BMRB Entry 18533
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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/BMR18533
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Title: NMR solution structure of apo-MptpA
Deposition date: 2012-06-19 Original release date: 2012-08-13
Authors: Stehle, Tanja; Sreeramulu, Sridhar; Loehr, Frank; Richter, Christian; Saxena, Krishna; Jonker, Hendrik; Schwalbe, Harald
Citation: Stehle, Tanja; Sreeramulu, Sridhar; Loehr, Frank; Richter, Christian; Saxena, Krishna; Jonker, Hendrik; Schwalbe, Harald. "The apo-structure of the low-molecular-weight protein tyrosine phosphatase A (MptpA) from Mycobacterium tuberculosis allows for better target-specific drug development" J. Biol. Chem. ., .-. (2012).
Assembly members:
mptpa, polymer, 164 residues, 17976.248 Da.
Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
mptpa: GMSDPLHVTFVCTGNICRSP
MAEKMFAQQLRHRGLGDAVR
VTSAGTGNWHVGSCADERAA
GVLRAHGYPTDHRAAQVGTE
HLAADLLVALDRNHARLLRQ
LGVEAARVRMLRSFDPRSGT
HALDVEDPYYGDHSDFEEVF
AVIESALPGLHDWVDERLAR
NGPS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 516 |
| 15N chemical shifts | 159 |
| 1H chemical shifts | 1056 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | mptpa | 1 |
Entities:
Entity 1, mptpa 164 residues - 17976.248 Da.
The N-terminal Glycine 0 originates from cloning
| 1 | GLY | MET | SER | ASP | PRO | LEU | HIS | VAL | THR | PHE | ||||
| 2 | VAL | CYS | THR | GLY | ASN | ILE | CYS | ARG | SER | PRO | ||||
| 3 | MET | ALA | GLU | LYS | MET | PHE | ALA | GLN | GLN | LEU | ||||
| 4 | ARG | HIS | ARG | GLY | LEU | GLY | ASP | ALA | VAL | ARG | ||||
| 5 | VAL | THR | SER | ALA | GLY | THR | GLY | ASN | TRP | HIS | ||||
| 6 | VAL | GLY | SER | CYS | ALA | ASP | GLU | ARG | ALA | ALA | ||||
| 7 | GLY | VAL | LEU | ARG | ALA | HIS | GLY | TYR | PRO | THR | ||||
| 8 | ASP | HIS | ARG | ALA | ALA | GLN | VAL | GLY | THR | GLU | ||||
| 9 | HIS | LEU | ALA | ALA | ASP | LEU | LEU | VAL | ALA | LEU | ||||
| 10 | ASP | ARG | ASN | HIS | ALA | ARG | LEU | LEU | ARG | GLN | ||||
| 11 | LEU | GLY | VAL | GLU | ALA | ALA | ARG | VAL | ARG | MET | ||||
| 12 | LEU | ARG | SER | PHE | ASP | PRO | ARG | SER | GLY | THR | ||||
| 13 | HIS | ALA | LEU | ASP | VAL | GLU | ASP | PRO | TYR | TYR | ||||
| 14 | GLY | ASP | HIS | SER | ASP | PHE | GLU | GLU | VAL | PHE | ||||
| 15 | ALA | VAL | ILE | GLU | SER | ALA | LEU | PRO | GLY | LEU | ||||
| 16 | HIS | ASP | TRP | VAL | ASP | GLU | ARG | LEU | ALA | ARG | ||||
| 17 | ASN | GLY | PRO | SER |
Samples:
sample_13C15N: mptpa, [U-100% 13C; U-100% 15N], 1.2 mM; arginine / glutamine 50 mM; HEPES 25 mM; DTT 10 mM; H2O 90%; D2O 10%
sample_15N: mptpa, [U-100% 15N], 1.0 mM; arginine / glutamine 50 mM; HEPES 25 mM; DTT 10 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0 M; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_15N | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_13C15N | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_13C15N | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_13C15N | isotropic | sample_conditions_1 |
| 3D (H)C(NC)H | sample_13C15N | isotropic | sample_conditions_1 |
| 3D HCD(CG)CB-TOCSY | sample_13C15N | isotropic | sample_conditions_1 |
| 3D (H)CC(CO)NH-TOCSY | sample_13C15N | isotropic | sample_conditions_1 |
| 3D (H)CB(CG)CCH-TOCSY | sample_13C15N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_13C15N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_13C15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_15N | isotropic | sample_conditions_1 |
| 2D (T1,T2,HetNOE) 1H-15N HSQC | sample_15N | isotropic | sample_conditions_1 |
| 2D (IPAP) 1H-15N HSQC | sample_15N | isotropic | sample_conditions_1 |
| 2D (IPAP) 1H-15N HSQC | sample_15N | anisotropic | sample_conditions_1 |
| 3D HNHA | sample_15N | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
SPARKY v3.114, Goddard - chemical shift assignment, data analysis, peak picking
CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA v3.9, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
ARIA v1.2, Linge, O, . - refinement, structure solution
NMR spectrometers:
- Bruker Avance 950 MHz
- Bruker Avance 900 MHz
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| UniProtKB/Swiss-Prot | P65716 |
| BMRB | 19361 19388 26513 |
| PDB | |
| DBJ | BAH26529 BAL66249 BAQ06307 GAA45923 |
| EMBL | CAL72239 CCC27315 CCC44588 CCC64828 CCE37704 |
| GB | AAK46577 ABQ74015 ABR06594 ACT24805 AEB03885 |
| REF | NP_216750 NP_855907 WP_003411510 WP_003899227 WP_015288274 |
| SP | P65717 P9WIA0 P9WIA1 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts