Header list of 1fd8.pdb file
Complete list - 23 20 Bytes
HEADER METAL TRANSPORT 20-JUL-00 1FD8
TITLE SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE,
TITLE 2 ATX1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATX1 COPPER CHAPERONE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ATX1;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11D
KEYWDS METALLOCHAPERONE, ATX1, HEAVY-METAL-ASSOCIATED DOMAIN, OXYGEN
KEYWDS 2 TOXICITY, METAL TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR F.ARNESANO,L.BANCI,I.BERTINI,D.L.HUFFMAN,T.V.O'HALLORAN
REVDAT 4 23-FEB-22 1FD8 1 REMARK LINK
REVDAT 3 24-FEB-09 1FD8 1 VERSN
REVDAT 2 01-APR-03 1FD8 1 JRNL
REVDAT 1 14-MAR-01 1FD8 0
JRNL AUTH F.ARNESANO,L.BANCI,I.BERTINI,D.L.HUFFMAN,T.V.O'HALLORAN
JRNL TITL SOLUTION STRUCTURE OF THE CU(I) AND APO FORMS OF THE YEAST
JRNL TITL 2 METALLOCHAPERONE, ATX1.
JRNL REF BIOCHEMISTRY V. 40 1528 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11327811
JRNL DOI 10.1021/BI0014711
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: 1184 MEANINGFUL NOES, 42 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS AND 60 1JHN RESIDUAL DIPOLAR COUPLINGS
REMARK 4
REMARK 4 1FD8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011496.
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 : 1.8MM CU(I)-ATX1 15N; 100MM
REMARK 210 PHOSPHATE BUFFER NA; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D NOESY-15N HMQC;
REMARK 210 HNHA; 2D TOCSY; 15N-1H 1J-
REMARK 210 MODULATED HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ; 400
REMARK 210 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
REMARK 210 ENERGY 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 ASP A 32 -50.06 -176.67
REMARK 500 GLN A 43 50.50 34.82
REMARK 500 ILE A 60 -70.36 -60.03
REMARK 500
REMARK 500 REMARK: NULL
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 CU1 A 74 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS A 15 N 79.7
REMARK 620 3 CYS A 18 SG 117.2 112.3
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 74
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CC8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HG(II) FORM OF ATX1 METALLOCHAPERONE
REMARK 900 PROTEIN AT 1.02 A RESOLUTION
DBREF 1FD8 A 1 73 UNP P38636 ATX1_YEAST 1 73
SEQRES 1 A 73 MET ALA GLU ILE LYS HIS TYR GLN PHE ASN VAL VAL MET
SEQRES 2 A 73 THR CYS SER GLY CYS SER GLY ALA VAL ASN LYS VAL LEU
SEQRES 3 A 73 THR LYS LEU GLU PRO ASP VAL SER LYS ILE ASP ILE SER
SEQRES 4 A 73 LEU GLU LYS GLN LEU VAL ASP VAL TYR THR THR LEU PRO
SEQRES 5 A 73 TYR ASP PHE ILE LEU GLU LYS ILE LYS LYS THR GLY LYS
SEQRES 6 A 73 GLU VAL ARG SER GLY LYS GLN LEU
HET CU1 A 74 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
HELIX 1 1 GLY A 17 GLU A 30 1 14
HELIX 2 2 PRO A 52 THR A 63 1 12
SHEET 1 A 4 LYS A 35 SER A 39 0
SHEET 2 A 4 LEU A 44 THR A 49 -1 O LEU A 44 N SER A 39
SHEET 3 A 4 LYS A 5 VAL A 11 -1 N LYS A 5 O THR A 49
SHEET 4 A 4 VAL A 67 LEU A 73 -1 N ARG A 68 O ASN A 10
LINK SG CYS A 15 CU CU1 A 74 1555 1555 2.14
LINK N CYS A 15 CU CU1 A 74 1555 1555 2.75
LINK SG CYS A 18 CU CU1 A 74 1555 1555 2.12
SITE 1 AC1 4 THR A 14 CYS A 15 CYS A 18 LYS A 65
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