HEADER CALCIUM-BINDING PROTEIN 02-JUN-96 1NCY TITLE TROPONIN-C, COMPLEX WITH MANGANESE COMPND MOL_ID: 1; COMPND 2 MOLECULE: TROPONIN C; COMPND 3 CHAIN: NULL SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 TISSUE: SKELETAL MUSCLE KEYWDS MUSCLE PROTEIN, CALCIUM-BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.SUNDARALINGAM,S.T.RAO REVDAT 1 11-JAN-97 1NCY 0 JRNL AUTH S.T.RAO,K.A.SATYSHUR,M.GREASER, JRNL AUTH 2 M.SUNDARALINGAM JRNL TITL X-RAY STRUCTURES OF MN, CD, TB METAL COMPLEXES OF JRNL TITL 2 TROPONIN-C JRNL REF TO BE PUBLISHED JRNL REFN 0353 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.A.SATYSHUR,D.PYZALSKA,S.T.RAO,M.GREASER, REMARK 1 AUTH 2 M.SUNDARALINGAM REMARK 1 TITL STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN-C REMARK 1 TITL 2 AT 1.78 ANGSTROMS RESOLUTION REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 50 40 1994 REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 0766 REMARK 1 REFERENCE 2 REMARK 1 AUTH K.A.SATYSHUR,S.T.RAO,D.PYZALSKA,W.DRENDEL, REMARK 1 AUTH 2 M.GREASER,M.SUNDARALINGAM REMARK 1 TITL REFINED STRUCTURE OF CHICKEN SKELETAL MUSCLE REMARK 1 TITL 2 TROPONIN C IN THE TWO-CALCIUM STATE AT 2-A REMARK 1 TITL 3 RESOLUTION REMARK 1 REF J.BIOL.CHEM. V. 263 1628 1988 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 REMARK 1 REFERENCE 3 REMARK 1 AUTH M.SUNDARALINGAM,R.BERGSTROM,G.STRASBURG,S.T.RAO, REMARK 1 AUTH 2 P.ROYCHOWDHURY,M.GREASER,B.C.WANG REMARK 1 TITL MOLECULAR STRUCTURE OF TROPONIN C FROM CHICKEN REMARK 1 TITL 2 SKELETAL MUSCLE AT 3-ANGSTROM RESOLUTION REMARK 1 REF SCIENCE V. 227 945 1985 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038 REMARK 1 REFERENCE 4 REMARK 1 AUTH G.M.STRASBURG,M.L.GREASER,M.SUNDARALINGAM REMARK 1 TITL X-RAY DIFFRACTION STUDIES OF TROPONIN-C CRYSTALS REMARK 1 TITL 2 FROM RABBIT AND CHICKEN SKELETAL MUSCLES REMARK 1 REF J.BIOL.CHEM. V. 255 3806 1980 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 REMARK 1 REFERENCE 5 REMARK 1 AUTH J.M.WILKINSON REMARK 1 TITL THE AMINO ACID SEQUENCE OF TROPONIN C FROM CHICKEN REMARK 1 TITL 2 SKELETAL MUSCLE REMARK 1 REF FEBS LETT. V. 70 254 1976 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 0165 REMARK 2 REMARK 2 RESOLUTION. 2.1 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.1 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.0 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 6380 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.13 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1271 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 7 REMARK 3 SOLVENT ATOMS : 124 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.2 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.012 ; 0.02 REMARK 3 ANGLE DISTANCE (A) : 0.046 ; 0.04 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.004 ; 0.01 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.004 ; 0.01 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.033 ; 5.0 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 2.5 ; 5.0 REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 3.3 ; 4.0 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.6 ; 6.0 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.3 ; 4.0 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.6 ; 6.0 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1NCY COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996 REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PURDUE PACKAGE REMARK 200 DATA SCALING SOFTWARE : PURDUE PACKAGE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29532 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.8 REMARK 200 RESOLUTION RANGE LOW (A) : 8.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 69.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.05 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 Y-X,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,1/3-Z REMARK 290 6555 -X,Y-X,2/3-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866004 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866047 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.53424 REMARK 290 SMTRY1 3 -0.500000 0.866004 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866047 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 20.26712 REMARK 290 SMTRY1 4 -0.500000 0.866004 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866047 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 20.26712 REMARK 290 SMTRY1 6 -0.500000 -0.866004 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866047 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.53424 REMARK 290 REMARK 290 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 0 HOH 317 DISTANCE = 5.55 ANGSTROMS DBREF 1NCY 1 162 SWS P02588 TPCS_CHICK 1 162 SEQRES 1 162 ALA SER MET THR ASP GLN GLN ALA GLU ALA ARG ALA PHE SEQRES 2 162 LEU SER GLU GLU MET ILE ALA GLU PHE LYS ALA ALA PHE SEQRES 3 162 ASP MET PHE ASP ALA ASP GLY GLY GLY ASP ILE SER THR SEQRES 4 162 LYS GLU LEU GLY THR VAL MET ARG MET LEU GLY GLN ASN SEQRES 5 162 PRO THR LYS GLU GLU LEU ASP ALA ILE ILE GLU GLU VAL SEQRES 6 162 ASP GLU ASP GLY SER GLY THR ILE ASP PHE GLU GLU PHE SEQRES 7 162 LEU VAL MET MET VAL ARG GLN MET LYS GLU ASP ALA LYS SEQRES 8 162 GLY LYS SER GLU GLU GLU LEU ALA ASN CYS PHE ARG ILE SEQRES 9 162 PHE ASP LYS ASN ALA ASP GLY PHE ILE ASP ILE GLU GLU SEQRES 10 162 LEU GLY GLU ILE LEU ARG ALA THR GLY GLU HIS VAL THR SEQRES 11 162 GLU GLU ASP ILE GLU ASP LEU MET LYS ASP SER ASP LYS SEQRES 12 162 ASN ASN ASP GLY ARG ILE ASP PHE ASP GLU PHE LEU LYS SEQRES 13 162 MET MET GLU GLY VAL GLN HET MN 163 1 HET MN 164 1 HET SO4 225 5 HETNAM MN MANGANESE (II) ION HETNAM SO4 SULFATE ION FORMUL 2 MN 2(MN1 2+) FORMUL 3 SO4 O4 S1 2- FORMUL 4 HOH *105(H2 O1) HELIX 1 1 MET 3 PHE 13 1 11 HELIX 2 2 GLU 16 ASP 30 1 15 HELIX 3 3 THR 39 MET 48 5 10 HELIX 4 4 LYS 55 VAL 65 1 11 HELIX 5 5 PHE 75 PHE 105 1 31 HELIX 6 6 ILE 115 THR 125 1 11 HELIX 7 7 GLU 131 SER 141 1 11 HELIX 8 8 PHE 151 GLU 159 1 9 SHEET 1 A 2 ASP 36 SER 38 0 SHEET 2 A 2 THR 72 ASP 74 -1 N ILE 73 O ILE 37 LINK MN MN 163 OD1 ASP 106 LINK MN MN 163 OD1 ASN 108 LINK MN MN 163 OD1 ASP 110 LINK MN MN 163 O PHE 112 LINK MN MN 163 OE1 GLU 117 LINK MN MN 164 OD1 ASP 142 LINK MN MN 164 OD1 ASN 144 LINK MN MN 164 OD1 ASP 146 LINK MN MN 164 O ARG 148 CRYST1 66.700 66.700 60.800 90.00 90.00 120.00 P 32 2 1 6 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 0.014993 0.008656 0.000000 0.00000 SCALE2 0.000000 0.017312 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016447 0.00000 (ATOM LINES ARE NOT SHOWN.) END