BMRB Entry 16154

Name: Solution NMR structure of the OB domain (residues 67-166) of MM0293 from Methanosarcina mazei. Northeast Structural Genomics Consortium target MaR214a.
Published: 2009-03-05

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PDB ID: 2ken
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16154
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR structure of the OB domain (residues 67-166) of MM0293 from Methanosarcina mazei. Northeast Structural Genomics Consortium target MaR214a.

Deposition date: 2009-01-30 Original release date: 2009-03-05

Authors: Ramelot, Theresa; Ding, Keyang; Magliqui, Melissa; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Lui, Jinfeng; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhardt; Montelione, Gaetano; Kennedy, Michael

Citation: Kennedy, Michael; Ramelot, Theresa; Ding, Keyang; Magliqui, Melissa; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Lui, Jinfeng; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhardt; Montelione, Gaetano. "NMR structure of the OB domain of MM0293 from the archea Methanosarcina mazei" Not known ., .-..

Assembly members:
OB-domain, polymer, 109 residues, 12519.227 Da.

Natural source: Common Name: Methanosarcina mazei Taxonomy ID: 2209 Superkingdom: Archaea Kingdom: not available Genus/species: Methanosarcina mazei

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

Entity Sequences (FASTA):
OB-domain: MEPQLTKIVDIVENGQWANL KAKVIQLWENTHESISQVGL LGDETGIIKFTIWKNAELPL LEQGESYLLRSVVVGEYNDR FQVQVNKNSSIEKLSEPIEV GLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	464
15N chemical shifts	119
1H chemical shifts	769

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OB-domain	1

Entities:

Entity 1, OB-domain 109 residues - 12519.227 Da.

Residues 2-100 correspond to residues 67-166 in the full-length protein. Residues 101-109 correspond to residues associated with the C-terminal His tag.

1

MET

GLU

PRO

GLN

LEU

THR

LYS

ILE

VAL

ASP

2

ILE

VAL

GLU

ASN

GLY

GLN

TRP

ALA

ASN

LEU

3

LYS

ALA

LYS

VAL

ILE

GLN

LEU

TRP

GLU

ASN

4

THR

HIS

GLU

SER

ILE

SER

GLN

VAL

GLY

LEU

5

LEU

GLY

ASP

GLU

THR

GLY

ILE

LYS

PHE

6

THR

ILE

TRP

LYS

ASN

ALA

GLU

LEU

PRO

LEU

7

LEU

GLU

GLN

GLY

GLU

SER

TYR

LEU

ARG

8

SER

VAL

GLY

GLU

TYR

ASN

ASP

ARG

9

PHE

GLN

VAL

GLN

VAL

ASN

LYS

ASN

SER

10

ILE

GLU

LYS

LEU

SER

GLU

PRO

ILE

GLU

VAL

11

GLY

LEU

GLU

HIS

Samples:

sample_1: OB domain, [U-100% 13C; U-100% 15N], 1.2 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide .02%

sample_2_PEG: OB domain, [U-5% 13C; U-99% 15N], 1.2 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide .02%

sample_2: OB domain, [U-5% 13C; U-99% 15N], 1.2 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide .02%

sample_2_phage: OB domain, [U-5% 13C; U-99% 15N], 1.2 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide .02%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1.0 atm; temperature: 293 K

sample_conditions_2: ionic strength: 0.1 M; pH: 6.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
4D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC-TROSY	sample_2_phage	anisotropic	sample_conditions_2
2D 1H-15N HSQC-TROSY	sample_2_PEG	anisotropic	sample_conditions_2

Software:

TOPSPIN v2.1, Bruker Biospin - collection

SPARKY v3.113, Goddard - data analysis

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - data analysis

PSVS v1.3, Bhattacharya and Montelione - data analysis

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Bruker Avance 850 MHz
Varian INOVA 600 MHz

Biological Magnetic Resonance Data Bank