Header list of 1q8l.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 21-AUG-03 1Q8L
TITLE SECOND METAL BINDING DOMAIN OF THE MENKES ATPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER-TRANSPORTING ATPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SECOND COPPER BINDING DOMAIN (RESIDUES 164-246);
COMPND 5 SYNONYM: COPPER PUMP 1, MENKES DISEASE-ASSOCIATED PROTEIN;
COMPND 6 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: ATP7A OR MNK OR MC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET29-A
KEYWDS METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.E.JONES,N.L.DALY,P.A.COBINE,D.J.CRAIK,C.T.DAMERON
REVDAT 3 02-MAR-22 1Q8L 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Q8L 1 VERSN
REVDAT 1 20-JAN-04 1Q8L 0
JRNL AUTH C.E.JONES,N.L.DALY,P.A.COBINE,D.J.CRAIK,C.T.DAMERON
JRNL TITL STRUCTURE AND METAL BINDING STUDIES OF THE SECOND COPPER
JRNL TITL 2 BINDING DOMAIN OF THE MENKES ATPASE.
JRNL REF J.STRUCT.BIOL. V. 143 209 2003
JRNL REFN ISSN 1047-8477
JRNL PMID 14572476
JRNL DOI 10.1016/J.JSB.2003.08.008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUGNER A. T
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Q8L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000020052.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 30MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM MNKR2, U-15N, 20MM
REMARK 210 POTASSIUM PHOSPHATE, 10 MM
REMARK 210 SODIUM CHLORIDE, PH6.5.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; DQF-COSY; 3D_
REMARK 210 15N-SEPERATED_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, XEASY 3.2
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 6 PHE A 72 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 ALA A 4 -94.53 -163.56
REMARK 500 1 GLN A 5 79.01 -105.73
REMARK 500 1 ALA A 6 -56.89 -121.45
REMARK 500 1 MET A 18 -78.78 61.68
REMARK 500 1 THR A 19 -48.26 -133.99
REMARK 500 1 CYS A 20 53.35 -173.16
REMARK 500 1 CYS A 23 -87.19 -145.85
REMARK 500 1 THR A 24 -8.79 52.58
REMARK 500 1 GLN A 38 -77.22 -93.36
REMARK 500 1 ASP A 45 -86.47 56.59
REMARK 500 1 GLN A 47 52.18 33.87
REMARK 500 1 GLU A 48 95.66 -67.48
REMARK 500 1 PRO A 55 40.14 -85.71
REMARK 500 1 HIS A 56 16.06 -151.07
REMARK 500 1 PHE A 72 75.09 -118.92
REMARK 500 1 LYS A 78 94.88 -60.91
REMARK 500 2 SER A 2 -33.09 -144.71
REMARK 500 2 MET A 18 101.56 44.48
REMARK 500 2 HIS A 21 -121.10 -163.88
REMARK 500 2 CYS A 23 26.93 -146.00
REMARK 500 2 GLN A 38 -81.97 -95.81
REMARK 500 2 LEU A 44 1.56 -67.31
REMARK 500 2 ASN A 46 71.93 54.35
REMARK 500 2 HIS A 56 23.46 -154.17
REMARK 500 2 LYS A 77 -92.02 -32.18
REMARK 500 2 LYS A 78 -81.53 58.61
REMARK 500 2 LEU A 83 76.75 -155.41
REMARK 500 3 SER A 2 -51.89 -158.03
REMARK 500 3 MET A 18 -144.66 63.34
REMARK 500 3 THR A 19 -40.41 -172.83
REMARK 500 3 CYS A 23 36.84 -85.15
REMARK 500 3 GLU A 28 -70.36 -59.96
REMARK 500 3 GLN A 38 -83.22 -94.76
REMARK 500 3 ASP A 45 87.96 -62.19
REMARK 500 3 PRO A 55 38.36 -87.18
REMARK 500 3 HIS A 56 18.46 -156.23
REMARK 500 3 PHE A 75 89.52 -69.13
REMARK 500 3 GLN A 79 66.31 -172.31
REMARK 500 4 SER A 2 92.06 56.76
REMARK 500 4 MET A 3 -170.70 58.22
REMARK 500 4 ALA A 6 -47.44 -153.83
REMARK 500 4 GLU A 8 -176.96 41.73
REMARK 500 4 MET A 18 -114.46 58.54
REMARK 500 4 THR A 19 -43.01 177.15
REMARK 500 4 GLN A 38 -78.19 -95.63
REMARK 500 4 ASP A 45 -103.96 57.72
REMARK 500 4 GLN A 47 80.64 32.16
REMARK 500 4 HIS A 56 19.66 -156.96
REMARK 500 4 LYS A 77 133.19 71.60
REMARK 500 4 LYS A 78 165.13 65.08
REMARK 500
REMARK 500 THIS ENTRY HAS 272 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AW0 RELATED DB: PDB
REMARK 900 FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER TRANSPORTING
REMARK 900 ATPASE.
DBREF 1Q8L A 2 84 UNP Q04656 ATP7A_HUMAN 164 246
SEQADV 1Q8L GLY A 1 UNP Q04656 CLONING ARTIFACT
SEQRES 1 A 84 GLY SER MET ALA GLN ALA GLY GLU VAL VAL LEU LYS MET
SEQRES 2 A 84 LYS VAL GLU GLY MET THR CYS HIS SER CYS THR SER THR
SEQRES 3 A 84 ILE GLU GLY LYS ILE GLY LYS LEU GLN GLY VAL GLN ARG
SEQRES 4 A 84 ILE LYS VAL SER LEU ASP ASN GLN GLU ALA THR ILE VAL
SEQRES 5 A 84 TYR GLN PRO HIS LEU ILE SER VAL GLU GLU MET LYS LYS
SEQRES 6 A 84 GLN ILE GLU ALA MET GLY PHE PRO ALA PHE VAL LYS LYS
SEQRES 7 A 84 GLN PRO LYS TYR LEU LYS
HELIX 1 1 THR A 24 LYS A 33 1 10
HELIX 2 2 SER A 59 MET A 70 1 12
SHEET 1 A 4 VAL A 37 VAL A 42 0
SHEET 2 A 4 GLU A 48 TYR A 53 -1 O THR A 50 N LYS A 41
SHEET 3 A 4 VAL A 9 VAL A 15 -1 N VAL A 9 O TYR A 53
SHEET 4 A 4 ALA A 74 PHE A 75 -1 O PHE A 75 N LYS A 14
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 2 2 Bytes