BMRB Entry 25294

Name: NMR structure of the protein NP_809137.1 from Bacteroides thetaiotaomicron
Published: 2014-11-10

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PDB ID: 2mw1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25294
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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_809137.1 from Bacteroides thetaiotaomicron

Deposition date:

2014-10-27

Original release date:

2014-11-10

Authors:

Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Proudfoot, Andrew; Wuthrich, Kurt; Serrano, Pedro; Geralt, Michael; Dutta, Samit. "NMR structure of the protein YP_002937094.1 from Eubacterium rectale" .

Assembly members:

Assembly members:
entity, polymer, 118 residues, 13189.811 Da.

Natural source:

Natural source: Common Name: CFB group bacteria Taxonomy ID: 818 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides thetaiotaomicron

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GCELSDPDGLADPMKWSKVP SGLKNGELKVEAEGGSSLFA CKNYKSFWISSVKEEGKFKE NTSYKEFDGGWYLVKIEDNE LKVIINRNETNASRSFTVCV EAGNAFDEFKFVQDAAKQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	762
13C chemical shifts	384
15N chemical shifts	124

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 118 residues - 13189.811 Da.

1

GLY

CYS

GLU

LEU

SER

ASP

PRO

ASP

GLY

LEU

2

ALA

ASP

PRO

MET

LYS

TRP

SER

LYS

VAL

PRO

3

SER

GLY

LEU

LYS

ASN

GLY

GLU

LEU

LYS

VAL

4

GLU

ALA

GLU

GLY

SER

LEU

PHE

ALA

5

CYS

LYS

ASN

TYR

LYS

SER

PHE

TRP

ILE

SER

6

SER

VAL

LYS

GLU

GLY

LYS

PHE

LYS

GLU

7

ASN

THR

SER

TYR

LYS

GLU

PHE

ASP

GLY

8

TRP

TYR

LEU

VAL

LYS

ILE

GLU

ASP

ASN

GLU

9

LEU

LYS

VAL

ILE

ASN

ARG

ASN

GLU

THR

10

ASN

ALA

SER

ARG

SER

PHE

THR

VAL

CYS

VAL

11

GLU

ALA

GLY

ASN

ALA

PHE

ASP

GLU

PHE

LYS

12

PHE

VAL

GLN

ASP

ALA

LYS

GLN

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; DTT, [U-99% 2H], 5 mM; H2O 95%; D2O 5%

sample_conditions_1: temperature: 298 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.220 M

Experiments:

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

Software:

CYANA, G ntert P., Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution

MDDNMR, Maxim Mayzel, Vladislav Orekhov - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2MW1
GB	AAO75331
REF	NP_809137 WP_011107173