Header list of 1tnw.pdb file
Complete list - r 2 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 23-AUG-95 1TNW
TITLE NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: SKELETAL;
SOURCE 6 TISSUE: SKELETAL MUSCLE;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3A-TNC
KEYWDS EF-HAND, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR C.M.SLUPSKY,B.D.SYKES
REVDAT 3 02-MAR-22 1TNW 1 REMARK
REVDAT 2 24-FEB-09 1TNW 1 VERSN
REVDAT 1 15-OCT-95 1TNW 0
JRNL AUTH C.M.SLUPSKY,B.D.SYKES
JRNL TITL NMR SOLUTION STRUCTURE OF CALCIUM-SATURATED SKELETAL MUSCLE
JRNL TITL 2 TROPONIN C.
JRNL REF BIOCHEMISTRY V. 34 15953 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 8519752
JRNL DOI 10.1021/BI00049A010
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.M.SLUPSKY,F.C.REINACH,L.B.SMILLIE,B.D.SYKES
REMARK 1 TITL SOLUTION SECONDARY STRUCTURE OF CALCIUM SATURATED TROPONIN C
REMARK 1 TITL 2 MONOMER DETERMINED BY MULTIDIMENSIONAL HETERONUCLEAR NMR
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF PROTEIN SCI. V. 4 1279 1995
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.M.SLUPSKY,C.M.KAY,F.C.REINACH,L.B.SMILLIE,B.D.SYKES
REMARK 1 TITL CALCIUM-INDUCED DIMERIZATION OF TROPONIN C: MODE OF
REMARK 1 TITL 2 INTERACTION AND USE OF TRIFLUOROETHANOL AS A DENATURANT OF
REMARK 1 TITL 3 QUATERNARY STRUCTURE
REMARK 1 REF BIOCHEMISTRY V. 34 7365 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TNW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176764.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
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 1 ASP A 30 43.09 -84.40
REMARK 500 1 ASP A 32 42.42 -105.06
REMARK 500 1 LYS A 87 87.50 -66.72
REMARK 500 1 GLU A 95 86.01 -65.58
REMARK 500 1 ASN A 145 85.17 64.50
REMARK 500 1 VAL A 161 66.81 -102.93
REMARK 500 2 ASP A 30 40.85 -80.67
REMARK 500 2 ASN A 145 80.22 63.38
REMARK 500 3 ASP A 30 42.19 -82.66
REMARK 500 3 ASN A 145 96.40 63.71
REMARK 500 3 VAL A 161 62.22 -104.38
REMARK 500 4 THR A 4 77.04 41.89
REMARK 500 4 ASP A 30 48.61 -85.62
REMARK 500 4 ASN A 145 79.10 64.28
REMARK 500 4 VAL A 161 56.95 -107.93
REMARK 500 5 SER A 2 53.35 -99.01
REMARK 500 5 THR A 4 55.85 -91.93
REMARK 500 5 ASP A 30 47.28 -85.05
REMARK 500 5 ASN A 52 76.50 -119.28
REMARK 500 5 SER A 70 -62.01 -94.67
REMARK 500 5 GLU A 127 -77.08 -84.66
REMARK 500 5 HIS A 128 55.50 -174.81
REMARK 500 5 ASN A 145 135.49 70.75
REMARK 500 5 MET A 158 -157.41 -80.76
REMARK 500 6 ASP A 30 44.70 -83.97
REMARK 500 6 SER A 70 -62.92 -91.08
REMARK 500 6 ALA A 109 81.03 65.23
REMARK 500 6 ASP A 110 -43.46 -130.00
REMARK 500 7 ASP A 30 45.35 -83.48
REMARK 500 7 ASP A 32 42.39 -105.16
REMARK 500 7 ALA A 109 67.45 62.76
REMARK 500 7 GLU A 127 -77.66 -84.01
REMARK 500 7 HIS A 128 51.51 -172.02
REMARK 500 7 ASN A 145 76.04 56.56
REMARK 500 7 VAL A 161 61.08 -102.14
REMARK 500 8 ASP A 30 47.10 -85.14
REMARK 500 8 SER A 70 -73.18 -96.71
REMARK 500 8 THR A 72 -169.66 -108.30
REMARK 500 8 LYS A 87 -112.33 -79.14
REMARK 500 8 ALA A 90 98.23 -61.20
REMARK 500 8 ASN A 145 80.52 59.16
REMARK 500 9 MET A 3 -23.68 79.00
REMARK 500 9 ASP A 30 43.41 -85.26
REMARK 500 9 GLU A 88 -60.84 -90.60
REMARK 500 9 ALA A 90 29.04 -77.73
REMARK 500 9 ASN A 145 70.04 67.14
REMARK 500 9 VAL A 161 54.11 -104.36
REMARK 500 10 SER A 2 74.14 44.85
REMARK 500 10 ASP A 30 48.20 -84.56
REMARK 500 10 ALA A 109 81.34 63.30
REMARK 500
REMARK 500 THIS ENTRY HAS 130 RAMACHANDRAN OUTLIERS.
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 1 ARG A 11 0.31 SIDE CHAIN
REMARK 500 1 ARG A 47 0.30 SIDE CHAIN
REMARK 500 1 ARG A 84 0.32 SIDE CHAIN
REMARK 500 1 ARG A 103 0.29 SIDE CHAIN
REMARK 500 1 ARG A 123 0.31 SIDE CHAIN
REMARK 500 1 ARG A 148 0.31 SIDE CHAIN
REMARK 500 2 ARG A 11 0.30 SIDE CHAIN
REMARK 500 2 ARG A 47 0.28 SIDE CHAIN
REMARK 500 2 ARG A 84 0.30 SIDE CHAIN
REMARK 500 2 ARG A 103 0.31 SIDE CHAIN
REMARK 500 2 ARG A 123 0.31 SIDE CHAIN
REMARK 500 2 ARG A 148 0.28 SIDE CHAIN
REMARK 500 3 ARG A 11 0.31 SIDE CHAIN
REMARK 500 3 ARG A 47 0.29 SIDE CHAIN
REMARK 500 3 ARG A 84 0.32 SIDE CHAIN
REMARK 500 3 ARG A 103 0.31 SIDE CHAIN
REMARK 500 3 ARG A 123 0.30 SIDE CHAIN
REMARK 500 3 ARG A 148 0.31 SIDE CHAIN
REMARK 500 4 ARG A 11 0.32 SIDE CHAIN
REMARK 500 4 ARG A 47 0.28 SIDE CHAIN
REMARK 500 4 ARG A 84 0.32 SIDE CHAIN
REMARK 500 4 ARG A 103 0.32 SIDE CHAIN
REMARK 500 4 ARG A 123 0.30 SIDE CHAIN
REMARK 500 4 ARG A 148 0.29 SIDE CHAIN
REMARK 500 5 ARG A 11 0.31 SIDE CHAIN
REMARK 500 5 ARG A 47 0.32 SIDE CHAIN
REMARK 500 5 ARG A 84 0.31 SIDE CHAIN
REMARK 500 5 ARG A 103 0.32 SIDE CHAIN
REMARK 500 5 ARG A 123 0.32 SIDE CHAIN
REMARK 500 5 ARG A 148 0.31 SIDE CHAIN
REMARK 500 6 ARG A 11 0.29 SIDE CHAIN
REMARK 500 6 ARG A 47 0.32 SIDE CHAIN
REMARK 500 6 ARG A 84 0.28 SIDE CHAIN
REMARK 500 6 ARG A 103 0.29 SIDE CHAIN
REMARK 500 6 ARG A 123 0.32 SIDE CHAIN
REMARK 500 6 ARG A 148 0.30 SIDE CHAIN
REMARK 500 7 ARG A 11 0.31 SIDE CHAIN
REMARK 500 7 ARG A 47 0.29 SIDE CHAIN
REMARK 500 7 ARG A 84 0.31 SIDE CHAIN
REMARK 500 7 ARG A 103 0.31 SIDE CHAIN
REMARK 500 7 ARG A 123 0.31 SIDE CHAIN
REMARK 500 7 ARG A 148 0.31 SIDE CHAIN
REMARK 500 8 ARG A 11 0.32 SIDE CHAIN
REMARK 500 8 ARG A 47 0.31 SIDE CHAIN
REMARK 500 8 ARG A 84 0.31 SIDE CHAIN
REMARK 500 8 ARG A 103 0.31 SIDE CHAIN
REMARK 500 8 ARG A 123 0.32 SIDE CHAIN
REMARK 500 8 ARG A 148 0.31 SIDE CHAIN
REMARK 500 9 ARG A 11 0.30 SIDE CHAIN
REMARK 500 9 ARG A 47 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 138 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: I
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: II
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: III
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: IV
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TNX RELATED DB: PDB
DBREF 1TNW A 1 162 UNP P02588 TNNC2_CHICK 2 163
SEQRES 1 A 162 ALA SER MET THR ASP GLN GLN ALA GLU ALA ARG ALA PHE
SEQRES 2 A 162 LEU SER GLU GLU MET ILE ALA GLU PHE LYS ALA ALA PHE
SEQRES 3 A 162 ASP MET PHE ASP ALA ASP GLY GLY GLY ASP ILE SER THR
SEQRES 4 A 162 LYS GLU LEU GLY THR VAL MET ARG MET LEU GLY GLN ASN
SEQRES 5 A 162 PRO THR LYS GLU GLU LEU ASP ALA ILE ILE GLU GLU VAL
SEQRES 6 A 162 ASP GLU ASP GLY SER GLY THR ILE ASP PHE GLU GLU PHE
SEQRES 7 A 162 LEU VAL MET MET VAL ARG GLN MET LYS GLU ASP ALA LYS
SEQRES 8 A 162 GLY LYS SER GLU GLU GLU LEU ALA ASN CYS PHE ARG ILE
SEQRES 9 A 162 PHE ASP LYS ASN ALA ASP GLY PHE ILE ASP ILE GLU GLU
SEQRES 10 A 162 LEU GLY GLU ILE LEU ARG ALA THR GLY GLU HIS VAL ILE
SEQRES 11 A 162 GLU GLU ASP ILE GLU ASP LEU MET LYS ASP SER ASP LYS
SEQRES 12 A 162 ASN ASN ASP GLY ARG ILE ASP PHE ASP GLU PHE LEU LYS
SEQRES 13 A 162 MET MET GLU GLY VAL GLN
HELIX 1 N GLN A 6 PHE A 13 1 8
HELIX 2 A GLU A 16 PHE A 29 1 14
HELIX 3 B THR A 39 MET A 48 1 10
HELIX 4 C LYS A 55 VAL A 65 1 11
HELIX 5 D PHE A 75 ARG A 84 1 10
HELIX 6 E GLU A 96 PHE A 105 1 10
HELIX 7 F ILE A 115 ALA A 124 1 10
HELIX 8 G GLU A 131 SER A 141 1 11
HELIX 9 H PHE A 151 MET A 157 1 7
SHEET 1 S1 2 ASP A 36 SER A 38 0
SHEET 2 S1 2 THR A 72 ASP A 74 -1
SHEET 1 S2 2 PHE A 112 ASP A 114 0
SHEET 2 S2 2 ARG A 148 ASP A 150 -1
SITE 1 I 12 ASP A 30 ALA A 31 ASP A 32 GLY A 33
SITE 2 I 12 GLY A 34 GLY A 35 ASP A 36 ILE A 37
SITE 3 I 12 SER A 38 THR A 39 LYS A 40 GLU A 41
SITE 1 II 12 ASP A 66 GLU A 67 ASP A 68 GLY A 69
SITE 2 II 12 SER A 70 GLY A 71 THR A 72 ILE A 73
SITE 3 II 12 ASP A 74 PHE A 75 GLU A 76 GLU A 77
SITE 1 III 12 ASP A 106 LYS A 107 ASN A 108 ALA A 109
SITE 2 III 12 ASP A 110 GLY A 111 PHE A 112 ILE A 113
SITE 3 III 12 ASP A 114 ILE A 115 GLU A 116 GLU A 117
SITE 1 IV 12 ASP A 142 LYS A 143 ASN A 144 ASN A 145
SITE 2 IV 12 ASP A 146 GLY A 147 ARG A 148 ILE A 149
SITE 3 IV 12 ASP A 150 PHE A 151 ASP A 152 GLU A 153
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
Complete list - r 2 2 Bytes