BMRB Entry 5629
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5629
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Title: 1H, 13C, and 15N resonance assignments and topology of MTH187, a conserved protein from Methanobacterium thermoautotrophicum PubMed: 16819590
Deposition date: 2002-12-18 Original release date: 2007-11-05
Authors: Gignac, Isabelle; Yee, Adelinda; Suh, Jeong Yong; Ziembirka, Anna; Arrowsmith, Cheryl; Sykes, Brian; Gagne, Stephane
Citation: Julien, Olivier; Gignac, Isabelle; Hutton, Anna; Yee, Adelinda; Arrowsmith, Cheryl; Gagne, Stephane. "MTH187 from Methanobacterium thermoautotrophicum has three HEAT-like Repeats" J. Biomol. NMR 35, 149-154 (2006).
Assembly members:
MTH187, polymer, 111 residues, 12395 Da.
Natural source: Common Name: Methanobacteria thermoautotrophicum Taxonomy ID: 183925 Superkingdom: Archaea Kingdom: not available Genus/species: Methanobacteria thermoautotrophicum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MTH187: MADENKWVRRDVSTALSRMG
DEAFEPLLESLSNEDWRIRG
AAAWIIGNFQDERAVEPLIK
LLEDDSGFVRSGAARSLEQI
GGERVRAAMEKLAETGTGFA
RKVAVNYLETH
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 725 |
| 13C chemical shifts | 440 |
| 15N chemical shifts | 118 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MTH187 | 1 |
Entities:
Entity 1, MTH187 111 residues - 12395 Da.
| 1 | MET | ALA | ASP | GLU | ASN | LYS | TRP | VAL | ARG | ARG | ||||
| 2 | ASP | VAL | SER | THR | ALA | LEU | SER | ARG | MET | GLY | ||||
| 3 | ASP | GLU | ALA | PHE | GLU | PRO | LEU | LEU | GLU | SER | ||||
| 4 | LEU | SER | ASN | GLU | ASP | TRP | ARG | ILE | ARG | GLY | ||||
| 5 | ALA | ALA | ALA | TRP | ILE | ILE | GLY | ASN | PHE | GLN | ||||
| 6 | ASP | GLU | ARG | ALA | VAL | GLU | PRO | LEU | ILE | LYS | ||||
| 7 | LEU | LEU | GLU | ASP | ASP | SER | GLY | PHE | VAL | ARG | ||||
| 8 | SER | GLY | ALA | ALA | ARG | SER | LEU | GLU | GLN | ILE | ||||
| 9 | GLY | GLY | GLU | ARG | VAL | ARG | ALA | ALA | MET | GLU | ||||
| 10 | LYS | LEU | ALA | GLU | THR | GLY | THR | GLY | PHE | ALA | ||||
| 11 | ARG | LYS | VAL | ALA | VAL | ASN | TYR | LEU | GLU | THR | ||||
| 12 | HIS |
Samples:
sample_1: MTH187, [U-13C; U-15N], 0.47 mM; potassium phosphate 25 mM; CHAPS 22 mM; NaCl 10 mM; DSS 0.5 mM; H2O 90%; D2O 10%
sample_2: MTH187, [U-15N], 0.4 – 0.7 mM; potassium phosphate 25 mM; CHAPS 22 mM; NaCl 10 mM; DSS 0.5 mM
condition_set_1: pH: 6.2 na; temperature: 321.2 K; ionic strength: 0.06 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 15N-TOCSY-HSQC acquired at 500MHz, mix=100ms | not available | not available | condition_set_1 |
| 15N-NOESY-HSQC acquired at 800MHz, mix=100ms | not available | not available | condition_set_1 |
| others acquired at 600MHz | not available | not available | condition_set_1 |
Software:
nmrview v5.0.4 -
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts