HEADER CALCIUM-BINDING PROTEIN 23-AUG-95 1TNW 1TNW 2 COMPND MOL_ID: 1; 1TNW 3 COMPND 2 MOLECULE: TROPONIN C; 1TNW 4 COMPND 3 CHAIN: NULL; 1TNW 5 COMPND 4 ENGINEERED: YES; 1TNW 6 COMPND 5 MUTATION: T130I 1TNW 7 SOURCE MOL_ID: 1; 1TNW 8 SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; 1TNW 9 SOURCE 3 ORGANISM_COMMON: CHICKEN; 1TNW 10 SOURCE 4 TISSUE: SKELETAL MUSCLE; 1TNW 11 SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; 1TNW 12 SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET3A-TNC 1TNW 13 KEYWDS EF-HAND 1TNW 14 EXPDTA NMR, 23 STRUCTURES 1TNW 15 AUTHOR C.M.SLUPSKY,B.D.SYKES 1TNW 16 REVDAT 1 15-OCT-95 1TNW 0 1TNW 17 JRNL AUTH C.M.SLUPSKY,B.D.SYKES 1TNW 18 JRNL TITL NMR SOLUTION STRUCTURE OF CALCIUM SATURATED 1TNW 19 JRNL TITL 2 SKELETAL MUSCLE TROPONIN C 1TNW 20 JRNL REF TO BE PUBLISHED 1TNW 21 JRNL REFN 0353 1TNW 22 REMARK 1 1TNW 23 REMARK 1 REFERENCE 1 1TNW 24 REMARK 1 AUTH C.M.SLUPSKY,F.C.REINACH,L.B.SMILLIE,B.D.SYKES 1TNW 25 REMARK 1 TITL SOLUTION SECONDARY STRUCTURE OF CALCIUM SATURATED 1TNW 26 REMARK 1 TITL 2 TROPONIN C MONOMER DETERMINED BY MULTIDIMENSIONAL 1TNW 27 REMARK 1 TITL 3 HETERONUCLEAR NMR SPECTROSCOPY 1TNW 28 REMARK 1 REF PROTEIN SCI. V. 4 1279 1995 1TNW 29 REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 0795 1TNW 30 REMARK 1 REFERENCE 2 1TNW 31 REMARK 1 AUTH C.M.SLUPSKY,C.M.KAY,F.C.REINACH,L.B.SMILLIE, 1TNW 32 REMARK 1 AUTH 2 B.D.SYKES 1TNW 33 REMARK 1 TITL CALCIUM-INDUCED DIMERIZATION OF TROPONIN C: MODE OF 1TNW 34 REMARK 1 TITL 2 INTERACTION AND USE OF TRIFLUOROETHANOL AS A 1TNW 35 REMARK 1 TITL 3 DENATURANT OF QUATERNARY STRUCTURE 1TNW 36 REMARK 1 REF BIOCHEMISTRY V. 34 7365 1995 1TNW 37 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1TNW 38 REMARK 2 1TNW 39 REMARK 2 RESOLUTION. NOT APPLICABLE. SEE REMARK 4. 1TNW 40 REMARK 3 1TNW 41 REMARK 3 REFINEMENT. 1TNW 42 REMARK 3 PROGRAM X-PLOR 3.1 1TNW 43 REMARK 3 AUTHORS BRUNGER 1TNW 44 REMARK 3 1TNW 45 REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1TNW 46 REMARK 3 NUMBER OF PROTEIN ATOMS 2471 1TNW 47 REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1TNW 48 REMARK 3 NUMBER OF HETEROGEN ATOMS 0 1TNW 49 REMARK 3 NUMBER OF SOLVENT ATOMS 0 1TNW 50 REMARK 3 1TNW 51 REMARK 3 SIMULATED ANNEALING USING NMR-DERIVED RESTRAINTS 1TNW 52 REMARK 3 AND X-PLOR 3.0 1TNW 53 REMARK 3 RMSD (RESIDUES 10-80) 1TNW 54 REMARK 3 BACKBONE HEAVY ATOMS - 0.66 + OR - 0.17 ANGSTROMS 1TNW 55 REMARK 3 ALL NON-HYDROGEN ATOMS - 1.07 + OR - 0.14 ANGSTROMS 1TNW 56 REMARK 3 RMSD (RESIDUES 98-155) 1TNW 57 REMARK 3 BACKBONE HEAVY ATOMS - 0.69 + OR - 0.18 ANGSTROMS 1TNW 58 REMARK 3 ALL NON-HYDROGEN ATOMS - 1.17 + OR - 0.16 ANGSTROMS 1TNW 59 REMARK 3 1TNW 60 REMARK 3 THE STRUCTURES WERE CALCULATED USING SIMULATED ANNEALING 1TNW 61 REMARK 3 (X-PLOR). 1TNW 62 REMARK 4 1TNW 63 REMARK 4 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION 1TNW 64 REMARK 4 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT 1TNW 65 REMARK 4 *CRYST1* AND *SCALE* RECORDS BE INCLUDED, BUT THE VALUES ON 1TNW 66 REMARK 4 THESE RECORDS ARE MEANINGLESS. 1TNW 67 REMARK 5 1TNW 68 REMARK 5 COMPND 1TNW 69 REMARK 5 PH 7.0; TEMPERATURE 313 K; 150 MM POTASSIUM CHLORIDE; 1TNW 70 REMARK 5 15 MM CALCIUM CHLORIDE; 15% V:V TRIFLUOROETHANOL; 1TNW 71 REMARK 5 CONCENTRATION 1.4 MM 1TNW 72 REMARK 6 1TNW 73 REMARK 6 THE TROPONIN C MOLECULE PRESENTED IN THIS ENTRY CONSISTS OF 1TNW 74 REMARK 6 TWO DOMAINS. THE N-TERMINAL DOMAIN CONTAINS RESIDUES 1 - 1TNW 75 REMARK 6 90, AND THE C-TERMINAL DOMAIN CONTAINS RESIDUES 91 - 162. 1TNW 76 REMARK 6 DUE TO SIGNIFICANT FLEXIBILITY FOR THE N-TERMINAL 4 1TNW 77 REMARK 6 RESIDUES, THE C-TERMINAL 4 RESIDUES AND 9 RESIDUES IN THE 1TNW 78 REMARK 6 LINKER BETWEEN THE TWO DOMAINS (RESIDUES 86 - 94), THESE 1TNW 79 REMARK 6 RESIDUES ARE NOT SHOWN IN THE AVERAGE STRUCTURE. THE 1TNW 80 REMARK 6 REMAINING STRUCTURES ARE SUPERIMPOSED USING THE C-TERMINAL 1TNW 81 REMARK 6 DOMAIN (RESIDUES 98 - 155) SINCE IT IS NOT POSSIBLE TO 1TNW 82 REMARK 6 ALIGN BOTH DOMAINS SIMULTANEOUSLY. ONE MAY ALSO 1TNW 83 REMARK 6 SUPERIMPOSE THE N-TERMINAL DOMAIN ONTO THE N-TERMINAL 1TNW 84 REMARK 6 DOMAIN AVERAGE STRUCTURE (RESIDUES 10 - 80). 1TNW 85 REMARK 7 1TNW 86 REMARK 7 A COMPLETE LIST OF EXPERIMENTAL CONSTRAINTS HAS BEEN 1TNW 87 REMARK 7 DEPOSITED WITH THE PROTEIN DATA BANK. 1TNW 88 REMARK 8 1TNW 89 REMARK 8 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE 1TNW 90 REMARK 8 TRACKING NUMBER: T6960, DATE REVISED: 18-SEP-95 1TNW 91 REMARK 999 1TNW 92 REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE 1TNW 93 REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1TNW 94 REMARK 999 TPCS_CHICK 1TNW 95 REMARK 999 1TNW 96 REMARK 999 SEQUENCE ADVISORY NOTICE 1TNW 97 REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1TNW 98 REMARK 999 1TNW 99 REMARK 999 SWISS-PROT ENTRY NAME: TPCS_CHICK 1TNW 100 REMARK 999 1TNW 101 REMARK 999 SWISS-PROT RESIDUE PDB SEQRES 1TNW 102 REMARK 999 1TNW 103 REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1TNW 104 REMARK 999 THR 130 ILE 130 1TNW 105 REMARK 999 1TNW 106 REMARK 999 THIS SEQUENCE DIFFERENCE IS A CLONING ARTIFACT. 1TNW 107 SEQRES 1 162 ALA SER MET THR ASP GLN GLN ALA GLU ALA ARG ALA PHE 1TNW 108 SEQRES 2 162 LEU SER GLU GLU MET ILE ALA GLU PHE LYS ALA ALA PHE 1TNW 109 SEQRES 3 162 ASP MET PHE ASP ALA ASP GLY GLY GLY ASP ILE SER THR 1TNW 110 SEQRES 4 162 LYS GLU LEU GLY THR VAL MET ARG MET LEU GLY GLN ASN 1TNW 111 SEQRES 5 162 PRO THR LYS GLU GLU LEU ASP ALA ILE ILE GLU GLU VAL 1TNW 112 SEQRES 6 162 ASP GLU ASP GLY SER GLY THR ILE ASP PHE GLU GLU PHE 1TNW 113 SEQRES 7 162 LEU VAL MET MET VAL ARG GLN MET LYS GLU ASP ALA LYS 1TNW 114 SEQRES 8 162 GLY LYS SER GLU GLU GLU LEU ALA ASN CYS PHE ARG ILE 1TNW 115 SEQRES 9 162 PHE ASP LYS ASN ALA ASP GLY PHE ILE ASP ILE GLU GLU 1TNW 116 SEQRES 10 162 LEU GLY GLU ILE LEU ARG ALA THR GLY GLU HIS VAL ILE 1TNW 117 SEQRES 11 162 GLU GLU ASP ILE GLU ASP LEU MET LYS ASP SER ASP LYS 1TNW 118 SEQRES 12 162 ASN ASN ASP GLY ARG ILE ASP PHE ASP GLU PHE LEU LYS 1TNW 119 SEQRES 13 162 MET MET GLU GLY VAL GLN 1TNW 120 HELIX 1 N GLN 6 PHE 13 1 1TNW 121 HELIX 2 A GLU 16 PHE 29 1 1TNW 122 HELIX 3 B THR 39 MET 48 1 1TNW 123 HELIX 4 C LYS 55 VAL 65 1 1TNW 124 HELIX 5 D PHE 75 ARG 84 1 1TNW 125 HELIX 6 E GLU 96 PHE 105 1 1TNW 126 HELIX 7 F ILE 115 ALA 124 1 1TNW 127 HELIX 8 G GLU 131 SER 141 1 1TNW 128 HELIX 9 H PHE 151 MET 157 1 1TNW 129 SHEET 1 S1 2 ASP 36 SER 38 0 1TNW 130 SHEET 2 S1 2 THR 72 ASP 74 -1 1TNW 131 SHEET 1 S2 2 PHE 112 ASP 114 0 1TNW 132 SHEET 2 S2 2 ARG 148 ASP 150 -1 1TNW 133 SITE 1 I 12 ASP 30 ALA 31 ASP 32 GLY 33 1TNW 134 SITE 2 I 12 GLY 34 GLY 35 ASP 36 ILE 37 1TNW 135 SITE 3 I 12 SER 38 THR 39 LYS 40 GLU 41 1TNW 136 SITE 1 II 12 ASP 66 GLU 67 ASP 68 GLY 69 1TNW 137 SITE 2 II 12 SER 70 GLY 71 THR 72 ILE 73 1TNW 138 SITE 3 II 12 ASP 74 PHE 75 GLU 76 GLU 77 1TNW 139 SITE 1 III 12 ASP 106 LYS 107 ASN 108 ALA 109 1TNW 140 SITE 2 III 12 ASP 110 GLY 111 PHE 112 ILE 113 1TNW 141 SITE 3 III 12 ASP 114 ILE 115 GLU 116 GLU 117 1TNW 142 SITE 1 IV 12 ASP 142 LYS 143 ASN 144 ASN 145 1TNW 143 SITE 2 IV 12 ASP 146 GLY 147 ARG 148 ILE 149 1TNW 144 SITE 3 IV 12 ASP 150 PHE 151 ASP 152 GLU 153 1TNW 145 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 1TNW 146 ORIGX1 1.000000 0.000000 0.000000 0.00000 1TNW 147 ORIGX2 0.000000 1.000000 0.000000 0.00000 1TNW 148 ORIGX3 0.000000 0.000000 1.000000 0.00000 1TNW 149 SCALE1 1.000000 0.000000 0.000000 0.00000 1TNW 150 SCALE2 0.000000 1.000000 0.000000 0.00000 1TNW 151 SCALE3 0.000000 0.000000 1.000000 0.00000 1TNW 152 MODEL 1 1TNW 153 (ATOM LINES ARE NOT SHOWN.) END