Header list of 1dxw.pdb file
Complete list - n 15 2 Bytes
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
Complete list - n 15 2 Bytes