BMRB Entry 18011

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18011
MolProbity Validation Chart

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Title:
NMR assignments for TB24
Deposition date:
2011-10-19
Original release date:
2012-03-27
Authors:
Ames, James
Citation:

Citation: Xu, Xianzhong; Olson, Cheryl; Engman, David; Ames, James. "(1)H, (15)N, and (13)C chemical shift assignments of the calflagin Tb24 flagellar calcium binding protein of Trypanosoma brucei."  Biomol. NMR Assignments 7, 9-12 (2013).
PubMed: 22382573

Assembly members:

Assembly members:
Tb24, polymer, 218 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Tb24: MGCSGSKDTTNSKDGAASKG GKDGKTTADRKVAWERIRCA IPRDKDAESKSRRIELFKQF DTNGTGKLGFREVLDGCYGI LKLDEFTTHLPDIVQRAFDK AKDLGNKVKGVGEEDLVEFL EFRLMLCYIYDIFELTVMFD TMDKDGSLLLELQEFKEALP KLKEWGVDITDATTVFNEID TNGSGVVTFDEFSCWAVTKK LQVCGDPDGEENGANEGN

Data sets:
Data typeCount
13C chemical shifts817
15N chemical shifts201
1H chemical shifts1262

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Tb241

Entities:

Entity 1, Tb24 218 residues - Formula weight is not available

The first three residues from N-terminus are disordered and the assignments begin at residue 4 (Ser 4) and end at residue 218 (N218).

1   METGLYCYSSERGLYSERLYSASPTHRTHR
2   ASNSERLYSASPGLYALAALASERLYSGLY
3   GLYLYSASPGLYLYSTHRTHRALAASPARG
4   LYSVALALATRPGLUARGILEARGCYSALA
5   ILEPROARGASPLYSASPALAGLUSERLYS
6   SERARGARGILEGLULEUPHELYSGLNPHE
7   ASPTHRASNGLYTHRGLYLYSLEUGLYPHE
8   ARGGLUVALLEUASPGLYCYSTYRGLYILE
9   LEULYSLEUASPGLUPHETHRTHRHISLEU
10   PROASPILEVALGLNARGALAPHEASPLYS
11   ALALYSASPLEUGLYASNLYSVALLYSGLY
12   VALGLYGLUGLUASPLEUVALGLUPHELEU
13   GLUPHEARGLEUMETLEUCYSTYRILETYR
14   ASPILEPHEGLULEUTHRVALMETPHEASP
15   THRMETASPLYSASPGLYSERLEULEULEU
16   GLULEUGLNGLUPHELYSGLUALALEUPRO
17   LYSLEULYSGLUTRPGLYVALASPILETHR
18   ASPALATHRTHRVALPHEASNGLUILEASP
19   THRASNGLYSERGLYVALVALTHRPHEASP
20   GLUPHESERCYSTRPALAVALTHRLYSLYS
21   LEUGLNVALCYSGLYASPPROASPGLYGLU
22   GLUASNGLYALAASNGLUGLYASN

Samples:

sample_1: Tb24, [U-98% 13C; U-98% 15N], 1.0 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CBH13602 CBH13605
GB AAA75582 AAA75583 AAB40004 AAX70701 AAX70703
REF XP_011775879 XP_011775881 XP_847374 XP_847376
SP Q26677 Q26678 Q26680
AlphaFold Q26677 Q26678 Q26680

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