BMRB Entry 18158

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18158
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution NMR structure of N-terminal domain (6-74) of human ZBP1 protein, Northeast Structural Genomics Consortium Target HR8174A.
Deposition date:
2011-12-20
Original release date:
2012-01-26
Authors:
Yang, Yunhuang; Ramelot, Theresa; Hamilton, Keith; Kohan, Eitan; Wang, Dongyan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Yang, Yunhuang; Ramelot, Theresa; Hamilton, Keith; Kohan, Eitan; Wang, Dongyan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of N-terminal domain (6-74) of human ZBP1 protein, Northeast Structural Genomics Consortium Target HR8174A."  .

Assembly members:

Assembly members:
N-terminal_domain_(6-74)_of_human_ZBP1_protein, polymer, 80 residues, 9023.3 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: pET15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-terminal_domain_(6-74)_of_human_ZBP1_protein: MGHHHHHHSHMADPGREGHL EQRILQVLTEAGSPVKLAQL VKECQAPKRELNQVLYRMKK ELKVSLTSPATWCLGGTDPE

Data sets:
Data typeCount
13C chemical shifts317
15N chemical shifts75
1H chemical shifts517

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain (6-74) of human ZBP1 protein1

Entities:

Entity 1, N-terminal domain (6-74) of human ZBP1 protein 80 residues - 9023.3 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METALAASPPROGLYARGGLUGLYHISLEU
3   GLUGLNARGILELEUGLNVALLEUTHRGLU
4   ALAGLYSERPROVALLYSLEUALAGLNLEU
5   VALLYSGLUCYSGLNALAPROLYSARGGLU
6   LEUASNGLNVALLEUTYRARGMETLYSLYS
7   GLULEULYSVALSERLEUTHRSERPROALA
8   THRTRPCYSLEUGLYGLYTHRASPPROGLU

Samples:

NC_sample: N-terminal domain (6-74) of human ZBP1 protein, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; calcium chloride 5 ± 0.25 mM

NC5_sample: N-terminal domain (6-74) of human ZBP1 protein, [U-5% 13C; U-100% 15N], 1.00 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; calcium chloride 5 ± 0.25 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D 1H-13C arom NOESYNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlyNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC5_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NUS-NOESY aliphaticNC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D CCH-TOCSYNC_sampleisotropicsample_conditions_1
4D CC-NOESYNC_sampleisotropicsample_conditions_1

Software:

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

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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

TOPSPIN v2.1.4, Bruker Biospin - collection

VNMR, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAF83607
EMBL CAC18810
GB AAH28218 AAI31707 AIC57208 AIC62264 EAW75509
REF NP_001153889 NP_001153891 NP_110403 XP_011527359 XP_011527360
SP Q9H171
AlphaFold Q9H171

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