BMRB Entry 19974

Name: NMR structure of BA42 protein from the psychrophilic bacteria Bizionia argentinensis sp. nov.
Published: 2014-08-25

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PDB ID: 2mpb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19974
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 of BA42 protein from the psychrophilic bacteria Bizionia argentinensis sp. nov.

Deposition date:

2014-05-14

Original release date:

2014-08-25

Authors:

Cicero, Daniel; Aran, Martin; Smal, Clara; Pellizza, Leonardo; Gallo, Mariana

Citation:

Citation: Aran, Martin; Smal, Clara; Pellizza, Leonardo; Gallo, Mariana; Otero, Lisandro; Klinke, Sebastian; Goldbaum, Fernando; Ithurralde, Esteban; Bercovich, Andres; MacCormack, Walter; Turjanski, Adrian; Cicero, Daniel. "Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain" Proteins ., .-. (2014).
PubMed: 25116514

Assembly members:

Assembly members:
entity, polymer, 145 residues, 16498.727 Da.

Natural source:

Natural source: Common Name: CFB group bacteria Taxonomy ID: 1046627 Superkingdom: Bacteria Kingdom: not available Genus/species: Bizionia argentinensis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pDEST527

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MSKIEEFLTAEEEKAIVDAI RDAEKNTSGEIRVHLEKTSE IDVFDRAMDVFHNLKMDNTK LQNGVLIYVAVEDKTFVIYG DKGINDVVSDDFWDTTRNAI QLQFKQGNFKQGLVDGIEKA GMALAKYFPWKKDDIDELPN TISKG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	638
15N chemical shifts	145
1H chemical shifts	987

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BA42 protein	1

Entities:

Entity 1, BA42 protein 145 residues - 16498.727 Da.

1

MET

SER

LYS

ILE

GLU

PHE

LEU

THR

ALA

2

GLU

LYS

ALA

ILE

VAL

ASP

ALA

ILE

3

ARG

ASP

ALA

GLU

LYS

ASN

THR

SER

GLY

GLU

4

ILE

ARG

VAL

HIS

LEU

GLU

LYS

THR

SER

GLU

5

ILE

ASP

VAL

PHE

ASP

ARG

ALA

MET

ASP

VAL

6

PHE

HIS

ASN

LEU

LYS

MET

ASP

ASN

THR

LYS

7

LEU

GLN

ASN

GLY

VAL

LEU

ILE

TYR

VAL

ALA

8

VAL

GLU

ASP

LYS

THR

PHE

VAL

ILE

TYR

GLY

9

ASP

LYS

GLY

ILE

ASN

ASP

VAL

SER

ASP

10

ASP

PHE

TRP

ASP

THR

ARG

ASN

ALA

ILE

11

GLN

LEU

GLN

PHE

LYS

GLN

GLY

ASN

PHE

LYS

12

GLN

GLY

LEU

VAL

ASP

GLY

ILE

GLU

LYS

ALA

13

GLY

MET

ALA

LEU

ALA

LYS

TYR

PHE

PRO

TRP

14

LYS

ASP

ILE

ASP

GLU

LEU

PRO

ASN

15

THR

ILE

SER

LYS

GLY

Samples:

sample_1: TRIS 10 mM; D2O, [U-100% 2H], 5%; H2O 95%; entity, [U-15N; U-13C], mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.5; pressure: 1 atm; temperature: 301 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	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
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TOPSPIN, Bruker Biospin - collection

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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