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 15638

Title: Backbone 1H, 15N and 13C assignment of Rv1567c, an integral membrane protein from Mycobacterium tuberculosis   PubMed: 19636922

Deposition date: 2008-01-25 Original release date: 2008-06-05

Authors: Nguyen, Hau; Cross, Timothy

Citation: Nguyen, Hau; Cross, Timothy. "1H, 15N and 13C backbone resonance assignment of Rv1567c, an integral membrane protein from Mycobacterium tuberculosis"  Biomol. NMR Assignments 2, 47-49 (2008).

Assembly members:
Rv1567c, polymer, 97 residues, 10362.2 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):
Rv1567c: GSHMVTMTSWPSRLFAFTDN VCPPDACPLVPFGVNYYIYP VMWGGIGAAIATAVIGPFVS MLKGWYMSFWPIISIAVITV TSIAGYAIAGFSERYWH

Data sets:
Data typeCount
13C chemical shifts166
15N chemical shifts83
1H chemical shifts83

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv1567c1

Entities:

Entity 1, Rv1567c 97 residues - 10362.2 Da.

Residue 1 to 3 (GSH) represent cloning artifact residues

1   GLYSERHISMETVALTHRMETTHRSERTRP
2   PROSERARGLEUPHEALAPHETHRASPASN
3   VALCYSPROPROASPALACYSPROLEUVAL
4   PROPHEGLYVALASNTYRTYRILETYRPRO
5   VALMETTRPGLYGLYILEGLYALAALAILE
6   ALATHRALAVALILEGLYPROPHEVALSER
7   METLEULYSGLYTRPTYRMETSERPHETRP
8   PROILEILESERILEALAVALILETHRVAL
9   THRSERILEALAGLYTYRALAILEALAGLY
10   PHESERGLUARGTYRTRPHIS

Samples:

sample_1: Rv1567c, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM

sample_2: Rv1567c, [U-99% 15N], 1 ± 0.2 mM

sample_conditions_1: ionic strength: 10 mM; pH: 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

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 720 MHz

Related Database Links:

GB 886349 AAB96955 AAK45885 ABQ73324 ABR05943 ACT25484
SWS O06623
DBJ BAH25883 BAL65539 BAQ05567 GAA45311
EMBL CAL71607 CCC26666 CCC43922 CCC64180 CCE37081
REF NP_216083 NP_855246 WP_003407802 WP_003911567 WP_020424437

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