BMRB Entry 15774

Title:
Rv1761c
Deposition date:
2008-05-14
Original release date:
2008-12-30
Authors:
Page, Richard; Moore, Jacob; Lee, Sangwon; Opella, Stanley; Cross, Timothy
Citation:

Citation: Page, Richard; Lee, Sangwon; Moore, Jacob; Opella, Stanley; Cross, Timothy. "Backbone structure of a small helical integral membrane protein: A unique structural characterization"  Protein Sci. 18, 134-146 (2009).
PubMed: 19177358

Assembly members:

Assembly members:
Rv1761c, polymer, 151 residues, 13491.678 Da.
MTN, non-polymer, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacillus 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

Data sets:
Data typeCount
13C chemical shifts335
15N chemical shifts118
1H chemical shifts118
residual dipolar couplings217

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv1761c1
2MTN2

Entities:

Entity 1, Rv1761c 151 residues - 13491.678 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   VALASPLEUGLYTHRGLUASNLEUTYRPHE
3   GLNSERASNALAMETSERASPPHEASPTHR
4   GLUARGVALSERARGALAVALALAALAALA
5   LEUVALGLYPROGLYGLYVALALALEUVAL
6   VALLYSVALPHEALAGLYLEUPROGLYVAL
7   ILEHISTHRPROALAARGARGGLYPHEPHE
8   ARGSERASNPROGLUARGILEGLNILEGLY
9   ASPTRPARGTYRGLUVALALAHISASPGLY
10   ARGLEULEUALAALAHISMETVALASNGLY
11   ILEVALILEALAGLUASPALALEUILEALA
12   GLUALAVALGLYPROHISLEUALAARGALA
13   LEUGLYGLNILEVALSERARGTYRGLYALA
14   THRVALILEPROASNILEASNALAALAILE
15   GLUVALLEUGLYTHRGLYTHRASPTYRARG
16   PHE

Entity 2, MTN - Formula weight is not available

1   MTN

Samples:

F30C-MTSL_Rv1761c: Rv1761c, [U-100% 15N], 0.4 ± 0.05 mM; CYSP 0.4 ± 0.05 mM; D2O 10 ± 1 %; H2O 90 ± 1 %; sodium acetate 20 ± 1 mM; DPC 150 ± 5 mM

S48C-MTSL_Rv1761c: Rv1761c, [U-100% 15N], 0.4 ± 0.05 mM; CYSP 0.4 ± 0.05 mM; D2O 10 ± 1 %; H2O 90 ± 1 %; sodium acetate 20 ± 1 mM; DPC 150 ± 5 mM

S102C-MTSL_Rv1761c: Rv1761c, [U-100% 15N], 0.4 ± 0.05 mM; CYSP 0.4 ± 0.05 mM; D2O 10 ± 1 %; H2O 90 ± 1 %; sodium acetate 20 ± 1 mM; DPC 150 ± 5 mM

15N_13C_Rv1761c: Rv1761c, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; D2O 10 ± 1 %; H2O 90 ± 1 %; sodium acetate 20 ± 1 mM; DPC 150 ± 5 mM

15N_Rv1761c: Rv1761c, [U-100% 15N], 1 ± 0.05 mM; D2O 10 ± 1 %; H2O 90 ± 1 %; sodium acetate 20 ± 1 mM; DPC 150 ± 5 mM

15N_Rv1761c-neutral_gel: Rv1761c, [U-100% 15N], 1 ± 0.05 mM; D2O 10 ± 1 %; H2O 90 ± 1 %; sodium acetate 20 ± 1 mM; DPC 150 ± 5 mM; polyacrylamide gel 5 ± 0.1 %

15N_Rv1761c-charged_gel: Rv1761c, [U-100% 15N], 1 ± 0.05 mM; D2O 10 ± 1 %; H2O 90 ± 1 %; sodium acetate 20 ± 1 mM; DPC 150 ± 5 mM; polyacrylamide gel 4.4 ± 0.1 %; 2-acrylamido-2-methyl-1-propanesulfonic acid 1.1 ± 0.1 %

sample_conditions_1: ionic strength: 170 mM; pH: 4; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_13C_Rv1761cisotropicsample_conditions_1
2D 1H-15N HSQCF30C-MTSL_Rv1761cisotropicsample_conditions_1
2D 1H-15N HSQCS48C-MTSL_Rv1761cisotropicsample_conditions_1
2D 1H-15N HSQCS102C-MTSL_Rv1761cisotropicsample_conditions_1
3D HNCO15N_13C_Rv1761cisotropicsample_conditions_1
3D HNCA15N_13C_Rv1761cisotropicsample_conditions_1
3D HNCACB15N_13C_Rv1761cisotropicsample_conditions_1
3D HN(CO)CA15N_13C_Rv1761cisotropicsample_conditions_1
3D CBCA(CO)NH15N_13C_Rv1761cisotropicsample_conditions_1
2D 1H-15N HSQC15N_Rv1761cisotropicsample_conditions_1
2D 1H-15N HSQC15N_Rv1761cisotropicsample_conditions_1
3D 1H-15N NOESY15N_Rv1761cisotropicsample_conditions_1
2D 1H-15N HSQC-IPAP15N_Rv1761c-neutral_gelisotropicsample_conditions_1
2D 1H-15N HSQC-IPAP15N_Rv1761c-charged_gelisotropicsample_conditions_1

Software:

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

SPARKY, Goddard - data analysis

X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

VNMR, Varian - chemical shift assignment

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 720 MHz
  • Varian Avance 900 MHz

Related Database Links:

PDB
DBJ BAH26065 BAL65739
EMBL CAL71789 CCC26851 CCC44109 CCC64362 CCG11637
GB AAK46081 ABQ73528 ABR06126 ACT25304 AEB04376
REF NP_216277 NP_855444 WP_003899008 WP_003910433 WP_014000931

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