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 15849

Title: SOLUTION NMR STRUCTURE OF the second OB-fold domain of replication protein A from Methanococcus maripaludis. NORTHEAST STRUCTURAL GENOMICS TARGET MrR110B.

Authors: Aramini, James; Maglaqui, Melissa; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Aramini, James; Maglaqui, Melissa; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.; Acton, Thomas; Montelione, Gaetano. "SOLUTION NMR STRUCTURE OF the second OB-fold domain of replication protein A from Methanococcus maripaludis. NORTHEAST STRUCTURAL GENOMICS TARGET MrR110B."  Not known ., .-..

Assembly members:
MrR110B, polymer, 104 residues, 11631.229 Da.

Natural source:   Common Name: Methanococcus maripaludis   Taxonomy ID: 39152   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanococcus maripaludis

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

Entity Sequences (FASTA):
MrR110B: MNYKISELMPNLSGTINAEV VAAYPKKEFSRKDGTKGQLK SLFLKDDTGSIRGTLWNELA DFEVKKGDIAEVSGYVKQGY SGLEISVDNIGIIEKSLEHH HHHH

Data sets:
Data typeCount
13C chemical shifts450
15N chemical shifts105
1H chemical shifts708

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MrR110B1

Entities:

Entity 1, MrR110B 104 residues - 11631.229 Da.

C-terminal LEHHHHHH purification tag.

1   METASNTYRLYSILESERGLULEUMETPRO
2   ASNLEUSERGLYTHRILEASNALAGLUVAL
3   VALALAALATYRPROLYSLYSGLUPHESER
4   ARGLYSASPGLYTHRLYSGLYGLNLEULYS
5   SERLEUPHELEULYSASPASPTHRGLYSER
6   ILEARGGLYTHRLEUTRPASNGLULEUALA
7   ASPPHEGLUVALLYSLYSGLYASPILEALA
8   GLUVALSERGLYTYRVALLYSGLNGLYTYR
9   SERGLYLEUGLUILESERVALASPASNILE
10   GLYILEILEGLULYSSERLEUGLUHISHIS
11   HISHISHISHIS

Samples:

sample_1: MrR110B, [U-100% 13C; U-100% 15N], 1.18 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%

sample_2: MrR110B, [U-100% 13C; U-100% 15N], 1.18 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%

sample_3: MrR110B, [U-5% 13C; U-100% 15N], 0.94 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC (aliph)sample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSY aliphaticsample_1isotropicsample_conditions_1
3D CCH-TOCSY aliphaticsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D simultaneous CN NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D simultaneous CN NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC high res. (L/V stereoassignment)sample_3isotropicsample_conditions_1
2D 1H-15N hetNOEsample_3isotropicsample_conditions_1
2D 1H-15N T1sample_3isotropicsample_conditions_1
2D 1H-13C HSQC (arom)sample_1isotropicsample_conditions_1
2D 1H-15N T2sample_3isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY v3.113, Goddard - data analysis, peak picking

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF validation

PSVS v1.3, Bhattacharya and Montelione - structure validation

PDBStat v5.0, Tejero and Montelione - PDB analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB