BMRB Entry 18725
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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/BMR18725
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Title: Structure of Faap24 residues 141-215 PubMed: 23661679
Deposition date: 2012-09-18 Original release date: 2013-04-29
Authors: Wienk, Hans; Slootweg, Jack; Kaptein, Robert; Boelens, Rolf; Folkers, Gert
Citation: Wienk, Hans; Slootweg, Jack; Speerstra, Sietske; Kaptein, Robert; Boelens, Rolf; Folkers, Gert. "The Fanconi anemia associated protein FAAP24 uses two substrate specific binding surfaces for DNA recognition." Nucleic Acids Res. 41, 6739-6749 (2013).
Assembly members:
Faap24, polymer, 95 residues, 10411.190 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):
Faap24: MGSSHHHHHHSSHMLVPRGS
SKNPLLGKKRALLLSEPSLL
RTVQQIPGVGKVKAPLLLQK
FPSIQQLSNASIGELEQVVG
QAVAQQIHAFFTQPR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 341 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 560 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Faap24 | 1 |
Entities:
Entity 1, Faap24 95 residues - 10411.190 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | HIS | MET | LEU | VAL | PRO | ARG | GLY | SER | ||||
| 3 | SER | LYS | ASN | PRO | LEU | LEU | GLY | LYS | LYS | ARG | ||||
| 4 | ALA | LEU | LEU | LEU | SER | GLU | PRO | SER | LEU | LEU | ||||
| 5 | ARG | THR | VAL | GLN | GLN | ILE | PRO | GLY | VAL | GLY | ||||
| 6 | LYS | VAL | LYS | ALA | PRO | LEU | LEU | LEU | GLN | LYS | ||||
| 7 | PHE | PRO | SER | ILE | GLN | GLN | LEU | SER | ASN | ALA | ||||
| 8 | SER | ILE | GLY | GLU | LEU | GLU | GLN | VAL | VAL | GLY | ||||
| 9 | GLN | ALA | VAL | ALA | GLN | GLN | ILE | HIS | ALA | PHE | ||||
| 10 | PHE | THR | GLN | PRO | ARG |
Samples:
sample_1: FAAP24, [U-100% 13C; U-100% 15N], 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; PMSF 0.2 mM; D2O 7%; H2O 93%
sample_conditions_1: pH: 6.5; 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 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
ProcheckNMR, Laskowski and MacArthur - data analysis
WhatIF, Vriend - data analysis
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 19303 |
| PDB | |
| DBJ | BAG54708 |
| GB | AAH03535 AAH10170 AAH20247 ADQ32151 AIC52732 |
| REF | NP_001287907 NP_689479 XP_002762034 XP_003780763 XP_003816251 |
| SP | Q9BTP7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts