BMRB Entry 18016
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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/BMR18016
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Title: Solution structure of MSMEG_1053, the second DUF3349 annotated protein in the genome of Mycobacterium smegmatis. Seattle Structural Genomics Center for Infectious Disease (SSGCID) target MysmA.17112.b
Deposition date: 2011-10-22 Original release date: 2011-11-29
Authors: Buchko, Garry
Citation: Buchko, Garry; Edwards, Thomas; Abendroth, Jan; Napuli, Alberto; Hewitt, Stephen; Phan, Isabelle; Van Voorhis, Wesley; Kim, Chang-Yub; Myler, Peter. "Different structures for two DUF3349 annotated proteins in the genome of Mycobacterium smegmatis suggest a structural diversity within the DUF3349 superfamily." Not known ., .-..
Assembly members:
entity, polymer, 112 residues, 12434.074 Da.
Natural source: Common Name: High GC Gram+ Taxonomy ID: 1772 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium smegmatis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GPGSMVNAFLAKIAAWLNAG
YPEGVPGPDRVPLLALLTRR
LTNDEIKAIAEDLEKRAHFD
HIDIGVLITQMTDEMPREED
IERVRRHLALQGWPLDDPRD
GEEPDGESGGPR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 453 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 744 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SSGCID | 1 |
Entities:
Entity 1, SSGCID 112 residues - 12434.074 Da.
Residues 1-4 represent non-native residues that remain after the removal of an N-terminal affinity tag.
| 1 | GLY | PRO | GLY | SER | MET | VAL | ASN | ALA | PHE | LEU | ||||
| 2 | ALA | LYS | ILE | ALA | ALA | TRP | LEU | ASN | ALA | GLY | ||||
| 3 | TYR | PRO | GLU | GLY | VAL | PRO | GLY | PRO | ASP | ARG | ||||
| 4 | VAL | PRO | LEU | LEU | ALA | LEU | LEU | THR | ARG | ARG | ||||
| 5 | LEU | THR | ASN | ASP | GLU | ILE | LYS | ALA | ILE | ALA | ||||
| 6 | GLU | ASP | LEU | GLU | LYS | ARG | ALA | HIS | PHE | ASP | ||||
| 7 | HIS | ILE | ASP | ILE | GLY | VAL | LEU | ILE | THR | GLN | ||||
| 8 | MET | THR | ASP | GLU | MET | PRO | ARG | GLU | GLU | ASP | ||||
| 9 | ILE | GLU | ARG | VAL | ARG | ARG | HIS | LEU | ALA | LEU | ||||
| 10 | GLN | GLY | TRP | PRO | LEU | ASP | ASP | PRO | ARG | ASP | ||||
| 11 | GLY | GLU | GLU | PRO | ASP | GLY | GLU | SER | GLY | GLY | ||||
| 12 | PRO | ARG |
Samples:
sample_1: MSMEG_1053, [U-99% 13C; U-99% 15N], 1.0 ± 0.1 mM; sodium chloride 100 ± 2 mM; DTT 1 ± 0.1 mM; TRIS 20 ± 0.5 mM; H2O 93%; D2O 7%
sample_2: MSMEG_1053, [U-99% 13C; U-99% 15N], 1.0 ± 0.1 mM; sodium chloride 100 ± 2 mM; DTT 1 ± 0.1 mM; TRIS 20 ± 0.5 mM; D2O 100%
sample_conditions_1: ionic strength: 0.12 M; pH: 7.0; pressure: 1 atm; temperature: 293 K
sample_conditions_2: ionic strength: 0.12 M; pH: 7.0; 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 | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCDHD | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
| DEUTERIUM EXCHANGE | sample_2 | isotropic | sample_conditions_2 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
FELIX v2007, Accelrys Software Inc. - processing
SPARKY v3.115, Goddard - data analysis, peak picking
CNSSOLVE v2.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS v1.3, Bhattacharya and Montelione - data analysis
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
Related Database Links:
| PDB | |
| EMBL | CKH10149 |
| GB | ABK71419 AFP37510 AIU06313 AIU12938 AIU19562 |
| REF | WP_003892430 YP_885459 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts