BMRB Entry 15819
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15819
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Title: Solution NMR Structure of the replication Factor A Related Protein from Methanobacterium thermoautotrophicum. Northeast Structural Genomics Target TR91A.
Deposition date: 2008-06-23 Original release date: 2008-08-08
Authors: Rossi, Paolo; Xiao, Rong; Maglaqui, Melissa; Foote, Erica; Ciccosanti, Coleen; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Everett, John; Montelione, Gaetano
Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Solution NMR Structure of the replication Factor A Related Protein from Methanobacterium thermoautotrophicum. Northeast Structural Genomics Target TR91A." Not known ., .-..
Assembly members:
TR91A, polymer, 110 residues, 12479.563 Da.
Natural source: Common Name: Methanobacterium thermoautotrophicum Taxonomy ID: 145262 Superkingdom: Archaea Kingdom: not available Genus/species: Methanobacterium thermoautotrophicum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TR91A: MKPEHRMDTISKLEEGAETP
VTGRVMKISSPRTFTTRKGR
EGKLANVIIADDTGELRAVF
WTENIKLLKKFREGDVIRIK
DVNIRGGFGGRKEAHLMPRS
TVEVLDPLEH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 475 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 761 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TR91A | 1 |
Entities:
Entity 1, TR91A 110 residues - 12479.563 Da.
| 1 | MET | LYS | PRO | GLU | HIS | ARG | MET | ASP | THR | ILE | |
| 2 | SER | LYS | LEU | GLU | GLU | GLY | ALA | GLU | THR | PRO | |
| 3 | VAL | THR | GLY | ARG | VAL | MET | LYS | ILE | SER | SER | |
| 4 | PRO | ARG | THR | PHE | THR | THR | ARG | LYS | GLY | ARG | |
| 5 | GLU | GLY | LYS | LEU | ALA | ASN | VAL | ILE | ILE | ALA | |
| 6 | ASP | ASP | THR | GLY | GLU | LEU | ARG | ALA | VAL | PHE | |
| 7 | TRP | THR | GLU | ASN | ILE | LYS | LEU | LEU | LYS | LYS | |
| 8 | PHE | ARG | GLU | GLY | ASP | VAL | ILE | ARG | ILE | LYS | |
| 9 | ASP | VAL | ASN | ILE | ARG | GLY | GLY | PHE | GLY | GLY | |
| 10 | ARG | LYS | GLU | ALA | HIS | LEU | MET | PRO | ARG | SER | |
| 11 | THR | VAL | GLU | VAL | LEU | ASP | PRO | LEU | GLU | HIS |
Samples:
sample_1: TR91A, [U-100% 13C; U-100% 15N], 1.25 mM; MES 20 mM; sodium chloride 100 mM; DTT 100 mM; Calcium Chloride 5 mM; sodium azide 0.02%
sample_2: TR91A, [U-100% 15N; 5% 13C], 1.33 mM; MES 20 mM; sodium chloride 100 mM; DTT 100 mM; Calcium Chloride 5 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_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom) | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D HET NOE | sample_2 | isotropic | sample_conditions_1 |
| Pseudo 2D T1 | sample_2 | isotropic | sample_conditions_1 |
| Pseudo 2D T2 (CPMG) | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (arom) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (stereomethyl) | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
SPARKY v3.113, Goddard - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
TOPSPIN v2.1, Bruker Biospin - collection
PSVS, Bhattacharya and Montelione - validation
RPF(AutoStructure), Huang, Tejero, Powers and Montelione - validation
Molmol, Koradi, Billeter and Wuthrich - visualization
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - validation
MolProbity, Richardson - validation
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts