BMRB Entry 36535

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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/BMR36535
MolProbity Validation Chart

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

Title:
Solution structure of ubiquitin-like domain (UBL) of human ZFAND1
Deposition date:
2022-12-29
Original release date:
2026-03-16
Authors:
Lai, C.; Ko, K.; Fan, P.; Yu, T.; Chang, C.; Hsu, S.
Citation:

Citation: Lai, Chih-Hsuan; Ko, Kuang-Ting; Fan, Pei-Ju; Yu, Tsun-Ai; Chang, Chi-Fon; Draczkowski, Piotr; Hsu, Shang-Te. "Structural insight into the ZFAND1-p97 interaction involved in stress granule clearance."  J. Biol. Chem. 300, 107230-107230 (2024).
PubMed: 38537699

Assembly members:

Assembly members:
AN1-type zinc finger protein 1, polymer, 139 residues, 15679.98 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: not available   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AN1-type zinc finger protein 1: GGSGAKNSETAAKVALMKLK MHADGDKSLPQTERIYFQVF LPKGSKEKSKPMFFCHRWSI GKAIDFAASLARLKNDNNKF TAKKLRLCHITSGEALPLDH TLETWIAKEDCPLYNGGNII LEYLNDEEQFCKNVESYLE

Data sets:
Data typeCount
13C chemical shifts526
15N chemical shifts143
1H chemical shifts889

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 139 residues - 15679.98 Da.

1   GLYGLYSERGLYALALYSASNSERGLUTHR
2   ALAALALYSVALALALEUMETLYSLEULYS
3   METHISALAASPGLYASPLYSSERLEUPRO
4   GLNTHRGLUARGILETYRPHEGLNVALPHE
5   LEUPROLYSGLYSERLYSGLULYSSERLYS
6   PROMETPHEPHECYSHISARGTRPSERILE
7   GLYLYSALAILEASPPHEALAALASERLEU
8   ALAARGLEULYSASNASPASNASNLYSPHE
9   THRALALYSLYSLEUARGLEUCYSHISILE
10   THRSERGLYGLUALALEUPROLEUASPHIS
11   THRLEUGLUTHRTRPILEALALYSGLUASP
12   CYSPROLEUTYRASNGLYGLYASNILEILE
13   LEUGLUTYRLEUASNASPGLUGLUGLNPHE
14   CYSLYSASNVALGLUSERTYRLEUGLU

Samples:

sample_2: UBL prtoein, [U-13C; U-15N], 0.4 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.1; pressure: 1 atm; temperature: 300 K

sample_conditions_2: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 13C/15N simultaneous NOESYsample_2isotropicsample_conditions_1
3D 13C/15N simultaneous NOESYsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_2anisotropicsample_conditions_2

Software:

CYANA v3.98.13, Peter Guntert - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

  • Bruker AVANCE 850 MHz

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