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 6682

Title: Solution Structure of a Human C2H2-type Zinc Finger Protein   PubMed: 18287285

Deposition date: 2005-06-09 Original release date: 2005-07-27

Authors: Lytle, B.; Peterson, F.; Volkman, B.

Citation: Hayes, P.; Lytle, B.; Volkman, B.; Peterson, F.. "The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein"  Protein Sci. 17, 571-576 (2008).

Assembly members:
Zinc finger protein 593, polymer, 124 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis

Entity Sequences (FASTA):
Zinc finger protein 593: GHHHHHHLEKAKRRRPDLDE IHRELRPQGSARPQPDPNAE FDPDLPGGGLHRCLACARYF IDSTNLKTHFRSKDHKKRLK QLSVEPYSQEEAERAAGMGS YVPPRRLAVPTEVSTEVPEM DTST

Data sets:
Data typeCount
1H chemical shifts404
13C chemical shifts278
15N chemical shifts68

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Zinc finger protein 5931
2ZINC ION2

Entities:

Entity 1, Zinc finger protein 593 124 residues - Formula weight is not available

1   GLYHISHISHISHISHISHISLEUGLULYS
2   ALALYSARGARGARGPROASPLEUASPGLU
3   ILEHISARGGLULEUARGPROGLNGLYSER
4   ALAARGPROGLNPROASPPROASNALAGLU
5   PHEASPPROASPLEUPROGLYGLYGLYLEU
6   HISARGCYSLEUALACYSALAARGTYRPHE
7   ILEASPSERTHRASNLEULYSTHRHISPHE
8   ARGSERLYSASPHISLYSLYSARGLEULYS
9   GLNLEUSERVALGLUPROTYRSERGLNGLU
10   GLUALAGLUARGALAALAGLYMETGLYSER
11   TYRVALPROPROARGARGLEUALAVALPRO
12   THRGLUVALSERTHRGLUVALPROGLUMET
13   ASPTHRSERTHR

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Zinc finger protein 593, [U-15N; U-13C], 0.6 mM; Bis Tris 10 mM; NaCl 100 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6.0; temperature: 298 K; ionic strength: 100 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1not availablesample_cond_1
HNCAsample_1not availablesample_cond_1
HNCOsample_1not availablesample_cond_1
HN(CO)CAsample_1not availablesample_cond_1
HNCACBsample_1not availablesample_cond_1
HN(CA)COsample_1not availablesample_cond_1
C(CO)NHsample_1not availablesample_cond_1
HBHA(CO)NHsample_1not availablesample_cond_1
HCCH-TOCSYsample_1not availablesample_cond_1
3D 13C-separated NOESY (aliph)sample_1not availablesample_cond_1
3D 15N-separated NOESYsample_1not availablesample_cond_1
3D 13C-separated NOESY (AROMATIC)sample_1not availablesample_cond_1

Software:

XWINNMR v3.5 - collection

NMRPipe v2004 - processing

SPSCAN v1.1.0 - data analysis

XEASY v1.3 - data analysis

GARANT v2.1 - data analysis

CYANA v1.0.6 - structure solution

XPLOR-NIH v2.0.6 - refinement

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

SWISS-PROT O00488
GenBank ABZ92327 AAH19267 AAH02580
DBJ BAG34867 BAA20369
PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts