HEADER CONTRACTILE PROTEIN 18-APR-01 1IH0
TITLE STRUCTURE OF THE C-DOMAIN OF HUMAN CARDIAC TROPONIN C IN COMPLEX WITH
TITLE 2 CA2+ SENSITIZER EMD 57033
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C, SLOW SKELETAL AND CARDIAC MUSCLES;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 91-161);
COMPND 5 SYNONYM: TN-C;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CTNC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3C
KEYWDS CA2+ BINDING PROTEIN, CA2+ SENSITIZER, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR X.WANG,M.X.LI,L.SPYRACOPOULOS,N.BEIER,M.CHANDRA,R.J.SOLARO,B.D.SYKES
REVDAT 3 23-FEB-22 1IH0 1 REMARK LINK
REVDAT 2 24-FEB-09 1IH0 1 VERSN
REVDAT 1 10-OCT-01 1IH0 0
JRNL AUTH X.WANG,M.X.LI,L.SPYRACOPOULOS,N.BEIER,M.CHANDRA,R.J.SOLARO,
JRNL AUTH 2 B.D.SYKES
JRNL TITL STRUCTURE OF THE C-DOMAIN OF HUMAN CARDIAC TROPONIN C IN
JRNL TITL 2 COMPLEX WITH THE CA2+ SENSITIZING DRUG EMD 57033.
JRNL REF J.BIOL.CHEM. V. 276 25456 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11320096
JRNL DOI 10.1074/JBC.M102418200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER, A.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ~1000 NOE RESTRAINTS WERE USED.
REMARK 3 61 DIHEDRAL RESTRAINTS AS WELL AS 14 NOE RESTRAINTS BETWEEN DRUG
REMARK 3 AND PROTEIN.
REMARK 4
REMARK 4 1IH0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013256.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : ~1MM C-DOMAIN OF CARDIAC
REMARK 210 TROPONIN C. 100MM KCL 10MM
REMARK 210 IMIDAZOLE 1MM DSS ~1MM EMD 57033
REMARK 210 TRACE DMSO-D6
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; HNHB; 3D-13C/15N-NOESY;
REMARK 210 HCCHTOCSY; 3D_15N-SEPARATED_
REMARK 210 NOESY; HNCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY INOVA; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE OF THE PROTEIN WAS DETERMINED USING MULTIDIMENSIONAL
REMARK 210 NMR SPECTROSCOPY.
REMARK 210 THE STRUCTURE OF EMD 57033 IN THE COMPLEX WAS DETERMINED USING 15N/
REMARK 210 13C-FILTERED-NOESY
REMARK 210 AND DIPSI EXPERIMENTS.
REMARK 210 THE CONTACTS BETWEEN PROTEIN AND EMD 57033 WERE DETERMINED USING
REMARK 210 15N/13C-FILTERED/EDITED EXPERIMENTS.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASP A 99 H MET A 103 1.52
REMARK 500 O GLU A 134 H LYS A 138 1.52
REMARK 500 OD2 ASP A 149 H GLU A 152 1.53
REMARK 500 O GLY A 91 H SER A 93 1.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 LYS A 92 -61.56 66.46
REMARK 500 1 SER A 93 -175.43 77.28
REMARK 500 1 GLU A 126 -143.24 -58.83
REMARK 500 1 THR A 129 152.23 -47.16
REMARK 500 1 ASP A 151 -62.02 -92.61
REMARK 500 1 MET A 157 56.13 -97.43
REMARK 500 2 LYS A 92 -81.97 -132.27
REMARK 500 2 SER A 93 160.27 172.15
REMARK 500 2 GLU A 126 91.09 31.73
REMARK 500 2 THR A 129 -151.77 -96.74
REMARK 500 2 GLU A 130 39.79 -93.57
REMARK 500 2 LYS A 158 64.45 -69.71
REMARK 500 3 LYS A 92 -68.74 71.20
REMARK 500 3 SER A 93 -178.19 62.04
REMARK 500 3 ASP A 105 90.41 -61.70
REMARK 500 3 ALA A 108 92.63 65.85
REMARK 500 3 ASP A 109 -37.95 -153.53
REMARK 500 3 ILE A 133 -72.77 -85.20
REMARK 500 3 ASP A 141 52.64 -117.22
REMARK 500 3 ASN A 144 57.03 39.39
REMARK 500 3 VAL A 160 -74.67 -94.32
REMARK 500 4 LYS A 92 -80.45 -103.75
REMARK 500 4 SER A 93 177.48 81.38
REMARK 500 4 LEU A 100 -70.40 -42.79
REMARK 500 4 ASN A 107 -41.84 -139.92
REMARK 500 4 ASP A 109 54.28 -157.44
REMARK 500 4 LEU A 121 -63.02 -107.81
REMARK 500 4 THR A 124 49.85 -100.66
REMARK 500 4 GLU A 126 49.63 37.66
REMARK 500 4 GLU A 135 -75.06 -51.41
REMARK 500 4 ASP A 139 -74.34 -83.21
REMARK 500 4 ASP A 141 49.70 -100.91
REMARK 500 4 LYS A 158 79.58 -65.24
REMARK 500 4 VAL A 160 -70.02 -68.73
REMARK 500 5 PHE A 101 -71.90 -61.50
REMARK 500 5 ASP A 105 99.45 -43.35
REMARK 500 5 ALA A 108 104.33 60.33
REMARK 500 5 ASP A 109 -39.61 -152.34
REMARK 500 5 LEU A 117 -80.25 -65.81
REMARK 500 5 LYS A 118 -35.20 -37.47
REMARK 500 5 LEU A 121 -72.82 -70.96
REMARK 500 5 GLU A 130 28.65 47.15
REMARK 500 5 ASP A 141 75.61 -162.69
REMARK 500 5 TYR A 150 -72.05 -44.09
REMARK 500 5 LYS A 158 34.71 -87.84
REMARK 500 6 GLU A 94 -32.30 -39.33
REMARK 500 6 SER A 98 -31.54 -39.86
REMARK 500 6 ALA A 108 55.36 78.37
REMARK 500 6 GLU A 116 -47.72 -130.51
REMARK 500 6 GLU A 126 39.41 38.95
REMARK 500
REMARK 500 THIS ENTRY HAS 289 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 105 OD1
REMARK 620 2 ASN A 107 ND2 124.1
REMARK 620 3 ASN A 107 OD1 76.5 50.8
REMARK 620 4 TYR A 111 O 72.7 89.0 90.9
REMARK 620 5 GLU A 116 OE1 135.6 100.1 146.3 106.9
REMARK 620 6 GLU A 116 OE2 135.0 72.4 93.0 152.0 58.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 OD1
REMARK 620 2 ARG A 147 O 53.6
REMARK 620 3 GLU A 152 OE1 113.1 118.0
REMARK 620 4 GLU A 152 OE2 130.3 167.4 49.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMD A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AJ4 RELATED DB: PDB
REMARK 900 STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 1 STRUCTURE
DBREF 1IH0 A 91 161 UNP P63316 TNNC1_HUMAN 91 161
SEQRES 1 A 71 GLY LYS SER GLU GLU GLU LEU SER ASP LEU PHE ARG MET
SEQRES 2 A 71 PHE ASP LYS ASN ALA ASP GLY TYR ILE ASP LEU GLU GLU
SEQRES 3 A 71 LEU LYS ILE MET LEU GLN ALA THR GLY GLU THR ILE THR
SEQRES 4 A 71 GLU ASP ASP ILE GLU GLU LEU MET LYS ASP GLY ASP LYS
SEQRES 5 A 71 ASN ASN ASP GLY ARG ILE ASP TYR ASP GLU PHE LEU GLU
SEQRES 6 A 71 PHE MET LYS GLY VAL GLU
HET CA A 2 1
HET CA A 3 1
HET EMD A 1 53
HETNAM CA CALCIUM ION
HETNAM EMD 5-[1-(3,4-DIMETHOXY-BENZOYL)-1,2,3,4-TETRAHYDRO-
HETNAM 2 EMD QUINOLIN-6-YL]-6-METHYL-3,6-DIHYDRO-[1,3,4]THIADIAZIN-
HETNAM 3 EMD 2-ONE
FORMUL 2 CA 2(CA 2+)
FORMUL 4 EMD C22 H23 N3 O4 S
HELIX 1 1 SER A 93 ASP A 105 1 13
HELIX 2 2 LEU A 114 GLU A 126 1 13
HELIX 3 3 THR A 129 ASP A 132 5 4
HELIX 4 4 ILE A 133 ASP A 139 1 7
HELIX 5 5 ASP A 151 MET A 157 1 7
SHEET 1 A 2 ILE A 112 ASP A 113 0
SHEET 2 A 2 ARG A 147 ILE A 148 -1 N ILE A 148 O ILE A 112
LINK CA CA A 2 OD1 ASP A 105 1555 1555 2.11
LINK CA CA A 2 ND2 ASN A 107 1555 1555 2.21
LINK CA CA A 2 OD1 ASN A 107 1555 1555 2.77
LINK CA CA A 2 O TYR A 111 1555 1555 2.71
LINK CA CA A 2 OE1 GLU A 116 1555 1555 2.00
LINK CA CA A 2 OE2 GLU A 116 1555 1555 2.38
LINK CA CA A 3 OD1 ASP A 141 1555 1555 2.76
LINK CA CA A 3 O ARG A 147 1555 1555 2.79
LINK CA CA A 3 OE1 GLU A 152 1555 1555 2.06
LINK CA CA A 3 OE2 GLU A 152 1555 1555 2.80
SITE 1 AC1 6 ASP A 105 LYS A 106 ASN A 107 ASP A 109
SITE 2 AC1 6 TYR A 111 GLU A 116
SITE 1 AC2 6 ASP A 141 ASN A 143 ASP A 145 ARG A 147
SITE 2 AC2 6 ASP A 149 GLU A 152
SITE 1 AC3 11 PHE A 104 LEU A 121 THR A 124 LEU A 136
SITE 2 AC3 11 GLY A 140 ILE A 148 PHE A 153 PHE A 156
SITE 3 AC3 11 MET A 157 VAL A 160 GLU A 161
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
