BMRB Entry 16188

Name: NMR structure of Rv2175c
Published: 2009-05-29

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PDB ID: 2kfs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16188
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of Rv2175c

Deposition date:

2009-02-27

Original release date:

2009-05-29

Authors:

Barthe, Philippe; Cohen-Gonsaud, Martin; Roumestand, Christian; Molle, Virginie

Citation:

Citation: Cohen-Gonsaud, Martin; Barthe, Philippe; Canova, Marc; Stagier-Simon, Charlotte; Kremer, Laurent; Roumestand, Christian; Molle, Virginie. "The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation" J. Biol. Chem. 284, 19290-19300 (2009).
PubMed: 19457863

Assembly members:

Assembly members:
Rv2175c, polymer, 146 residues, 15763.063 Da.

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 83332 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rv2175c: MPGRAPGSTLARVGSIPAGD DVLDPDEPTYDLPRVAELLG VPVSKVAQQLREGHLVAVRR AGGVVIPQVFFTNSGQVVKS LPGLLTILHDGGYRDTEIMR WLFTPDPSLTITRDGSRDAV SNARPVDALHAHQAREVVRR AQAMAY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	369
15N chemical shifts	152
1H chemical shifts	998

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rv2175c	1

Entities:

Entity 1, Rv2175c 146 residues - 15763.063 Da.

1

MET

PRO

GLY

ARG

ALA

PRO

GLY

SER

THR

LEU

2

ALA

ARG

VAL

GLY

SER

ILE

PRO

ALA

GLY

ASP

3

ASP

VAL

LEU

ASP

PRO

ASP

GLU

PRO

THR

TYR

4

ASP

LEU

PRO

ARG

VAL

ALA

GLU

LEU

GLY

5

VAL

PRO

VAL

SER

LYS

VAL

ALA

GLN

LEU

6

ARG

GLU

GLY

HIS

LEU

VAL

ALA

VAL

ARG

7

ALA

GLY

VAL

ILE

PRO

GLN

VAL

PHE

8

PHE

THR

ASN

SER

GLY

GLN

VAL

LYS

SER

9

LEU

PRO

GLY

LEU

THR

ILE

LEU

HIS

ASP

10

GLY

TYR

ARG

ASP

THR

GLU

ILE

MET

ARG

11

TRP

LEU

PHE

THR

PRO

ASP

PRO

SER

LEU

THR

12

ILE

THR

ARG

ASP

GLY

SER

ARG

ASP

ALA

VAL

13

SER

ASN

ALA

ARG

PRO

VAL

ASP

ALA

LEU

HIS

14

ALA

HIS

GLN

ALA

ARG

GLU

VAL

ARG

15

ALA

GLN

ALA

MET

ALA

TYR

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HCACO	sample_2	isotropic	sample_conditions_1

PDB	2KFS
DBJ	BAH26468 BAL66184 BAQ06242
EMBL	CAL72178 CCC27256 CCC44529 CCC64767 CCE37647
GB	AAK46516 ABQ73952 ABR06534 ACT24868 AEB03948
REF	NP_216691 NP_855846 WP_003411249 WP_003900481 WP_003910516
SP	O53509
AlphaFold	O53509

BMRB Entry 16188

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: