BMRB Entry 19433

Name: NMR structure of the protein YP_002937094.1 from Eubacterium rectale
Published: 2013-09-03

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PDB ID: 2mca
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19433
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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 YP_002937094.1 from Eubacterium rectale

Deposition date:

2013-08-19

Original release date:

2013-09-03

Authors:

Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Dutta, Samit; 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, 103 residues, 11358.535 Da.

Natural source:

Natural source: Common Name: Eubacterium rectale Taxonomy ID: 39491 Superkingdom: Bacteria Kingdom: not available Genus/species: Eubacterium rectale

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAQDGKETTTIRLINQTYFN VKNIKVTWNDGKEQTVNTLG SHDSIDFSSDAGSVYKMDVT GTTQSGEKFTGHFKGLVGKD TRVFIELDENADVQVFIPQG EID

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	339
15N chemical shifts	112
1H chemical shifts	693

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	YP_002937094.1	1

Entities:

Entity 1, YP_002937094.1 103 residues - 11358.535 Da.

1

GLY

ALA

GLN

ASP

GLY

LYS

GLU

THR

2

ILE

ARG

LEU

ILE

ASN

GLN

THR

TYR

PHE

ASN

3

VAL

LYS

ASN

ILE

LYS

VAL

THR

TRP

ASN

ASP

4

GLY

LYS

GLU

GLN

THR

VAL

ASN

THR

LEU

GLY

5

SER

HIS

ASP

SER

ILE

ASP

PHE

SER

ASP

6

ALA

GLY

SER

VAL

TYR

LYS

MET

ASP

VAL

THR

7

GLY

THR

GLN

SER

GLY

GLU

LYS

PHE

THR

8

GLY

HIS

PHE

LYS

GLY

LEU

VAL

GLY

LYS

ASP

9

THR

ARG

VAL

PHE

ILE

GLU

LEU

ASP

GLU

ASN

10

ALA

ASP

VAL

GLN

VAL

PHE

ILE

PRO

GLN

GLY

11

GLU

ILE

ASP

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; H20 95%; D2O 5%

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

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, Guntert, Mumenthaler and Wuthrich - refinement

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

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2MCA
EMBL	CBK93813 CDC69040 CUN23035 CUN83241
GB	ACR74960
REF	WP_012742060 WP_055223681