HEADER OXIDOREDUCTASE 19-FEB-92 1COB COMPND SUPEROXIDE DISMUTASE (CO SUBSTITUTED) (E.C.1.15.1.1) SOURCE BOVINE (BOS TAURUS) ERYTHROCYTES AUTHOR K.DJINOVIC,A.CODA,L.ANTOLINI,G.PELOSI,A.DESIDERI, AUTHOR 2 M.FALCONI,G.ROTILIO,M.BOLOGNESI REVDAT 1 31-OCT-93 1COB 0 JRNL AUTH K.DJINOVIC,A.CODA,L.ANTOLINI,G.PELOSI,A.DESIDERI, JRNL AUTH 2 M.FALCONI,G.ROTILIO,M.BOLOGNESI JRNL TITL CRYSTAL STRUCTURE SOLUTION AND REFINEMENT OF THE JRNL TITL 2 SEMISYNTHETIC COBALT SUBSTITUTED BOVINE JRNL TITL 3 ERYTHROCYTE ENZYME SUPEROXIDE DISMUTASE AT 2.0 JRNL TITL 4 ANGSTROMS RESOLUTION JRNL REF J.MOL.BIOL. V. 226 227 1992 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.DJINOVIC,G.GATTI,A.CODA,L.ANTOLINI,G.PELOSI, REMARK 1 AUTH 2 A.DESIDERI,M.FALCONI,F.MARMOCCHI,G.ROTILIO, REMARK 1 AUTH 3 M.BOLOGNESI REMARK 1 TITL CRYSTAL STRUCTURE OF YEAST CU,ZN SUPEROXIDE REMARK 1 TITL 2 DISMUTASE. CRYSTALLOGRAPHIC REFINEMENT AT 2.5 REMARK 1 TITL 3 ANGSTROMS RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 225 791 1992 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 2 REMARK 1 AUTH K.DJINOVIC,G.GATTI,A.CODA REMARK 1 TITL STRUCTURE SOLUTION AND MOLECULAR DYNAMICS REMARK 1 TITL 2 REFINEMENT OF THE YEAST CU,ZN ENZYME SUPEROXIDE REMARK 1 TITL 3 DISMUTASE REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 47 918 1991 REMARK 1 REFN ASTM ASBSDK DK ISSN 0108-7681 622 REMARK 1 REFERENCE 3 REMARK 1 AUTH Y.KITAGAWA,N.TANAKA,Y.HATA,M.KUSONOKI,G.LEE, REMARK 1 AUTH 2 Y.KATSUBE,K.ASADA,S.AIBARA,Y.MORITA REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF CU,ZN SUPEROXIDE REMARK 1 TITL 2 DISMUTASE FROM SPINACH AT 2.0 ANGSTROMS REMARK 1 TITL 3 RESOLUTION REMARK 1 REF J.BIOCHEM.(TOKYO) V. 109 447 1991 REMARK 1 REFN ASTM JOBIAO JA ISSN 0021-924X 418 REMARK 1 REFERENCE 4 REMARK 1 AUTH E.D.GETZOFF,J.A.TAINER,M.M.STEMPIEN,G.I.BELL, REMARK 1 AUTH 2 R.A.HALLEWELL REMARK 1 TITL EVOLUTION OF CU,ZN SUPEROXIDE DISMUTASE AND THE REMARK 1 TITL 2 GREEK-KEY B-BARREL STRUCTURAL MOTIF REMARK 1 REF PROTEINS.STRUCT.,FUNCT., V. 5 322 1989 REMARK 1 REF 2 GENET. REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 867 REMARK 1 REFERENCE 5 REMARK 1 AUTH J.A.TAINER,E.D.GETZOFF,K.M.BEEM,J.S.RICHARDSON, REMARK 1 AUTH 2 D.C.RICHARDSON REMARK 1 TITL DETERMINATION AND ANALYSIS OF THE 2 ANGSTROMS REMARK 1 TITL 2 STRUCTURE OF COPPER, ZINC SUPEROXIDE DISMUTASE REMARK 1 REF J.MOL.BIOL. V. 160 181 1982 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 2 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM 1 GROMOS REMARK 3 AUTHORS 1 VAN GUNSTEREN,BERENDSEN REMARK 3 PROGRAM 2 TNT REMARK 3 AUTHORS 2 TRONRUD,TEN EYCK,MATTHEWS REMARK 3 PROGRAM 3 FRODO REMARK 3 AUTHORS 3 JONES REMARK 3 R VALUE 0.176 REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS REMARK 3 RMSD BOND ANGLES 1.748 DEGREES REMARK 3 REMARK 3 NUMBER OF REFLECTIONS 18876 REMARK 3 RESOLUTION RANGE 10.0 - 2.0 ANGSTROMS REMARK 3 PERCENT COMPLETION 75.2 REMARK 3 REMARK 3 NUMBER OF PROTEIN ATOMS 2184 REMARK 3 NUMBER OF SOLVENT ATOMS 199 REMARK 4 REMARK 4 HELIX H1 EXTENDS TO RESIDUE 129 AND RESIDUES 136 - 138 WITH REMARK 4 B-TURNS. REMARK 5 REMARK 5 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL REMARK 5 YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED TO REMARK 5 CHAIN A. THE RMS DEVIATION OF THE CA ATOMS IS 0.282 REMARK 5 ANGSTROMS. REMARK 6 REMARK 6 STRAND 4 OF SHEETS SMA AND SMB EXTENDS FROM 141 - 146. REMARK 6 ACCORDING TO KABSCH AND SANDER CRITERIA RESIDUE 147 CANNOT REMARK 6 BE ATTRIBUTED AN EXTENDED CONFORMATION AND, THEREFORE, THE REMARK 6 BETA STRAND IS INTERRUPTED AT THIS SITE. NEVERTHELESS REMARK 6 THERE IS A HYDROGEN-BONDING INTERACTION BETWEEN RESIDUES REMARK 6 CAL 5 AND GLY 148, AS IF THE BETA STRAND ACTUALLY CONTINUED REMARK 6 FOR ONE RESIDUE AFTER 147. SEQRES 1 A 151 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO SEQRES 2 A 151 VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP THR SEQRES 3 A 151 VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU GLY SEQRES 4 A 151 ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN THR SEQRES 5 A 151 GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO LEU SEQRES 6 A 151 SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG HIS SEQRES 7 A 151 VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN GLY SEQRES 8 A 151 VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER LEU SEQRES 9 A 151 SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL VAL SEQRES 10 A 151 HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN GLU SEQRES 11 A 151 GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU ALA SEQRES 12 A 151 CYS GLY VAL ILE GLY ILE ALA LYS SEQRES 1 B 151 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO SEQRES 2 B 151 VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP THR SEQRES 3 B 151 VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU GLY SEQRES 4 B 151 ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN THR SEQRES 5 B 151 GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO LEU SEQRES 6 B 151 SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG HIS SEQRES 7 B 151 VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN GLY SEQRES 8 B 151 VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER LEU SEQRES 9 B 151 SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL VAL SEQRES 10 B 151 HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN GLU SEQRES 11 B 151 GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU ALA SEQRES 12 B 151 CYS GLY VAL ILE GLY ILE ALA LYS FTNOTE 1 FTNOTE 1 RESIDUES WITH POOR ELECTRON DENSITY: CHAIN A: LYS 3, LYS FTNOTE 1 9, GLN 15, LYS 23, LYS 73, LYS 89, ASN 90, GLU 107, TYR FTNOTE 1 108, LYS 120, LYS 151. CHAIN B: LYS 3, ASP 11, LYS 23, FTNOTE 1 ASN 51, LYS 73, LYS 89, GLU 107, LYS 151. HET CU A 152 1 COPPER ++ ION HET CO A 153 1 COBALT ++ CATION HET CU B 152 1 COPPER ++ ION HET CO B 153 1 COBALT ++ CATION FORMUL 3 CU 2(CU1 ++) FORMUL 4 CO 2(CO1 ++) FORMUL 5 HOH *199(H2 O1) HELIX 1 H1 GLU A 130 THR A 135 1 SEE REMARK 6 SHEET 1 BGA 4 LYS A 3 LEU A 8 0 SHEET 2 BGA 4 GLN A 15 LYS A 23 -1 O PHE A 20 N ALA A 4 SHEET 3 BGA 4 VAL A 27 THR A 34 -1 O VAL A 28 N GLU A 21 SHEET 4 BGA 4 ALA A 93 ASP A 99 -1 O ASP A 99 N VAL A 27 SHEET 1 SMA 5 ASP A 81 ALA A 87 0 SHEET 2 SMA 5 GLY A 39 HIS A 46 -1 N GLY A 39 O ALA A 87 SHEET 3 SMA 5 THR A 114 HIS A 118 -1 O VAL A 116 N HIS A 44 SHEET 4 SMA 5 ARG A 141 VAL A 146 -1 O GLY A 145 N MET A 115 SHEET 5 SMA 5 LYS A 3 LEU A 8 -1 SHEET 1 BGB 4 LYS B 3 LEU B 8 0 SHEET 2 BGB 4 GLN B 15 LYS B 23 -1 O PHE B 20 N ALA B 4 SHEET 3 BGB 4 VAL B 27 THR B 34 -1 O VAL B 28 N GLU B 21 SHEET 4 BGB 4 ALA B 93 ASP B 99 -1 O ASP B 99 N VAL B 27 SHEET 1 SMB 5 ASP B 81 ALA B 87 0 SHEET 2 SMB 5 GLY B 39 HIS B 46 -1 N GLY B 39 O ALA B 87 SHEET 3 SMB 5 THR B 114 HIS B 118 -1 O VAL B 116 N HIS B 44 SHEET 4 SMB 5 ARG B 141 VAL B 146 -1 O GLY B 145 N MET B 115 SHEET 5 SMB 5 LYS B 3 LEU B 8 -1 TURN 1 23A LYS A 23 THR A 26 TURN 2 D1A ASN A 51 GLY A 54 TURN 3 D2A GLN A 53 THR A 56 TURN 4 D3A GLY A 54 SER A 57 TURN 5 D4A CYS A 55 ALA A 58 TURN 6 D5A THR A 56 GLY A 59 TURN 7 Z1A ASN A 63 SER A 66 TURN 8 Z2A GLY A 71 ASP A 74 TURN 9 Z3A HIS A 78 ASP A 81 TURN 10 54A ASP A 88 GLY A 91 TURN 11 G1A GLY A 106 SER A 109 TURN 12 G2A ILE A 110 ARG A 113 TURN 13 HEA ASP A 123 ARG A 126 TURN 14 23B LYS B 23 THR B 26 TURN 15 D1B ASN B 51 GLY B 54 TURN 16 D2B GLN B 53 THR B 56 TURN 17 D3B GLY B 54 SER B 57 TURN 18 D4B CYS B 55 ALA B 58 TURN 19 D5B THR B 56 GLY B 59 TURN 20 Z1B ASN B 63 SER B 66 TURN 21 Z2B GLY B 71 ASP B 74 TURN 22 Z3B HIS B 78 ASP B 81 TURN 23 54B ASP B 88 GLY B 91 TURN 24 G1B GLY B 106 SER B 109 TURN 25 G2B ILE B 110 ARG B 113 TURN 26 HEB ASP B 123 ARG B 126 SSBOND 1 CYS A 55 CYS A 144 SSBOND 2 CYS B 55 CYS B 144 SITE 1 A 9 CU A 152 HIS A 44 HIS A 46 HIS A 61 SITE 2 A 9 HIS A 118 CO A 153 HIS A 69 HIS A 78 SITE 3 A 9 ASP A 81 SITE 1 B 9 CU B 152 HIS B 44 HIS B 46 HIS B 61 SITE 2 B 9 HIS B 118 CO B 153 HIS B 69 HIS B 78 SITE 3 B 9 ASP B 81 CRYST1 50.990 147.630 47.530 90.00 90.00 90.00 P 21 21 21 8 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 0.019612 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006774 0.000000 0.00000 SCALE3 0.000000 0.000000 0.021039 0.00000 MTRIX1 1 0.568180 -0.204340 -0.797130 27.52600 1 MTRIX2 1 -0.220220 -0.971100 0.091970 119.95300 1 MTRIX3 1 -0.792890 0.123290 -0.596760 22.21900 1