BMRB Entry 18570
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18570
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Title: Solution structure of the zinc finger AFV1p06 protein from the hyperthermophilic archaeal virus AFV1 PubMed: 23326363
Deposition date: 2012-07-05 Original release date: 2013-01-28
Authors: Guilliere, Florence; Sezonov, Guennadi; Prangishvili, David; Delepierre, Muriel; Guijarro, J. Inaki
Citation: Guilliere, Florence; Danioux, Chloe; Jaubert, Carole; Desnoues, Nicole; Delepierre, Muriel; Prangishvili, David; Sezonov, Guennadi; Guijarro, J. Inaki. "Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold" PLoS One 8, e52908-e52908 (2013).
Assembly members:
AFV1p06, polymer, 59 residues, 5437.367 Da.
ZINC ION, non-polymer, 65.409 Da.
Natural source: Common Name: Acidianus Filamentous Virus 1 (AFV1) Taxonomy ID: 235266 Superkingdom: Viruses Kingdom: not available Genus/species: Gammalipothrixvirus Acidianus Filamentous Virus 1 (AFV1)
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
AFV1p06: MIEVSSMERVYQCLRCGLTF
RTKKQLIRHLVNTEKVNPLS
IDYYYQSFSVSLKDVNKII
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 271 |
| 15N chemical shifts | 59 |
| 1H chemical shifts | 434 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | zinc finger AFV1p06 protein | 1 |
| 2 | ZINC ION | 2 |
Entities:
Entity 1, zinc finger AFV1p06 protein 59 residues - 5437.367 Da.
Residues 1-7 and 51-59 are disordered; only residues 7-51 are included in the structures
| 1 | MET | ILE | GLU | VAL | SER | SER | MET | GLU | ARG | VAL | ||||
| 2 | TYR | GLN | CYS | LEU | ARG | CYS | GLY | LEU | THR | PHE | ||||
| 3 | ARG | THR | LYS | LYS | GLN | LEU | ILE | ARG | HIS | LEU | ||||
| 4 | VAL | ASN | THR | GLU | LYS | VAL | ASN | PRO | LEU | SER | ||||
| 5 | ILE | ASP | TYR | TYR | TYR | GLN | SER | PHE | SER | VAL | ||||
| 6 | SER | LEU | LYS | ASP | VAL | ASN | LYS | ILE | ILE |
Entity 2, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: AFV1p06, [U-98% 13C; U-98% 15N], 0.8-1 mM; Na-HEPES 50 mM; NaCl 150 mM; ZnCl2 50 uM; DTT 3 mM
sample_conditions_1: ionic strength: 200 mM; pH: 7.4; pressure: 1 atm; temperature: 298.15 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-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCD)HD aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCDCE)HE aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.3A, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5.3, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
ARIA v2.2, Linge, O, . - Automated NOE assignment, structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution, water refinement
TALOS, Cornilescu, Delaglio and Bax - Dihedral constraints
Procheck v3.5.4, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - Structure analysis
WhatCheck, Vriend - Structure analysis
Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis
NMR spectrometers:
- Varian NMR System 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts