BMRB Entry 15821
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15821
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Title: Structure of uncharacterized protein MJ1198 from Methanocaldococcus jannaschii. Northeast Structural Genomics Target MjR117B
Deposition date: 2008-06-24 Original release date: 2008-07-15
Authors: Rossi, Paolo; Maglaqui, Melissa; Foote, Erica; Hamilton, Keith; Ciccosanti, Coleen; Xiao, Rong; Nair, Rajesh; Swapna, G.V.T.; Everett, John; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Structure of uncharacterized protein MJ1198 from Methanocaldococcus jannaschii. Northeast Structural Genomics Target MjR117B" Not known ., .-..
Assembly members:
MjR117B, polymer, 74 residues, 8674.141 Da.
Natural source: Common Name: Methanococcus jannaschii Taxonomy ID: 2190 Superkingdom: Archaea Kingdom: not available Genus/species: Methanococcus jannaschii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MjR117B: MDVEPGKFYKGVVTRIEKYG
AFINLNEQVRGLLRPRDMIS
LRLENLNVGDEIIVQAIDVR
PEKREIDFKYIPLE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 346 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 566 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MJ1198 | 1 |
Entities:
Entity 1, MJ1198 74 residues - 8674.141 Da.
N-term M is a cloning artifact and the C-term LE is part of the purification tag
| 1 | MET | ASP | VAL | GLU | PRO | GLY | LYS | PHE | TYR | LYS | ||||
| 2 | GLY | VAL | VAL | THR | ARG | ILE | GLU | LYS | TYR | GLY | ||||
| 3 | ALA | PHE | ILE | ASN | LEU | ASN | GLU | GLN | VAL | ARG | ||||
| 4 | GLY | LEU | LEU | ARG | PRO | ARG | ASP | MET | ILE | SER | ||||
| 5 | LEU | ARG | LEU | GLU | ASN | LEU | ASN | VAL | GLY | ASP | ||||
| 6 | GLU | ILE | ILE | VAL | GLN | ALA | ILE | ASP | VAL | ARG | ||||
| 7 | PRO | GLU | LYS | ARG | GLU | ILE | ASP | PHE | LYS | TYR | ||||
| 8 | ILE | PRO | LEU | GLU |
Samples:
sample_1: MjR117B, [U-100% 13C; U-100% 15N], 1.682 mM; ammonium acetate 20 mM; sodium chloride 100 mM; sodium azide 0.02 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; protease inhibitor 1x mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_2: MjR117B, [5% 13C; U-100% 15N], 1.226 mM; ammonium acetate 20 mM; sodium chloride 100 mM; sodium azide 0.02 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; protease inhibitor 1x mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 4.5; 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 SIM 13C,15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D ARO 13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC Stereo | sample_2 | isotropic | sample_conditions_1 |
| 2D HETNOE | sample_2 | isotropic | sample_conditions_1 |
| pseudo 2D N15 T1 | sample_2 | isotropic | sample_conditions_1 |
| pseudo 2D N15 T2 (CPMG) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC CT ARO | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
SPARKY v3.113, Goddard - data analysis
TOPSPIN v2.1, Bruker Biospin - collection
RPF(AutoStructure) v2.2.1, Huang, Tejero, Powers and Montelione - validation
PSVS v1.3, Bhattacharya and Montelione - validation
Molmol, Koradi, Billeter and Wuthrich - visualization
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - validation
MolProbity, Richardson - validation
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| GB | AAB99202 ACV24909 ADC69513 AIJ05492 |
| REF | WP_012980423 WP_015791645 WP_048201674 |
| SP | Q58598 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts