BMRB Entry 30704

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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/BMR30704
MolProbity Validation Chart

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Title:
Solution structure of the TTD and linker region of mouse UHRF1 (NP95)
Deposition date:
2019-12-31
Original release date:
2020-06-11
Authors:
Lemak, A.; Houliston, S.; Duan, S.; Arrowsmith, C.
Citation:

Citation: Tauber, Maria; Kreuz, Sarah; Lemak, Alexander; Mandal, Papita; Yerkesh, Zhadyra; Veluchamy, Alaguraj; Al-Gashgari, Bothayna; Aljahani, Abrar; Cortes-Medina, Lorena; Azhibek, Dulat; Fan, Lixin; Ong, Michelle; Duan, Shili; Houliston, Scott; Arrowsmith, Cheryl; Fischle, Wolfgang. "Alternative splicing and allosteric regulation modulate the chromatin binding of UHRF1"  Nucleic Acids Res. 48, 7728-7747 (2020).
PubMed: 32609811

Assembly members:

Assembly members:
entity_1, polymer, 187 residues, 21690.576 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMVWEDTDLGLYKVNEYVD VRDNIFGAWFEAQVVQVQKR ALSEDEPCSSSAVKTSEDDI MYHVKYDDYPEHGVDIVKAK NVRARARTVIPWENLEVGQV VMANYNVDYPRKRGFWYDVE ICRKRQTRTARELYGNIRLL NDSQLNNCRIMFVDEVLMIE LPKERRPLIASPSQPPPALR NTGKSGP

Data sets:
Data typeCount
13C chemical shifts677
15N chemical shifts166
1H chemical shifts1120

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 187 residues - 21690.576 Da.

1   GLYHISMETVALTRPGLUASPTHRASPLEU
2   GLYLEUTYRLYSVALASNGLUTYRVALASP
3   VALARGASPASNILEPHEGLYALATRPPHE
4   GLUALAGLNVALVALGLNVALGLNLYSARG
5   ALALEUSERGLUASPGLUPROCYSSERSER
6   SERALAVALLYSTHRSERGLUASPASPILE
7   METTYRHISVALLYSTYRASPASPTYRPRO
8   GLUHISGLYVALASPILEVALLYSALALYS
9   ASNVALARGALAARGALAARGTHRVALILE
10   PROTRPGLUASNLEUGLUVALGLYGLNVAL
11   VALMETALAASNTYRASNVALASPTYRPRO
12   ARGLYSARGGLYPHETRPTYRASPVALGLU
13   ILECYSARGLYSARGGLNTHRARGTHRALA
14   ARGGLULEUTYRGLYASNILEARGLEULEU
15   ASNASPSERGLNLEUASNASNCYSARGILE
16   METPHEVALASPGLUVALLEUMETILEGLU
17   LEUPROLYSGLUARGARGPROLEUILEALA
18   SERPROSERGLNPROPROPROALALEUARG
19   ASNTHRGLYLYSSERGLYPRO

Samples:

sample_1: TTD-linker, [U-99% 13C; U-99% 15N], 250 uM; sodium phosphate 50 mM; DTT 5 mM; TCEP 5 mM; beta-mercaptoethanol 2 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ABACUS, Lemak and Arrowsmith - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

  • Bruker AVANCE II 800 MHz
  • Bruker AVANCE III 600 MHz

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