HEADER CONTRACTILE SYSTEM PROTEINS 27-MAY-88 5TNC 5TNC 3 COMPND TROPONIN-*C 5TNC 4 SOURCE TURKEY (MELEAGRIS $GALLOPAVO) SKELETAL MUSCLE 5TNC 5 AUTHOR O.HERZBERG,M.N.G.JAMES 5TNC 6 REVDAT 2 09-JAN-89 5TNCA 1 JRNL SEQRES 5TNCA 1 REVDAT 1 09-OCT-88 5TNC 0 5TNC 7 SPRSDE 09-OCT-88 5TNC 2TNC 5TNC 8 JRNL AUTH O.HERZBERG,M.N.G.JAMES 5TNC 9 JRNL TITL REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY 5TNC 10 JRNL TITL 2 SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION 5TNC 11 JRNL REF J.MOL.BIOL. V. 203 761 1988 5TNCA 2 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 5TNCA 3 REMARK 1 5TNC 14 REMARK 1 REFERENCE 1 5TNC 15 REMARK 1 AUTH O.HERZBERG,J.MOULT,M.N.G.JAMES 5TNC 16 REMARK 1 TITL MOLECULAR STRUCTURE OF TROPONIN C AND ITS 5TNC 17 REMARK 1 TITL 2 IMPLICATIONS FOR THE CA==2+== TRIGGERING OF MUSCLE 5TNC 18 REMARK 1 TITL 3 CONTRACTION 5TNC 19 REMARK 1 REF METHODS ENZYMOL. V. 139 610 1987 5TNC 20 REMARK 1 REFN ASTM MENZAU US ISSN 0076-6879 878 5TNC 21 REMARK 1 REFERENCE 2 5TNC 22 REMARK 1 AUTH O.HERZBERG,J.MOULT,M.N.G.JAMES 5TNC 23 REMARK 1 TITL CONFORMATIONAL FLEXIBILITY OF TROPONIN C 5TNC 24 REMARK 1 EDIT A.W.NORMAN,T.C.VANAMAN,A.R.MEANS 5TNC 25 REMARK 1 REF CALCIUM-*BINDING PROTEINS 312 1987 5TNC 26 REMARK 1 REF 2 IN HEALTH AND DISEASE 5TNC 27 REMARK 1 PUBL ACADEMIC PRESS, SAN DIEGO, CA 5TNC 28 REMARK 1 REFN US ISBN 0-12-521040-X 847 5TNC 29 REMARK 1 REFERENCE 3 5TNC 30 REMARK 1 AUTH O.HERZBERG,J.MOULT,M.N.G.JAMES 5TNC 31 REMARK 1 TITL CALCIUM BINDING TO SKELETAL MUSCLE TROPONIN C AND 5TNC 32 REMARK 1 TITL 2 THE REGULATION OF MUSCLE CONTRACTION 5TNC 33 REMARK 1 REF CIBA FOUND.SYMP. V. 122 120 1986 5TNC 34 REMARK 1 REFN ASTM CIBSB4 NE ISSN 0300-5208 846 5TNC 35 REMARK 1 REFERENCE 4 5TNC 36 REMARK 1 AUTH O.HERZBERG,M.N.G.JAMES 5TNC 37 REMARK 1 TITL CRYSTALLOGRAPHIC DETERMINATION OF LANTHANIDE ION 5TNC 38 REMARK 1 TITL 2 BINDING TO TROPONIN C 5TNC 39 REMARK 1 REF /FEBS$ LETT. V. 199 279 1986 5TNC 40 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 5TNC 41 REMARK 1 REFERENCE 5 5TNC 42 REMARK 1 AUTH O.HERZBERG,J.MOULT,M.N.G.JAMES 5TNC 43 REMARK 1 TITL A MODEL FOR THE CA==2+==-INDUCED CONFORMATIONAL 5TNC 44 REMARK 1 TITL 2 TRANSITION OF TROPONIN C. A TRIGGER FOR MUSCLE 5TNC 45 REMARK 1 TITL 3 CONTRACTION 5TNC 46 REMARK 1 REF J.BIOL.CHEM. V. 261 2638 1986 5TNC 47 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 5TNC 48 REMARK 1 REFERENCE 6 5TNC 49 REMARK 1 AUTH O.HERZBERG,M.N.G.JAMES 5TNC 50 REMARK 1 TITL COMMON STRUCTURAL FRAMEWORK OF THE TWO 5TNC 51 REMARK 1 TITL 2 CA==2+==(SLASH)*MG==2+== BINDING LOOPS OF TROPONIN 5TNC 52 REMARK 1 TITL 3 C AND OTHER CA==2+== BINDING PROTEINS 5TNC 53 REMARK 1 REF BIOCHEMISTRY V. 24 5298 1985 5TNC 54 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 5TNC 55 REMARK 1 REFERENCE 7 5TNC 56 REMARK 1 AUTH O.HERZBERG,M.N.G.JAMES 5TNC 57 REMARK 1 TITL STRUCTURE OF THE CALCIUM REGULATORY MUSCLE PROTEIN 5TNC 58 REMARK 1 TITL 2 TROPONIN-*C AT 2.8 ANGSTROMS RESOLUTION 5TNC 59 REMARK 1 REF NATURE V. 313 653 1985 5TNC 60 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 5TNC 61 REMARK 1 REFERENCE 8 5TNC 62 REMARK 1 AUTH O.HERZBERG,K.HAYAKAWA,M.N.G.JAMES 5TNC 63 REMARK 1 TITL CRYSTALLOGRAPHIC DATA FOR TROPONIN C FROM TURKEY 5TNC 64 REMARK 1 TITL 2 SKELETAL MUSCLE 5TNC 65 REMARK 1 REF J.MOL.BIOL. V. 172 345 1984 5TNC 66 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 5TNC 67 REMARK 1 REFERENCE 9 5TNC 68 REMARK 1 AUTH O.HERZBERG,M.N.G.JAMES 5TNC 69 REMARK 1 TITL THE CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY 5TNC 70 REMARK 1 TITL 2 SKELETAL MUSCLE AT 2.8 ANGSTROMS RESOLUTION 5TNC 71 REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 40 C37 1984 5TNC 72 REMARK 1 REFN ASTM ACACEQ DK ISSN 0108-7673 621 5TNC 73 REMARK 2 5TNC 74 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 5TNC 75 REMARK 3 5TNC 76 REMARK 3 REFINEMENT. THE STRUCTURE WAS DETERMINED AT 2.8 ANGSTROMS 5TNC 77 REMARK 3 USING THE MIR METHOD. PHASES FROM 11 HEAVY-ATOM 5TNC 78 REMARK 3 DERIVATIVES GAVE AN OVERALL FIGURE OF MERIT OF 0.90. THE 5TNC 79 REMARK 3 POLYPEPTIDE CHAIN WAS TRACED IN AGREEMENT WITH THE 5TNC 80 REMARK 3 SEQUENCE OF CHICKEN SKELETAL MUSCLE TNC (J.M.WILKINSON, 5TNC 81 REMARK 3 FEBS LETT., V. 70, P. 254, 1976). 193 CYCLES OF 5TNC 82 REMARK 3 REFINEMENT WERE CARRIED OUT AT 2.0 ANGSTROMS RESOLUTION BY 5TNC 83 REMARK 3 THE RESTRAINED LEAST SQUARES PROCEDURE OF J. KONNERT AND 5TNC 84 REMARK 3 W. HENDRICKSON (PROGRAM *PROLSQ*). THE R VALUE IS 0.155. 5TNC 85 REMARK 3 THE MEAN ERROR IN THE COORDINATES IS ESTIMATED BY THE 5TNC 86 REMARK 3 METHOD OF READ (ACTA CRYSTALLOGR., V. A42, P. 140, 1986) 5TNC 87 REMARK 3 TO BE 0.3 ANGSTROMS. 5TNC 88 REMARK 3 5TNC 89 REMARK 3 NUMBER OF PROTEIN ATOMS 1261 5TNC 90 REMARK 3 NUMBER OF CALCIUM IONS 2 5TNC 91 REMARK 3 NUMBER OF SOLVENT ATOMS 158 5TNC 92 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 5TNC 93 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 5TNC 94 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 5TNC 95 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS.) 5TNC 96 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 5TNC 97 REMARK 3 BOND DISTANCE 0.019(0.017) 5TNC 98 REMARK 3 ANGLE DISTANCE 0.045(0.028) 5TNC 99 REMARK 3 PLANAR 1-4 DISTANCE 0.049(0.034) 5TNC 100 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.012(0.015) 5TNC 101 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.198(0.140) 5TNC 102 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 5TNC 103 REMARK 3 SINGLE TORSION CONTACT 0.239(0.400) 5TNC 104 REMARK 3 MULTIPLE TORSION CONTACT 0.286(0.400) 5TNC 105 REMARK 3 POSSIBLE HYDROGEN BOND 0.283(0.400) 5TNC 106 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 5TNC 107 REMARK 3 PLANAR (OMEGA) 2.5(3.5) 5TNC 108 REMARK 4 5TNC 109 REMARK 4 THE FIRST RESIDUE OF THE AMINO ACID SEQUENCE HAS NO CLEAR 5TNC 110 REMARK 4 ELECTRON DENSITY ASSOCIATED WITH IT AND, THEREFORE, IS NOT 5TNC 111 REMARK 4 INCLUDED. THE SIDE CHAINS OF RESIDUES GLU 67 BEYOND CB AND 5TNC 112 REMARK 4 RESIDUE GLN 162 WERE ALSO NOT IDENTIFIED. 5TNC 113 REMARK 5 5TNC 114 REMARK 5 BASED ON AMINO ACID COMPOSITION AND THE ELECTRON DENSITY 5TNC 115 REMARK 5 MAP, ALA 99 IN CHICKEN TNC WAS IDENTIFIED AS GLU 99 IN 5TNC 116 REMARK 5 TURKEY TNC. 5TNC 117 REMARK 6 5TNC 118 REMARK 6 THE SIDE CHAIN OF CYS 101 HAS TWO ALTERNATE CONFORMATIONS. 5TNC 119 REMARK 7 5TNC 120 REMARK 7 TROPONIN-C HAS FOUR CA ++ BINDING SITES - I, II, III, IV. 5TNC 121 REMARK 7 TWO BIND CA ++ WITH HIGH AFFINITY (ASSOCIATION CONSTANT OF 5TNC 122 REMARK 7 APPROXIMATELY 10**7/M) AND ARE LOCATED IN THE C-TERMINAL 5TNC 123 REMARK 7 HALF OF THE MOLECULE (SITES III AND IV). TWO BIND CA ++ 5TNC 124 REMARK 7 WITH LOW AFFINITY (ASSOCIATION CONSTANT OF APPROXIMATELY 5TNC 125 REMARK 7 10**5/M) AND ARE LOCATED IN THE N-TERMINAL HALF OF THE 5TNC 126 REMARK 7 MOLECULE (SITES I AND II). IN THIS STRUCTURE ONLY THE 5TNC 127 REMARK 7 C-TERMINAL DOMAIN (SITES III AND IV) IS OCCUPIED BY CA ++ 5TNC 128 REMARK 7 IONS. 5TNC 129 REMARK 8 5TNC 130 REMARK 8 THE WATER MOLECULES ARE ARRANGED IN DESCENDING ORDER OF 5TNC 131 REMARK 8 RELIABILITY WHERE RELIABILITY IS DEFINED BY THE QUALITY 5TNC 132 REMARK 8 FACTOR OCCUPANCY**2/B (M.N.G.JAMES, A.R.SIELECKI, J.MOL. 5TNC 133 REMARK 8 BIOL., V. 163, P. 299 (1983)). THUS A QUALITY FACTOR OF 5TNC 134 REMARK 8 0.025 CORRESPONDS TO B=40.0 AND OCCUPANCY=1.0. 5TNC 135 REMARK 9 5TNCA 4 REMARK 9 CORRECTION. CORRECT TYPOGRAPHICAL ERROR ON SEQRES RECORD. 5TNCA 5 REMARK 9 UPDATE JRNL REFERENCE TO REFLECT PUBLICATION. 09-JAN-89. 5TNCA 6 SEQRES 1 162 ALA SER MET THR ASP GLN GLN ALA GLU ALA ARG ALA PHE 5TNCA 7 SEQRES 2 162 LEU SER GLU GLU MET ILE ALA GLU PHE LYS ALA ALA PHE 5TNC 137 SEQRES 3 162 ASP MET PHE ASP ALA ASP GLY GLY GLY ASP ILE SER THR 5TNC 138 SEQRES 4 162 LYS GLU LEU GLY THR VAL MET ARG MET LEU GLY GLN ASN 5TNC 139 SEQRES 5 162 PRO THR LYS GLU GLU LEU ASP ALA ILE ILE GLU GLU VAL 5TNC 140 SEQRES 6 162 ASP GLU ASP GLY SER GLY THR ILE ASP PHE GLU GLU PHE 5TNC 141 SEQRES 7 162 LEU VAL MET MET VAL ARG GLN MET LYS GLU ASP ALA LYS 5TNC 142 SEQRES 8 162 GLY LYS SER GLU GLU GLU LEU GLU ASP CYS PHE ARG ILE 5TNC 143 SEQRES 9 162 PHE ASP LYS ASN ALA ASP GLY PHE ILE ASP ILE GLU GLU 5TNC 144 SEQRES 10 162 LEU GLY GLU ILE LEU ARG ALA THR GLY GLU HIS VAL THR 5TNC 145 SEQRES 11 162 GLU GLU ASP ILE GLU ASP LEU MET LYS ASP SER ASP LYS 5TNC 146 SEQRES 12 162 ASN ASN ASP GLY ARG ILE ASP PHE ASP GLU PHE LEU LYS 5TNC 147 SEQRES 13 162 MET MET GLU GLY VAL GLN 5TNC 148 FTNOTE 1 5TNC 149 FTNOTE 1 SEE REMARK 4. 5TNC 150 FTNOTE 2 5TNC 151 FTNOTE 2 SEE REMARK 6. 5TNC 152 HET CA 163 1 CALCIUM ION IN BINDING SITE III 5TNC 153 HET CA 164 1 CALCIUM ION IN BINDING SITE IV 5TNC 154 FORMUL 2 CA 2(CA1 ++) 5TNC 155 FORMUL 3 HOH *157(H2 O1) 5TNC 156 HELIX 1 N MET 3 PHE 13 1 5TNC 157 HELIX 2 A GLU 16 MET 28 1 5TNC 158 HELIX 3 B THR 39 MET 48 1 5TNC 159 HELIX 4 C LYS 55 VAL 65 1 5TNC 160 HELIX 5 D PHE 75 MET 86 1 5TNC 161 HELIX 6 DE LYS 87 GLU 97 1 5TNC 162 HELIX 7 E LEU 98 PHE 105 1 5TNC 163 HELIX 8 F ILE 115 THR 125 1 5TNC 164 HELIX 9 G GLU 131 SER 141 1 5TNC 165 HELIX 10 H PHE 151 MET 158 1 5TNC 166 SITE 1 I 12 ASP 30 ALA 31 ASP 32 GLY 33 5TNC 167 SITE 2 I 12 GLY 34 GLY 35 ASP 36 ILE 37 5TNC 168 SITE 3 I 12 SER 38 THR 39 LYS 40 GLU 41 5TNC 169 SITE 1 II 12 ASP 66 GLU 67 ASP 68 GLY 69 5TNC 170 SITE 2 II 12 SER 70 GLY 71 THR 72 ILE 73 5TNC 171 SITE 3 II 12 ASP 74 PHE 75 GLU 76 GLU 77 5TNC 172 SITE 1 III 12 ASP 106 LYS 107 ASN 108 ALA 109 5TNC 173 SITE 2 III 12 ASP 110 GLY 111 PHE 112 ILE 113 5TNC 174 SITE 3 III 12 ASP 114 ILE 115 GLU 116 GLU 117 5TNC 175 SITE 1 IV 12 ASP 142 LYS 143 ASN 144 ASN 145 5TNC 176 SITE 2 IV 12 ASP 146 GLY 147 ARG 148 ILE 149 5TNC 177 SITE 3 IV 12 ASP 150 PHE 151 ASP 152 GLU 153 5TNC 178 CRYST1 66.550 66.550 60.910 90.00 90.00 120.00 P 32 2 1 6 5TNC 179 ORIGX1 1.000000 0.000000 0.000000 0.00000 5TNC 180 ORIGX2 0.000000 1.000000 0.000000 0.00000 5TNC 181 ORIGX3 0.000000 0.000000 1.000000 0.00000 5TNC 182 SCALE1 0.015026 0.008675 0.000000 0.00000 5TNC 183 SCALE2 0.000000 0.017351 0.000000 0.00000 5TNC 184 SCALE3 0.000000 0.000000 0.016418 0.00000 5TNC 185 (ATOM LINES ARE NOT SHOWN.) END