BMRB Entry 15849
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15849
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Title: SOLUTION NMR STRUCTURE OF the second OB-fold domain of replication protein A from Methanococcus maripaludis. NORTHEAST STRUCTURAL GENOMICS TARGET MrR110B.
Deposition date: 2008-06-30 Original release date: 2008-07-01
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 450 |
| 15N chemical shifts | 105 |
| 1H chemical shifts | 708 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MrR110B | 1 |
Entities:
Entity 1, MrR110B 104 residues - 11631.229 Da.
C-terminal LEHHHHHH purification tag.
| 1 | MET | ASN | TYR | LYS | ILE | SER | GLU | LEU | MET | PRO | ||||
| 2 | ASN | LEU | SER | GLY | THR | ILE | ASN | ALA | GLU | VAL | ||||
| 3 | VAL | ALA | ALA | TYR | PRO | LYS | LYS | GLU | PHE | SER | ||||
| 4 | ARG | LYS | ASP | GLY | THR | LYS | GLY | GLN | LEU | LYS | ||||
| 5 | SER | LEU | PHE | LEU | LYS | ASP | ASP | THR | GLY | SER | ||||
| 6 | ILE | ARG | GLY | THR | LEU | TRP | ASN | GLU | LEU | ALA | ||||
| 7 | ASP | PHE | GLU | VAL | LYS | LYS | GLY | ASP | ILE | ALA | ||||
| 8 | GLU | VAL | SER | GLY | TYR | VAL | LYS | GLN | GLY | TYR | ||||
| 9 | SER | GLY | LEU | GLU | ILE | SER | VAL | ASP | ASN | ILE | ||||
| 10 | GLY | ILE | ILE | GLU | LYS | SER | LEU | GLU | HIS | HIS | ||||
| 11 | HIS | HIS | HIS | HIS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D simultaneous CN NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D simultaneous CN NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC high res. (L/V stereoassignment) | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N hetNOE | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N T1 | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N T2 | sample_3 | isotropic | sample_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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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