Header list of 1cur.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 19-APR-96 1CUR
TITLE REDUCED RUSTICYANIN, NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CU(I) RUSTICYANIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: REDUCED RUSTICYANIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACIDITHIOBACILLUS FERROOXIDANS;
SOURCE 3 ORGANISM_TAXID: 920;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 7 OTHER_DETAILS: PART OF NMR DATA ACQUIRED WITH LABELED NATIVE
SOURCE 8 MATERIAL FROM THIOBACILLUS FERROOXIDANS, AND PART WITH RECOMBINANT
SOURCE 9 MATERIAL FROM ESCHERICHIA COLI
KEYWDS RUSTICYANIN, TYPE 1 COPPER PROTEIN, SOLUTION STRUCTURE, ELECTRON
KEYWDS 2 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR M.V.BOTUYAN,H.J.DYSON
REVDAT 4 16-FEB-22 1CUR 1 REMARK LINK
REVDAT 3 24-FEB-09 1CUR 1 VERSN
REVDAT 2 01-APR-03 1CUR 1 JRNL
REVDAT 1 08-NOV-96 1CUR 0
JRNL AUTH M.V.BOTUYAN,A.TOY-PALMER,J.CHUNG,R.C.BLAKE 2ND.,P.BEROZA,
JRNL AUTH 2 D.A.CASE,H.J.DYSON
JRNL TITL NMR SOLUTION STRUCTURE OF CU(I) RUSTICYANIN FROM
JRNL TITL 2 THIOBACILLUS FERROOXIDANS: STRUCTURAL BASIS FOR THE EXTREME
JRNL TITL 3 ACID STABILITY AND REDOX POTENTIAL.
JRNL REF J.MOL.BIOL. V. 263 752 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8947573
JRNL DOI 10.1006/JMBI.1996.0613
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.TOY-PALMER,S.PRYTULLA,H.J.DYSON
REMARK 1 TITL COMPLETE 13C ASSIGNMENTS FOR RECOMBINANT CU(I) RUSTICYANIN.
REMARK 1 TITL 2 PREDICTION OF SECONDARY STRUCTURE FROM PATTERNS OF CHEMICAL
REMARK 1 TITL 3 SHIFTS
REMARK 1 REF FEBS LETT. V. 365 35 1995
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.R.CASIMIRO,A.TOY-PALMER,R.C.BLAKE II,H.J.DYSON
REMARK 1 TITL GENE SYNTHESIS, HIGH-LEVEL EXPRESSION, AND MUTAGENESIS OF
REMARK 1 TITL 2 THIOBACILLUS FERROOXIDANS RUSTICYANIN: HIS 85 IS A LIGAND TO
REMARK 1 TITL 3 THE BLUE COPPER CENTER
REMARK 1 REF BIOCHEMISTRY V. 340 6640 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.H.HUNT,A.TOY-PALMER,N.ASSA-MUNT,J.CAVANAGH,R.C.BLAKE II,
REMARK 1 AUTH 2 H.J.DYSON
REMARK 1 TITL NUCLEAR MAGNETIC RESONANCE 15N AND 1H RESONANCE ASSIGNMENTS
REMARK 1 TITL 2 AND GLOBAL FOLD OF RUSTICYANIN
REMARK 1 REF J.MOL.BIOL. V. 244 370 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : FERGUSON,SIEBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CUR 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_1000172546.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 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 CU A 156 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 85 ND1
REMARK 620 2 CYS A 138 SG 126.9
REMARK 620 3 HIS A 143 ND1 106.7 122.2
REMARK 620 4 MET A 148 SD 87.6 95.2 108.1
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 CU A 156
DBREF 1CUR A 1 155 UNP P24930 RUS2_THIFE 1 155
SEQRES 1 A 155 GLY THR LEU ASP THR THR TRP LYS GLU ALA THR LEU PRO
SEQRES 2 A 155 GLN VAL LYS ALA MET LEU GLU LYS ASP THR GLY LYS VAL
SEQRES 3 A 155 SER GLY ASP THR VAL THR TYR SER GLY LYS THR VAL HIS
SEQRES 4 A 155 VAL VAL ALA ALA ALA VAL LEU PRO GLY PHE PRO PHE PRO
SEQRES 5 A 155 SER PHE GLU VAL HIS ASP LYS LYS ASN PRO THR LEU GLU
SEQRES 6 A 155 ILE PRO ALA GLY ALA THR VAL ASP VAL THR PHE ILE ASN
SEQRES 7 A 155 THR ASN LYS GLY PHE GLY HIS SER PHE ASP ILE THR LYS
SEQRES 8 A 155 LYS GLY PRO PRO TYR ALA VAL MET PRO VAL ILE ASP PRO
SEQRES 9 A 155 ILE VAL ALA GLY THR GLY PHE SER PRO VAL PRO LYS ASP
SEQRES 10 A 155 GLY LYS PHE GLY TYR THR ASP PHE THR TRP HIS PRO THR
SEQRES 11 A 155 ALA GLY THR TYR TYR TYR VAL CYS GLN ILE PRO GLY HIS
SEQRES 12 A 155 ALA ALA THR GLY MET PHE GLY LYS ILE VAL VAL LYS
HET CU A 156 1
HETNAM CU COPPER (II) ION
FORMUL 2 CU CU 2+
HELIX 1 1 LEU A 12 LYS A 21 1 10
HELIX 2 2 GLY A 142 GLY A 147 1 6
SHEET 1 B1 5 LYS A 8 ALA A 10 0
SHEET 2 B1 5 LYS A 119 HIS A 128 -1 O PHE A 120 N ALA A 10
SHEET 3 B1 5 ALA A 70 ASN A 78 -1 O ASN A 78 N GLY A 121
SHEET 4 B1 5 THR A 37 ALA A 44 1 N VAL A 38 O THR A 71
SHEET 5 B1 5 SER A 53 ASN A 61 -1 O GLU A 55 N ALA A 43
SHEET 1 B2 6 ALA A 107 THR A 109 0
SHEET 2 B2 6 GLY A 84 THR A 90 -1 O PHE A 87 N THR A 109
SHEET 3 B2 6 THR A 133 CYS A 138 -1 O TYR A 135 N THR A 90
SHEET 4 B2 6 PHE A 149 LYS A 155 -1 O GLY A 150 N TYR A 136
SHEET 5 B2 6 THR A 63 ILE A 66 1 O LEU A 64 N VAL A 153
SHEET 6 B2 6 GLY A 24 TYR A 33 1 O VAL A 31 N GLU A 65
LINK ND1 HIS A 85 CU CU A 156 1555 1555 2.08
LINK SG CYS A 138 CU CU A 156 1555 1555 2.16
LINK ND1 HIS A 143 CU CU A 156 1555 1555 1.90
LINK SD MET A 148 CU CU A 156 1555 1555 2.60
CISPEP 1 PHE A 51 PRO A 52 1 0.20
CISPEP 2 PRO A 94 PRO A 95 1 -5.01
CISPEP 3 PHE A 51 PRO A 52 2 -6.06
CISPEP 4 PRO A 94 PRO A 95 2 -4.49
CISPEP 5 PHE A 51 PRO A 52 3 -4.30
CISPEP 6 PRO A 94 PRO A 95 3 -2.35
CISPEP 7 PHE A 51 PRO A 52 4 -5.08
CISPEP 8 PRO A 94 PRO A 95 4 -3.95
CISPEP 9 ASP A 103 PRO A 104 4 0.02
CISPEP 10 PHE A 51 PRO A 52 5 -5.23
CISPEP 11 PRO A 94 PRO A 95 5 0.90
CISPEP 12 PHE A 51 PRO A 52 6 -4.39
CISPEP 13 PRO A 94 PRO A 95 6 -5.43
CISPEP 14 ASP A 103 PRO A 104 6 -0.92
CISPEP 15 PHE A 51 PRO A 52 7 -5.55
CISPEP 16 PRO A 94 PRO A 95 7 -5.72
CISPEP 17 ASP A 103 PRO A 104 7 1.40
CISPEP 18 PHE A 51 PRO A 52 8 -6.73
CISPEP 19 PRO A 94 PRO A 95 8 -1.58
CISPEP 20 PHE A 51 PRO A 52 9 -3.82
CISPEP 21 PRO A 94 PRO A 95 9 -3.63
CISPEP 22 PHE A 51 PRO A 52 10 -7.12
CISPEP 23 PRO A 94 PRO A 95 10 -3.25
CISPEP 24 PHE A 51 PRO A 52 11 -5.47
CISPEP 25 PRO A 94 PRO A 95 11 -5.49
CISPEP 26 ASP A 103 PRO A 104 11 -2.25
CISPEP 27 PHE A 51 PRO A 52 12 -5.53
CISPEP 28 PRO A 94 PRO A 95 12 -3.88
CISPEP 29 PHE A 51 PRO A 52 13 -6.23
CISPEP 30 PRO A 94 PRO A 95 13 -4.22
CISPEP 31 PHE A 51 PRO A 52 14 -6.85
CISPEP 32 PRO A 94 PRO A 95 14 -4.57
CISPEP 33 ASP A 103 PRO A 104 14 -6.07
CISPEP 34 PHE A 51 PRO A 52 15 -5.93
CISPEP 35 PRO A 94 PRO A 95 15 -5.69
SITE 1 AC1 4 HIS A 85 CYS A 138 HIS A 143 MET A 148
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