BMRB Entry 19628

Name: NMR structure of the protein NP_419126.1 from CAULOBACTER CRESCENTUS
Published: 2014-03-03

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PDB ID: 2mhe
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19628
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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 the protein NP_419126.1 from CAULOBACTER CRESCENTUS

Deposition date:

2013-11-21

Original release date:

2014-03-03

Authors:

Serrano, Pedro; Dutta, Samit; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Serrano, Pedro; Dutta, Samit; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the protein NP_419126.1 from CAULOBACTER CRESCENTUS" .

Assembly members:

Assembly members:
entity, polymer, 74 residues, 16470.863 Da.

Natural source:

Natural source: Common Name: Caulobacter vibrioides Taxonomy ID: 155892 Superkingdom: Bacteria Kingdom: not available Genus/species: Caulobacter crescentus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MPDKQLLHIVVGGELKDVAG VEFRDLSKVEFVGAYPSYDE AHKAWKAKAQATVDNAHARY FIIHAHKLLDPSEG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	302
15N chemical shifts	74
1H chemical shifts	491

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 74 residues - 16470.863 Da.

1

MET

PRO

ASP

LYS

GLN

LEU

HIS

ILE

VAL

2

VAL

GLY

GLU

LEU

LYS

ASP

VAL

ALA

GLY

3

VAL

GLU

PHE

ARG

ASP

LEU

SER

LYS

VAL

GLU

4

PHE

VAL

GLY

ALA

TYR

PRO

SER

TYR

ASP

GLU

5

ALA

HIS

LYS

ALA

TRP

LYS

ALA

LYS

ALA

GLN

6

ALA

THR

VAL

ASP

ASN

ALA

HIS

ALA

ARG

TYR

7

PHE

ILE

HIS

ALA

HIS

LYS

LEU

ASP

8

PRO

SER

GLU

GLY

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; entity, [U-99% 13C; U-99% 15N], 1.2 mM

sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
4D HACANH APSY	sample_1	isotropic	sample_conditions_1
5D HACACONH APSY	sample_1	isotropic	sample_conditions_1
5D CBCACONH APSY	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
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al., Keller and Wuthrich - chemical shift assignment, data analysis, refinement

j-UNIO, Herrmann and Wuthrich - chemical shift assignment, chemical shift calculation, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2MHE
GB	AAK22294 ACL93776
REF	NP_419126 WP_010918196 WP_012639934 YP_002515684