BMRB Entry 19508
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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/BMR19508
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Title: Solution structure of the human wild type FAPP1-PH domain
Deposition date: 2013-09-19 Original release date: 2014-09-22
Authors: Lenoir, Marc; Overduin, Michael
Citation: Lenoir, Marc; Overduin, Michael. "Solution structure of the human wild type FAPP1-PH domain" Not known ., .-..
Assembly members:
entity, polymer, 108 residues, 12236.042 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
Entity Sequences (FASTA):
entity: GPLGSPEFMEGVLYKWTNYL
TGWQPRWFVLDNGILSYYDS
QDDVCKGSKGSIKMAVCEIK
VHSADNTRMELIIPGEQHFY
MKAVNAAERQRWLVALGSSK
ACLTDTRT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 400 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 688 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | human wild type FAPP1-PH domain | 1 |
Entities:
Entity 1, human wild type FAPP1-PH domain 108 residues - 12236.042 Da.
| 1 | GLY | PRO | LEU | GLY | SER | PRO | GLU | PHE | MET | GLU | ||||
| 2 | GLY | VAL | LEU | TYR | LYS | TRP | THR | ASN | TYR | LEU | ||||
| 3 | THR | GLY | TRP | GLN | PRO | ARG | TRP | PHE | VAL | LEU | ||||
| 4 | ASP | ASN | GLY | ILE | LEU | SER | TYR | TYR | ASP | SER | ||||
| 5 | GLN | ASP | ASP | VAL | CYS | LYS | GLY | SER | LYS | GLY | ||||
| 6 | SER | ILE | LYS | MET | ALA | VAL | CYS | GLU | ILE | LYS | ||||
| 7 | VAL | HIS | SER | ALA | ASP | ASN | THR | ARG | MET | GLU | ||||
| 8 | LEU | ILE | ILE | PRO | GLY | GLU | GLN | HIS | PHE | TYR | ||||
| 9 | MET | LYS | ALA | VAL | ASN | ALA | ALA | GLU | ARG | GLN | ||||
| 10 | ARG | TRP | LEU | VAL | ALA | LEU | GLY | SER | SER | LYS | ||||
| 11 | ALA | CYS | LEU | THR | ASP | THR | ARG | THR |
Samples:
sample_1: entity, [U-13C; U-15N], 500 – 800 uM; DTT 1 mM; TRIS 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 240 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
ANALYSIS v2.2, CCPN - assignment
ARIA, Linge, O, . - structure solution
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 900 MHz
Related Database Links:
| BMRB | 16082 19576 |
| PDB | |
| DBJ | BAG37067 |
| GB | AAG15199 AAG15200 AAH31110 AAH44567 AAH83759 |
| REF | NP_001013095 NP_001095383 NP_001230393 NP_061964 NP_112546 |
| SP | Q9ERS4 Q9HB20 |
| TPG | DAA32821 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts