BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18570

Title: Solution structure of the zinc finger AFV1p06 protein from the hyperthermophilic archaeal virus AFV1   PubMed: 23326363

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

Data sets:
Data typeCount
13C chemical shifts271
15N chemical shifts59
1H chemical shifts434

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1zinc finger AFV1p06 protein1
2ZINC ION2

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   METILEGLUVALSERSERMETGLUARGVAL
2   TYRGLNCYSLEUARGCYSGLYLEUTHRPHE
3   ARGTHRLYSLYSGLNLEUILEARGHISLEU
4   VALASNTHRGLULYSVALASNPROLEUSER
5   ILEASPTYRTYRTYRGLNSERPHESERVAL
6   SERLEULYSASPVALASNLYSILEILE

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HD aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HE aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_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

Related Database Links:

EMBL Q70LE5 CAD98935
GB YP_003731
PDB 2LVH
REF YP_003731
SP Q70LE5