Header list of 1fmy.pdb file
Complete list - 23 202 Bytes
HEADER METAL BINDING PROTEIN 18-AUG-00 1FMY
TITLE HIGH RESOLUTION SOLUTION STRUCTURE OF THE PROTEIN PART OF CU7
TITLE 2 METALLOTHIONEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOTHIONEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 9 TO 48
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 STRAIN: X-2180-1AA
KEYWDS METALLOTHIONEIN, COPPER, SACCHAROMYCES CEREVISIAE, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR I.BERTINI,H.J.HARTMANN,T.KLEIN,G.LIU,C.LUCHINAT,U.WESER
REVDAT 3 23-FEB-22 1FMY 1 REMARK
REVDAT 2 24-FEB-09 1FMY 1 VERSN
REVDAT 1 13-SEP-00 1FMY 0
JRNL AUTH I.BERTINI,H.J.HARTMANN,T.KLEIN,G.LIU,C.LUCHINAT,U.WESER
JRNL TITL HIGH RESOLUTION SOLUTION STRUCTURE OF THE PROTEIN PART OF
JRNL TITL 2 CU7 METALLOTHIONEIN.
JRNL REF EUR.J.BIOCHEM. V. 267 1008 2000
JRNL REFN ISSN 0014-2956
JRNL PMID 10672009
JRNL DOI 10.1046/J.1432-1327.2000.01093.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, AMBER 5
REMARK 3 AUTHORS : BRUKER (XWINNMR), PEARLMAN, D. A., ET. AL (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 1192 NOES, OF WHICH 1048 ARE
REMARK 3 MEANINGFUL, WERE USED TO DETERMINE THE SOLUTION STRUCTURE.
REMARK 4
REMARK 4 1FMY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011725.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283; 298
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : 0.02; 0.02
REMARK 210 PRESSURE : NORMAL; NORMAL
REMARK 210 SAMPLE CONTENTS : 5MM UNENRICH METALLOTHIONEIN;
REMARK 210 18MM PHOSPHATE BUFFER; 90% H2O,
REMARK 210 10% D2O;PH=6.5; 0.03% BETA-
REMARK 210 MERCAPTOETHANOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1, DYANA 1.5, XEASY
REMARK 210 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MEAN STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 HIS A 5 -171.32 177.56
REMARK 500 GLN A 8 -0.75 53.91
REMARK 500 CYS A 9 119.89 -37.49
REMARK 500 LYS A 15 68.07 -69.67
REMARK 500 ASN A 16 -35.99 -171.38
REMARK 500 LYS A 35 52.85 -113.46
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FMY A 1 40 UNP P07215 MTCU_YEAST 9 48
SEQRES 1 A 40 GLN ASN GLU GLY HIS GLU CYS GLN CYS GLN CYS GLY SER
SEQRES 2 A 40 CYS LYS ASN ASN GLU GLN CYS GLN LYS SER CYS SER CYS
SEQRES 3 A 40 PRO THR GLY CYS ASN SER ASP ASP LYS CYS PRO CYS GLY
SEQRES 4 A 40 ASN
HELIX 1 1 ASN A 17 SER A 23 1 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