Header list of 1nm4.pdb file
Complete list - 23 20 Bytes
HEADER METAL BINDING PROTEIN 09-JAN-03 1NM4
TITLE SOLUTION STRUCTURE OF CU(I)-COPC FROM PSEUDOMONAS SYRINGAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER RESISTANCE PROTEIN C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COPC;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SYRINGAE;
SOURCE 3 ORGANISM_TAXID: 317;
SOURCE 4 GENE: COPC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET20B
KEYWDS COPPER TRAFFICKING, REDOX SWITCH, STRUCTURAL PROTEOMICS IN EUROPE,
KEYWDS 2 SPINE, STRUCTURAL GENOMICS, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR F.ARNESANO,L.BANCI,I.BERTINI,S.MANGANI,A.R.THOMPSETT,STRUCTURAL
AUTHOR 2 PROTEOMICS IN EUROPE (SPINE)
REVDAT 4 23-FEB-22 1NM4 1 REMARK
REVDAT 3 24-FEB-09 1NM4 1 VERSN
REVDAT 2 13-JAN-04 1NM4 3 JRNL ATOM
REVDAT 1 08-APR-03 1NM4 0
JRNL AUTH F.ARNESANO,L.BANCI,I.BERTINI,S.MANGANI,A.R.THOMPSETT
JRNL TITL A REDOX SWITCH IN COPC: AN INTRIGUING COPPER TRAFFICKING
JRNL TITL 2 PROTEIN THAT BINDS COPPER(I) AND COPPER(II) AT DIFFERENT
JRNL TITL 3 SITES
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 3814 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 12651950
JRNL DOI 10.1073/PNAS.0636904100
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, AMBER 6
REMARK 3 AUTHORS : CASE, KOLLMAN ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1464 MEANINGFUL NOES, 129 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS AND 34 EXPERIMENTAL HYDROGEN BONDS
REMARK 4
REMARK 4 1NM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017996.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.5 MM CU(I)-COPC 15N,13C; 100MM
REMARK 210 PHOSPHATE BUFFER NA; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, DYANA, CORMA
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS RESTRAINED ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: CU(I)-COPC WAS OBTAINED BY REDUCING CU(II)-COPC WITH ONE
REMARK 210 EQUIVALENT OF SODIUM ASCORBATE
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 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 LYS A 3 -163.62 62.63
REMARK 500 PRO A 9 -79.03 -88.19
REMARK 500 ALA A 10 43.08 175.45
REMARK 500 GLU A 11 96.67 -50.56
REMARK 500 LEU A 29 -152.86 -94.79
REMARK 500 VAL A 30 59.38 81.88
REMARK 500 THR A 31 43.18 -82.90
REMARK 500 GLN A 32 30.05 70.64
REMARK 500 PHE A 33 35.72 -144.76
REMARK 500 ASP A 89 45.92 -78.28
REMARK 500 THR A 90 -103.09 57.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M42 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APOCOPC FROM PSEUDOMONAS SYRINGAE
REMARK 900 RELATED ID: CIRMMP01 RELATED DB: TARGETDB
DBREF 1NM4 A 1 102 UNP P12376 COPC_PSESM 25 126
SEQRES 1 A 102 HIS PRO LYS LEU VAL SER SER THR PRO ALA GLU GLY SER
SEQRES 2 A 102 GLU GLY ALA ALA PRO ALA LYS ILE GLU LEU HIS PHE SER
SEQRES 3 A 102 GLU ASN LEU VAL THR GLN PHE SER GLY ALA LYS LEU VAL
SEQRES 4 A 102 MET THR ALA MET PRO GLY MET GLU HIS SER PRO MET ALA
SEQRES 5 A 102 VAL LYS ALA ALA VAL SER GLY GLY GLY ASP PRO LYS THR
SEQRES 6 A 102 MET VAL ILE THR PRO ALA SER PRO LEU THR ALA GLY THR
SEQRES 7 A 102 TYR LYS VAL ASP TRP ARG ALA VAL SER SER ASP THR HIS
SEQRES 8 A 102 PRO ILE THR GLY SER VAL THR PHE LYS VAL LYS
SHEET 1 A 4 LEU A 4 THR A 8 0
SHEET 2 A 4 ILE A 21 PHE A 25 -1 O HIS A 24 N SER A 6
SHEET 3 A 4 THR A 65 PRO A 70 -1 O ILE A 68 N ILE A 21
SHEET 4 A 4 ALA A 55 GLY A 59 -1 N ALA A 56 O THR A 69
SHEET 1 B 4 MET A 51 VAL A 53 0
SHEET 2 B 4 GLY A 35 ALA A 42 -1 N MET A 40 O MET A 51
SHEET 3 B 4 GLY A 77 SER A 87 -1 O ARG A 84 N GLY A 35
SHEET 4 B 4 THR A 90 VAL A 101 -1 O VAL A 97 N VAL A 81
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
Complete list - 23 20 Bytes