Header list of 1fvq.pdb file
Complete list - 23 202 Bytes
HEADER HYDROLASE 20-SEP-00 1FVQ
TITLE SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE
TITLE 2 APO AND CU(I) LOADED STATES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER-TRANSPORTING ATPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CCC2A DOMAIN;
COMPND 5 EC: 3.6.1.36;
COMPND 6 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDLHV021
KEYWDS APO-CCC2A, HYDROLASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR L.BANCI,I.BERTINI,S.CIOFI BAFFONI,D.L.HUFFMAN,T.V.O'HALLORAN
REVDAT 4 23-FEB-22 1FVQ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1FVQ 1 VERSN
REVDAT 2 01-APR-03 1FVQ 1 JRNL
REVDAT 1 14-MAR-01 1FVQ 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,D.L.HUFFMAN,T.V.O'HALLORAN
JRNL TITL SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN
JRNL TITL 2 CCC2A IN THE APO AND CU(I)-LOADED STATES.
JRNL REF J.BIOL.CHEM. V. 276 8415 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11083871
JRNL DOI 10.1074/JBC.M008389200
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: 1960 MEANINGFUL NOES, 35 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS COUPLINGS
REMARK 4
REMARK 4 1FVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000011940.
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 : 2.2MM APO-CCC2A(15N); 100MM
REMARK 210 PHOSPHATE BUFFER NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D NOESY-15N HMQC;
REMARK 210 HNHA; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, DIANA, 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 : 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 THR A 12 22.04 -146.74
REMARK 500 LEU A 27 -73.79 -63.84
REMARK 500 LYS A 28 -69.74 -172.07
REMARK 500 VAL A 38 -65.93 -125.25
REMARK 500 ASP A 71 52.95 -113.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FVS RELATED DB: PDB
REMARK 900 1FVS CONTAINS THE SAME PROTEIN IN THE COPPER STATE.
DBREF 1FVQ A 1 72 UNP P38995 ATU2_YEAST 1 72
SEQADV 1FVQ ALA A 1 UNP P38995 MET 1 EXPRESSION TAG
SEQRES 1 A 72 ALA ARG GLU VAL ILE LEU ALA VAL HIS GLY MET THR CYS
SEQRES 2 A 72 SER ALA CYS THR ASN THR ILE ASN THR GLN LEU ARG ALA
SEQRES 3 A 72 LEU LYS GLY VAL THR LYS CYS ASP ILE SER LEU VAL THR
SEQRES 4 A 72 ASN GLU CYS GLN VAL THR TYR ASP ASN GLU VAL THR ALA
SEQRES 5 A 72 ASP SER ILE LYS GLU ILE ILE GLU ASP CYS GLY PHE ASP
SEQRES 6 A 72 CYS GLU ILE LEU ARG ASP SER
HELIX 1 1 CYS A 13 ALA A 26 1 14
HELIX 2 2 THR A 51 GLY A 63 1 13
SHEET 1 A 4 VAL A 30 CYS A 33 0
SHEET 2 A 4 GLU A 41 TYR A 46 -1 O THR A 45 N THR A 31
SHEET 3 A 4 ARG A 2 VAL A 8 -1 N ARG A 2 O TYR A 46
SHEET 4 A 4 CYS A 66 ARG A 70 -1 O GLU A 67 N ALA A 7
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 - 23 202 Bytes