Header list of 1s6o.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 26-JAN-04 1S6O TITLE SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE APO-FORM OF THE SECOND TITLE 2 METAL-BINDING DOMAIN OF THE MENKES PROTEIN ATP7A COMPND MOL_ID: 1; COMPND 2 MOLECULE: COPPER-TRANSPORTING ATPASE 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SECOND SOLUBLE DOMAIN; COMPND 5 SYNONYM: COPPER PUMP 1, MENKES 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: ATP7A, MNK, MC1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET20B+ KEYWDS COPPER HOMEOSTASIS, METAL TRANSPORT, MENKES, STRUCTURAL PROTEOMICS IN KEYWDS 2 EUROPE, SPINE, STRUCTURAL GENOMICS, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR L.BANCI,I.BERTINI,R.DEL CONTE,M.D'ONOFRIO,A.ROSATO,STRUCTURAL AUTHOR 2 PROTEOMICS IN EUROPE (SPINE) REVDAT 3 02-MAR-22 1S6O 1 REMARK SEQADV REVDAT 2 24-FEB-09 1S6O 1 VERSN REVDAT 1 06-APR-04 1S6O 0 JRNL AUTH L.BANCI,I.BERTINI,R.DEL CONTE,M.D'ONOFRIO,A.ROSATO JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE CU(I) AND JRNL TITL 2 APO FORMS OF THE SECOND METAL-BINDING DOMAIN OF THE MENKES JRNL TITL 3 PROTEIN ATP7A. JRNL REF BIOCHEMISTRY V. 43 3396 2004 JRNL REFN ISSN 0006-2960 JRNL PMID 15035611 JRNL DOI 10.1021/BI036042S REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5 REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1S6O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-04. REMARK 100 THE DEPOSITION ID IS D_1000021434. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : PHOSPHATE 100 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN, PH 7; 1 MM PROTEIN REMARK 210 U-15N, PH 7; 1 MM PROTEIN U-15N, REMARK 210 13C, PH 7 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : [1H-1H]-NOESY; 13C-NOESY-HSQC; REMARK 210 15N-NOESY-HSQC; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : RESTRAINED ENERGY MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 THR A 13 24.13 46.92 REMARK 500 1 SER A 16 21.20 -149.67 REMARK 500 1 THR A 18 -78.01 -121.30 REMARK 500 1 HIS A 50 -57.26 -149.36 REMARK 500 1 VAL A 54 -60.21 72.28 REMARK 500 1 LYS A 71 -61.01 -98.57 REMARK 500 2 THR A 13 24.13 46.92 REMARK 500 2 SER A 16 21.20 -149.67 REMARK 500 2 THR A 18 -78.01 -121.30 REMARK 500 2 HIS A 50 -57.26 -149.36 REMARK 500 2 VAL A 54 -60.21 72.28 REMARK 500 2 LYS A 71 -61.01 -98.57 REMARK 500 3 VAL A 9 60.32 -115.05 REMARK 500 3 CYS A 14 -81.48 -77.39 REMARK 500 3 HIS A 15 130.90 -170.62 REMARK 500 3 THR A 18 -69.61 -135.59 REMARK 500 3 LEU A 38 -67.93 -95.87 REMARK 500 3 GLN A 41 18.82 55.06 REMARK 500 3 HIS A 50 -57.00 -139.58 REMARK 500 3 VAL A 54 -65.74 71.13 REMARK 500 3 LYS A 71 -73.21 -78.52 REMARK 500 4 CYS A 14 122.51 68.00 REMARK 500 4 HIS A 15 103.48 -47.85 REMARK 500 4 SER A 16 -64.49 -170.03 REMARK 500 4 THR A 18 -75.71 -136.09 REMARK 500 4 GLN A 29 108.00 -54.69 REMARK 500 4 HIS A 50 -62.28 -146.84 REMARK 500 4 VAL A 54 -59.63 68.64 REMARK 500 4 ALA A 68 -169.24 -108.79 REMARK 500 4 LYS A 71 -94.46 -73.22 REMARK 500 5 GLU A 2 84.10 7.23 REMARK 500 5 THR A 13 -33.03 -132.84 REMARK 500 5 SER A 16 -85.29 -168.39 REMARK 500 5 THR A 18 -80.26 -132.55 REMARK 500 5 GLN A 29 106.06 -56.54 REMARK 500 5 PRO A 49 75.06 -69.43 REMARK 500 5 HIS A 50 -54.55 -140.52 REMARK 500 5 VAL A 54 -56.69 74.02 REMARK 500 5 LYS A 71 -77.77 -88.03 REMARK 500 6 VAL A 9 71.01 -116.30 REMARK 500 6 THR A 13 -170.59 50.78 REMARK 500 6 CYS A 14 156.20 65.40 REMARK 500 6 HIS A 15 39.52 -79.73 REMARK 500 6 SER A 16 108.14 -171.00 REMARK 500 6 CYS A 17 53.44 178.82 REMARK 500 6 THR A 18 -73.52 -130.54 REMARK 500 6 GLN A 29 107.98 -57.97 REMARK 500 6 ASP A 39 -65.05 67.54 REMARK 500 6 HIS A 50 -57.64 -140.01 REMARK 500 6 SER A 53 31.05 -81.57 REMARK 500 REMARK 500 THIS ENTRY HAS 299 RAMACHANDRAN OUTLIERS. 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 3 TYR A 47 0.12 SIDE CHAIN REMARK 500 3 PHE A 69 0.08 SIDE CHAIN REMARK 500 5 TYR A 47 0.10 SIDE CHAIN REMARK 500 7 TYR A 47 0.17 SIDE CHAIN REMARK 500 8 TYR A 47 0.18 SIDE CHAIN REMARK 500 9 TYR A 47 0.12 SIDE CHAIN REMARK 500 11 TYR A 47 0.09 SIDE CHAIN REMARK 500 15 TYR A 47 0.07 SIDE CHAIN REMARK 500 16 TYR A 47 0.14 SIDE CHAIN REMARK 500 17 TYR A 47 0.13 SIDE CHAIN REMARK 500 18 TYR A 47 0.07 SIDE CHAIN REMARK 500 19 TYR A 47 0.09 SIDE CHAIN REMARK 500 20 TYR A 47 0.15 SIDE CHAIN REMARK 500 22 TYR A 47 0.14 SIDE CHAIN REMARK 500 23 TYR A 47 0.14 SIDE CHAIN REMARK 500 24 TYR A 47 0.10 SIDE CHAIN REMARK 500 25 TYR A 47 0.09 SIDE CHAIN REMARK 500 26 TYR A 47 0.16 SIDE CHAIN REMARK 500 28 TYR A 47 0.08 SIDE CHAIN REMARK 500 29 TYR A 47 0.15 SIDE CHAIN REMARK 500 30 TYR A 47 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1S6O RELATED DB: PDB REMARK 900 CU(I) FORM OF THE SECOND METAL-BINDING DOMAIN OF THE MENKES PROTEIN REMARK 900 ATP7A REMARK 900 RELATED ID: CIRMMP25 RELATED DB: TARGETDB DBREF 1S6O A 1 72 UNP Q04656 ATP7A_HUMAN 169 240 SEQADV 1S6O ILE A 73 UNP Q04656 CLONING ARTIFACT SEQADV 1S6O GLU A 74 UNP Q04656 CLONING ARTIFACT SEQADV 1S6O GLY A 75 UNP Q04656 CLONING ARTIFACT SEQADV 1S6O ARG A 76 UNP Q04656 CLONING ARTIFACT SEQRES 1 A 76 GLY GLU VAL VAL LEU LYS MET LYS VAL GLU GLY MET THR SEQRES 2 A 76 CYS HIS SER CYS THR SER THR ILE GLU GLY LYS ILE GLY SEQRES 3 A 76 LYS LEU GLN GLY VAL GLN ARG ILE LYS VAL SER LEU ASP SEQRES 4 A 76 ASN GLN GLU ALA THR ILE VAL TYR GLN PRO HIS LEU ILE SEQRES 5 A 76 SER VAL GLU GLU MET LYS LYS GLN ILE GLU ALA MET GLY SEQRES 6 A 76 PHE PRO ALA PHE VAL LYS LYS ILE GLU GLY ARG HELIX 1 1 THR A 18 GLY A 26 1 9 HELIX 2 2 GLU A 55 GLY A 65 1 11 SHEET 1 A 4 VAL A 31 SER A 37 0 SHEET 2 A 4 GLU A 42 TYR A 47 -1 O THR A 44 N LYS A 35 SHEET 3 A 4 VAL A 3 LYS A 8 -1 N VAL A 3 O TYR A 47 SHEET 4 A 4 PHE A 69 VAL A 70 -1 O PHE A 69 N LYS A 8 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