BMRB Entry 17200

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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/BMR17200
MolProbity Validation Chart

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Title:
NMR structure of UHRF1 Tandem Tudor Domains in a complex with Histone H3 peptide
Deposition date:
2010-09-21
Original release date:
2011-05-02
Authors:
Nady, Nataliya; Lemak, Alexander; Fares, Christopher; Gutmanas, Aleksandras; Avvakumov, George; Xue, Sheng; Arrowsmith, Cheryl
Citation:

Citation: Nady, Nataliya; Lemak, Alexander; Walker, John; Avvakumov, George; Kareta, Michael; Achour, Mayada; Xue, Sheng; Duan, Shili; Allali-Hassani, Abdellah; Zuo, Xiaobing; Wang, Yun-Xing; Bronner, Christian; Chedin, Frederic; Arrowsmith, Cheryl; Dhe-Paganon, Sirano. "Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein."  J. Biol. Chem. 286, 24300-24311 (2011).
PubMed: 21489993

Assembly members:

Assembly members:
UHRF1 Tandem Tudor Domains, polymer, 162 residues, 18824.107 Da.
Histone H3, polymer, 11 residues, 1293.529 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UHRF1 Tandem Tudor Domains: GGMWDETELGLYKVNEYVDA RDTNMGAWFEAQVVRVTRKA PSRDEPCSSTSRPALEEDVI YHVKYDDYPENGVVQMNSRD VRARARTIIKWQDLEVGQVV MLNYNPDNPKERGFWYDAEI SRKRETRTARELYANVVLGD DSLNDCRIIFVDEVFKIERP GE
Histone H3: ARTKQTARXST

Data sets:
Data typeCount
13C chemical shifts644
15N chemical shifts160
1H chemical shifts1122

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UHRF1 Tandem Tudor Domains1
2Histone H32

Entities:

Entity 1, UHRF1 Tandem Tudor Domains 162 residues - 18824.107 Da.

1   GLYGLYMETTRPASPGLUTHRGLULEUGLY
2   LEUTYRLYSVALASNGLUTYRVALASPALA
3   ARGASPTHRASNMETGLYALATRPPHEGLU
4   ALAGLNVALVALARGVALTHRARGLYSALA
5   PROSERARGASPGLUPROCYSSERSERTHR
6   SERARGPROALALEUGLUGLUASPVALILE
7   TYRHISVALLYSTYRASPASPTYRPROGLU
8   ASNGLYVALVALGLNMETASNSERARGASP
9   VALARGALAARGALAARGTHRILEILELYS
10   TRPGLNASPLEUGLUVALGLYGLNVALVAL
11   METLEUASNTYRASNPROASPASNPROLYS
12   GLUARGGLYPHETRPTYRASPALAGLUILE
13   SERARGLYSARGGLUTHRARGTHRALAARG
14   GLULEUTYRALAASNVALVALLEUGLYASP
15   ASPSERLEUASNASPCYSARGILEILEPHE
16   VALASPGLUVALPHELYSILEGLUARGPRO
17   GLYGLU

Entity 2, Histone H3 11 residues - 1293.529 Da.

1   ALAARGTHRLYSGLNTHRALAARGM3LSER
2   THR

Samples:

sample_1: UHRF1 Tandem Tudor Domains, [U-100% 15N], 0.6 mM; UHRF1 Tandem Tudor Domains, [U-100% 13C], 0.6 mM; Histone H3 3 mM; Sodium Phosphate 20 mM; Sodium Chloride 250 mM; DTT 2 mM; Benzamidine 1 mM; PMSF 0.5 mM; H2O 90%; D2O 10%

sample_2: UHRF1 Tandem Tudor Domains, [U-100% 15N], 0.6 mM; UHRF1 Tandem Tudor Domains, [U-100% 13C], 0.6 mM; Histone H3 3 mM; Sodium Phosphate 20 mM; Sodium Chloride 250 mM; DTT 2 mM; Benzamidine 1 mM; PMSF 0.5 mM; Pf1 phage 10 mg/ml; H2O 90%; D2O 10%

sample_3: UHRF1 Tandem Tudor Domains, [U-100% 15N], 0.6 mM; UHRF1 Tandem Tudor Domains, [U-100% 13C], 0.6 mM; Histone H3 3 mM; Sodium Phosphate 20 mM; Sodium Chloride 250 mM; DTT 2 mM; Benzamidine 1 mM; PMSF 0.5 mM; C12E5 peg/hexanol 6%; H2O 90%; D2O 10%

sample_4: UHRF1 Tandem Tudor Domains, [U-100% 15N], 0.6 mM; UHRF1 Tandem Tudor Domains, [U-100% 13C], 0.6 mM; Histone H3 3 mM; Sodium Phosphate 20 mM; Sodium Chloride 250 mM; DTT 2 mM; Benzamidine 1 mM; PMSF 0.5 mM; C12E5 peg/hexanol 3.3%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 250 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
Aro-NOESYsample_1isotropicsample_conditions_1
Aro-2D-1H-13C HSQCsample_1isotropicsample_conditions_1
Aro-3D-TOCSYsample_1isotropicsample_conditions_1
2D-TOCSYsample_1isotropicsample_conditions_1
3D-Edited-15N/13C NOESYsample_1isotropicsample_conditions_1
IPAP-15N-1H HSQCsample_1isotropicsample_conditions_1
J-evolution-13CO-13CAsample_1isotropicsample_conditions_1
J-evolution-15N-13COsample_1isotropicsample_conditions_1
IPAP-15N-1H HSQCsample_2anisotropicsample_conditions_1
IPAP-15N-1H HSQCsample_3anisotropicsample_conditions_1
IPAP-15N-1H HSQCsample_4anisotropicsample_conditions_1
J-evolution-13CO-13CAsample_4anisotropicsample_conditions_1
J-evolution-15N-13COsample_4anisotropicsample_conditions_1

Software:

ABACUS, Lemak - chemical shift assignment

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

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

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY, Goddard - peak picking

FuDA, Flemming Hansen - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAF36719 BAF36720 BAF82078 BAG37156
GB AAF28469 AAI13876 AAK55744 AAV40831 ABQ59043
REF NP_001041666 NP_001276979 NP_001276980 NP_001276981 NP_037414
SP Q96T88
AlphaFold Q96T88 Q3BDD9

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