6 ALA A 388 TYR A 391 1 O VAL A 389 N VAL A 409
SHEET 1 AF 2 ILE A 347 PHE A 349 0
SHEET 2 AF 2 LYS A 352 ILE A 354 -1 O LYS A 352 N PHE A 349
SHEET 1 AG 2 THR A 430 ASP A 437 0
SHEET 2 AG 2 THR A 445 PRO A 452 -1 O THR A 445 N ASP A 437
SHEET 1 AH 2 THR A 596 PRO A 597 0
SHEET 2 AH 2 VAL A 609 THR A 610 1 N THR A 610 O THR A 596
SHEET 1 BA 7 ALA B 5 GLN B 9 0
SHEET 2 BA 7 VAL B 708 LEU B 715 -1 O ARG B 712 N GLN B 8
SHEET 3 BA 7 VAL B 33 SER B 37 -1 O VAL B 33 N ILE B 713
SHEET 4 BA 7 SER B 42 VAL B 48 -1 O PHE B 43 N VAL B 36
SHEET 5 BA 7 VAL B 51 THR B 54 -1 O VAL B 51 N VAL B 48
SHEET 6 BA 7 LEU B 82 GLN B 86 -1 O VAL B 83 N THR B 54
SHEET 7 BA 7 TYR B 75 ASN B 77 -1 O TYR B 75 N GLY B 84
SHEET 1 BB 2 LEU B 64 GLY B 66 0
SHEET 2 BB 2 GLY B 69 ILE B 71 -1 O GLY B 69 N GLY B 66
SHEET 1 BC 7 ASP B 103 VAL B 107 0
SHEET 2 BC 7 VAL B 113 ARG B 118 -1 O ILE B 114 N LEU B 106
SHEET 3 BC 7 ARG B 123 PRO B 131 -1 O SER B 125 N ARG B 117
SHEET 4 BC 7 VAL B 163 PRO B 171 -1 O ALA B 164 N ARG B 130
SHEET 5 BC 7 ALA B 150 THR B 160 1 O ILE B 153 N VAL B 170
SHEET 6 BC 7 PRO B 142 LEU B 144 -1 O LEU B 143 N VAL B 151
SHEET 7 BC 7 ASP B 103 VAL B 107 0
SHEET 1 BD 7 GLN B 198 HIS B 203 0
SHEET 2 BD 7 LEU B 317 THR B 322 1 O VAL B 318 N ALA B 200
SHEET 3 BD 7 ILE B 286 ASP B 290 1 O ILE B 287 N VAL B 319
SHEET 4 BD 7 VAL B 225 ASN B 229 1 O LEU B 226 N ILE B 288
SHEET 5 BD 7 VAL B 265 THR B 269 1 O THR B 266 N VAL B 227
SHEET 6 BD 7 ASN B 251 ARG B 253 1 O ASN B 251 N TYR B 267
SHEET 7 BD 7 THR B 258 ILE B 259 -1 O ILE B 259 N ILE B 252
SHEET 1 BE 6 ILE B 336 ALA B 340 0
SHEET 2 BE 6 GLY B 471 PHE B 475 1 O GLY B 471 N GLU B 337
SHEET 3 BE 6 SER B 424 ASP B 427 1 O VAL B 425 N ARG B 474
SHEET 4 BE 6 ARG B 363 PHE B 367 1 O LEU B 365 N ILE B 426
SHEET 5 BE 6 VAL B 406 ALA B 410 1 O VAL B 406 N HIS B 364
SHEET 6 BE 6 ALA B 388 TYR B 391 1 O VAL B 389 N VAL B 409
SHEET 1 BF 2 ILE B 347 PHE B 349 0
SHEET 2 BF 2 LYS B 352 ILE B 354 -1 O LYS B 352 N PHE B 349
SHEET 1 BG 2 THR B 430 ASP B 437 0
SHEET 2 BG 2 THR B 445 PRO B 452 -1 O THR B 445 N ASP B 437
SHEET 1 BH 2 THR B 596 PRO B 597 0
SHEET 2 BH 2 VAL B 609 THR B 610 1 N THR B 610 O THR B 596
CISPEP 1 ASP A 441 PRO A 442 0 5.15
CISPEP 2 ASP B 441 PRO B 442 0 5.98
SITE 1 AC1 4 SER B 370 LYS B 371 VAL B 432 HOH B2200
SITE 1 AC2 5 SER A 370 LYS A 371 VAL A 432 GLN A 434
SITE 2 AC2 5 HOH A2403
CRYST1 90.902 109.773 142.004 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011001 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009110 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007042 0.00000
MTRIX1 1 -0.913570 0.406320 -0.017050 40.61900 1
MTRIX2 1 0.406670 0.913030 -0.031540 -10.02500 1
MTRIX3 1 0.002750 -0.035750 -0.999360 -80.33100 1
(ATOM LINES ARE NOT SHOWN.)
END
