BMRB Entry 19431

Name: NMR structure of hypothetical protein RUMGNA_01855 from Ruminococcus gnavus ATCC 29149
Published: 2013-10-21

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PDB ID: 2mc8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19431
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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 hypothetical protein RUMGNA_01855 from Ruminococcus gnavus ATCC 29149

Deposition date:

2013-08-21

Original release date:

2013-10-21

Authors:

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

Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of a hypothetical protein RUMGNA_01855 from Ruminococcus gnavus ATCC 29149" .

Assembly members:

Assembly members:
entity, polymer, 114 residues, 13280.990 Da.

Natural source:

Natural source: Common Name: Ruminococcus gnavus ATCC 29149 Taxonomy ID: 411470 Superkingdom: Bacteria Kingdom: not available Genus/species: Blautia Ruminococcus gnavus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GEILKELPEGFDKETVRKQA MEDIEIAQSKDYESWKSRFT KDLQSSLTEESYDSYLKILE KQGEFKEFGKCTYLGQIKDN KKYGGVIIVVKYEEGNVNYS LAYDEDMNLVSFTM

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	801
13C chemical shifts	398
15N chemical shifts	121

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hypothetical protein	1

Entities:

Entity 1, hypothetical protein 114 residues - 13280.990 Da.

1

GLY

GLU

ILE

LEU

LYS

GLU

LEU

PRO

GLU

GLY

2

PHE

ASP

LYS

GLU

THR

VAL

ARG

LYS

GLN

ALA

3

MET

GLU

ASP

ILE

GLU

ILE

ALA

GLN

SER

LYS

4

ASP

TYR

GLU

SER

TRP

LYS

SER

ARG

PHE

THR

5

LYS

ASP

LEU

GLN

SER

LEU

THR

GLU

6

SER

TYR

ASP

SER

TYR

LEU

LYS

ILE

LEU

GLU

7

LYS

GLN

GLY

GLU

PHE

LYS

GLU

PHE

GLY

LYS

8

CYS

THR

TYR

LEU

GLY

GLN

ILE

LYS

ASP

ASN

9

LYS

TYR

GLY

VAL

ILE

VAL

10

LYS

TYR

GLU

GLY

ASN

VAL

ASN

TYR

SER

11

LEU

ALA

TYR

ASP

GLU

ASP

MET

ASN

LEU

VAL

12

SER

PHE

THR

MET

Samples:

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

sample_conditions_1: temperature: 298 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.0798 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
4D APSY HACANH	sample_1	isotropic	sample_conditions_1
5D APSY HACACONH	sample_1	isotropic	sample_conditions_1
5D APSY CBCACONH	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

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

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

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

TOPSPIN v3.1, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2MC8 4HYZ
EMBL	CCZ66509 CUO03677
GB	EDN77700 EGN48378 ETD20298
REF	WP_004842842 WP_022038064 WP_055168981