BMRB Entry 25744

Name: NMR structure and dynamics of the resuscitation promoting factor RpfC catalytic domain
Published: 2015-11-17

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PDB ID: 2n5z
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25744
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:

NMR structure and dynamics of the resuscitation promoting factor RpfC catalytic domain

Deposition date:

2015-08-07

Original release date:

2015-11-17

Authors:

Maione, Vincenzo; Russo, Luigi; Isernia, Carla

Citation:

Citation: Maione, Vincenzo; Ruggiero, Alessia; Russo, Luigi; De Simone, Alfonso; Pedone, Paolo; Malgieri, Gaetano; Berisio, Rita; Isernia, Carla. "NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain" PLoS One 10, e0142807-e0142807 (2015).
PubMed: 26576056

Assembly members:

Assembly members:
entity, polymer, 82 residues, 8180.004 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: pETM-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAMGPSPNWDAVAQCESGGN WAANTGNGKYGGLQFKPATW AAFGGVGNPAAASREQQIAV ANRVLAEQGLDAWPTCGAAS GL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	227
15N chemical shifts	72
1H chemical shifts	450

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 82 residues - 8180.004 Da.

1

GLY

ALA

MET

GLY

PRO

SER

PRO

ASN

TRP

ASP

2

ALA

VAL

ALA

GLN

CYS

GLU

SER

GLY

ASN

3

TRP

ALA

ASN

THR

GLY

ASN

GLY

LYS

TYR

4

GLY

LEU

GLN

PHE

LYS

PRO

ALA

THR

TRP

5

ALA

PHE

GLY

VAL

GLY

ASN

PRO

ALA

6

ALA

SER

ARG

GLU

GLN

ILE

ALA

VAL

7

ALA

ASN

ARG

VAL

LEU

ALA

GLU

GLN

GLY

LEU

8

ASP

ALA

TRP

PRO

THR

CYS

GLY

ALA

SER

9

GLY

LEU

Samples:

sample_1: entity, [U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

VNMRJ, Varian - collection, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Varian INOVA 500 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks