Header list of 1z2g.pdb file
Complete list - 2 20 Bytes
HEADER CHAPERONE 08-MAR-05 1Z2G
TITLE SOLUTION STRUCTURE OF APO, OXIDIZED YEAST COX17
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C OXIDASE COPPER CHAPERONE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COX17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: YLL009C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PAED4
KEYWDS COPPER CHAPERONE, CYTOCHROME C OXIDASE ASSEMBLY, DISULFIDE BONDS,
KEYWDS 2 COILED COIL-HELIX-COILED COIL-HELIX DOMAIN, STRUCTURAL GENOMICS,
KEYWDS 3 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, CHAPERONE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR F.ARNESANO,E.BALATRI,L.BANCI,I.BERTINI,D.R.WINGE,STRUCTURAL
AUTHOR 2 PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 02-MAR-22 1Z2G 1 REMARK
REVDAT 2 24-FEB-09 1Z2G 1 VERSN
REVDAT 1 07-JUN-05 1Z2G 0
JRNL AUTH F.ARNESANO,E.BALATRI,L.BANCI,I.BERTINI,D.R.WINGE
JRNL TITL FOLDING STUDIES OF COX17 REVEAL AN IMPORTANT INTERPLAY OF
JRNL TITL 2 CYSTEINE OXIDATION AND COPPER BINDING
JRNL REF STRUCTURE V. 13 713 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 15893662
JRNL DOI 10.1016/J.STR.2005.02.015
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, AMBER 6
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032213.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM COX17 15N, 13C; 1MM
REMARK 210 DITHIOTHREITOL; 50MM PHOSPHATE
REMARK 210 BUFFER; PH 7
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HNHA; 2D TOCSY
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
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
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 : 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 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 ASP A 5 -78.73 -79.07
REMARK 500 LYS A 6 82.93 -64.89
REMARK 500 LYS A 7 -93.88 -122.70
REMARK 500 GLU A 9 -62.01 -104.00
REMARK 500 GLU A 15 63.56 -69.83
REMARK 500 ASP A 18 74.75 -66.61
REMARK 500 CYS A 23 166.77 74.33
REMARK 500 CYS A 24 -91.21 57.43
REMARK 500 VAL A 25 -132.46 36.29
REMARK 500 CYS A 26 35.58 -169.65
REMARK 500 ASN A 40 46.94 -158.23
REMARK 500 GLN A 42 -73.22 59.26
REMARK 500 CYS A 57 -69.92 -17.36
REMARK 500 VAL A 65 143.62 78.40
REMARK 500 ALA A 68 90.61 -169.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 43 SER A 44 -141.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U96 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF YEAST COX17 WITH COPPER BOUND
REMARK 900 RELATED ID: 1U97 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APO, REDUCED YEAST COX17
REMARK 900 RELATED ID: CIRMMP23 RELATED DB: TARGETDB
DBREF 1Z2G A 1 69 UNP Q12287 COX17_YEAST 0 68
SEQRES 1 A 69 MET THR GLU THR ASP LYS LYS GLN GLU GLN GLU ASN HIS
SEQRES 2 A 69 ALA GLU CYS GLU ASP LYS PRO LYS PRO CYS CYS VAL CYS
SEQRES 3 A 69 LYS PRO GLU LYS GLU GLU ARG ASP THR CYS ILE LEU PHE
SEQRES 4 A 69 ASN GLY GLN ASP SER GLU LYS CYS LYS GLU PHE ILE GLU
SEQRES 5 A 69 LYS TYR LYS GLU CYS MET LYS GLY TYR GLY PHE GLU VAL
SEQRES 6 A 69 PRO SER ALA ASN
HELIX 1 1 MET A 1 LYS A 6 1 6
HELIX 2 2 CYS A 26 GLY A 41 1 16
HELIX 3 3 CYS A 47 GLY A 62 1 16
SSBOND 1 CYS A 26 CYS A 57 1555 1555 2.08
SSBOND 2 CYS A 36 CYS A 47 1555 1555 2.08
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 - 2 20 Bytes