BMRB Entry 5561
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5561
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Jimenez, M. Angeles; Villegas, Virtudes; Santoro, Jorge; Serrano, Luis; Vendrell, Josep; Aviles, F. Xavier; Rico, Manuel. "NMR Solution Structure of the Activation Domain of Human Procarboxipeptidase A2" Protein Sci. 12, 296-305 (2003).
PubMed: 12538893
Assembly members:
Activation domain of human procarboxipeptidase, polymer, 81 residues, 9212 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: pTZ18U
Entity Sequences (FASTA):
Activation domain of human procarboxipeptidase: MRSLETFVGDQVLEIVPSNE
EQIKNLLQLEAQEHLQLDFW
KSPTTPGETAHVRVPFVNVQ
AVKVFLESQGIAYSIMIEDV
Q
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 87 |
| 1H chemical shifts | 599 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ADA2h | 1 |
Entities:
Entity 1, ADA2h 81 residues - 9212 Da.
| 1 | MET | ARG | SER | LEU | GLU | THR | PHE | VAL | GLY | ASP | ||||
| 2 | GLN | VAL | LEU | GLU | ILE | VAL | PRO | SER | ASN | GLU | ||||
| 3 | GLU | GLN | ILE | LYS | ASN | LEU | LEU | GLN | LEU | GLU | ||||
| 4 | ALA | GLN | GLU | HIS | LEU | GLN | LEU | ASP | PHE | TRP | ||||
| 5 | LYS | SER | PRO | THR | THR | PRO | GLY | GLU | THR | ALA | ||||
| 6 | HIS | VAL | ARG | VAL | PRO | PHE | VAL | ASN | VAL | GLN | ||||
| 7 | ALA | VAL | LYS | VAL | PHE | LEU | GLU | SER | GLN | GLY | ||||
| 8 | ILE | ALA | TYR | SER | ILE | MET | ILE | GLU | ASP | VAL | ||||
| 9 | GLN |
Samples:
sample-1: Activation domain of human procarboxipeptidase 2.0 mM; sodium phosphate buffer 50 mM
sample-2: Activation domain of human procarboxipeptidase, [U-95.5% 15N], 2.0 mM; sodium phosphate buffer 50 mM
Exp_cond-1: pH: 7.0; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H COSY | not available | not available | not available |
| 2D 1H-1H TOCSY | not available | not available | not available |
| 2D 1H-1H NOESY | not available | not available | not available |
| 2D 1H-15N HSQC | not available | not available | not available |
| 3D 1H-1H-15N NOESY | not available | not available | not available |
| 3D 1H-1H-15N TOCSY | not available | not available | not available |
| 2D 1H-13C HSQC | not available | not available | not available |
Software:
XEASY -
NMR spectrometers:
- Bruker AMX 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAG56890 |
| GB | AAA74425 AAH07009 AAH14571 AAH15140 AAP36067 |
| REF | NP_001860 XP_001156440 XP_002818494 XP_003813529 |
| SP | P48052 |
| AlphaFold | P48052 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks