BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 16052

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16052

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Title: Assignment of 1HN, 13C, and 15N chemical shift resonances for the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis   PubMed: 19636956

Deposition date: 2008-12-04 Original release date: 2009-03-23

Authors: Sharma, Alok; Ye, Liwen; Zolotarev, Alexander; Alper, Seth; Rigby, Alan

Citation: Sharma, Alok; Ye, Liwen; Zolotarev, Alexander; Alper, Seth; Rigby, Alan. "NMR assignment and secondary structure of the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis"  Biomol. NMR Assignments 3, 99-102 (2009).

Assembly members:
STAS_domain_of_Rv1739C, polymer, 130 residues, Formula weight is not available

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

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

Entity Sequences (FASTA):
STAS_domain_of_Rv1739C: MHDIDDYPQAKRVPGLVVYR YDAPLCFANAEDFRRRALTV VDQDPGQVEWFVLNAESNVE VDLTALDALDQLRTELLRRG IVFAMARVKQDLRESLRAAS LLDKIGEDHIFMTLPTAVQA FRRRHHHHHH

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts122
1H chemical shifts875

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1STAS domain of Rv1739c1

Entities:

Entity 1, STAS domain of Rv1739c 130 residues - Formula weight is not available

1   METHISASPILEASPASPTYRPROGLNALA
2   LYSARGVALPROGLYLEUVALVALTYRARG
3   TYRASPALAPROLEUCYSPHEALAASNALA
4   GLUASPPHEARGARGARGALALEUTHRVAL
5   VALASPGLNASPPROGLYGLNVALGLUTRP
6   PHEVALLEUASNALAGLUSERASNVALGLU
7   VALASPLEUTHRALALEUASPALALEUASP
8   GLNLEUARGTHRGLULEULEUARGARGGLY
9   ILEVALPHEALAMETALAARGVALLYSGLN
10   ASPLEUARGGLUSERLEUARGALAALASER
11   LEULEUASPLYSILEGLYGLUASPHISILE
12   PHEMETTHRLEUPROTHRALAVALGLNALA
13   PHEARGARGARGHISHISHISHISHISHIS

Samples:

sample_1: STAS domain of Rv1739C, [U-100% 13C; U-100% 15N], 0.6 – 0.8 mM; sodium phosphate 50 mM; sodium chloride 275 mM; DTT-d10 2 mM; DSS 0.25 mM; sodium azide 0.05 %w/v

sample_conditions_1: ionic strength: 275 mM; pH: 7.2; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HC(CO)NH, HCCH-TOCSYsample_1isotropicsample_conditions_1
15N-TOCSY-HSQCsample_1isotropicsample_conditions_1
1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe v2007.030.16.06, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw v3.0 Rev 2007.068.09.07, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, peak picking

ANSIG v3.3, Kraulis - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAH26041 BAL65707 BAQ05756 GAA45466
EMBL CAL71765 CCC26828 CCC44085 CCC64338 CCE37238
GB AAK46054 ABQ73499 ABR06098 ACT25325 AEB04397
REF NP_216255 NP_855420 WP_003408524 WP_003898994 WP_003901239
SP P9WGF6 P9WGF7

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts