BMRB Entry 16007
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16007
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR structure of the protein TM1367 PubMed: 20944235
Deposition date: 2008-10-27 Original release date: 2009-04-14
Authors: Mohanty, Biswaranjan; Pedrini, Bill; Serrano, Pedro; Geralt, Michel; Horst, Reto; Wilson, Ian; Wuthrich, Kurt
Citation: Mohanty, Biswaranjan; Serrano, Pedro; Pedrini, Bill; Jaudzems, Kristaps; Geralt, Michael; Horst, Reto; Herrmann, Torsten; Elsliger, Marc Andre; Wilson, Ian; Wuthrich, Kurt. "Comparison of NMR and crystal structures for the proteins TM1112 and TM1367." Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 1381-1392 (2010).
Assembly members:
TM1367, polymer, 124 residues, 13923 Da.
Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: thermotogae Genus/species: Thermotoga maritima
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TM1367: MRVELLFESGKCVIDLNEEY
EVVKLLKEKIPFESVVNTWG
EEIYFSTPVNVQKMENPREV
VEIGDVGYWPPGKALCLFFG
KTPMSDDKIQPASAVNVIGK
IVEGLEDLKKIKDGEKVAVR
FASS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 439 |
| 15N chemical shifts | 126 |
| 1H chemical shifts | 920 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TM1367 | 1 |
Entities:
Entity 1, TM1367 124 residues - 13923 Da.
| 1 | MET | ARG | VAL | GLU | LEU | LEU | PHE | GLU | SER | GLY | ||||
| 2 | LYS | CYS | VAL | ILE | ASP | LEU | ASN | GLU | GLU | TYR | ||||
| 3 | GLU | VAL | VAL | LYS | LEU | LEU | LYS | GLU | LYS | ILE | ||||
| 4 | PRO | PHE | GLU | SER | VAL | VAL | ASN | THR | TRP | GLY | ||||
| 5 | GLU | GLU | ILE | TYR | PHE | SER | THR | PRO | VAL | ASN | ||||
| 6 | VAL | GLN | LYS | MET | GLU | ASN | PRO | ARG | GLU | VAL | ||||
| 7 | VAL | GLU | ILE | GLY | ASP | VAL | GLY | TYR | TRP | PRO | ||||
| 8 | PRO | GLY | LYS | ALA | LEU | CYS | LEU | PHE | PHE | GLY | ||||
| 9 | LYS | THR | PRO | MET | SER | ASP | ASP | LYS | ILE | GLN | ||||
| 10 | PRO | ALA | SER | ALA | VAL | ASN | VAL | ILE | GLY | LYS | ||||
| 11 | ILE | VAL | GLU | GLY | LEU | GLU | ASP | LEU | LYS | LYS | ||||
| 12 | ILE | LYS | ASP | GLY | GLU | LYS | VAL | ALA | VAL | ARG | ||||
| 13 | PHE | ALA | SER | SER |
Samples:
sample_1: DTT 0.5 mM; D10-DTT 4.5 mM; sodium azide 0.03%; sodium chloride 50 mM; sodium phosphate 25 mM; D2O 10%; H2O 90%; TM1367, [U-98% 13C; U-98% 15N], 1.5 mM
sample_conditions_1: ionic strength: 0.2 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D [15N,1H] HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D [13C,1H] HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N - resolved [1H,1H] NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-resolved [1H,1H] NOESY, aliphatic 13C | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-resolved [1H,1H] NOESY, aromatic 13C | sample_1 | isotropic | sample_conditions_1 |
| 4D-APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D-APSY-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D-APSY-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA vCYANA3.0, Guntert, Mumenthaler and Wuthrich - structure solution
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
CARA, Keller and Wuthrich - data analysis
Molmol, Koradi, Billeter and Wuthrich - data analysis
TOPSPIN v1.3, Bruker Biospin - processing
ASCAN, (ASCAN)-Fiorito,Herrmann,Damberger and Wuthrich - chemical shift assignment
MATCH, (MATCH)-Volk, Herrmann and K. Wuthrich - chemical shift assignment
ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| GB | AAD36437 ABQ47429 ACB09806 ADA67518 AGL50298 |
| REF | NP_229168 WP_004081563 WP_011943885 WP_012311149 WP_038034479 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts