Header list of 1la0.pdb file
Complete list - 23 20 Bytes
HEADER CONTRACTILE PROTEIN 27-MAR-02 1LA0
TITLE SOLUTION STRUCTURE OF CALCIUM SATURATED CARDIAC TROPONIN C IN THE
TITLE 2 TROPONIN C-TROPONIN I COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C, SLOW SKELETAL AND CARDIAC MUSCLES;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TN-C;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23D+
KEYWDS EF-HAND, TROPONIN, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR A.DVORETSKY,E.M.ABUSAMHADNEH,J.W.HOWARTH,P.R.ROSEVEAR
REVDAT 3 23-FEB-22 1LA0 1 REMARK LINK
REVDAT 2 24-FEB-09 1LA0 1 VERSN
REVDAT 1 11-DEC-02 1LA0 0
JRNL AUTH A.DVORETSKY,E.M.ABUSAMHADNEH,J.W.HOWARTH,P.R.ROSEVEAR
JRNL TITL SOLUTION STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C
JRNL TITL 2 BOUND TO CARDIAC TROPONIN I.
JRNL REF J.BIOL.CHEM. V. 277 38565 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12147696
JRNL DOI 10.1074/JBC.M205306200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.84
REMARK 3 AUTHORS : BRUNGER/CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LA0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015782.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 311; 313
REMARK 210 PH : 6.8; 6.8
REMARK 210 IONIC STRENGTH : 500 MM KCL, 10 MM CACL2; 500 MM
REMARK 210 KCL, 10 MM CACL2
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : [15N, 2H]CTNC/CTNI COMPLEXES;
REMARK 210 [15N, 2H]CTNC/CTNI COMPLEXES;
REMARK 210 [15N, 2H]CTNC/CTNI COMPLEXES
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : A/B TROSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : RIGID BODY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: 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 ASP A 2 92.83 -65.34
REMARK 500 ASP A 3 107.09 56.23
REMARK 500 GLN A 11 55.22 -108.00
REMARK 500 VAL A 28 36.40 -95.20
REMARK 500 ALA A 31 -163.73 -59.51
REMARK 500 SER A 37 -68.60 -93.61
REMARK 500 THR A 38 -49.78 -155.90
REMARK 500 ASN A 51 74.88 -117.52
REMARK 500 ASP A 67 -53.18 -121.47
REMARK 500 ASP A 87 108.60 -171.67
REMARK 500 LYS A 90 -174.45 -68.96
REMARK 500 THR A 93 -92.48 45.87
REMARK 500 TYR A 111 -78.01 -173.77
REMARK 500 THR A 129 -166.46 -126.49
REMARK 500 LYS A 138 -77.48 -58.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 46 0.23 SIDE CHAIN
REMARK 500 ARG A 83 0.29 SIDE CHAIN
REMARK 500 ARG A 102 0.22 SIDE CHAIN
REMARK 500 ARG A 147 0.22 SIDE CHAIN
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 162 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 65 OD2
REMARK 620 2 ASP A 65 OD1 44.9
REMARK 620 3 GLU A 76 OE1 48.3 74.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 163 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 105 OD1
REMARK 620 2 ASN A 107 OD1 91.5
REMARK 620 3 ASP A 109 OD2 155.1 78.8
REMARK 620 4 ASP A 109 N 68.4 61.1 86.9
REMARK 620 5 ASP A 109 OD1 100.9 99.7 59.1 52.6
REMARK 620 6 GLU A 116 OE2 116.0 73.1 83.3 134.2 142.3
REMARK 620 7 GLU A 116 OE1 115.0 133.4 87.6 162.8 110.9 61.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 164 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 OD1
REMARK 620 2 ASN A 143 OD1 113.4
REMARK 620 3 ASN A 143 N 63.5 55.6
REMARK 620 4 ASP A 145 OD1 109.7 128.0 129.3
REMARK 620 5 GLU A 152 OE2 90.5 65.6 89.1 141.3
REMARK 620 N 1 2 3 4
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 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 164
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MXL RELATED DB: PDB
REMARK 900 STRUCTURE OF CARDIAC TROPONIN C-TROPONIN I COMPLEX
REMARK 900 RELATED ID: 1FI5 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND
REMARK 900 TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I
DBREF 1LA0 A 1 161 UNP P09860 TNNC1_CHICK 1 161
SEQRES 1 A 161 MET ASP ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR
SEQRES 2 A 161 GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE
SEQRES 3 A 161 PHE VAL LEU GLY ALA GLU ASP GLY CYS ILE SER THR LYS
SEQRES 4 A 161 GLU LEU GLY LYS VAL MET ARG MET LEU GLY GLN ASN PRO
SEQRES 5 A 161 THR PRO GLU GLU LEU GLN GLU MET ILE ASP GLU VAL ASP
SEQRES 6 A 161 GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU
SEQRES 7 A 161 VAL MET MET VAL ARG CYS MET LYS ASP ASP SER LYS GLY
SEQRES 8 A 161 LYS THR GLU GLU GLU LEU SER ASP LEU PHE ARG MET PHE
SEQRES 9 A 161 ASP LYS ASN ALA ASP GLY TYR ILE ASP LEU GLU GLU LEU
SEQRES 10 A 161 LYS ILE MET LEU GLN ALA THR GLY GLU THR ILE THR GLU
SEQRES 11 A 161 ASP ASP ILE GLU GLU LEU MET LYS ASP GLY ASP LYS ASN
SEQRES 12 A 161 ASN ASP GLY ARG ILE ASP TYR ASP GLU PHE LEU GLU PHE
SEQRES 13 A 161 MET LYS GLY VAL GLU
HET CA A 162 1
HET CA A 163 1
HET CA A 164 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 3(CA 2+)
HELIX 1 1 ILE A 4 GLN A 11 1 8
HELIX 2 2 THR A 13 VAL A 28 1 16
HELIX 3 3 LEU A 41 GLY A 49 1 9
HELIX 4 4 THR A 53 ASP A 65 1 13
HELIX 5 5 ASP A 73 MET A 81 1 9
HELIX 6 6 THR A 93 SER A 98 1 6
HELIX 7 7 SER A 98 ASP A 105 1 8
HELIX 8 8 GLU A 116 THR A 124 1 9
HELIX 9 9 THR A 129 ASP A 141 1 13
HELIX 10 10 ASP A 149 MET A 157 1 9
LINK OD2 ASP A 65 CA CA A 162 1555 1555 2.43
LINK OD1 ASP A 65 CA CA A 162 1555 1555 3.02
LINK OE1 GLU A 76 CA CA A 162 1555 1555 3.32
LINK OD1 ASP A 105 CA CA A 163 1555 1555 2.43
LINK OD1 ASN A 107 CA CA A 163 1555 1555 2.90
LINK OD2 ASP A 109 CA CA A 163 1555 1555 2.39
LINK N ASP A 109 CA CA A 163 1555 1555 3.31
LINK OD1 ASP A 109 CA CA A 163 1555 1555 1.88
LINK OE2 GLU A 116 CA CA A 163 1555 1555 2.22
LINK OE1 GLU A 116 CA CA A 163 1555 1555 2.01
LINK OD1 ASP A 141 CA CA A 164 1555 1555 2.43
LINK OD1 ASN A 143 CA CA A 164 1555 1555 3.40
LINK N ASN A 143 CA CA A 164 1555 1555 3.29
LINK OD1 ASP A 145 CA CA A 164 1555 1555 2.12
LINK OE2 GLU A 152 CA CA A 164 1555 1555 2.12
SITE 1 AC1 4 ASP A 65 ASP A 67 THR A 71 GLU A 76
SITE 1 AC2 6 ASP A 105 LYS A 106 ASN A 107 ASP A 109
SITE 2 AC2 6 TYR A 111 GLU A 116
SITE 1 AC3 6 ASP A 141 ASN A 143 ASN A 144 ASP A 145
SITE 2 AC3 6 ARG A 147 GLU A 152
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
Complete list - 23 20 Bytes