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 30703

Title: Solution structure of the TTD and linker region of UHRF1

Deposition date: 2019-12-31 Original release date: 2020-06-11

Authors: Lemak, A.; Houliston, S.; Duan, S.; Ong, M.; Arrowsmith, C.

Citation: Lemak, A.; Houliston, S.; Duan, S.; Ong, M.; Arrowsmith, C.. "Solution structure of the TTD and linker region of UHRF1"  To be published ., .-..

Assembly members:
entity_1, polymer, 168 residues, 19475.812 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):
entity_1: GLYKVNEYVDARDTNMGAWF EAQVVRVTRKAPSRDEPCSS TSRPALEEDVIYHVKYDDYP ENGVVQMNSRDVRARARTII KWQDLEVGQVVMLNYNPDNP KERGFWYDAEISRKRETRTA RELYANVVLGDDSLNDCRII FVDEVFKIERPGEGSPMVDN PMRRKSGP

Data sets:
Data typeCount
13C chemical shifts616
15N chemical shifts149
1H chemical shifts1027

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 168 residues - 19475.812 Da.

1   GLYLEUTYRLYSVALASNGLUTYRVALASP
2   ALAARGASPTHRASNMETGLYALATRPPHE
3   GLUALAGLNVALVALARGVALTHRARGLYS
4   ALAPROSERARGASPGLUPROCYSSERSER
5   THRSERARGPROALALEUGLUGLUASPVAL
6   ILETYRHISVALLYSTYRASPASPTYRPRO
7   GLUASNGLYVALVALGLNMETASNSERARG
8   ASPVALARGALAARGALAARGTHRILEILE
9   LYSTRPGLNASPLEUGLUVALGLYGLNVAL
10   VALMETLEUASNTYRASNPROASPASNPRO
11   LYSGLUARGGLYPHETRPTYRASPALAGLU
12   ILESERARGLYSARGGLUTHRARGTHRALA
13   ARGGLULEUTYRALAASNVALVALLEUGLY
14   ASPASPSERLEUASNASPCYSARGILEILE
15   PHEVALASPGLUVALPHELYSILEGLUARG
16   PROGLYGLUGLYSERPROMETVALASPASN
17   PROMETARGARGLYSSERGLYPRO

Samples:

sample_1: TTD-linker, [U-99% 13C; U-99% 15N], 250 uM; sodium chloride 150 mM; sodium phosphate 25 mM; DTT 5 mM; beta-mercaptoethanol 2 mM; TCEP 2 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 HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_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 III 600 MHz
  • Bruker AVANCE II 800 MHz

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