BMRB Entry 15903

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15903

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Title:
1H, 15N and 13C backbone and side chain resonance assignment of Rv0008c, an integral membrane protein from Mycobacterium tuberculosis
Deposition date:
2008-08-04
Original release date:
2014-03-05
Authors:
Nguyen, Hau; Cross, Timothy
Citation:

Citation: Nguyen, Hau; Cross, Timothy. "1H, 15N and 13C backbone and side chain resonance assignment of Rv0008c, an integral membrane protein from Mycobacterium tuberculosis"  .

Assembly members:

Assembly members:
Rv0008c, polymer, 169 residues, 15670.8 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTBSG1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rv0008c: MHHHHHHSSGVDLGTENLYF QSNAMSEQVETRLTPRERLT RGLAYSAVGPVDVTRGLLEL GVGLGLQSARSTAAGLRRRY REGRLAREVAAAQETLAQEL TAAQDVVANLPQALQDARTQ RRSKHHLWIFAGIAAAILAG GAVAFSIVRRSSRPEPSPRP PSVEVQPRS

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts128
1H chemical shifts548

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv0008c1

Entities:

Entity 1, Rv0008c 169 residues - 15670.8 Da.

Residue 1 to 24 represent cloning artifact residues (Histidine tag plus TEV cleavage site)

1   METHISHISHISHISHISHISSERSERGLY
2   VALASPLEUGLYTHRGLUASNLEUTYRPHE
3   GLNSERASNALAMETSERGLUGLNVALGLU
4   THRARGLEUTHRPROARGGLUARGLEUTHR
5   ARGGLYLEUALATYRSERALAVALGLYPRO
6   VALASPVALTHRARGGLYLEULEUGLULEU
7   GLYVALGLYLEUGLYLEUGLNSERALAARG
8   SERTHRALAALAGLYLEUARGARGARGTYR
9   ARGGLUGLYARGLEUALAARGGLUVALALA
10   ALAALAGLNGLUTHRLEUALAGLNGLULEU
11   THRALAALAGLNASPVALVALALAASNLEU
12   PROGLNALALEUGLNASPALAARGTHRGLN
13   ARGARGSERLYSHISHISLEUTRPILEPHE
14   ALAGLYILEALAALAALAILELEUALAGLY
15   GLYALAVALALAPHESERILEVALARGARG
16   SERSERARGPROGLUPROSERPROARGPRO
17   PROSERVALGLUVALGLNPROARGSER

Samples:

sample_1: Rv0008c, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: Rv0008c, [U-99% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 10 mM; pH: 4.4; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_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 HNHAsample_1isotropicsample_conditions_1
3D HC(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

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

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

SPARKY, Goddard - data analysis, peak picking

MARS, Jung and Zweckstetter - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 720 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 900 MHz

Related Database Links:

GB 887085 AAK44232 ABQ71726 ABR04351 ACT23029 AEB02137
SWS P71577
DBJ BAH24310 BAL63830 BAQ03837 GAA43814
EMBL CAL69992 CAL70022 CCC25082 CCC42348 CCC62601
REF NP_214522 NP_853678 WP_003400307 WP_003900784 WP_003910023
SP P59977 P9WJF2 P9WJF3
AlphaFold P59977 P9WJF2 P9WJF3

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