BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16051

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

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:
MM0293, 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):
MM0293: MEPQLTKIVDIVENGQWANL KAKVIQLWENTHESISQVGL LGDETGIIKFTIWKNAELPL LEQGESYLLRSVVVGEYNDR FQVQVNKNSSIEKLSEPIEV GLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts463
15N chemical shifts119
1H chemical shifts769

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MM02931

Entities:

Entity 1, MM0293 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   METGLUPROGLNLEUTHRLYSILEVALASP
2   ILEVALGLUASNGLYGLNTRPALAASNLEU
3   LYSALALYSVALILEGLNLEUTRPGLUASN
4   THRHISGLUSERILESERGLNVALGLYLEU
5   LEUGLYASPGLUTHRGLYILEILELYSPHE
6   THRILETRPLYSASNALAGLULEUPROLEU
7   LEUGLUGLNGLYGLUSERTYRLEULEUARG
8   SERVALVALVALGLYGLUTYRASNASPARG
9   PHEGLNVALGLNVALASNLYSASNSERSER
10   ILEGLULYSLEUSERGLUPROILEGLUVAL
11   GLYLEUGLUHISHISHISHISHISHIS

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 0.02%

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 0.02%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
4D 1H-13C NOESYsample_1isotropicsample_conditions_1

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

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

X-PLOR NIH v2.2.1, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16154
PDB