BMRB Entry 10012

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10012
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Structure of actin-interacting domain of troponin
Deposition date:
2005-11-18
Original release date:
2009-06-01
Authors:
Murakami, Kenji; Yumoto, Fumiaki; Ohki, Shin-ya; Yasunaga, Takuo; Tanokura, Masaru; Wakabayashi, Takeyuki
Citation:

Citation: Murakami, Kenji; Yumoto, Fumiaki; Ohki, Shin-ya; Yasunaga, Takuo; Tanokura, Masaru; Wakabayashi, Takeyuki. "Structural Basis for Ca(2+)-regulated Muscle Relaxation at Interaction Sites of Troponin with Actin and Tropomyosin"  J. Mol. Biol. 352, 178-201 (2005).
PubMed: 16061251

Assembly members:

Assembly members:
TnI, polymer, 52 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TnI: KVNMDLRANLKQVKKEDTEK EKDLRDVGDWRKNIEEKSGM EGRKKMFEAGES

Data sets:
Data typeCount
13C chemical shifts195
15N chemical shifts49
1H chemical shifts340

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Troponin I1
2Troponin C.
3Troponin T2.

Entities:

Entity 1, Troponin I 52 residues - Formula weight is not available

1   LYSVALASNMETASPLEUARGALAASNLEU
2   LYSGLNVALLYSLYSGLUASPTHRGLULYS
3   GLULYSASPLEUARGASPVALGLYASPTRP
4   ARGLYSASNILEGLUGLULYSSERGLYMET
5   GLUGLYARGLYSLYSMETPHEGLUALAGLY
6   GLUSER

Entity ., Troponin C

Samples:

sample_1: Troponin I, [U-13C; U-15N], 0.8 – 1.2 mM; Troponin C0.8 – 1.2 mM; Troponin T20.8 – 1.2 mM; KCl 240 mM; NaHCO3 0.3 mM; MgCl2 3 mM; EGTA 0.2 mM; H2O 90%; D2O 10%

sample_2: Troponin I, [U-13C; U-15N], 0.8 – 1.2 mM; Troponin C0.8 – 1.2 mM; Troponin T20.8 – 1.2 mM; KCl 240 mM; NaHCO3 0.3 mM; MgCl2 3 mM; EGTA 0.2 mM; D2O 100%

condition_1: pH: 7; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
HNCACBsample_1isotropiccondition_1
CBCA(CO)NHsample_1isotropiccondition_1
HNCAsample_1isotropiccondition_1
HN(CO)CAsample_1isotropiccondition_1
HNCOsample_1isotropiccondition_1
H(CCO)NHsample_1isotropiccondition_1
C(CO)NHsample_1isotropiccondition_1
HCCH-TOCSYsample_1isotropiccondition_1
2D 13C-NOESYsample_1isotropiccondition_1
2D aromatic 13C-edited NOESYsample_2isotropiccondition_1
3D 13C-edited NOESYsample_1isotropiccondition_1
3D 15N-edited NOESYsample_1isotropiccondition_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
EMBL CAA27447
GB AAA61952 AAB00122 ACU12238 ACU12239 EMC88037
REF NP_990748 XP_002199061 XP_003206335 XP_003206336 XP_005019798
SP P68246 P68247
AlphaFold P68246 P68247

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks