HEADER OXYGEN TRANSPORT 23-JUN-93 3SDH 3SDH 2 COMPND HEMOGLOBIN I (HOMODIMER) (CARBON-MONOXY) 3SDH 3 SOURCE ARK CLAM (SCAPHARCA INAEQUIVALVIS) 3SDH 4 AUTHOR W.E.ROYER *JUNIOR 3SDH 5 REVDAT 2 15-OCT-94 3SDHA 1 JRNL 3SDHA 1 REVDAT 1 31-OCT-93 3SDH 0 3SDH 6 SPRSDE 15-OCT-93 3SDH 1SDH 3SDH 7 JRNL AUTH W.E.ROYER JUNIOR 3SDH 8 JRNL TITL HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF A 3SDH 9 JRNL TITL 2 COOPERATIVE DIMERIC HEMOGLOBIN 3SDH 10 JRNL REF J.MOL.BIOL. V. 235 657 1994 3SDHA 2 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 0070 3SDHA 3 REMARK 1 3SDH 13 REMARK 1 REFERENCE 1 3SDH 14 REMARK 1 AUTH W.E.ROYER JUNIOR,W.A.HENDRICKSON,E.CHIANCONE 3SDH 15 REMARK 1 TITL STRUCTURAL TRANSITIONS UPON LIGAND BINDING IN A 3SDH 16 REMARK 1 TITL 2 COOPERATIVE DIMERIC HEMOGLOBIN 3SDH 17 REMARK 1 REF SCIENCE V. 249 518 1990 3SDH 18 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 038 3SDH 19 REMARK 1 REFERENCE 2 3SDH 20 REMARK 1 AUTH W.E.ROYER JUNIOR,W.A.HENDRICKSON,E.CHIANCONE 3SDH 21 REMARK 1 TITL THE 2.4 ANGSTROMS CRYSTAL STRUCTURE OF SCAPHARCA 3SDH 22 REMARK 1 TITL 2 DIMERIC HEMOGLOBIN. COOPERATIVELY BASED ON 3SDH 23 REMARK 1 TITL 3 DIRECTLY COMMUNICATING HEMES AT A NOVEL SUBUNIT 3SDH 24 REMARK 1 TITL 4 INTERFACE 3SDH 25 REMARK 1 REF J.BIOL.CHEM. V. 264 21052 1989 3SDH 26 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 3SDH 27 REMARK 2 3SDH 28 REMARK 2 RESOLUTION. 1.4 ANGSTROMS. 3SDH 29 REMARK 3 3SDH 30 REMARK 3 REFINEMENT. 3SDH 31 REMARK 3 PROGRAM 1 X-PLOR 3SDH 32 REMARK 3 AUTHORS 1 BRUNGER 3SDH 33 REMARK 3 PROGRAM 2 PROLSQ 3SDH 34 REMARK 3 AUTHORS 2 KONNERT,HENDRICKSON 3SDH 35 REMARK 3 R VALUE 0.159 3SDH 36 REMARK 3 RMSD BOND DISTANCES 0.017 ANGSTROMS 3SDH 37 REMARK 3 RMSD BOND ANGLES 0.9 DEGREES 3SDH 38 REMARK 4 3SDH 39 REMARK 4 THE COORDINATES FOR THE DEOXY STRUCTURE OF THIS MOLECULE 3SDH 40 REMARK 4 ARE AVAILABLE FROM THE PROTEIN DATA BANK AS A SEPARATE 3SDH 41 REMARK 4 ENTRY. 3SDH 42 REMARK 5 3SDH 43 REMARK 5 THERE ARE ALTERNATE CONFORMATIONS INCLUDED FOR SIDE CHAINS 3SDH 44 REMARK 5 OF THE FOLLOWING RESIDUES: A 3, A 4, A 16, A 25, A 36, 3SDH 45 REMARK 5 A 93, A 113, B 13, B 15, B 19, B 25, B 36, B 59, B 64, 3SDH 46 REMARK 5 B 93, AND B 110. 3SDH 47 REMARK 6 3SDH 48 REMARK 6 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 3SDH 49 REMARK 6 YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO 3SDH 50 REMARK 6 CHAIN *B*. 3SDH 51 REMARK 7 3SDH 52 REMARK 7 STRUCTURE FACTORS CORRESPONDING TO THIS ENTRY ARE AVAILABLE 3SDH 53 REMARK 7 FROM THE PROTEIN DATA BANK AS A SEPARATE ENTRY. 3SDH 54 REMARK 8 3SDHA 4 REMARK 8 CORRECTION. UPDATE JRNL REFERENCE TO REFLECT PUBLICATION. 3SDHA 5 REMARK 8 15-OCT-94. 3SDHA 6 SEQRES 1 A 146 PRO SER VAL TYR ASP ALA ALA ALA GLN LEU THR ALA ASP 3SDH 55 SEQRES 2 A 146 VAL LYS LYS ASP LEU ARG ASP SER TRP LYS VAL ILE GLY 3SDH 56 SEQRES 3 A 146 SER ASP LYS LYS GLY ASN GLY VAL ALA LEU MET THR THR 3SDH 57 SEQRES 4 A 146 LEU PHE ALA ASP ASN GLN GLU THR ILE GLY TYR PHE LYS 3SDH 58 SEQRES 5 A 146 ARG LEU GLY ASN VAL SER GLN GLY MET ALA ASN ASP LYS 3SDH 59 SEQRES 6 A 146 LEU ARG GLY HIS SER ILE THR LEU MET TYR ALA LEU GLN 3SDH 60 SEQRES 7 A 146 ASN PHE ILE ASP GLN LEU ASP ASN PRO ASP ASP LEU VAL 3SDH 61 SEQRES 8 A 146 CYS VAL VAL GLU LYS PHE ALA VAL ASN HIS ILE THR ARG 3SDH 62 SEQRES 9 A 146 LYS ILE SER ALA ALA GLU PHE GLY LYS ILE ASN GLY PRO 3SDH 63 SEQRES 10 A 146 ILE LYS LYS VAL LEU ALA SER LYS ASN PHE GLY ASP LYS 3SDH 64 SEQRES 11 A 146 TYR ALA ASN ALA TRP ALA LYS LEU VAL ALA VAL VAL GLN 3SDH 65 SEQRES 12 A 146 ALA ALA LEU 3SDH 66 SEQRES 1 B 146 PRO SER VAL TYR ASP ALA ALA ALA GLN LEU THR ALA ASP 3SDH 67 SEQRES 2 B 146 VAL LYS LYS ASP LEU ARG ASP SER TRP LYS VAL ILE GLY 3SDH 68 SEQRES 3 B 146 SER ASP LYS LYS GLY ASN GLY VAL ALA LEU MET THR THR 3SDH 69 SEQRES 4 B 146 LEU PHE ALA ASP ASN GLN GLU THR ILE GLY TYR PHE LYS 3SDH 70 SEQRES 5 B 146 ARG LEU GLY ASN VAL SER GLN GLY MET ALA ASN ASP LYS 3SDH 71 SEQRES 6 B 146 LEU ARG GLY HIS SER ILE THR LEU MET TYR ALA LEU GLN 3SDH 72 SEQRES 7 B 146 ASN PHE ILE ASP GLN LEU ASP ASN PRO ASP ASP LEU VAL 3SDH 73 SEQRES 8 B 146 CYS VAL VAL GLU LYS PHE ALA VAL ASN HIS ILE THR ARG 3SDH 74 SEQRES 9 B 146 LYS ILE SER ALA ALA GLU PHE GLY LYS ILE ASN GLY PRO 3SDH 75 SEQRES 10 B 146 ILE LYS LYS VAL LEU ALA SER LYS ASN PHE GLY ASP LYS 3SDH 76 SEQRES 11 B 146 TYR ALA ASN ALA TRP ALA LYS LEU VAL ALA VAL VAL GLN 3SDH 77 SEQRES 12 B 146 ALA ALA LEU 3SDH 78 HET HEM A 1 45 PROTOPORPHYRIN IX CONTAINS FE(II) AND CO 3SDH 79 HET HEM B 1 45 PROTOPORPHYRIN IX CONTAINS FE(II) AND CO 3SDH 80 FORMUL 3 HEM 2(C34 H32 N4 O4 FE1 ++ .) 3SDH 81 FORMUL 3 HEM 2(C1 O1) 3SDH 82 FORMUL 4 HOH *265(H2 O1) 3SDH 83 HELIX 1 PRA VAL A 3 GLN A 9 1 1ST TURN-ALPHA, 2ND TURN 3/10 3SDH 84 HELIX 2 AA ALA A 12 ILE A 25 1 3SDH 85 HELIX 3 BA LYS A 29 ASP A 43 1 3SDH 86 HELIX 4 CA GLN A 45 TYR A 50 5 3SDH 87 HELIX 5 EA ASP A 64 ASP A 82 1 3SDH 88 HELIX 6 FA PRO A 87 THR A 103 1 3SDH 89 HELIX 7 GA ALA A 108 SER A 124 1 KINK AT PRO 117 3SDH 90 HELIX 8 HA ASP A 129 ALA A 144 1 3SDH 91 HELIX 9 PRB VAL B 3 GLN B 9 1 1ST TURN-ALPHA, 2ND TURN 3/10 3SDH 92 HELIX 10 AB ALA B 12 ILE B 25 1 3SDH 93 HELIX 11 BB LYS B 29 ASP B 43 1 3SDH 94 HELIX 12 CB GLN B 45 TYR B 50 5 3SDH 95 HELIX 13 EB ASP B 64 ASP B 82 1 3SDH 96 HELIX 14 FB PRO B 87 THR B 103 1 3SDH 97 HELIX 15 GB ALA B 108 SER B 124 1 KINK AT PRO 117 3SDH 98 HELIX 16 HB ASP B 129 ALA B 144 1 3SDH 99 CRYST1 93.250 43.980 83.500 90.00 122.03 90.00 C 2 8 3SDH 100 ORIGX1 1.000000 0.000000 0.000000 0.00000 3SDH 101 ORIGX2 0.000000 1.000000 0.000000 0.00000 3SDH 102 ORIGX3 0.000000 0.000000 1.000000 0.00000 3SDH 103 SCALE1 0.010724 0.000000 0.006709 0.00000 3SDH 104 SCALE2 0.000000 0.022738 0.000000 0.00000 3SDH 105 SCALE3 0.000000 0.000000 0.014127 0.00000 3SDH 106 MTRIX1 1 -0.336300 -0.269500 -0.902400 60.83000 1 3SDH 107 MTRIX2 1 -0.257800 -0.895300 0.363400 2.57000 1 3SDH 108 MTRIX3 1 -0.905800 0.354800 0.231600 43.88000 1 3SDH 109