HEADER TRANSFERASE 06-MAY-05 2BRK
TITLE CRYSTAL STRUCTURE OF HEPATITIS C VIRUS POLYMERASE IN COMPLEX WITH AN
TITLE 2 ALLOSTERIC INHIBITOR (COMPOUND 1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA-DIRECTED RNA POLYMERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NS5B CATALYTIC DOMAIN, RESIDUES 2420-2955;
COMPND 5 SYNONYM: HEPATITIS C VIRUS POLYMERASE, P68, NS5B;
COMPND 6 EC: 2.7.7.48;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_TAXID: 11103;
SOURCE 4 STRAIN: GENOTYPE 1B, STRAIN BK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: T7;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7.7;
SOURCE 10 OTHER_DETAILS: GENBANK ACCESSION NUMBER AB016785
KEYWDS TRANSFERASE, HEPATITIS C VIRUS, HCV, NS5B, POLYMERASE, RNA-DEPENDENT
KEYWDS 2 RNA- POLYMERASE, ALLOSTERIC INHIBITOR, ATP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DI MARCO,C.VOLPARI,A.CARFI
REVDAT 3 13-DEC-23 2BRK 1 LINK
REVDAT 2 24-FEB-09 2BRK 1 VERSN
REVDAT 1 14-JUN-05 2BRK 0
JRNL AUTH S.DI MARCO,C.VOLPARI,L.TOMEI,S.ALTAMURA,S.HARPER,F.NARJES,
JRNL AUTH 2 U.KOCH,M.ROWLEY,R.DE FRANCESCO,G.MIGLIACCIO,A.CARFI
JRNL TITL INTERDOMAIN COMMUNICATION IN HEPATITIS C VIRUS POLYMERASE
JRNL TITL 2 ABOLISHED BY SMALL-MOLECULE INHIBITORS BOUND TO A NOVEL
JRNL TITL 3 ALLOSTERIC SITE
JRNL REF J.BIOL.CHEM. V. 280 29765 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15955819
JRNL DOI 10.1074/JBC.M505423200
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 95.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 26513
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1405
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1896
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3968
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 445
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.12000
REMARK 3 B22 (A**2) : -2.51000
REMARK 3 B33 (A**2) : 1.39000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.309
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.235
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.151
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.127
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4091 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3717 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5548 ; 1.382 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8641 ; 1.136 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 509 ; 5.770 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 627 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4497 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 827 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 935 ; 0.217 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4502 ; 0.253 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2438 ; 0.107 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 300 ; 0.193 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 18 ; 0.450 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 68 ; 0.297 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.229 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2554 ; 0.721 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4123 ; 1.428 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1537 ; 2.183 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1425 ; 3.731 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2BRK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1290023923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 5
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9340
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28007
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CSJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 34.00100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.24400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.00100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.24400
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 22
REMARK 465 ILE A 23
REMARK 465 ASN A 24
REMARK 465 ALA A 25
REMARK 465 LEU A 26
REMARK 465 SER A 27
REMARK 465 ASN A 28
REMARK 465 SER A 29
REMARK 465 LEU A 30
REMARK 465 LEU A 31
REMARK 465 ARG A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 ASN A 35
REMARK 465 GLN A 148
REMARK 465 PRO A 149
REMARK 465 GLU A 150
REMARK 465 LYS A 151
REMARK 465 GLY A 152
REMARK 465 THR A 532
REMARK 465 LYS A 533
REMARK 465 LEU A 534
REMARK 465 LYS A 535
REMARK 465 LEU A 536
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 GLU A 18 CG CD OE1 OE2
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 LEU A 21 CG CD1 CD2
REMARK 470 HIS A 402 CG ND1 CD2 CE1 NE2
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 OD2 ASP A 177 O HOH A 2183 2.04
REMARK 500 O HOH A 2204 O HOH A 2208 2.13
REMARK 500 OE1 GLU A 236 O HOH A 2255 2.17
REMARK 500 O HOH A 2183 O HOH A 2187 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASN A 483 OD1 ASN A 483 2655 1.78
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 ASP A 319 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 387 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 MET A 414 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 MET A 414 CA - CB - CG ANGL. DEV. = -12.9 DEGREES
REMARK 500 ASP A 458 CB - CG - OD2 ANGL. DEV. = 6.1 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 LEU A 260 -51.64 -126.53
REMARK 500 SER A 347 3.60 110.92
REMARK 500 SER A 367 17.04 54.91
REMARK 500 ARG A 401 -120.46 -81.25
REMARK 500 HIS A 402 140.60 151.13
REMARK 500 ASN A 406 64.28 39.87
REMARK 500 PRO A 495 154.38 -46.74
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 A2027 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH A2032 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A2053 DISTANCE = 7.62 ANGSTROMS
REMARK 525 HOH A2102 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A2203 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH A2224 DISTANCE = 6.43 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1532 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 220 OD2
REMARK 620 2 THR A 221 O 86.2
REMARK 620 3 ASP A 318 OD2 96.5 90.5
REMARK 620 4 HOH A2442 O 95.5 98.4 165.5
REMARK 620 5 HOH A2443 O 147.8 95.0 115.6 52.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1533 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 220 OD1
REMARK 620 2 ASP A 318 OD1 97.0
REMARK 620 3 ASP A 319 OD1 93.2 97.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMF A1534
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A1Q RELATED DB: PDB
REMARK 900 HEPATITIS C VIRUS NS3 PROTEINASE
REMARK 900 RELATED ID: 1C2P RELATED DB: PDB
REMARK 900 HEPATITIS C VIRUS NS5B RIBONUCLEIC ACID- DEPENDENT RIBONUCLEIC ACID
REMARK 900 POLYMERASE
REMARK 900 RELATED ID: 1CSJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE RIBONUCLEIC ACID- DEPENDENT RIBONUCLEIC
REMARK 900 ACID POLYMERASE OF HEPATITIS C VIRUS
REMARK 900 RELATED ID: 1CU1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN ENZYME COMPLEX FROM HEPATITIS C VIRUS
REMARK 900 RELATED ID: 1GX5 RELATED DB: PDB
REMARK 900 HEPATITIS C VIRUS RNA POLYMERASE IN COMPLEX WITH GTP AND MANGANESE
REMARK 900 RELATED ID: 1GX6 RELATED DB: PDB
REMARK 900 HEPATITIS C VIRUS RNA POLYMERASE IN COMPLEX WITH UTP AND MANGANESE
REMARK 900 RELATED ID: 1JXP RELATED DB: PDB
REMARK 900 BK STRAIN HEPATITIS C VIRUS (HCV) NS3-NS4A
REMARK 900 RELATED ID: 1NS3 RELATED DB: PDB
REMARK 900 STRUCTURE OF HCV PROTEASE (BK STRAIN)
REMARK 900 RELATED ID: 1QUV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE RIBONUCLEIC ACID DIRECTED RIBONUCLEIC ACID
REMARK 900 POLYMERASE OF HEPATITIS C VIRUS
REMARK 900 RELATED ID: 2BRL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEPATITIS C VIRUS POLYMERASE IN COMPLEX WITH
REMARK 900 AN ALLOSTERIC INHIBITOR (COMPOUND 2)
REMARK 900 RELATED ID: 8OHM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEIC ACID HELICASE FROM GENOTYPE 1B
REMARK 900 HEPATITIS C VIRUS: MECHANISM OF UNWINDING DUPLEX RIBONUCLEIC ACID
DBREF 2BRK A 1 536 UNP P26663 POLG_HCVBK 2420 2955
SEQRES 1 A 536 SER MET SER TYR THR TRP THR GLY ALA LEU ILE THR PRO
SEQRES 2 A 536 CYS ALA ALA GLU GLU SER LYS LEU PRO ILE ASN ALA LEU
SEQRES 3 A 536 SER ASN SER LEU LEU ARG HIS HIS ASN MET VAL TYR ALA
SEQRES 4 A 536 THR THR SER ARG SER ALA GLY LEU ARG GLN LYS LYS VAL
SEQRES 5 A 536 THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS TYR ARG
SEQRES 6 A 536 ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER THR VAL
SEQRES 7 A 536 LYS ALA LYS LEU LEU SER VAL GLU GLU ALA CYS LYS LEU
SEQRES 8 A 536 THR PRO PRO HIS SER ALA LYS SER LYS PHE GLY TYR GLY
SEQRES 9 A 536 ALA LYS ASP VAL ARG ASN LEU SER SER LYS ALA VAL ASN
SEQRES 10 A 536 HIS ILE HIS SER VAL TRP LYS ASP LEU LEU GLU ASP THR
SEQRES 11 A 536 VAL THR PRO ILE ASP THR THR ILE MET ALA LYS ASN GLU
SEQRES 12 A 536 VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG LYS PRO
SEQRES 13 A 536 ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL ARG VAL
SEQRES 14 A 536 CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER THR LEU
SEQRES 15 A 536 PRO GLN VAL VAL MET GLY SER SER TYR GLY PHE GLN TYR
SEQRES 16 A 536 SER PRO GLY GLN ARG VAL GLU PHE LEU VAL ASN THR TRP
SEQRES 17 A 536 LYS SER LYS LYS ASN PRO MET GLY PHE SER TYR ASP THR
SEQRES 18 A 536 ARG CYS PHE ASP SER THR VAL THR GLU ASN ASP ILE ARG
SEQRES 19 A 536 VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU ALA PRO
SEQRES 20 A 536 GLU ALA ARG GLN ALA ILE LYS SER LEU THR GLU ARG LEU
SEQRES 21 A 536 TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY GLN ASN
SEQRES 22 A 536 CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL LEU THR
SEQRES 23 A 536 THR SER CYS GLY ASN THR LEU THR CYS TYR LEU LYS ALA
SEQRES 24 A 536 SER ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP CYS THR
SEQRES 25 A 536 MET LEU VAL ASN GLY ASP ASP LEU VAL VAL ILE CYS GLU
SEQRES 26 A 536 SER ALA GLY THR GLN GLU ASP ALA ALA SER LEU ARG VAL
SEQRES 27 A 536 PHE THR GLU ALA MET THR ARG TYR SER ALA PRO PRO GLY
SEQRES 28 A 536 ASP PRO PRO GLN PRO GLU TYR ASP LEU GLU LEU ILE THR
SEQRES 29 A 536 SER CYS SER SER ASN VAL SER VAL ALA HIS ASP ALA SER
SEQRES 30 A 536 GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO THR THR
SEQRES 31 A 536 PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG HIS THR
SEQRES 32 A 536 PRO VAL ASN SER TRP LEU GLY ASN ILE ILE MET TYR ALA
SEQRES 33 A 536 PRO THR LEU TRP ALA ARG MET ILE LEU MET THR HIS PHE
SEQRES 34 A 536 PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLU LYS ALA
SEQRES 35 A 536 LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER ILE GLU
SEQRES 36 A 536 PRO LEU ASP LEU PRO GLN ILE ILE GLU ARG LEU HIS GLY
SEQRES 37 A 536 LEU SER ALA PHE SER LEU HIS SER TYR SER PRO GLY GLU
SEQRES 38 A 536 ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU GLY VAL
SEQRES 39 A 536 PRO PRO LEU ARG VAL TRP ARG HIS ARG ALA ARG SER VAL
SEQRES 40 A 536 ARG ALA ARG LEU LEU SER GLN GLY GLY ARG ALA ALA THR
SEQRES 41 A 536 CYS GLY LYS TYR LEU PHE ASN TRP ALA VAL LYS THR LYS
SEQRES 42 A 536 LEU LYS LEU
HET MN A1532 1
HET MN A1533 1
HET CMF A1534 33
HETNAM MN MANGANESE (II) ION
HETNAM CMF 3-CYCLOHEXYL-1-(2-MORPHOLIN-4-YL-2-OXOETHYL)-2-PHENYL-
HETNAM 2 CMF 1H-INDOLE-6-CARBOXYLIC ACID
FORMUL 2 MN 2(MN 2+)
FORMUL 4 CMF C27 H30 N2 O4
FORMUL 5 HOH *445(H2 O)
HELIX 1 1 THR A 41 ARG A 43 5 3
HELIX 2 2 SER A 44 THR A 53 1 10
HELIX 3 3 ASP A 61 SER A 76 1 16
HELIX 4 4 SER A 84 LEU A 91 1 8
HELIX 5 5 GLY A 104 ASN A 110 1 7
HELIX 6 6 SER A 112 ASP A 129 1 18
HELIX 7 7 ASP A 164 SER A 180 1 17
HELIX 8 8 THR A 181 GLY A 188 1 8
HELIX 9 9 GLY A 192 TYR A 195 5 4
HELIX 10 10 SER A 196 SER A 210 1 15
HELIX 11 11 CYS A 223 VAL A 228 1 6
HELIX 12 12 THR A 229 GLN A 241 1 13
HELIX 13 13 ALA A 246 LEU A 260 1 15
HELIX 14 14 THR A 286 ALA A 306 1 21
HELIX 15 15 GLY A 328 TYR A 346 1 19
HELIX 16 16 ASP A 359 ILE A 363 5 5
HELIX 17 17 PRO A 388 ARG A 401 1 14
HELIX 18 18 ASN A 406 TYR A 415 1 10
HELIX 19 19 THR A 418 ILE A 424 1 7
HELIX 20 20 ILE A 424 GLN A 436 1 13
HELIX 21 21 GLU A 455 LEU A 457 5 3
HELIX 22 22 ASP A 458 GLY A 468 1 11
HELIX 23 23 LEU A 469 SER A 473 5 5
HELIX 24 24 SER A 478 GLY A 493 1 16
HELIX 25 25 PRO A 496 GLN A 514 1 19
HELIX 26 26 GLY A 515 PHE A 526 1 12
HELIX 27 27 ASN A 527 VAL A 530 5 4
SHEET 1 AA 5 TYR A 4 TRP A 6 0
SHEET 2 AA 5 ASN A 273 ARG A 277 -1 O TYR A 276 N THR A 5
SHEET 3 AA 5 GLY A 264 THR A 267 -1 O GLY A 264 N ARG A 277
SHEET 4 AA 5 THR A 136 ALA A 140 1 O THR A 136 N THR A 267
SHEET 5 AA 5 LEU A 159 PRO A 163 -1 O ILE A 160 N MET A 139
SHEET 1 AB 2 VAL A 37 ALA A 39 0
SHEET 2 AB 2 VAL A 144 CYS A 146 -1 O PHE A 145 N TYR A 38
SHEET 1 AC 3 PRO A 214 ASP A 220 0
SHEET 2 AC 3 ASP A 319 GLU A 325 -1 O LEU A 320 N TYR A 219
SHEET 3 AC 3 GLN A 309 ASN A 316 -1 O GLN A 309 N GLU A 325
SHEET 1 AD 2 SER A 368 HIS A 374 0
SHEET 2 AD 2 ARG A 380 ARG A 386 -1 O VAL A 381 N ALA A 373
SHEET 1 AE 2 LEU A 443 ILE A 447 0
SHEET 2 AE 2 ALA A 450 ILE A 454 -1 O ALA A 450 N ILE A 447
LINK OD2 ASP A 220 MN MN A1532 1555 1555 2.25
LINK OD1 ASP A 220 MN MN A1533 1555 1555 2.29
LINK O THR A 221 MN MN A1532 1555 1555 2.10
LINK OD2 ASP A 318 MN MN A1532 1555 1555 2.33
LINK OD1 ASP A 318 MN MN A1533 1555 1555 2.13
LINK OD1 ASP A 319 MN MN A1533 1555 1555 2.20
LINK MN MN A1532 O HOH A2442 1555 1555 2.67
LINK MN MN A1532 O HOH A2443 1555 1555 2.75
SITE 1 AC1 6 ASP A 220 THR A 221 ASP A 318 MN A1533
SITE 2 AC1 6 HOH A2442 HOH A2443
SITE 1 AC2 5 ASP A 220 ASP A 318 ASP A 319 MN A1532
SITE 2 AC2 5 HOH A2444
SITE 1 AC3 8 VAL A 37 LEU A 392 ALA A 396 HIS A 428
SITE 2 AC3 8 GLY A 493 PRO A 495 ARG A 503 HOH A2425
CRYST1 68.002 94.488 95.730 90.00 90.00 90.00 P 21 21 2 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014705 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010583 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010446 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
