Header list of 1dsw.pdb file
Complete list - 16 20 Bytes
HEADER OXIDOREDUCTASE 10-JAN-00 1DSW TITLE THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OF HUMAN COPPER, TITLE 2 ZINC SUPEROXIDE DISMUTASE BEARING THE SAME CHARGE AS THE NATIVE TITLE 3 PROTEIN CAVEAT 1DSW ONE RESIDUE HAS INCORRECT CHIRALITY COMPND MOL_ID: 1; COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE (CU-ZN); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: M4SOD IS A MONOMERIC VARIANT OF HUMAN SOD. THE MUTANT IS COMPND 5 STUDIED IN THE REDUCED FORM, EACH MOLECULE CONTAINS A CU(I) AND A COMPND 6 ZN(II) IONS.; COMPND 7 EC: 1.15.1.1; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 OTHER_DETAILS: COPPER, ZINC SUPEROXIDE DISMUTASE (SOD) IS AN ENZYME COMPND 11 WHICH CATALYZES THE DISMUTATION OF SUPEROXIDE 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; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PBR322 KEYWDS REDUCED COPPER-ZINC-PROTEIN, BETA BARREL, SINGLE ALPHA HELIX, KEYWDS 2 OXIDOREDUCTASE EXPDTA SOLUTION NMR AUTHOR L.BANCI,I.BERTINI,R.DEL CONTE,R.FADIN,S.MANGANI,M.S.VIEZZOLI REVDAT 3 16-FEB-22 1DSW 1 REMARK REVDAT 2 24-FEB-09 1DSW 1 VERSN REVDAT 1 22-MAR-00 1DSW 0 JRNL AUTH L.BANCI,I.BERTINI,R.DEL CONTE,R.FADIN,S.MANGANI,M.S.VIEZZOLI JRNL TITL THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OF HUMAN JRNL TITL 2 COPPER,ZINC SUPEROXIDE DISMUTASE BEARING THE SAME CHARGE AS JRNL TITL 3 THE NATIVE PROTEIN. JRNL REF J.BIOL.INORG.CHEM. V. 4 795 1999 JRNL REFN ISSN 0949-8257 JRNL PMID 10631612 JRNL DOI 10.1007/S007750050353 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER 4.0 REMARK 3 AUTHORS : PEALRMAN, DA, ET AL. (1991) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: INTENSITIES OF DIPOLAR CONNECTIVITIES REMARK 3 IN 3D NOESY-HSQC, 3D HNHA AND 2D NOESY WERE MEASURED WITH THE REMARK 3 INTEGRATION ROUTINES OF THE PROGRAM XEASY. PEAK VOLUMES WERE REMARK 3 CONVERTED INTO UPPER DISTANCE LIMITS BY FOLLOWING THE REMARK 3 METHODOLOGY OF THE PROGRAM CALIBA. 3JHNHA COUPLING CONSTANTS REMARK 3 WERE OBTAINED FROM THE RATIO BETWEEN THE INTENSITY OF THE REMARK 3 DIAGONAL PEAK AND THAT OF THE CROSS PEAK OF THE 3D HNHA REMARK 3 EXPERIMENT. THE 3D STRUCTURE WAS CALCULATED WITH THE PROGRAM REMARK 3 DYANA; THE FINAL DYANA FAMILY WAS FORMED BY THE 36 CONFORMERS REMARK 3 WITH THE LOWEST TARGET FUNCTION. REFINEMENT WAS PERFORMED REMARK 3 THROUGH RESTRAINED ENERGY MINIMIZATION WITH THE SANDER MODULE OF REMARK 3 THE PROGRAM AMBER. NOESY CROSS PEAKS WERE BACK -CALCULATED ON REMARK 3 THE FINAL STRUCTURE WITH THE PROGRAM CORMA. REMARK 4 REMARK 4 1DSW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-00. REMARK 100 THE DEPOSITION ID IS D_1000010336. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.00 REMARK 210 PH : 5.00 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : ATMOSPHERIC ATM REMARK 210 SAMPLE CONTENTS : 2MM M4SOD FULLY ENRICHED IN 15N; REMARK 210 20MM PHOSPHATE BUFFER PH 5.0; 90% REMARK 210 H2O, 10% D2O. THE PROTEIN WAS REMARK 210 REDUCED WITH SODIUM ISOASCORBATE REMARK 210 UNDER UNAEROBIC CONDITIONS. REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N NOESY-HSQC; 3D HNHA; 2D REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.1, CALIBA 1.5, DYANA REMARK 210 1.4, CORMA REMARK 210 METHOD USED : THE NMR STRUCTURE CALCULATION REMARK 210 PROGRAM USED DYANA THAT USES REMARK 210 SIMULATED ANNEALING COMBINED REMARK 210 WITH MOLECULAR DYNAMICS IN REMARK 210 TORSION ANGLE SPACE (TORSION REMARK 210 ANGLE DYNAMICS) REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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: 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 GLU A 24 -169.37 -174.91 REMARK 500 GLU A 50 -77.11 -163.69 REMARK 500 GLU A 51 -44.96 62.20 REMARK 500 ALA A 55 -50.48 -120.56 REMARK 500 THR A 58 -72.16 -79.06 REMARK 500 SER A 59 43.48 -100.28 REMARK 500 PRO A 62 -175.24 -65.14 REMARK 500 LEU A 67 -80.72 -144.16 REMARK 500 LYS A 75 -53.59 -146.35 REMARK 500 VAL A 81 -49.87 171.44 REMARK 500 SER A 98 95.23 -166.31 REMARK 500 ASP A 109 -67.48 -23.31 REMARK 500 SER A 111 66.85 33.55 REMARK 500 ARG A 115 142.67 -35.83 REMARK 500 ARG A 143 70.72 52.99 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 HIS A 43 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU A 154 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 46 ND1 REMARK 620 2 HIS A 48 NE2 151.2 REMARK 620 3 HIS A 120 NE2 81.4 110.4 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 155 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 63 ND1 REMARK 620 2 HIS A 71 ND1 97.6 REMARK 620 3 HIS A 80 ND1 104.8 118.2 REMARK 620 4 ASP A 83 OD1 85.7 121.8 116.8 REMARK 620 5 ASP A 83 OD2 150.7 91.9 94.8 65.9 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 154 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155 DBREF 1DSW A 1 153 UNP P00441 SODC_HUMAN 2 154 SEQRES 1 A 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO SEQRES 2 A 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN SEQRES 3 A 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR SEQRES 4 A 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU GLU GLU ASP SEQRES 5 A 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN SEQRES 6 A 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU SEQRES 7 A 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS SEQRES 8 A 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE SEQRES 9 A 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU SEQRES 10 A 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY SEQRES 11 A 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG SEQRES 12 A 153 LEU ALA CYS GLY LYS ILE GLY LYS ALA GLN HET CU A 154 1 HET ZN A 155 1 HETNAM CU COPPER (II) ION HETNAM ZN ZINC ION FORMUL 2 CU CU 2+ FORMUL 3 ZN ZN 2+ HELIX 1 1 ASN A 131 GLY A 138 1 8 SHEET 1 A 5 VAL A 94 ASP A 101 0 SHEET 2 A 5 VAL A 29 LYS A 36 -1 N VAL A 29 O ASP A 101 SHEET 3 A 5 GLN A 15 GLN A 22 -1 O GLN A 15 N LYS A 36 SHEET 4 A 5 LYS A 3 LYS A 9 -1 O ALA A 4 N PHE A 20 SHEET 5 A 5 ILE A 149 LYS A 151 -1 N GLY A 150 O VAL A 5 SHEET 1 B 4 ASP A 83 ALA A 89 0 SHEET 2 B 4 GLY A 41 HIS A 48 -1 N GLY A 41 O ALA A 89 SHEET 3 B 4 THR A 116 VAL A 119 -1 O THR A 116 N HIS A 48 SHEET 4 B 4 ALA A 145 CYS A 146 -1 O ALA A 145 N VAL A 119 SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.05 LINK ND1 HIS A 46 CU CU A 154 1555 1555 2.13 LINK NE2 HIS A 48 CU CU A 154 1555 1555 2.01 LINK ND1 HIS A 63 ZN ZN A 155 1555 1555 2.10 LINK ND1 HIS A 71 ZN ZN A 155 1555 1555 2.10 LINK ND1 HIS A 80 ZN ZN A 155 1555 1555 2.14 LINK OD1 ASP A 83 ZN ZN A 155 1555 1555 2.03 LINK OD2 ASP A 83 ZN ZN A 155 1555 1555 1.99 LINK NE2 HIS A 120 CU CU A 154 1555 1555 2.18 SITE 1 AC1 5 HIS A 46 HIS A 48 HIS A 63 VAL A 118 SITE 2 AC1 5 HIS A 120 SITE 1 AC2 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83 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
Complete list - 16 20 Bytes