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 19486

Title: Solution NMR Structure of Zinc finger protein 423 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7298F

Deposition date: 2013-09-10 Original release date: 2013-09-23

Authors: Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Everett, John; Acton, Thomas; Montelione, Gaetano; Prestegard, James

Citation: Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Everett, John; Acton, Thomas; Montelione, Gaetano; Prestegard, James. "Solution NMR Structure of Zinc finger protein 423 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7298F"  To be published ., .-..

Assembly members:
HR7298F, polymer, 55 residues, 6432.094 Da.
ZINC ION, 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: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
HR7298F: MGSHKCNVCSRTFFSENGLR EHLQTHRGPAKHYMCPICGE RFPSLLTLTEHKVTH

Data sets:
Data typeCount
13C chemical shifts212
15N chemical shifts51
1H chemical shifts335

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR7298F1
2Zn ion 12
3Zn ion 22

Entities:

Entity 1, HR7298F 55 residues - 6432.094 Da.

M at N-terminal is part of His-Tag.

1   METGLYSERHISLYSCYSASNVALCYSSER
2   ARGTHRPHEPHESERGLUASNGLYLEUARG
3   GLUHISLEUGLNTHRHISARGGLYPROALA
4   LYSHISTYRMETCYSPROILECYSGLYGLU
5   ARGPHEPROSERLEULEUTHRLEUTHRGLU
6   HISLYSVALTHRHIS

Entity 2, Zn ion 1 - Zn - 65.409 Da.

1   ZN

Samples:

NC: HR7298F.005, [U-100% 13C; U-100% 15N], 0.17 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 10%; DSS 50 uM; ZnSO4 50 uM; H2O 90%

C12E5_NC5: HR7298F.0059, [U-5% 13C; U-100% 15N], 0.51 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 5%; DSS 50 uM; C12E5 PEG/Hexanol 4.2%; ZnSO4 50 uM; H2O 95%

NC5: HR7298F.009, [U-5% 13C; U-100% 15N], 0.51 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 5%; DSS 50 uM; ZnSO4 50 uM; H2O 95%

C12E5_NC: HR7298F.005, [U-100% 13C; U-100% 15N], 0.17 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O, [U-100% 2H], 10%; DSS 50 uM; ZnSO4 50 uM; C12E5 PEG?Hexanol 4.2%; H2O 90%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D H(CCO)NHNCisotropicsample_conditions_1
3D HCCH-TOCSYNCisotropicsample_conditions_1
3D 1H-15N NOESYNC5isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT HSQCNC5isotropicsample_conditions_1
2D 1H-15N J-modulation HSQCNCisotropicsample_conditions_1
2D 1H-15N J-modulation HSQCC12E5_NC5anisotropicsample_conditions_1
2D 1H-15N CO filtered TROSYNCisotropicsample_conditions_1
2D 1H-15N CO-filtered TROSYC12E5_NCanisotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

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

VNMRJ, Varian - collection

SPARKY v3.113, Goddard - chemical shift assignment

PALES, PALES (Zweckstetter, Bax) - structure validation

PSVS v1.5, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian Avance 900 MHz
  • Varian Avance 600 MHz

Related Database Links:

EMBL ZN423_HUMAN
PDB
DBJ BAA34480 BAC65647 BAE21688 BAG51329 BAG72439
GB AAB58646 AAF28354 AAG17053 AAH59234 AAI12316
REF NP_001095363 NP_001258549 NP_001297449 NP_055884 NP_201584
SP O08961 Q2M1K9 Q80TS5
TPG DAA20039

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