Header list of 1y3k.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 25-NOV-04 1Y3K TITLE SOLUTION STRUCTURE OF THE APO FORM OF THE FIFTH DOMAIN OF MENKES TITLE 2 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: COPPER-TRANSPORTING ATPASE 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FIFTH DOMAIN OF THE MENKES PROTEIN; COMPND 5 SYNONYM: MENKES PROTEIN, COPPER PUMP 1, MENKES DISEASE-ASSOCIATED COMPND 6 PROTEIN; COMPND 7 EC: 3.6.3.4; COMPND 8 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; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET20B(+) KEYWDS FERRODOXIN-LIKE FOLD, BETA-ALPHA-BETA-BETA-ALPHA-BETA STRUCTURE, KEYWDS 2 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL GENOMICS, KEYWDS 3 HYDROLASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR L.BANCI,C.T.CHASAPIS,S.CIOFI-BAFFONI,N.HADJILIADIS,A.ROSATO, AUTHOR 2 STRUCTURAL PROTEOMICS IN EUROPE (SPINE) REVDAT 3 02-MAR-22 1Y3K 1 REMARK SEQADV REVDAT 2 24-FEB-09 1Y3K 1 VERSN REVDAT 1 08-MAR-05 1Y3K 0 JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,C.T.CHASAPIS, JRNL AUTH 2 N.HADJILIADIS,A.ROSATO JRNL TITL AN NMR STUDY OF THE INTERACTION BETWEEN THE HUMAN COPPER(I) JRNL TITL 2 CHAPERONE AND THE SECOND AND FIFTH METAL-BINDING DOMAINS OF JRNL TITL 3 THE MENKES PROTEIN JRNL REF FEBS J. V. 272 865 2005 JRNL REFN ISSN 1742-464X JRNL PMID 15670166 JRNL DOI 10.1111/J.1742-4658.2004.04526.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.1, 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 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS AND DIHEDRAL ANGLE RESTRAINTS. REMARK 4 REMARK 4 1Y3K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-DEC-04. REMARK 100 THE DEPOSITION ID IS D_1000031071. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 50MM SODIUM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM MNK5 DOMAIN U-15N,13C; 50MM REMARK 210 PHOSPHATE BUFFER NA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HCCH-TOCSY; REMARK 210 HNHA; CBCANH; CBCA(CO)NH; HNCO; REMARK 210 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.1, NEASY, DYANA REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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 SER A 2 83.02 52.77 REMARK 500 1 CYS A 14 47.02 -79.50 REMARK 500 1 ALA A 15 -95.03 18.69 REMARK 500 1 VAL A 36 103.74 -160.73 REMARK 500 1 ALA A 37 41.44 -151.66 REMARK 500 1 MET A 39 -54.38 -24.29 REMARK 500 1 ALA A 50 -62.23 -136.95 REMARK 500 1 GLN A 53 127.86 77.10 REMARK 500 2 THR A 13 -64.50 -19.14 REMARK 500 2 CYS A 14 -174.23 -174.24 REMARK 500 2 ALA A 15 -70.40 -51.75 REMARK 500 2 CYS A 17 -34.76 -175.25 REMARK 500 2 GLU A 29 78.46 -68.63 REMARK 500 2 VAL A 36 81.63 -156.03 REMARK 500 2 ALA A 37 47.22 -142.18 REMARK 500 2 MET A 39 -46.16 -28.35 REMARK 500 2 ALA A 50 -70.28 -137.52 REMARK 500 2 GLN A 53 126.85 84.68 REMARK 500 2 GLU A 63 -31.98 -39.65 REMARK 500 3 CYS A 14 66.47 -113.97 REMARK 500 3 ALA A 15 -73.91 57.72 REMARK 500 3 SER A 16 25.45 -152.63 REMARK 500 3 ARG A 27 -71.29 -90.92 REMARK 500 3 GLU A 28 -153.71 44.66 REMARK 500 3 VAL A 36 82.96 -162.32 REMARK 500 3 ALA A 50 -61.85 -145.25 REMARK 500 3 GLN A 53 118.48 69.86 REMARK 500 3 ASN A 73 -47.62 -157.42 REMARK 500 4 THR A 10 55.36 -93.31 REMARK 500 4 CYS A 17 -54.09 -136.61 REMARK 500 4 GLU A 22 -79.81 -49.67 REMARK 500 4 GLU A 29 84.05 -65.74 REMARK 500 4 VAL A 36 91.31 -160.83 REMARK 500 4 ALA A 37 48.71 -148.09 REMARK 500 4 ALA A 50 -47.05 -146.46 REMARK 500 4 GLN A 53 128.21 79.31 REMARK 500 4 ASN A 73 85.41 57.56 REMARK 500 4 ILE A 74 177.45 57.08 REMARK 500 5 SER A 2 147.04 77.74 REMARK 500 5 ALA A 15 -46.08 71.26 REMARK 500 5 SER A 16 -89.20 -147.67 REMARK 500 5 CYS A 17 -77.06 57.84 REMARK 500 5 GLU A 28 123.74 -33.89 REMARK 500 5 GLU A 29 76.84 -66.59 REMARK 500 5 ALA A 37 49.67 -146.69 REMARK 500 5 ALA A 50 -69.09 -147.44 REMARK 500 5 GLN A 53 115.50 71.67 REMARK 500 5 ILE A 74 -167.12 52.22 REMARK 500 6 SER A 2 102.64 14.97 REMARK 500 6 ALA A 15 -57.36 -16.28 REMARK 500 REMARK 500 THIS ENTRY HAS 216 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 ASN A 1 SER A 2 6 136.35 REMARK 500 ASN A 1 SER A 2 9 -144.39 REMARK 500 ASN A 1 SER A 2 13 142.03 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 0.16 SIDE CHAIN REMARK 500 1 ARG A 62 0.10 SIDE CHAIN REMARK 500 1 PHE A 66 0.11 SIDE CHAIN REMARK 500 2 TYR A 47 0.11 SIDE CHAIN REMARK 500 3 TYR A 47 0.07 SIDE CHAIN REMARK 500 4 TYR A 32 0.07 SIDE CHAIN REMARK 500 5 TYR A 6 0.09 SIDE CHAIN REMARK 500 5 TYR A 47 0.09 SIDE CHAIN REMARK 500 6 TYR A 32 0.07 SIDE CHAIN REMARK 500 8 ARG A 23 0.09 SIDE CHAIN REMARK 500 9 TYR A 47 0.09 SIDE CHAIN REMARK 500 11 TYR A 47 0.12 SIDE CHAIN REMARK 500 12 TYR A 6 0.07 SIDE CHAIN REMARK 500 14 TYR A 6 0.07 SIDE CHAIN REMARK 500 15 TYR A 6 0.10 SIDE CHAIN REMARK 500 15 TYR A 47 0.08 SIDE CHAIN REMARK 500 15 ARG A 62 0.09 SIDE CHAIN REMARK 500 17 TYR A 6 0.11 SIDE CHAIN REMARK 500 18 TYR A 6 0.07 SIDE CHAIN REMARK 500 18 TYR A 47 0.07 SIDE CHAIN REMARK 500 20 ARG A 26 0.09 SIDE CHAIN REMARK 500 20 TYR A 47 0.13 SIDE CHAIN REMARK 500 20 ARG A 62 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1Y3J RELATED DB: PDB REMARK 900 THE SAME PROTEIN WITH COPPER(I) REMARK 900 RELATED ID: CIRMMP26 RELATED DB: TARGETDB DBREF 1Y3K A 1 73 UNP Q04656 ATP7A_HUMAN 486 558 SEQADV 1Y3K ILE A 74 UNP Q04656 CLONING ARTIFACT SEQADV 1Y3K GLU A 75 UNP Q04656 CLONING ARTIFACT SEQADV 1Y3K GLY A 76 UNP Q04656 CLONING ARTIFACT SEQADV 1Y3K ARG A 77 UNP Q04656 CLONING ARTIFACT SEQRES 1 A 77 ASN SER SER LYS CYS TYR ILE GLN VAL THR GLY MET THR SEQRES 2 A 77 CYS ALA SER CYS VAL ALA ASN ILE GLU ARG ASN LEU ARG SEQRES 3 A 77 ARG GLU GLU GLY ILE TYR SER ILE LEU VAL ALA LEU MET SEQRES 4 A 77 ALA GLY LYS ALA GLU VAL ARG TYR ASN PRO ALA VAL ILE SEQRES 5 A 77 GLN PRO PRO MET ILE ALA GLU PHE ILE ARG GLU LEU GLY SEQRES 6 A 77 PHE GLY ALA THR VAL ILE GLU ASN ILE GLU GLY ARG HELIX 1 1 ALA A 15 ARG A 27 1 13 HELIX 2 2 ALA A 37 GLY A 41 5 5 HELIX 3 3 GLN A 53 GLU A 63 1 11 SHEET 1 A 3 ALA A 43 TYR A 47 0 SHEET 2 A 3 SER A 3 VAL A 9 -1 N CYS A 5 O VAL A 45 SHEET 3 A 3 ALA A 68 GLU A 72 -1 O ILE A 71 N TYR A 6 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