HEADER HYDROLASE/HYDROLASE INHIBITOR 17-JAN-00 1DXW
TITLE STRUCTURE OF HETERO COMPLEX OF NON STRUCTURAL PROTEIN (NS) OF
TITLE 2 HEPATITIS C VIRUS (HCV) AND SYNTHETIC PEPTIDIC COMPOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 1027-1206;
COMPND 5 SYNONYM: NS3;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: COVALENT BOND BETWEEN SER 139 OG AND ABK 190 C1 (DI-
COMPND 8 FLUORO-ABU-KETOACID) OF INHIBITOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_COMMON: HCV;
SOURCE 4 ORGANISM_TAXID: 11103;
SOURCE 5 STRAIN: BK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS NON STRUCTURAL PROTEIN, HEPATITIS C VIRUS, SERINE PROTEASE,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.BARBATO,D.O.CICERO,F.CORDIER,F.NARJES,B.GERLACH,S.SAMBUCINI,
AUTHOR 2 S.GRZESIEK,V.G.MATASSA,R.DEFRANCESCO,R.BAZZO
REVDAT 5 15-JAN-20 1DXW 1 REMARK LINK
REVDAT 4 13-JUL-11 1DXW 1 VERSN
REVDAT 3 24-FEB-09 1DXW 1 VERSN
REVDAT 2 03-MAY-05 1DXW 1 COMPND ATOM MODEL
REVDAT 1 12-JAN-01 1DXW 0
JRNL AUTH G.BARBATO,D.O.CICERO,F.CORDIER,F.NARJES,B.GERLACH,
JRNL AUTH 2 S.SAMBUCINI,S.GRZESIEK,V.G.MATASSA,R.DEFRANCESCO,R.BAZZO
JRNL TITL INHIBITOR BINDING INDUCES ACTIVE SITE STABILISATION OF THE
JRNL TITL 2 HCV NS3 PROTEIN SERINE PROTEASE DOMAIN
JRNL REF EMBO J. V. 19 1195 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 10716920
JRNL DOI 10.1093/EMBOJ/19.6.1195
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.BARBATO,D.O.CICERO,M.C.NARDI,C.STEINKUHLER,R.CORTESE,
REMARK 1 AUTH 2 R.DEFRANCESCO,R.BAZZO
REMARK 1 TITL THE SOLUTION STRUCTURE OF THE N-TERMINAL SERINE PROTEASE
REMARK 1 TITL 2 DOMAIN OF THE HEPATITIS C VIRUS NS3 PROTEIN PROVIDES NEW
REMARK 1 TITL 3 INSIGHTS INTO ITS ACTIVATION AND CATALYTIC MECHANISM
REMARK 1 REF J.MOL.BIOL. V. 289 371 1999
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 10366511
REMARK 1 DOI 10.1006/JMBI.1999.2745
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.O.CICERO,G.BARBATO,U.KOCH,P.INGALLINELLA,E.BIANCHI,
REMARK 1 AUTH 2 M.C.NARDI,C.STEINKUHLER,R.CORTESE,V.MATASSA,R.DEFRANCESCO,
REMARK 1 AUTH 3 A.PESSI,R.BAZZO
REMARK 1 TITL STRUCTURAL CHARACTERIZATION OF THE INTERACTIONS OF OPTIMIZED
REMARK 1 TITL 2 PRODUCT INHIBITORS WITH THE N-TERMINAL PROTEINASE DOMAIN OF
REMARK 1 TITL 3 THE HEPATITIS C VIRUS (HCV) NS3 PROTEIN BY NMR AND MODELLING
REMARK 1 TITL 4 STUDIES
REMARK 1 REF J.MOL.BIOL. V. 289 385 1999
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 10366512
REMARK 1 DOI 10.1006/JMBI.1999.2746
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.URBANI,R.BAZZO,M.C.NARDI,D.O.CICERO,R.DEFRANCESCO,
REMARK 1 AUTH 2 C.STEINKUHLER,G.BARBATO
REMARK 1 TITL THE METAL BINDING SITE OF THE HEPATITIS C VIRUS NS3 PROTEASE
REMARK 1 REF J.BIOL.CHEM. V. 273 18760 1998
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 9668049
REMARK 1 DOI 10.1074/JBC.273.30.18760
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE. RESIDUES OF NS3 1-21 ARE NOT INCLUDED IN
REMARK 3 THE MODELS SINCE THEY ARE AFFECTED BY MOBILITY IN SOLUTION.
REMARK 4
REMARK 4 1DXW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1290004533.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 95% WATER/10 % D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE
REMARK 210 EXPERIMENTS, 3D HETERONUCLEAR NOESY EXPERIMENTS, 3D AND 2D
REMARK 210 COUPLING CONSTANT MEASUREMENTS, 10% GLUCOSE C13 LABELLING FOR
REMARK 210 METHYL STEREOSPECIFIC ASSINGMENT, COMBINED USE OF SEVERAL
REMARK 210 COUPLING CONSTANTS AND ROESY SPECTROSCOPY TO DETERMINE CHI1
REMARK 210 ANGLES.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 PRO A 2
REMARK 465 ILE A 3
REMARK 465 THR A 4
REMARK 465 ALA A 5
REMARK 465 TYR A 6
REMARK 465 SER A 7
REMARK 465 GLN A 8
REMARK 465 GLN A 9
REMARK 465 THR A 10
REMARK 465 ARG A 11
REMARK 465 GLY A 12
REMARK 465 LEU A 13
REMARK 465 LEU A 14
REMARK 465 GLY A 15
REMARK 465 CYS A 16
REMARK 465 ILE A 17
REMARK 465 ILE A 18
REMARK 465 THR A 19
REMARK 465 SER A 20
REMARK 465 LEU A 21
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HG1 THR A 38 O GLY A 58 1.54
REMARK 500 O LEU A 44 HG1 THR A 54 1.58
REMARK 500 O ALA A 157 HN2 2ZF A 188 1.60
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 1 ASN A 27 123.94 63.77
REMARK 500 1 GLN A 41 -169.14 -173.60
REMARK 500 1 PHE A 43 -138.12 -160.26
REMARK 500 1 SER A 61 46.36 -91.28
REMARK 500 1 LYS A 62 -130.34 37.54
REMARK 500 1 LEU A 64 -132.79 -86.95
REMARK 500 1 LYS A 68 -2.67 -153.33
REMARK 500 1 GLN A 86 73.71 -110.07
REMARK 500 1 PRO A 88 -91.96 -134.14
REMARK 500 1 ALA A 91 134.68 -175.43
REMARK 500 1 SER A 93 115.35 59.67
REMARK 500 1 PRO A 96 -85.33 -66.10
REMARK 500 1 CYS A 97 114.97 59.34
REMARK 500 1 CYS A 99 117.30 61.79
REMARK 500 1 ALA A 111 -93.63 -156.86
REMARK 500 1 ASP A 112 73.67 47.08
REMARK 500 1 CYS A 145 175.60 -58.82
REMARK 500 1 THR A 160 -102.07 -87.10
REMARK 500 1 ALA A 166 137.86 -175.26
REMARK 500 1 LYS A 183 -61.78 63.58
REMARK 500 2 ASN A 27 25.05 47.26
REMARK 500 2 THR A 38 79.03 -116.80
REMARK 500 2 ALA A 39 -52.51 63.45
REMARK 500 2 PHE A 43 -148.14 -160.32
REMARK 500 2 ALA A 59 -79.97 -90.02
REMARK 500 2 LYS A 62 -71.29 60.05
REMARK 500 2 LEU A 64 -119.29 -147.05
REMARK 500 2 ASN A 77 74.23 -101.05
REMARK 500 2 ASP A 103 75.56 -69.95
REMARK 500 2 HIS A 110 -71.33 -94.06
REMARK 500 2 ALA A 111 -50.88 -153.91
REMARK 500 2 ILE A 114 178.65 59.97
REMARK 500 2 CYS A 145 -174.03 -63.95
REMARK 500 2 ALA A 166 141.94 -174.33
REMARK 500 2 ALA A 181 111.27 10.86
REMARK 500 2 SER A 182 36.65 -172.18
REMARK 500 2 LYS A 185 86.79 54.07
REMARK 500 3 ARG A 24 -139.06 -147.51
REMARK 500 3 ASP A 25 130.02 63.61
REMARK 500 3 ASN A 27 163.50 59.11
REMARK 500 3 VAL A 29 -73.13 59.35
REMARK 500 3 GLU A 30 -86.83 -166.29
REMARK 500 3 GLN A 41 -170.56 -173.17
REMARK 500 3 PHE A 43 -146.38 -161.79
REMARK 500 3 ALA A 59 -70.08 -79.87
REMARK 500 3 LYS A 62 -129.57 36.28
REMARK 500 3 THR A 63 73.13 49.79
REMARK 500 3 ALA A 91 -144.75 -86.85
REMARK 500 3 ARG A 109 -32.93 -34.39
REMARK 500 3 HIS A 110 -85.34 -97.73
REMARK 500
REMARK 500 THIS ENTRY HAS 376 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 24 0.28 SIDE CHAIN
REMARK 500 1 ARG A 92 0.29 SIDE CHAIN
REMARK 500 1 ARG A 109 0.32 SIDE CHAIN
REMARK 500 1 ARG A 117 0.18 SIDE CHAIN
REMARK 500 1 ARG A 118 0.31 SIDE CHAIN
REMARK 500 1 ARG A 119 0.24 SIDE CHAIN
REMARK 500 1 ARG A 123 0.28 SIDE CHAIN
REMARK 500 1 ARG A 130 0.22 SIDE CHAIN
REMARK 500 1 ARG A 155 0.30 SIDE CHAIN
REMARK 500 1 ARG A 161 0.25 SIDE CHAIN
REMARK 500 1 ARG A 180 0.28 SIDE CHAIN
REMARK 500 2 ARG A 24 0.28 SIDE CHAIN
REMARK 500 2 ARG A 92 0.30 SIDE CHAIN
REMARK 500 2 ARG A 109 0.31 SIDE CHAIN
REMARK 500 2 ARG A 117 0.27 SIDE CHAIN
REMARK 500 2 ARG A 118 0.24 SIDE CHAIN
REMARK 500 2 ARG A 119 0.23 SIDE CHAIN
REMARK 500 2 ARG A 123 0.28 SIDE CHAIN
REMARK 500 2 ARG A 130 0.23 SIDE CHAIN
REMARK 500 2 ARG A 155 0.20 SIDE CHAIN
REMARK 500 2 ARG A 161 0.30 SIDE CHAIN
REMARK 500 2 ARG A 180 0.29 SIDE CHAIN
REMARK 500 3 ARG A 24 0.28 SIDE CHAIN
REMARK 500 3 ARG A 92 0.31 SIDE CHAIN
REMARK 500 3 ARG A 109 0.25 SIDE CHAIN
REMARK 500 3 ARG A 117 0.26 SIDE CHAIN
REMARK 500 3 ARG A 118 0.29 SIDE CHAIN
REMARK 500 3 ARG A 119 0.30 SIDE CHAIN
REMARK 500 3 ARG A 123 0.19 SIDE CHAIN
REMARK 500 3 ARG A 130 0.25 SIDE CHAIN
REMARK 500 3 ARG A 155 0.29 SIDE CHAIN
REMARK 500 3 ARG A 161 0.23 SIDE CHAIN
REMARK 500 3 ARG A 180 0.28 SIDE CHAIN
REMARK 500 4 ARG A 24 0.32 SIDE CHAIN
REMARK 500 4 ARG A 92 0.31 SIDE CHAIN
REMARK 500 4 ARG A 109 0.27 SIDE CHAIN
REMARK 500 4 ARG A 117 0.31 SIDE CHAIN
REMARK 500 4 ARG A 118 0.31 SIDE CHAIN
REMARK 500 4 ARG A 119 0.22 SIDE CHAIN
REMARK 500 4 ARG A 123 0.27 SIDE CHAIN
REMARK 500 4 ARG A 130 0.32 SIDE CHAIN
REMARK 500 4 ARG A 155 0.26 SIDE CHAIN
REMARK 500 4 ARG A 161 0.22 SIDE CHAIN
REMARK 500 4 ARG A 180 0.23 SIDE CHAIN
REMARK 500 5 ARG A 24 0.27 SIDE CHAIN
REMARK 500 5 ARG A 92 0.28 SIDE CHAIN
REMARK 500 5 ARG A 109 0.32 SIDE CHAIN
REMARK 500 5 ARG A 117 0.29 SIDE CHAIN
REMARK 500 5 ARG A 118 0.31 SIDE CHAIN
REMARK 500 5 ARG A 119 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 220 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1 2ZF A 188
REMARK 610 2 2ZF A 188
REMARK 610 3 2ZF A 188
REMARK 610 4 2ZF A 188
REMARK 610 5 2ZF A 188
REMARK 610 6 2ZF A 188
REMARK 610 7 2ZF A 188
REMARK 610 8 2ZF A 188
REMARK 610 9 2ZF A 188
REMARK 610 10 2ZF A 188
REMARK 610 11 2ZF A 188
REMARK 610 12 2ZF A 188
REMARK 610 13 2ZF A 188
REMARK 610 14 2ZF A 188
REMARK 610 15 2ZF A 188
REMARK 610 16 2ZF A 188
REMARK 610 17 2ZF A 188
REMARK 610 18 2ZF A 188
REMARK 610 19 2ZF A 188
REMARK 610 20 2ZF A 188
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 145 SG 168.3
REMARK 620 3 CYS A 99 SG 82.5 85.9
REMARK 620 N 1 2
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: N-(TERT-BUTOXYCARBONYL)-L-ALPHA-GLUTAMYL-N-[(1R)-1-
REMARK 630 (CARBOXYCARBONYL)-3,3-DIFLUOROPROPYL]-L-LEUCINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 1 2ZF A 188
REMARK 630 2 2ZF A 188
REMARK 630 3 2ZF A 188
REMARK 630 4 2ZF A 188
REMARK 630 5 2ZF A 188
REMARK 630 6 2ZF A 188
REMARK 630 7 2ZF A 188
REMARK 630 8 2ZF A 188
REMARK 630 9 2ZF A 188
REMARK 630 10 2ZF A 188
REMARK 630 11 2ZF A 188
REMARK 630 12 2ZF A 188
REMARK 630 13 2ZF A 188
REMARK 630 14 2ZF A 188
REMARK 630 15 2ZF A 188
REMARK 630 16 2ZF A 188
REMARK 630 17 2ZF A 188
REMARK 630 18 2ZF A 188
REMARK 630 19 2ZF A 188
REMARK 630 20 2ZF A 188
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: BOC GLU LEU FKI
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2ZF A 188
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BT7 RELATED DB: PDB
REMARK 900 THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE
REMARK 900 HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES
REMARK 900 RELATED ID: 4617 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 6 RESIDUES INSERTED AT THE C TERMINAL
REMARK 999 (ALA SER LYS LYS LYS LYS)
DBREF 1DXW A 1 180 UNP P90191 P90191_9HEPC 1027 1206
SEQADV 1DXW ALA A 181 UNP P90191 SEE REMARK 999
SEQADV 1DXW SER A 182 UNP P90191 SEE REMARK 999
SEQADV 1DXW LYS A 183 UNP P90191 SEE REMARK 999
SEQADV 1DXW LYS A 184 UNP P90191 SEE REMARK 999
SEQADV 1DXW LYS A 185 UNP P90191 SEE REMARK 999
SEQADV 1DXW LYS A 186 UNP P90191 SEE REMARK 999
SEQRES 1 A 186 ALA PRO ILE THR ALA TYR SER GLN GLN THR ARG GLY LEU
SEQRES 2 A 186 LEU GLY CYS ILE ILE THR SER LEU THR GLY ARG ASP LYS
SEQRES 3 A 186 ASN GLN VAL GLU GLY GLU VAL GLN VAL VAL SER THR ALA
SEQRES 4 A 186 THR GLN SER PHE LEU ALA THR CYS VAL ASN GLY VAL CYS
SEQRES 5 A 186 TRP THR VAL TYR HIS GLY ALA GLY SER LYS THR LEU ALA
SEQRES 6 A 186 GLY PRO LYS GLY PRO ILE THR GLN MET TYR THR ASN VAL
SEQRES 7 A 186 ASP GLN ASP LEU VAL GLY TRP GLN ALA PRO PRO GLY ALA
SEQRES 8 A 186 ARG SER LEU THR PRO CYS THR CYS GLY SER SER ASP LEU
SEQRES 9 A 186 TYR LEU VAL THR ARG HIS ALA ASP VAL ILE PRO VAL ARG
SEQRES 10 A 186 ARG ARG GLY ASP SER ARG GLY SER LEU LEU SER PRO ARG
SEQRES 11 A 186 PRO VAL SER TYR LEU LYS GLY SER SER GLY GLY PRO LEU
SEQRES 12 A 186 LEU CYS PRO SER GLY HIS ALA VAL GLY ILE PHE ARG ALA
SEQRES 13 A 186 ALA VAL CYS THR ARG GLY VAL ALA LYS ALA VAL ASP PHE
SEQRES 14 A 186 VAL PRO VAL GLU SER MET GLU THR THR MET ARG ALA SER
SEQRES 15 A 186 LYS LYS LYS LYS
HET 2ZF A 188 52
HET ZN A 301 1
HETNAM 2ZF N-(TERT-BUTOXYCARBONYL)-L-ALPHA-GLUTAMYL-N-[(1R)-1-
HETNAM 2 2ZF (CARBOXYCARBONYL)-3,3-DIFLUOROPROPYL]-L-LEUCINAMIDE
HETNAM ZN ZINC ION
FORMUL 2 2ZF C21 H33 F2 N3 O9
FORMUL 3 ZN ZN 2+
HELIX 1 1 TYR A 56 GLY A 60 1 5
HELIX 2 2 VAL A 78 GLN A 80 5 3
HELIX 3 3 PRO A 131 LYS A 136 5 6
HELIX 4 4 VAL A 172 ALA A 181 1 10
SHEET 1 A 5 VAL A 33 SER A 37 0
SHEET 2 A 5 SER A 42 VAL A 48 -1 N ALA A 45 O GLN A 34
SHEET 3 A 5 VAL A 51 VAL A 55 -1 N TRP A 53 O THR A 46
SHEET 4 A 5 LEU A 82 GLY A 84 -1 N VAL A 83 O THR A 54
SHEET 5 A 5 TYR A 75 ASN A 77 -1 N ASN A 77 O LEU A 82
SHEET 1 B 3 ASP A 103 LEU A 106 0
SHEET 2 B 3 ILE A 114 GLY A 120 -1 N VAL A 116 O LEU A 104
SHEET 3 B 3 ARG A 123 LEU A 126 -1 N SER A 125 O ARG A 117
SHEET 1 C 2 GLY A 152 ALA A 157 0
SHEET 2 C 2 VAL A 167 PRO A 171 -1 N VAL A 170 O ILE A 153
LINK ZN ZN A 301 SG CYS A 97 1555 1555 2.30
LINK ZN ZN A 301 SG CYS A 145 1555 1555 2.30
LINK ZN ZN A 301 SG CYS A 99 1555 1555 2.30
LINK OG SER A 139 C6 2ZF A 188 1555 1555 1.42
SITE 1 AC1 11 PHE A 43 HIS A 57 LEU A 135 LYS A 136
SITE 2 AC1 11 GLY A 137 SER A 139 PHE A 154 ARG A 155
SITE 3 AC1 11 ALA A 156 ALA A 157 CYS A 159
SITE 1 AC2 6 PRO A 96 CYS A 97 CYS A 99 CYS A 145
SITE 2 AC2 6 HIS A 149 VAL A 151
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
