Header list of 2aw0.pdb file
Complete list - v 29 2 Bytes
HEADER COPPER TRANSPORT 08-OCT-97 2AW0
TITLE FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE,
TITLE 2 NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MENKES COPPER-TRANSPORTING ATPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FOURTH METAL-BINDING DOMAIN;
COMPND 5 EC: 3.6.1.36;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: AG(I)-BOUND STATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COPPER-TRANSPORTING ATPASE, COPPER-BINDING DOMAIN, HYDROLASE, COPPER
KEYWDS 2 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.GITSCHIER,W.J.FAIRBROTHER
REVDAT 3 29-NOV-17 2AW0 1 REMARK HELIX
REVDAT 2 24-FEB-09 2AW0 1 VERSN
REVDAT 1 14-JAN-98 2AW0 0
JRNL AUTH J.GITSCHIER,B.MOFFAT,D.REILLY,W.I.WOOD,W.J.FAIRBROTHER
JRNL TITL SOLUTION STRUCTURE OF THE FOURTH METAL-BINDING DOMAIN FROM
JRNL TITL 2 THE MENKES COPPER-TRANSPORTING ATPASE.
JRNL REF NAT.STRUCT.BIOL. V. 5 47 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9437429
JRNL DOI 10.1038/NSB0198-47
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : MSI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2AW0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177786.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2QF_COSY; TOCSY (30 AND 70 MS);
REMARK 210 NOESY(100 AND 200 MS); ROESY(40
REMARK 210 MS); COSY-35
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DGII, DISCOVER
REMARK 210 METHOD USED : DISTANCE GEOMETRY/ SIMULATED
REMARK 210 ANNEALING/RESTRAINED MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESIDUAL RESTRAINT
REMARK 210 VIOLATION ENERGIES
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 1 LYS A 32 -102.60 -119.95
REMARK 500 2 LYS A 32 -98.30 -114.24
REMARK 500 3 LYS A 32 -103.47 -99.68
REMARK 500 4 LYS A 32 -105.65 -121.12
REMARK 500 4 SER A 71 45.69 -90.31
REMARK 500 5 LYS A 32 -105.09 -90.03
REMARK 500 6 LYS A 32 -96.88 -96.92
REMARK 500 6 SER A 71 47.89 -141.20
REMARK 500 7 LYS A 32 -100.97 -115.67
REMARK 500 8 LYS A 32 -100.67 -111.48
REMARK 500 9 LYS A 32 -96.42 -116.67
REMARK 500 10 LYS A 32 -98.70 -119.37
REMARK 500 11 LYS A 32 -102.41 -98.02
REMARK 500 12 LYS A 32 -109.44 -118.39
REMARK 500 13 LYS A 32 -95.33 -117.63
REMARK 500 14 LYS A 32 -98.10 -107.25
REMARK 500 15 LYS A 32 -103.06 -119.22
REMARK 500 16 LYS A 32 -101.50 -101.20
REMARK 500 17 LYS A 32 -94.28 -112.91
REMARK 500 18 LYS A 32 -94.48 -105.44
REMARK 500 19 LYS A 32 -102.85 -120.73
REMARK 500 20 LYS A 32 -99.62 -111.47
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 AG A 73 AG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 CYS A 17 SG 171.5
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AG A 73
DBREF 2AW0 A 1 72 UNP Q04656 ATP7A_HUMAN 375 446
SEQRES 1 A 72 LEU THR GLN GLU THR VAL ILE ASN ILE ASP GLY MET THR
SEQRES 2 A 72 CYS ASN SER CYS VAL GLN SER ILE GLU GLY VAL ILE SER
SEQRES 3 A 72 LYS LYS PRO GLY VAL LYS SER ILE ARG VAL SER LEU ALA
SEQRES 4 A 72 ASN SER ASN GLY THR VAL GLU TYR ASP PRO LEU LEU THR
SEQRES 5 A 72 SER PRO GLU THR LEU ARG GLY ALA ILE GLU ASP MET GLY
SEQRES 6 A 72 PHE ASP ALA THR LEU SER ASP
HET AG A 73 1
HETNAM AG SILVER ION
FORMUL 2 AG AG 1+
HELIX 1 HA SER A 16 SER A 26 1 11
HELIX 2 HB PRO A 54 MET A 64 1 11
SHEET 1 S1 4 VAL A 31 SER A 37 0
SHEET 2 S1 4 ASN A 42 TYR A 47 -1 N ASN A 42 O SER A 37
SHEET 3 S1 4 GLN A 3 ASP A 10 -1 N GLN A 3 O TYR A 47
SHEET 4 S1 4 ASP A 67 LEU A 70 -1 N ASP A 67 O ASP A 10
LINK AG AG A 73 SG CYS A 14 1555 1555 2.49
LINK AG AG A 73 SG CYS A 17 1555 1555 2.49
SITE 1 AC1 4 THR A 13 CYS A 14 SER A 16 CYS A 17
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
MODEL 1
Complete list - v 29 2 Bytes