BMRB Entry 25763
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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/BMR25763
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Title: Solution structure of an MbtH-like protein from Mycobacterium avium, Seattle Structural Genomics Center for Infectious Disease target MyavA.01649.c
Deposition date: 2015-08-20 Original release date: 2015-12-28
Authors: Buchko, Garry
Citation: Buchko, Garry; Hewitt, Stephen; Van Voorhis, Wesley; Myler, Peter. "Solution structure of a MbtH-like protein from Mycobacterium avium." Not known ., .-..
Assembly members:
entity, polymer, 80 residues, 8994.921 Da.
Natural source: Common Name: high GC Gram+ Taxonomy ID: 1794 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium avium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GPGSMSINPFDDDNGSFFVL
VNDEEQHSLWPAFADVPAGW
RVVHGEADRAACLEYIEEHW
PDIRPKSLRDKLATGRGFDQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 235 |
| 15N chemical shifts | 62 |
| 1H chemical shifts | 322 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 80 residues - 8994.921 Da.
The first four residues are non-native and remain after removal of the N-terminal tag containing a poly-histidine site.
| 1 | GLY | PRO | GLY | SER | MET | SER | ILE | ASN | PRO | PHE | |
| 2 | ASP | ASP | ASP | ASN | GLY | SER | PHE | PHE | VAL | LEU | |
| 3 | VAL | ASN | ASP | GLU | GLU | GLN | HIS | SER | LEU | TRP | |
| 4 | PRO | ALA | PHE | ALA | ASP | VAL | PRO | ALA | GLY | TRP | |
| 5 | ARG | VAL | VAL | HIS | GLY | GLU | ALA | ASP | ARG | ALA | |
| 6 | ALA | CYS | LEU | GLU | TYR | ILE | GLU | GLU | HIS | TRP | |
| 7 | PRO | ASP | ILE | ARG | PRO | LYS | SER | LEU | ARG | ASP | |
| 8 | LYS | LEU | ALA | THR | GLY | ARG | GLY | PHE | ASP | GLN |
Samples:
sample_1: sodium chloride 100 ± 3 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.01 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| deuterium exchange | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
Felix v2007, Accelrys Software Inc. - processing
SPARKY v3.115, Goddard - data analysis, peak picking
PSVS v1.5, Bhattacharya and Montelione - data analysis
NMR spectrometers:
- Agilent INOVA 600 MHz
- Agilent INOVA 500 MHz
- Agilent VNMRS 750 MHz
- Agilent VNMRS 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts