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 17863

Title: Rv0899 from Mycobacterium tuberculosis contains two seperated domains   PubMed: 22108166

Deposition date: 2011-08-14 Original release date: 2011-09-02

Authors: Shi, Chaowei; Li, Juan; Gao, Yuan; Wu, Kaiqi; Huang, Hongda; Tian, Changlin

Citation: Li, Juan; Shi, Chaowei; Gao, Yuan; Wu, Kaiqi; Shi, Pan; Lai, Chaohua; Chen, Liu; Wu, Fangming; Tian, Changlin. "Structural Studies of Mycobacterium tuberculosis Rv0899 Reveal a Monomeric Membrane-Anchoring Protein with Two Separate Domains."  J. Mol. Biol. 415, 382-392 (2012).

Assembly members:
Rv0899, polymer, 284 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):
Rv0899: MRPQSVTGPTGVLPTLTPTS TRGASALSLSLLSISRSGNT VTLIGDFPDEAAKAALMTAL NGLLAPGVNVIDQIHVDPVV RSLDFSSAEPVFTASVPIPD FGLKVERDTVTLTGTAPSSE HKDAVKRAATSTWPDMKIVN NIEVTGQAPPGPPASGPCAD LQSAINAVTGGPIAFGNDGA SLIPADYEILNRVADKLKAC PDARVTINGYTDNTGSEGIN IPLSAQRAKIVADYLVARGV AGDHIATVGLGSVNPIASNA TPEGRAKNRRVEIVVNLEHH HHHH

Data sets:
Data typeCount
13C chemical shifts919
15N chemical shifts218
1H chemical shifts1304

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv08991

Entities:

Entity 1, Rv0899 284 residues - Formula weight is not available

1   METARGPROGLNSERVALTHRGLYPROTHR
2   GLYVALLEUPROTHRLEUTHRPROTHRSER
3   THRARGGLYALASERALALEUSERLEUSER
4   LEULEUSERILESERARGSERGLYASNTHR
5   VALTHRLEUILEGLYASPPHEPROASPGLU
6   ALAALALYSALAALALEUMETTHRALALEU
7   ASNGLYLEULEUALAPROGLYVALASNVAL
8   ILEASPGLNILEHISVALASPPROVALVAL
9   ARGSERLEUASPPHESERSERALAGLUPRO
10   VALPHETHRALASERVALPROILEPROASP
11   PHEGLYLEULYSVALGLUARGASPTHRVAL
12   THRLEUTHRGLYTHRALAPROSERSERGLU
13   HISLYSASPALAVALLYSARGALAALATHR
14   SERTHRTRPPROASPMETLYSILEVALASN
15   ASNILEGLUVALTHRGLYGLNALAPROPRO
16   GLYPROPROALASERGLYPROCYSALAASP
17   LEUGLNSERALAILEASNALAVALTHRGLY
18   GLYPROILEALAPHEGLYASNASPGLYALA
19   SERLEUILEPROALAASPTYRGLUILELEU
20   ASNARGVALALAASPLYSLEULYSALACYS
21   PROASPALAARGVALTHRILEASNGLYTYR
22   THRASPASNTHRGLYSERGLUGLYILEASN
23   ILEPROLEUSERALAGLNARGALALYSILE
24   VALALAASPTYRLEUVALALAARGGLYVAL
25   ALAGLYASPHISILEALATHRVALGLYLEU
26   GLYSERVALASNPROILEALASERASNALA
27   THRPROGLUGLYARGALALYSASNARGARG
28   VALGLUILEVALVALASNLEUGLUHISHIS
29   HISHISHISHIS

Samples:

sample_1: Rv0899, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16237
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