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 30399

Title: NMR-based structure of the FHA-2 domain from Mycobacterium tuberculosis ABC transporter Rv1747   PubMed: 29861345

Deposition date: 2018-01-30 Original release date: 2018-06-18

Authors: Heinkel, F.; Okon, M.; Gsponer, J.; McIntosh, L.

Citation: Heinkel, Florian; Shen, Leo; Richard-Greenblatt, Melissa; Okon, Mark; Bui, Jennifer; Gee, Christine; Gay, Laurie; Alber, Tom; Av-Gay, Yossef; Gsponer, Jorg; McIntosh, Lawrence. "Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747."  Structure 26, 972-986 (2018).

Assembly members:
entity_1, polymer, 108 residues, 11602.129 Da.

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 83332   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

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

Entity Sequences (FASTA):
entity_1: GHMWNLATSMMKILRPGRLT GELPPGAVRIGRANDNDIVI PEVLASRHHATLVPTPGGTE IRDNRSINGTFVNGARVDAA LLHDGDVVTIGNIDLVFADG TLARREEN

Data typeCount
13C chemical shifts417
15N chemical shifts110
1H chemical shifts634

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 108 residues - 11602.129 Da.

1   GLYHISMETTRPASNLEUALATHRSERMET
2   METLYSILELEUARGPROGLYARGLEUTHR
3   GLYGLULEUPROPROGLYALAVALARGILE
4   GLYARGALAASNASPASNASPILEVALILE
5   PROGLUVALLEUALASERARGHISHISALA
6   THRLEUVALPROTHRPROGLYGLYTHRGLU
7   ILEARGASPASNARGSERILEASNGLYTHR
8   PHEVALASNGLYALAARGVALASPALAALA
9   LEULEUHISASPGLYASPVALVALTHRILE
10   GLYASNILEASPLEUVALPHEALAASPGLY
11   THRLEUALAARGARGGLUGLUASN

Samples:

sample_1: Rv1747 FHA-2, [U-100% 13C; U-100% 15N], 300 uM; Sodium Phosphate 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment, peak picking

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRe, Ryu, Lim, Sung and Lee - refinement

NMR spectrometers:

  • Bruker AvanceIII 850 MHz

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