BMRB Entry 15774

Name: Rv1761c
Published: 2008-12-30

Click here to enlarge.

PDB ID: 2k3m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15774
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rv1761c: MHHHHHHSSGVDLGTENLYF QSNAMSDFDTERVSRAVAAA LVGPGGVALVVKVFAGLPGV IHTPARRGFFRSNPERIQIG DWRYEVAHDGRLLAAHMVNG IVIAEDALIAEAVGPHLARA LGQIVSRYGATVIPNINAAI EVLGTGTDYRF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- RDC_list_1
- RDC_list_2

Data type	Count
13C chemical shifts	335
15N chemical shifts	118
1H chemical shifts	118
residual dipolar couplings	217

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rv1761c	1
2	MTN	2

Entities:

Entity 1, Rv1761c 151 residues - 13491.678 Da.

1

MET

HIS

SER

GLY

2

VAL

ASP

LEU

GLY

THR

GLU

ASN

LEU

TYR

PHE

3

GLN

SER

ASN

ALA

MET

SER

ASP

PHE

ASP

THR

4

GLU

ARG

VAL

SER

ARG

ALA

VAL

ALA

5

LEU

VAL

GLY

PRO

GLY

VAL

ALA

LEU

VAL

6

VAL

LYS

VAL

PHE

ALA

GLY

LEU

PRO

GLY

VAL

7

ILE

HIS

THR

PRO

ALA

ARG

GLY

PHE

8

ARG

SER

ASN

PRO

GLU

ARG

ILE

GLN

ILE

GLY

9

ASP

TRP

ARG

TYR

GLU

VAL

ALA

HIS

ASP

GLY

10

ARG

LEU

ALA

HIS

MET

VAL

ASN

GLY

11

ILE

VAL

ILE

ALA

GLU

ASP

ALA

LEU

ILE

ALA

12

GLU

ALA

VAL

GLY

PRO

HIS

LEU

ALA

ARG

ALA

13

LEU

GLY

GLN

ILE

VAL

SER

ARG

TYR

GLY

ALA

14

THR

VAL

ILE

PRO

ASN

ILE

ASN

ALA

ILE

15

GLU

VAL

LEU

GLY

THR

GLY

THR

ASP

TYR

ARG

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N_13C_Rv1761c	isotropic	sample_conditions_1
2D 1H-15N HSQC	F30C-MTSL_Rv1761c	isotropic	sample_conditions_1
2D 1H-15N HSQC	S48C-MTSL_Rv1761c	isotropic	sample_conditions_1
2D 1H-15N HSQC	S102C-MTSL_Rv1761c	isotropic	sample_conditions_1
3D HNCO	15N_13C_Rv1761c	isotropic	sample_conditions_1
3D HNCA	15N_13C_Rv1761c	isotropic	sample_conditions_1
3D HNCACB	15N_13C_Rv1761c	isotropic	sample_conditions_1
3D HN(CO)CA	15N_13C_Rv1761c	isotropic	sample_conditions_1
3D CBCA(CO)NH	15N_13C_Rv1761c	isotropic	sample_conditions_1
2D 1H-15N HSQC	15N_Rv1761c	isotropic	sample_conditions_1
2D 1H-15N HSQC	15N_Rv1761c	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N_Rv1761c	isotropic	sample_conditions_1
2D 1H-15N HSQC-IPAP	15N_Rv1761c-neutral_gel	isotropic	sample_conditions_1
2D 1H-15N HSQC-IPAP	15N_Rv1761c-charged_gel	isotropic	sample_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

PDB	2K3M
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