BMRB Entry 11334

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11334
MolProbity Validation Chart

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Title:
Solution structure of the TFIIS domain II of human PHD finger protein 3
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Yoneyama, M.; Tochio, N.; Koshiba, S.; Watabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Watabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the TFIIS domain II of human PHD finger protein 3"  .

Assembly members:

Assembly members:
TFSII_M domain, polymer, 120 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P051216-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TFSII_M domain: GSSGSSGSADQIRQSVRHSL KDILMKRLTDSNLKVPEEKA AKVATKIEKELFSFFRDTDA KYKNKYRSLMFNLKDPKNNI LFKKVLKGEVTPDHLIRMSP EELASKELAAWRRRSGPSSG

Data sets:
Data typeCount
13C chemical shifts520
15N chemical shifts111
1H chemical shifts823

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1TFSII_M domain1

Entities:

Entity 1, TFSII_M domain 120 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYSERALAASP
2   GLNILEARGGLNSERVALARGHISSERLEU
3   LYSASPILELEUMETLYSARGLEUTHRASP
4   SERASNLEULYSVALPROGLUGLULYSALA
5   ALALYSVALALATHRLYSILEGLULYSGLU
6   LEUPHESERPHEPHEARGASPTHRASPALA
7   LYSTYRLYSASNLYSTYRARGSERLEUMET
8   PHEASNLEULYSASPPROLYSASNASNILE
9   LEUPHELYSLYSVALLEULYSGLYGLUVAL
10   THRPROASPHISLEUILEARGMETSERPRO
11   GLUGLULEUALASERLYSGLULEUALAALA
12   TRPARGARGARGSERGLYPROSERSERGLY

Samples:

sample_1: TFSII_M domain, [U-13C; U-15N], 1.20 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.9736, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAC65512
GB AAI37914 EDL14421 EDL99332 EHB14770 ELK35434
REF NP_001074549 NP_001102261 NP_001179500 XP_004011630 XP_004011631
TPG DAA26423

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