HEADER TRANSFERASE/TRANSFERASE INHIBITOR 18-NOV-11 3UPH
TITLE SYNTHESIS OF NOVEL 4,5-DIHYDROFURANO INDOLES AND THEIR EVALUATION AS
TITLE 2 HCV NS5B POLYMERASE INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA-DIRECTED RNA POLYMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 2420-2989;
COMPND 5 SYNONYM: 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_COMMON: HCV;
SOURCE 4 ORGANISM_TAXID: 420174;
SOURCE 5 STRAIN: HC-J4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.VELAZQUEZ,S.VENKATARAMAN,C.A.LESBURG,J.S.DUCA,S.B.ROSENBLUM,
AUTHOR 2 J.A.KOZLOWSKI,F.G.NJOROGE
REVDAT 2 01-FEB-12 3UPH 1 JRNL
REVDAT 1 25-JAN-12 3UPH 0
JRNL AUTH F.VELAZQUEZ,S.VENKATRAMAN,C.A.LESBURG,J.DUCA,S.B.ROSENBLUM,
JRNL AUTH 2 J.A.KOZLOWSKI,F.G.NJOROGE
JRNL TITL SYNTHESIS OF NEW 4,5-DIHYDROFURANOINDOLES AND THEIR
JRNL TITL 2 EVALUATION AS HCV NS5B POLYMERASE INHIBITORS.
JRNL REF ORG.LETT. V. 14 556 2012
JRNL REFN ISSN 1523-7060
JRNL PMID 22220815
JRNL DOI 10.1021/OL203177G
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.4
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.4
REMARK 3 NUMBER OF REFLECTIONS : 75551
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) : 0.185
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 3755
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.05
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.38
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3918
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2024
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3727
REMARK 3 BIN R VALUE (WORKING SET) : 0.2012
REMARK 3 BIN FREE R VALUE : 0.2239
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.87
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 191
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8735
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 1012
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.50670
REMARK 3 B22 (A**2) : -1.73670
REMARK 3 B33 (A**2) : 7.24340
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) : 0.22
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.22
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.18
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.20
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.17
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 : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9033 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 12274 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3102 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 196 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1433 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9033 ; 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 : 1198 ; 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 : 11463 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.14
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.87
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3UPH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-11.
REMARK 100 THE RCSB ID CODE IS RCSB069046.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76031
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: BUSTER 2.9.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11.6% W/V PEG3350, 0.1 M SODIUM
REMARK 280 CITRATE, PH 5.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K
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 44.98500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.14850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.16400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.14850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.98500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.16400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 PRO A 149
REMARK 465 GLU A 150
REMARK 465 LYS A 151
REMARK 465 GLY A 152
REMARK 465 GLY A 153
REMARK 465 PRO A 569
REMARK 465 ARG A 570
REMARK 465 GLU A 571
REMARK 465 ASN A 572
REMARK 465 LEU A 573
REMARK 465 TYR A 574
REMARK 465 PHE A 575
REMARK 465 GLN A 576
REMARK 465 PRO B 149
REMARK 465 GLU B 150
REMARK 465 LYS B 151
REMARK 465 GLY B 152
REMARK 465 GLY B 153
REMARK 465 LEU B 564
REMARK 465 SER B 565
REMARK 465 ARG B 566
REMARK 465 ALA B 567
REMARK 465 ARG B 568
REMARK 465 PRO B 569
REMARK 465 ARG B 570
REMARK 465 GLU B 571
REMARK 465 ASN B 572
REMARK 465 LEU B 573
REMARK 465 TYR B 574
REMARK 465 PHE B 575
REMARK 465 GLN B 576
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 -56.96 -128.88
REMARK 500 SER A 347 55.18 71.44
REMARK 500 ALA A 348 56.53 -148.62
REMARK 500 ILE A 424 -63.40 -105.26
REMARK 500 SER B 27 -12.83 83.85
REMARK 500 GLU B 131 -32.13 -133.71
REMARK 500 LEU B 260 -56.18 -127.96
REMARK 500 ALA B 348 59.69 -148.18
REMARK 500 ILE B 424 -64.82 -91.80
REMARK 500 ALA B 541 9.17 -67.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU B 131 25.0 L L OUTSIDE RANGE
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 A 648 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A 682 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH A 714 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 758 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A 806 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A 931 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH A 971 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 972 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH B 613 DISTANCE = 11.63 ANGSTROMS
REMARK 525 HOH B 656 DISTANCE = 5.41 ANGSTROMS
REMARK 525 HOH B 748 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH B 829 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH B 866 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B 914 DISTANCE = 9.74 ANGSTROMS
REMARK 525 HOH B 947 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH B 974 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH B 979 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH B 983 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B1008 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH B1042 DISTANCE = 6.55 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 577
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0C1 A 578
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0C1 B 577
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UPI RELATED DB: PDB
DBREF 3UPH A 1 570 UNP O92972 POLG_HCVJ4 2420 2989
DBREF 3UPH B 1 570 UNP O92972 POLG_HCVJ4 2420 2989
SEQADV 3UPH GLY A 440 UNP O92972 GLU 2859 CONFLICT
SEQADV 3UPH ILE A 520 UNP O92972 THR 2939 CONFLICT
SEQADV 3UPH GLU A 571 UNP O92972 EXPRESSION TAG
SEQADV 3UPH ASN A 572 UNP O92972 EXPRESSION TAG
SEQADV 3UPH LEU A 573 UNP O92972 EXPRESSION TAG
SEQADV 3UPH TYR A 574 UNP O92972 EXPRESSION TAG
SEQADV 3UPH PHE A 575 UNP O92972 EXPRESSION TAG
SEQADV 3UPH GLN A 576 UNP O92972 EXPRESSION TAG
SEQADV 3UPH GLY B 440 UNP O92972 GLU 2859 CONFLICT
SEQADV 3UPH ILE B 520 UNP O92972 THR 2939 CONFLICT
SEQADV 3UPH GLU B 571 UNP O92972 EXPRESSION TAG
SEQADV 3UPH ASN B 572 UNP O92972 EXPRESSION TAG
SEQADV 3UPH LEU B 573 UNP O92972 EXPRESSION TAG
SEQADV 3UPH TYR B 574 UNP O92972 EXPRESSION TAG
SEQADV 3UPH PHE B 575 UNP O92972 EXPRESSION TAG
SEQADV 3UPH GLN B 576 UNP O92972 EXPRESSION TAG
SEQRES 1 A 576 SER MET SER TYR THR TRP THR GLY ALA LEU ILE THR PRO
SEQRES 2 A 576 CYS ALA ALA GLU GLU SER LYS LEU PRO ILE ASN PRO LEU
SEQRES 3 A 576 SER ASN SER LEU LEU ARG HIS HIS ASN MET VAL TYR ALA
SEQRES 4 A 576 THR THR SER ARG SER ALA SER LEU ARG GLN LYS LYS VAL
SEQRES 5 A 576 THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS TYR ARG
SEQRES 6 A 576 ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER THR VAL
SEQRES 7 A 576 LYS ALA LYS LEU LEU SER ILE GLU GLU ALA CYS LYS LEU
SEQRES 8 A 576 THR PRO PRO HIS SER ALA LYS SER LYS PHE GLY TYR GLY
SEQRES 9 A 576 ALA LYS ASP VAL ARG ASN LEU SER SER ARG ALA VAL ASN
SEQRES 10 A 576 HIS ILE ARG SER VAL TRP GLU ASP LEU LEU GLU ASP THR
SEQRES 11 A 576 GLU THR PRO ILE ASP THR THR ILE MET ALA LYS SER GLU
SEQRES 12 A 576 VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG LYS PRO
SEQRES 13 A 576 ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL ARG VAL
SEQRES 14 A 576 CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER THR LEU
SEQRES 15 A 576 PRO GLN ALA VAL MET GLY SER SER TYR GLY PHE GLN TYR
SEQRES 16 A 576 SER PRO LYS GLN ARG VAL GLU PHE LEU VAL ASN THR TRP
SEQRES 17 A 576 LYS SER LYS LYS CYS PRO MET GLY PHE SER TYR ASP THR
SEQRES 18 A 576 ARG CYS PHE ASP SER THR VAL THR GLU SER ASP ILE ARG
SEQRES 19 A 576 VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU ALA PRO
SEQRES 20 A 576 GLU ALA ARG GLN ALA ILE ARG SER LEU THR GLU ARG LEU
SEQRES 21 A 576 TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY GLN ASN
SEQRES 22 A 576 CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL LEU THR
SEQRES 23 A 576 THR SER CYS GLY ASN THR LEU THR CYS TYR LEU LYS ALA
SEQRES 24 A 576 THR ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP CYS THR
SEQRES 25 A 576 MET LEU VAL ASN GLY ASP ASP LEU VAL VAL ILE CYS GLU
SEQRES 26 A 576 SER ALA GLY THR GLN GLU ASP ALA ALA ALA LEU ARG ALA
SEQRES 27 A 576 PHE THR GLU ALA MET THR ARG TYR SER ALA PRO PRO GLY
SEQRES 28 A 576 ASP PRO PRO GLN PRO GLU TYR ASP LEU GLU LEU ILE THR
SEQRES 29 A 576 SER CYS SER SER ASN VAL SER VAL ALA HIS ASP ALA SER
SEQRES 30 A 576 GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO THR THR
SEQRES 31 A 576 PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG HIS THR
SEQRES 32 A 576 PRO ILE ASN SER TRP LEU GLY ASN ILE ILE MET TYR ALA
SEQRES 33 A 576 PRO THR LEU TRP ALA ARG MET ILE LEU MET THR HIS PHE
SEQRES 34 A 576 PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLY LYS ALA
SEQRES 35 A 576 LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER ILE GLU
SEQRES 36 A 576 PRO LEU ASP LEU PRO GLN ILE ILE GLU ARG LEU HIS GLY
SEQRES 37 A 576 LEU SER ALA PHE THR LEU HIS SER TYR SER PRO GLY GLU
SEQRES 38 A 576 ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU GLY VAL
SEQRES 39 A 576 PRO PRO LEU ARG THR TRP ARG HIS ARG ALA ARG SER VAL
SEQRES 40 A 576 ARG ALA LYS LEU LEU SER GLN GLY GLY ARG ALA ALA ILE
SEQRES 41 A 576 CYS GLY ARG TYR LEU PHE ASN TRP ALA VAL ARG THR LYS
SEQRES 42 A 576 LEU LYS LEU THR PRO ILE PRO ALA ALA SER GLN LEU ASP
SEQRES 43 A 576 LEU SER GLY TRP PHE VAL ALA GLY TYR SER GLY GLY ASP
SEQRES 44 A 576 ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG GLU ASN
SEQRES 45 A 576 LEU TYR PHE GLN
SEQRES 1 B 576 SER MET SER TYR THR TRP THR GLY ALA LEU ILE THR PRO
SEQRES 2 B 576 CYS ALA ALA GLU GLU SER LYS LEU PRO ILE ASN PRO LEU
SEQRES 3 B 576 SER ASN SER LEU LEU ARG HIS HIS ASN MET VAL TYR ALA
SEQRES 4 B 576 THR THR SER ARG SER ALA SER LEU ARG GLN LYS LYS VAL
SEQRES 5 B 576 THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS TYR ARG
SEQRES 6 B 576 ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER THR VAL
SEQRES 7 B 576 LYS ALA LYS LEU LEU SER ILE GLU GLU ALA CYS LYS LEU
SEQRES 8 B 576 THR PRO PRO HIS SER ALA LYS SER LYS PHE GLY TYR GLY
SEQRES 9 B 576 ALA LYS ASP VAL ARG ASN LEU SER SER ARG ALA VAL ASN
SEQRES 10 B 576 HIS ILE ARG SER VAL TRP GLU ASP LEU LEU GLU ASP THR
SEQRES 11 B 576 GLU THR PRO ILE ASP THR THR ILE MET ALA LYS SER GLU
SEQRES 12 B 576 VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG LYS PRO
SEQRES 13 B 576 ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL ARG VAL
SEQRES 14 B 576 CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER THR LEU
SEQRES 15 B 576 PRO GLN ALA VAL MET GLY SER SER TYR GLY PHE GLN TYR
SEQRES 16 B 576 SER PRO LYS GLN ARG VAL GLU PHE LEU VAL ASN THR TRP
SEQRES 17 B 576 LYS SER LYS LYS CYS PRO MET GLY PHE SER TYR ASP THR
SEQRES 18 B 576 ARG CYS PHE ASP SER THR VAL THR GLU SER ASP ILE ARG
SEQRES 19 B 576 VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU ALA PRO
SEQRES 20 B 576 GLU ALA ARG GLN ALA ILE ARG SER LEU THR GLU ARG LEU
SEQRES 21 B 576 TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY GLN ASN
SEQRES 22 B 576 CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL LEU THR
SEQRES 23 B 576 THR SER CYS GLY ASN THR LEU THR CYS TYR LEU LYS ALA
SEQRES 24 B 576 THR ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP CYS THR
SEQRES 25 B 576 MET LEU VAL ASN GLY ASP ASP LEU VAL VAL ILE CYS GLU
SEQRES 26 B 576 SER ALA GLY THR GLN GLU ASP ALA ALA ALA LEU ARG ALA
SEQRES 27 B 576 PHE THR GLU ALA MET THR ARG TYR SER ALA PRO PRO GLY
SEQRES 28 B 576 ASP PRO PRO GLN PRO GLU TYR ASP LEU GLU LEU ILE THR
SEQRES 29 B 576 SER CYS SER SER ASN VAL SER VAL ALA HIS ASP ALA SER
SEQRES 30 B 576 GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO THR THR
SEQRES 31 B 576 PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG HIS THR
SEQRES 32 B 576 PRO ILE ASN SER TRP LEU GLY ASN ILE ILE MET TYR ALA
SEQRES 33 B 576 PRO THR LEU TRP ALA ARG MET ILE LEU MET THR HIS PHE
SEQRES 34 B 576 PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLY LYS ALA
SEQRES 35 B 576 LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER ILE GLU
SEQRES 36 B 576 PRO LEU ASP LEU PRO GLN ILE ILE GLU ARG LEU HIS GLY
SEQRES 37 B 576 LEU SER ALA PHE THR LEU HIS SER TYR SER PRO GLY GLU
SEQRES 38 B 576 ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU GLY VAL
SEQRES 39 B 576 PRO PRO LEU ARG THR TRP ARG HIS ARG ALA ARG SER VAL
SEQRES 40 B 576 ARG ALA LYS LEU LEU SER GLN GLY GLY ARG ALA ALA ILE
SEQRES 41 B 576 CYS GLY ARG TYR LEU PHE ASN TRP ALA VAL ARG THR LYS
SEQRES 42 B 576 LEU LYS LEU THR PRO ILE PRO ALA ALA SER GLN LEU ASP
SEQRES 43 B 576 LEU SER GLY TRP PHE VAL ALA GLY TYR SER GLY GLY ASP
SEQRES 44 B 576 ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG GLU ASN
SEQRES 45 B 576 LEU TYR PHE GLN
HET PO4 A 577 5
HET 0C1 A 578 35
HET 0C1 B 577 35
HETNAM PO4 PHOSPHATE ION
HETNAM 0C1 6-(2,5-DIFLUOROBENZYL)-N-(METHYLSULFONYL)-8-(2-OXO-1,2-
HETNAM 2 0C1 DIHYDROPYRIDIN-3-YL)-3,6-DIHYDRO-2H-FURO[2,3-E]INDOLE-
HETNAM 3 0C1 7-CARBOXAMIDE
FORMUL 3 PO4 O4 P 3-
FORMUL 4 0C1 2(C24 H19 F2 N3 O5 S)
FORMUL 6 HOH *1012(H2 O)
HELIX 1 1 ASN A 24 SER A 29 1 6
HELIX 2 2 HIS A 33 ASN A 35 5 3
HELIX 3 3 THR A 41 ARG A 43 5 3
HELIX 4 4 SER A 44 THR A 53 1 10
HELIX 5 5 ASP A 61 SER A 76 1 16
HELIX 6 6 SER A 84 LYS A 90 1 7
HELIX 7 7 GLY A 104 ASN A 110 1 7
HELIX 8 8 SER A 112 ASP A 129 1 18
HELIX 9 9 ASP A 164 GLY A 188 1 25
HELIX 10 10 SER A 189 TYR A 195 5 7
HELIX 11 11 SER A 196 SER A 210 1 15
HELIX 12 12 CYS A 223 VAL A 228 1 6
HELIX 13 13 THR A 229 GLN A 241 1 13
HELIX 14 14 ALA A 246 LEU A 260 1 15
HELIX 15 15 THR A 286 LYS A 307 1 22
HELIX 16 16 GLY A 328 TYR A 346 1 19
HELIX 17 17 ASP A 359 ILE A 363 5 5
HELIX 18 18 PRO A 388 ARG A 401 1 14
HELIX 19 19 ASN A 406 TYR A 415 1 10
HELIX 20 20 THR A 418 ILE A 424 1 7
HELIX 21 21 ILE A 424 GLN A 436 1 13
HELIX 22 22 GLU A 455 LEU A 457 5 3
HELIX 23 23 ASP A 458 GLY A 468 1 11
HELIX 24 24 LEU A 469 THR A 473 5 5
HELIX 25 25 SER A 478 GLY A 493 1 16
HELIX 26 26 PRO A 496 GLN A 514 1 19
HELIX 27 27 GLY A 515 PHE A 526 1 12
HELIX 28 28 ASN A 527 VAL A 530 5 4
HELIX 29 29 ILE A 539 LEU A 545 1 7
HELIX 30 30 HIS B 33 ASN B 35 5 3
HELIX 31 31 THR B 41 ARG B 43 5 3
HELIX 32 32 SER B 44 THR B 53 1 10
HELIX 33 33 ASP B 61 SER B 76 1 16
HELIX 34 34 SER B 84 LEU B 91 1 8
HELIX 35 35 GLY B 104 ASN B 110 1 7
HELIX 36 36 SER B 112 ASP B 129 1 18
HELIX 37 37 ASP B 164 GLY B 188 1 25
HELIX 38 38 SER B 189 TYR B 195 5 7
HELIX 39 39 SER B 196 SER B 210 1 15
HELIX 40 40 CYS B 223 VAL B 228 1 6
HELIX 41 41 THR B 229 GLN B 241 1 13
HELIX 42 42 ALA B 246 LEU B 260 1 15
HELIX 43 43 THR B 286 LYS B 307 1 22
HELIX 44 44 GLY B 328 TYR B 346 1 19
HELIX 45 45 ASP B 359 ILE B 363 5 5
HELIX 46 46 PRO B 388 ARG B 401 1 14
HELIX 47 47 ASN B 406 TYR B 415 1 10
HELIX 48 48 THR B 418 ILE B 424 1 7
HELIX 49 49 ILE B 424 GLU B 437 1 14
HELIX 50 50 GLU B 455 LEU B 457 5 3
HELIX 51 51 ASP B 458 GLY B 468 1 11
HELIX 52 52 LEU B 469 THR B 473 5 5
HELIX 53 53 SER B 478 GLY B 493 1 16
HELIX 54 54 ARG B 498 GLN B 514 1 17
HELIX 55 55 GLY B 515 PHE B 526 1 12
HELIX 56 56 PRO B 540 LEU B 545 1 6
HELIX 57 57 LEU B 547 VAL B 552 5 6
SHEET 1 A 5 TYR A 4 TRP A 6 0
SHEET 2 A 5 ASN A 273 ARG A 277 -1 O TYR A 276 N THR A 5
SHEET 3 A 5 GLY A 264 THR A 267 -1 N LEU A 266 O CYS A 274
SHEET 4 A 5 THR A 136 ALA A 140 1 N ILE A 138 O THR A 267
SHEET 5 A 5 LEU A 159 PHE A 162 -1 O ILE A 160 N MET A 139
SHEET 1 B 2 VAL A 37 ALA A 39 0
SHEET 2 B 2 VAL A 144 CYS A 146 -1 O PHE A 145 N TYR A 38
SHEET 1 C 3 PRO A 214 TYR A 219 0
SHEET 2 C 3 ASP A 319 GLU A 325 -1 O CYS A 324 N MET A 215
SHEET 3 C 3 GLN A 309 ASN A 316 -1 N GLN A 309 O GLU A 325
SHEET 1 D 2 ASN A 369 HIS A 374 0
SHEET 2 D 2 ARG A 380 THR A 385 -1 O TYR A 383 N SER A 371
SHEET 1 E 2 LEU A 443 ILE A 447 0
SHEET 2 E 2 ALA A 450 ILE A 454 -1 O ILE A 454 N LEU A 443
SHEET 1 F 5 TYR B 4 TRP B 6 0
SHEET 2 F 5 ASN B 273 ARG B 277 -1 O TYR B 276 N THR B 5
SHEET 3 F 5 GLY B 264 THR B 267 -1 N LEU B 266 O CYS B 274
SHEET 4 F 5 THR B 136 ALA B 140 1 N ILE B 138 O THR B 267
SHEET 5 F 5 LEU B 159 PHE B 162 -1 O ILE B 160 N MET B 139
SHEET 1 G 2 VAL B 37 ALA B 39 0
SHEET 2 G 2 VAL B 144 CYS B 146 -1 O PHE B 145 N TYR B 38
SHEET 1 H 3 PRO B 214 TYR B 219 0
SHEET 2 H 3 ASP B 319 GLU B 325 -1 O CYS B 324 N MET B 215
SHEET 3 H 3 GLN B 309 ASN B 316 -1 N THR B 312 O ILE B 323
SHEET 1 I 2 ASN B 369 HIS B 374 0
SHEET 2 I 2 ARG B 380 THR B 385 -1 O VAL B 381 N ALA B 373
SHEET 1 J 2 LEU B 443 ILE B 447 0
SHEET 2 J 2 ALA B 450 ILE B 454 -1 O ILE B 454 N LEU B 443
SSBOND 1 CYS A 303 CYS A 311 1555 1555 2.89
SSBOND 2 CYS B 303 CYS B 311 1555 1555 2.41
SITE 1 AC1 9 ARG A 505 VAL A 530 ARG A 531 THR A 532
SITE 2 AC1 9 HOH A 632 HOH A 670 HOH A 870 HOH A 999
SITE 3 AC1 9 HOH A1094
SITE 1 AC2 18 PHE A 193 ARG A 200 ASN A 316 CYS A 366
SITE 2 AC2 18 SER A 367 GLY A 410 ASN A 411 MET A 414
SITE 3 AC2 18 TYR A 415 GLN A 446 ILE A 447 TYR A 448
SITE 4 AC2 18 GLY A 449 SER A 556 HOH A 691 HOH A 751
SITE 5 AC2 18 HOH A 963 HOH A1099
SITE 1 AC3 15 PHE B 193 ASN B 316 CYS B 366 SER B 367
SITE 2 AC3 15 GLY B 410 ASN B 411 MET B 414 TYR B 415
SITE 3 AC3 15 GLN B 446 ILE B 447 TYR B 448 GLY B 449
SITE 4 AC3 15 SER B 556 HOH B 894 HOH B4001
CRYST1 89.970 106.328 134.297 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 0.011115 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009405 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007446 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
