BMRB Entry 15599
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15599
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Citation: Gong, Weibin; Li, Yifei; Cui, Gaofeng; Hu, Jicheng; Fang, Huaming; Jin, Changwen; Xia, Bin. "Solution structure and catalytic mechanism of human protein histidine phosphatase 1." Biochemistry 418, 337-344 (2008).
PubMed: 18991813
Assembly members:
entity_phpt1_lower, polymer, 125 residues, 13833.00 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
entity_phpt1_lower: MAVADLALIPDVDIDSDGVF
KYVLIRVHSAPRSGAPAAES
KEIVRGYKWAEYHADIYDKV
SGDMQKQGCDCECLGGGRIS
HQSQDKKIHVYGYSMAYGPA
QHAISTEKIKAKYPDYEVTW
ANDGY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 357 |
| 15N chemical shifts | 109 |
| 1H chemical shifts | 706 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PHPT1 monomer | 1 |
Entities:
Entity 1, PHPT1 monomer 125 residues - 13833.00 Da.
| 1 | MET | ALA | VAL | ALA | ASP | LEU | ALA | LEU | ILE | PRO | ||||
| 2 | ASP | VAL | ASP | ILE | ASP | SER | ASP | GLY | VAL | PHE | ||||
| 3 | LYS | TYR | VAL | LEU | ILE | ARG | VAL | HIS | SER | ALA | ||||
| 4 | PRO | ARG | SER | GLY | ALA | PRO | ALA | ALA | GLU | SER | ||||
| 5 | LYS | GLU | ILE | VAL | ARG | GLY | TYR | LYS | TRP | ALA | ||||
| 6 | GLU | TYR | HIS | ALA | ASP | ILE | TYR | ASP | LYS | VAL | ||||
| 7 | SER | GLY | ASP | MET | GLN | LYS | GLN | GLY | CYS | ASP | ||||
| 8 | CYS | GLU | CYS | LEU | GLY | GLY | GLY | ARG | ILE | SER | ||||
| 9 | HIS | GLN | SER | GLN | ASP | LYS | LYS | ILE | HIS | VAL | ||||
| 10 | TYR | GLY | TYR | SER | MET | ALA | TYR | GLY | PRO | ALA | ||||
| 11 | GLN | HIS | ALA | ILE | SER | THR | GLU | LYS | ILE | LYS | ||||
| 12 | ALA | LYS | TYR | PRO | ASP | TYR | GLU | VAL | THR | TRP | ||||
| 13 | ALA | ASN | ASP | GLY | TYR |
Samples:
sample_1: entity_phpt1_lower, [U-95% 13C; U-95% 15N], 1 mM; Tris-HCl 50 mM; NaCl 50 mM; D2O, [U-100% 2H], 10%; H2O 90%
sample_conditions_1: ionic strength: 0.15 M; pH: 7.2; pressure: 1 atm; temperature: 298 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Zhengrong and Bax - data analysis
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAI46371 |
| EMBL | CAB66579 CAG38512 CAL38548 |
| GB | AAF80759 AAG01156 AAH24648 AAN52504 ACJ13700 |
| REF | NP_001129333 NP_001274271 NP_054891 XP_001117869 XP_004048950 |
| SP | Q9NRX4 |
| AlphaFold | Q9NRX4 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks