BMRB Entry 17602
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17602
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Sarma, Akella; Anbanandam, Asokan; Kelm, Allek; Mehra-Chaudhary, Ritcha; Wei, Yirui; Qin, Peiwu; Lee, Yingying; Berjanskii, Mark; Mick, Jacob; Beamer, Lesa; Van Doren, Steven. "Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect." Biochemistry 51, 807-819 (2012).
PubMed: 22242625
Assembly members:
PMM-PGM, polymer, 463 residues, Formula weight is not available
MG, non-polymer, 24.305 Da.
Natural source: Common Name: P. aeruginosa Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET14b_PMM/PGM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 1394 |
| 15N chemical shifts | 523 |
| 1H chemical shifts | 523 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Monomer | 1 |
| 2 | Mg2+ | 2 |
Entities:
Entity 1, Monomer 463 residues - Formula weight is not available
| 1 | MET | SER | THR | VAL | LYS | ALA | PRO | THR | LEU | PRO | ||||
| 2 | ALA | SER | ILE | PHE | ARG | ALA | TYR | ASP | ILE | ARG | ||||
| 3 | GLY | VAL | VAL | GLY | ASP | THR | LEU | THR | ALA | GLU | ||||
| 4 | THR | ALA | TYR | TRP | ILE | GLY | ARG | ALA | ILE | GLY | ||||
| 5 | SER | GLU | SER | LEU | ALA | ARG | GLY | GLU | PRO | CYS | ||||
| 6 | VAL | ALA | VAL | GLY | ARG | ASP | GLY | ARG | LEU | SER | ||||
| 7 | GLY | PRO | GLU | LEU | VAL | LYS | GLN | LEU | ILE | GLN | ||||
| 8 | GLY | LEU | VAL | ASP | CYS | GLY | CYS | GLN | VAL | SER | ||||
| 9 | ASP | VAL | GLY | MET | VAL | PRO | THR | PRO | VAL | LEU | ||||
| 10 | TYR | TYR | ALA | ALA | ASN | VAL | LEU | GLU | GLY | LYS | ||||
| 11 | SER | GLY | VAL | MET | LEU | THR | GLY | SER | HIS | ASN | ||||
| 12 | PRO | PRO | ASP | TYR | ASN | GLY | PHE | LYS | ILE | VAL | ||||
| 13 | VAL | ALA | GLY | GLU | THR | LEU | ALA | ASN | GLU | GLN | ||||
| 14 | ILE | GLN | ALA | LEU | ARG | GLU | ARG | ILE | GLU | LYS | ||||
| 15 | ASN | ASP | LEU | ALA | SER | GLY | VAL | GLY | SER | VAL | ||||
| 16 | GLU | GLN | VAL | ASP | ILE | LEU | PRO | ARG | TYR | PHE | ||||
| 17 | LYS | GLN | ILE | ARG | ASP | ASP | ILE | ALA | MET | ALA | ||||
| 18 | LYS | PRO | MET | LYS | VAL | VAL | VAL | ASP | CYS | GLY | ||||
| 19 | ASN | GLY | VAL | ALA | GLY | VAL | ILE | ALA | PRO | GLN | ||||
| 20 | LEU | ILE | GLU | ALA | LEU | GLY | CYS | SER | VAL | ILE | ||||
| 21 | PRO | LEU | TYR | CYS | GLU | VAL | ASP | GLY | ASN | PHE | ||||
| 22 | PRO | ASN | HIS | HIS | PRO | ASP | PRO | GLY | LYS | PRO | ||||
| 23 | GLU | ASN | LEU | LYS | ASP | LEU | ILE | ALA | LYS | VAL | ||||
| 24 | LYS | ALA | GLU | ASN | ALA | ASP | LEU | GLY | LEU | ALA | ||||
| 25 | PHE | ASP | GLY | ASP | GLY | ASP | ARG | VAL | GLY | VAL | ||||
| 26 | VAL | THR | ASN | THR | GLY | THR | ILE | ILE | TYR | PRO | ||||
| 27 | ASP | ARG | LEU | LEU | MET | LEU | PHE | ALA | LYS | ASP | ||||
| 28 | VAL | VAL | SER | ARG | ASN | PRO | GLY | ALA | ASP | ILE | ||||
| 29 | ILE | PHE | ASP | VAL | LYS | CYS | THR | ARG | ARG | LEU | ||||
| 30 | ILE | ALA | LEU | ILE | SER | GLY | TYR | GLY | GLY | ARG | ||||
| 31 | PRO | VAL | MET | TRP | LYS | THR | GLY | HIS | SER | LEU | ||||
| 32 | ILE | LYS | LYS | LYS | MET | LYS | GLU | THR | GLY | ALA | ||||
| 33 | LEU | LEU | ALA | GLY | GLU | MET | SER | GLY | HIS | VAL | ||||
| 34 | PHE | PHE | LYS | GLU | ARG | TRP | PHE | GLY | PHE | ASP | ||||
| 35 | ASP | GLY | ILE | TYR | SER | ALA | ALA | ARG | LEU | LEU | ||||
| 36 | GLU | ILE | LEU | SER | GLN | ASP | GLN | ARG | ASP | SER | ||||
| 37 | GLU | HIS | VAL | PHE | SER | ALA | PHE | PRO | SER | ASP | ||||
| 38 | ILE | SER | THR | PRO | GLU | ILE | ASN | ILE | THR | VAL | ||||
| 39 | THR | GLU | ASP | SER | LYS | PHE | ALA | ILE | ILE | GLU | ||||
| 40 | ALA | LEU | GLN | ARG | ASP | ALA | GLN | TRP | GLY | GLU | ||||
| 41 | GLY | ASN | ILE | THR | THR | LEU | ASP | GLY | VAL | ARG | ||||
| 42 | VAL | ASP | TYR | PRO | LYS | GLY | TRP | GLY | LEU | VAL | ||||
| 43 | ARG | ALA | SER | ASN | THR | THR | PRO | VAL | LEU | VAL | ||||
| 44 | LEU | ARG | PHE | GLU | ALA | ASP | THR | GLU | GLU | GLU | ||||
| 45 | LEU | GLU | ARG | ILE | LYS | THR | VAL | PHE | ARG | ASN | ||||
| 46 | GLN | LEU | LYS | ALA | VAL | ASP | SER | SER | LEU | PRO | ||||
| 47 | VAL | PRO | PHE |
Entity 2, Mg2+ - Mg - 24.305 Da.
| 1 | MG |
Samples:
sample_1: PMM-PGM, [U-100% 13C; U-100% 15N; U-80% 2H], 1.0 mM; D2O, [U-99.9% 2H], 5%; H2O 95%; Magnesium Chloride 1 mM; MOPS 50 mM
PMM_sample_conditions_1: ionic strength: 0.003 M; pH: 7.4; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | PMM_sample_conditions_1 |
| 3D TROSY-HNCO | sample_1 | isotropic | PMM_sample_conditions_1 |
| 3D TROSY-HNCA | sample_1 | isotropic | PMM_sample_conditions_1 |
| 3D TROSY-HN(CO)CA | sample_1 | isotropic | PMM_sample_conditions_1 |
| 3D TROSY-HNCACB | sample_1 | isotropic | PMM_sample_conditions_1 |
| 3D TROSY-HNCACO | sample_1 | isotropic | PMM_sample_conditions_1 |
Software:
TOPSPIN v2.1.3, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 17652 |
| PDB | |
| DBJ | BAK92897 BAP25224 BAP54026 BAQ43263 BAR70810 |
| EMBL | CAW30471 CCQ87804 CDH74092 CDH80443 CDI93917 |
| GB | AAA25701 AAG08707 ABJ14705 ABR82184 AEO77919 |
| REF | NP_254009 WP_003098295 WP_003114359 WP_003117161 WP_003121305 |
| SP | P26276 Q02E40 |
| AlphaFold | P26276 Q02E40 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks