BMRB Entry 30034

Name: Solution structure of Rv1466 from Mycobacterium tuberculosis, a protein associated with [Fe-S] complex assembly and repair - Seattle Structural Genomics Center for Infectious Disease target MytuD.17486.a
Published: 2016-05-23

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PDB ID: 5ird
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30034
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:

Solution structure of Rv1466 from Mycobacterium tuberculosis, a protein associated with [Fe-S] complex assembly and repair - Seattle Structural Genomics Center for Infectious Disease target MytuD.17486.a

Deposition date:

2016-03-13

Original release date:

2016-05-23

Authors:

Buchko, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID

Citation:

Citation: Buchko, G.; Hewitt, S.; Van Voorhis, W.C.; Myler, P.. "Solution structure of Rv1466, a Mycobacterium tuberculosis protein associated with [Fe-S] cluster assembly and repair." .

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, 12688.023 Da.

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) Taxonomy ID: 419947 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSMSETSAPAEELLADVE EAMRDVVDPELGINVVDLGL VYGLDVQDGDEGTVALIDMT LTSAACPLTDVIEDQSRSAL VGSGLVDDIRINWVWNPPWG PDKITEDGREQLRALGFTV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	439
15N chemical shifts	115
1H chemical shifts	703

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 119 residues - 12688.023 Da.

1

GLY

PRO

GLY

SER

MET

SER

GLU

THR

SER

ALA

2

PRO

ALA

GLU

LEU

ALA

ASP

VAL

GLU

3

GLU

ALA

MET

ARG

ASP

VAL

ASP

PRO

GLU

4

LEU

GLY

ILE

ASN

VAL

ASP

LEU

GLY

LEU

5

VAL

TYR

GLY

LEU

ASP

VAL

GLN

ASP

GLY

ASP

6

GLU

GLY

THR

VAL

ALA

LEU

ILE

ASP

MET

THR

7

LEU

THR

SER

ALA

CYS

PRO

LEU

THR

ASP

8

VAL

ILE

GLU

ASP

GLN

SER

ARG

SER

ALA

LEU

9

VAL

GLY

SER

GLY

LEU

VAL

ASP

ILE

ARG

10

ILE

ASN

TRP

VAL

TRP

ASN

PRO

TRP

GLY

11

PRO

ASP

LYS

ILE

THR

GLU

ASP

GLY

ARG

GLU

12

GLN

LEU

ARG

ALA

LEU

GLY

PHE

THR

VAL

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	anisotropic	sample_conditions_1
3D HNCACB	sample_1	anisotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	anisotropic	sample_conditions_1
3D H(CCO)NH	sample_1	anisotropic	sample_conditions_1
3D HNCO	sample_1	anisotropic	sample_conditions_1
Deuterium exchange	sample_2	anisotropic	sample_conditions_1
2D Delta	sample_1	anisotropic	sample_conditions_1
3D C(CO)NH	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	anisotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	anisotropic	sample_conditions_1

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CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 30034

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: