BMRB Entry 36489

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36489
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:
Solution structure of T. brucei RAP1
Deposition date:
2022-05-12
Original release date:
2023-07-28
Authors:
Yang, X.; Pan, X.; Ji, Z.; Wong, K.; Zhang, M.; Zhao, Y.
Citation:

Citation: Gaurav, A.; Afrin, M.; Yang, X.; Saha, A.; Pan, X.; Ji, Z.; Zhang, M.; Zhao, Y.; Li, B.. "The RRM-mediated RNA binding activity in T. brucei RAP1 is essential for VSG monoallelic expression."  Nat. Commun. 14, 1576-1576 (2023).
PubMed: 36949076

Assembly members:

Assembly members:
Repressor activator protein 1, polymer, 127 residues, 14207.05 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Repressor activator protein 1: GPGSEATEEIAALDQPFEKC FIPTEALGSDREGLDRTQLE RQLPFRNYPIKLNVSKSGIF CQFPTVSDAKRFYEEGTVEI LNRSLPIKPVFEKRNETVAP AERKRRRSVSPGGVHPQTAA VSALSRR

Data sets:
Data typeCount
13C chemical shifts381
15N chemical shifts111
1H chemical shifts720
torsion angle constraints48

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 127 residues - 14207.05 Da.

1   GLYPROGLYSERGLUALATHRGLUGLUILE
2   ALAALALEUASPGLNPROPHEGLULYSCYS
3   PHEILEPROTHRGLUALALEUGLYSERASP
4   ARGGLUGLYLEUASPARGTHRGLNLEUGLU
5   ARGGLNLEUPROPHEARGASNTYRPROILE
6   LYSLEUASNVALSERLYSSERGLYILEPHE
7   CYSGLNPHEPROTHRVALSERASPALALYS
8   ARGPHETYRGLUGLUGLYTHRVALGLUILE
9   LEUASNARGSERLEUPROILELYSPROVAL
10   PHEGLULYSARGASNGLUTHRVALALAPRO
11   ALAGLUARGLYSARGARGARGSERVALSER
12   PROGLYGLYVALHISPROGLNTHRALAALA
13   VALSERALALEUSERARGARG

Samples:

sample_1: TbRAP1, [U-100% 15N], 0.1 mM; sodium phosphate 100 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: TbRAP1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 100 mM; H2O 90%; D2O, [U-2H], 10%

sample_3: TbRAP1 0.6 mM; sodium phosphate 100 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 800 MHz

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