Header list of 1bt7.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE 01-SEP-98 1BT7
TITLE THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE
TITLE 2 HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NS3 SERINE PROTEASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: COMPOUND ENGINEERED ADDING A SOLUBILISING TAIL AT THE
COMPND 7 C-TERMINUS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_TAXID: 11103;
SOURCE 4 STRAIN: BK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7.7
KEYWDS HYDROLASE, VIRAL NON-STRUCTURAL PROTEIN, SERINE PROTEASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.BARBATO,D.O.CICERO,M.C.NARDI,C.STEINKUHLER,R.CORTESE,R.DE
AUTHOR 2 FRANCESCO,R.BAZZO
REVDAT 3 16-FEB-22 1BT7 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1BT7 1 VERSN
REVDAT 1 22-JUN-99 1BT7 0
JRNL AUTH G.BARBATO,D.O.CICERO,M.C.NARDI,C.STEINKUHLER,R.CORTESE,
JRNL AUTH 2 R.DE FRANCESCO,R.BAZZO
JRNL TITL THE SOLUTION STRUCTURE OF THE N-TERMINAL PROTEINASE DOMAIN
JRNL TITL 2 OF THE HEPATITIS C VIRUS (HCV) NS3 PROTEIN PROVIDES NEW
JRNL TITL 3 INSIGHTS INTO ITS ACTIVATION AND CATALYTIC MECHANISM.
JRNL REF J.MOL.BIOL. V. 289 371 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10366511
JRNL DOI 10.1006/JMBI.1999.2745
REMARK 1
REMARK 1 REFERENCE 1
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 2.2 A 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 REFERENCE 2
REMARK 1 AUTH A.URBANI,R.BAZZO,M.C.NARDI,D.O.CICERO,R.DE FRANCESCO,
REMARK 1 AUTH 2 C.STEINKUHLER,G.BARBATO
REMARK 1 TITL THE METAL BINDING SITE OF THE HEPATITIS C VIRUS NS3
REMARK 1 TITL 2 PROTEASE. A SPECTROSCOPIC INVESTIGATION
REMARK 1 REF J.BIOL.CHEM. V. 273 18760 1998
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
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 ERRATUM. CRYSTAL STRUCTURE OF THE HEPATITIS C VIRUS NS3
REMARK 1 TITL 2 PROTEASE DOMAIN COMPLEXED WITH A SYNTHETIC NS4A COFACTOR
REMARK 1 TITL 3 PEPTIDE
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 89 159 1997
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 4
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 REFERENCE 5
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 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. R.M.S. DEVIATIONS FROM EXPERIMENTAL
REMARK 3 RESTRAINTS: DISTANCE (ANGSTROMS) : 0.076 +/- 0.003 DIHEDRAL
REMARK 3 (DEGREES) : 1.331 +/- 0.148 IDEALIZED GEOMETRY BONDS (ANGSTROMS):
REMARK 3 0.005 +/- 0.0006 ANGLES (DEGREES) : 0.761 +/- 0.032 IMPROPERS
REMARK 3 (DEGREES) : 0.543 +/- 0.017
REMARK 4
REMARK 4 1BT7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172063.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 90% H2O/5% D2O/ 5% GLYCEROL-D
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW
REMARK 210 METHOD USED : DG-SA HYBRID
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT
REMARK 210 VIOLATIONS/MINIMUM ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING N15, N15/C13,
REMARK 210 N15/C13/2H, AND 15N SELECTIVELY LABELED SAMPLES, WITH TRIPLE
REMARK 210 RESONANCE EXPERIMENTS
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 H LEU A 143 O GLY A 152 1.53
REMARK 500 O ARG A 130 H ALA A 164 1.55
REMARK 500 H GLN A 34 O ALA A 45 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 GLN A 28 77.84 -153.43
REMARK 500 1 VAL A 29 -158.51 -64.14
REMARK 500 1 GLU A 30 79.64 59.92
REMARK 500 1 GLU A 32 -41.23 -171.15
REMARK 500 1 THR A 40 -58.32 178.70
REMARK 500 1 GLN A 41 -156.05 -179.72
REMARK 500 1 ASN A 49 18.97 57.80
REMARK 500 1 LYS A 62 -165.59 -77.70
REMARK 500 1 LEU A 64 171.39 -52.24
REMARK 500 1 LYS A 68 41.45 -152.27
REMARK 500 1 MET A 74 -44.90 -135.10
REMARK 500 1 VAL A 78 -133.28 11.77
REMARK 500 1 ASP A 81 -114.41 -163.59
REMARK 500 1 LEU A 82 176.53 173.47
REMARK 500 1 LEU A 94 -147.30 -77.66
REMARK 500 1 THR A 98 38.55 -170.98
REMARK 500 1 SER A 101 -155.38 -99.02
REMARK 500 1 SER A 102 19.92 -149.76
REMARK 500 1 LEU A 106 100.45 -51.33
REMARK 500 1 ARG A 109 52.99 -96.38
REMARK 500 1 HIS A 110 44.83 -177.09
REMARK 500 1 LEU A 127 54.16 -107.27
REMARK 500 1 SER A 128 126.60 169.34
REMARK 500 1 CYS A 145 -92.17 -49.90
REMARK 500 1 PRO A 146 -81.20 -92.30
REMARK 500 1 HIS A 149 98.53 54.46
REMARK 500 1 ARG A 161 90.79 -46.00
REMARK 500 1 LYS A 185 -80.93 -86.70
REMARK 500 2 ARG A 24 107.18 57.74
REMARK 500 2 GLN A 28 80.09 -160.73
REMARK 500 2 GLU A 30 81.04 -170.82
REMARK 500 2 ALA A 39 96.69 -50.18
REMARK 500 2 LYS A 62 -165.17 -105.53
REMARK 500 2 LEU A 64 177.77 -56.22
REMARK 500 2 THR A 72 -153.80 43.17
REMARK 500 2 GLN A 73 118.75 -161.66
REMARK 500 2 THR A 76 113.52 -160.44
REMARK 500 2 VAL A 78 -162.87 36.01
REMARK 500 2 ASP A 81 -102.26 -126.97
REMARK 500 2 LEU A 82 168.42 179.22
REMARK 500 2 PRO A 88 -79.12 -67.29
REMARK 500 2 PRO A 89 36.04 -97.65
REMARK 500 2 ALA A 91 -178.39 50.15
REMARK 500 2 SER A 93 95.88 -41.74
REMARK 500 2 LEU A 94 -157.05 -68.88
REMARK 500 2 CYS A 97 -72.78 -79.56
REMARK 500 2 THR A 98 74.48 49.77
REMARK 500 2 CYS A 99 -64.92 -138.14
REMARK 500 2 SER A 102 -151.83 -135.64
REMARK 500 2 ASP A 103 109.79 62.23
REMARK 500
REMARK 500 THIS ENTRY HAS 593 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 0.25 SIDE CHAIN
REMARK 500 1 ARG A 92 0.23 SIDE CHAIN
REMARK 500 1 ARG A 109 0.30 SIDE CHAIN
REMARK 500 1 ARG A 117 0.27 SIDE CHAIN
REMARK 500 1 ARG A 118 0.23 SIDE CHAIN
REMARK 500 1 ARG A 119 0.25 SIDE CHAIN
REMARK 500 1 ARG A 123 0.23 SIDE CHAIN
REMARK 500 1 ARG A 130 0.32 SIDE CHAIN
REMARK 500 1 ARG A 155 0.32 SIDE CHAIN
REMARK 500 1 ARG A 161 0.26 SIDE CHAIN
REMARK 500 1 ARG A 180 0.29 SIDE CHAIN
REMARK 500 2 ARG A 24 0.32 SIDE CHAIN
REMARK 500 2 ARG A 92 0.29 SIDE CHAIN
REMARK 500 2 ARG A 109 0.30 SIDE CHAIN
REMARK 500 2 ARG A 117 0.30 SIDE CHAIN
REMARK 500 2 ARG A 118 0.31 SIDE CHAIN
REMARK 500 2 ARG A 119 0.25 SIDE CHAIN
REMARK 500 2 ARG A 123 0.25 SIDE CHAIN
REMARK 500 2 ARG A 130 0.21 SIDE CHAIN
REMARK 500 2 ARG A 155 0.31 SIDE CHAIN
REMARK 500 2 ARG A 161 0.30 SIDE CHAIN
REMARK 500 2 ARG A 180 0.32 SIDE CHAIN
REMARK 500 3 ARG A 24 0.27 SIDE CHAIN
REMARK 500 3 ARG A 92 0.25 SIDE CHAIN
REMARK 500 3 ARG A 109 0.24 SIDE CHAIN
REMARK 500 3 ARG A 117 0.23 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 0.31 SIDE CHAIN
REMARK 500 3 ARG A 130 0.22 SIDE CHAIN
REMARK 500 3 ARG A 155 0.30 SIDE CHAIN
REMARK 500 3 ARG A 161 0.21 SIDE CHAIN
REMARK 500 3 ARG A 180 0.32 SIDE CHAIN
REMARK 500 4 ARG A 24 0.29 SIDE CHAIN
REMARK 500 4 ARG A 92 0.25 SIDE CHAIN
REMARK 500 4 ARG A 109 0.28 SIDE CHAIN
REMARK 500 4 ARG A 117 0.31 SIDE CHAIN
REMARK 500 4 ARG A 118 0.23 SIDE CHAIN
REMARK 500 4 ARG A 119 0.23 SIDE CHAIN
REMARK 500 4 ARG A 123 0.28 SIDE CHAIN
REMARK 500 4 ARG A 130 0.32 SIDE CHAIN
REMARK 500 4 ARG A 155 0.30 SIDE CHAIN
REMARK 500 4 ARG A 161 0.31 SIDE CHAIN
REMARK 500 4 ARG A 180 0.26 SIDE CHAIN
REMARK 500 5 ARG A 24 0.29 SIDE CHAIN
REMARK 500 5 ARG A 92 0.32 SIDE CHAIN
REMARK 500 5 ARG A 109 0.30 SIDE CHAIN
REMARK 500 5 ARG A 117 0.24 SIDE CHAIN
REMARK 500 5 ARG A 118 0.23 SIDE CHAIN
REMARK 500 5 ARG A 119 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 220 PLANE DEVIATIONS.
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 114.2
REMARK 620 3 CYS A 145 SG 143.4 92.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CTS
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZNB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
DBREF 1BT7 A 1 180 UNP P26663 POLG_HCVBK 1025 1204
SEQADV 1BT7 TYR A 56 UNP P26663 PHE 1080 CONFLICT
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 ZN A 301 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 VAL A 132 LEU A 135 1 4
HELIX 2 2 SER A 174 ALA A 181 1 8
SHEET 1 A 4 VAL A 33 VAL A 35 0
SHEET 2 A 4 LEU A 44 VAL A 48 -1 N ALA A 45 O GLN A 34
SHEET 3 A 4 VAL A 51 THR A 54 -1 N TRP A 53 O THR A 46
SHEET 4 A 4 VAL A 83 GLN A 86 -1 N TRP A 85 O CYS A 52
SHEET 1 B 5 ASP A 103 VAL A 107 0
SHEET 2 B 5 VAL A 113 GLY A 120 -1 N VAL A 116 O LEU A 104
SHEET 3 B 5 ARG A 123 LEU A 126 -1 N SER A 125 O ARG A 117
SHEET 4 B 5 ALA A 166 PRO A 171 -1 N VAL A 167 O GLY A 124
SHEET 5 B 5 GLY A 152 ALA A 156 -1 N ALA A 156 O ASP A 168
LINK SG CYS A 97 ZN ZN A 301 1555 1555 2.29
LINK SG CYS A 99 ZN ZN A 301 1555 1555 2.31
LINK SG CYS A 145 ZN ZN A 301 1555 1555 2.30
SITE 1 CTS 3 HIS A 57 ASP A 81 SER A 139
SITE 1 ZNB 3 CYS A 97 CYS A 99 CYS A 145
SITE 1 AC1 4 CYS A 97 CYS A 99 CYS A 145 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 - b 16 2 Bytes