BMRB Entry 17585

Name: Rv0020c_Nter structure
Published: 2011-10-26

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PDB ID: 2lc0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17585
MolProbity Validation Chart

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

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Title:

Rv0020c_Nter structure

Deposition date:

2011-04-11

Original release date:

2011-10-26

Authors:

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

Citation:

Citation: Roumestand, Christian; Leiba, Jade; Galophe, Nathalie; Margeat, Emmanuel; Padilla, Andre; Bessin, Yannick; Barthe, Philippe; Molle, Virginie; Cohen-Gonsaud, Martin. "Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase." Structure 19, 1525-1534 (2011).
PubMed: 22000520

Assembly members:

Assembly members:
Rv0020c_Nter, polymer, 132 residues, 14773.583 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: pET15b-tev

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rv0020c_Nter: MGSQKRLVQRVERKLEQTVG DAFARIFGGSIVPQEVEALL RREAADGIQSLQGNRLLAPN EYIITLGVHDFEKLGADPEL KSTGFARDLADYIQEQGWQT YGDVVVRFEQSSNLHTGQFR ARGTVNPDVETH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	342
15N chemical shifts	140
1H chemical shifts	844

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rv0020c_Nter	1

Entities:

Entity 1, Rv0020c_Nter 132 residues - 14773.583 Da.

1

MET

GLY

SER

GLN

LYS

ARG

LEU

VAL

GLN

ARG

2

VAL

GLU

ARG

LYS

LEU

GLU

GLN

THR

VAL

GLY

3

ASP

ALA

PHE

ALA

ARG

ILE

PHE

GLY

SER

4

ILE

VAL

PRO

GLN

GLU

VAL

GLU

ALA

LEU

5

ARG

GLU

ALA

ASP

GLY

ILE

GLN

SER

6

LEU

GLN

GLY

ASN

ARG

LEU

ALA

PRO

ASN

7

GLU

TYR

ILE

THR

LEU

GLY

VAL

HIS

ASP

8

PHE

GLU

LYS

LEU

GLY

ALA

ASP

PRO

GLU

LEU

9

LYS

SER

THR

GLY

PHE

ALA

ARG

ASP

LEU

ALA

10

ASP

TYR

ILE

GLN

GLU

GLN

GLY

TRP

GLN

THR

11

TYR

GLY

ASP

VAL

ARG

PHE

GLU

GLN

12

SER

ASN

LEU

HIS

THR

GLY

GLN

PHE

ARG

13

ALA

ARG

GLY

THR

VAL

ASN

PRO

ASP

VAL

GLU

14

THR

HIS

Samples:

15N: Rv0020c_Nter, [U-15N], 0.5 ± 0.01 mM

13C-15N: Rv0020c_Nter, [U-13C; U-15N], 0.5 ± 0.01 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	15N	isotropic	sample_conditions_1
3D 1H-15N TOCSY	15N	isotropic	sample_conditions_1
3D HNCA	13C-15N	isotropic	sample_conditions_1
3D CBCA(CO)NH	13C-15N	isotropic	sample_conditions_1
3D HNCACB	13C-15N	isotropic	sample_conditions_1
3D HNCO	13C-15N	isotropic	sample_conditions_1
3D HCACO	13C-15N	isotropic	sample_conditions_1

Software:

GIFA v4.44, Delsuc - processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TALOS+ v1.2009.0721.18, Cornilescu, Delaglio and Bax - angle prediction

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 500 MHz

PDB	2LC0
DBJ	BAH24322 BAL63843 BAQ03850
EMBL	CAL70034 CCC25094 CCC42360 CCC62613 CCE35563
GB	AAK44245 ABQ71740 ABR04363 ACT23041 AEB02149
REF	NP_214534 NP_853690 WP_003400376 WP_003899777 WP_003905210
SP	P71590
AlphaFold	P71590