BMRB Entry 16815

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16815

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Title:
Structure of the three-Cys2His2 domain of mouse testis zinc finger protein
Deposition date:
2010-03-31
Original release date:
2010-07-27
Authors:
Chou, Chun-Chi; Lou, Yuan-Chao; Chen, Chinpan
Citation:

Citation: Chou, Chun-Chi; Lou, Yuan-Chao; Tang, Tang; Chen, Chinpan. "Structure and DNA binding characteristics of the three-Cys2His2 domain of mouse testis zinc finger protein."  Proteins 78, 2202-2212 (2010).
PubMed: 20544958

Assembly members:

Assembly members:
mTZD_finger3, polymer, 27 residues, 2872.3 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETBlue-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mTZD_finger3: AAPYRCPLCRAGCPSLASMQ AHMRGHS

Data sets:
Data typeCount
13C chemical shifts103
15N chemical shifts25
1H chemical shifts157

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1mTZD_finger31
2ZINC ION2

Entities:

Entity 1, mTZD_finger3 27 residues - 2872.3 Da.

1   ALAALAPROTYRARGCYSPROLEUCYSARG
2   ALAGLYCYSPROSERLEUALASERMETGLN
3   ALAHISMETARGGLYHISSER

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: acetic acid, [U-99% 2H], 50 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMRView v5, Johnson, One Moon Scientific - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAB30015
GB AAF61244 AAI37688 AAK13198 EDL24005 EDM07732
REF NP_001102987 NP_067372 XP_002920975 XP_004396532 XP_005616754
SP Q9JKD9
AlphaFold Q9JKD9

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