BMRB Entry 17679

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17679
MolProbity Validation Chart

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Human Just Another Zinc Finger Protein residues 168-227
Deposition date:
2011-05-31
Original release date:
2014-02-24
Authors:
Burge, Russell; Martinez-Yamout, Maria; Dyson, H.; Wright, Peter
Citation:

Citation: Burge, Russell; Martinez-Yamout, Maria; Dyson, H. Jane; Wright, Peter. "Structural Characterization of Interactions between the Double-Stranded RNA-Binding Zinc Finger Protein JAZ and Nucleic Acids."  Biochemistry ., .-. (2014).
PubMed: 24521053

Assembly members:

Assembly members:
JAZ_ZF3, polymer, 60 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
JAZ_ZF3: STKVEALHQNREMIDPDKFC SLCHATFNDPVMAQQHYVGK KHRKQETKLKLMARYGRLAD

Data sets:
Data typeCount
13C chemical shifts113
15N chemical shifts55
1H chemical shifts55

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1JAZ ZF31
2zinc2

Entities:

Entity 1, JAZ ZF3 60 residues - Formula weight is not available

1   SERTHRLYSVALGLUALALEUHISGLNASN
2   ARGGLUMETILEASPPROASPLYSPHECYS
3   SERLEUCYSHISALATHRPHEASNASPPRO
4   VALMETALAGLNGLNHISTYRVALGLYLYS
5   LYSHISARGLYSGLNGLUTHRLYSLEULYS
6   LEUMETALAARGTYRGLYARGLEUALAASP

Entity 2, zinc - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: JAZ ZF3, [U-98% 13C; U-98% 15N], 300 uM; TRIS 25 mM; potassium chloride 50 mM; DTT 2 mM; zinc 50 uM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 75 mM; pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

GB EAW85038 AAD52018 AAH07775 AIC50988 EAW85040 EFB17692
PDB
DBJ BAD18614 BAG72878 BAH12103 BAH12584
EMBL CAH18475 CAL37677 CAL38643
REF NP_001231409 NP_001295142 NP_001295143 NP_001295147 NP_036411
SP Q9UL40
AlphaFold Q9UL40

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