BMRB Entry 25027

Name: NMR structure of the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482
Published: 2014-09-02

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PDB ID: 2mqc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25027
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 the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482

Deposition date:

2014-06-18

Original release date:

2014-09-02

Authors:

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

Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482" .

Assembly members:

Assembly members:
entity, polymer, 105 residues, 11296.354 Da.

Natural source:

Natural source: Common Name: CFB group bacteria Taxonomy ID: 435590 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides vulgatus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GHMGSPVSYYFSYADGGTSH TEYPDDSSAGSFILDITSYK KTGNSTKALSWNASGDSWIH VNGSSVSYDENPAKERRTGL VTLKQDESGKTLSLKIVQPG KTSID

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	654
13C chemical shifts	324
15N chemical shifts	107

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 105 residues - 11296.354 Da.

1

GLY

HIS

MET

GLY

SER

PRO

VAL

SER

TYR

2

PHE

SER

TYR

ALA

ASP

GLY

THR

SER

HIS

3

THR

GLU

TYR

PRO

ASP

SER

ALA

GLY

4

SER

PHE

ILE

LEU

ASP

ILE

THR

SER

TYR

LYS

5

LYS

THR

GLY

ASN

SER

THR

LYS

ALA

LEU

SER

6

TRP

ASN

ALA

SER

GLY

ASP

SER

TRP

ILE

HIS

7

VAL

ASN

GLY

SER

VAL

SER

TYR

ASP

GLU

8

ASN

PRO

ALA

LYS

GLU

ARG

THR

GLY

LEU

9

VAL

THR

LEU

LYS

GLN

ASP

GLU

SER

GLY

LYS

10

THR

LEU

SER

LEU

LYS

ILE

VAL

GLN

PRO

GLY

11

LYS

THR

SER

ILE

ASP

Samples:

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

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

Experiments:

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

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

TOPSPIN v3.1, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - data analysis, chemical shift assignment

j-UNIO, Herrmann, Guntert and Wuthrich - peak picking, chemical shift assignment, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

UNP	A6KYV6_BACV8
PDB	2MQC
EMBL	CUN71160 CUP76619
GB	ABR38620 EGX27430
REF	WP_008670674 WP_011964947 WP_057249593 WP_057279461
AlphaFold	A6KYV6