BMRB Entry 25028

Name: NMR structure of the hypotheical protein Lreu_0056 from Lactobacillus reuteri
Published: 2014-09-02

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PDB ID: 2mqd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25028
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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 hypotheical protein Lreu_0056 from Lactobacillus reuteri

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 hypotheical protein Lreu_0056 from Lactobacillus reuteri" .

Assembly members:

Assembly members:
entity, polymer, 119 residues, 13287.176 Da.

Natural source:

Natural source: Common Name: firmicutes Taxonomy ID: 1598 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactobacillus reuteri

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GHMKFTDQQIGVLAGLAISP EWLKQNIAANQLVYGIVKPS DTVPAGVDDYSYLVAADDQD GTIIFFKAEGQTVIIKYTSQ RNTKLKAKALTLSQLKKEFY QTRSQKREVDDYVAGLRTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	859
13C chemical shifts	419
15N chemical shifts	125

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 119 residues - 13287.176 Da.

1

GLY

HIS

MET

LYS

PHE

THR

ASP

GLN

ILE

2

GLY

VAL

LEU

ALA

GLY

LEU

ALA

ILE

SER

PRO

3

GLU

TRP

LEU

LYS

GLN

ASN

ILE

ALA

ASN

4

GLN

LEU

VAL

TYR

GLY

ILE

VAL

LYS

PRO

SER

5

ASP

THR

VAL

PRO

ALA

GLY

VAL

ASP

TYR

6

SER

TYR

LEU

VAL

ALA

ASP

GLN

ASP

7

GLY

THR

ILE

PHE

LYS

ALA

GLU

GLY

8

GLN

THR

VAL

ILE

LYS

TYR

THR

SER

GLN

9

ARG

ASN

THR

LYS

LEU

LYS

ALA

LYS

ALA

LEU

10

THR

LEU

SER

GLN

LEU

LYS

GLU

PHE

TYR

11

GLN

THR

ARG

SER

GLN

LYS

ARG

GLU

VAL

ASP

12

ASP

TYR

VAL

ALA

GLY

LEU

ARG

THR

GLU

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 - structure solution, refinement

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

TOPSPIN, Bruker Biospin - collection, processing

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

UNP	A5VHK8_LACRD
PDB	2MQD
GB	ABQ82332 AKP00282 EEI09009 EGC14866 KRK50377
REF	WP_003669575
AlphaFold	A5VHK8