HEADER VIRAL PROTEIN 20-DEC-06 2OC0
TITLE STRUCTURE OF NS3 COMPLEXED WITH A KETOAMIDE INHIBITOR SCH491762
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATITIS C VIRUS;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEPATITIS C VIRUS;
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_TAXID: 11103;
SOURCE 4 GENE: NS3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BLR(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-3A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES
KEYWDS HEPATITIS C VIRUS, HCV, NS3 PROTEASE DOMAIN, KETOAMIDE INHIBITOR,
KEYWDS 2 VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.PRONGAY,Z.GUO,N.YAO,T.FISCHMANN,C.STRICKLAND,J.MYERS JR.,
AUTHOR 2 P.C.WEBER,B.MALCOLM,B.M.BEYER,R.INGRAM,J.PICHARDO,Z.HONG,
AUTHOR 3 W.W.PROSISE,L.RAMANATHAN,S.S.TAREMI,T.YAROSH-TOMAINE,R.ZHANG,
AUTHOR 4 M.SENIOR,R.YANG,A.ARASAPPAN,F.BENNETT,S.F.BOGEN,K.CHEN,E.JAO,Y.LIU,
AUTHOR 5 R.G.LOVE,A.K.SAKSENA,S.VENKATRAMAN,V.GIRIJAVALLABHAN,F.G.NJOROGE,
AUTHOR 6 V.MADISON
REVDAT 5 30-AUG-23 2OC0 1 REMARK SEQADV LINK
REVDAT 4 22-FEB-12 2OC0 1 AUTHOR REMARK
REVDAT 3 13-JUL-11 2OC0 1 VERSN
REVDAT 2 24-FEB-09 2OC0 1 VERSN
REVDAT 1 31-JUL-07 2OC0 0
JRNL AUTH A.J.PRONGAY,Z.GUO,N.YAO,J.PICHARDO,T.FISCHMANN,C.STRICKLAND,
JRNL AUTH 2 J.MYERS JR.,P.C.WEBER,B.M.BEYER,R.INGRAM,Z.HONG,W.W.PROSISE,
JRNL AUTH 3 L.RAMANATHAN,S.S.TAREMI,T.YAROSH-TOMAINE,R.ZHANG,M.SENIOR,
JRNL AUTH 4 R.S.YANG,B.MALCOLM,A.ARASAPPAN,F.BENNETT,S.L.BOGEN,K.CHEN,
JRNL AUTH 5 E.JAO,Y.T.LIU,R.G.LOVEY,A.K.SAKSENA,S.VENKATRAMAN,
JRNL AUTH 6 V.GIRIJAVALLABHAN,F.G.NJOROGE,V.MADISON
JRNL TITL DISCOVERY OF THE HCV NS3/4A PROTEASE INHIBITOR
JRNL TITL 2 (1R,5S)-N-[3-AMINO-1-(CYCLOBUTYLMETHYL)-2,3-DIOXOPROPYL]-3-
JRNL TITL 3 [2(S)-[[[(1,1-DIMETHYLETHYL)AMINO]CARBONYL]AMINO]-3,
JRNL TITL 4 3-DIMETHYL-1-OXOBUTYL]-
JRNL TITL 5 6,6-DIMETHYL-3-AZABICYCLO[3.1.0]HEXAN-2(S)-CARBOXAMIDE (SCH
JRNL TITL 6 503034) II. KEY STEPS IN STRUCTURE-BASED OPTIMIZATION.
JRNL REF J.MED.CHEM. V. 50 2310 2007
JRNL REFN ISSN 0022-2623
JRNL PMID 17444623
JRNL DOI 10.1021/JM060173K
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.L.KIM,K.A.MORGENSTERN,C.LIN,T.FOX,M.D.DWYER,J.A.LANDRO,
REMARK 1 AUTH 2 S.P.CHAMBERS,W.MARKLAND,C.A.LEPRE,E.T.O'MALLEY,S.L.HARBESON,
REMARK 1 AUTH 3 C.M.RICE,M.A.MURCKO,P.R.CARON,J.A.THOMSON
REMARK 1 TITL CRYSTAL STRUCTURE OF THE HEPATITIS C VIRUS NS3 PROTEASE
REMARK 1 TITL 2 DOMAIN COMPLEXED WITH A SYNTHETIC NS4A COFACTOR PEPTIDE.
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 87 343 1996
REMARK 1 REFN ISSN 0092-8674
REMARK 1 PMID 8861917
REMARK 1 DOI 10.1016/S0092-8674(00)81351-3
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.ARASAPPAN,F.G.NJOROGE,T.Y.CHAN,F.BENNETT,S.L.BOGEN,K.CHEN,
REMARK 1 AUTH 2 H.GU,L.HONG,E.JAO,Y.T.LIU,R.G.LOVEY,T.PAREKH,R.E.PIKE,
REMARK 1 AUTH 3 P.PINTO,B.SANTHANAM,S.VENKATRAMAN,H.VACCARO,H.WANG,X.YANG,
REMARK 1 AUTH 4 Z.ZHU,B.MCKITTRICK,A.K.SAKSENA,V.GIRIJAVALLABHAN,J.PICHARDO,
REMARK 1 AUTH 5 N.BUTKIEWICZ,R.INGRAM,B.MALCOLM,A.PRONGAY,N.YAO,B.MARTEN,
REMARK 1 AUTH 6 V.MADISON,S.KEMP,O.LEVY,M.LIM-WILBY,S.TAMURA,A.K.GANGULY
REMARK 1 TITL HEPATITIS C VIRUS NS3-4A SERINE PROTEASE INHIBITORS: SAR OF
REMARK 1 TITL 2 P'2 MOIETY WITH IMPROVED POTENCY.
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 15 4180 2005
REMARK 1 REFN ISSN 0960-894X
REMARK 1 PMID 16087332
REMARK 1 DOI 10.1016/J.BMCL.2005.06.091
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.X.CHEN,F.G.NJOROGE,A.PRONGAY,J.PICHARDO,V.MADISON,
REMARK 1 AUTH 2 V.GIRIJAVALLABHAN
REMARK 1 TITL SYNTHESIS AND BIOLOGICAL ACTIVITY OF MACROCYCLIC INHIBITORS
REMARK 1 TITL 2 OF HEPATITIS C VIRUS (HCV) NS3 PROTEASE.
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 15 4475 2005
REMARK 1 REFN ISSN 0960-894X
REMARK 1 PMID 16112859
REMARK 1 DOI 10.1016/J.BMCL.2005.07.033
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.BOGEN,A.K.SAKSENA,A.ARASAPPAN,H.GU,F.G.NJOROGE,
REMARK 1 AUTH 2 V.GIRIJAVALLABHAN,J.PICHARDO,N.BUTKIEWICZ,A.PRONGAY,
REMARK 1 AUTH 3 V.MADISON
REMARK 1 TITL HEPATITIS C VIRUS NS3-4A SERINE PROTEASE INHIBITORS: USE OF
REMARK 1 TITL 2 A P2-P1 CYCLOPROPYL ALANINE COMBINATION FOR IMPROVED
REMARK 1 TITL 3 POTENCY.
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 15 4515 2005
REMARK 1 REFN ISSN 0960-894X
REMARK 1 PMID 16112862
REMARK 1 DOI 10.1016/J.BMCL.2005.07.009
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.YI,X.TONG,A.SKELTON,R.CHASE,T.CHEN,A.PRONGAY,S.L.BOGEN,
REMARK 1 AUTH 2 A.K.SAKSENA,F.G.NJOROGE,R.L.VESELENAK,R.B.PYLES,N.BOURNE,
REMARK 1 AUTH 3 B.A.MALCOLM,S.M.LEMON
REMARK 1 TITL MUTATIONS CONFERRING RESISTANCE TO SCH6, A NOVEL HEPATITIS C
REMARK 1 TITL 2 VIRUS NS3/4A PROTEASE INHIBITOR. REDUCED RNA REPLICATION
REMARK 1 TITL 3 FITNESS AND PARTIAL RESCUE BY SECOND-SITE MUTATIONS.
REMARK 1 REF J.BIOL.CHEM. V. 281 8205 2006
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 16352601
REMARK 1 DOI 10.1074/JBC.M510246200
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 31235
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2895
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3111
REMARK 3 BIN FREE R VALUE : 0.3201
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 302
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 : 2724
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.90
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 1.930
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.479
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000040945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 5.6
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) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33806
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: 2O8M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN (NS3 COMPLEXED WITH KK
REMARK 280 -NS4A(21-39)-KK PEPTIDE) WAS AT 12-15 MG/ML IN 15 MM MES, PH 6.5
REMARK 280 1 M NACL 20 MM B -MERCAPTOETHANOL. HANGING DROPS WERE FORMED BY
REMARK 280 MIXING 4:L PROTEIN SOLUTION WITH 4:L {0.75-1.0 M NACL 0.1M NA/K
REMARK 280 PHOSPHATE 0.1 M MES, PH 5.8-6.1 20 MM B-MERCAPTOETHANOL} THE
REMARK 280 DROP WAS EQUILIBRATED THE DROPS OVER 1 ML {(1.25-1.50 M) NACL -
REMARK 280 0.1M NA/K PHOSPHATE 0.1 M MES, PH 5.6-5.8, 20 MM B-
REMARK 280 MERCAPTOETHANOL} , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 112.13200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 64.73944
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 25.15033
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 112.13200
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 64.73944
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 25.15033
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 112.13200
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 64.73944
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 25.15033
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 112.13200
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 64.73944
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 25.15033
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 112.13200
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 64.73944
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 25.15033
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 112.13200
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 64.73944
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 25.15033
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 129.47888
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 50.30067
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 129.47888
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 50.30067
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 129.47888
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 50.30067
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 129.47888
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 50.30067
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 129.47888
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 50.30067
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 129.47888
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 50.30067
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 -10
REMARK 465 ALA A -9
REMARK 465 SER A -8
REMARK 465 MET A -7
REMARK 465 THR A -6
REMARK 465 GLY A -5
REMARK 465 GLY A -4
REMARK 465 GLN A -3
REMARK 465 GLN A -2
REMARK 465 MET A -1
REMARK 465 GLY A 0
REMARK 465 GLY A 182
REMARK 465 SER A 183
REMARK 465 HIS A 184
REMARK 465 HIS A 185
REMARK 465 HIS A 186
REMARK 465 HIS A 187
REMARK 465 HIS A 188
REMARK 465 HIS A 189
REMARK 465 LYS B 19
REMARK 465 MET C -10
REMARK 465 ALA C -9
REMARK 465 SER C -8
REMARK 465 MET C -7
REMARK 465 THR C -6
REMARK 465 GLY C -5
REMARK 465 GLY C -4
REMARK 465 GLN C -3
REMARK 465 GLN C -2
REMARK 465 MET C -1
REMARK 465 GLY C 0
REMARK 465 ALA C 1
REMARK 465 PRO C 2
REMARK 465 ILE C 3
REMARK 465 THR C 4
REMARK 465 ALA C 5
REMARK 465 TYR C 6
REMARK 465 ALA C 7
REMARK 465 GLN C 8
REMARK 465 GLN C 9
REMARK 465 THR C 10
REMARK 465 ARG C 11
REMARK 465 GLY C 12
REMARK 465 LEU C 13
REMARK 465 LEU C 14
REMARK 465 GLY C 15
REMARK 465 CYS C 16
REMARK 465 ILE C 17
REMARK 465 ILE C 18
REMARK 465 THR C 19
REMARK 465 SER C 20
REMARK 465 LEU C 21
REMARK 465 THR C 22
REMARK 465 GLY C 23
REMARK 465 ARG C 24
REMARK 465 ASP C 25
REMARK 465 LYS C 26
REMARK 465 ASN C 27
REMARK 465 GLN C 28
REMARK 465 ARG C 180
REMARK 465 SER C 181
REMARK 465 GLY C 182
REMARK 465 SER C 183
REMARK 465 HIS C 184
REMARK 465 HIS C 185
REMARK 465 HIS C 186
REMARK 465 HIS C 187
REMARK 465 HIS C 188
REMARK 465 HIS C 189
REMARK 465 LYS D 19
REMARK 465 LYS D 20
REMARK 465 ILE D 37
REMARK 465 ILE D 38
REMARK 465 PRO D 39
REMARK 465 LYS D 40
REMARK 465 LYS D 41
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 PHE A 43 -156.83 -153.52
REMARK 500 ARG A 161 16.13 59.76
REMARK 500 THR C 38 -168.85 -103.45
REMARK 500 SER C 122 39.56 -148.69
REMARK 500
REMARK 500 REMARK: NULL
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 ZN A 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 97 SG
REMARK 620 2 CYS A 99 SG 101.0
REMARK 620 3 CYS A 145 SG 111.1 113.1
REMARK 620 4 HOH A1000 O 114.5 105.9 110.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 902 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 97 SG
REMARK 620 2 CYS C 99 SG 99.1
REMARK 620 3 CYS C 145 SG 100.7 113.6
REMARK 620 4 HOH C 915 O 109.6 109.5 121.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HU1 A 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A1R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HEPATITIS C VIRUS NS3 PROTEASE DOMAIN
REMARK 900 COMPLEXED WITH A SYNTHETIC NS4A COFACTOR PEPTIDE.
REMARK 900 RELATED ID: 2A4G RELATED DB: PDB
REMARK 900 HEPATITIS C VIRUS NS3-4A SERINE PROTEASE INHIBITORS. SAR OF P2'
REMARK 900 MOIETY WITH IMPROVED POTENCY.
REMARK 900 RELATED ID: 2A4Q RELATED DB: PDB
REMARK 900 SYNTHESIS AND BIOLOGICAL ACTIVITY OF MACROCYCLIC INHIBITORS OF
REMARK 900 HEPATITIS C VIRUS (HCV) NS3 PROTEASE
REMARK 900 RELATED ID: 2A4R RELATED DB: PDB
REMARK 900 HEPATITIS C VIRUS NS3-4A SERINE PROTEASE INHIBITORS: USE OF A P2-P1
REMARK 900 CYCLOPROPYL ALANINE COMBINATION FOR IMPROVED POTENCY.
REMARK 900 RELATED ID: 2FM2 RELATED DB: PDB
REMARK 900 MUTATIONS CONFERRING RESISTANCE TO SCH6, A NOVEL HEPATITIS C VIRUS
REMARK 900 NS3/4A PROTEASE INHIBITOR REDUCED RNA REPLICATION FITNESS AND
REMARK 900 PARTIAL RESCUE BY SECOND SITE MUTATIONS
REMARK 900 RELATED ID: 2F9V RELATED DB: PDB
REMARK 900 MUTATIONS CONFERRING RESISTANCE TO SCH6, A NOVEL HEPATITIS C VIRUS
REMARK 900 NS3/4A PROTEASE INHIBITOR REDUCED RNA REPLICATION FITNESS AND
REMARK 900 PARTIAL RESCUE BY SECOND SITE MUTATIONS
DBREF 2OC0 A 1 181 UNP Q9ELS8 Q9ELS8_9HEPC 1027 1207
DBREF 2OC0 C 1 181 UNP Q9ELS8 Q9ELS8_9HEPC 1027 1207
DBREF 2OC0 B 21 39 UNP Q9QP06 Q9QP06_9HEPC 1678 1696
DBREF 2OC0 D 21 39 UNP Q9QP06 Q9QP06_9HEPC 1678 1696
SEQADV 2OC0 MET A -10 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 ALA A -9 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 SER A -8 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 MET A -7 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 THR A -6 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLY A -5 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLY A -4 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLN A -3 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLN A -2 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 MET A -1 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLY A 0 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 ARG A 119 UNP Q9ELS8 GLN 1145 CONFLICT
SEQADV 2OC0 GLY A 182 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 SER A 183 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 HIS A 184 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS A 185 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS A 186 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS A 187 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS A 188 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS A 189 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 MET C -10 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 ALA C -9 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 SER C -8 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 MET C -7 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 THR C -6 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLY C -5 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLY C -4 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLN C -3 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLN C -2 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 MET C -1 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 GLY C 0 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 ARG C 119 UNP Q9ELS8 GLN 1145 CONFLICT
SEQADV 2OC0 GLY C 182 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 SER C 183 UNP Q9ELS8 CLONING ARTIFACT
SEQADV 2OC0 HIS C 184 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS C 185 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS C 186 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS C 187 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS C 188 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 HIS C 189 UNP Q9ELS8 EXPRESSION TAG
SEQADV 2OC0 LYS B 19 UNP Q9QP06 CLONING ARTIFACT
SEQADV 2OC0 LYS B 20 UNP Q9QP06 CLONING ARTIFACT
SEQADV 2OC0 LYS B 40 UNP Q9QP06 CLONING ARTIFACT
SEQADV 2OC0 LYS B 41 UNP Q9QP06 CLONING ARTIFACT
SEQADV 2OC0 LYS D 19 UNP Q9QP06 CLONING ARTIFACT
SEQADV 2OC0 LYS D 20 UNP Q9QP06 CLONING ARTIFACT
SEQADV 2OC0 LYS D 40 UNP Q9QP06 CLONING ARTIFACT
SEQADV 2OC0 LYS D 41 UNP Q9QP06 CLONING ARTIFACT
SEQRES 1 A 200 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ALA PRO
SEQRES 2 A 200 ILE THR ALA TYR ALA GLN GLN THR ARG GLY LEU LEU GLY
SEQRES 3 A 200 CYS ILE ILE THR SER LEU THR GLY ARG ASP LYS ASN GLN
SEQRES 4 A 200 VAL GLU GLY GLU VAL GLN ILE VAL SER THR ALA THR GLN
SEQRES 5 A 200 THR PHE LEU ALA THR CYS ILE ASN GLY VAL CYS TRP THR
SEQRES 6 A 200 VAL TYR HIS GLY ALA GLY THR ARG THR ILE ALA SER PRO
SEQRES 7 A 200 LYS GLY PRO VAL ILE GLN MET TYR THR ASN VAL ASP GLN
SEQRES 8 A 200 ASP LEU VAL GLY TRP PRO ALA PRO GLN GLY SER ARG SER
SEQRES 9 A 200 LEU THR PRO CYS THR CYS GLY SER SER ASP LEU TYR LEU
SEQRES 10 A 200 VAL THR ARG HIS ALA ASP VAL ILE PRO VAL ARG ARG ARG
SEQRES 11 A 200 GLY ASP SER ARG GLY SER LEU LEU SER PRO ARG PRO ILE
SEQRES 12 A 200 SER TYR LEU LYS GLY SER SER GLY GLY PRO LEU LEU CYS
SEQRES 13 A 200 PRO ALA GLY HIS ALA VAL GLY LEU PHE ARG ALA ALA VAL
SEQRES 14 A 200 CYS THR ARG GLY VAL ALA LYS ALA VAL ASP PHE ILE PRO
SEQRES 15 A 200 VAL GLU ASN LEU GLU THR THR MET ARG SER GLY SER HIS
SEQRES 16 A 200 HIS HIS HIS HIS HIS
SEQRES 1 B 23 LYS LYS GLY SER VAL VAL ILE VAL GLY ARG ILE VAL LEU
SEQRES 2 B 23 SER GLY LYS PRO ALA ILE ILE PRO LYS LYS
SEQRES 1 C 200 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ALA PRO
SEQRES 2 C 200 ILE THR ALA TYR ALA GLN GLN THR ARG GLY LEU LEU GLY
SEQRES 3 C 200 CYS ILE ILE THR SER LEU THR GLY ARG ASP LYS ASN GLN
SEQRES 4 C 200 VAL GLU GLY GLU VAL GLN ILE VAL SER THR ALA THR GLN
SEQRES 5 C 200 THR PHE LEU ALA THR CYS ILE ASN GLY VAL CYS TRP THR
SEQRES 6 C 200 VAL TYR HIS GLY ALA GLY THR ARG THR ILE ALA SER PRO
SEQRES 7 C 200 LYS GLY PRO VAL ILE GLN MET TYR THR ASN VAL ASP GLN
SEQRES 8 C 200 ASP LEU VAL GLY TRP PRO ALA PRO GLN GLY SER ARG SER
SEQRES 9 C 200 LEU THR PRO CYS THR CYS GLY SER SER ASP LEU TYR LEU
SEQRES 10 C 200 VAL THR ARG HIS ALA ASP VAL ILE PRO VAL ARG ARG ARG
SEQRES 11 C 200 GLY ASP SER ARG GLY SER LEU LEU SER PRO ARG PRO ILE
SEQRES 12 C 200 SER TYR LEU LYS GLY SER SER GLY GLY PRO LEU LEU CYS
SEQRES 13 C 200 PRO ALA GLY HIS ALA VAL GLY LEU PHE ARG ALA ALA VAL
SEQRES 14 C 200 CYS THR ARG GLY VAL ALA LYS ALA VAL ASP PHE ILE PRO
SEQRES 15 C 200 VAL GLU ASN LEU GLU THR THR MET ARG SER GLY SER HIS
SEQRES 16 C 200 HIS HIS HIS HIS HIS
SEQRES 1 D 23 LYS LYS GLY SER VAL VAL ILE VAL GLY ARG ILE VAL LEU
SEQRES 2 D 23 SER GLY LYS PRO ALA ILE ILE PRO LYS LYS
HET ZN A 901 1
HET BME A 801 4
HET HU1 A 999 39
HET ZN C 902 1
HETNAM ZN ZINC ION
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM HU1 TERT-BUTYL {(1S)-2-[(1R,2S,5S)-2-({[(1S)-3-AMINO-1-
HETNAM 2 HU1 (CYCLOBUTYLMETHYL)-2,3-DIOXOPROPYL]AMINO}CARBONYL)-6,
HETNAM 3 HU1 6-DIMETHYL-3-AZABICYCLO[3.1.0]HEX-3-YL]-1-CYCLOHEXYL-
HETNAM 4 HU1 2-OXOETHYL}CARBAMATE
HETSYN HU1 KETOAMIDE INHIBITOR SCH491762, BOUND FORM
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 BME C2 H6 O S
FORMUL 7 HU1 C29 H46 N4 O6
FORMUL 9 HOH *210(H2 O)
HELIX 1 1 GLY A 12 GLY A 23 1 12
HELIX 2 2 TYR A 56 GLY A 60 1 5
HELIX 3 3 ILE A 132 LYS A 136 1 5
HELIX 4 4 VAL A 172 SER A 181 1 10
HELIX 5 5 TYR C 56 GLY C 60 1 5
HELIX 6 6 ILE C 132 LYS C 136 1 5
HELIX 7 7 VAL C 172 MET C 179 1 8
SHEET 1 A 7 TYR A 6 GLN A 9 0
SHEET 2 A 7 VAL B 24 VAL B 30 -1 O VAL B 30 N TYR A 6
SHEET 3 A 7 VAL A 33 SER A 37 -1 N SER A 37 O VAL B 24
SHEET 4 A 7 THR A 42 ILE A 48 -1 O ALA A 45 N GLN A 34
SHEET 5 A 7 VAL A 51 VAL A 55 -1 O TRP A 53 N THR A 46
SHEET 6 A 7 LEU A 82 PRO A 86 -1 O TRP A 85 N CYS A 52
SHEET 7 A 7 TYR A 75 ASN A 77 -1 N ASN A 77 O LEU A 82
SHEET 1 B 2 ILE A 64 SER A 66 0
SHEET 2 B 2 GLY A 69 VAL A 71 -1 O VAL A 71 N ILE A 64
SHEET 1 C 7 ASP A 103 VAL A 107 0
SHEET 2 C 7 VAL A 113 ARG A 118 -1 O VAL A 116 N LEU A 104
SHEET 3 C 7 ARG A 123 PRO A 131 -1 O SER A 125 N ARG A 117
SHEET 4 C 7 VAL A 163 PRO A 171 -1 O ALA A 164 N ARG A 130
SHEET 5 C 7 ALA A 150 THR A 160 -1 N ALA A 156 O ASP A 168
SHEET 6 C 7 PRO A 142 LEU A 144 -1 N LEU A 143 O VAL A 151
SHEET 7 C 7 ASP A 103 VAL A 107 -1 N TYR A 105 O LEU A 144
SHEET 1 D 7 ALA B 36 ILE B 37 0
SHEET 2 D 7 VAL D 24 VAL D 30 -1 O VAL D 30 N ALA B 36
SHEET 3 D 7 VAL C 33 SER C 37 -1 N ILE C 35 O VAL D 26
SHEET 4 D 7 THR C 42 ILE C 48 -1 O PHE C 43 N VAL C 36
SHEET 5 D 7 VAL C 51 VAL C 55 -1 O TRP C 53 N THR C 46
SHEET 6 D 7 LEU C 82 PRO C 86 -1 O TRP C 85 N CYS C 52
SHEET 7 D 7 TYR C 75 ASN C 77 -1 N ASN C 77 O LEU C 82
SHEET 1 E 7 ASP C 103 VAL C 107 0
SHEET 2 E 7 VAL C 113 GLY C 120 -1 O ILE C 114 N LEU C 106
SHEET 3 E 7 ARG C 123 PRO C 131 -1 O SER C 125 N ARG C 117
SHEET 4 E 7 VAL C 163 PRO C 171 -1 O ALA C 164 N ARG C 130
SHEET 5 E 7 ALA C 150 THR C 160 -1 N ALA C 156 O ASP C 168
SHEET 6 E 7 PRO C 142 LEU C 144 -1 N LEU C 143 O VAL C 151
SHEET 7 E 7 ASP C 103 VAL C 107 -1 N TYR C 105 O LEU C 144
LINK SG CYS A 16 S2 BME A 801 1555 1555 2.02
LINK OG SER A 139 C36 HU1 A 999 1555 1555 1.46
LINK SG CYS A 97 ZN ZN A 901 1555 1555 2.09
LINK SG CYS A 99 ZN ZN A 901 1555 1555 2.34
LINK SG CYS A 145 ZN ZN A 901 1555 1555 2.18
LINK ZN ZN A 901 O HOH A1000 1555 1555 1.82
LINK SG CYS C 97 ZN ZN C 902 1555 1555 2.19
LINK SG CYS C 99 ZN ZN C 902 1555 1555 2.41
LINK SG CYS C 145 ZN ZN C 902 1555 1555 2.11
LINK ZN ZN C 902 O HOH C 915 1555 1555 2.14
SITE 1 AC1 4 CYS A 97 CYS A 99 CYS A 145 HOH A1000
SITE 1 AC2 4 CYS C 97 CYS C 99 CYS C 145 HOH C 915
SITE 1 AC3 3 CYS A 16 ILE A 17 THR A 38
SITE 1 AC4 12 GLN A 41 HIS A 57 ILE A 132 LYS A 136
SITE 2 AC4 12 GLY A 137 SER A 138 SER A 139 PHE A 154
SITE 3 AC4 12 ARG A 155 ALA A 156 ALA A 157 CYS A 159
CRYST1 224.264 224.264 75.451 90.00 90.00 120.00 H 3 2 36
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 0.004459 0.002574 0.000000 0.00000
SCALE2 0.000000 0.005149 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013254 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
