Header list of 3ctn.pdb file
Complete list - r 16 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 08-MAY-97 3CTN
TITLE STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: STRUCTURAL C-DOMAIN RESIDUES 86 - 161;
COMPND 5 SYNONYM: CTNC;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: CARDIAC TROPONIN C WITH CALCIUM IONS BOUND AT SITES
COMPND 8 III AND IV
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGAN: HEART;
SOURCE 7 TISSUE: MUSCLE;
SOURCE 8 CELLULAR_LOCATION: THIN FILAMENT;
SOURCE 9 GENE: CTNC(A-CYS);
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET-23D;
SOURCE 14 EXPRESSION_SYSTEM_GENE: CTNC(A-CYS)
KEYWDS CARDIAC, MUSCLE, REGULATORY, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR S.K.SIA,M.X.LI,L.SPYRACOPOULOS,S.M.GAGNE,W.LIU,J.A.PUTKEY,B.D.SYKES
REVDAT 3 16-MAR-22 3CTN 1 REMARK LINK
REVDAT 2 24-FEB-09 3CTN 1 VERSN
REVDAT 1 13-MAY-98 3CTN 0
JRNL AUTH S.K.SIA,M.X.LI,L.SPYRACOPOULOS,S.M.GAGNE,W.LIU,J.A.PUTKEY,
JRNL AUTH 2 B.D.SYKES
JRNL TITL STRUCTURE OF CARDIAC MUSCLE TROPONIN C UNEXPECTEDLY REVEALS
JRNL TITL 2 A CLOSED REGULATORY DOMAIN.
JRNL REF J.BIOL.CHEM. V. 272 18216 1997
JRNL REFN ISSN 0021-9258
JRNL PMID 9218458
JRNL DOI 10.1074/JBC.272.29.18216
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION.
REMARK 4
REMARK 4 3CTN 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_1000178928.
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 : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
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 87 -52.48 -141.42
REMARK 500 1 ASP A 88 42.71 -161.22
REMARK 500 1 LYS A 90 176.63 61.30
REMARK 500 1 ASP A 105 84.67 -68.83
REMARK 500 1 ALA A 108 61.86 62.68
REMARK 500 1 GLU A 126 71.91 52.34
REMARK 500 1 THR A 129 -167.99 -105.08
REMARK 500 1 LYS A 138 -75.38 -50.83
REMARK 500 1 ASN A 144 78.02 42.92
REMARK 500 1 ASP A 149 -163.16 -100.73
REMARK 500 2 ASP A 87 -47.60 -130.71
REMARK 500 2 ASP A 88 -37.04 -139.32
REMARK 500 2 SER A 89 -74.24 -174.08
REMARK 500 2 LYS A 90 -82.87 -166.15
REMARK 500 2 THR A 93 -178.08 -61.00
REMARK 500 2 ALA A 108 66.44 62.18
REMARK 500 2 THR A 129 -159.77 -83.20
REMARK 500 2 ASP A 141 92.56 -62.34
REMARK 500 2 ASN A 144 81.43 54.93
REMARK 500 2 ASP A 149 -164.77 -125.08
REMARK 500 2 LYS A 158 -88.70 -58.82
REMARK 500 3 ASP A 87 17.42 -148.30
REMARK 500 3 ASP A 88 -82.18 -141.72
REMARK 500 3 LYS A 90 -153.70 42.82
REMARK 500 3 THR A 93 178.90 -48.38
REMARK 500 3 ASP A 109 13.22 -143.87
REMARK 500 3 ASP A 149 -164.85 -118.79
REMARK 500 4 ASP A 88 26.74 -153.77
REMARK 500 4 SER A 89 78.82 51.84
REMARK 500 4 LYS A 92 81.56 -161.34
REMARK 500 4 ALA A 108 70.14 57.29
REMARK 500 4 ASN A 144 84.33 43.57
REMARK 500 4 ASP A 149 -164.15 -102.12
REMARK 500 5 ASP A 88 27.21 -159.84
REMARK 500 5 LYS A 90 57.82 -111.18
REMARK 500 5 LYS A 92 114.45 58.57
REMARK 500 5 THR A 93 -161.09 -102.77
REMARK 500 5 ASP A 105 88.81 -50.63
REMARK 500 5 ALA A 108 66.57 61.73
REMARK 500 5 ASP A 109 10.36 -142.91
REMARK 500 5 GLU A 126 84.37 45.76
REMARK 500 5 ASN A 144 74.98 56.20
REMARK 500 5 ASP A 149 -168.70 -114.20
REMARK 500 5 VAL A 160 -61.73 -91.52
REMARK 500 6 SER A 89 82.12 44.04
REMARK 500 6 LYS A 92 148.25 -172.76
REMARK 500 6 ALA A 108 62.64 65.14
REMARK 500 6 THR A 127 -94.10 41.04
REMARK 500 6 ILE A 128 -132.98 -146.02
REMARK 500 6 ASN A 144 82.12 48.31
REMARK 500
REMARK 500 THIS ENTRY HAS 210 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 102 0.28 SIDE CHAIN
REMARK 500 1 ARG A 147 0.31 SIDE CHAIN
REMARK 500 2 ARG A 102 0.31 SIDE CHAIN
REMARK 500 2 ARG A 147 0.32 SIDE CHAIN
REMARK 500 3 ARG A 102 0.19 SIDE CHAIN
REMARK 500 3 ARG A 147 0.15 SIDE CHAIN
REMARK 500 4 ARG A 102 0.30 SIDE CHAIN
REMARK 500 4 ARG A 147 0.24 SIDE CHAIN
REMARK 500 5 ARG A 102 0.26 SIDE CHAIN
REMARK 500 5 ARG A 147 0.32 SIDE CHAIN
REMARK 500 6 ARG A 102 0.16 SIDE CHAIN
REMARK 500 6 ARG A 147 0.20 SIDE CHAIN
REMARK 500 7 ARG A 102 0.26 SIDE CHAIN
REMARK 500 7 ARG A 147 0.31 SIDE CHAIN
REMARK 500 8 ARG A 102 0.14 SIDE CHAIN
REMARK 500 8 ARG A 147 0.14 SIDE CHAIN
REMARK 500 9 ARG A 102 0.12 SIDE CHAIN
REMARK 500 9 ARG A 147 0.14 SIDE CHAIN
REMARK 500 10 ARG A 102 0.31 SIDE CHAIN
REMARK 500 10 ARG A 147 0.30 SIDE CHAIN
REMARK 500 11 ARG A 102 0.32 SIDE CHAIN
REMARK 500 12 ARG A 102 0.32 SIDE CHAIN
REMARK 500 12 ARG A 147 0.20 SIDE CHAIN
REMARK 500 13 ARG A 102 0.32 SIDE CHAIN
REMARK 500 13 ARG A 147 0.25 SIDE CHAIN
REMARK 500 14 ARG A 102 0.29 SIDE CHAIN
REMARK 500 14 ARG A 147 0.22 SIDE CHAIN
REMARK 500 15 ARG A 102 0.15 SIDE CHAIN
REMARK 500 15 ARG A 147 0.12 SIDE CHAIN
REMARK 500 16 ARG A 102 0.23 SIDE CHAIN
REMARK 500 16 ARG A 147 0.22 SIDE CHAIN
REMARK 500 17 ARG A 147 0.30 SIDE CHAIN
REMARK 500 18 ARG A 102 0.15 SIDE CHAIN
REMARK 500 18 ARG A 147 0.20 SIDE CHAIN
REMARK 500 19 ARG A 102 0.28 SIDE CHAIN
REMARK 500 19 ARG A 147 0.28 SIDE CHAIN
REMARK 500 20 ARG A 102 0.24 SIDE CHAIN
REMARK 500 20 ARG A 147 0.29 SIDE CHAIN
REMARK 500 21 ARG A 102 0.17 SIDE CHAIN
REMARK 500 21 ARG A 147 0.26 SIDE CHAIN
REMARK 500 22 ARG A 102 0.32 SIDE CHAIN
REMARK 500 22 ARG A 147 0.11 SIDE CHAIN
REMARK 500 23 ARG A 102 0.14 SIDE CHAIN
REMARK 500 24 ARG A 102 0.30 SIDE CHAIN
REMARK 500 24 ARG A 147 0.24 SIDE CHAIN
REMARK 500 25 ARG A 102 0.32 SIDE CHAIN
REMARK 500 25 ARG A 147 0.23 SIDE CHAIN
REMARK 500 26 ARG A 102 0.10 SIDE CHAIN
REMARK 500 26 ARG A 147 0.21 SIDE CHAIN
REMARK 500 27 ARG A 102 0.20 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 57 PLANE DEVIATIONS.
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 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 105 OD1
REMARK 620 2 ASN A 107 OD1 120.3
REMARK 620 3 ASP A 109 OD1 93.3 55.7
REMARK 620 4 TYR A 111 O 65.9 121.1 65.7
REMARK 620 5 GLU A 116 OE1 89.7 128.4 172.0 109.0
REMARK 620 6 GLU A 116 OE2 126.0 80.9 133.4 147.9 48.3
REMARK 620 N 1 2 3 4 5
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 141 OD1
REMARK 620 2 ASN A 143 OD1 68.1
REMARK 620 3 ASP A 145 OD2 116.7 53.3
REMARK 620 4 ARG A 147 O 73.0 141.0 159.3
REMARK 620 5 GLU A 152 OE1 65.0 100.9 141.5 58.6
REMARK 620 6 GLU A 152 OE2 99.0 82.7 95.7 100.9 48.8
REMARK 620 N 1 2 3 4 5
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2
DBREF 3CTN A 86 161 UNP P09860 TNNC1_CHICK 86 161
SEQRES 1 A 76 LYS ASP ASP SER LYS GLY LYS THR GLU GLU GLU LEU SER
SEQRES 2 A 76 ASP LEU PHE ARG MET PHE ASP LYS ASN ALA ASP GLY TYR
SEQRES 3 A 76 ILE ASP LEU GLU GLU LEU LYS ILE MET LEU GLN ALA THR
SEQRES 4 A 76 GLY GLU THR ILE THR GLU ASP ASP ILE GLU GLU LEU MET
SEQRES 5 A 76 LYS ASP GLY ASP LYS ASN ASN ASP GLY ARG ILE ASP TYR
SEQRES 6 A 76 ASP GLU PHE LEU GLU PHE MET LYS GLY VAL GLU
HET CA A 1 1
HET CA A 2 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 HE GLU A 95 MET A 103 1 9
HELIX 2 HF LEU A 114 ALA A 123 1 10
HELIX 3 HG GLU A 130 GLY A 140 1 11
HELIX 4 HH TYR A 150 LYS A 158 1 9
SHEET 1 S1 2 TYR A 111 ASP A 113 0
SHEET 2 S1 2 ARG A 147 ASP A 149 -1 N ILE A 148 O ILE A 112
LINK CA CA A 1 OD1 ASP A 105 1555 1555 2.80
LINK CA CA A 1 OD1 ASN A 107 1555 1555 2.81
LINK CA CA A 1 OD1 ASP A 109 1555 1555 2.10
LINK CA CA A 1 O TYR A 111 1555 1555 2.27
LINK CA CA A 1 OE1 GLU A 116 1555 1555 2.38
LINK CA CA A 1 OE2 GLU A 116 1555 1555 2.80
LINK CA CA A 2 OD1 ASP A 141 1555 1555 2.80
LINK CA CA A 2 OD1 ASN A 143 1555 1555 2.46
LINK CA CA A 2 OD2 ASP A 145 1555 1555 2.81
LINK CA CA A 2 O ARG A 147 1555 1555 2.81
LINK CA CA A 2 OE1 GLU A 152 1555 1555 2.29
LINK CA CA A 2 OE2 GLU A 152 1555 1555 2.80
SITE 1 AC1 6 ASP A 105 ASN A 107 ASP A 109 TYR A 111
SITE 2 AC1 6 ILE A 112 GLU A 116
SITE 1 AC2 5 ASP A 141 ASN A 143 ASP A 145 ARG A 147
SITE 2 AC2 5 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
MODEL 1
Complete list - r 16 2 Bytes