BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17575

Title: solution structure of the C domain of Rv0899 from mycobacterium tuberculosis   PubMed: 22206986

Deposition date: 2011-04-06 Original release date: 2012-01-04

Authors: Yao, Yong; Marassi, Francesca

Citation: Yao, Yong; Barghava, Neha; Kim, Johnny; Niederweis, Michael; Marassi, Francesca. "Molecular Structure and Peptidoglycan Recognition of Mycobacterium tuberculosis ArfA (Rv0899)."  J. Mol. Biol. 416, 208-220 (2012).

Assembly members:
entity, polymer, 137 residues, 14052.831 Da.

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):
entity: GQAPPGPPASGPCADLQSAI NAVTGGPIAFGNDGASLIPA AYEILNRVADKLKACPDARV TINGYTDNTGSEGINIPLSA QRAKIVADYLVARGVAGDHI ATVGLGSVNPIASNATPEGR AKNRRVEIVVNHHHHHH

Data sets:
Data typeCount
13C chemical shifts350
15N chemical shifts129
1H chemical shifts795

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1C domain of Rv08991

Entities:

Entity 1, C domain of Rv0899 137 residues - 14052.831 Da.

1   GLYGLNALAPROPROGLYPROPROALASER
2   GLYPROCYSALAASPLEUGLNSERALAILE
3   ASNALAVALTHRGLYGLYPROILEALAPHE
4   GLYASNASPGLYALASERLEUILEPROALA
5   ALATYRGLUILELEUASNARGVALALAASP
6   LYSLEULYSALACYSPROASPALAARGVAL
7   THRILEASNGLYTYRTHRASPASNTHRGLY
8   SERGLUGLYILEASNILEPROLEUSERALA
9   GLNARGALALYSILEVALALAASPTYRLEU
10   VALALAARGGLYVALALAGLYASPHISILE
11   ALATHRVALGLYLEUGLYSERVALASNPRO
12   ILEALASERASNALATHRPROGLUGLYARG
13   ALALYSASNARGARGVALGLUILEVALVAL
14   ASNHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.5 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16237 17863
PDB
DBJ BAH25212 BAL64801 BAQ04819 GAA44658
EMBL CAL70937 CCC25980 CCC43237 CCC63509 CCE36433
GB AAK45169 ABI54278 ABQ72638 ABR05261 ACT26182
REF NP_215414 NP_854580 WP_003404684 WP_003915129 WP_014000491
SP A1KH31 P65594 P9WIU4 P9WIU5

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