Header list of 1aw0.pdb file
Complete list - v 29 2 Bytes
HEADER HYDROLASE 08-OCT-97 1AW0
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: REDUCED APO 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
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.GITSCHIER,W.J.FAIRBROTHER
REVDAT 3 29-NOV-17 1AW0 1 REMARK HELIX
REVDAT 2 24-FEB-09 1AW0 1 VERSN
REVDAT 1 28-JAN-98 1AW0 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 : MOLECULAR SIMULATIONS, INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1AW0 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_1000171325.
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; 3QF-COSY; TOCSY(70 AND
REMARK 210 100 MS); NOESY(50; AND 200 MS);
REMARK 210 ROESY (40 MS); 15N-HSQC; 15N-
REMARK 210 TOCSY-HSQC(30 AND 70 MS); 15N-
REMARK 210 NOESY-HSQC(100 MS); HNHB
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 CYS A 14 163.37 77.00
REMARK 500 1 LYS A 32 -88.42 -114.29
REMARK 500 2 LYS A 32 -99.96 -106.34
REMARK 500 2 ASP A 67 96.60 -68.44
REMARK 500 3 CYS A 14 164.54 75.77
REMARK 500 3 LYS A 32 -103.69 -118.18
REMARK 500 3 SER A 71 -50.84 -121.13
REMARK 500 4 LYS A 32 -101.35 -94.38
REMARK 500 5 CYS A 14 148.78 118.85
REMARK 500 5 LYS A 32 -102.59 -89.84
REMARK 500 6 CYS A 14 -157.07 -161.00
REMARK 500 6 SER A 16 -57.25 -165.86
REMARK 500 6 LYS A 32 -102.94 -113.88
REMARK 500 7 THR A 13 -63.06 77.45
REMARK 500 7 LYS A 32 -102.09 -104.61
REMARK 500 8 THR A 13 -63.33 75.15
REMARK 500 8 LYS A 32 -101.63 -104.07
REMARK 500 9 ASN A 15 -54.05 64.85
REMARK 500 9 LYS A 32 -103.04 -95.90
REMARK 500 9 ASP A 67 92.36 -69.75
REMARK 500 10 LYS A 32 -98.67 -109.29
REMARK 500 11 CYS A 14 -164.96 -164.00
REMARK 500 11 SER A 16 -54.94 -168.72
REMARK 500 11 LYS A 32 -98.67 -116.72
REMARK 500 12 THR A 13 98.34 -63.74
REMARK 500 12 CYS A 14 169.27 71.27
REMARK 500 12 SER A 16 -54.24 -156.92
REMARK 500 12 LYS A 32 -101.83 -108.68
REMARK 500 13 CYS A 14 -171.11 55.26
REMARK 500 13 LYS A 32 -101.41 -94.56
REMARK 500 14 THR A 13 -42.23 76.47
REMARK 500 14 LYS A 32 -98.79 -106.22
REMARK 500 14 ASP A 67 97.94 -69.33
REMARK 500 14 SER A 71 46.72 -148.34
REMARK 500 15 THR A 13 10.87 -141.58
REMARK 500 15 LYS A 32 -101.87 -100.66
REMARK 500 16 CYS A 14 163.45 73.74
REMARK 500 16 SER A 16 -52.13 -162.33
REMARK 500 16 LYS A 32 -100.79 -96.82
REMARK 500 17 LYS A 32 -102.65 -93.26
REMARK 500 18 LYS A 32 -89.50 -112.80
REMARK 500 19 CYS A 14 148.47 79.92
REMARK 500 19 LYS A 32 -101.50 -91.58
REMARK 500 20 CYS A 14 -81.09 69.29
REMARK 500 20 ASN A 15 -38.73 -138.70
REMARK 500 20 LYS A 32 -105.09 -90.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 TYR A 47 0.07 SIDE CHAIN
REMARK 500 2 TYR A 47 0.06 SIDE CHAIN
REMARK 500 6 TYR A 47 0.07 SIDE CHAIN
REMARK 500 17 TYR A 47 0.06 SIDE CHAIN
REMARK 500 18 TYR A 47 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AW0 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
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 H ASN A 42 O SER A 37
SHEET 3 S1 4 GLN A 3 ASP A 10 -1 H GLN A 3 O TYR A 47
SHEET 4 S1 4 ASP A 67 LEU A 70 -1 H ASP A 67 O ASP A 10
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