BMRB Entry 17575

Name: solution structure of the C domain of Rv0899 from mycobacterium tuberculosis
Published: 2012-01-04

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PDB ID: 2lbt
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17575
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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:

solution structure of the C domain of Rv0899 from mycobacterium tuberculosis

Deposition date:

2011-04-06

Original release date:

2012-01-04

Authors:

Yao, Yong; Marassi, Francesca

Citation:

Citation: Yao, Yong; Barghava, Neha; Kim, Johnny; Niederweis, Michael; Marassi, Francesca. "Molecular Structure and Peptidoglycan Recognition of Mycobacterium tuberculosis ArfA (Rv0899)." J. Mol. Biol. 416, 208-220 (2012).
PubMed: 22206986

Assembly members:

Assembly members:
entity, polymer, 137 residues, 14052.831 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: pet21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GQAPPGPPASGPCADLQSAI NAVTGGPIAFGNDGASLIPA AYEILNRVADKLKACPDARV TINGYTDNTGSEGINIPLSA QRAKIVADYLVARGVAGDHI ATVGLGSVNPIASNATPEGR AKNRRVEIVVNHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	350
15N chemical shifts	129
1H chemical shifts	795

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C domain of Rv0899	1

Entities:

Entity 1, C domain of Rv0899 137 residues - 14052.831 Da.

1

GLY

GLN

ALA

PRO

GLY

PRO

ALA

SER

2

GLY

PRO

CYS

ALA

ASP

LEU

GLN

SER

ALA

ILE

3

ASN

ALA

VAL

THR

GLY

PRO

ILE

ALA

PHE

4

GLY

ASN

ASP

GLY

ALA

SER

LEU

ILE

PRO

ALA

5

ALA

TYR

GLU

ILE

LEU

ASN

ARG

VAL

ALA

ASP

6

LYS

LEU

LYS

ALA

CYS

PRO

ASP

ALA

ARG

VAL

7

THR

ILE

ASN

GLY

TYR

THR

ASP

ASN

THR

GLY

8

SER

GLU

GLY

ILE

ASN

ILE

PRO

LEU

SER

ALA

9

GLN

ARG

ALA

LYS

ILE

VAL

ALA

ASP

TYR

LEU

10

VAL

ALA

ARG

GLY

VAL

ALA

GLY

ASP

HIS

ILE

11

ALA

THR

VAL

GLY

LEU

GLY

SER

VAL

ASN

PRO

12

ILE

ALA

SER

ASN

ALA

THR

PRO

GLU

GLY

ARG

13

ALA

LYS

ASN

ARG

VAL

GLU

ILE

VAL

14

ASN

HIS

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.5 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	16237 17863
PDB	2KGW 2L26 2LBT 2LCA
DBJ	BAH25212 BAL64801 BAQ04819 GAA44658
EMBL	CAL70937 CCC25980 CCC43237 CCC63509 CCE36433
GB	AAK45169 ABI54278 ABQ72638 ABR05261 ACT26182
REF	NP_215414 NP_854580 WP_003404684 WP_003915129 WP_014000491
SP	A1KH31 P65594 P9WIU4 P9WIU5
AlphaFold	A1KH31 P65594 P9WIU4 P9WIU5