HEADER VIRAL PROTEIN 29-JUN-05 2A4R
TITLE HCV NS3 PROTEASE DOMAIN WITH A KETOAMIDE INHIBITOR COVALENTLY BOUND.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NS3 PROTEASE/HELICASE;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: PROTEASE DOMAIN, RESIDUES 1-181;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NS4A PEPTIDE;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: RESIDUES 21-39;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_TAXID: 11103;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 9 OF THE PROTEIN IS NATURALLY FOUND IN HEPATITIS C VIRUS TYPE 1B.
KEYWDS VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BOGEN,A.K.SAKSENA,A.ARASAPPAN,H.GU,F.G.NJOROGE,V.GIRIJAVALLABHAN,
AUTHOR 2 J.PICHARDO,N.BUTKIEWICZ,A.PRONGAY,V.MADISON
REVDAT 5 14-FEB-24 2A4R 1 REMARK
REVDAT 4 20-OCT-21 2A4R 1 REMARK SEQADV LINK
REVDAT 3 21-SEP-11 2A4R 1 HETATM VERSN
REVDAT 2 24-FEB-09 2A4R 1 VERSN
REVDAT 1 04-JUL-06 2A4R 0
JRNL AUTH S.BOGEN,A.K.SAKSENA,A.ARASAPPAN,H.GU,F.G.NJOROGE,
JRNL AUTH 2 V.GIRIJAVALLABHAN,J.PICHARDO,N.BUTKIEWICZ,A.PRONGAY,
JRNL AUTH 3 V.MADISON
JRNL TITL HEPATITIS C VIRUS NS3-4A SERINE PROTEASE INHIBITORS: USE OF
JRNL TITL 2 A P2-P1 CYCLOPROPYL ALANINE COMBINATION FOR IMPROVED
JRNL TITL 3 POTENCY.
JRNL REF BIOORG.MED.CHEM.LETT. V. 15 4515 2005
JRNL REFN ISSN 0960-894X
JRNL PMID 16112862
JRNL DOI 10.1016/J.BMCL.2005.07.009
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.J.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 P2' 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 R.A.LOVE,H.E.PARGE,J.A.WICKERSHAM,Z.HOSTOMSKY,N.HABUKA,
REMARK 1 AUTH 2 E.W.MOOMAW,T.ADACHI,Z.HOSTOMSKA
REMARK 1 TITL THE CRYSTAL STRUCTURE OF HEPATITIS C VIRUS NS3 PROTEINASE
REMARK 1 TITL 2 REVEALS A TRYPSIN-LIKE FOLD AND A STRUCTURAL ZINC BINDING
REMARK 1 TITL 3 SITE.
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 87 331 1996
REMARK 1 REFN ISSN 0092-8674
REMARK 1 PMID 8861916
REMARK 1 DOI 10.1016/S0092-8674(00)81350-1
REMARK 1 REFERENCE 4
REMARK 1 AUTH Y.YAN,Y.LI,S.MUNSHI,V.SARDANA,J.L.COLE,M.SARDANA,
REMARK 1 AUTH 2 C.STEINKUEHLER,L.TOMEI,R.DE FRANCESCO,L.C.KUO,Z.CHEN
REMARK 1 TITL COMPLEX OF NS3 PROTEASE AND NS4A PEPTIDE OF BK STRAIN
REMARK 1 TITL 2 HEPATITIS C VIRUS: A 2.2A RESOLUTION STRUCTURE IN A
REMARK 1 TITL 3 HEXAGONAL CRYSTAL FORM.
REMARK 1 REF PROTEIN SCI. V. 7 837 1998
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 9568891
REMARK 1 REFERENCE 5
REMARK 1 AUTH S.DIMARCO,M.RIZZI,C.VOLPARI,M.A.WALSH,F.NARJES,S.COLARUSSO,
REMARK 1 AUTH 2 R.DE FRANCESCO,V.G.MATASSA,M.SOLLAZZO
REMARK 1 TITL INHIBITION OF THE HEPATITIS C VIRUS NS3/4A PROTEASE. THE
REMARK 1 TITL 2 CRYSTAL STRUCTURES OF TWO PROTEASE-INHIBITOR COMPLEXES.
REMARK 1 REF J.BIOL.CHEM. V. 275 7152 2000
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 10702283
REMARK 1 DOI 10.1074/JBC.275.10.7152
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 10.0
REMARK 3 NUMBER OF REFLECTIONS : 25500
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 SET) : 0.201
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2540
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE : 0.3542
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 563
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 : 52
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.810
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.237
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 2A4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000033486.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-99
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 5.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28197
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.48900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 24.00
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, SODIUM POTASSIUM PHOSPHATE,
REMARK 280 SODIUM CHLORIDE, 2-MERCAPTOETHANOL, PH 5.7, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 273K. MES, SODIUM POTASSIUM PHOSPHATE,
REMARK 280 SODIUM CHLORIDE, 2-MERCAPTOETHANOL, PH 5.7, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 285K
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 111.80150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 64.54863
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 25.11800
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 111.80150
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 64.54863
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 25.11800
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 111.80150
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 64.54863
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 25.11800
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 111.80150
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 64.54863
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 25.11800
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 111.80150
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 64.54863
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 25.11800
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 111.80150
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 64.54863
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 25.11800
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 129.09725
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 50.23600
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 129.09725
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 50.23600
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 129.09725
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 50.23600
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 129.09725
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 50.23600
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 129.09725
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 50.23600
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 129.09725
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 50.23600
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
REMARK 350 TOTAL BURIED SURFACE AREA: 7660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -126.0 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: 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 OG SER A 139 C33 BNH A 401 1.43
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 PHE A 43 -153.84 -150.59
REMARK 500 THR A 98 50.04 -141.89
REMARK 500 ALA A 111 32.71 70.10
REMARK 500 PHE C 43 -158.74 -157.90
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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 97 SG
REMARK 620 2 CYS A 99 SG 94.5
REMARK 620 3 CYS A 145 SG 98.8 106.1
REMARK 620 4 HOH A 405 O 113.7 115.3 123.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 97 SG
REMARK 620 2 CYS C 99 SG 99.7
REMARK 620 3 CYS C 145 SG 98.4 114.4
REMARK 620 4 HOH C 304 O 113.3 106.4 122.2
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A1R RELATED DB: PDB
REMARK 900 HCV NS3 PROTEASE DOMAIN: NS4A PEPTIDE COMPLEX
REMARK 900 RELATED ID: 2A4G RELATED DB: PDB
REMARK 900 HCV NS3 PROTEASE DOMAIN WITH KETOAMIDE INHIBITOR SCH225724.
REMARK 900 RELATED ID: 1JXP RELATED DB: PDB
REMARK 900 BK STRAIN HEPATITIS C VIRUS (HCV) NS3-NS4A
REMARK 900 RELATED ID: 1N1L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN: NS4A PEPTIDE COMPLEX
REMARK 900 WITH COVALENTLY BOUND INHIBITOR (GW472467X)
REMARK 900 RELATED ID: 1NS3 RELATED DB: PDB
REMARK 900 STRUCTURE OF HCV PROTEASE (BK STRAIN)
REMARK 900 RELATED ID: 1RTL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN: NS4A PEPTIDE COMPLEX
REMARK 900 WITH COVALENTLY BOUND PYRROLIDINE-5,5-TRANSLACTAM INHIBITOR
DBREF 2A4R A 1 181 UNP Q91RS4 Q91RS4_9HEPC 1 181
DBREF 2A4R B 21 39 UNP O39914 O39914_9HEPC 6 24
DBREF 2A4R C 1 181 UNP Q91RS4 Q91RS4_9HEPC 1 181
DBREF 2A4R D 21 39 UNP O39914 O39914_9HEPC 6 24
SEQADV 2A4R MET A -10 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R ALA A -9 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R SER A -8 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R MET A -7 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R THR A -6 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLY A -5 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLY A -4 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLN A -3 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLN A -2 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R MET A -1 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLY A 0 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLY A 182 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R SER A 183 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R HIS A 184 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS A 185 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS A 186 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS A 187 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS A 188 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS A 189 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R MET C -10 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R ALA C -9 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R SER C -8 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R MET C -7 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R THR C -6 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLY C -5 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLY C -4 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLN C -3 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLN C -2 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R MET C -1 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLY C 0 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R GLY C 182 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R SER C 183 UNP Q91RS4 CLONING ARTIFACT
SEQADV 2A4R HIS C 184 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS C 185 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS C 186 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS C 187 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS C 188 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R HIS C 189 UNP Q91RS4 EXPRESSION TAG
SEQADV 2A4R LYS B 19 UNP O39914 CLONING ARTIFACT
SEQADV 2A4R LYS B 20 UNP O39914 CLONING ARTIFACT
SEQADV 2A4R VAL B 30 UNP O39914 ILE 15 ENGINEERED MUTATION
SEQADV 2A4R LYS B 40 UNP O39914 CLONING ARTIFACT
SEQADV 2A4R LYS B 41 UNP O39914 CLONING ARTIFACT
SEQADV 2A4R LYS D 19 UNP O39914 CLONING ARTIFACT
SEQADV 2A4R LYS D 20 UNP O39914 CLONING ARTIFACT
SEQADV 2A4R VAL D 30 UNP O39914 ILE 15 ENGINEERED MUTATION
SEQADV 2A4R LYS D 40 UNP O39914 CLONING ARTIFACT
SEQADV 2A4R LYS D 41 UNP O39914 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 301 1
HET BNH A 401 50
HET ZN C 302 1
HETNAM ZN ZINC ION
HETNAM BNH [(N-{3-[(N-{CYCLOHEXYL[(ISOBUTOXYCARBONYL)
HETNAM 2 BNH AMINO]ACETYL}-3-CYCLOPROPYLALANYL)AMINO]-4-
HETNAM 3 BNH CYCLOPROPYL-2-OXOBUTANOYL}GLYCYL)AMINO](PHENYL)ACETIC
HETNAM 4 BNH ACID
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 BNH C36 H51 N5 O9
FORMUL 8 HOH *161(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 ARG A 180 1 9
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 GLY A 120 -1 O ILE A 114 N LEU A 106
SHEET 3 C 7 ARG A 123 PRO A 131 -1 O ARG A 123 N ARG A 119
SHEET 4 C 7 VAL A 163 PRO A 171 -1 O VAL A 167 N GLY A 124
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 3 ALA B 36 ILE B 37 0
SHEET 2 D 3 SER D 22 VAL D 30 -1 O VAL D 30 N ALA B 36
SHEET 3 D 3 THR C 63 ILE C 64 1 N THR C 63 O VAL D 23
SHEET 1 E 7 ALA B 36 ILE B 37 0
SHEET 2 E 7 SER D 22 VAL D 30 -1 O VAL D 30 N ALA B 36
SHEET 3 E 7 VAL C 33 SER C 37 -1 N ILE C 35 O VAL D 26
SHEET 4 E 7 THR C 42 ILE C 48 -1 O PHE C 43 N VAL C 36
SHEET 5 E 7 VAL C 51 VAL C 55 -1 O TRP C 53 N THR C 46
SHEET 6 E 7 LEU C 82 PRO C 86 -1 O TRP C 85 N CYS C 52
SHEET 7 E 7 TYR C 75 ASN C 77 -1 N ASN C 77 O LEU C 82
SHEET 1 F 7 ASP C 103 VAL C 107 0
SHEET 2 F 7 VAL C 113 GLY C 120 -1 O ILE C 114 N LEU C 106
SHEET 3 F 7 ARG C 123 PRO C 131 -1 O SER C 125 N ARG C 117
SHEET 4 F 7 VAL C 163 PRO C 171 -1 O ALA C 164 N ARG C 130
SHEET 5 F 7 ALA C 150 THR C 160 -1 N ALA C 156 O ASP C 168
SHEET 6 F 7 PRO C 142 LEU C 144 -1 N LEU C 143 O VAL C 151
SHEET 7 F 7 ASP C 103 VAL C 107 -1 N TYR C 105 O LEU C 144
LINK SG CYS A 97 ZN ZN A 301 1555 1555 2.19
LINK SG CYS A 99 ZN ZN A 301 1555 1555 2.44
LINK SG CYS A 145 ZN ZN A 301 1555 1555 2.28
LINK ZN ZN A 301 O HOH A 405 1555 1555 2.01
LINK SG CYS C 97 ZN ZN C 302 1555 1555 2.20
LINK SG CYS C 99 ZN ZN C 302 1555 1555 2.23
LINK SG CYS C 145 ZN ZN C 302 1555 1555 2.14
LINK ZN ZN C 302 O HOH C 304 1555 1555 2.14
SITE 1 AC1 5 CYS A 97 THR A 98 CYS A 99 CYS A 145
SITE 2 AC1 5 HOH A 405
SITE 1 AC2 15 GLN A 41 THR A 42 HIS A 57 ARG A 123
SITE 2 AC2 15 ILE A 132 LYS A 136 GLY A 137 SER A 138
SITE 3 AC2 15 SER A 139 ARG A 155 ALA A 156 ALA A 157
SITE 4 AC2 15 VAL A 158 CYS A 159 HOH A 470
SITE 1 AC3 4 CYS C 97 CYS C 99 CYS C 145 HOH C 304
CRYST1 223.603 223.603 75.354 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 0.004472 0.002582 0.000000 0.00000
SCALE2 0.000000 0.005164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013271 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
