Header list of 2ew9.pdb file
Complete list - r 9 2 Bytes
HEADER HYDROLASE 02-NOV-05 2EW9
TITLE SOLUTION STRUCTURE OF APOWLN5-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER-TRANSPORTING ATPASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 486-633;
COMPND 5 SYNONYM: COPPER PUMP 2, WILSON DISEASE-ASSOCIATED PROTEIN;
COMPND 6 EC: 3.6.3.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ATP7B, PWD, WC1, WND;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET24D+
KEYWDS COPPER TRAFFICKING, FERRODOXIN-LIKE FOLD, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 31
MDLTYP MINIMIZED AVERAGE
AUTHOR S.CIOFI-BAFFONI,STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 09-MAR-22 2EW9 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2EW9 1 VERSN
REVDAT 1 16-MAY-06 2EW9 0
JRNL AUTH D.ACHILA,L.BANCI,I.BERTINI,J.BUNCE,S.CIOFI-BAFFONI,
JRNL AUTH 2 D.L.HUFFMAN
JRNL TITL STRUCTURE OF HUMAN WILSON PROTEIN DOMAINS 5 AND 6 AND THEIR
JRNL TITL 2 INTERPLAY WITH DOMAIN 4 AND THE COPPER CHAPERONE HAH1 IN
JRNL TITL 3 COPPER UPTAKE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 5729 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16571664
JRNL DOI 10.1073/PNAS.0504472103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, AMBER 5.0
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2900 RESTRAINTS, 2623 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 173
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 104 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS
REMARK 4
REMARK 4 2EW9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035169.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 100 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM APOWLN5-6 U-13C,15N, 100 MM
REMARK 210 PHOSPHATE BUFFER, 90% H2O, 10%
REMARK 210 D2O; 2MM APOWLN5-6 U-15N, 100 MM
REMARK 210 PHOSPHATE BUFFER, 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 2D
REMARK 210 NOESY; 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ; 600 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, CARA, DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 31
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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 MET A 13 75.01 50.92
REMARK 500 1 CYS A 15 -74.66 133.60
REMARK 500 1 SER A 17 0.47 -153.56
REMARK 500 1 ALA A 30 -117.07 -168.96
REMARK 500 1 LEU A 33 51.93 -143.54
REMARK 500 1 GLU A 73 -43.78 166.45
REMARK 500 1 ALA A 76 -97.31 -172.84
REMARK 500 1 SER A 78 -116.91 -144.90
REMARK 500 1 THR A 90 37.68 -159.94
REMARK 500 1 GLU A 127 -44.71 -163.56
REMARK 500 1 LEU A 147 105.81 -33.07
REMARK 500 2 MET A 13 80.66 54.25
REMARK 500 2 CYS A 15 -79.50 74.79
REMARK 500 2 ALA A 16 -87.22 4.83
REMARK 500 2 GLU A 29 -76.84 -74.18
REMARK 500 2 ALA A 30 -118.69 -156.74
REMARK 500 2 LEU A 33 57.01 -142.91
REMARK 500 2 PRO A 50 8.91 -69.11
REMARK 500 2 GLU A 73 7.37 98.51
REMARK 500 2 ASP A 74 65.16 -156.50
REMARK 500 2 TYR A 75 -63.28 -24.79
REMARK 500 2 ALA A 76 -71.24 -179.58
REMARK 500 2 SER A 78 -105.41 -135.34
REMARK 500 2 THR A 90 41.92 -169.82
REMARK 500 2 GLU A 127 -43.44 -162.10
REMARK 500 2 LEU A 147 119.91 -32.24
REMARK 500 2 ALA A 148 49.03 -98.56
REMARK 500 3 ALA A 2 98.79 59.79
REMARK 500 3 MET A 13 71.20 37.09
REMARK 500 3 CYS A 15 48.67 -165.87
REMARK 500 3 SER A 17 -36.97 -175.18
REMARK 500 3 ALA A 30 -125.09 -170.57
REMARK 500 3 LEU A 33 53.07 -146.86
REMARK 500 3 GLU A 73 54.72 -170.70
REMARK 500 3 ASP A 74 64.93 11.23
REMARK 500 3 ALA A 76 -103.49 93.79
REMARK 500 3 SER A 78 -61.11 -162.74
REMARK 500 3 THR A 90 44.65 -162.50
REMARK 500 3 THR A 109 -39.21 -131.53
REMARK 500 3 GLU A 127 -52.88 -147.11
REMARK 500 3 LEU A 147 -70.56 -158.30
REMARK 500 3 ALA A 148 80.09 40.68
REMARK 500 4 CYS A 15 -61.76 74.58
REMARK 500 4 ALA A 16 -72.69 -21.15
REMARK 500 4 SER A 17 10.88 -157.51
REMARK 500 4 ALA A 30 -133.99 -168.47
REMARK 500 4 LEU A 33 49.65 -140.82
REMARK 500 4 VAL A 52 -45.85 -131.87
REMARK 500 4 GLU A 73 -58.85 174.84
REMARK 500 4 TYR A 75 28.58 -68.70
REMARK 500
REMARK 500 THIS ENTRY HAS 448 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 33 SER A 34 2 149.04
REMARK 500 ALA A 76 GLY A 77 13 -148.46
REMARK 500 GLY A 80 ASN A 81 23 -140.94
REMARK 500 ALA A 76 GLY A 77 26 144.93
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 48 0.13 SIDE CHAIN
REMARK 500 1 TYR A 75 0.15 SIDE CHAIN
REMARK 500 2 TYR A 48 0.07 SIDE CHAIN
REMARK 500 3 TYR A 110 0.17 SIDE CHAIN
REMARK 500 4 TYR A 48 0.07 SIDE CHAIN
REMARK 500 4 TYR A 110 0.12 SIDE CHAIN
REMARK 500 5 PHE A 7 0.13 SIDE CHAIN
REMARK 500 5 TYR A 48 0.08 SIDE CHAIN
REMARK 500 6 TYR A 75 0.21 SIDE CHAIN
REMARK 500 6 PHE A 124 0.08 SIDE CHAIN
REMARK 500 7 TYR A 75 0.10 SIDE CHAIN
REMARK 500 8 TYR A 110 0.08 SIDE CHAIN
REMARK 500 9 TYR A 75 0.08 SIDE CHAIN
REMARK 500 9 ARG A 104 0.12 SIDE CHAIN
REMARK 500 10 PHE A 7 0.08 SIDE CHAIN
REMARK 500 10 TYR A 75 0.13 SIDE CHAIN
REMARK 500 11 TYR A 75 0.15 SIDE CHAIN
REMARK 500 11 TYR A 110 0.07 SIDE CHAIN
REMARK 500 11 ARG A 132 0.09 SIDE CHAIN
REMARK 500 12 TYR A 110 0.08 SIDE CHAIN
REMARK 500 14 PHE A 7 0.10 SIDE CHAIN
REMARK 500 14 TYR A 110 0.07 SIDE CHAIN
REMARK 500 15 TYR A 75 0.23 SIDE CHAIN
REMARK 500 15 TYR A 110 0.12 SIDE CHAIN
REMARK 500 16 TYR A 75 0.13 SIDE CHAIN
REMARK 500 17 TYR A 48 0.09 SIDE CHAIN
REMARK 500 17 TYR A 75 0.15 SIDE CHAIN
REMARK 500 18 PHE A 7 0.08 SIDE CHAIN
REMARK 500 18 TYR A 48 0.10 SIDE CHAIN
REMARK 500 18 TYR A 75 0.07 SIDE CHAIN
REMARK 500 19 TYR A 48 0.09 SIDE CHAIN
REMARK 500 19 TYR A 75 0.14 SIDE CHAIN
REMARK 500 19 TYR A 110 0.07 SIDE CHAIN
REMARK 500 21 TYR A 110 0.21 SIDE CHAIN
REMARK 500 22 TYR A 75 0.17 SIDE CHAIN
REMARK 500 22 TYR A 110 0.15 SIDE CHAIN
REMARK 500 23 TYR A 48 0.10 SIDE CHAIN
REMARK 500 23 TYR A 75 0.10 SIDE CHAIN
REMARK 500 24 TYR A 75 0.09 SIDE CHAIN
REMARK 500 24 TYR A 110 0.10 SIDE CHAIN
REMARK 500 25 TYR A 48 0.08 SIDE CHAIN
REMARK 500 25 TYR A 110 0.07 SIDE CHAIN
REMARK 500 26 TYR A 75 0.12 SIDE CHAIN
REMARK 500 27 TYR A 48 0.09 SIDE CHAIN
REMARK 500 28 TYR A 48 0.09 SIDE CHAIN
REMARK 500 28 TYR A 110 0.10 SIDE CHAIN
REMARK 500 29 PHE A 7 0.08 SIDE CHAIN
REMARK 500 29 TYR A 75 0.09 SIDE CHAIN
REMARK 500 30 TYR A 48 0.08 SIDE CHAIN
REMARK 500 30 TYR A 110 0.10 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 51 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2EW9 A 2 149 UNP P35670 ATP7B_HUMAN 486 633
SEQADV 2EW9 MET A 1 UNP P35670 INITIATING METHIONINE
SEQRES 1 A 149 MET ALA PRO GLN LYS CYS PHE LEU GLN ILE LYS GLY MET
SEQRES 2 A 149 THR CYS ALA SER CYS VAL SER ASN ILE GLU ARG ASN LEU
SEQRES 3 A 149 GLN LYS GLU ALA GLY VAL LEU SER VAL LEU VAL ALA LEU
SEQRES 4 A 149 MET ALA GLY LYS ALA GLU ILE LYS TYR ASP PRO GLU VAL
SEQRES 5 A 149 ILE GLN PRO LEU GLU ILE ALA GLN PHE ILE GLN ASP LEU
SEQRES 6 A 149 GLY PHE GLU ALA ALA VAL MET GLU ASP TYR ALA GLY SER
SEQRES 7 A 149 ASP GLY ASN ILE GLU LEU THR ILE THR GLY MET THR CYS
SEQRES 8 A 149 ALA SER CYS VAL HIS ASN ILE GLU SER LYS LEU THR ARG
SEQRES 9 A 149 THR ASN GLY ILE THR TYR ALA SER VAL ALA LEU ALA THR
SEQRES 10 A 149 SER LYS ALA LEU VAL LYS PHE ASP PRO GLU ILE ILE GLY
SEQRES 11 A 149 PRO ARG ASP ILE ILE LYS ILE ILE GLU GLU ILE GLY PHE
SEQRES 12 A 149 HIS ALA SER LEU ALA GLN
HELIX 1 1 SER A 17 LYS A 28 1 12
HELIX 2 2 GLN A 54 GLY A 66 1 13
HELIX 3 3 CYS A 91 THR A 105 1 15
HELIX 4 4 GLY A 130 GLY A 142 1 13
SHEET 1 A 4 VAL A 35 ALA A 38 0
SHEET 2 A 4 LYS A 43 TYR A 48 -1 O GLU A 45 N LEU A 36
SHEET 3 A 4 GLN A 4 LYS A 11 -1 N LEU A 8 O ALA A 44
SHEET 4 A 4 GLU A 68 VAL A 71 -1 O GLU A 68 N LYS A 11
SHEET 1 B 4 TYR A 110 ALA A 114 0
SHEET 2 B 4 LYS A 119 LYS A 123 -1 O LYS A 119 N ALA A 114
SHEET 3 B 4 ASN A 81 THR A 87 -1 N ILE A 82 O VAL A 122
SHEET 4 B 4 HIS A 144 SER A 146 -1 O HIS A 144 N THR A 87
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 - r 9 2 Bytes